CNRS Nantes University UFIP UFIP
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***  Elastic_net_trial  ***

elNémo ID: 19020320192746986

Job options:

ID        	=	 19020320192746986
JOBID     	=	 Elastic_net_trial
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 Elastic_net_trial

HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       09-DEC-15   5F9E              
TITLE     STRUCTURE OF PROTEIN KINASE C THETA WITH COMPOUND 10: 2,2-DIMETHYL-7- 
TITLE    2 (2-OXIDANYLIDENE-3~{H}-IMIDAZO[4,5-B]PYRIDIN-1-YL)-1-(PHENYLMETHYL)- 
TITLE    3 3~{H}-QUINAZOLIN-4-ONE                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN KINASE C THETA TYPE;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: NPKC-THETA;                                                 
COMPND   5 EC: 2.7.11.13;                                                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PRKCQ, PRKCT;                                                  
SOURCE   6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;                         
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10469                                       
KEYWDS    KINASE, INHIBITOR, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.KLEIN                                                               
REVDAT   1   11-MAY-16 5F9E    0                                                
JRNL        AUTH   T.KATOH,T.TAKAI,T.YUKAWA,T.TSUKAMOTO,E.WATANABE,H.MOTOTANI,  
JRNL        AUTH 2 T.ARITA,H.HAYASHI,H.NAKAGAWA,M.G.KLEIN,H.ZOU,B.C.SANG,       
JRNL        AUTH 3 G.SNELL,Y.NAKADA                                             
JRNL        TITL   DISCOVERY AND OPTIMIZATION OF                                
JRNL        TITL 2 1,7-DISUBSTITUTED-2,2-DIMETHYL-2,3-DIHYDROQUINAZOLIN-4(1H)   
JRNL        TITL 3 -ONES AS POTENT AND SELECTIVE PKC THETA INHIBITORS.          
JRNL        REF    BIOORG.MED.CHEM.              V.  24  2466 2016              
JRNL        REFN                   ESSN 1464-3391                               
JRNL        PMID   27117263                                                     
JRNL        DOI    10.1016/J.BMC.2016.04.008                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0025                                      
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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 54956                          
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) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.233                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2929                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3328                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 82.17                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2990                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 192                          
REMARK   3   BIN FREE R VALUE                    : 0.3470                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5248                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 60                                      
REMARK   3   SOLVENT ATOMS            : 164                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 54.73                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.74000                                              
REMARK   3    B22 (A**2) : -1.84000                                             
REMARK   3    B33 (A**2) : -0.90000                                             
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): 0.165         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.152         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.108         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.979         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.948                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5499 ; 0.009 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  5180 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7417 ; 1.422 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11958 ; 0.784 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   641 ; 6.264 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   279 ;34.549 ;24.014       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1007 ;16.338 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    30 ;18.334 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   753 ; 0.090 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6122 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1324 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
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   374        A   709                          
REMARK   3    RESIDUE RANGE :   A  1001        A  1001                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.6740  74.9240  30.2966              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1516 T22:   0.0199                                     
REMARK   3      T33:   0.0934 T12:   0.0040                                     
REMARK   3      T13:  -0.0064 T23:   0.0192                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3098 L22:   1.7655                                     
REMARK   3      L33:   1.6686 L12:   0.4868                                     
REMARK   3      L13:  -0.1754 L23:  -0.0871                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0537 S12:   0.0250 S13:   0.0296                       
REMARK   3      S21:  -0.1174 S22:  -0.0178 S23:   0.1679                       
REMARK   3      S31:   0.0360 S32:  -0.1571 S33:  -0.0358                       
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   375        B   700                          
REMARK   3    RESIDUE RANGE :   B  1001        B  1001                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.7446  84.1102  -8.8861              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2372 T22:   0.3061                                     
REMARK   3      T33:   0.2570 T12:   0.1107                                     
REMARK   3      T13:  -0.0996 T23:   0.0356                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1108 L22:   2.9367                                     
REMARK   3      L33:   2.9342 L12:  -0.3965                                     
REMARK   3      L13:   0.4318 L23:  -1.0389                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0503 S12:   0.0362 S13:  -0.0588                       
REMARK   3      S21:   0.0633 S22:  -0.1405 S23:  -0.4380                       
REMARK   3      S31:   0.4183 S32:   0.3618 S33:   0.0901                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5F9E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-DEC-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000216138.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-JUL-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.3                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59517                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 29.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7, 0.2M LITHIUM CITRATE,   
REMARK 280  AND 18% PEG M.W. 3,350, 1% HEXANEDIOL, VAPOR DIFFUSION, HANGING     
REMARK 280  DROP, TEMPERATURE 290K                                              
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       37.80150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       74.65200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.39300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       74.65200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.80150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.39300            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   360                                                      
REMARK 465     GLU A   361                                                      
REMARK 465     PRO A   362                                                      
REMARK 465     GLU A   363                                                      
REMARK 465     LEU A   364                                                      
REMARK 465     ASN A   365                                                      
REMARK 465     LYS A   366                                                      
REMARK 465     GLU A   367                                                      
REMARK 465     ARG A   368                                                      
REMARK 465     PRO A   369                                                      
REMARK 465     SER A   370                                                      
REMARK 465     LEU A   371                                                      
REMARK 465     GLN A   372                                                      
REMARK 465     ILE A   373                                                      
REMARK 465     HIS A   710                                                      
REMARK 465     HIS A   711                                                      
REMARK 465     HIS A   712                                                      
REMARK 465     MET B   360                                                      
REMARK 465     GLU B   361                                                      
REMARK 465     PRO B   362                                                      
REMARK 465     GLU B   363                                                      
REMARK 465     LEU B   364                                                      
REMARK 465     ASN B   365                                                      
REMARK 465     LYS B   366                                                      
REMARK 465     GLU B   367                                                      
REMARK 465     ARG B   368                                                      
REMARK 465     PRO B   369                                                      
REMARK 465     SER B   370                                                      
REMARK 465     LEU B   371                                                      
REMARK 465     GLN B   372                                                      
REMARK 465     ILE B   373                                                      
REMARK 465     LYS B   374                                                      
REMARK 465     SER B   657                                                      
REMARK 465     PRO B   658                                                      
REMARK 465     PHE B   659                                                      
REMARK 465     ASP B   660                                                      
REMARK 465     CYS B   661                                                      
REMARK 465     SER B   662                                                      
REMARK 465     ASN B   663                                                      
REMARK 465     PHE B   664                                                      
REMARK 465     ASP B   665                                                      
REMARK 465     LYS B   666                                                      
REMARK 465     GLU B   667                                                      
REMARK 465     PHE B   668                                                      
REMARK 465     LEU B   669                                                      
REMARK 465     ASN B   670                                                      
REMARK 465     GLU B   671                                                      
REMARK 465     LYS B   672                                                      
REMARK 465     PRO B   673                                                      
REMARK 465     ARG B   674                                                      
REMARK 465     LEU B   675                                                      
REMARK 465     SEP B   676                                                      
REMARK 465     PHE B   677                                                      
REMARK 465     ALA B   678                                                      
REMARK 465     ASP B   679                                                      
REMARK 465     ARG B   680                                                      
REMARK 465     ALA B   681                                                      
REMARK 465     LEU B   682                                                      
REMARK 465     ILE B   683                                                      
REMARK 465     ASN B   684                                                      
REMARK 465     SER B   685                                                      
REMARK 465     MET B   686                                                      
REMARK 465     ASP B   687                                                      
REMARK 465     GLN B   688                                                      
REMARK 465     MET B   701                                                      
REMARK 465     GLU B   702                                                      
REMARK 465     ARG B   703                                                      
REMARK 465     LEU B   704                                                      
REMARK 465     ILE B   705                                                      
REMARK 465     SER B   706                                                      
REMARK 465     HIS B   707                                                      
REMARK 465     HIS B   708                                                      
REMARK 465     HIS B   709                                                      
REMARK 465     HIS B   710                                                      
REMARK 465     HIS B   711                                                      
REMARK 465     HIS B   712                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A 400     -133.99     42.42                                   
REMARK 500    THR A 402      166.01    -48.69                                   
REMARK 500    ASN A 403       30.86    -90.86                                   
REMARK 500    HIS A 474      -46.17     74.61                                   
REMARK 500    ARG A 503       -5.11     73.24                                   
REMARK 500    ASP A 522       90.67     72.18                                   
REMARK 500    ASN A 537       17.26   -140.77                                   
REMARK 500    ASN A 557     -150.69   -125.13                                   
REMARK 500    PHE A 614       45.15    -89.66                                   
REMARK 500    ASN A 689      -19.58    -45.03                                   
REMARK 500    LYS B 400      -57.58     78.79                                   
REMARK 500    LYS B 401      -79.60    -66.56                                   
REMARK 500    HIS B 474      -55.55     70.97                                   
REMARK 500    ARG B 503       -7.56     71.76                                   
REMARK 500    ASP B 522       88.94     62.54                                   
REMARK 500    ASN B 537       21.83   -145.44                                   
REMARK 500    CYS B 540      135.47   -170.19                                   
REMARK 500    ASN B 557     -153.91   -123.77                                   
REMARK 500    PHE B 614       39.31    -81.90                                   
REMARK 500    MET B 690       33.94    -86.26                                   
REMARK 500    PHE B 691       42.11   -106.77                                   
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 PHE B  539     CYS B  540                 -147.91                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 5VS A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 5VS B 1001                
DBREF  5F9E A  361   706  UNP    Q04759   KPCT_HUMAN     361    706             
DBREF  5F9E B  361   706  UNP    Q04759   KPCT_HUMAN     361    706             
SEQADV 5F9E MET A  360  UNP  Q04759              INITIATING METHIONINE          
SEQADV 5F9E GLU A  381  UNP  Q04759    ILE   381 CONFLICT                       
SEQADV 5F9E GLU A  538  UNP  Q04759    THR   538 CONFLICT                       
SEQADV 5F9E HIS A  707  UNP  Q04759              EXPRESSION TAG                 
SEQADV 5F9E HIS A  708  UNP  Q04759              EXPRESSION TAG                 
SEQADV 5F9E HIS A  709  UNP  Q04759              EXPRESSION TAG                 
SEQADV 5F9E HIS A  710  UNP  Q04759              EXPRESSION TAG                 
SEQADV 5F9E HIS A  711  UNP  Q04759              EXPRESSION TAG                 
SEQADV 5F9E HIS A  712  UNP  Q04759              EXPRESSION TAG                 
SEQADV 5F9E MET B  360  UNP  Q04759              INITIATING METHIONINE          
SEQADV 5F9E GLU B  381  UNP  Q04759    ILE   381 CONFLICT                       
SEQADV 5F9E GLU B  538  UNP  Q04759    THR   538 CONFLICT                       
SEQADV 5F9E HIS B  707  UNP  Q04759              EXPRESSION TAG                 
SEQADV 5F9E HIS B  708  UNP  Q04759              EXPRESSION TAG                 
SEQADV 5F9E HIS B  709  UNP  Q04759              EXPRESSION TAG                 
SEQADV 5F9E HIS B  710  UNP  Q04759              EXPRESSION TAG                 
SEQADV 5F9E HIS B  711  UNP  Q04759              EXPRESSION TAG                 
SEQADV 5F9E HIS B  712  UNP  Q04759              EXPRESSION TAG                 
SEQRES   1 A  353  MET GLU PRO GLU LEU ASN LYS GLU ARG PRO SER LEU GLN          
SEQRES   2 A  353  ILE LYS LEU LYS ILE GLU ASP PHE GLU LEU HIS LYS MET          
SEQRES   3 A  353  LEU GLY LYS GLY SER PHE GLY LYS VAL PHE LEU ALA GLU          
SEQRES   4 A  353  PHE LYS LYS THR ASN GLN PHE PHE ALA ILE LYS ALA LEU          
SEQRES   5 A  353  LYS LYS ASP VAL VAL LEU MET ASP ASP ASP VAL GLU CYS          
SEQRES   6 A  353  THR MET VAL GLU LYS ARG VAL LEU SER LEU ALA TRP GLU          
SEQRES   7 A  353  HIS PRO PHE LEU THR HIS MET PHE CYS THR PHE GLN THR          
SEQRES   8 A  353  LYS GLU ASN LEU PHE PHE VAL MET GLU TYR LEU ASN GLY          
SEQRES   9 A  353  GLY ASP LEU MET TYR HIS ILE GLN SER CYS HIS LYS PHE          
SEQRES  10 A  353  ASP LEU SER ARG ALA THR PHE TYR ALA ALA GLU ILE ILE          
SEQRES  11 A  353  LEU GLY LEU GLN PHE LEU HIS SER LYS GLY ILE VAL TYR          
SEQRES  12 A  353  ARG ASP LEU LYS LEU ASP ASN ILE LEU LEU ASP LYS ASP          
SEQRES  13 A  353  GLY HIS ILE LYS ILE ALA ASP PHE GLY MET CYS LYS GLU          
SEQRES  14 A  353  ASN MET LEU GLY ASP ALA LYS THR ASN GLU PHE CYS GLY          
SEQRES  15 A  353  THR PRO ASP TYR ILE ALA PRO GLU ILE LEU LEU GLY GLN          
SEQRES  16 A  353  LYS TYR ASN HIS SER VAL ASP TRP TRP SER PHE GLY VAL          
SEQRES  17 A  353  LEU LEU TYR GLU MET LEU ILE GLY GLN SER PRO PHE HIS          
SEQRES  18 A  353  GLY GLN ASP GLU GLU GLU LEU PHE HIS SER ILE ARG MET          
SEQRES  19 A  353  ASP ASN PRO PHE TYR PRO ARG TRP LEU GLU LYS GLU ALA          
SEQRES  20 A  353  LYS ASP LEU LEU VAL LYS LEU PHE VAL ARG GLU PRO GLU          
SEQRES  21 A  353  LYS ARG LEU GLY VAL ARG GLY ASP ILE ARG GLN HIS PRO          
SEQRES  22 A  353  LEU PHE ARG GLU ILE ASN TRP GLU GLU LEU GLU ARG LYS          
SEQRES  23 A  353  GLU ILE ASP PRO PRO PHE ARG PRO LYS VAL LYS SER PRO          
SEQRES  24 A  353  PHE ASP CYS SER ASN PHE ASP LYS GLU PHE LEU ASN GLU          
SEQRES  25 A  353  LYS PRO ARG LEU SEP PHE ALA ASP ARG ALA LEU ILE ASN          
SEQRES  26 A  353  SER MET ASP GLN ASN MET PHE ARG ASN PHE SEP PHE MET          
SEQRES  27 A  353  ASN PRO GLY MET GLU ARG LEU ILE SER HIS HIS HIS HIS          
SEQRES  28 A  353  HIS HIS                                                      
SEQRES   1 B  353  MET GLU PRO GLU LEU ASN LYS GLU ARG PRO SER LEU GLN          
SEQRES   2 B  353  ILE LYS LEU LYS ILE GLU ASP PHE GLU LEU HIS LYS MET          
SEQRES   3 B  353  LEU GLY LYS GLY SER PHE GLY LYS VAL PHE LEU ALA GLU          
SEQRES   4 B  353  PHE LYS LYS THR ASN GLN PHE PHE ALA ILE LYS ALA LEU          
SEQRES   5 B  353  LYS LYS ASP VAL VAL LEU MET ASP ASP ASP VAL GLU CYS          
SEQRES   6 B  353  THR MET VAL GLU LYS ARG VAL LEU SER LEU ALA TRP GLU          
SEQRES   7 B  353  HIS PRO PHE LEU THR HIS MET PHE CYS THR PHE GLN THR          
SEQRES   8 B  353  LYS GLU ASN LEU PHE PHE VAL MET GLU TYR LEU ASN GLY          
SEQRES   9 B  353  GLY ASP LEU MET TYR HIS ILE GLN SER CYS HIS LYS PHE          
SEQRES  10 B  353  ASP LEU SER ARG ALA THR PHE TYR ALA ALA GLU ILE ILE          
SEQRES  11 B  353  LEU GLY LEU GLN PHE LEU HIS SER LYS GLY ILE VAL TYR          
SEQRES  12 B  353  ARG ASP LEU LYS LEU ASP ASN ILE LEU LEU ASP LYS ASP          
SEQRES  13 B  353  GLY HIS ILE LYS ILE ALA ASP PHE GLY MET CYS LYS GLU          
SEQRES  14 B  353  ASN MET LEU GLY ASP ALA LYS THR ASN GLU PHE CYS GLY          
SEQRES  15 B  353  THR PRO ASP TYR ILE ALA PRO GLU ILE LEU LEU GLY GLN          
SEQRES  16 B  353  LYS TYR ASN HIS SER VAL ASP TRP TRP SER PHE GLY VAL          
SEQRES  17 B  353  LEU LEU TYR GLU MET LEU ILE GLY GLN SER PRO PHE HIS          
SEQRES  18 B  353  GLY GLN ASP GLU GLU GLU LEU PHE HIS SER ILE ARG MET          
SEQRES  19 B  353  ASP ASN PRO PHE TYR PRO ARG TRP LEU GLU LYS GLU ALA          
SEQRES  20 B  353  LYS ASP LEU LEU VAL LYS LEU PHE VAL ARG GLU PRO GLU          
SEQRES  21 B  353  LYS ARG LEU GLY VAL ARG GLY ASP ILE ARG GLN HIS PRO          
SEQRES  22 B  353  LEU PHE ARG GLU ILE ASN TRP GLU GLU LEU GLU ARG LYS          
SEQRES  23 B  353  GLU ILE ASP PRO PRO PHE ARG PRO LYS VAL LYS SER PRO          
SEQRES  24 B  353  PHE ASP CYS SER ASN PHE ASP LYS GLU PHE LEU ASN GLU          
SEQRES  25 B  353  LYS PRO ARG LEU SEP PHE ALA ASP ARG ALA LEU ILE ASN          
SEQRES  26 B  353  SER MET ASP GLN ASN MET PHE ARG ASN PHE SEP PHE MET          
SEQRES  27 B  353  ASN PRO GLY MET GLU ARG LEU ILE SER HIS HIS HIS HIS          
SEQRES  28 B  353  HIS HIS                                                      
MODRES 5F9E SEP A  676  SER  MODIFIED RESIDUE                                   
MODRES 5F9E SEP A  695  SER  MODIFIED RESIDUE                                   
MODRES 5F9E SEP B  695  SER  MODIFIED RESIDUE                                   
HET    SEP  A 676      10                                                       
HET    SEP  A 695      10                                                       
HET    SEP  B 695      10                                                       
HET    5VS  A1001      30                                                       
HET    5VS  B1001      30                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     5VS 2,2-DIMETHYL-7-(2-OXIDANYLIDENE-3~{H}-IMIDAZO[4,5-               
HETNAM   2 5VS  B]PYRIDIN-1-YL)-1-(PHENYLMETHYL)-3~{H}-QUINAZOLIN-4-            
HETNAM   3 5VS  ONE                                                             
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   1  SEP    3(C3 H8 N O6 P)                                              
FORMUL   3  5VS    2(C23 H21 N5 O2)                                             
FORMUL   5  HOH   *164(H2 O)                                                    
HELIX    1 AA1 LYS A  376  GLU A  378  5                                   3    
HELIX    2 AA2 LYS A  413  ASP A  419  1                                   7    
HELIX    3 AA3 ASP A  421  TRP A  436  1                                  16    
HELIX    4 AA4 LEU A  466  HIS A  474  1                                   9    
HELIX    5 AA5 ASP A  477  LYS A  498  1                                  22    
HELIX    6 AA6 LYS A  506  ASP A  508  5                                   3    
HELIX    7 AA7 THR A  542  ILE A  546  5                                   5    
HELIX    8 AA8 ALA A  547  LEU A  552  1                                   6    
HELIX    9 AA9 HIS A  558  GLY A  575  1                                  18    
HELIX   10 AB1 ASP A  583  ASP A  594  1                                  12    
HELIX   11 AB2 GLU A  603  PHE A  614  1                                  12    
HELIX   12 AB3 GLU A  617  ARG A  621  5                                   5    
HELIX   13 AB4 ASP A  627  ARG A  635  5                                   9    
HELIX   14 AB5 ASN A  638  ARG A  644  1                                   7    
HELIX   15 AB6 ASP A  665  ASN A  670  1                                   6    
HELIX   16 AB7 ASP A  679  MET A  686  1                                   8    
HELIX   17 AB8 ASP A  687  ARG A  692  5                                   6    
HELIX   18 AB9 ASN A  698  HIS A  708  1                                  11    
HELIX   19 AC1 LYS B  376  PHE B  380  5                                   5    
HELIX   20 AC2 LYS B  413  ASP B  419  1                                   7    
HELIX   21 AC3 ASP B  421  TRP B  436  1                                  16    
HELIX   22 AC4 ASP B  465  HIS B  474  1                                  10    
HELIX   23 AC5 ASP B  477  LYS B  498  1                                  22    
HELIX   24 AC6 LYS B  506  ASP B  508  5                                   3    
HELIX   25 AC7 THR B  542  ILE B  546  5                                   5    
HELIX   26 AC8 ALA B  547  LEU B  552  1                                   6    
HELIX   27 AC9 HIS B  558  GLY B  575  1                                  18    
HELIX   28 AD1 ASP B  583  ASP B  594  1                                  12    
HELIX   29 AD2 GLU B  603  PHE B  614  1                                  12    
HELIX   30 AD3 GLU B  617  ARG B  621  5                                   5    
HELIX   31 AD4 ASP B  627  ARG B  635  5                                   9    
HELIX   32 AD5 ASN B  638  ARG B  644  1                                   7    
SHEET    1 AA1 6 PHE A 380  GLY A 389  0                                        
SHEET    2 AA1 6 GLY A 392  PHE A 399 -1  O  VAL A 394   N  GLY A 387           
SHEET    3 AA1 6 PHE A 405  LYS A 412 -1  O  ALA A 410   N  LYS A 393           
SHEET    4 AA1 6 ASN A 453  GLU A 459 -1  O  MET A 458   N  ALA A 407           
SHEET    5 AA1 6 MET A 444  GLN A 449 -1  N  CYS A 446   O  VAL A 457           
SHEET    6 AA1 6 PHE A 696  MET A 697 -1  O  PHE A 696   N  THR A 447           
SHEET    1 AA2 3 GLY A 464  ASP A 465  0                                        
SHEET    2 AA2 3 ILE A 510  LEU A 512 -1  O  LEU A 512   N  GLY A 464           
SHEET    3 AA2 3 ILE A 518  ILE A 520 -1  O  LYS A 519   N  LEU A 511           
SHEET    1 AA3 6 GLU B 381  GLY B 389  0                                        
SHEET    2 AA3 6 GLY B 392  GLU B 398 -1  O  LEU B 396   N  HIS B 383           
SHEET    3 AA3 6 PHE B 405  LYS B 412 -1  O  ALA B 410   N  LYS B 393           
SHEET    4 AA3 6 ASN B 453  MET B 458 -1  O  MET B 458   N  ALA B 407           
SHEET    5 AA3 6 MET B 444  GLN B 449 -1  N  CYS B 446   O  VAL B 457           
SHEET    6 AA3 6 PHE B 696  MET B 697 -1  O  PHE B 696   N  THR B 447           
SHEET    1 AA4 2 ILE B 510  LEU B 512  0                                        
SHEET    2 AA4 2 ILE B 518  ILE B 520 -1  O  LYS B 519   N  LEU B 511           
LINK         C   LEU A 675                 N   SEP A 676     1555   1555  1.32  
LINK         C   SEP A 676                 N   PHE A 677     1555   1555  1.32  
LINK         C   PHE A 694                 N   SEP A 695     1555   1555  1.33  
LINK         C   SEP A 695                 N   PHE A 696     1555   1555  1.32  
LINK         C   PHE B 694                 N   SEP B 695     1555   1555  1.33  
LINK         C   SEP B 695                 N   PHE B 696     1555   1555  1.33  
SITE     1 AC1 14 LEU A 386  GLY A 387  PHE A 391  VAL A 394                    
SITE     2 AC1 14 ALA A 407  LYS A 409  THR A 442  MET A 458                    
SITE     3 AC1 14 GLU A 459  LEU A 461  ASN A 509  LEU A 511                    
SITE     4 AC1 14 ASP A 522  PHE A 664                                          
SITE     1 AC2  9 LEU B 386  PHE B 391  ALA B 407  LYS B 409                    
SITE     2 AC2  9 THR B 442  MET B 458  GLU B 459  LEU B 461                    
SITE     3 AC2  9 ASN B 509                                                     
CRYST1   75.603   76.786  149.304  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      0.013227  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013023  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006698        0.00000                         
ATOM      1  N   LYS A 374       6.057  61.695  26.863  1.00 87.67           N  
ANISOU    1  N   LYS A 374     9218  11853  12239  -2302  -1340    189       N  
ATOM      2  CA  LYS A 374       5.866  62.798  27.858  1.00 86.23           C  
ANISOU    2  CA  LYS A 374     8862  11735  12165  -2124  -1189    231       C  
ATOM      3  C   LYS A 374       6.596  64.103  27.450  1.00 80.57           C  
ANISOU    3  C   LYS A 374     8199  10998  11413  -1867  -1216    258       C  
ATOM      4  O   LYS A 374       6.129  64.786  26.538  1.00 82.29           O  
ANISOU    4  O   LYS A 374     8292  11309  11663  -1793  -1372    289       O  
ATOM      5  CB  LYS A 374       6.195  62.337  29.304  1.00 87.09           C  
ANISOU    5  CB  LYS A 374     9042  11766  12280  -2168   -958    222       C  
ATOM      6  CG  LYS A 374       7.481  61.527  29.495  1.00 86.76           C  
ANISOU    6  CG  LYS A 374     9334  11534  12096  -2203   -898    191       C  
ATOM      7  CD  LYS A 374       7.323  60.448  30.561  1.00 87.32           C  
ANISOU    7  CD  LYS A 374     9452  11548  12175  -2380   -756    186       C  
ATOM      8  CE  LYS A 374       6.391  59.334  30.089  1.00 91.62           C  
ANISOU    8  CE  LYS A 374     9928  12130  12753  -2635   -855    167       C  
ATOM      9  NZ  LYS A 374       6.549  58.069  30.856  1.00 92.68           N  
ANISOU    9  NZ  LYS A 374    10211  12147  12854  -2822   -746    159       N  
ATOM     10  N   LEU A 375       7.729  64.434  28.076  1.00 72.26           N  
ANISOU   10  N   LEU A 375     7334   9825  10294  -1741  -1077    250       N  
ATOM     11  CA  LEU A 375       8.271  65.819  28.058  1.00 67.04           C  
ANISOU   11  CA  LEU A 375     6676   9157   9639  -1497  -1049    279       C  
ATOM     12  C   LEU A 375       8.444  66.482  26.663  1.00 64.17           C  
ANISOU   12  C   LEU A 375     6342   8812   9224  -1397  -1242    304       C  
ATOM     13  O   LEU A 375       8.991  65.884  25.735  1.00 62.26           O  
ANISOU   13  O   LEU A 375     6287   8509   8857  -1469  -1356    280       O  
ATOM     14  CB  LEU A 375       9.585  65.879  28.850  1.00 63.46           C  
ANISOU   14  CB  LEU A 375     6452   8561   9097  -1415   -892    259       C  
ATOM     15  CG  LEU A 375      10.207  67.251  29.167  1.00 62.09           C  
ANISOU   15  CG  LEU A 375     6293   8363   8934  -1186   -814    279       C  
ATOM     16  CD1 LEU A 375       9.370  68.043  30.162  1.00 62.43           C  
ANISOU   16  CD1 LEU A 375     6105   8498   9118  -1109   -685    295       C  
ATOM     17  CD2 LEU A 375      11.618  67.095  29.705  1.00 59.42           C  
ANISOU   17  CD2 LEU A 375     6211   7884   8483  -1143   -705    256       C  
ATOM     18  N   LYS A 376       7.970  67.728  26.549  1.00 61.95           N  
ANISOU   18  N   LYS A 376     5884   8614   9040  -1228  -1269    354       N  
ATOM     19  CA  LYS A 376       8.028  68.516  25.306  1.00 60.98           C  
ANISOU   19  CA  LYS A 376     5768   8520   8882  -1117  -1449    398       C  
ATOM     20  C   LYS A 376       8.502  69.942  25.583  1.00 58.78           C  
ANISOU   20  C   LYS A 376     5488   8204   8641   -877  -1371    436       C  
ATOM     21  O   LYS A 376       8.324  70.462  26.690  1.00 55.66           O  
ANISOU   21  O   LYS A 376     4987   7813   8348   -793  -1204    432       O  
ATOM     22  CB  LYS A 376       6.650  68.592  24.645  1.00 64.96           C  
ANISOU   22  CB  LYS A 376     6004   9185   9490  -1169  -1621    442       C  
ATOM     23  CG  LYS A 376       5.895  67.281  24.694  1.00 68.25           C  
ANISOU   23  CG  LYS A 376     6346   9663   9923  -1417  -1662    404       C  
ATOM     24  CD  LYS A 376       4.747  67.185  23.701  1.00 71.29           C  
ANISOU   24  CD  LYS A 376     6526  10200  10360  -1504  -1890    440       C  
ATOM     25  CE  LYS A 376       4.526  65.724  23.347  1.00 72.73           C  
ANISOU   25  CE  LYS A 376     6788  10380  10467  -1776  -1968    382       C  
ATOM     26  NZ  LYS A 376       3.216  65.502  22.688  1.00 76.76           N  
ANISOU   26  NZ  LYS A 376     7044  11060  11059  -1902  -2162    410       N  
ATOM     27  N   ILE A 377       9.088  70.576  24.568  1.00 57.11           N  
ANISOU   27  N   ILE A 377     5400   7954   8343   -774  -1489    470       N  
ATOM     28  CA  ILE A 377       9.574  71.951  24.695  1.00 57.04           C  
ANISOU   28  CA  ILE A 377     5411   7896   8364   -555  -1432    510       C  
ATOM     29  C   ILE A 377       8.446  72.935  25.047  1.00 58.80           C  
ANISOU   29  C   ILE A 377     5345   8218   8778   -426  -1424    563       C  
ATOM     30  O   ILE A 377       8.686  73.910  25.752  1.00 58.07           O  
ANISOU   30  O   ILE A 377     5232   8076   8754   -267  -1289    569       O  
ATOM     31  CB  ILE A 377      10.378  72.398  23.439  1.00 56.37           C  
ANISOU   31  CB  ILE A 377     5518   7755   8142   -489  -1569    545       C  
ATOM     32  CG1 ILE A 377      11.078  73.732  23.673  1.00 55.28           C  
ANISOU   32  CG1 ILE A 377     5445   7535   8020   -283  -1482    579       C  
ATOM     33  CG2 ILE A 377       9.492  72.486  22.204  1.00 58.94           C  
ANISOU   33  CG2 ILE A 377     5729   8193   8472   -516  -1805    607       C  
ATOM     34  CD1 ILE A 377      12.144  73.694  24.746  1.00 53.68           C  
ANISOU   34  CD1 ILE A 377     5395   7220   7781   -261  -1274    519       C  
ATOM     35  N   GLU A 378       7.220  72.640  24.608  1.00 62.35           N  
ANISOU   35  N   GLU A 378     5568   8804   9318   -500  -1559    594       N  
ATOM     36  CA  GLU A 378       6.053  73.478  24.897  1.00 64.64           C  
ANISOU   36  CA  GLU A 378     5550   9202   9808   -380  -1560    646       C  
ATOM     37  C   GLU A 378       5.684  73.454  26.384  1.00 63.56           C  
ANISOU   37  C   GLU A 378     5278   9077   9796   -376  -1323    596       C  
ATOM     38  O   GLU A 378       4.972  74.337  26.858  1.00 63.72           O  
ANISOU   38  O   GLU A 378     5080   9148   9981   -233  -1254    622       O  
ATOM     39  CB  GLU A 378       4.835  73.043  24.060  1.00 69.15           C  
ANISOU   39  CB  GLU A 378     5898   9930  10443   -484  -1774    691       C  
ATOM     40  CG  GLU A 378       5.001  73.221  22.553  1.00 70.91           C  
ANISOU   40  CG  GLU A 378     6221  10168  10551   -476  -2028    754       C  
ATOM     41  CD  GLU A 378       5.863  72.145  21.879  1.00 70.70           C  
ANISOU   41  CD  GLU A 378     6482  10074  10306   -655  -2097    699       C  
ATOM     42  OE1 GLU A 378       6.294  71.169  22.540  1.00 68.47           O  
ANISOU   42  OE1 GLU A 378     6314   9732   9969   -794  -1966    617       O  
ATOM     43  OE2 GLU A 378       6.106  72.277  20.662  1.00 72.14           O  
ANISOU   43  OE2 GLU A 378     6780  10260  10367   -655  -2285    741       O  
ATOM     44  N   ASP A 379       6.169  72.445  27.114  1.00 61.50           N  
ANISOU   44  N   ASP A 379     5150   8764   9452   -530  -1194    525       N  
ATOM     45  CA  ASP A 379       6.001  72.384  28.571  1.00 59.83           C  
ANISOU   45  CA  ASP A 379     4865   8550   9317   -538   -955    476       C  
ATOM     46  C   ASP A 379       6.731  73.510  29.298  1.00 58.11           C  
ANISOU   46  C   ASP A 379     4739   8232   9107   -344   -792    464       C  
ATOM     47  O   ASP A 379       6.456  73.745  30.475  1.00 59.63           O  
ANISOU   47  O   ASP A 379     4841   8435   9379   -315   -596    427       O  
ATOM     48  CB  ASP A 379       6.490  71.043  29.127  1.00 58.61           C  
ANISOU   48  CB  ASP A 379     4874   8344   9049   -745   -871    418       C  
ATOM     49  CG  ASP A 379       5.624  69.874  28.687  1.00 60.34           C  
ANISOU   49  CG  ASP A 379     4980   8660   9286   -962   -988    416       C  
ATOM     50  OD1 ASP A 379       6.159  68.758  28.541  1.00 59.56           O  
ANISOU   50  OD1 ASP A 379     5071   8494   9062  -1127  -1011    382       O  
ATOM     51  OD2 ASP A 379       4.410  70.067  28.505  1.00 61.80           O  
ANISOU   51  OD2 ASP A 379     4883   8983   9614   -968  -1054    447       O  
ATOM     52  N   PHE A 380       7.653  74.187  28.609  1.00 54.84           N  
ANISOU   52  N   PHE A 380     4510   7722   8604   -226   -867    489       N  
ATOM     53  CA  PHE A 380       8.398  75.302  29.182  1.00 54.43           C  
ANISOU   53  CA  PHE A 380     4560   7565   8553    -50   -731    478       C  
ATOM     54  C   PHE A 380       8.012  76.619  28.560  1.00 56.38           C  
ANISOU   54  C   PHE A 380     4697   7819   8906    151   -815    544       C  
ATOM     55  O   PHE A 380       7.580  76.676  27.418  1.00 56.33           O  
ANISOU   55  O   PHE A 380     4626   7868   8908    161  -1017    610       O  
ATOM     56  CB  PHE A 380       9.904  75.140  28.961  1.00 50.97           C  
ANISOU   56  CB  PHE A 380     4437   6994   7933    -65   -728    457       C  
ATOM     57  CG  PHE A 380      10.477  73.922  29.608  1.00 50.41           C  
ANISOU   57  CG  PHE A 380     4508   6888   7755   -236   -640    399       C  
ATOM     58  CD1 PHE A 380      10.972  73.971  30.906  1.00 49.79           C  
ANISOU   58  CD1 PHE A 380     4499   6756   7661   -231   -440    349       C  
ATOM     59  CD2 PHE A 380      10.507  72.709  28.929  1.00 51.58           C  
ANISOU   59  CD2 PHE A 380     4726   7054   7817   -404   -761    395       C  
ATOM     60  CE1 PHE A 380      11.485  72.829  31.513  1.00 49.11           C  
ANISOU   60  CE1 PHE A 380     4545   6635   7478   -385   -369    310       C  
ATOM     61  CE2 PHE A 380      11.038  71.565  29.528  1.00 50.19           C  
ANISOU   61  CE2 PHE A 380     4688   6829   7551   -554   -680    348       C  
ATOM     62  CZ  PHE A 380      11.513  71.629  30.830  1.00 48.64           C  
ANISOU   62  CZ  PHE A 380     4552   6581   7346   -540   -487    312       C  
ATOM     63  N   GLU A 381       8.230  77.675  29.329  1.00 57.45           N  
ANISOU   63  N   GLU A 381     4834   7885   9109    309   -659    525       N  
ATOM     64  CA  GLU A 381       8.184  79.026  28.835  1.00 58.89           C  
ANISOU   64  CA  GLU A 381     4985   8018   9370    518   -709    583       C  
ATOM     65  C   GLU A 381       9.601  79.548  28.748  1.00 56.59           C  
ANISOU   65  C   GLU A 381     4982   7575   8942    574   -672    572       C  
ATOM     66  O   GLU A 381      10.308  79.615  29.749  1.00 53.05           O  
ANISOU   66  O   GLU A 381     4655   7052   8447    566   -494    502       O  
ATOM     67  CB  GLU A 381       7.386  79.902  29.775  1.00 62.76           C  
ANISOU   67  CB  GLU A 381     5270   8526  10048    661   -547    562       C  
ATOM     68  CG  GLU A 381       7.340  81.338  29.299  1.00 66.96           C  
ANISOU   68  CG  GLU A 381     5781   8984  10677    890   -592    624       C  
ATOM     69  CD  GLU A 381       6.077  82.041  29.710  1.00 72.02           C  
ANISOU   69  CD  GLU A 381     6123   9692  11550   1035   -527    637       C  
ATOM     70  OE1 GLU A 381       5.522  81.689  30.774  1.00 75.79           O  
ANISOU   70  OE1 GLU A 381     6461  10232  12101    983   -352    565       O  
ATOM     71  OE2 GLU A 381       5.641  82.942  28.966  1.00 77.27           O  
ANISOU   71  OE2 GLU A 381     6691  10345  12322   1201   -648    724       O  
ATOM     72  N   LEU A 382      10.003  79.918  27.541  1.00 56.11           N  
ANISOU   72  N   LEU A 382     5026   7476   8814    624   -843    643       N  
ATOM     73  CA  LEU A 382      11.314  80.468  27.290  1.00 54.07           C  
ANISOU   73  CA  LEU A 382     5028   7083   8433    675   -825    644       C  
ATOM     74  C   LEU A 382      11.251  81.989  27.503  1.00 55.83           C  
ANISOU   74  C   LEU A 382     5219   7219   8771    886   -758    674       C  
ATOM     75  O   LEU A 382      10.841  82.748  26.600  1.00 56.56           O  
ANISOU   75  O   LEU A 382     5254   7308   8925   1005   -896    766       O  
ATOM     76  CB  LEU A 382      11.736  80.121  25.864  1.00 54.35           C  
ANISOU   76  CB  LEU A 382     5193   7123   8334    617  -1031    707       C  
ATOM     77  CG  LEU A 382      11.525  78.672  25.398  1.00 54.71           C  
ANISOU   77  CG  LEU A 382     5239   7260   8287    420  -1137    687       C  
ATOM     78  CD1 LEU A 382      12.046  78.522  23.982  1.00 54.89           C  
ANISOU   78  CD1 LEU A 382     5420   7269   8163    383  -1322    741       C  
ATOM     79  CD2 LEU A 382      12.188  77.663  26.332  1.00 52.94           C  
ANISOU   79  CD2 LEU A 382     5126   7005   7982    282   -990    593       C  
ATOM     80  N   HIS A 383      11.613  82.436  28.702  1.00 54.98           N  
ANISOU   80  N   HIS A 383     5152   7040   8697    931   -550    598       N  
ATOM     81  CA  HIS A 383      11.491  83.860  29.049  1.00 56.58           C  
ANISOU   81  CA  HIS A 383     5325   7149   9023   1126   -460    607       C  
ATOM     82  C   HIS A 383      12.546  84.728  28.370  1.00 55.59           C  
ANISOU   82  C   HIS A 383     5421   6887   8814   1203   -512    653       C  
ATOM     83  O   HIS A 383      12.278  85.881  28.037  1.00 57.49           O  
ANISOU   83  O   HIS A 383     5630   7057   9157   1369   -537    712       O  
ATOM     84  CB  HIS A 383      11.585  84.068  30.556  1.00 56.28           C  
ANISOU   84  CB  HIS A 383     5282   7074   9027   1135   -216    499       C  
ATOM     85  CG  HIS A 383      10.453  83.470  31.319  1.00 57.55           C  
ANISOU   85  CG  HIS A 383     5209   7359   9296   1087   -130    457       C  
ATOM     86  ND1 HIS A 383       9.276  84.144  31.538  1.00 60.65           N  
ANISOU   86  ND1 HIS A 383     5360   7795   9889   1226    -86    470       N  
ATOM     87  CD2 HIS A 383      10.326  82.277  31.941  1.00 58.60           C  
ANISOU   87  CD2 HIS A 383     5312   7581   9369    915    -70    403       C  
ATOM     88  CE1 HIS A 383       8.460  83.386  32.247  1.00 61.90           C  
ANISOU   88  CE1 HIS A 383     5340   8072  10104   1135      0    423       C  
ATOM     89  NE2 HIS A 383       9.071  82.246  32.500  1.00 60.46           N  
ANISOU   89  NE2 HIS A 383     5288   7918   9763    941      9    385       N  
ATOM     90  N   LYS A 384      13.744  84.193  28.186  1.00 51.87           N  
ANISOU   90  N   LYS A 384     5170   6372   8164   1086   -520    628       N  
ATOM     91  CA  LYS A 384      14.848  84.962  27.621  1.00 52.35           C  
ANISOU   91  CA  LYS A 384     5447   6306   8135   1137   -545    663       C  
ATOM     92  C   LYS A 384      15.787  84.074  26.840  1.00 52.99           C  
ANISOU   92  C   LYS A 384     5701   6400   8030    997   -643    673       C  
ATOM     93  O   LYS A 384      15.877  82.869  27.105  1.00 52.26           O  
ANISOU   93  O   LYS A 384     5608   6380   7865    854   -634    622       O  
ATOM     94  CB  LYS A 384      15.691  85.603  28.729  1.00 52.44           C  
ANISOU   94  CB  LYS A 384     5583   6202   8137   1165   -349    579       C  
ATOM     95  CG  LYS A 384      14.972  86.580  29.646  1.00 56.41           C  
ANISOU   95  CG  LYS A 384     5962   6660   8808   1305   -209    542       C  
ATOM     96  CD  LYS A 384      14.633  87.884  28.942  1.00 58.90           C  
ANISOU   96  CD  LYS A 384     6258   6884   9235   1487   -276    629       C  
ATOM     97  CE  LYS A 384      13.778  88.759  29.841  1.00 63.80           C  
ANISOU   97  CE  LYS A 384     6731   7465  10044   1635   -132    586       C  
ATOM     98  NZ  LYS A 384      14.072  90.191  29.585  1.00 66.30           N  
ANISOU   98  NZ  LYS A 384     7147   7613  10428   1795   -114    626       N  
ATOM     99  N   MET A 385      16.516  84.679  25.905  1.00 52.52           N  
ANISOU   99  N   MET A 385     5797   6263   7892   1037   -723    737       N  
ATOM    100  CA  MET A 385      17.679  84.046  25.329  1.00 53.34           C  
ANISOU  100  CA  MET A 385     6099   6349   7817    921   -761    728       C  
ATOM    101  C   MET A 385      18.905  84.637  25.995  1.00 51.97           C  
ANISOU  101  C   MET A 385     6090   6056   7597    932   -614    675       C  
ATOM    102  O   MET A 385      19.171  85.842  25.883  1.00 52.25           O  
ANISOU  102  O   MET A 385     6188   5990   7675   1040   -588    712       O  
ATOM    103  CB  MET A 385      17.764  84.241  23.822  1.00 55.88           C  
ANISOU  103  CB  MET A 385     6498   6673   8058    933   -938    829       C  
ATOM    104  CG  MET A 385      18.895  83.409  23.241  1.00 55.71           C  
ANISOU  104  CG  MET A 385     6666   6650   7850    800   -962    804       C  
ATOM    105  SD  MET A 385      19.338  83.909  21.590  1.00 62.49           S  
ANISOU  105  SD  MET A 385     7679   7480   8585    819  -1117    913       S  
ATOM    106  CE  MET A 385      18.103  83.017  20.688  1.00 65.90           C  
ANISOU  106  CE  MET A 385     7975   8058   9004    757  -1319    959       C  
ATOM    107  N   LEU A 386      19.642  83.773  26.679  1.00 48.30           N  
ANISOU  107  N   LEU A 386     5696   5604   7049    817   -527    594       N  
ATOM    108  CA  LEU A 386      20.760  84.181  27.499  1.00 48.57           C  
ANISOU  108  CA  LEU A 386     5861   5549   7043    808   -387    533       C  
ATOM    109  C   LEU A 386      22.008  84.288  26.643  1.00 48.36           C  
ANISOU  109  C   LEU A 386     6022   5464   6889    771   -430    562       C  
ATOM    110  O   LEU A 386      22.922  85.036  26.967  1.00 46.20           O  
ANISOU  110  O   LEU A 386     5860   5098   6595    791   -346    544       O  
ATOM    111  CB  LEU A 386      20.987  83.151  28.622  1.00 48.33           C  
ANISOU  111  CB  LEU A 386     5817   5566   6978    700   -287    444       C  
ATOM    112  CG  LEU A 386      19.815  82.957  29.588  1.00 49.18           C  
ANISOU  112  CG  LEU A 386     5747   5739   7200    713   -218    406       C  
ATOM    113  CD1 LEU A 386      20.030  81.762  30.497  1.00 48.44           C  
ANISOU  113  CD1 LEU A 386     5658   5699   7046    585   -146    339       C  
ATOM    114  CD2 LEU A 386      19.597  84.226  30.406  1.00 52.12           C  
ANISOU  114  CD2 LEU A 386     6088   6037   7676    829    -95    377       C  
ATOM    115  N   GLY A 387      22.053  83.509  25.564  1.00 47.28           N  
ANISOU  115  N   GLY A 387     5920   5384   6661    706   -552    602       N  
ATOM    116  CA  GLY A 387      23.194  83.543  24.657  1.00 48.04           C  
ANISOU  116  CA  GLY A 387     6188   5436   6628    667   -586    629       C  
ATOM    117  C   GLY A 387      22.994  82.660  23.441  1.00 50.12           C  
ANISOU  117  C   GLY A 387     6476   5772   6794    598   -725    666       C  
ATOM    118  O   GLY A 387      22.182  81.717  23.473  1.00 45.96           O  
ANISOU  118  O   GLY A 387     5846   5332   6283    544   -782    648       O  
ATOM    119  N   LYS A 388      23.721  82.983  22.370  1.00 50.69           N  
ANISOU  119  N   LYS A 388     6688   5808   6761    592   -776    715       N  
ATOM    120  CA  LYS A 388      23.802  82.132  21.179  1.00 53.00           C  
ANISOU  120  CA  LYS A 388     7051   6159   6925    511   -887    735       C  
ATOM    121  C   LYS A 388      25.176  82.249  20.520  1.00 55.16           C  
ANISOU  121  C   LYS A 388     7511   6379   7066    472   -846    736       C  
ATOM    122  O   LYS A 388      25.937  83.172  20.816  1.00 55.13           O  
ANISOU  122  O   LYS A 388     7573   6294   7079    516   -759    746       O  
ATOM    123  CB  LYS A 388      22.703  82.468  20.177  1.00 55.98           C  
ANISOU  123  CB  LYS A 388     7367   6588   7313    555  -1052    829       C  
ATOM    124  CG  LYS A 388      22.869  83.807  19.477  1.00 59.51           C  
ANISOU  124  CG  LYS A 388     7891   6964   7755    649  -1090    930       C  
ATOM    125  CD  LYS A 388      21.716  84.038  18.528  1.00 62.52           C  
ANISOU  125  CD  LYS A 388     8198   7408   8148    693  -1272   1031       C  
ATOM    126  CE  LYS A 388      21.935  85.257  17.650  1.00 65.20           C  
ANISOU  126  CE  LYS A 388     8644   7675   8452    774  -1330   1148       C  
ATOM    127  NZ  LYS A 388      20.713  85.509  16.841  1.00 67.15           N  
ANISOU  127  NZ  LYS A 388     8795   7988   8730    831  -1521   1257       N  
ATOM    128  N   GLY A 389      25.484  81.304  19.637  1.00 53.35           N  
ANISOU  128  N   GLY A 389     7365   6196   6709    383   -902    720       N  
ATOM    129  CA  GLY A 389      26.810  81.217  19.029  1.00 52.23           C  
ANISOU  129  CA  GLY A 389     7389   6016   6440    336   -845    705       C  
ATOM    130  C   GLY A 389      27.009  79.845  18.422  1.00 50.90           C  
ANISOU  130  C   GLY A 389     7279   5900   6157    233   -879    648       C  
ATOM    131  O   GLY A 389      26.061  79.223  18.007  1.00 50.57           O  
ANISOU  131  O   GLY A 389     7187   5924   6103    197   -990    652       O  
ATOM    132  N   SER A 390      28.245  79.363  18.403  1.00 54.08           N  
ANISOU  132  N   SER A 390     7786   6272   6487    187   -779    591       N  
ATOM    133  CA  SER A 390      28.550  78.048  17.833  1.00 53.63           C  
ANISOU  133  CA  SER A 390     7802   6246   6327     97   -790    525       C  
ATOM    134  C   SER A 390      27.945  76.893  18.639  1.00 51.40           C  
ANISOU  134  C   SER A 390     7424   5992   6112     53   -797    459       C  
ATOM    135  O   SER A 390      27.802  75.781  18.125  1.00 52.32           O  
ANISOU  135  O   SER A 390     7585   6134   6157    -23   -839    411       O  
ATOM    136  CB  SER A 390      30.059  77.862  17.762  1.00 52.69           C  
ANISOU  136  CB  SER A 390     7793   6080   6143     77   -663    479       C  
ATOM    137  OG  SER A 390      30.603  77.895  19.066  1.00 52.15           O  
ANISOU  137  OG  SER A 390     7660   5976   6178    104   -557    441       O  
ATOM    138  N   PHE A 391      27.587  77.162  19.895  1.00 49.67           N  
ANISOU  138  N   PHE A 391     7084   5763   6023     95   -751    455       N  
ATOM    139  CA  PHE A 391      26.978  76.169  20.801  1.00 46.85           C  
ANISOU  139  CA  PHE A 391     6631   5432   5737     51   -745    404       C  
ATOM    140  C   PHE A 391      25.458  76.065  20.658  1.00 47.14           C  
ANISOU  140  C   PHE A 391     6545   5537   5827     38   -863    434       C  
ATOM    141  O   PHE A 391      24.825  75.275  21.344  1.00 48.18           O  
ANISOU  141  O   PHE A 391     6589   5697   6018     -9   -863    398       O  
ATOM    142  CB  PHE A 391      27.322  76.517  22.259  1.00 46.65           C  
ANISOU  142  CB  PHE A 391     6538   5372   5813     93   -630    384       C  
ATOM    143  CG  PHE A 391      26.982  77.942  22.637  1.00 45.78           C  
ANISOU  143  CG  PHE A 391     6364   5246   5783    184   -617    437       C  
ATOM    144  CD1 PHE A 391      27.936  78.943  22.538  1.00 48.19           C  
ANISOU  144  CD1 PHE A 391     6746   5494   6069    232   -555    459       C  
ATOM    145  CD2 PHE A 391      25.695  78.285  23.050  1.00 46.80           C  
ANISOU  145  CD2 PHE A 391     6355   5414   6012    220   -662    463       C  
ATOM    146  CE1 PHE A 391      27.626  80.269  22.862  1.00 49.53           C  
ANISOU  146  CE1 PHE A 391     6873   5629   6314    314   -540    504       C  
ATOM    147  CE2 PHE A 391      25.383  79.592  23.387  1.00 49.17           C  
ANISOU  147  CE2 PHE A 391     6601   5685   6394    314   -640    506       C  
ATOM    148  CZ  PHE A 391      26.352  80.589  23.290  1.00 48.82           C  
ANISOU  148  CZ  PHE A 391     6653   5568   6327    362   -580    526       C  
ATOM    149  N   GLY A 392      24.869  76.857  19.774  1.00 46.00           N  
ANISOU  149  N   GLY A 392     6390   5423   5663     77   -967    506       N  
ATOM    150  CA  GLY A 392      23.425  76.880  19.608  1.00 45.49           C  
ANISOU  150  CA  GLY A 392     6188   5432   5662     76  -1091    547       C  
ATOM    151  C   GLY A 392      22.801  78.047  20.355  1.00 47.11           C  
ANISOU  151  C   GLY A 392     6258   5632   6009    188  -1069    599       C  
ATOM    152  O   GLY A 392      23.380  79.127  20.383  1.00 46.65           O  
ANISOU  152  O   GLY A 392     6252   5511   5959    271  -1016    637       O  
ATOM    153  N   LYS A 393      21.610  77.844  20.923  1.00 46.84           N  
ANISOU  153  N   LYS A 393     6051   5658   6087    188  -1104    600       N  
ATOM    154  CA  LYS A 393      20.931  78.856  21.753  1.00 46.86           C  
ANISOU  154  CA  LYS A 393     5907   5655   6241    298  -1062    634       C  
ATOM    155  C   LYS A 393      20.714  78.302  23.167  1.00 46.99           C  
ANISOU  155  C   LYS A 393     5826   5681   6347    266   -942    563       C  
ATOM    156  O   LYS A 393      20.393  77.118  23.327  1.00 44.45           O  
ANISOU  156  O   LYS A 393     5472   5407   6008    160   -958    518       O  
ATOM    157  CB  LYS A 393      19.574  79.196  21.166  1.00 50.71           C  
ANISOU  157  CB  LYS A 393     6247   6221   6798    338  -1209    707       C  
ATOM    158  CG  LYS A 393      19.620  79.784  19.766  1.00 52.58           C  
ANISOU  158  CG  LYS A 393     6573   6460   6945    371  -1349    795       C  
ATOM    159  CD  LYS A 393      18.239  79.861  19.143  1.00 58.52           C  
ANISOU  159  CD  LYS A 393     7169   7310   7755    388  -1524    868       C  
ATOM    160  CE  LYS A 393      18.252  80.726  17.878  1.00 61.97           C  
ANISOU  160  CE  LYS A 393     7690   7739   8117    451  -1662    979       C  
ATOM    161  NZ  LYS A 393      17.089  80.462  16.987  1.00 64.79           N  
ANISOU  161  NZ  LYS A 393     7939   8211   8467    420  -1872   1045       N  
ATOM    162  N   VAL A 394      20.907  79.154  24.178  1.00 43.77           N  
ANISOU  162  N   VAL A 394     5384   5220   6023    350   -820    552       N  
ATOM    163  CA  VAL A 394      20.632  78.831  25.568  1.00 42.06           C  
ANISOU  163  CA  VAL A 394     5076   5016   5888    331   -701    492       C  
ATOM    164  C   VAL A 394      19.565  79.794  26.090  1.00 43.70           C  
ANISOU  164  C   VAL A 394     5116   5242   6245    438   -676    519       C  
ATOM    165  O   VAL A 394      19.742  81.026  26.013  1.00 45.60           O  
ANISOU  165  O   VAL A 394     5379   5419   6527    552   -654    554       O  
ATOM    166  CB  VAL A 394      21.919  78.938  26.402  1.00 40.48           C  
ANISOU  166  CB  VAL A 394     5000   4737   5640    325   -563    441       C  
ATOM    167  CG1 VAL A 394      21.646  78.641  27.871  1.00 41.64           C  
ANISOU  167  CG1 VAL A 394     5068   4898   5852    300   -441    385       C  
ATOM    168  CG2 VAL A 394      22.981  77.996  25.868  1.00 40.05           C  
ANISOU  168  CG2 VAL A 394     5097   4663   5457    237   -582    417       C  
ATOM    169  N   PHE A 395      18.456  79.243  26.594  1.00 43.09           N  
ANISOU  169  N   PHE A 395     4870   5247   6253    401   -676    502       N  
ATOM    170  CA  PHE A 395      17.311  80.021  27.076  1.00 43.00           C  
ANISOU  170  CA  PHE A 395     4668   5269   6398    501   -649    522       C  
ATOM    171  C   PHE A 395      17.141  79.905  28.589  1.00 43.22           C  
ANISOU  171  C   PHE A 395     4629   5301   6490    486   -475    449       C  
ATOM    172  O   PHE A 395      17.463  78.858  29.179  1.00 40.75           O  
ANISOU  172  O   PHE A 395     4360   5007   6114    366   -420    398       O  
ATOM    173  CB  PHE A 395      16.014  79.499  26.434  1.00 45.61           C  
ANISOU  173  CB  PHE A 395     4824   5716   6790    466   -787    564       C  
ATOM    174  CG  PHE A 395      16.006  79.558  24.933  1.00 47.96           C  
ANISOU  174  CG  PHE A 395     5175   6030   7015    468   -975    638       C  
ATOM    175  CD1 PHE A 395      16.322  78.434  24.173  1.00 48.26           C  
ANISOU  175  CD1 PHE A 395     5311   6101   6922    331  -1071    625       C  
ATOM    176  CD2 PHE A 395      15.658  80.735  24.273  1.00 50.39           C  
ANISOU  176  CD2 PHE A 395     5444   6318   7383    608  -1056    723       C  
ATOM    177  CE1 PHE A 395      16.301  78.483  22.781  1.00 49.80           C  
ANISOU  177  CE1 PHE A 395     5570   6319   7033    322  -1243    689       C  
ATOM    178  CE2 PHE A 395      15.628  80.792  22.887  1.00 52.44           C  
ANISOU  178  CE2 PHE A 395     5763   6600   7560    603  -1237    800       C  
ATOM    179  CZ  PHE A 395      15.955  79.658  22.138  1.00 53.07           C  
ANISOU  179  CZ  PHE A 395     5945   6723   7493    454  -1329    779       C  
ATOM    180  N   LEU A 396      16.643  80.976  29.213  1.00 43.30           N  
ANISOU  180  N   LEU A 396     4543   5287   6622    609   -387    446       N  
ATOM    181  CA  LEU A 396      16.129  80.924  30.577  1.00 43.29           C  
ANISOU  181  CA  LEU A 396     4436   5313   6698    602   -227    380       C  
ATOM    182  C   LEU A 396      14.704  80.427  30.425  1.00 45.13           C  
ANISOU  182  C   LEU A 396     4440   5667   7039    579   -286    403       C  
ATOM    183  O   LEU A 396      13.887  81.085  29.765  1.00 46.80           O  
ANISOU  183  O   LEU A 396     4519   5906   7357    684   -375    463       O  
ATOM    184  CB  LEU A 396      16.133  82.295  31.261  1.00 43.83           C  
ANISOU  184  CB  LEU A 396     4495   5302   6856    745   -101    356       C  
ATOM    185  CG  LEU A 396      15.366  82.434  32.588  1.00 45.68           C  
ANISOU  185  CG  LEU A 396     4593   5571   7189    762     69    288       C  
ATOM    186  CD1 LEU A 396      15.869  81.433  33.617  1.00 44.74           C  
ANISOU  186  CD1 LEU A 396     4552   5479   6966    614    174    220       C  
ATOM    187  CD2 LEU A 396      15.469  83.861  33.145  1.00 45.68           C  
ANISOU  187  CD2 LEU A 396     4617   5470   7268    910    191    256       C  
ATOM    188  N   ALA A 397      14.422  79.265  31.015  1.00 44.07           N  
ANISOU  188  N   ALA A 397     4260   5604   6879    439   -242    363       N  
ATOM    189  CA  ALA A 397      13.140  78.573  30.837  1.00 45.89           C  
ANISOU  189  CA  ALA A 397     4281   5959   7196    374   -305    382       C  
ATOM    190  C   ALA A 397      12.487  78.224  32.167  1.00 47.75           C  
ANISOU  190  C   ALA A 397     4391   6251   7500    320   -135    323       C  
ATOM    191  O   ALA A 397      13.165  77.865  33.136  1.00 47.97           O  
ANISOU  191  O   ALA A 397     4541   6239   7446    252     -4    267       O  
ATOM    192  CB  ALA A 397      13.346  77.296  30.032  1.00 45.46           C  
ANISOU  192  CB  ALA A 397     4299   5940   7032    218   -443    397       C  
ATOM    193  N   GLU A 398      11.167  78.301  32.206  1.00 49.50           N  
ANISOU  193  N   GLU A 398     4366   6574   7868    344   -139    339       N  
ATOM    194  CA  GLU A 398      10.407  77.967  33.403  1.00 50.54           C  
ANISOU  194  CA  GLU A 398     4352   6776   8072    288     27    286       C  
ATOM    195  C   GLU A 398       9.542  76.778  33.084  1.00 51.33           C  
ANISOU  195  C   GLU A 398     4309   6994   8196    131    -59    306       C  
ATOM    196  O   GLU A 398       8.840  76.786  32.065  1.00 52.26           O  
ANISOU  196  O   GLU A 398     4290   7179   8384    149   -225    364       O  
ATOM    197  CB  GLU A 398       9.510  79.125  33.806  1.00 52.37           C  
ANISOU  197  CB  GLU A 398     4385   7030   8481    455    124    279       C  
ATOM    198  CG  GLU A 398       8.827  78.921  35.144  1.00 53.58           C  
ANISOU  198  CG  GLU A 398     4408   7249   8701    409    336    212       C  
ATOM    199  CD  GLU A 398       7.757  79.964  35.428  1.00 56.01           C  
ANISOU  199  CD  GLU A 398     4477   7595   9209    576    427    204       C  
ATOM    200  OE1 GLU A 398       7.804  81.075  34.858  1.00 55.88           O  
ANISOU  200  OE1 GLU A 398     4452   7510   9267    757    369    238       O  
ATOM    201  OE2 GLU A 398       6.870  79.661  36.234  1.00 57.46           O  
ANISOU  201  OE2 GLU A 398     4481   7873   9477    528    565    165       O  
ATOM    202  N   PHE A 399       9.586  75.750  33.924  1.00 50.52           N  
ANISOU  202  N   PHE A 399     4243   6917   8032    -29     42    264       N  
ATOM    203  CA  PHE A 399       8.802  74.558  33.640  1.00 52.96           C  
ANISOU  203  CA  PHE A 399     4435   7327   8360   -200    -35    280       C  
ATOM    204  C   PHE A 399       7.359  74.844  33.972  1.00 55.85           C  
ANISOU  204  C   PHE A 399     4490   7819   8908   -172     23    284       C  
ATOM    205  O   PHE A 399       7.041  75.085  35.120  1.00 55.28           O  
ANISOU  205  O   PHE A 399     4346   7768   8888   -157    222    238       O  
ATOM    206  CB  PHE A 399       9.269  73.344  34.438  1.00 51.86           C  
ANISOU  206  CB  PHE A 399     4436   7164   8104   -386     56    244       C  
ATOM    207  CG  PHE A 399       8.391  72.146  34.253  1.00 52.27           C  
ANISOU  207  CG  PHE A 399     4363   7310   8187   -572     -1    257       C  
ATOM    208  CD1 PHE A 399       7.482  71.775  35.233  1.00 55.30           C  
ANISOU  208  CD1 PHE A 399     4580   7781   8648   -664    145    235       C  
ATOM    209  CD2 PHE A 399       8.434  71.420  33.078  1.00 52.38           C  
ANISOU  209  CD2 PHE A 399     4422   7326   8152   -663   -201    287       C  
ATOM    210  CE1 PHE A 399       6.648  70.685  35.052  1.00 56.36           C  
ANISOU  210  CE1 PHE A 399     4592   8002   8818   -849     92    248       C  
ATOM    211  CE2 PHE A 399       7.609  70.324  32.888  1.00 53.72           C  
ANISOU  211  CE2 PHE A 399     4481   7578   8352   -848   -260    293       C  
ATOM    212  CZ  PHE A 399       6.718  69.954  33.877  1.00 56.05           C  
ANISOU  212  CZ  PHE A 399     4606   7957   8732   -944   -115    276       C  
ATOM    213  N   LYS A 400       6.505  74.826  32.954  1.00 61.10           N  
ANISOU  213  N   LYS A 400     4972   8572   9668   -165   -150    338       N  
ATOM    214  CA  LYS A 400       5.066  75.008  33.110  1.00 65.46           C  
ANISOU  214  CA  LYS A 400     5195   9264  10412   -145   -126    351       C  
ATOM    215  C   LYS A 400       4.706  76.112  34.085  1.00 68.36           C  
ANISOU  215  C   LYS A 400     5440   9627  10904     22     79    315       C  
ATOM    216  O   LYS A 400       5.275  77.198  34.049  1.00 68.12           O  
ANISOU  216  O   LYS A 400     5507   9499  10873    201    105    314       O  
ATOM    217  CB  LYS A 400       4.404  73.700  33.561  1.00 67.14           C  
ANISOU  217  CB  LYS A 400     5308   9575  10627   -376    -84    331       C  
ATOM    218  CG  LYS A 400       4.384  72.624  32.508  1.00 68.02           C  
ANISOU  218  CG  LYS A 400     5467   9714  10663   -547   -299    364       C  
ATOM    219  CD  LYS A 400       3.401  71.528  32.872  1.00 69.14           C  
ANISOU  219  CD  LYS A 400     5432   9973  10863   -759   -268    352       C  
ATOM    220  CE  LYS A 400       3.013  70.746  31.634  1.00 70.19           C  
ANISOU  220  CE  LYS A 400     5524  10165  10977   -896   -515    390       C  
ATOM    221  NZ  LYS A 400       2.431  69.437  32.010  1.00 71.89           N  
ANISOU  221  NZ  LYS A 400     5676  10445  11194  -1150   -481    368       N  
ATOM    222  N   LYS A 401       3.758  75.796  34.960  1.00 74.16           N  
ANISOU  222  N   LYS A 401     5967  10468  11743    -46    232    281       N  
ATOM    223  CA  LYS A 401       3.265  76.693  35.974  1.00 78.70           C  
ANISOU  223  CA  LYS A 401     6404  11057  12442     88    456    232       C  
ATOM    224  C   LYS A 401       4.390  76.977  36.958  1.00 77.64           C  
ANISOU  224  C   LYS A 401     6543  10793  12163    107    635    164       C  
ATOM    225  O   LYS A 401       4.680  78.134  37.261  1.00 77.85           O  
ANISOU  225  O   LYS A 401     6613  10740  12227    289    728    135       O  
ATOM    226  CB  LYS A 401       2.096  76.027  36.720  1.00 82.33           C  
ANISOU  226  CB  LYS A 401     6607  11664  13008    -43    591    205       C  
ATOM    227  CG  LYS A 401       0.974  75.519  35.826  1.00 85.00           C  
ANISOU  227  CG  LYS A 401     6667  12150  13477   -116    411    268       C  
ATOM    228  CD  LYS A 401      -0.056  74.725  36.601  1.00 87.36           C  
ANISOU  228  CD  LYS A 401     6741  12590  13859   -286    553    240       C  
ATOM    229  CE  LYS A 401      -1.146  74.251  35.657  1.00 89.70           C  
ANISOU  229  CE  LYS A 401     6755  13037  14290   -366    353    304       C  
ATOM    230  NZ  LYS A 401      -2.284  73.609  36.371  1.00 93.10           N  
ANISOU  230  NZ  LYS A 401     6912  13621  14838   -519    496    281       N  
ATOM    231  N   THR A 402       5.039  75.903  37.409  1.00 74.46           N  
ANISOU  231  N   THR A 402     6332  10365  11594    -84    669    143       N  
ATOM    232  CA  THR A 402       5.818  75.905  38.645  1.00 71.17           C  
ANISOU  232  CA  THR A 402     6116   9874  11049   -120    871     77       C  
ATOM    233  C   THR A 402       6.741  77.084  38.692  1.00 70.03           C  
ANISOU  233  C   THR A 402     6143   9601  10864     59    899     52       C  
ATOM    234  O   THR A 402       6.984  77.735  37.683  1.00 74.16           O  
ANISOU  234  O   THR A 402     6681  10072  11423    188    745     95       O  
ATOM    235  CB  THR A 402       6.674  74.635  38.803  1.00 69.21           C  
ANISOU  235  CB  THR A 402     6102   9582  10611   -323    832     85       C  
ATOM    236  OG1 THR A 402       7.811  74.692  37.918  1.00 65.58           O  
ANISOU  236  OG1 THR A 402     5863   9012  10041   -281    661    116       O  
ATOM    237  CG2 THR A 402       5.840  73.384  38.530  1.00 69.92           C  
ANISOU  237  CG2 THR A 402     6053   9778  10735   -518    763    118       C  
ATOM    238  N   ASN A 403       7.288  77.367  39.852  1.00 66.68           N  
ANISOU  238  N   ASN A 403     5860   9121  10353     59   1093    -15       N  
ATOM    239  CA  ASN A 403       8.212  78.477  39.913  1.00 66.46           C  
ANISOU  239  CA  ASN A 403     6006   8965  10280    212   1118    -45       C  
ATOM    240  C   ASN A 403       9.663  78.018  39.662  1.00 60.12           C  
ANISOU  240  C   ASN A 403     5499   8061   9282    136   1013    -27       C  
ATOM    241  O   ASN A 403      10.593  78.626  40.162  1.00 59.42           O  
ANISOU  241  O   ASN A 403     5596   7876   9103    189   1085    -69       O  
ATOM    242  CB  ASN A 403       8.062  79.193  41.257  1.00 68.83           C  
ANISOU  242  CB  ASN A 403     6306   9253  10592    268   1377   -138       C  
ATOM    243  CG  ASN A 403       8.260  80.684  41.135  1.00 71.05           C  
ANISOU  243  CG  ASN A 403     6607   9433  10953    486   1414   -170       C  
ATOM    244  OD1 ASN A 403       7.376  81.394  40.674  1.00 74.05           O  
ANISOU  244  OD1 ASN A 403     6777   9839  11518    635   1400   -154       O  
ATOM    245  ND2 ASN A 403       9.424  81.165  41.536  1.00 71.14           N  
ANISOU  245  ND2 ASN A 403     6870   9327  10832    506   1455   -212       N  
ATOM    246  N   GLN A 404       9.848  76.972  38.856  1.00 56.91           N  
ANISOU  246  N   GLN A 404     5131   7675   8817     17    842     31       N  
ATOM    247  CA  GLN A 404      11.167  76.327  38.708  1.00 55.49           C  
ANISOU  247  CA  GLN A 404     5214   7409   8458    -71    763     45       C  
ATOM    248  C   GLN A 404      11.844  76.641  37.369  1.00 51.77           C  
ANISOU  248  C   GLN A 404     4836   6868   7965      8    564     95       C  
ATOM    249  O   GLN A 404      11.290  76.375  36.302  1.00 50.81           O  
ANISOU  249  O   GLN A 404     4605   6795   7906      4    409    146       O  
ATOM    250  CB  GLN A 404      11.014  74.823  38.867  1.00 56.44           C  
ANISOU  250  CB  GLN A 404     5351   7582   8509   -276    738     66       C  
ATOM    251  CG  GLN A 404      10.124  74.430  40.033  1.00 60.24           C  
ANISOU  251  CG  GLN A 404     5707   8154   9028   -373    922     32       C  
ATOM    252  CD  GLN A 404      10.888  74.089  41.289  1.00 61.28           C  
ANISOU  252  CD  GLN A 404     6030   8242   9009   -460   1069     -2       C  
ATOM    253  OE1 GLN A 404      10.409  73.305  42.104  1.00 66.59           O  
ANISOU  253  OE1 GLN A 404     6669   8976   9655   -601   1178     -7       O  
ATOM    254  NE2 GLN A 404      12.082  74.645  41.447  1.00 60.37           N  
ANISOU  254  NE2 GLN A 404     6119   8026   8790   -387   1065    -21       N  
ATOM    255  N   PHE A 405      13.054  77.191  37.444  1.00 49.76           N  
ANISOU  255  N   PHE A 405     4787   6506   7612     68    572     79       N  
ATOM    256  CA  PHE A 405      13.751  77.703  36.287  1.00 47.55           C  
ANISOU  256  CA  PHE A 405     4603   6153   7310    157    419    120       C  
ATOM    257  C   PHE A 405      14.955  76.825  35.921  1.00 45.39           C  
ANISOU  257  C   PHE A 405     4541   5823   6880     55    330    137       C  
ATOM    258  O   PHE A 405      15.543  76.171  36.789  1.00 44.19           O  
ANISOU  258  O   PHE A 405     4505   5655   6630    -43    411    109       O  
ATOM    259  CB  PHE A 405      14.187  79.143  36.550  1.00 48.01           C  
ANISOU  259  CB  PHE A 405     4718   6125   7398    316    497     91       C  
ATOM    260  CG  PHE A 405      13.055  80.090  36.689  1.00 51.84           C  
ANISOU  260  CG  PHE A 405     5000   6644   8053    448    567     81       C  
ATOM    261  CD1 PHE A 405      12.510  80.352  37.931  1.00 54.07           C  
ANISOU  261  CD1 PHE A 405     5203   6956   8384    455    765     12       C  
ATOM    262  CD2 PHE A 405      12.503  80.701  35.574  1.00 53.35           C  
ANISOU  262  CD2 PHE A 405     5076   6838   8356    568    434    143       C  
ATOM    263  CE1 PHE A 405      11.439  81.209  38.069  1.00 55.00           C  
ANISOU  263  CE1 PHE A 405     5121   7103   8673    588    843     -3       C  
ATOM    264  CE2 PHE A 405      11.431  81.563  35.701  1.00 56.56           C  
ANISOU  264  CE2 PHE A 405     5280   7273   8937    705    494    141       C  
ATOM    265  CZ  PHE A 405      10.894  81.813  36.953  1.00 57.24           C  
ANISOU  265  CZ  PHE A 405     5277   7386   9084    719    705     63       C  
ATOM    266  N   PHE A 406      15.286  76.804  34.628  1.00 43.14           N  
ANISOU  266  N   PHE A 406     4303   5511   6574     82    164    185       N  
ATOM    267  CA  PHE A 406      16.385  76.003  34.071  1.00 40.81           C  
ANISOU  267  CA  PHE A 406     4195   5162   6146      2     72    200       C  
ATOM    268  C   PHE A 406      17.010  76.771  32.914  1.00 40.20           C  
ANISOU  268  C   PHE A 406     4201   5025   6049    104    -41    235       C  
ATOM    269  O   PHE A 406      16.379  77.645  32.331  1.00 40.12           O  
ANISOU  269  O   PHE A 406     4084   5029   6129    212    -93    267       O  
ATOM    270  CB  PHE A 406      15.853  74.677  33.513  1.00 41.52           C  
ANISOU  270  CB  PHE A 406     4240   5312   6224   -134    -29    222       C  
ATOM    271  CG  PHE A 406      15.041  73.882  34.494  1.00 42.00           C  
ANISOU  271  CG  PHE A 406     4196   5442   6319   -249     69    201       C  
ATOM    272  CD1 PHE A 406      13.710  74.171  34.696  1.00 43.56           C  
ANISOU  272  CD1 PHE A 406     4167   5734   6648   -231    105    202       C  
ATOM    273  CD2 PHE A 406      15.624  72.863  35.224  1.00 41.32           C  
ANISOU  273  CD2 PHE A 406     4236   5326   6138   -371    128    185       C  
ATOM    274  CE1 PHE A 406      12.955  73.456  35.605  1.00 45.00           C  
ANISOU  274  CE1 PHE A 406     4249   5985   6862   -347    209    183       C  
ATOM    275  CE2 PHE A 406      14.880  72.128  36.136  1.00 43.69           C  
ANISOU  275  CE2 PHE A 406     4452   5685   6460   -488    224    173       C  
ATOM    276  CZ  PHE A 406      13.536  72.433  36.334  1.00 44.45           C  
ANISOU  276  CZ  PHE A 406     4322   5882   6685   -481    272    170       C  
ATOM    277  N   ALA A 407      18.249  76.436  32.580  1.00 39.79           N  
ANISOU  277  N   ALA A 407     4336   4904   5879     72    -79    236       N  
ATOM    278  CA  ALA A 407      18.821  76.867  31.324  1.00 37.77           C  
ANISOU  278  CA  ALA A 407     4164   4603   5582    131   -198    274       C  
ATOM    279  C   ALA A 407      18.680  75.728  30.316  1.00 37.80           C  
ANISOU  279  C   ALA A 407     4188   4641   5531     31   -332    296       C  
ATOM    280  O   ALA A 407      19.203  74.632  30.540  1.00 37.72           O  
ANISOU  280  O   ALA A 407     4270   4614   5444    -74   -320    273       O  
ATOM    281  CB  ALA A 407      20.259  77.240  31.513  1.00 36.06           C  
ANISOU  281  CB  ALA A 407     4127   4297   5275    157   -150    257       C  
ATOM    282  N   ILE A 408      17.955  75.973  29.222  1.00 38.19           N  
ANISOU  282  N   ILE A 408     4154   4735   5619     63   -462    341       N  
ATOM    283  CA  ILE A 408      17.807  74.977  28.146  1.00 37.62           C  
ANISOU  283  CA  ILE A 408     4114   4695   5483    -36   -602    356       C  
ATOM    284  C   ILE A 408      18.689  75.336  26.968  1.00 38.17           C  
ANISOU  284  C   ILE A 408     4335   4711   5455      6   -692    384       C  
ATOM    285  O   ILE A 408      18.552  76.412  26.384  1.00 39.42           O  
ANISOU  285  O   ILE A 408     4470   4863   5642    113   -743    432       O  
ATOM    286  CB  ILE A 408      16.343  74.830  27.703  1.00 38.97           C  
ANISOU  286  CB  ILE A 408     4086   4972   5746    -61   -703    387       C  
ATOM    287  CG1 ILE A 408      15.528  74.293  28.887  1.00 39.14           C  
ANISOU  287  CG1 ILE A 408     3966   5051   5854   -132   -597    354       C  
ATOM    288  CG2 ILE A 408      16.245  73.934  26.465  1.00 39.03           C  
ANISOU  288  CG2 ILE A 408     4148   5008   5671   -165   -864    400       C  
ATOM    289  CD1 ILE A 408      14.050  74.064  28.617  1.00 40.15           C  
ANISOU  289  CD1 ILE A 408     3868   5295   6090   -174   -677    379       C  
ATOM    290  N   LYS A 409      19.630  74.445  26.636  1.00 37.69           N  
ANISOU  290  N   LYS A 409     4434   4604   5279    -74   -701    355       N  
ATOM    291  CA  LYS A 409      20.405  74.585  25.409  1.00 38.36           C  
ANISOU  291  CA  LYS A 409     4663   4651   5259    -58   -784    374       C  
ATOM    292  C   LYS A 409      19.700  73.816  24.296  1.00 39.03           C  
ANISOU  292  C   LYS A 409     4730   4796   5301   -147   -934    384       C  
ATOM    293  O   LYS A 409      19.399  72.607  24.420  1.00 38.08           O  
ANISOU  293  O   LYS A 409     4606   4696   5166   -268   -948    345       O  
ATOM    294  CB  LYS A 409      21.812  74.064  25.612  1.00 37.59           C  
ANISOU  294  CB  LYS A 409     4739   4474   5068    -88   -706    332       C  
ATOM    295  CG  LYS A 409      22.743  73.998  24.402  1.00 39.92           C  
ANISOU  295  CG  LYS A 409     5194   4729   5244    -90   -763    335       C  
ATOM    296  CD  LYS A 409      24.011  73.372  24.980  1.00 41.33           C  
ANISOU  296  CD  LYS A 409     5494   4836   5371   -117   -659    287       C  
ATOM    297  CE  LYS A 409      25.020  72.903  23.983  1.00 43.37           C  
ANISOU  297  CE  LYS A 409     5910   5051   5516   -141   -680    267       C  
ATOM    298  NZ  LYS A 409      26.311  72.696  24.682  1.00 41.07           N  
ANISOU  298  NZ  LYS A 409     5703   4694   5206   -125   -568    237       N  
ATOM    299  N   ALA A 410      19.439  74.522  23.209  1.00 39.22           N  
ANISOU  299  N   ALA A 410     4752   4846   5301    -93  -1050    439       N  
ATOM    300  CA  ALA A 410      18.651  73.992  22.116  1.00 41.02           C  
ANISOU  300  CA  ALA A 410     4950   5148   5487   -171  -1214    458       C  
ATOM    301  C   ALA A 410      19.509  73.983  20.871  1.00 41.76           C  
ANISOU  301  C   ALA A 410     5234   5205   5428   -182  -1281    465       C  
ATOM    302  O   ALA A 410      20.159  74.969  20.562  1.00 42.31           O  
ANISOU  302  O   ALA A 410     5378   5229   5466    -85  -1260    505       O  
ATOM    303  CB  ALA A 410      17.410  74.843  21.896  1.00 42.79           C  
ANISOU  303  CB  ALA A 410     4983   5454   5819    -98  -1312    531       C  
ATOM    304  N   LEU A 411      19.499  72.854  20.174  1.00 43.29           N  
ANISOU  304  N   LEU A 411     5510   5413   5523   -310  -1353    422       N  
ATOM    305  CA  LEU A 411      20.265  72.640  18.963  1.00 44.85           C  
ANISOU  305  CA  LEU A 411     5897   5581   5560   -344  -1408    410       C  
ATOM    306  C   LEU A 411      19.332  72.136  17.874  1.00 45.90           C  
ANISOU  306  C   LEU A 411     6010   5800   5628   -445  -1590    420       C  
ATOM    307  O   LEU A 411      18.382  71.389  18.146  1.00 46.63           O  
ANISOU  307  O   LEU A 411     5985   5949   5781   -539  -1644    397       O  
ATOM    308  CB  LEU A 411      21.363  71.576  19.203  1.00 44.42           C  
ANISOU  308  CB  LEU A 411     6002   5442   5433   -412  -1296    321       C  
ATOM    309  CG  LEU A 411      22.406  71.841  20.280  1.00 44.47           C  
ANISOU  309  CG  LEU A 411     6042   5368   5487   -337  -1126    302       C  
ATOM    310  CD1 LEU A 411      23.293  70.637  20.542  1.00 45.64           C  
ANISOU  310  CD1 LEU A 411     6314   5441   5584   -406  -1039    223       C  
ATOM    311  CD2 LEU A 411      23.274  73.010  19.867  1.00 46.90           C  
ANISOU  311  CD2 LEU A 411     6429   5641   5748   -230  -1092    346       C  
ATOM    312  N   LYS A 412      19.602  72.557  16.643  1.00 46.34           N  
ANISOU  312  N   LYS A 412     6183   5868   5555   -434  -1685    457       N  
ATOM    313  CA  LYS A 412      18.896  72.063  15.473  1.00 47.85           C  
ANISOU  313  CA  LYS A 412     6398   6137   5642   -542  -1866    462       C  
ATOM    314  C   LYS A 412      19.693  70.903  14.902  1.00 46.20           C  
ANISOU  314  C   LYS A 412     6398   5872   5280   -662  -1831    360       C  
ATOM    315  O   LYS A 412      20.876  71.029  14.634  1.00 44.40           O  
ANISOU  315  O   LYS A 412     6338   5569   4961   -624  -1732    335       O  
ATOM    316  CB  LYS A 412      18.742  73.175  14.417  1.00 50.80           C  
ANISOU  316  CB  LYS A 412     6801   6557   5942   -468  -1995    565       C  
ATOM    317  CG  LYS A 412      17.943  74.393  14.871  1.00 51.90           C  
ANISOU  317  CG  LYS A 412     6742   6739   6238   -331  -2037    673       C  
ATOM    318  CD  LYS A 412      16.525  74.065  15.323  1.00 53.11           C  
ANISOU  318  CD  LYS A 412     6654   6991   6533   -371  -2131    685       C  
ATOM    319  CE  LYS A 412      15.713  73.434  14.215  1.00 55.93           C  
ANISOU  319  CE  LYS A 412     7006   7452   6791   -503  -2342    693       C  
ATOM    320  NZ  LYS A 412      14.256  73.339  14.529  1.00 57.85           N  
ANISOU  320  NZ  LYS A 412     6984   7812   7183   -529  -2459    729       N  
ATOM    321  N   LYS A 413      19.048  69.757  14.742  1.00 46.80           N  
ANISOU  321  N   LYS A 413     6461   5981   5339   -808  -1904    297       N  
ATOM    322  CA  LYS A 413      19.717  68.562  14.228  1.00 46.22           C  
ANISOU  322  CA  LYS A 413     6587   5840   5132   -926  -1867    189       C  
ATOM    323  C   LYS A 413      20.365  68.728  12.838  1.00 46.69           C  
ANISOU  323  C   LYS A 413     6855   5896   4987   -943  -1919    180       C  
ATOM    324  O   LYS A 413      21.459  68.208  12.593  1.00 44.88           O  
ANISOU  324  O   LYS A 413     6811   5578   4662   -957  -1804    102       O  
ATOM    325  CB  LYS A 413      18.734  67.383  14.200  1.00 48.09           C  
ANISOU  325  CB  LYS A 413     6769   6117   5385  -1096  -1963    129       C  
ATOM    326  CG  LYS A 413      18.422  66.820  15.582  1.00 47.04           C  
ANISOU  326  CG  LYS A 413     6503   5951   5418  -1115  -1860    104       C  
ATOM    327  CD  LYS A 413      17.309  65.787  15.547  1.00 49.28           C  
ANISOU  327  CD  LYS A 413     6706   6285   5731  -1291  -1965     62       C  
ATOM    328  CE  LYS A 413      17.278  64.991  16.838  1.00 48.91           C  
ANISOU  328  CE  LYS A 413     6600   6171   5810  -1333  -1832     21       C  
ATOM    329  NZ  LYS A 413      16.242  63.938  16.797  1.00 51.81           N  
ANISOU  329  NZ  LYS A 413     6902   6578   6205  -1521  -1924    -22       N  
ATOM    330  N   ASP A 414      19.696  69.433  11.928  1.00 48.50           N  
ANISOU  330  N   ASP A 414     7054   6224   5148   -942  -2089    261       N  
ATOM    331  CA  ASP A 414      20.293  69.704  10.625  1.00 49.02           C  
ANISOU  331  CA  ASP A 414     7322   6294   5008   -957  -2135    267       C  
ATOM    332  C   ASP A 414      21.605  70.500  10.767  1.00 47.76           C  
ANISOU  332  C   ASP A 414     7267   6051   4827   -824  -1969    290       C  
ATOM    333  O   ASP A 414      22.578  70.205  10.092  1.00 47.82           O  
ANISOU  333  O   ASP A 414     7476   6007   4686   -853  -1893    231       O  
ATOM    334  CB  ASP A 414      19.295  70.382   9.670  1.00 51.28           C  
ANISOU  334  CB  ASP A 414     7551   6705   5226   -974  -2363    371       C  
ATOM    335  CG  ASP A 414      18.786  71.718  10.175  1.00 51.26           C  
ANISOU  335  CG  ASP A 414     7358   6744   5374   -819  -2401    509       C  
ATOM    336  OD1 ASP A 414      18.510  72.618   9.343  1.00 53.21           O  
ANISOU  336  OD1 ASP A 414     7619   7050   5546   -772  -2534    617       O  
ATOM    337  OD2 ASP A 414      18.633  71.871  11.395  1.00 51.38           O  
ANISOU  337  OD2 ASP A 414     7212   6729   5579   -744  -2301    513       O  
ATOM    338  N   VAL A 415      21.648  71.470  11.674  1.00 47.26           N  
ANISOU  338  N   VAL A 415     7066   5971   4917   -687  -1902    367       N  
ATOM    339  CA  VAL A 415      22.870  72.263  11.900  1.00 46.75           C  
ANISOU  339  CA  VAL A 415     7084   5828   4848   -573  -1745    389       C  
ATOM    340  C   VAL A 415      23.997  71.415  12.519  1.00 46.68           C  
ANISOU  340  C   VAL A 415     7164   5719   4851   -586  -1556    279       C  
ATOM    341  O   VAL A 415      25.164  71.508  12.124  1.00 46.05           O  
ANISOU  341  O   VAL A 415     7235   5583   4676   -563  -1446    250       O  
ATOM    342  CB  VAL A 415      22.566  73.515  12.754  1.00 46.24           C  
ANISOU  342  CB  VAL A 415     6852   5765   4949   -431  -1726    491       C  
ATOM    343  CG1 VAL A 415      23.836  74.215  13.222  1.00 46.01           C  
ANISOU  343  CG1 VAL A 415     6894   5647   4940   -332  -1551    497       C  
ATOM    344  CG2 VAL A 415      21.669  74.493  11.972  1.00 48.75           C  
ANISOU  344  CG2 VAL A 415     7114   6164   5243   -391  -1907    616       C  
ATOM    345  N   VAL A 416      23.642  70.593  13.498  1.00 46.33           N  
ANISOU  345  N   VAL A 416     7021   5655   4927   -621  -1517    223       N  
ATOM    346  CA  VAL A 416      24.607  69.713  14.136  1.00 45.84           C  
ANISOU  346  CA  VAL A 416     7032   5496   4888   -632  -1357    130       C  
ATOM    347  C   VAL A 416      25.214  68.771  13.098  1.00 47.15           C  
ANISOU  347  C   VAL A 416     7402   5623   4887   -723  -1341     35       C  
ATOM    348  O   VAL A 416      26.439  68.590  13.046  1.00 45.94           O  
ANISOU  348  O   VAL A 416     7368   5395   4690   -686  -1201    -14       O  
ATOM    349  CB  VAL A 416      23.932  68.888  15.245  1.00 45.43           C  
ANISOU  349  CB  VAL A 416     6851   5434   4975   -679  -1345     95       C  
ATOM    350  CG1 VAL A 416      24.841  67.763  15.728  1.00 45.32           C  
ANISOU  350  CG1 VAL A 416     6938   5314   4965   -709  -1209      0       C  
ATOM    351  CG2 VAL A 416      23.522  69.802  16.377  1.00 42.66           C  
ANISOU  351  CG2 VAL A 416     6314   5108   4784   -581  -1317    171       C  
ATOM    352  N   LEU A 417      24.351  68.189  12.275  1.00 48.93           N  
ANISOU  352  N   LEU A 417     7664   5904   5022   -842  -1485      8       N  
ATOM    353  CA  LEU A 417      24.785  67.276  11.225  1.00 52.87           C  
ANISOU  353  CA  LEU A 417     8368   6370   5350   -944  -1481    -92       C  
ATOM    354  C   LEU A 417      25.781  67.931  10.257  1.00 53.67           C  
ANISOU  354  C   LEU A 417     8630   6466   5296   -896  -1423    -80       C  
ATOM    355  O   LEU A 417      26.843  67.370  10.001  1.00 53.39           O  
ANISOU  355  O   LEU A 417     8742   6352   5191   -898  -1286   -168       O  
ATOM    356  CB  LEU A 417      23.578  66.745  10.448  1.00 55.91           C  
ANISOU  356  CB  LEU A 417     8755   6834   5651  -1090  -1673   -110       C  
ATOM    357  CG  LEU A 417      23.862  65.804   9.272  1.00 59.66           C  
ANISOU  357  CG  LEU A 417     9455   7284   5929  -1218  -1691   -224       C  
ATOM    358  CD1 LEU A 417      24.549  64.523   9.723  1.00 59.92           C  
ANISOU  358  CD1 LEU A 417     9586   7184   5995  -1255  -1542   -355       C  
ATOM    359  CD2 LEU A 417      22.572  65.495   8.522  1.00 62.48           C  
ANISOU  359  CD2 LEU A 417     9792   7743   6204  -1365  -1912   -221       C  
ATOM    360  N   MET A 418      25.444  69.101   9.715  1.00 54.53           N  
ANISOU  360  N   MET A 418     8710   6653   5352   -853  -1521     29       N  
ATOM    361  CA AMET A 418      26.319  69.718   8.715  0.50 54.65           C  
ANISOU  361  CA AMET A 418     8891   6669   5203   -828  -1473     48       C  
ATOM    362  CA BMET A 418      26.291  69.778   8.723  0.50 55.98           C  
ANISOU  362  CA BMET A 418     9053   6841   5374   -824  -1477     55       C  
ATOM    363  C   MET A 418      27.574  70.319   9.347  1.00 53.36           C  
ANISOU  363  C   MET A 418     8726   6433   5114   -706  -1280     63       C  
ATOM    364  O   MET A 418      28.563  70.509   8.658  1.00 54.93           O  
ANISOU  364  O   MET A 418     9071   6608   5189   -697  -1182     42       O  
ATOM    365  CB AMET A 418      25.565  70.740   7.855  0.50 55.24           C  
ANISOU  365  CB AMET A 418     8959   6845   5185   -829  -1649    171       C  
ATOM    366  CB BMET A 418      25.528  70.921   8.028  0.50 58.25           C  
ANISOU  366  CB BMET A 418     9307   7227   5598   -807  -1648    190       C  
ATOM    367  CG AMET A 418      24.582  70.105   6.874  0.50 57.48           C  
ANISOU  367  CG AMET A 418     9303   7210   5326   -972  -1841    144       C  
ATOM    368  CG BMET A 418      24.533  70.465   6.970  0.50 62.21           C  
ANISOU  368  CG BMET A 418     9867   7817   5950   -939  -1850    183       C  
ATOM    369  SD AMET A 418      25.286  69.004   5.614  0.50 57.87           S  
ANISOU  369  SD AMET A 418     9641   7230   5116  -1112  -1788     -4       S  
ATOM    370  SD BMET A 418      23.458  71.808   6.408  0.50 66.20           S  
ANISOU  370  SD BMET A 418    10276   8441   6436   -895  -2077    367       S  
ATOM    371  CE AMET A 418      25.300  67.454   6.492  0.50 58.08           C  
ANISOU  371  CE AMET A 418     9636   7162   5266  -1175  -1694   -158       C  
ATOM    372  CE BMET A 418      22.904  72.348   8.016  0.50 62.46           C  
ANISOU  372  CE BMET A 418     9516   7948   6265   -766  -2045    432       C  
ATOM    373  N   ASP A 419      27.546  70.587  10.655  1.00 51.14           N  
ANISOU  373  N   ASP A 419     8280   6121   5029   -623  -1223     95       N  
ATOM    374  CA  ASP A 419      28.740  71.027  11.378  1.00 49.65           C  
ANISOU  374  CA  ASP A 419     8078   5864   4920   -522  -1046     97       C  
ATOM    375  C   ASP A 419      29.604  69.845  11.823  1.00 50.10           C  
ANISOU  375  C   ASP A 419     8190   5836   5006   -538   -903    -21       C  
ATOM    376  O   ASP A 419      30.622  70.054  12.483  1.00 48.66           O  
ANISOU  376  O   ASP A 419     7987   5600   4898   -461   -761    -26       O  
ATOM    377  CB  ASP A 419      28.367  71.818  12.638  1.00 48.00           C  
ANISOU  377  CB  ASP A 419     7681   5656   4900   -431  -1044    174       C  
ATOM    378  CG  ASP A 419      27.833  73.207  12.340  1.00 49.97           C  
ANISOU  378  CG  ASP A 419     7877   5958   5151   -372  -1138    300       C  
ATOM    379  OD1 ASP A 419      27.365  73.857  13.286  1.00 50.91           O  
ANISOU  379  OD1 ASP A 419     7844   6079   5420   -301  -1147    357       O  
ATOM    380  OD2 ASP A 419      27.891  73.665  11.191  1.00 50.37           O  
ANISOU  380  OD2 ASP A 419     8041   6041   5055   -394  -1197    342       O  
ATOM    381  N   ASP A 420      29.177  68.622  11.516  1.00 51.29           N  
ANISOU  381  N   ASP A 420     8404   5972   5110   -635   -946   -110       N  
ATOM    382  CA  ASP A 420      29.911  67.410  11.898  1.00 55.44           C  
ANISOU  382  CA  ASP A 420     8992   6402   5670   -648   -820   -222       C  
ATOM    383  C   ASP A 420      30.045  67.305  13.424  1.00 51.55           C  
ANISOU  383  C   ASP A 420     8351   5863   5372   -579   -753   -201       C  
ATOM    384  O   ASP A 420      31.074  66.898  13.934  1.00 48.43           O  
ANISOU  384  O   ASP A 420     7977   5392   5030   -524   -616   -244       O  
ATOM    385  CB  ASP A 420      31.293  67.380  11.218  1.00 60.03           C  
ANISOU  385  CB  ASP A 420     9721   6937   6149   -613   -669   -278       C  
ATOM    386  CG  ASP A 420      31.950  66.006  11.260  1.00 65.29           C  
ANISOU  386  CG  ASP A 420    10485   7502   6819   -635   -557   -406       C  
ATOM    387  OD1 ASP A 420      31.258  64.979  11.090  1.00 70.15           O  
ANISOU  387  OD1 ASP A 420    11150   8090   7412   -729   -625   -476       O  
ATOM    388  OD2 ASP A 420      33.176  65.952  11.476  1.00 72.64           O  
ANISOU  388  OD2 ASP A 420    11439   8376   7783   -557   -399   -436       O  
ATOM    389  N   ASP A 421      28.971  67.643  14.132  1.00 50.20           N  
ANISOU  389  N   ASP A 421     8029   5741   5303   -584   -853   -136       N  
ATOM    390  CA  ASP A 421      28.978  67.712  15.595  1.00 49.92           C  
ANISOU  390  CA  ASP A 421     7850   5678   5436   -524   -797   -105       C  
ATOM    391  C   ASP A 421      28.141  66.633  16.258  1.00 46.44           C  
ANISOU  391  C   ASP A 421     7354   5216   5074   -602   -840   -142       C  
ATOM    392  O   ASP A 421      27.779  66.770  17.442  1.00 42.16           O  
ANISOU  392  O   ASP A 421     6677   4678   4662   -574   -826   -101       O  
ATOM    393  CB  ASP A 421      28.444  69.072  16.049  1.00 52.20           C  
ANISOU  393  CB  ASP A 421     7999   6037   5797   -456   -848      1       C  
ATOM    394  CG  ASP A 421      29.520  70.123  16.120  1.00 57.87           C  
ANISOU  394  CG  ASP A 421     8734   6739   6513   -357   -750     43       C  
ATOM    395  OD1 ASP A 421      30.696  69.813  15.801  1.00 60.91           O  
ANISOU  395  OD1 ASP A 421     9227   7073   6843   -341   -642     -6       O  
ATOM    396  OD2 ASP A 421      29.183  71.264  16.497  1.00 62.57           O  
ANISOU  396  OD2 ASP A 421     9233   7371   7168   -296   -777    124       O  
ATOM    397  N   VAL A 422      27.831  65.571  15.520  1.00 45.35           N  
ANISOU  397  N   VAL A 422     7323   5053   4854   -708   -887   -220       N  
ATOM    398  CA  VAL A 422      26.915  64.549  16.034  1.00 45.49           C  
ANISOU  398  CA  VAL A 422     7294   5051   4938   -808   -942   -253       C  
ATOM    399  C   VAL A 422      27.550  63.850  17.229  1.00 44.40           C  
ANISOU  399  C   VAL A 422     7141   4812   4914   -769   -819   -274       C  
ATOM    400  O   VAL A 422      26.931  63.734  18.293  1.00 42.27           O  
ANISOU  400  O   VAL A 422     6749   4553   4759   -783   -829   -236       O  
ATOM    401  CB  VAL A 422      26.524  63.524  14.953  1.00 48.08           C  
ANISOU  401  CB  VAL A 422     7763   5358   5146   -943  -1014   -344       C  
ATOM    402  CG1 VAL A 422      25.742  62.352  15.563  1.00 48.00           C  
ANISOU  402  CG1 VAL A 422     7721   5302   5215  -1055  -1047   -386       C  
ATOM    403  CG2 VAL A 422      25.701  64.198  13.865  1.00 49.14           C  
ANISOU  403  CG2 VAL A 422     7892   5610   5168   -997  -1169   -308       C  
ATOM    404  N   GLU A 423      28.788  63.395  17.055  1.00 45.31           N  
ANISOU  404  N   GLU A 423     7379   4836   4998   -717   -702   -330       N  
ATOM    405  CA  GLU A 423      29.489  62.681  18.121  1.00 46.13           C  
ANISOU  405  CA  GLU A 423     7481   4839   5205   -671   -595   -343       C  
ATOM    406  C   GLU A 423      29.781  63.596  19.329  1.00 43.32           C  
ANISOU  406  C   GLU A 423     6983   4520   4956   -571   -548   -255       C  
ATOM    407  O   GLU A 423      29.642  63.149  20.465  1.00 40.04           O  
ANISOU  407  O   GLU A 423     6505   4067   4638   -573   -522   -233       O  
ATOM    408  CB  GLU A 423      30.788  62.035  17.588  1.00 48.35           C  
ANISOU  408  CB  GLU A 423     7914   5017   5437   -623   -480   -422       C  
ATOM    409  CG  GLU A 423      31.635  61.298  18.648  1.00 49.25           C  
ANISOU  409  CG  GLU A 423     8027   5022   5663   -555   -373   -426       C  
ATOM    410  CD  GLU A 423      30.911  60.144  19.350  1.00 50.63           C  
ANISOU  410  CD  GLU A 423     8205   5120   5909   -641   -405   -440       C  
ATOM    411  OE1 GLU A 423      29.881  59.655  18.852  1.00 52.03           O  
ANISOU  411  OE1 GLU A 423     8417   5307   6043   -765   -494   -477       O  
ATOM    412  OE2 GLU A 423      31.379  59.697  20.412  1.00 51.50           O  
ANISOU  412  OE2 GLU A 423     8287   5159   6119   -590   -344   -410       O  
ATOM    413  N   CYS A 424      30.191  64.850  19.085  1.00 41.65           N  
ANISOU  413  N   CYS A 424     6732   4374   4717   -492   -535   -207       N  
ATOM    414  CA  CYS A 424      30.374  65.839  20.162  1.00 41.12           C  
ANISOU  414  CA  CYS A 424     6537   4346   4741   -410   -500   -130       C  
ATOM    415  C   CYS A 424      29.117  66.002  21.007  1.00 39.55           C  
ANISOU  415  C   CYS A 424     6202   4200   4622   -453   -569    -83       C  
ATOM    416  O   CYS A 424      29.193  66.133  22.210  1.00 37.95           O  
ANISOU  416  O   CYS A 424     5918   3991   4507   -419   -522    -48       O  
ATOM    417  CB  CYS A 424      30.751  67.216  19.607  1.00 42.80           C  
ANISOU  417  CB  CYS A 424     6736   4619   4904   -343   -497    -85       C  
ATOM    418  SG  CYS A 424      32.361  67.252  18.789  1.00 45.26           S  
ANISOU  418  SG  CYS A 424     7176   4884   5135   -285   -385   -129       S  
ATOM    419  N   THR A 425      27.963  65.988  20.361  1.00 39.25           N  
ANISOU  419  N   THR A 425     6140   4221   4551   -530   -679    -82       N  
ATOM    420  CA  THR A 425      26.682  66.107  21.047  1.00 40.33           C  
ANISOU  420  CA  THR A 425     6133   4420   4769   -577   -745    -41       C  
ATOM    421  C   THR A 425      26.400  64.893  21.973  1.00 38.79           C  
ANISOU  421  C   THR A 425     5930   4166   4642   -651   -713    -67       C  
ATOM    422  O   THR A 425      25.909  65.056  23.095  1.00 35.75           O  
ANISOU  422  O   THR A 425     5429   3807   4347   -650   -689    -27       O  
ATOM    423  CB  THR A 425      25.557  66.270  20.013  1.00 43.60           C  
ANISOU  423  CB  THR A 425     6521   4915   5128   -650   -884    -36       C  
ATOM    424  OG1 THR A 425      25.708  67.545  19.357  1.00 43.81           O  
ANISOU  424  OG1 THR A 425     6537   4999   5109   -571   -917     14       O  
ATOM    425  CG2 THR A 425      24.197  66.178  20.673  1.00 43.98           C  
ANISOU  425  CG2 THR A 425     6411   5029   5271   -713   -948     -5       C  
ATOM    426  N   MET A 426      26.750  63.697  21.509  1.00 39.13           N  
ANISOU  426  N   MET A 426     6105   4122   4638   -714   -702   -135       N  
ATOM    427  CA  MET A 426      26.613  62.495  22.308  1.00 39.15           C  
ANISOU  427  CA  MET A 426     6130   4044   4701   -782   -666   -156       C  
ATOM    428  C   MET A 426      27.654  62.452  23.421  1.00 37.45           C  
ANISOU  428  C   MET A 426     5920   3764   4545   -690   -554   -128       C  
ATOM    429  O   MET A 426      27.356  62.059  24.564  1.00 36.55           O  
ANISOU  429  O   MET A 426     5752   3630   4504   -718   -526    -95       O  
ATOM    430  CB  MET A 426      26.711  61.248  21.417  1.00 42.36           C  
ANISOU  430  CB  MET A 426     6694   4359   5041   -871   -686   -243       C  
ATOM    431  CG  MET A 426      25.627  61.190  20.341  1.00 45.89           C  
ANISOU  431  CG  MET A 426     7141   4875   5417   -986   -813   -274       C  
ATOM    432  SD  MET A 426      23.931  61.355  20.953  1.00 49.71           S  
ANISOU  432  SD  MET A 426     7429   5471   5987  -1091   -913   -219       S  
ATOM    433  CE  MET A 426      23.828  59.955  22.050  1.00 48.51           C  
ANISOU  433  CE  MET A 426     7311   5202   5918  -1182   -845   -237       C  
ATOM    434  N   VAL A 427      28.875  62.877  23.123  1.00 36.40           N  
ANISOU  434  N   VAL A 427     5847   3603   4378   -586   -493   -136       N  
ATOM    435  CA  VAL A 427      29.893  62.989  24.179  1.00 35.35           C  
ANISOU  435  CA  VAL A 427     5698   3429   4302   -495   -402   -101       C  
ATOM    436  C   VAL A 427      29.393  63.901  25.289  1.00 35.55           C  
ANISOU  436  C   VAL A 427     5582   3536   4388   -474   -401    -32       C  
ATOM    437  O   VAL A 427      29.463  63.571  26.479  1.00 35.11           O  
ANISOU  437  O   VAL A 427     5494   3455   4389   -476   -361      0       O  
ATOM    438  CB  VAL A 427      31.225  63.521  23.625  1.00 35.15           C  
ANISOU  438  CB  VAL A 427     5728   3390   4237   -391   -341   -116       C  
ATOM    439  CG1 VAL A 427      32.196  63.877  24.751  1.00 34.83           C  
ANISOU  439  CG1 VAL A 427     5638   3338   4258   -302   -268    -69       C  
ATOM    440  CG2 VAL A 427      31.856  62.484  22.692  1.00 36.85           C  
ANISOU  440  CG2 VAL A 427     6090   3509   4402   -400   -311   -193       C  
ATOM    441  N   GLU A 428      28.870  65.057  24.896  1.00 36.30           N  
ANISOU  441  N   GLU A 428     5599   3724   4467   -454   -443     -9       N  
ATOM    442  CA  GLU A 428      28.387  66.035  25.849  1.00 35.03           C  
ANISOU  442  CA  GLU A 428     5309   3635   4364   -424   -432     44       C  
ATOM    443  C   GLU A 428      27.339  65.400  26.749  1.00 34.31           C  
ANISOU  443  C   GLU A 428     5146   3557   4331   -510   -442     59       C  
ATOM    444  O   GLU A 428      27.392  65.522  27.979  1.00 34.49           O  
ANISOU  444  O   GLU A 428     5117   3584   4400   -497   -386     91       O  
ATOM    445  CB  GLU A 428      27.817  67.299  25.140  1.00 35.85           C  
ANISOU  445  CB  GLU A 428     5344   3825   4450   -390   -488     67       C  
ATOM    446  CG  GLU A 428      27.384  68.359  26.144  1.00 37.88           C  
ANISOU  446  CG  GLU A 428     5475   4140   4776   -343   -460    113       C  
ATOM    447  CD  GLU A 428      26.899  69.679  25.541  1.00 40.63           C  
ANISOU  447  CD  GLU A 428     5758   4553   5124   -288   -507    145       C  
ATOM    448  OE1 GLU A 428      26.882  69.854  24.304  1.00 42.68           O  
ANISOU  448  OE1 GLU A 428     6070   4825   5322   -288   -572    142       O  
ATOM    449  OE2 GLU A 428      26.495  70.548  26.335  1.00 42.85           O  
ANISOU  449  OE2 GLU A 428     5941   4872   5469   -245   -477    175       O  
ATOM    450  N   LYS A 429      26.394  64.704  26.157  1.00 35.90           N  
ANISOU  450  N   LYS A 429     5349   3766   4524   -608   -511     34       N  
ATOM    451  CA  LYS A 429      25.357  64.044  26.964  1.00 37.91           C  
ANISOU  451  CA  LYS A 429     5532   4034   4837   -709   -516     47       C  
ATOM    452  C   LYS A 429      25.926  63.049  27.949  1.00 37.09           C  
ANISOU  452  C   LYS A 429     5500   3837   4754   -732   -446     54       C  
ATOM    453  O   LYS A 429      25.559  63.053  29.145  1.00 36.15           O  
ANISOU  453  O   LYS A 429     5312   3740   4681   -756   -399     94       O  
ATOM    454  CB  LYS A 429      24.302  63.388  26.075  1.00 39.24           C  
ANISOU  454  CB  LYS A 429     5696   4224   4990   -828   -611     14       C  
ATOM    455  CG  LYS A 429      23.235  62.602  26.832  1.00 41.76           C  
ANISOU  455  CG  LYS A 429     5942   4553   5370   -954   -613     25       C  
ATOM    456  CD  LYS A 429      23.592  61.132  26.934  1.00 43.40           C  
ANISOU  456  CD  LYS A 429     6290   4634   5565  -1039   -590     -7       C  
ATOM    457  CE  LYS A 429      22.481  60.377  27.640  1.00 46.31           C  
ANISOU  457  CE  LYS A 429     6589   5013   5991  -1181   -592      8       C  
ATOM    458  NZ  LYS A 429      22.716  58.919  27.535  1.00 47.10           N  
ANISOU  458  NZ  LYS A 429     6840   4977   6078  -1279   -586    -26       N  
ATOM    459  N   ARG A 430      26.827  62.194  27.477  1.00 37.02           N  
ANISOU  459  N   ARG A 430     5633   3723   4710   -723   -433     19       N  
ATOM    460  CA  ARG A 430      27.453  61.192  28.364  1.00 36.47           C  
ANISOU  460  CA  ARG A 430     5641   3547   4665   -731   -375     36       C  
ATOM    461  C   ARG A 430      28.265  61.818  29.480  1.00 34.92           C  
ANISOU  461  C   ARG A 430     5411   3368   4489   -637   -309     89       C  
ATOM    462  O   ARG A 430      28.144  61.415  30.644  1.00 33.09           O  
ANISOU  462  O   ARG A 430     5167   3118   4287   -671   -274    134       O  
ATOM    463  CB  ARG A 430      28.355  60.227  27.557  1.00 37.09           C  
ANISOU  463  CB  ARG A 430     5876   3501   4712   -714   -367    -16       C  
ATOM    464  CG  ARG A 430      27.556  59.307  26.622  1.00 39.82           C  
ANISOU  464  CG  ARG A 430     6290   3803   5033   -836   -427    -77       C  
ATOM    465  CD  ARG A 430      28.413  58.172  26.050  1.00 41.71           C  
ANISOU  465  CD  ARG A 430     6700   3892   5254   -825   -398   -136       C  
ATOM    466  NE  ARG A 430      29.505  58.659  25.199  1.00 39.10           N  
ANISOU  466  NE  ARG A 430     6424   3556   4875   -711   -368   -174       N  
ATOM    467  CZ  ARG A 430      29.453  58.763  23.866  1.00 42.28           C  
ANISOU  467  CZ  ARG A 430     6889   3973   5200   -729   -402   -244       C  
ATOM    468  NH1 ARG A 430      28.356  58.451  23.180  1.00 44.16           N  
ANISOU  468  NH1 ARG A 430     7139   4238   5399   -857   -483   -284       N  
ATOM    469  NH2 ARG A 430      30.514  59.183  23.201  1.00 41.63           N  
ANISOU  469  NH2 ARG A 430     6858   3884   5074   -627   -355   -273       N  
ATOM    470  N   VAL A 431      29.127  62.784  29.143  1.00 35.25           N  
ANISOU  470  N   VAL A 431     5443   3441   4508   -529   -293     86       N  
ATOM    471  CA  VAL A 431      29.947  63.421  30.163  1.00 34.14           C  
ANISOU  471  CA  VAL A 431     5270   3319   4380   -450   -240    130       C  
ATOM    472  C   VAL A 431      29.077  64.131  31.227  1.00 35.16           C  
ANISOU  472  C   VAL A 431     5287   3536   4535   -482   -223    169       C  
ATOM    473  O   VAL A 431      29.372  64.096  32.441  1.00 34.55           O  
ANISOU  473  O   VAL A 431     5202   3457   4465   -478   -181    209       O  
ATOM    474  CB  VAL A 431      30.981  64.393  29.580  1.00 34.48           C  
ANISOU  474  CB  VAL A 431     5317   3385   4398   -345   -224    117       C  
ATOM    475  CG1 VAL A 431      31.625  65.152  30.706  1.00 34.53           C  
ANISOU  475  CG1 VAL A 431     5273   3426   4418   -289   -181    160       C  
ATOM    476  CG2 VAL A 431      32.071  63.643  28.813  1.00 37.55           C  
ANISOU  476  CG2 VAL A 431     5813   3684   4769   -301   -209     83       C  
ATOM    477  N   LEU A 432      28.012  64.779  30.774  1.00 36.69           N  
ANISOU  477  N   LEU A 432     5393   3807   4737   -510   -256    156       N  
ATOM    478  CA  LEU A 432      27.082  65.447  31.677  1.00 37.24           C  
ANISOU  478  CA  LEU A 432     5346   3960   4840   -535   -229    181       C  
ATOM    479  C   LEU A 432      26.394  64.459  32.644  1.00 42.93           C  
ANISOU  479  C   LEU A 432     6061   4666   5584   -640   -203    205       C  
ATOM    480  O   LEU A 432      26.181  64.787  33.811  1.00 44.36           O  
ANISOU  480  O   LEU A 432     6193   4887   5775   -650   -144    234       O  
ATOM    481  CB  LEU A 432      26.043  66.235  30.878  1.00 37.05           C  
ANISOU  481  CB  LEU A 432     5222   4016   4837   -536   -280    167       C  
ATOM    482  CG  LEU A 432      26.477  67.609  30.343  1.00 37.51           C  
ANISOU  482  CG  LEU A 432     5255   4111   4884   -429   -286    166       C  
ATOM    483  CD1 LEU A 432      25.337  68.208  29.520  1.00 38.42           C  
ANISOU  483  CD1 LEU A 432     5275   4298   5025   -435   -353    165       C  
ATOM    484  CD2 LEU A 432      26.897  68.582  31.444  1.00 36.31           C  
ANISOU  484  CD2 LEU A 432     5065   3982   4747   -366   -211    184       C  
ATOM    485  N   SER A 433      26.066  63.245  32.196  1.00 44.04           N  
ANISOU  485  N   SER A 433     6262   4744   5726   -727   -238    192       N  
ATOM    486  CA  SER A 433      25.613  62.207  33.156  1.00 49.29           C  
ANISOU  486  CA  SER A 433     6949   5370   6407   -832   -206    224       C  
ATOM    487  C   SER A 433      26.614  61.964  34.296  1.00 49.43           C  
ANISOU  487  C   SER A 433     7041   5335   6404   -791   -150    272       C  
ATOM    488  O   SER A 433      26.225  61.722  35.427  1.00 57.06           O  
ANISOU  488  O   SER A 433     7992   6318   7370   -853   -103    314       O  
ATOM    489  CB  SER A 433      25.301  60.895  32.432  1.00 50.60           C  
ANISOU  489  CB  SER A 433     7199   5448   6577   -929   -253    198       C  
ATOM    490  OG  SER A 433      24.434  61.162  31.356  1.00 51.49           O  
ANISOU  490  OG  SER A 433     7245   5621   6697   -970   -320    154       O  
ATOM    491  N   LEU A 434      27.903  62.051  34.018  1.00 48.23           N  
ANISOU  491  N   LEU A 434     6965   5128   6230   -691   -156    269       N  
ATOM    492  CA  LEU A 434      28.931  61.922  35.069  1.00 49.49           C  
ANISOU  492  CA  LEU A 434     7180   5253   6371   -642   -122    321       C  
ATOM    493  C   LEU A 434      29.076  63.159  35.969  1.00 50.25           C  
ANISOU  493  C   LEU A 434     7199   5446   6446   -597    -81    339       C  
ATOM    494  O   LEU A 434      29.543  63.063  37.107  1.00 45.91           O  
ANISOU  494  O   LEU A 434     6679   4895   5869   -598    -53    388       O  
ATOM    495  CB  LEU A 434      30.300  61.662  34.433  1.00 53.58           C  
ANISOU  495  CB  LEU A 434     7781   5691   6886   -543   -141    309       C  
ATOM    496  CG  LEU A 434      30.898  60.259  34.571  1.00 59.62           C  
ANISOU  496  CG  LEU A 434     8665   6321   7665   -550   -148    337       C  
ATOM    497  CD1 LEU A 434      29.863  59.140  34.642  1.00 64.30           C  
ANISOU  497  CD1 LEU A 434     9302   6852   8275   -678   -155    343       C  
ATOM    498  CD2 LEU A 434      31.872  60.044  33.425  1.00 58.99           C  
ANISOU  498  CD2 LEU A 434     8645   6172   7595   -461   -161    289       C  
ATOM    499  N   ALA A 435      28.657  64.310  35.453  1.00 49.25           N  
ANISOU  499  N   ALA A 435     6984   5400   6328   -561    -81    300       N  
ATOM    500  CA  ALA A 435      28.952  65.626  36.061  1.00 44.08           C  
ANISOU  500  CA  ALA A 435     6272   4818   5658   -500    -43    300       C  
ATOM    501  C   ALA A 435      28.119  66.016  37.256  1.00 41.02           C  
ANISOU  501  C   ALA A 435     5820   4500   5263   -555     17    315       C  
ATOM    502  O   ALA A 435      28.551  66.862  38.040  1.00 41.55           O  
ANISOU  502  O   ALA A 435     5877   4606   5301   -519     57    318       O  
ATOM    503  CB  ALA A 435      28.820  66.700  35.001  1.00 42.82           C  
ANISOU  503  CB  ALA A 435     6054   4700   5516   -436    -65    258       C  
ATOM    504  N   TRP A 436      26.934  65.442  37.419  1.00 44.78           N  
ANISOU  504  N   TRP A 436     6254   4995   5763   -649     32    320       N  
ATOM    505  CA  TRP A 436      26.141  65.757  38.606  1.00 50.64           C  
ANISOU  505  CA  TRP A 436     6936   5806   6496   -707    110    332       C  
ATOM    506  C   TRP A 436      26.881  65.393  39.898  1.00 48.24           C  
ANISOU  506  C   TRP A 436     6722   5482   6124   -731    147    380       C  
ATOM    507  O   TRP A 436      26.520  65.891  40.936  1.00 51.84           O  
ANISOU  507  O   TRP A 436     7148   6000   6547   -760    219    383       O  
ATOM    508  CB  TRP A 436      24.739  65.125  38.585  1.00 60.42           C  
ANISOU  508  CB  TRP A 436     8103   7075   7777   -817    127    332       C  
ATOM    509  CG  TRP A 436      24.706  63.676  38.344  1.00 68.37           C  
ANISOU  509  CG  TRP A 436     9192   7999   8785   -904     87    361       C  
ATOM    510  CD1 TRP A 436      24.464  63.048  37.150  1.00 74.57           C  
ANISOU  510  CD1 TRP A 436     9988   8737   9606   -929     14    337       C  
ATOM    511  CD2 TRP A 436      24.893  62.635  39.316  1.00 78.61           C  
ANISOU  511  CD2 TRP A 436    10583   9240  10043   -987    117    419       C  
ATOM    512  NE1 TRP A 436      24.503  61.677  37.318  1.00 77.64           N  
ANISOU  512  NE1 TRP A 436    10476   9035   9988  -1020      3    369       N  
ATOM    513  CE2 TRP A 436      24.769  61.398  38.635  1.00 81.11           C  
ANISOU  513  CE2 TRP A 436    10967   9463  10385  -1053     63    426       C  
ATOM    514  CE3 TRP A 436      25.159  62.624  40.696  1.00 83.18           C  
ANISOU  514  CE3 TRP A 436    11207   9836  10560  -1015    181    468       C  
ATOM    515  CZ2 TRP A 436      24.901  60.161  39.291  1.00 85.16           C  
ANISOU  515  CZ2 TRP A 436    11592   9888  10877  -1139     74    486       C  
ATOM    516  CZ3 TRP A 436      25.292  61.384  41.348  1.00 86.03           C  
ANISOU  516  CZ3 TRP A 436    11677  10119  10889  -1102    185    536       C  
ATOM    517  CH2 TRP A 436      25.162  60.176  40.639  1.00 84.44           C  
ANISOU  517  CH2 TRP A 436    11540   9814  10727  -1160    133    546       C  
ATOM    518  N   GLU A 437      27.937  64.573  39.807  1.00 46.64           N  
ANISOU  518  N   GLU A 437     6626   5194   5898   -710     96    418       N  
ATOM    519  CA  GLU A 437      28.738  64.160  40.967  1.00 51.44           C  
ANISOU  519  CA  GLU A 437     7323   5779   6442   -724    106    479       C  
ATOM    520  C   GLU A 437      29.756  65.176  41.434  1.00 49.40           C  
ANISOU  520  C   GLU A 437     7069   5560   6139   -646    107    473       C  
ATOM    521  O   GLU A 437      30.425  64.923  42.439  1.00 47.75           O  
ANISOU  521  O   GLU A 437     6927   5347   5867   -660    103    525       O  
ATOM    522  CB  GLU A 437      29.494  62.847  40.700  1.00 56.24           C  
ANISOU  522  CB  GLU A 437     8038   6271   7058   -720     46    529       C  
ATOM    523  CG  GLU A 437      28.708  61.611  41.082  1.00 61.47           C  
ANISOU  523  CG  GLU A 437     8751   6880   7722   -837     60    576       C  
ATOM    524  CD  GLU A 437      29.466  60.317  40.844  1.00 67.24           C  
ANISOU  524  CD  GLU A 437     9601   7476   8471   -823      6    626       C  
ATOM    525  OE1 GLU A 437      28.852  59.388  40.282  1.00 72.69           O  
ANISOU  525  OE1 GLU A 437    10323   8093   9202   -891     -3    619       O  
ATOM    526  OE2 GLU A 437      30.659  60.221  41.216  1.00 72.91           O  
ANISOU  526  OE2 GLU A 437    10378   8157   9166   -747    -26    670       O  
ATOM    527  N   HIS A 438      29.893  66.301  40.725  1.00 42.75           N  
ANISOU  527  N   HIS A 438     6162   4753   5325   -571    106    414       N  
ATOM    528  CA  HIS A 438      30.862  67.304  41.124  1.00 40.05           C  
ANISOU  528  CA  HIS A 438     5826   4444   4946   -509    107    402       C  
ATOM    529  C   HIS A 438      30.263  68.702  41.207  1.00 37.99           C  
ANISOU  529  C   HIS A 438     5489   4253   4692   -491    166    341       C  
ATOM    530  O   HIS A 438      29.522  69.103  40.295  1.00 40.63           O  
ANISOU  530  O   HIS A 438     5753   4595   5087   -465    170    303       O  
ATOM    531  CB  HIS A 438      32.027  67.287  40.155  1.00 38.84           C  
ANISOU  531  CB  HIS A 438     5695   4239   4820   -423     44    398       C  
ATOM    532  CG  HIS A 438      33.258  67.866  40.740  1.00 37.40           C  
ANISOU  532  CG  HIS A 438     5535   4077   4597   -382     29    410       C  
ATOM    533  ND1 HIS A 438      33.528  69.208  40.666  1.00 37.70           N  
ANISOU  533  ND1 HIS A 438     5533   4161   4630   -345     51    363       N  
ATOM    534  CD2 HIS A 438      34.227  67.322  41.506  1.00 36.25           C  
ANISOU  534  CD2 HIS A 438     5444   3916   4410   -383     -8    468       C  
ATOM    535  CE1 HIS A 438      34.648  69.465  41.311  1.00 40.18           C  
ANISOU  535  CE1 HIS A 438     5873   4490   4901   -333     26    383       C  
ATOM    536  NE2 HIS A 438      35.090  68.337  41.833  1.00 40.05           N  
ANISOU  536  NE2 HIS A 438     5910   4444   4863   -352    -14    450       N  
ATOM    537  N   PRO A 439      30.584  69.464  42.282  1.00 37.73           N  
ANISOU  537  N   PRO A 439     5471   4266   4597   -501    209    331       N  
ATOM    538  CA  PRO A 439      30.025  70.815  42.453  1.00 37.16           C  
ANISOU  538  CA  PRO A 439     5339   4244   4534   -480    279    267       C  
ATOM    539  C   PRO A 439      30.462  71.865  41.415  1.00 36.75           C  
ANISOU  539  C   PRO A 439     5252   4175   4534   -389    253    224       C  
ATOM    540  O   PRO A 439      29.774  72.866  41.246  1.00 35.57           O  
ANISOU  540  O   PRO A 439     5044   4046   4423   -358    303    177       O  
ATOM    541  CB  PRO A 439      30.531  71.234  43.842  1.00 39.97           C  
ANISOU  541  CB  PRO A 439     5753   4639   4792   -521    318    265       C  
ATOM    542  CG  PRO A 439      31.801  70.468  44.034  1.00 40.44           C  
ANISOU  542  CG  PRO A 439     5889   4668   4807   -522    234    328       C  
ATOM    543  CD  PRO A 439      31.503  69.124  43.404  1.00 40.11           C  
ANISOU  543  CD  PRO A 439     5854   4573   4811   -534    191    379       C  
ATOM    544  N   PHE A 440      31.591  71.668  40.732  1.00 34.14           N  
ANISOU  544  N   PHE A 440     4959   3804   4209   -344    184    244       N  
ATOM    545  CA  PHE A 440      32.116  72.746  39.869  1.00 33.65           C  
ANISOU  545  CA  PHE A 440     4876   3727   4180   -271    171    209       C  
ATOM    546  C   PHE A 440      31.904  72.486  38.373  1.00 32.34           C  
ANISOU  546  C   PHE A 440     4685   3526   4074   -226    125    210       C  
ATOM    547  O   PHE A 440      32.568  73.062  37.563  1.00 31.56           O  
ANISOU  547  O   PHE A 440     4592   3407   3990   -173    103    199       O  
ATOM    548  CB  PHE A 440      33.573  73.087  40.232  1.00 33.08           C  
ANISOU  548  CB  PHE A 440     4850   3651   4065   -259    144    216       C  
ATOM    549  CG  PHE A 440      33.754  73.461  41.680  1.00 34.85           C  
ANISOU  549  CG  PHE A 440     5108   3918   4216   -313    179    209       C  
ATOM    550  CD1 PHE A 440      32.846  74.281  42.322  1.00 36.44           C  
ANISOU  550  CD1 PHE A 440     5292   4149   4404   -336    259    160       C  
ATOM    551  CD2 PHE A 440      34.813  72.964  42.422  1.00 38.71           C  
ANISOU  551  CD2 PHE A 440     5645   4418   4644   -342    133    250       C  
ATOM    552  CE1 PHE A 440      32.989  74.596  43.655  1.00 38.00           C  
ANISOU  552  CE1 PHE A 440     5534   4386   4516   -396    299    144       C  
ATOM    553  CE2 PHE A 440      34.959  73.287  43.756  1.00 37.00           C  
ANISOU  553  CE2 PHE A 440     5470   4247   4341   -404    156    244       C  
ATOM    554  CZ  PHE A 440      34.046  74.103  44.374  1.00 36.08           C  
ANISOU  554  CZ  PHE A 440     5350   4159   4198   -436    243    187       C  
ATOM    555  N   LEU A 441      30.944  71.615  38.037  1.00 32.27           N  
ANISOU  555  N   LEU A 441     4652   3514   4091   -258    114    222       N  
ATOM    556  CA  LEU A 441      30.561  71.359  36.667  1.00 31.24           C  
ANISOU  556  CA  LEU A 441     4502   3361   4004   -233     67    217       C  
ATOM    557  C   LEU A 441      29.051  71.605  36.557  1.00 31.34           C  
ANISOU  557  C   LEU A 441     4430   3415   4063   -253     87    202       C  
ATOM    558  O   LEU A 441      28.321  71.383  37.520  1.00 30.38           O  
ANISOU  558  O   LEU A 441     4276   3327   3939   -308    137    204       O  
ATOM    559  CB  LEU A 441      30.857  69.900  36.311  1.00 33.28           C  
ANISOU  559  CB  LEU A 441     4816   3572   4256   -264     21    244       C  
ATOM    560  CG  LEU A 441      32.235  69.312  36.629  1.00 32.59           C  
ANISOU  560  CG  LEU A 441     4800   3443   4137   -247      3    272       C  
ATOM    561  CD1 LEU A 441      32.242  67.824  36.256  1.00 35.69           C  
ANISOU  561  CD1 LEU A 441     5247   3772   4540   -276    -31    294       C  
ATOM    562  CD2 LEU A 441      33.355  70.049  35.935  1.00 33.27           C  
ANISOU  562  CD2 LEU A 441     4897   3520   4224   -176     -8    256       C  
ATOM    563  N   THR A 442      28.598  72.062  35.396  1.00 31.04           N  
ANISOU  563  N   THR A 442     4350   3378   4064   -211     48    191       N  
ATOM    564  CA  THR A 442      27.177  72.312  35.140  1.00 32.03           C  
ANISOU  564  CA  THR A 442     4375   3548   4246   -220     48    184       C  
ATOM    565  C   THR A 442      26.405  71.003  35.237  1.00 31.91           C  
ANISOU  565  C   THR A 442     4341   3543   4240   -310     30    197       C  
ATOM    566  O   THR A 442      26.799  69.999  34.665  1.00 32.32           O  
ANISOU  566  O   THR A 442     4458   3553   4269   -343    -21    207       O  
ATOM    567  CB  THR A 442      26.912  72.902  33.716  1.00 31.92           C  
ANISOU  567  CB  THR A 442     4333   3531   4262   -161    -18    184       C  
ATOM    568  OG1 THR A 442      27.469  72.039  32.718  1.00 31.42           O  
ANISOU  568  OG1 THR A 442     4342   3430   4163   -179    -86    191       O  
ATOM    569  CG2 THR A 442      27.503  74.266  33.578  1.00 31.92           C  
ANISOU  569  CG2 THR A 442     4348   3514   4265    -78      3    176       C  
ATOM    570  N   HIS A 443      25.312  71.027  35.966  1.00 31.89           N  
ANISOU  570  N   HIS A 443     4251   3593   4272   -354     82    194       N  
ATOM    571  CA  HIS A 443      24.503  69.855  36.183  1.00 33.40           C  
ANISOU  571  CA  HIS A 443     4416   3798   4475   -456     79    208       C  
ATOM    572  C   HIS A 443      23.352  69.878  35.175  1.00 34.17           C  
ANISOU  572  C   HIS A 443     4405   3938   4639   -466     18    202       C  
ATOM    573  O   HIS A 443      22.716  70.922  34.942  1.00 35.03           O  
ANISOU  573  O   HIS A 443     4411   4094   4803   -402     25    192       O  
ATOM    574  CB  HIS A 443      23.954  69.864  37.623  1.00 36.22           C  
ANISOU  574  CB  HIS A 443     4733   4200   4827   -511    183    209       C  
ATOM    575  CG  HIS A 443      25.008  69.650  38.669  1.00 39.31           C  
ANISOU  575  CG  HIS A 443     5237   4559   5139   -525    225    224       C  
ATOM    576  ND1 HIS A 443      24.777  69.849  40.009  1.00 43.52           N  
ANISOU  576  ND1 HIS A 443     5766   5131   5636   -566    322    222       N  
ATOM    577  CD2 HIS A 443      26.308  69.271  38.566  1.00 38.86           C  
ANISOU  577  CD2 HIS A 443     5295   4440   5028   -503    181    244       C  
ATOM    578  CE1 HIS A 443      25.878  69.589  40.692  1.00 42.11           C  
ANISOU  578  CE1 HIS A 443     5701   4919   5379   -574    321    245       C  
ATOM    579  NE2 HIS A 443      26.813  69.216  39.838  1.00 40.89           N  
ANISOU  579  NE2 HIS A 443     5611   4704   5222   -533    235    261       N  
ATOM    580  N   MET A 444      23.113  68.720  34.595  1.00 33.89           N  
ANISOU  580  N   MET A 444     4398   3880   4598   -547    -44    210       N  
ATOM    581  CA  MET A 444      22.044  68.439  33.657  1.00 35.39           C  
ANISOU  581  CA  MET A 444     4499   4110   4837   -592   -120    206       C  
ATOM    582  C   MET A 444      20.919  67.658  34.345  1.00 36.96           C  
ANISOU  582  C   MET A 444     4611   4354   5077   -713    -81    214       C  
ATOM    583  O   MET A 444      21.165  66.657  34.974  1.00 36.44           O  
ANISOU  583  O   MET A 444     4623   4243   4976   -798    -48    226       O  
ATOM    584  CB  MET A 444      22.614  67.605  32.531  1.00 36.19           C  
ANISOU  584  CB  MET A 444     4711   4146   4892   -618   -213    199       C  
ATOM    585  CG  MET A 444      21.612  67.247  31.429  1.00 38.87           C  
ANISOU  585  CG  MET A 444     4983   4525   5259   -679   -313    190       C  
ATOM    586  SD  MET A 444      20.921  65.601  31.655  1.00 45.16           S  
ANISOU  586  SD  MET A 444     5795   5297   6064   -854   -325    186       S  
ATOM    587  CE  MET A 444      22.437  64.735  31.187  1.00 43.63           C  
ANISOU  587  CE  MET A 444     5823   4967   5785   -838   -343    169       C  
ATOM    588  N   PHE A 445      19.677  68.093  34.187  1.00 38.53           N  
ANISOU  588  N   PHE A 445     4645   4641   5354   -723    -88    211       N  
ATOM    589  CA  PHE A 445      18.540  67.383  34.780  1.00 40.16           C  
ANISOU  589  CA  PHE A 445     4745   4902   5609   -848    -46    217       C  
ATOM    590  C   PHE A 445      17.992  66.362  33.794  1.00 40.88           C  
ANISOU  590  C   PHE A 445     4829   4990   5711   -957   -158    215       C  
ATOM    591  O   PHE A 445      17.606  65.228  34.165  1.00 41.03           O  
ANISOU  591  O   PHE A 445     4867   4992   5728  -1097   -141    222       O  
ATOM    592  CB  PHE A 445      17.438  68.365  35.185  1.00 42.59           C  
ANISOU  592  CB  PHE A 445     4856   5316   6011   -802     14    211       C  
ATOM    593  CG  PHE A 445      17.788  69.219  36.372  1.00 44.30           C  
ANISOU  593  CG  PHE A 445     5081   5537   6214   -729    150    199       C  
ATOM    594  CD1 PHE A 445      18.240  70.522  36.200  1.00 43.56           C  
ANISOU  594  CD1 PHE A 445     4988   5433   6130   -583    158    186       C  
ATOM    595  CD2 PHE A 445      17.635  68.726  37.674  1.00 48.40           C  
ANISOU  595  CD2 PHE A 445     5616   6068   6705   -816    272    202       C  
ATOM    596  CE1 PHE A 445      18.552  71.321  37.285  1.00 43.20           C  
ANISOU  596  CE1 PHE A 445     4959   5385   6067   -525    282    164       C  
ATOM    597  CE2 PHE A 445      17.956  69.520  38.775  1.00 48.25           C  
ANISOU  597  CE2 PHE A 445     5618   6058   6657   -759    396    183       C  
ATOM    598  CZ  PHE A 445      18.425  70.821  38.570  1.00 46.72           C  
ANISOU  598  CZ  PHE A 445     5426   5849   6474   -614    399    159       C  
ATOM    599  N   CYS A 446      17.904  66.772  32.534  1.00 39.95           N  
ANISOU  599  N   CYS A 446     4687   4889   5602   -904   -273    208       N  
ATOM    600  CA  CYS A 446      17.450  65.873  31.502  1.00 40.26           C  
ANISOU  600  CA  CYS A 446     4736   4925   5634  -1010   -391    198       C  
ATOM    601  C   CYS A 446      17.763  66.326  30.112  1.00 38.62           C  
ANISOU  601  C   CYS A 446     4570   4713   5391   -940   -515    190       C  
ATOM    602  O   CYS A 446      18.074  67.475  29.856  1.00 37.16           O  
ANISOU  602  O   CYS A 446     4364   4546   5209   -806   -521    202       O  
ATOM    603  CB  CYS A 446      15.946  65.617  31.616  1.00 46.23           C  
ANISOU  603  CB  CYS A 446     5297   5786   6482  -1118   -407    204       C  
ATOM    604  SG  CYS A 446      14.947  67.051  31.231  1.00 50.04           S  
ANISOU  604  SG  CYS A 446     5545   6399   7068  -1001   -448    221       S  
ATOM    605  N   THR A 447      17.567  65.411  29.188  1.00 40.66           N  
ANISOU  605  N   THR A 447     4884   4951   5614  -1044   -618    170       N  
ATOM    606  CA  THR A 447      18.026  65.573  27.833  1.00 40.52           C  
ANISOU  606  CA  THR A 447     4957   4911   5526  -1004   -731    155       C  
ATOM    607  C   THR A 447      16.906  64.891  27.021  1.00 41.62           C  
ANISOU  607  C   THR A 447     5020   5111   5680  -1144   -856    141       C  
ATOM    608  O   THR A 447      16.439  63.817  27.409  1.00 40.21           O  
ANISOU  608  O   THR A 447     4840   4915   5522  -1288   -841    124       O  
ATOM    609  CB  THR A 447      19.452  64.949  27.890  1.00 42.57           C  
ANISOU  609  CB  THR A 447     5437   5038   5699   -986   -678    129       C  
ATOM    610  OG1 THR A 447      20.482  65.844  27.403  1.00 42.89           O  
ANISOU  610  OG1 THR A 447     5558   5051   5686   -847   -676    133       O  
ATOM    611  CG2 THR A 447      19.533  63.625  27.361  1.00 40.71           C  
ANISOU  611  CG2 THR A 447     5322   4729   5415  -1110   -724     90       C  
ATOM    612  N   PHE A 448      16.364  65.567  26.006  1.00 40.39           N  
ANISOU  612  N   PHE A 448     4781   5038   5527  -1108   -980    157       N  
ATOM    613  CA  PHE A 448      15.375  64.947  25.113  1.00 42.27           C  
ANISOU  613  CA  PHE A 448     4955   5340   5762  -1245  -1124    143       C  
ATOM    614  C   PHE A 448      15.498  65.471  23.689  1.00 42.80           C  
ANISOU  614  C   PHE A 448     5073   5439   5749  -1197  -1270    149       C  
ATOM    615  O   PHE A 448      16.151  66.495  23.442  1.00 40.61           O  
ANISOU  615  O   PHE A 448     4835   5149   5442  -1047  -1257    177       O  
ATOM    616  CB  PHE A 448      13.914  65.054  25.629  1.00 43.81           C  
ANISOU  616  CB  PHE A 448     4892   5662   6088  -1311  -1138    172       C  
ATOM    617  CG  PHE A 448      13.362  66.464  25.662  1.00 45.27           C  
ANISOU  617  CG  PHE A 448     4887   5951   6360  -1162  -1155    227       C  
ATOM    618  CD1 PHE A 448      12.479  66.907  24.688  1.00 47.12           C  
ANISOU  618  CD1 PHE A 448     4984   6293   6622  -1160  -1318    259       C  
ATOM    619  CD2 PHE A 448      13.722  67.345  26.676  1.00 44.74           C  
ANISOU  619  CD2 PHE A 448     4783   5868   6348  -1023  -1012    247       C  
ATOM    620  CE1 PHE A 448      11.962  68.200  24.723  1.00 47.50           C  
ANISOU  620  CE1 PHE A 448     4858   6424   6765  -1009  -1334    317       C  
ATOM    621  CE2 PHE A 448      13.217  68.634  26.711  1.00 45.15           C  
ANISOU  621  CE2 PHE A 448     4671   5995   6487   -881  -1018    292       C  
ATOM    622  CZ  PHE A 448      12.341  69.065  25.733  1.00 46.23           C  
ANISOU  622  CZ  PHE A 448     4670   6230   6664   -866  -1178    330       C  
ATOM    623  N   GLN A 449      14.905  64.737  22.753  1.00 44.88           N  
ANISOU  623  N   GLN A 449     5349   5736   5966  -1337  -1407    121       N  
ATOM    624  CA  GLN A 449      14.953  65.111  21.343  1.00 46.51           C  
ANISOU  624  CA  GLN A 449     5617   5979   6072  -1320  -1560    126       C  
ATOM    625  C   GLN A 449      13.587  65.063  20.699  1.00 49.31           C  
ANISOU  625  C   GLN A 449     5798   6470   6465  -1422  -1732    148       C  
ATOM    626  O   GLN A 449      12.708  64.358  21.179  1.00 50.33           O  
ANISOU  626  O   GLN A 449     5804   6642   6675  -1556  -1737    134       O  
ATOM    627  CB  GLN A 449      15.888  64.177  20.583  1.00 47.12           C  
ANISOU  627  CB  GLN A 449     5955   5943   6004  -1394  -1568     51       C  
ATOM    628  CG  GLN A 449      15.456  62.716  20.527  1.00 50.39           C  
ANISOU  628  CG  GLN A 449     6424   6316   6403  -1599  -1597    -16       C  
ATOM    629  CD  GLN A 449      16.510  61.851  19.865  1.00 50.85           C  
ANISOU  629  CD  GLN A 449     6754   6239   6327  -1642  -1574    -98       C  
ATOM    630  OE1 GLN A 449      16.900  62.106  18.723  1.00 51.59           O  
ANISOU  630  OE1 GLN A 449     6964   6338   6299  -1619  -1654   -117       O  
ATOM    631  NE2 GLN A 449      16.981  60.833  20.573  1.00 49.03           N  
ANISOU  631  NE2 GLN A 449     6629   5883   6115  -1701  -1460   -143       N  
ATOM    632  N   THR A 450      13.444  65.807  19.596  1.00 51.11           N  
ANISOU  632  N   THR A 450     6022   6766   6630  -1364  -1877    188       N  
ATOM    633  CA  THR A 450      12.332  65.657  18.620  1.00 52.57           C  
ANISOU  633  CA  THR A 450     6097   7077   6798  -1477  -2088    205       C  
ATOM    634  C   THR A 450      12.938  65.441  17.245  1.00 52.26           C  
ANISOU  634  C   THR A 450     6284   7006   6567  -1519  -2202    171       C  
ATOM    635  O   THR A 450      14.166  65.464  17.095  1.00 49.25           O  
ANISOU  635  O   THR A 450     6117   6510   6084  -1450  -2105    138       O  
ATOM    636  CB  THR A 450      11.473  66.938  18.534  1.00 55.26           C  
ANISOU  636  CB  THR A 450     6198   7550   7246  -1347  -2180    308       C  
ATOM    637  OG1 THR A 450      12.298  68.040  18.116  1.00 55.04           O  
ANISOU  637  OG1 THR A 450     6275   7481   7154  -1168  -2168    357       O  
ATOM    638  CG2 THR A 450      10.839  67.270  19.894  1.00 55.83           C  
ANISOU  638  CG2 THR A 450     6037   7662   7513  -1289  -2052    337       C  
ATOM    639  N   LYS A 451      12.098  65.285  16.219  1.00 56.24           N  
ANISOU  639  N   LYS A 451     6737   7616   7013  -1629  -2408    181       N  
ATOM    640  CA  LYS A 451      12.623  65.070  14.866  1.00 57.43           C  
ANISOU  640  CA  LYS A 451     7115   7745   6959  -1684  -2519    144       C  
ATOM    641  C   LYS A 451      13.611  66.170  14.434  1.00 55.09           C  
ANISOU  641  C   LYS A 451     6944   7409   6577  -1497  -2479    197       C  
ATOM    642  O   LYS A 451      14.597  65.856  13.787  1.00 55.21           O  
ANISOU  642  O   LYS A 451     7205   7337   6434  -1512  -2442    138       O  
ATOM    643  CB  LYS A 451      11.502  64.811  13.827  1.00 61.90           C  
ANISOU  643  CB  LYS A 451     7598   8451   7468  -1836  -2768    156       C  
ATOM    644  CG  LYS A 451      10.699  66.007  13.352  1.00 64.71           C  
ANISOU  644  CG  LYS A 451     7758   8957   7870  -1732  -2937    282       C  
ATOM    645  CD  LYS A 451       9.705  65.605  12.257  1.00 69.19           C  
ANISOU  645  CD  LYS A 451     8274   9660   8354  -1904  -3198    285       C  
ATOM    646  CE  LYS A 451       8.629  66.668  12.063  1.00 71.14           C  
ANISOU  646  CE  LYS A 451     8243  10073   8712  -1808  -3370    422       C  
ATOM    647  NZ  LYS A 451       7.700  66.356  10.940  1.00 75.60           N  
ANISOU  647  NZ  LYS A 451     8756  10783   9185  -1970  -3647    439       N  
ATOM    648  N   GLU A 452      13.397  67.423  14.857  1.00 54.18           N  
ANISOU  648  N   GLU A 452     6667   7344   6575  -1323  -2465    300       N  
ATOM    649  CA  GLU A 452      14.276  68.564  14.480  1.00 52.57           C  
ANISOU  649  CA  GLU A 452     6571   7099   6304  -1149  -2428    361       C  
ATOM    650  C   GLU A 452      15.287  69.037  15.524  1.00 49.39           C  
ANISOU  650  C   GLU A 452     6210   6583   5972  -1004  -2205    356       C  
ATOM    651  O   GLU A 452      16.287  69.679  15.173  1.00 46.45           O  
ANISOU  651  O   GLU A 452     5988   6146   5513   -901  -2148    374       O  
ATOM    652  CB  GLU A 452      13.431  69.809  14.143  1.00 54.46           C  
ANISOU  652  CB  GLU A 452     6624   7453   6615  -1033  -2572    490       C  
ATOM    653  CG  GLU A 452      12.575  69.706  12.892  1.00 58.03           C  
ANISOU  653  CG  GLU A 452     7051   8030   6969  -1135  -2827    529       C  
ATOM    654  CD  GLU A 452      11.949  71.037  12.487  1.00 59.01           C  
ANISOU  654  CD  GLU A 452     7024   8244   7150   -989  -2966    674       C  
ATOM    655  OE1 GLU A 452      11.173  71.058  11.540  1.00 62.53           O  
ANISOU  655  OE1 GLU A 452     7419   8806   7533  -1056  -3189    726       O  
ATOM    656  OE2 GLU A 452      12.231  72.077  13.095  1.00 60.38           O  
ANISOU  656  OE2 GLU A 452     7137   8373   7432   -805  -2860    738       O  
ATOM    657  N   ASN A 453      14.991  68.793  16.799  1.00 47.67           N  
ANISOU  657  N   ASN A 453     5852   6350   5909   -999  -2087    339       N  
ATOM    658  CA  ASN A 453      15.686  69.468  17.885  1.00 46.03           C  
ANISOU  658  CA  ASN A 453     5630   6068   5791   -852  -1903    355       C  
ATOM    659  C   ASN A 453      16.354  68.536  18.866  1.00 43.95           C  
ANISOU  659  C   ASN A 453     5449   5704   5546   -907  -1733    274       C  
ATOM    660  O   ASN A 453      15.900  67.423  19.081  1.00 43.81           O  
ANISOU  660  O   ASN A 453     5415   5688   5542  -1051  -1743    220       O  
ATOM    661  CB  ASN A 453      14.717  70.355  18.670  1.00 46.84           C  
ANISOU  661  CB  ASN A 453     5473   6249   6075   -754  -1898    427       C  
ATOM    662  CG  ASN A 453      14.018  71.368  17.788  1.00 48.17           C  
ANISOU  662  CG  ASN A 453     5538   6510   6252   -673  -2067    525       C  
ATOM    663  OD1 ASN A 453      14.665  72.177  17.142  1.00 46.61           O  
ANISOU  663  OD1 ASN A 453     5460   6276   5971   -574  -2090    571       O  
ATOM    664  ND2 ASN A 453      12.694  71.302  17.737  1.00 49.26           N  
ANISOU  664  ND2 ASN A 453     5454   6770   6491   -720  -2192    561       N  
ATOM    665  N   LEU A 454      17.443  69.024  19.448  1.00 42.10           N  
ANISOU  665  N   LEU A 454     5303   5379   5310   -791  -1584    273       N  
ATOM    666  CA  LEU A 454      18.040  68.434  20.631  1.00 41.05           C  
ANISOU  666  CA  LEU A 454     5207   5163   5227   -801  -1418    225       C  
ATOM    667  C   LEU A 454      17.999  69.443  21.781  1.00 40.50           C  
ANISOU  667  C   LEU A 454     5005   5100   5281   -670  -1307    271       C  
ATOM    668  O   LEU A 454      18.336  70.626  21.594  1.00 40.25           O  
ANISOU  668  O   LEU A 454     4973   5067   5252   -537  -1301    320       O  
ATOM    669  CB  LEU A 454      19.483  68.050  20.346  1.00 39.88           C  
ANISOU  669  CB  LEU A 454     5289   4900   4962   -786  -1336    174       C  
ATOM    670  CG  LEU A 454      19.704  66.995  19.274  1.00 41.57           C  
ANISOU  670  CG  LEU A 454     5668   5081   5044   -908  -1409    107       C  
ATOM    671  CD1 LEU A 454      21.100  67.156  18.677  1.00 41.81           C  
ANISOU  671  CD1 LEU A 454     5900   5028   4956   -841  -1343     81       C  
ATOM    672  CD2 LEU A 454      19.520  65.590  19.836  1.00 42.60           C  
ANISOU  672  CD2 LEU A 454     5826   5156   5204  -1042  -1366     41       C  
ATOM    673  N   PHE A 455      17.642  68.961  22.969  1.00 39.89           N  
ANISOU  673  N   PHE A 455     4836   5021   5297   -714  -1212    252       N  
ATOM    674  CA  PHE A 455      17.488  69.801  24.161  1.00 39.57           C  
ANISOU  674  CA  PHE A 455     4670   4993   5371   -611  -1095    281       C  
ATOM    675  C   PHE A 455      18.256  69.233  25.365  1.00 38.70           C  
ANISOU  675  C   PHE A 455     4638   4801   5262   -631   -937    242       C  
ATOM    676  O   PHE A 455      18.048  68.067  25.733  1.00 38.76           O  
ANISOU  676  O   PHE A 455     4665   4791   5269   -757   -918    208       O  
ATOM    677  CB  PHE A 455      16.009  69.893  24.548  1.00 41.20           C  
ANISOU  677  CB  PHE A 455     4637   5310   5706   -646  -1133    307       C  
ATOM    678  CG  PHE A 455      15.127  70.553  23.518  1.00 42.63           C  
ANISOU  678  CG  PHE A 455     4698   5586   5912   -610  -1296    361       C  
ATOM    679  CD1 PHE A 455      15.234  71.916  23.262  1.00 43.53           C  
ANISOU  679  CD1 PHE A 455     4778   5704   6054   -447  -1311    420       C  
ATOM    680  CD2 PHE A 455      14.144  69.833  22.861  1.00 45.13           C  
ANISOU  680  CD2 PHE A 455     4927   5987   6231   -741  -1436    360       C  
ATOM    681  CE1 PHE A 455      14.418  72.538  22.332  1.00 44.65           C  
ANISOU  681  CE1 PHE A 455     4810   5930   6223   -404  -1470    484       C  
ATOM    682  CE2 PHE A 455      13.300  70.448  21.942  1.00 46.87           C  
ANISOU  682  CE2 PHE A 455     5024   6307   6477   -707  -1602    420       C  
ATOM    683  CZ  PHE A 455      13.444  71.809  21.677  1.00 47.17           C  
ANISOU  683  CZ  PHE A 455     5035   6345   6542   -531  -1621    487       C  
ATOM    684  N   PHE A 456      19.136  70.061  25.942  1.00 36.66           N  
ANISOU  684  N   PHE A 456     4431   4492   5004   -513   -835    252       N  
ATOM    685  CA  PHE A 456      19.750  69.854  27.259  1.00 35.98           C  
ANISOU  685  CA  PHE A 456     4382   4352   4935   -507   -688    232       C  
ATOM    686  C   PHE A 456      19.084  70.776  28.279  1.00 35.76           C  
ANISOU  686  C   PHE A 456     4196   4378   5013   -438   -606    253       C  
ATOM    687  O   PHE A 456      19.152  72.009  28.171  1.00 37.12           O  
ANISOU  687  O   PHE A 456     4330   4557   5216   -316   -599    277       O  
ATOM    688  CB  PHE A 456      21.239  70.210  27.244  1.00 34.19           C  
ANISOU  688  CB  PHE A 456     4317   4038   4633   -427   -629    223       C  
ATOM    689  CG  PHE A 456      22.062  69.423  26.262  1.00 34.90           C  
ANISOU  689  CG  PHE A 456     4572   4068   4621   -470   -682    195       C  
ATOM    690  CD1 PHE A 456      22.098  69.778  24.932  1.00 35.76           C  
ANISOU  690  CD1 PHE A 456     4727   4192   4669   -449   -782    204       C  
ATOM    691  CD2 PHE A 456      22.837  68.352  26.679  1.00 35.37           C  
ANISOU  691  CD2 PHE A 456     4747   4050   4641   -526   -624    161       C  
ATOM    692  CE1 PHE A 456      22.891  69.081  24.020  1.00 36.18           C  
ANISOU  692  CE1 PHE A 456     4940   4188   4616   -487   -812    169       C  
ATOM    693  CE2 PHE A 456      23.622  67.646  25.773  1.00 35.37           C  
ANISOU  693  CE2 PHE A 456     4897   3985   4554   -553   -656    127       C  
ATOM    694  CZ  PHE A 456      23.647  68.011  24.445  1.00 35.73           C  
ANISOU  694  CZ  PHE A 456     4990   4051   4534   -536   -743    125       C  
ATOM    695  N   VAL A 457      18.444  70.193  29.271  1.00 35.50           N  
ANISOU  695  N   VAL A 457     4077   4376   5036   -516   -536    241       N  
ATOM    696  CA  VAL A 457      17.798  70.959  30.328  1.00 35.79           C  
ANISOU  696  CA  VAL A 457     3968   4463   5167   -461   -434    248       C  
ATOM    697  C   VAL A 457      18.774  70.974  31.477  1.00 34.84           C  
ANISOU  697  C   VAL A 457     3958   4277   5002   -444   -300    228       C  
ATOM    698  O   VAL A 457      18.968  69.947  32.162  1.00 34.28           O  
ANISOU  698  O   VAL A 457     3946   4181   4897   -545   -248    216       O  
ATOM    699  CB  VAL A 457      16.462  70.322  30.742  1.00 37.44           C  
ANISOU  699  CB  VAL A 457     4008   4758   5458   -569   -427    247       C  
ATOM    700  CG1 VAL A 457      15.761  71.159  31.808  1.00 38.03           C  
ANISOU  700  CG1 VAL A 457     3925   4891   5634   -505   -305    247       C  
ATOM    701  CG2 VAL A 457      15.576  70.135  29.508  1.00 39.80           C  
ANISOU  701  CG2 VAL A 457     4209   5125   5786   -611   -588    267       C  
ATOM    702  N   MET A 458      19.440  72.122  31.616  1.00 34.73           N  
ANISOU  702  N   MET A 458     3983   4230   4982   -320   -257    229       N  
ATOM    703  CA  MET A 458      20.443  72.384  32.619  1.00 33.67           C  
ANISOU  703  CA  MET A 458     3950   4040   4802   -290   -146    211       C  
ATOM    704  C   MET A 458      19.915  73.224  33.803  1.00 35.91           C  
ANISOU  704  C   MET A 458     4134   4360   5150   -243    -21    195       C  
ATOM    705  O   MET A 458      18.865  73.896  33.751  1.00 34.70           O  
ANISOU  705  O   MET A 458     3827   4264   5092   -193    -13    199       O  
ATOM    706  CB  MET A 458      21.623  73.162  31.989  1.00 34.46           C  
ANISOU  706  CB  MET A 458     4170   4074   4846   -195   -175    216       C  
ATOM    707  CG  MET A 458      22.088  72.639  30.643  1.00 33.85           C  
ANISOU  707  CG  MET A 458     4183   3969   4708   -215   -291    227       C  
ATOM    708  SD  MET A 458      22.753  70.960  30.727  1.00 34.31           S  
ANISOU  708  SD  MET A 458     4368   3976   4690   -334   -298    209       S  
ATOM    709  CE  MET A 458      24.227  71.324  31.688  1.00 33.62           C  
ANISOU  709  CE  MET A 458     4395   3825   4554   -280   -197    200       C  
ATOM    710  N   GLU A 459      20.655  73.089  34.890  1.00 34.52           N  
ANISOU  710  N   GLU A 459     4049   4150   4916   -267     76    176       N  
ATOM    711  CA  GLU A 459      20.722  73.989  36.026  1.00 37.43           C  
ANISOU  711  CA  GLU A 459     4403   4521   5295   -216    202    147       C  
ATOM    712  C   GLU A 459      20.835  75.440  35.506  1.00 36.62           C  
ANISOU  712  C   GLU A 459     4280   4393   5241    -79    191    142       C  
ATOM    713  O   GLU A 459      21.691  75.700  34.662  1.00 32.19           O  
ANISOU  713  O   GLU A 459     3812   3779   4639    -36    116    159       O  
ATOM    714  CB  GLU A 459      22.059  73.586  36.689  1.00 40.59           C  
ANISOU  714  CB  GLU A 459     4970   4863   5587   -253    234    142       C  
ATOM    715  CG  GLU A 459      22.506  74.373  37.846  1.00 45.98           C  
ANISOU  715  CG  GLU A 459     5694   5537   6239   -223    345    109       C  
ATOM    716  CD  GLU A 459      23.728  73.808  38.514  1.00 41.70           C  
ANISOU  716  CD  GLU A 459     5297   4955   5591   -275    356    116       C  
ATOM    717  OE1 GLU A 459      24.699  73.262  37.892  1.00 38.80           O  
ANISOU  717  OE1 GLU A 459     5023   4539   5178   -280    274    140       O  
ATOM    718  OE2 GLU A 459      23.680  73.948  39.721  1.00 47.48           O  
ANISOU  718  OE2 GLU A 459     6043   5708   6286   -309    453     94       O  
ATOM    719  N   TYR A 460      19.968  76.346  35.969  1.00 35.60           N  
ANISOU  719  N   TYR A 460     4030   4295   5200    -12    269    122       N  
ATOM    720  CA  TYR A 460      20.094  77.773  35.643  1.00 36.46           C  
ANISOU  720  CA  TYR A 460     4133   4358   5360    122    277    116       C  
ATOM    721  C   TYR A 460      21.089  78.438  36.596  1.00 35.98           C  
ANISOU  721  C   TYR A 460     4196   4237   5236    140    381     71       C  
ATOM    722  O   TYR A 460      20.894  78.409  37.810  1.00 35.64           O  
ANISOU  722  O   TYR A 460     4145   4218   5179    102    501     28       O  
ATOM    723  CB  TYR A 460      18.739  78.497  35.737  1.00 37.64           C  
ANISOU  723  CB  TYR A 460     4098   4556   5646    201    322    111       C  
ATOM    724  CG  TYR A 460      18.857  79.992  35.461  1.00 38.23           C  
ANISOU  724  CG  TYR A 460     4179   4563   5783    349    338    108       C  
ATOM    725  CD1 TYR A 460      19.499  80.463  34.319  1.00 38.86           C  
ANISOU  725  CD1 TYR A 460     4341   4581   5840    408    224    154       C  
ATOM    726  CD2 TYR A 460      18.371  80.926  36.367  1.00 39.82           C  
ANISOU  726  CD2 TYR A 460     4318   4750   6058    424    477     57       C  
ATOM    727  CE1 TYR A 460      19.647  81.818  34.090  1.00 40.74           C  
ANISOU  727  CE1 TYR A 460     4602   4743   6133    534    242    158       C  
ATOM    728  CE2 TYR A 460      18.489  82.281  36.133  1.00 41.87           C  
ANISOU  728  CE2 TYR A 460     4597   4929   6381    558    497     53       C  
ATOM    729  CZ  TYR A 460      19.123  82.729  34.997  1.00 41.84           C  
ANISOU  729  CZ  TYR A 460     4678   4860   6358    612    375    108       C  
ATOM    730  OH  TYR A 460      19.240  84.087  34.783  1.00 43.60           O  
ANISOU  730  OH  TYR A 460     4931   4988   6644    740    398    110       O  
ATOM    731  N   LEU A 461      22.146  79.021  36.044  1.00 34.93           N  
ANISOU  731  N   LEU A 461     4179   4032   5059    188    333     81       N  
ATOM    732  CA  LEU A 461      23.243  79.616  36.825  1.00 35.42           C  
ANISOU  732  CA  LEU A 461     4367   4036   5053    189    407     41       C  
ATOM    733  C   LEU A 461      23.291  81.098  36.490  1.00 36.56           C  
ANISOU  733  C   LEU A 461     4519   4113   5259    305    426     31       C  
ATOM    734  O   LEU A 461      23.604  81.434  35.351  1.00 37.50           O  
ANISOU  734  O   LEU A 461     4666   4193   5388    355    333     76       O  
ATOM    735  CB  LEU A 461      24.580  78.948  36.437  1.00 34.86           C  
ANISOU  735  CB  LEU A 461     4428   3936   4880    132    334     65       C  
ATOM    736  CG  LEU A 461      24.649  77.452  36.777  1.00 35.35           C  
ANISOU  736  CG  LEU A 461     4505   4042   4882     24    313     79       C  
ATOM    737  CD1 LEU A 461      25.716  76.699  35.997  1.00 37.13           C  
ANISOU  737  CD1 LEU A 461     4828   4236   5041     -6    221    112       C  
ATOM    738  CD2 LEU A 461      24.871  77.277  38.273  1.00 35.96           C  
ANISOU  738  CD2 LEU A 461     4623   4138   4902    -38    417     44       C  
ATOM    739  N   ASN A 462      22.964  81.986  37.435  1.00 38.57           N  
ANISOU  739  N   ASN A 462     4756   4346   5553    348    549    -26       N  
ATOM    740  CA  ASN A 462      22.778  83.413  37.081  1.00 40.24           C  
ANISOU  740  CA  ASN A 462     4960   4478   5850    471    572    -33       C  
ATOM    741  C   ASN A 462      23.842  84.396  37.563  1.00 38.89           C  
ANISOU  741  C   ASN A 462     4931   4215   5631    480    633    -81       C  
ATOM    742  O   ASN A 462      23.639  85.613  37.563  1.00 38.84           O  
ANISOU  742  O   ASN A 462     4931   4128   5696    574    686   -104       O  
ATOM    743  CB  ASN A 462      21.376  83.896  37.446  1.00 42.80           C  
ANISOU  743  CB  ASN A 462     5133   4828   6302    552    653    -58       C  
ATOM    744  CG  ASN A 462      21.080  83.841  38.922  1.00 45.70           C  
ANISOU  744  CG  ASN A 462     5489   5226   6645    504    812   -141       C  
ATOM    745  OD1 ASN A 462      21.910  83.464  39.745  1.00 43.92           O  
ANISOU  745  OD1 ASN A 462     5378   5007   6303    407    855   -178       O  
ATOM    746  ND2 ASN A 462      19.863  84.253  39.269  1.00 52.11           N  
ANISOU  746  ND2 ASN A 462     6159   6065   7574    577    903   -170       N  
ATOM    747  N   GLY A 463      24.993  83.868  37.920  1.00 37.78           N  
ANISOU  747  N   GLY A 463     4902   4079   5373    384    619    -91       N  
ATOM    748  CA  GLY A 463      26.081  84.698  38.387  1.00 38.64           C  
ANISOU  748  CA  GLY A 463     5140   4115   5426    368    663   -135       C  
ATOM    749  C   GLY A 463      26.793  85.385  37.257  1.00 39.04           C  
ANISOU  749  C   GLY A 463     5254   4086   5491    416    586    -89       C  
ATOM    750  O   GLY A 463      27.481  86.385  37.488  1.00 41.86           O  
ANISOU  750  O   GLY A 463     5703   4361   5839    423    628   -124       O  
ATOM    751  N   GLY A 464      26.666  84.826  36.051  1.00 38.51           N  
ANISOU  751  N   GLY A 464     5149   4044   5437    434    475    -13       N  
ATOM    752  CA  GLY A 464      27.336  85.318  34.839  1.00 36.65           C  
ANISOU  752  CA  GLY A 464     4979   3748   5198    467    395     43       C  
ATOM    753  C   GLY A 464      28.664  84.640  34.549  1.00 36.78           C  
ANISOU  753  C   GLY A 464     5081   3780   5110    382    344     59       C  
ATOM    754  O   GLY A 464      29.328  84.084  35.457  1.00 34.04           O  
ANISOU  754  O   GLY A 464     4769   3468   4696    301    377     20       O  
ATOM    755  N   ASP A 465      29.077  84.684  33.290  1.00 35.04           N  
ANISOU  755  N   ASP A 465     4896   3538   4877    400    264    119       N  
ATOM    756  CA  ASP A 465      30.304  84.007  32.883  1.00 36.16           C  
ANISOU  756  CA  ASP A 465     5106   3698   4933    330    222    135       C  
ATOM    757  C   ASP A 465      31.544  84.881  33.068  1.00 35.68           C  
ANISOU  757  C   ASP A 465     5140   3574   4842    303    263    116       C  
ATOM    758  O   ASP A 465      31.453  86.118  33.160  1.00 35.38           O  
ANISOU  758  O   ASP A 465     5136   3458   4849    345    306    104       O  
ATOM    759  CB  ASP A 465      30.179  83.410  31.472  1.00 40.21           C  
ANISOU  759  CB  ASP A 465     5615   4236   5427    343    126    199       C  
ATOM    760  CG  ASP A 465      30.322  84.417  30.385  1.00 45.56           C  
ANISOU  760  CG  ASP A 465     6344   4848   6118    397     95    249       C  
ATOM    761  OD1 ASP A 465      29.307  84.724  29.754  1.00 55.04           O  
ANISOU  761  OD1 ASP A 465     7497   6045   7370    464     46    292       O  
ATOM    762  OD2 ASP A 465      31.449  84.912  30.151  1.00 51.05           O  
ANISOU  762  OD2 ASP A 465     7125   5498   6773    371    116    252       O  
ATOM    763  N   LEU A 466      32.688  84.231  33.200  1.00 33.78           N  
ANISOU  763  N   LEU A 466     4938   3365   4532    231    253    109       N  
ATOM    764  CA  LEU A 466      33.900  84.943  33.505  1.00 36.95           C  
ANISOU  764  CA  LEU A 466     5408   3724   4905    186    288     86       C  
ATOM    765  C   LEU A 466      34.317  85.922  32.413  1.00 38.45           C  
ANISOU  765  C   LEU A 466     5656   3841   5109    214    279    126       C  
ATOM    766  O   LEU A 466      34.813  86.994  32.746  1.00 37.37           O  
ANISOU  766  O   LEU A 466     5575   3636   4985    196    326    102       O  
ATOM    767  CB  LEU A 466      35.032  83.994  33.841  1.00 35.54           C  
ANISOU  767  CB  LEU A 466     5237   3604   4662    112    271     79       C  
ATOM    768  CG  LEU A 466      34.823  83.260  35.163  1.00 37.55           C  
ANISOU  768  CG  LEU A 466     5460   3915   4890     71    289     41       C  
ATOM    769  CD1 LEU A 466      36.108  82.558  35.561  1.00 39.16           C  
ANISOU  769  CD1 LEU A 466     5678   4162   5037      4    266     42       C  
ATOM    770  CD2 LEU A 466      34.364  84.191  36.269  1.00 38.62           C  
ANISOU  770  CD2 LEU A 466     5610   4020   5040     65    360    -17       C  
ATOM    771  N   MET A 467      34.088  85.568  31.143  1.00 38.75           N  
ANISOU  771  N   MET A 467     5693   3890   5140    247    219    187       N  
ATOM    772  CA  MET A 467      34.373  86.465  30.002  1.00 40.44           C  
ANISOU  772  CA  MET A 467     5972   4037   5356    273    206    241       C  
ATOM    773  C   MET A 467      33.582  87.749  30.134  1.00 39.72           C  
ANISOU  773  C   MET A 467     5897   3855   5340    341    232    247       C  
ATOM    774  O   MET A 467      34.107  88.826  29.969  1.00 41.69           O  
ANISOU  774  O   MET A 467     6220   4019   5602    335    266    256       O  
ATOM    775  CB  MET A 467      34.057  85.771  28.651  1.00 44.17           C  
ANISOU  775  CB  MET A 467     6441   4547   5791    296    130    303       C  
ATOM    776  CG  MET A 467      34.568  86.522  27.430  1.00 52.84           C  
ANISOU  776  CG  MET A 467     7624   5592   6860    301    118    365       C  
ATOM    777  SD  MET A 467      36.335  86.917  27.523  1.00 57.40           S  
ANISOU  777  SD  MET A 467     8269   6146   7394    212    187    344       S  
ATOM    778  CE  MET A 467      37.061  85.429  26.904  1.00 59.43           C  
ANISOU  778  CE  MET A 467     8508   6498   7574    170    164    341       C  
ATOM    779  N   TYR A 468      32.310  87.634  30.479  1.00 39.04           N  
ANISOU  779  N   TYR A 468     5737   3785   5312    406    223    240       N  
ATOM    780  CA  TYR A 468      31.473  88.769  30.703  1.00 39.85           C  
ANISOU  780  CA  TYR A 468     5836   3802   5502    488    257    239       C  
ATOM    781  C   TYR A 468      31.994  89.584  31.895  1.00 40.50           C  
ANISOU  781  C   TYR A 468     5970   3819   5600    452    356    159       C  
ATOM    782  O   TYR A 468      32.066  90.809  31.817  1.00 37.56           O  
ANISOU  782  O   TYR A 468     5665   3333   5274    486    394    162       O  
ATOM    783  CB  TYR A 468      30.040  88.315  30.974  1.00 41.83           C  
ANISOU  783  CB  TYR A 468     5971   4105   5816    556    239    236       C  
ATOM    784  CG  TYR A 468      29.143  89.386  31.482  1.00 43.82           C  
ANISOU  784  CG  TYR A 468     6196   4278   6174    649    297    215       C  
ATOM    785  CD1 TYR A 468      28.527  90.265  30.609  1.00 48.21           C  
ANISOU  785  CD1 TYR A 468     6756   4758   6803    752    256    287       C  
ATOM    786  CD2 TYR A 468      28.893  89.531  32.846  1.00 48.00           C  
ANISOU  786  CD2 TYR A 468     6700   4806   6732    639    397    124       C  
ATOM    787  CE1 TYR A 468      27.704  91.253  31.075  1.00 50.20           C  
ANISOU  787  CE1 TYR A 468     6980   4925   7168    852    315    267       C  
ATOM    788  CE2 TYR A 468      28.052  90.524  33.321  1.00 48.74           C  
ANISOU  788  CE2 TYR A 468     6769   4819   6928    732    468     93       C  
ATOM    789  CZ  TYR A 468      27.468  91.376  32.423  1.00 52.32           C  
ANISOU  789  CZ  TYR A 468     7220   5190   7468    845    427    165       C  
ATOM    790  OH  TYR A 468      26.633  92.369  32.852  1.00 56.24           O  
ANISOU  790  OH  TYR A 468     7689   5595   8083    955    499    138       O  
ATOM    791  N   HIS A 469      32.380  88.921  32.986  1.00 36.01           N  
ANISOU  791  N   HIS A 469     5379   3315   4985    379    393     90       N  
ATOM    792  CA  HIS A 469      32.857  89.688  34.159  1.00 34.83           C  
ANISOU  792  CA  HIS A 469     5286   3112   4833    331    480      7       C  
ATOM    793  C   HIS A 469      34.223  90.368  33.928  1.00 35.35           C  
ANISOU  793  C   HIS A 469     5450   3118   4861    255    489      7       C  
ATOM    794  O   HIS A 469      34.467  91.479  34.436  1.00 36.45           O  
ANISOU  794  O   HIS A 469     5662   3160   5025    239    553    -40       O  
ATOM    795  CB  HIS A 469      32.877  88.814  35.413  1.00 34.48           C  
ANISOU  795  CB  HIS A 469     5201   3160   4737    267    509    -58       C  
ATOM    796  CG  HIS A 469      31.514  88.572  35.999  1.00 33.79           C  
ANISOU  796  CG  HIS A 469     5034   3103   4701    328    547    -86       C  
ATOM    797  ND1 HIS A 469      30.693  89.595  36.422  1.00 34.23           N  
ANISOU  797  ND1 HIS A 469     5091   3079   4835    400    625   -129       N  
ATOM    798  CD2 HIS A 469      30.816  87.429  36.191  1.00 30.90           C  
ANISOU  798  CD2 HIS A 469     4580   2836   4325    328    524    -75       C  
ATOM    799  CE1 HIS A 469      29.555  89.094  36.872  1.00 34.57           C  
ANISOU  799  CE1 HIS A 469     5038   3180   4914    443    653   -146       C  
ATOM    800  NE2 HIS A 469      29.609  87.780  36.744  1.00 33.96           N  
ANISOU  800  NE2 HIS A 469     4906   3213   4782    392    591   -112       N  
ATOM    801  N   ILE A 470      35.120  89.713  33.195  1.00 33.58           N  
ANISOU  801  N   ILE A 470     5228   2949   4578    203    434     55       N  
ATOM    802  CA  ILE A 470      36.467  90.252  32.997  1.00 34.93           C  
ANISOU  802  CA  ILE A 470     5471   3084   4715    119    448     55       C  
ATOM    803  C   ILE A 470      36.474  91.430  32.024  1.00 37.54           C  
ANISOU  803  C   ILE A 470     5880   3295   5087    155    458    109       C  
ATOM    804  O   ILE A 470      37.431  92.214  32.011  1.00 38.31           O  
ANISOU  804  O   ILE A 470     6049   3329   5174     82    491     99       O  
ATOM    805  CB  ILE A 470      37.483  89.171  32.540  1.00 34.21           C  
ANISOU  805  CB  ILE A 470     5347   3092   4557     57    402     85       C  
ATOM    806  CG1 ILE A 470      38.886  89.589  32.951  1.00 35.78           C  
ANISOU  806  CG1 ILE A 470     5582   3285   4725    -50    430     53       C  
ATOM    807  CG2 ILE A 470      37.443  88.953  31.022  1.00 34.63           C  
ANISOU  807  CG2 ILE A 470     5410   3145   4601     98    358    168       C  
ATOM    808  CD1 ILE A 470      39.916  88.520  32.851  1.00 35.94           C  
ANISOU  808  CD1 ILE A 470     5551   3410   4695   -106    396     65       C  
ATOM    809  N   GLN A 471      35.407  91.570  31.234  1.00 41.19           N  
ANISOU  809  N   GLN A 471     6328   3725   5596    260    425    170       N  
ATOM    810  CA  GLN A 471      35.289  92.680  30.283  1.00 44.25           C  
ANISOU  810  CA  GLN A 471     6797   3992   6023    308    422    238       C  
ATOM    811  C   GLN A 471      35.280  94.031  30.990  1.00 44.04           C  
ANISOU  811  C   GLN A 471     6847   3824   6059    310    500    188       C  
ATOM    812  O   GLN A 471      35.907  94.950  30.502  1.00 40.98           O  
ANISOU  812  O   GLN A 471     6558   3336   5677    275    520    220       O  
ATOM    813  CB  GLN A 471      34.018  92.610  29.419  1.00 48.53           C  
ANISOU  813  CB  GLN A 471     7299   4528   6609    431    358    317       C  
ATOM    814  CG  GLN A 471      33.971  91.544  28.336  1.00 55.16           C  
ANISOU  814  CG  GLN A 471     8100   5472   7383    431    272    385       C  
ATOM    815  CD  GLN A 471      35.302  91.342  27.648  1.00 58.07           C  
ANISOU  815  CD  GLN A 471     8533   5865   7665    335    274    410       C  
ATOM    816  OE1 GLN A 471      35.781  92.212  26.910  1.00 65.54           O  
ANISOU  816  OE1 GLN A 471     9572   6727   8601    320    285    466       O  
ATOM    817  NE2 GLN A 471      35.920  90.207  27.903  1.00 60.02           N  
ANISOU  817  NE2 GLN A 471     8730   6220   7852    270    270    371       N  
ATOM    818  N   SER A 472      34.532  94.175  32.086  1.00 43.10           N  
ANISOU  818  N   SER A 472     6694   3690   5990    351    549    109       N  
ATOM    819  CA  SER A 472      34.452  95.480  32.735  1.00 46.57           C  
ANISOU  819  CA  SER A 472     7220   3981   6493    362    632     50       C  
ATOM    820  C   SER A 472      35.667  95.786  33.627  1.00 43.57           C  
ANISOU  820  C   SER A 472     6908   3589   6056    216    686    -37       C  
ATOM    821  O   SER A 472      36.059  96.918  33.714  1.00 46.49           O  
ANISOU  821  O   SER A 472     7383   3823   6456    183    737    -60       O  
ATOM    822  CB  SER A 472      33.145  95.665  33.518  1.00 48.93           C  
ANISOU  822  CB  SER A 472     7464   4253   6873    470    682     -5       C  
ATOM    823  OG  SER A 472      33.025  94.679  34.502  1.00 49.21           O  
ANISOU  823  OG  SER A 472     7420   4419   6857    425    697    -77       O  
ATOM    824  N   CYS A 473      36.274  94.785  34.251  1.00 40.88           N  
ANISOU  824  N   CYS A 473     6511   3387   5635    125    667    -80       N  
ATOM    825  CA  CYS A 473      37.401  95.045  35.162  1.00 40.97           C  
ANISOU  825  CA  CYS A 473     6573   3402   5590    -15    702   -161       C  
ATOM    826  C   CYS A 473      38.778  94.787  34.542  1.00 40.20           C  
ANISOU  826  C   CYS A 473     6480   3357   5437   -124    660   -115       C  
ATOM    827  O   CYS A 473      39.790  95.118  35.155  1.00 37.81           O  
ANISOU  827  O   CYS A 473     6213   3054   5097   -248    679   -171       O  
ATOM    828  CB  CYS A 473      37.233  94.242  36.467  1.00 40.01           C  
ANISOU  828  CB  CYS A 473     6394   3392   5415    -53    713   -245       C  
ATOM    829  SG  CYS A 473      37.335  92.466  36.301  1.00 37.40           S  
ANISOU  829  SG  CYS A 473     5939   3251   5020    -56    630   -194       S  
ATOM    830  N   HIS A 474      38.796  94.192  33.347  1.00 38.68           N  
ANISOU  830  N   HIS A 474     6245   3213   5236    -80    605    -19       N  
ATOM    831  CA  HIS A 474      40.008  93.909  32.564  1.00 39.48           C  
ANISOU  831  CA  HIS A 474     6343   3366   5291   -163    579     32       C  
ATOM    832  C   HIS A 474      40.829  92.749  33.095  1.00 36.59           C  
ANISOU  832  C   HIS A 474     5889   3150   4863   -237    546      4       C  
ATOM    833  O   HIS A 474      41.259  91.908  32.330  1.00 36.09           O  
ANISOU  833  O   HIS A 474     5774   3169   4769   -235    509     58       O  
ATOM    834  CB  HIS A 474      40.892  95.162  32.401  1.00 45.29           C  
ANISOU  834  CB  HIS A 474     7179   3986   6042   -258    627     28       C  
ATOM    835  CG  HIS A 474      41.997  94.979  31.413  1.00 49.80           C  
ANISOU  835  CG  HIS A 474     7744   4600   6576   -331    615     93       C  
ATOM    836  ND1 HIS A 474      43.307  94.786  31.794  1.00 52.88           N  
ANISOU  836  ND1 HIS A 474     8097   5063   6931   -463    621     59       N  
ATOM    837  CD2 HIS A 474      41.986  94.916  30.058  1.00 51.88           C  
ANISOU  837  CD2 HIS A 474     8028   4854   6829   -293    601    190       C  
ATOM    838  CE1 HIS A 474      44.063  94.644  30.717  1.00 52.68           C  
ANISOU  838  CE1 HIS A 474     8063   5067   6884   -499    624    128       C  
ATOM    839  NE2 HIS A 474      43.283  94.712  29.652  1.00 50.68           N  
ANISOU  839  NE2 HIS A 474     7854   4765   6637   -401    615    206       N  
ATOM    840  N   LYS A 475      41.062  92.711  34.398  1.00 36.02           N  
ANISOU  840  N   LYS A 475     5806   3110   4769   -301    558    -79       N  
ATOM    841  CA  LYS A 475      41.699  91.585  35.013  1.00 37.98           C  
ANISOU  841  CA  LYS A 475     5970   3496   4961   -355    515    -97       C  
ATOM    842  C   LYS A 475      41.220  91.374  36.434  1.00 35.51           C  
ANISOU  842  C   LYS A 475     5652   3218   4622   -369    522   -175       C  
ATOM    843  O   LYS A 475      40.733  92.300  37.076  1.00 35.75           O  
ANISOU  843  O   LYS A 475     5754   3160   4669   -374    576   -239       O  
ATOM    844  CB  LYS A 475      43.211  91.721  34.964  1.00 41.13           C  
ANISOU  844  CB  LYS A 475     6355   3934   5337   -477    506    -97       C  
ATOM    845  CG  LYS A 475      43.788  92.942  35.603  1.00 44.62           C  
ANISOU  845  CG  LYS A 475     6872   4295   5783   -588    545   -160       C  
ATOM    846  CD  LYS A 475      45.051  93.292  34.832  1.00 47.69           C  
ANISOU  846  CD  LYS A 475     7253   4686   6178   -680    551   -120       C  
ATOM    847  CE  LYS A 475      45.531  94.678  35.152  1.00 51.82           C  
ANISOU  847  CE  LYS A 475     7873   5096   6720   -791    598   -169       C  
ATOM    848  NZ  LYS A 475      45.615  95.496  33.921  1.00 53.45           N  
ANISOU  848  NZ  LYS A 475     8148   5191   6966   -784    642   -103       N  
ATOM    849  N   PHE A 476      41.300  90.132  36.882  1.00 33.32           N  
ANISOU  849  N   PHE A 476     5298   3062   4300   -370    475   -168       N  
ATOM    850  CA  PHE A 476      40.848  89.774  38.209  1.00 33.72           C  
ANISOU  850  CA  PHE A 476     5344   3159   4306   -389    479   -230       C  
ATOM    851  C   PHE A 476      41.950  90.004  39.210  1.00 36.43           C  
ANISOU  851  C   PHE A 476     5704   3544   4590   -521    461   -283       C  
ATOM    852  O   PHE A 476      43.130  89.735  38.930  1.00 34.78           O  
ANISOU  852  O   PHE A 476     5451   3392   4369   -585    414   -251       O  
ATOM    853  CB  PHE A 476      40.388  88.329  38.276  1.00 33.25           C  
ANISOU  853  CB  PHE A 476     5206   3202   4224   -336    433   -190       C  
ATOM    854  CG  PHE A 476      39.206  88.024  37.394  1.00 33.09           C  
ANISOU  854  CG  PHE A 476     5161   3155   4255   -219    440   -144       C  
ATOM    855  CD1 PHE A 476      38.210  88.964  37.169  1.00 33.08           C  
ANISOU  855  CD1 PHE A 476     5201   3056   4311   -152    493   -161       C  
ATOM    856  CD2 PHE A 476      39.085  86.778  36.809  1.00 34.21           C  
ANISOU  856  CD2 PHE A 476     5238   3368   4391   -177    388    -86       C  
ATOM    857  CE1 PHE A 476      37.135  88.660  36.353  1.00 33.85           C  
ANISOU  857  CE1 PHE A 476     5260   3143   4457    -47    482   -112       C  
ATOM    858  CE2 PHE A 476      38.012  86.469  35.995  1.00 31.55           C  
ANISOU  858  CE2 PHE A 476     4876   3016   4094    -85    381    -46       C  
ATOM    859  CZ  PHE A 476      37.042  87.407  35.767  1.00 33.27           C  
ANISOU  859  CZ  PHE A 476     5121   3151   4367    -22    422    -56       C  
ATOM    860  N   ASP A 477      41.570  90.509  40.379  1.00 37.03           N  
ANISOU  860  N   ASP A 477     5843   3599   4628   -565    500   -367       N  
ATOM    861  CA  ASP A 477      42.539  90.681  41.458  1.00 38.83           C  
ANISOU  861  CA  ASP A 477     6093   3878   4779   -702    471   -423       C  
ATOM    862  C   ASP A 477      43.098  89.316  41.850  1.00 37.82           C  
ANISOU  862  C   ASP A 477     5877   3897   4594   -724    382   -374       C  
ATOM    863  O   ASP A 477      42.486  88.266  41.551  1.00 34.87           O  
ANISOU  863  O   ASP A 477     5447   3570   4231   -635    364   -318       O  
ATOM    864  CB  ASP A 477      41.934  91.415  42.651  1.00 42.00           C  
ANISOU  864  CB  ASP A 477     6592   4230   5134   -745    537   -531       C  
ATOM    865  CG  ASP A 477      40.807  90.661  43.297  1.00 43.69           C  
ANISOU  865  CG  ASP A 477     6791   4493   5313   -677    562   -542       C  
ATOM    866  OD1 ASP A 477      41.093  89.823  44.167  1.00 47.92           O  
ANISOU  866  OD1 ASP A 477     7304   5140   5760   -735    511   -540       O  
ATOM    867  OD2 ASP A 477      39.634  90.900  42.947  1.00 47.00           O  
ANISOU  867  OD2 ASP A 477     7218   4843   5797   -569    632   -548       O  
ATOM    868  N   LEU A 478      44.269  89.325  42.478  1.00 38.70           N  
ANISOU  868  N   LEU A 478     5975   4077   4652   -843    322   -388       N  
ATOM    869  CA  LEU A 478      44.991  88.087  42.794  1.00 39.96           C  
ANISOU  869  CA  LEU A 478     6042   4370   4770   -861    225   -328       C  
ATOM    870  C   LEU A 478      44.167  87.049  43.574  1.00 38.01           C  
ANISOU  870  C   LEU A 478     5793   4184   4462   -816    209   -315       C  
ATOM    871  O   LEU A 478      44.154  85.875  43.206  1.00 37.93           O  
ANISOU  871  O   LEU A 478     5711   4231   4469   -749    163   -239       O  
ATOM    872  CB  LEU A 478      46.292  88.399  43.548  1.00 42.82           C  
ANISOU  872  CB  LEU A 478     6391   4798   5077  -1006    156   -354       C  
ATOM    873  CG  LEU A 478      47.127  87.188  43.983  1.00 44.86           C  
ANISOU  873  CG  LEU A 478     6549   5195   5299  -1024     43   -286       C  
ATOM    874  CD1 LEU A 478      47.580  86.427  42.752  1.00 43.44           C  
ANISOU  874  CD1 LEU A 478     6259   5036   5209   -933     25   -198       C  
ATOM    875  CD2 LEU A 478      48.341  87.640  44.808  1.00 47.84           C  
ANISOU  875  CD2 LEU A 478     6912   5643   5619  -1177    -34   -317       C  
ATOM    876  N   SER A 479      43.480  87.463  44.640  1.00 37.56           N  
ANISOU  876  N   SER A 479     5823   4113   4335   -857    254   -390       N  
ATOM    877  CA ASER A 479      42.729  86.499  45.443  0.50 37.44           C  
ANISOU  877  CA ASER A 479     5812   4162   4251   -833    248   -376       C  
ATOM    878  CA BSER A 479      42.694  86.537  45.460  0.50 37.07           C  
ANISOU  878  CA BSER A 479     5768   4111   4203   -834    252   -380       C  
ATOM    879  C   SER A 479      41.544  85.918  44.642  1.00 35.57           C  
ANISOU  879  C   SER A 479     5539   3889   4088   -700    298   -334       C  
ATOM    880  O   SER A 479      41.280  84.726  44.701  1.00 33.19           O  
ANISOU  880  O   SER A 479     5190   3647   3771   -661    259   -271       O  
ATOM    881  CB ASER A 479      42.301  87.100  46.786  0.50 39.72           C  
ANISOU  881  CB ASER A 479     6207   4450   4435   -919    298   -474       C  
ATOM    882  CB BSER A 479      42.163  87.252  46.708  0.50 39.00           C  
ANISOU  882  CB BSER A 479     6123   4341   4354   -910    316   -483       C  
ATOM    883  OG ASER A 479      41.689  88.357  46.616  0.50 41.87           O  
ANISOU  883  OG ASER A 479     6553   4604   4751   -904    407   -561       O  
ATOM    884  OG BSER A 479      41.529  86.341  47.595  0.50 39.71           O  
ANISOU  884  OG BSER A 479     6224   4503   4358   -910    314   -469       O  
ATOM    885  N   ARG A 480      40.875  86.736  43.845  1.00 33.37           N  
ANISOU  885  N   ARG A 480     5278   3509   3891   -632    374   -360       N  
ATOM    886  CA  ARG A 480      39.748  86.256  43.049  1.00 32.75           C  
ANISOU  886  CA  ARG A 480     5158   3403   3883   -513    408   -319       C  
ATOM    887  C   ARG A 480      40.222  85.262  42.002  1.00 31.30           C  
ANISOU  887  C   ARG A 480     4893   3257   3742   -462    335   -225       C  
ATOM    888  O   ARG A 480      39.639  84.182  41.828  1.00 31.52           O  
ANISOU  888  O   ARG A 480     4877   3323   3776   -409    316   -177       O  
ATOM    889  CB  ARG A 480      39.034  87.456  42.415  1.00 32.91           C  
ANISOU  889  CB  ARG A 480     5215   3303   3983   -451    490   -359       C  
ATOM    890  CG  ARG A 480      37.886  87.133  41.513  1.00 32.02           C  
ANISOU  890  CG  ARG A 480     5053   3161   3949   -330    513   -315       C  
ATOM    891  CD  ARG A 480      37.313  88.433  40.986  1.00 33.41           C  
ANISOU  891  CD  ARG A 480     5272   3216   4205   -271    583   -349       C  
ATOM    892  NE  ARG A 480      36.108  88.200  40.201  1.00 32.66           N  
ANISOU  892  NE  ARG A 480     5122   3098   4187   -154    598   -307       N  
ATOM    893  CZ  ARG A 480      35.513  89.124  39.453  1.00 34.52           C  
ANISOU  893  CZ  ARG A 480     5373   3233   4508    -72    634   -302       C  
ATOM    894  NH1 ARG A 480      36.000  90.379  39.351  1.00 35.41           N  
ANISOU  894  NH1 ARG A 480     5567   3241   4646    -93    670   -336       N  
ATOM    895  NH2 ARG A 480      34.418  88.799  38.801  1.00 33.56           N  
ANISOU  895  NH2 ARG A 480     5187   3113   4452     28    629   -258       N  
ATOM    896  N   ALA A 481      41.290  85.605  41.295  1.00 32.21           N  
ANISOU  896  N   ALA A 481     4990   3359   3887   -484    302   -203       N  
ATOM    897  CA  ALA A 481      41.852  84.681  40.301  1.00 33.18           C  
ANISOU  897  CA  ALA A 481     5041   3518   4047   -439    247   -125       C  
ATOM    898  C   ALA A 481      42.348  83.371  40.901  1.00 33.99           C  
ANISOU  898  C   ALA A 481     5094   3714   4104   -456    174    -80       C  
ATOM    899  O   ALA A 481      42.156  82.288  40.302  1.00 31.64           O  
ANISOU  899  O   ALA A 481     4752   3435   3832   -390    148    -24       O  
ATOM    900  CB  ALA A 481      42.990  85.342  39.528  1.00 34.38           C  
ANISOU  900  CB  ALA A 481     5180   3648   4235   -473    240   -114       C  
ATOM    901  N   THR A 482      43.022  83.488  42.054  1.00 34.45           N  
ANISOU  901  N   THR A 482     5168   3827   4093   -547    137   -104       N  
ATOM    902  CA  THR A 482      43.545  82.331  42.788  1.00 33.09           C  
ANISOU  902  CA  THR A 482     4959   3744   3870   -570     55    -54       C  
ATOM    903  C   THR A 482      42.397  81.380  43.146  1.00 33.35           C  
ANISOU  903  C   THR A 482     5010   3784   3877   -523     69    -31       C  
ATOM    904  O   THR A 482      42.514  80.166  42.988  1.00 35.11           O  
ANISOU  904  O   THR A 482     5192   4038   4109   -482     19     36       O  
ATOM    905  CB  THR A 482      44.342  82.773  44.041  1.00 34.43           C  
ANISOU  905  CB  THR A 482     5156   3972   3953   -688      6    -87       C  
ATOM    906  OG1 THR A 482      45.540  83.475  43.622  1.00 32.75           O  
ANISOU  906  OG1 THR A 482     4902   3763   3776   -739    -19    -95       O  
ATOM    907  CG2 THR A 482      44.743  81.580  44.869  1.00 35.82           C  
ANISOU  907  CG2 THR A 482     5305   4237   4068   -704    -85    -22       C  
ATOM    908  N   PHE A 483      41.303  81.946  43.643  1.00 32.88           N  
ANISOU  908  N   PHE A 483     5010   3693   3789   -532    143    -89       N  
ATOM    909  CA  PHE A 483      40.097  81.201  43.972  1.00 32.46           C  
ANISOU  909  CA  PHE A 483     4967   3647   3718   -498    177    -77       C  
ATOM    910  C   PHE A 483      39.466  80.477  42.778  1.00 31.23           C  
ANISOU  910  C   PHE A 483     4760   3459   3647   -402    181    -28       C  
ATOM    911  O   PHE A 483      39.106  79.269  42.850  1.00 29.72           O  
ANISOU  911  O   PHE A 483     4550   3294   3448   -383    152     23       O  
ATOM    912  CB  PHE A 483      39.066  82.158  44.593  1.00 33.68           C  
ANISOU  912  CB  PHE A 483     5181   3767   3847   -517    276   -161       C  
ATOM    913  CG  PHE A 483      37.787  81.488  45.002  1.00 34.26           C  
ANISOU  913  CG  PHE A 483     5255   3857   3905   -493    327   -156       C  
ATOM    914  CD1 PHE A 483      37.644  80.947  46.271  1.00 35.67           C  
ANISOU  914  CD1 PHE A 483     5476   4098   3976   -565    327   -155       C  
ATOM    915  CD2 PHE A 483      36.713  81.442  44.143  1.00 35.12           C  
ANISOU  915  CD2 PHE A 483     5319   3922   4101   -409    375   -150       C  
ATOM    916  CE1 PHE A 483      36.456  80.350  46.656  1.00 36.60           C  
ANISOU  916  CE1 PHE A 483     5592   4234   4080   -556    387   -150       C  
ATOM    917  CE2 PHE A 483      35.531  80.841  44.525  1.00 34.08           C  
ANISOU  917  CE2 PHE A 483     5172   3813   3963   -398    424   -147       C  
ATOM    918  CZ  PHE A 483      35.398  80.303  45.778  1.00 34.90           C  
ANISOU  918  CZ  PHE A 483     5317   3977   3964   -473    437   -148       C  
ATOM    919  N   TYR A 484      39.290  81.209  41.683  1.00 30.87           N  
ANISOU  919  N   TYR A 484     4701   3352   3675   -349    214    -44       N  
ATOM    920  CA  TYR A 484      38.783  80.603  40.455  1.00 29.51           C  
ANISOU  920  CA  TYR A 484     4487   3153   3570   -268    207     -1       C  
ATOM    921  C   TYR A 484      39.713  79.480  39.960  1.00 29.75           C  
ANISOU  921  C   TYR A 484     4480   3213   3609   -254    136     60       C  
ATOM    922  O   TYR A 484      39.276  78.383  39.577  1.00 28.02           O  
ANISOU  922  O   TYR A 484     4243   2997   3406   -216    115    100       O  
ATOM    923  CB  TYR A 484      38.597  81.645  39.346  1.00 29.39           C  
ANISOU  923  CB  TYR A 484     4476   3071   3620   -221    243    -19       C  
ATOM    924  CG  TYR A 484      37.543  82.682  39.584  1.00 28.26           C  
ANISOU  924  CG  TYR A 484     4359   2878   3497   -202    315    -71       C  
ATOM    925  CD1 TYR A 484      36.435  82.433  40.384  1.00 29.44           C  
ANISOU  925  CD1 TYR A 484     4505   3047   3631   -201    357    -96       C  
ATOM    926  CD2 TYR A 484      37.625  83.901  38.953  1.00 30.15           C  
ANISOU  926  CD2 TYR A 484     4626   3046   3782   -180    347    -93       C  
ATOM    927  CE1 TYR A 484      35.468  83.381  40.567  1.00 29.52           C  
ANISOU  927  CE1 TYR A 484     4528   3010   3677   -168    432   -147       C  
ATOM    928  CE2 TYR A 484      36.656  84.856  39.117  1.00 28.54           C  
ANISOU  928  CE2 TYR A 484     4446   2783   3615   -144    414   -137       C  
ATOM    929  CZ  TYR A 484      35.605  84.608  39.958  1.00 30.40           C  
ANISOU  929  CZ  TYR A 484     4668   3042   3840   -136    459   -169       C  
ATOM    930  OH  TYR A 484      34.672  85.592  40.147  1.00 29.15           O  
ANISOU  930  OH  TYR A 484     4524   2822   3729    -91    537   -219       O  
ATOM    931  N   ALA A 485      40.995  79.748  39.959  1.00 30.22           N  
ANISOU  931  N   ALA A 485     4526   3290   3663   -284    103     66       N  
ATOM    932  CA  ALA A 485      41.960  78.727  39.552  1.00 30.25           C  
ANISOU  932  CA  ALA A 485     4483   3323   3687   -260     45    122       C  
ATOM    933  C   ALA A 485      41.853  77.432  40.379  1.00 31.02           C  
ANISOU  933  C   ALA A 485     4579   3457   3747   -264     -4    168       C  
ATOM    934  O   ALA A 485      41.919  76.335  39.826  1.00 30.75           O  
ANISOU  934  O   ALA A 485     4524   3411   3746   -213    -29    212       O  
ATOM    935  CB  ALA A 485      43.340  79.286  39.658  1.00 31.13           C  
ANISOU  935  CB  ALA A 485     4564   3464   3800   -304     18    119       C  
ATOM    936  N   ALA A 486      41.705  77.578  41.701  1.00 30.53           N  
ANISOU  936  N   ALA A 486     4552   3433   3612   -330    -14    156       N  
ATOM    937  CA  ALA A 486      41.630  76.445  42.587  1.00 29.92           C  
ANISOU  937  CA  ALA A 486     4489   3391   3486   -347    -63    209       C  
ATOM    938  C   ALA A 486      40.357  75.622  42.313  1.00 30.61           C  
ANISOU  938  C   ALA A 486     4594   3444   3590   -312    -28    224       C  
ATOM    939  O   ALA A 486      40.398  74.390  42.251  1.00 30.18           O  
ANISOU  939  O   ALA A 486     4537   3382   3548   -287    -68    283       O  
ATOM    940  CB  ALA A 486      41.700  76.906  44.034  1.00 31.26           C  
ANISOU  940  CB  ALA A 486     4707   3614   3556   -438    -74    188       C  
ATOM    941  N   GLU A 487      39.222  76.285  42.127  1.00 28.97           N  
ANISOU  941  N   GLU A 487     4401   3212   3391   -310     44    173       N  
ATOM    942  CA  GLU A 487      38.009  75.540  41.873  1.00 28.61           C  
ANISOU  942  CA  GLU A 487     4356   3147   3367   -289     71    186       C  
ATOM    943  C   GLU A 487      38.083  74.868  40.515  1.00 28.80           C  
ANISOU  943  C   GLU A 487     4350   3128   3465   -222     47    213       C  
ATOM    944  O   GLU A 487      37.629  73.723  40.348  1.00 28.06           O  
ANISOU  944  O   GLU A 487     4260   3017   3382   -213     29    250       O  
ATOM    945  CB  GLU A 487      36.760  76.427  42.021  1.00 30.37           C  
ANISOU  945  CB  GLU A 487     4581   3362   3594   -296    154    126       C  
ATOM    946  CG  GLU A 487      36.481  76.825  43.465  1.00 30.34           C  
ANISOU  946  CG  GLU A 487     4621   3400   3506   -368    197     94       C  
ATOM    947  CD  GLU A 487      35.101  77.445  43.706  1.00 31.95           C  
ANISOU  947  CD  GLU A 487     4819   3598   3723   -367    295     37       C  
ATOM    948  OE1 GLU A 487      34.656  77.405  44.888  1.00 31.97           O  
ANISOU  948  OE1 GLU A 487     4858   3639   3650   -429    343     17       O  
ATOM    949  OE2 GLU A 487      34.475  77.979  42.755  1.00 30.76           O  
ANISOU  949  OE2 GLU A 487     4625   3407   3654   -304    325     14       O  
ATOM    950  N   ILE A 488      38.688  75.538  39.542  1.00 28.58           N  
ANISOU  950  N   ILE A 488     4300   3080   3479   -183     48    195       N  
ATOM    951  CA  ILE A 488      38.844  74.947  38.216  1.00 29.15           C  
ANISOU  951  CA  ILE A 488     4355   3115   3603   -125     32    213       C  
ATOM    952  C   ILE A 488      39.760  73.691  38.297  1.00 30.32           C  
ANISOU  952  C   ILE A 488     4499   3261   3757   -109    -19    264       C  
ATOM    953  O   ILE A 488      39.506  72.673  37.634  1.00 29.27           O  
ANISOU  953  O   ILE A 488     4375   3092   3652    -76    -31    283       O  
ATOM    954  CB  ILE A 488      39.361  75.984  37.200  1.00 28.18           C  
ANISOU  954  CB  ILE A 488     4220   2974   3511    -97     53    187       C  
ATOM    955  CG1 ILE A 488      38.256  76.995  36.884  1.00 30.00           C  
ANISOU  955  CG1 ILE A 488     4459   3183   3755    -90     97    151       C  
ATOM    956  CG2 ILE A 488      39.889  75.316  35.933  1.00 29.33           C  
ANISOU  956  CG2 ILE A 488     4357   3094   3692    -47     39    205       C  
ATOM    957  CD1 ILE A 488      38.766  78.216  36.181  1.00 30.69           C  
ANISOU  957  CD1 ILE A 488     4552   3246   3861    -77    121    131       C  
ATOM    958  N   ILE A 489      40.790  73.749  39.131  1.00 30.74           N  
ANISOU  958  N   ILE A 489     4541   3351   3785   -131    -54    285       N  
ATOM    959  CA  ILE A 489      41.664  72.593  39.356  1.00 31.07           C  
ANISOU  959  CA  ILE A 489     4571   3391   3840   -105   -111    344       C  
ATOM    960  C   ILE A 489      40.868  71.390  39.823  1.00 31.87           C  
ANISOU  960  C   ILE A 489     4717   3466   3926   -114   -127    384       C  
ATOM    961  O   ILE A 489      41.041  70.268  39.300  1.00 32.91           O  
ANISOU  961  O   ILE A 489     4856   3548   4100    -66   -146    417       O  
ATOM    962  CB  ILE A 489      42.817  72.940  40.315  1.00 32.35           C  
ANISOU  962  CB  ILE A 489     4705   3613   3973   -138   -162    367       C  
ATOM    963  CG1 ILE A 489      43.843  73.771  39.557  1.00 32.42           C  
ANISOU  963  CG1 ILE A 489     4657   3636   4025   -120   -149    339       C  
ATOM    964  CG2 ILE A 489      43.483  71.689  40.893  1.00 33.05           C  
ANISOU  964  CG2 ILE A 489     4787   3703   4066   -113   -234    445       C  
ATOM    965  CD1 ILE A 489      44.871  74.427  40.451  1.00 34.22           C  
ANISOU  965  CD1 ILE A 489     4848   3930   4221   -175   -196    345       C  
ATOM    966  N   LEU A 490      39.977  71.611  40.782  1.00 32.89           N  
ANISOU  966  N   LEU A 490     4879   3621   3996   -177   -109    379       N  
ATOM    967  CA  LEU A 490      39.157  70.527  41.310  1.00 34.57           C  
ANISOU  967  CA  LEU A 490     5135   3812   4186   -205   -114    420       C  
ATOM    968  C   LEU A 490      38.249  69.940  40.247  1.00 33.01           C  
ANISOU  968  C   LEU A 490     4942   3558   4042   -179    -87    404       C  
ATOM    969  O   LEU A 490      38.167  68.720  40.123  1.00 32.66           O  
ANISOU  969  O   LEU A 490     4927   3462   4018   -169   -111    446       O  
ATOM    970  CB  LEU A 490      38.324  70.963  42.528  1.00 35.30           C  
ANISOU  970  CB  LEU A 490     5260   3952   4199   -286    -80    409       C  
ATOM    971  CG  LEU A 490      39.134  71.262  43.796  1.00 37.91           C  
ANISOU  971  CG  LEU A 490     5613   4342   4447   -334   -122    436       C  
ATOM    972  CD1 LEU A 490      38.210  71.840  44.851  1.00 41.13           C  
ANISOU  972  CD1 LEU A 490     6061   4794   4769   -415    -62    401       C  
ATOM    973  CD2 LEU A 490      39.829  70.010  44.322  1.00 38.96           C  
ANISOU  973  CD2 LEU A 490     5773   4463   4565   -327   -202    531       C  
ATOM    974  N   GLY A 491      37.590  70.788  39.476  1.00 29.25           N  
ANISOU  974  N   GLY A 491     4439   3084   3588   -170    -43    346       N  
ATOM    975  CA  GLY A 491      36.754  70.302  38.375  1.00 31.30           C  
ANISOU  975  CA  GLY A 491     4698   3301   3893   -151    -32    329       C  
ATOM    976  C   GLY A 491      37.534  69.502  37.330  1.00 32.02           C  
ANISOU  976  C   GLY A 491     4802   3336   4026    -93    -60    339       C  
ATOM    977  O   GLY A 491      37.089  68.433  36.869  1.00 31.64           O  
ANISOU  977  O   GLY A 491     4786   3236   3999    -95    -71    349       O  
ATOM    978  N   LEU A 492      38.711  69.999  36.975  1.00 31.48           N  
ANISOU  978  N   LEU A 492     4711   3277   3971    -48    -66    333       N  
ATOM    979  CA  LEU A 492      39.536  69.344  35.956  1.00 33.13           C  
ANISOU  979  CA  LEU A 492     4924   3439   4221     13    -73    333       C  
ATOM    980  C   LEU A 492      40.079  68.005  36.445  1.00 32.61           C  
ANISOU  980  C   LEU A 492     4885   3328   4176     35   -108    385       C  
ATOM    981  O   LEU A 492      40.102  67.006  35.696  1.00 32.95           O  
ANISOU  981  O   LEU A 492     4963   3301   4254     70   -107    382       O  
ATOM    982  CB  LEU A 492      40.734  70.208  35.541  1.00 33.14           C  
ANISOU  982  CB  LEU A 492     4882   3470   4237     50    -60    317       C  
ATOM    983  CG  LEU A 492      40.622  71.342  34.542  1.00 37.06           C  
ANISOU  983  CG  LEU A 492     5367   3982   4732     56    -22    272       C  
ATOM    984  CD1 LEU A 492      42.009  71.960  34.369  1.00 36.62           C  
ANISOU  984  CD1 LEU A 492     5266   3954   4694     79    -10    271       C  
ATOM    985  CD2 LEU A 492      40.073  70.888  33.194  1.00 36.85           C  
ANISOU  985  CD2 LEU A 492     5376   3910   4713     79     -6    244       C  
ATOM    986  N   GLN A 493      40.548  67.984  37.686  1.00 32.42           N  
ANISOU  986  N   GLN A 493     4851   3338   4128     16   -143    435       N  
ATOM    987  CA  GLN A 493      41.076  66.760  38.258  1.00 32.76           C  
ANISOU  987  CA  GLN A 493     4921   3335   4189     41   -188    502       C  
ATOM    988  C   GLN A 493      40.014  65.673  38.401  1.00 33.96           C  
ANISOU  988  C   GLN A 493     5144   3421   4336      3   -187    524       C  
ATOM    989  O   GLN A 493      40.307  64.477  38.247  1.00 33.16           O  
ANISOU  989  O   GLN A 493     5085   3237   4276     42   -207    560       O  
ATOM    990  CB  GLN A 493      41.752  67.032  39.601  1.00 33.60           C  
ANISOU  990  CB  GLN A 493     5007   3505   4254     17   -239    559       C  
ATOM    991  CG  GLN A 493      43.138  67.638  39.436  1.00 34.45           C  
ANISOU  991  CG  GLN A 493     5038   3658   4393     66   -260    557       C  
ATOM    992  CD  GLN A 493      43.849  67.878  40.755  1.00 35.80           C  
ANISOU  992  CD  GLN A 493     5186   3899   4517     33   -329    614       C  
ATOM    993  OE1 GLN A 493      43.224  68.031  41.816  1.00 36.20           O  
ANISOU  993  OE1 GLN A 493     5282   3984   4486    -43   -344    634       O  
ATOM    994  NE2 GLN A 493      45.162  67.927  40.693  1.00 36.89           N  
ANISOU  994  NE2 GLN A 493     5249   4065   4702     85   -369    639       N  
ATOM    995  N   PHE A 494      38.797  66.088  38.711  1.00 31.01           N  
ANISOU  995  N   PHE A 494     4783   3080   3919    -72   -161    502       N  
ATOM    996  CA  PHE A 494      37.682  65.178  38.712  1.00 32.26           C  
ANISOU  996  CA  PHE A 494     4993   3185   4077   -124   -151    512       C  
ATOM    997  C   PHE A 494      37.500  64.575  37.319  1.00 32.48           C  
ANISOU  997  C   PHE A 494     5043   3138   4158    -90   -140    468       C  
ATOM    998  O   PHE A 494      37.398  63.340  37.181  1.00 34.64           O  
ANISOU  998  O   PHE A 494     5379   3322   4460    -91   -153    492       O  
ATOM    999  CB  PHE A 494      36.409  65.896  39.194  1.00 32.97           C  
ANISOU  999  CB  PHE A 494     5063   3340   4122   -206   -113    486       C  
ATOM   1000  CG  PHE A 494      35.174  65.069  39.105  1.00 34.45           C  
ANISOU 1000  CG  PHE A 494     5282   3488   4317   -273    -97    489       C  
ATOM   1001  CD1 PHE A 494      34.802  64.251  40.155  1.00 37.21           C  
ANISOU 1001  CD1 PHE A 494     5682   3820   4635   -340   -100    552       C  
ATOM   1002  CD2 PHE A 494      34.373  65.123  37.984  1.00 37.29           C  
ANISOU 1002  CD2 PHE A 494     5622   3835   4712   -279    -83    433       C  
ATOM   1003  CE1 PHE A 494      33.641  63.473  40.083  1.00 39.95           C  
ANISOU 1003  CE1 PHE A 494     6055   4131   4993   -418    -80    555       C  
ATOM   1004  CE2 PHE A 494      33.220  64.349  37.898  1.00 38.35           C  
ANISOU 1004  CE2 PHE A 494     5774   3939   4857   -355    -75    434       C  
ATOM   1005  CZ  PHE A 494      32.863  63.518  38.945  1.00 37.84           C  
ANISOU 1005  CZ  PHE A 494     5755   3853   4769   -426    -69    494       C  
ATOM   1006  N   LEU A 495      37.467  65.415  36.287  1.00 31.64           N  
ANISOU 1006  N   LEU A 495     4899   3062   4061    -63   -117    404       N  
ATOM   1007  CA  LEU A 495      37.271  64.922  34.928  1.00 31.83           C  
ANISOU 1007  CA  LEU A 495     4954   3025   4112    -41   -107    356       C  
ATOM   1008  C   LEU A 495      38.400  63.951  34.568  1.00 30.76           C  
ANISOU 1008  C   LEU A 495     4858   2807   4022     33   -112    369       C  
ATOM   1009  O   LEU A 495      38.138  62.857  34.099  1.00 30.56           O  
ANISOU 1009  O   LEU A 495     4899   2692   4019     29   -113    359       O  
ATOM   1010  CB  LEU A 495      37.170  66.067  33.910  1.00 33.33           C  
ANISOU 1010  CB  LEU A 495     5105   3267   4292    -23    -86    298       C  
ATOM   1011  CG  LEU A 495      35.913  66.955  33.954  1.00 33.92           C  
ANISOU 1011  CG  LEU A 495     5140   3403   4342    -79    -81    278       C  
ATOM   1012  CD1 LEU A 495      36.080  68.162  33.063  1.00 34.85           C  
ANISOU 1012  CD1 LEU A 495     5226   3563   4452    -44    -66    241       C  
ATOM   1013  CD2 LEU A 495      34.668  66.188  33.573  1.00 35.23           C  
ANISOU 1013  CD2 LEU A 495     5330   3540   4513   -141    -95    264       C  
ATOM   1014  N   HIS A 496      39.647  64.339  34.824  1.00 32.11           N  
ANISOU 1014  N   HIS A 496     4984   3006   4209     99   -115    390       N  
ATOM   1015  CA  HIS A 496      40.799  63.434  34.560  1.00 31.80           C  
ANISOU 1015  CA  HIS A 496     4960   2893   4229    187   -115    408       C  
ATOM   1016  C   HIS A 496      40.708  62.085  35.286  1.00 32.40           C  
ANISOU 1016  C   HIS A 496     5101   2876   4331    187   -148    472       C  
ATOM   1017  O   HIS A 496      41.005  61.076  34.699  1.00 34.19           O  
ANISOU 1017  O   HIS A 496     5382   2999   4609    238   -135    460       O  
ATOM   1018  CB  HIS A 496      42.141  64.115  34.839  1.00 31.65           C  
ANISOU 1018  CB  HIS A 496     4857   2937   4231    251   -120    429       C  
ATOM   1019  CG  HIS A 496      42.358  65.372  34.039  1.00 30.73           C  
ANISOU 1019  CG  HIS A 496     4688   2892   4096    251    -79    371       C  
ATOM   1020  ND1 HIS A 496      43.292  66.321  34.383  1.00 32.05           N  
ANISOU 1020  ND1 HIS A 496     4774   3137   4265    267    -82    383       N  
ATOM   1021  CD2 HIS A 496      41.743  65.844  32.933  1.00 29.11           C  
ANISOU 1021  CD2 HIS A 496     4505   2689   3863    230    -40    307       C  
ATOM   1022  CE1 HIS A 496      43.250  67.320  33.519  1.00 31.15           C  
ANISOU 1022  CE1 HIS A 496     4642   3063   4131    255    -39    329       C  
ATOM   1023  NE2 HIS A 496      42.310  67.056  32.632  1.00 30.59           N  
ANISOU 1023  NE2 HIS A 496     4633   2948   4039    237    -16    287       N  
ATOM   1024  N   SER A 497      40.324  62.066  36.568  1.00 33.56           N  
ANISOU 1024  N   SER A 497     5254   3055   4443    129   -187    540       N  
ATOM   1025  CA  SER A 497      40.226  60.831  37.338  1.00 33.91           C  
ANISOU 1025  CA  SER A 497     5370   3010   4502    119   -221    617       C  
ATOM   1026  C   SER A 497      39.186  59.868  36.726  1.00 33.54           C  
ANISOU 1026  C   SER A 497     5414   2860   4469     65   -198    584       C  
ATOM   1027  O   SER A 497      39.241  58.662  36.951  1.00 34.50           O  
ANISOU 1027  O   SER A 497     5615   2865   4626     75   -214    631       O  
ATOM   1028  CB  SER A 497      39.859  61.157  38.806  1.00 36.03           C  
ANISOU 1028  CB  SER A 497     5635   3352   4702     43   -257    690       C  
ATOM   1029  OG  SER A 497      38.468  61.479  38.914  1.00 34.00           O  
ANISOU 1029  OG  SER A 497     5394   3132   4393    -64   -225    657       O  
ATOM   1030  N   LYS A 498      38.240  60.406  35.967  1.00 34.44           N  
ANISOU 1030  N   LYS A 498     5516   3013   4554      5   -168    508       N  
ATOM   1031  CA  LYS A 498      37.259  59.583  35.230  1.00 36.81           C  
ANISOU 1031  CA  LYS A 498     5890   3229   4863    -57   -154    463       C  
ATOM   1032  C   LYS A 498      37.674  59.229  33.800  1.00 36.08           C  
ANISOU 1032  C   LYS A 498     5835   3066   4805      3   -127    383       C  
ATOM   1033  O   LYS A 498      36.878  58.662  33.065  1.00 38.06           O  
ANISOU 1033  O   LYS A 498     6149   3258   5053    -56   -120    331       O  
ATOM   1034  CB  LYS A 498      35.926  60.303  35.139  1.00 37.04           C  
ANISOU 1034  CB  LYS A 498     5879   3346   4846   -159   -146    427       C  
ATOM   1035  CG  LYS A 498      35.402  60.839  36.452  1.00 39.10           C  
ANISOU 1035  CG  LYS A 498     6097   3693   5064   -224   -150    483       C  
ATOM   1036  CD  LYS A 498      35.042  59.721  37.397  1.00 40.77           C  
ANISOU 1036  CD  LYS A 498     6382   3832   5274   -288   -162    557       C  
ATOM   1037  CE  LYS A 498      34.375  60.294  38.624  1.00 41.15           C  
ANISOU 1037  CE  LYS A 498     6393   3978   5264   -369   -149    600       C  
ATOM   1038  NZ  LYS A 498      34.106  59.214  39.584  1.00 43.35           N  
ANISOU 1038  NZ  LYS A 498     6753   4188   5529   -436   -157    685       N  
ATOM   1039  N   GLY A 499      38.893  59.582  33.387  1.00 34.43           N  
ANISOU 1039  N   GLY A 499     5588   2870   4624    111   -108    368       N  
ATOM   1040  CA  GLY A 499      39.360  59.306  32.027  1.00 33.29           C  
ANISOU 1040  CA  GLY A 499     5480   2666   4501    170    -64    286       C  
ATOM   1041  C   GLY A 499      38.838  60.272  30.973  1.00 33.63           C  
ANISOU 1041  C   GLY A 499     5498   2792   4487    131    -45    209       C  
ATOM   1042  O   GLY A 499      38.775  59.911  29.791  1.00 33.11           O  
ANISOU 1042  O   GLY A 499     5495   2674   4411    135    -15    133       O  
ATOM   1043  N   ILE A 500      38.477  61.485  31.398  1.00 32.62           N  
ANISOU 1043  N   ILE A 500     5288   2786   4319     95    -61    228       N  
ATOM   1044  CA  ILE A 500      37.956  62.504  30.503  1.00 34.24           C  
ANISOU 1044  CA  ILE A 500     5465   3069   4474     64    -53    174       C  
ATOM   1045  C   ILE A 500      38.985  63.622  30.363  1.00 35.13           C  
ANISOU 1045  C   ILE A 500     5506   3257   4584    132    -25    174       C  
ATOM   1046  O   ILE A 500      39.410  64.187  31.369  1.00 37.13           O  
ANISOU 1046  O   ILE A 500     5694   3564   4847    145    -37    225       O  
ATOM   1047  CB  ILE A 500      36.641  63.090  31.038  1.00 34.74           C  
ANISOU 1047  CB  ILE A 500     5488   3204   4505    -26    -87    192       C  
ATOM   1048  CG1 ILE A 500      35.601  61.978  31.143  1.00 38.98           C  
ANISOU 1048  CG1 ILE A 500     6087   3673   5049   -110   -111    191       C  
ATOM   1049  CG2 ILE A 500      36.144  64.210  30.137  1.00 37.59           C  
ANISOU 1049  CG2 ILE A 500     5814   3643   4824    -41    -88    150       C  
ATOM   1050  CD1 ILE A 500      34.411  62.317  31.996  1.00 42.44           C  
ANISOU 1050  CD1 ILE A 500     6474   4176   5474   -197   -132    225       C  
ATOM   1051  N   VAL A 501      39.399  63.900  29.122  1.00 34.34           N  
ANISOU 1051  N   VAL A 501     5425   3158   4464    164     13    117       N  
ATOM   1052  CA  VAL A 501      40.215  65.068  28.793  1.00 33.45           C  
ANISOU 1052  CA  VAL A 501     5250   3120   4338    205     47    111       C  
ATOM   1053  C   VAL A 501      39.297  66.112  28.169  1.00 32.80           C  
ANISOU 1053  C   VAL A 501     5165   3103   4195    150     32     90       C  
ATOM   1054  O   VAL A 501      38.526  65.813  27.280  1.00 32.77           O  
ANISOU 1054  O   VAL A 501     5221   3077   4151    112     19     51       O  
ATOM   1055  CB  VAL A 501      41.383  64.697  27.873  1.00 35.30           C  
ANISOU 1055  CB  VAL A 501     5505   3314   4592    281    113     69       C  
ATOM   1056  CG1 VAL A 501      42.247  65.902  27.562  1.00 35.02           C  
ANISOU 1056  CG1 VAL A 501     5401   3358   4545    309    154     69       C  
ATOM   1057  CG2 VAL A 501      42.234  63.636  28.539  1.00 37.33           C  
ANISOU 1057  CG2 VAL A 501     5755   3499   4927    350    120     99       C  
ATOM   1058  N   TYR A 502      39.337  67.324  28.692  1.00 32.33           N  
ANISOU 1058  N   TYR A 502     5036   3117   4129    143     26    120       N  
ATOM   1059  CA  TYR A 502      38.295  68.319  28.414  1.00 34.13           C  
ANISOU 1059  CA  TYR A 502     5250   3398   4317     97      1    118       C  
ATOM   1060  C   TYR A 502      38.511  69.010  27.085  1.00 33.12           C  
ANISOU 1060  C   TYR A 502     5151   3288   4142    110     25     88       C  
ATOM   1061  O   TYR A 502      37.586  69.131  26.283  1.00 32.31           O  
ANISOU 1061  O   TYR A 502     5086   3194   3997     76     -5     71       O  
ATOM   1062  CB  TYR A 502      38.236  69.325  29.548  1.00 35.46           C  
ANISOU 1062  CB  TYR A 502     5348   3622   4500     87     -5    155       C  
ATOM   1063  CG  TYR A 502      37.208  70.424  29.380  1.00 35.86           C  
ANISOU 1063  CG  TYR A 502     5376   3719   4530     58    -23    156       C  
ATOM   1064  CD1 TYR A 502      35.843  70.173  29.504  1.00 36.87           C  
ANISOU 1064  CD1 TYR A 502     5497   3852   4657     14    -61    157       C  
ATOM   1065  CD2 TYR A 502      37.600  71.722  29.101  1.00 38.80           C  
ANISOU 1065  CD2 TYR A 502     5727   4122   4890     76     -1    159       C  
ATOM   1066  CE1 TYR A 502      34.912  71.187  29.351  1.00 36.30           C  
ANISOU 1066  CE1 TYR A 502     5389   3821   4581      3    -77    161       C  
ATOM   1067  CE2 TYR A 502      36.666  72.735  28.942  1.00 39.78           C  
ANISOU 1067  CE2 TYR A 502     5833   4273   5006     63    -17    165       C  
ATOM   1068  CZ  TYR A 502      35.333  72.467  29.075  1.00 35.69           C  
ANISOU 1068  CZ  TYR A 502     5299   3765   4496     35    -56    167       C  
ATOM   1069  OH  TYR A 502      34.467  73.507  28.925  1.00 36.86           O  
ANISOU 1069  OH  TYR A 502     5415   3938   4651     39    -71    177       O  
ATOM   1070  N   ARG A 503      39.742  69.456  26.869  1.00 33.67           N  
ANISOU 1070  N   ARG A 503     5203   3370   4219    153     79     86       N  
ATOM   1071  CA  ARG A 503      40.241  69.921  25.564  1.00 34.09           C  
ANISOU 1071  CA  ARG A 503     5297   3432   4223    165    125     58       C  
ATOM   1072  C   ARG A 503      39.717  71.292  25.089  1.00 36.04           C  
ANISOU 1072  C   ARG A 503     5543   3725   4424    139    110     77       C  
ATOM   1073  O   ARG A 503      40.178  71.799  24.079  1.00 39.35           O  
ANISOU 1073  O   ARG A 503     6001   4155   4796    143    149     67       O  
ATOM   1074  CB  ARG A 503      39.992  68.881  24.473  1.00 34.92           C  
ANISOU 1074  CB  ARG A 503     5495   3488   4285    160    133      6       C  
ATOM   1075  CG  ARG A 503      40.747  67.587  24.702  1.00 35.06           C  
ANISOU 1075  CG  ARG A 503     5528   3440   4352    204    171    -18       C  
ATOM   1076  CD  ARG A 503      40.838  66.754  23.443  1.00 36.27           C  
ANISOU 1076  CD  ARG A 503     5783   3540   4456    207    212    -87       C  
ATOM   1077  NE  ARG A 503      39.539  66.308  22.974  1.00 34.72           N  
ANISOU 1077  NE  ARG A 503     5661   3324   4205    139    146   -111       N  
ATOM   1078  CZ  ARG A 503      39.357  65.453  21.974  1.00 37.05           C  
ANISOU 1078  CZ  ARG A 503     6062   3565   4446    118    161   -178       C  
ATOM   1079  NH1 ARG A 503      40.401  64.940  21.318  1.00 37.65           N  
ANISOU 1079  NH1 ARG A 503     6189   3597   4517    170    255   -233       N  
ATOM   1080  NH2 ARG A 503      38.127  65.091  21.640  1.00 36.42           N  
ANISOU 1080  NH2 ARG A 503     6037   3478   4320     41     86   -196       N  
ATOM   1081  N   ASP A 504      38.793  71.915  25.806  1.00 36.29           N  
ANISOU 1081  N   ASP A 504     5535   3779   4471    116     60    107       N  
ATOM   1082  CA  ASP A 504      38.354  73.259  25.386  1.00 37.38           C  
ANISOU 1082  CA  ASP A 504     5671   3946   4582    107     48    131       C  
ATOM   1083  C   ASP A 504      38.269  74.247  26.518  1.00 35.92           C  
ANISOU 1083  C   ASP A 504     5423   3782   4443    106     48    159       C  
ATOM   1084  O   ASP A 504      37.339  75.072  26.587  1.00 38.03           O  
ANISOU 1084  O   ASP A 504     5676   4059   4714    101     17    178       O  
ATOM   1085  CB  ASP A 504      36.995  73.165  24.687  1.00 37.90           C  
ANISOU 1085  CB  ASP A 504     5771   4019   4610     82    -18    133       C  
ATOM   1086  CG  ASP A 504      36.694  74.392  23.823  1.00 42.92           C  
ANISOU 1086  CG  ASP A 504     6432   4672   5202     85    -33    163       C  
ATOM   1087  OD1 ASP A 504      37.635  75.019  23.273  1.00 47.51           O  
ANISOU 1087  OD1 ASP A 504     7045   5251   5753     95     19    170       O  
ATOM   1088  OD2 ASP A 504      35.503  74.710  23.687  1.00 46.05           O  
ANISOU 1088  OD2 ASP A 504     6813   5085   5599     77   -100    185       O  
ATOM   1089  N   LEU A 505      39.217  74.161  27.434  1.00 35.38           N  
ANISOU 1089  N   LEU A 505     5313   3718   4412    113     79    160       N  
ATOM   1090  CA  LEU A 505      39.230  75.032  28.599  1.00 34.41           C  
ANISOU 1090  CA  LEU A 505     5140   3614   4321    100     81    175       C  
ATOM   1091  C   LEU A 505      39.463  76.463  28.135  1.00 35.55           C  
ANISOU 1091  C   LEU A 505     5296   3758   4453     97    108    186       C  
ATOM   1092  O   LEU A 505      40.433  76.749  27.431  1.00 37.56           O  
ANISOU 1092  O   LEU A 505     5567   4012   4691     99    149    186       O  
ATOM   1093  CB  LEU A 505      40.294  74.560  29.600  1.00 36.68           C  
ANISOU 1093  CB  LEU A 505     5386   3913   4638    101     95    177       C  
ATOM   1094  CG  LEU A 505      40.267  75.221  30.959  1.00 38.08           C  
ANISOU 1094  CG  LEU A 505     5523   4113   4831     74     88    186       C  
ATOM   1095  CD1 LEU A 505      38.912  75.015  31.627  1.00 37.42           C  
ANISOU 1095  CD1 LEU A 505     5440   4029   4747     57     59    187       C  
ATOM   1096  CD2 LEU A 505      41.404  74.713  31.847  1.00 39.78           C  
ANISOU 1096  CD2 LEU A 505     5698   4349   5066     72     84    198       C  
ATOM   1097  N   LYS A 506      38.518  77.348  28.440  1.00 34.34           N  
ANISOU 1097  N   LYS A 506     5136   3600   4310     94     90    196       N  
ATOM   1098  CA  LYS A 506      38.650  78.758  28.079  1.00 34.94           C  
ANISOU 1098  CA  LYS A 506     5233   3656   4384     95    113    212       C  
ATOM   1099  C   LYS A 506      37.736  79.568  28.955  1.00 34.15           C  
ANISOU 1099  C   LYS A 506     5109   3544   4320     99    105    212       C  
ATOM   1100  O   LYS A 506      36.856  79.009  29.603  1.00 30.77           O  
ANISOU 1100  O   LYS A 506     4648   3133   3910    102     81    202       O  
ATOM   1101  CB  LYS A 506      38.316  78.999  26.621  1.00 35.98           C  
ANISOU 1101  CB  LYS A 506     5423   3774   4473    110     99    236       C  
ATOM   1102  CG  LYS A 506      36.951  78.498  26.216  1.00 37.66           C  
ANISOU 1102  CG  LYS A 506     5637   3993   4676    126     34    244       C  
ATOM   1103  CD  LYS A 506      36.692  78.837  24.756  1.00 40.77           C  
ANISOU 1103  CD  LYS A 506     6097   4380   5012    134      8    274       C  
ATOM   1104  CE  LYS A 506      35.542  78.064  24.181  1.00 42.03           C  
ANISOU 1104  CE  LYS A 506     6261   4561   5148    134    -66    276       C  
ATOM   1105  NZ  LYS A 506      35.423  78.416  22.740  1.00 47.26           N  
ANISOU 1105  NZ  LYS A 506     7000   5222   5733    133    -97    308       N  
ATOM   1106  N   LEU A 507      37.969  80.877  28.999  1.00 33.37           N  
ANISOU 1106  N   LEU A 507     5030   3412   4234     96    135    219       N  
ATOM   1107  CA  LEU A 507      37.220  81.736  29.911  1.00 35.66           C  
ANISOU 1107  CA  LEU A 507     5303   3679   4564    104    146    206       C  
ATOM   1108  C   LEU A 507      35.730  81.743  29.616  1.00 34.87           C  
ANISOU 1108  C   LEU A 507     5184   3574   4488    151    108    222       C  
ATOM   1109  O   LEU A 507      34.918  81.864  30.525  1.00 35.92           O  
ANISOU 1109  O   LEU A 507     5276   3712   4658    161    118    201       O  
ATOM   1110  CB  LEU A 507      37.707  83.185  29.844  1.00 36.89           C  
ANISOU 1110  CB  LEU A 507     5502   3780   4735     95    187    210       C  
ATOM   1111  CG  LEU A 507      38.881  83.545  30.730  1.00 43.97           C  
ANISOU 1111  CG  LEU A 507     6396   4680   5629     35    227    178       C  
ATOM   1112  CD1 LEU A 507      39.221  85.008  30.481  1.00 45.37           C  
ANISOU 1112  CD1 LEU A 507     6628   4787   5824     18    266    184       C  
ATOM   1113  CD2 LEU A 507      38.587  83.257  32.193  1.00 43.43           C  
ANISOU 1113  CD2 LEU A 507     6291   4640   5570     15    230    136       C  
ATOM   1114  N   ASP A 508      35.398  81.676  28.334  1.00 34.75           N  
ANISOU 1114  N   ASP A 508     5197   3555   4451    176     68    259       N  
ATOM   1115  CA  ASP A 508      34.016  81.658  27.861  1.00 35.01           C  
ANISOU 1115  CA  ASP A 508     5201   3593   4505    218     12    285       C  
ATOM   1116  C   ASP A 508      33.212  80.489  28.412  1.00 33.96           C  
ANISOU 1116  C   ASP A 508     5004   3511   4386    205    -15    262       C  
ATOM   1117  O   ASP A 508      31.994  80.543  28.415  1.00 33.10           O  
ANISOU 1117  O   ASP A 508     4842   3416   4317    233    -49    274       O  
ATOM   1118  CB  ASP A 508      33.999  81.544  26.342  1.00 38.53           C  
ANISOU 1118  CB  ASP A 508     5701   4041   4897    227    -38    329       C  
ATOM   1119  CG  ASP A 508      34.979  82.486  25.693  1.00 44.46           C  
ANISOU 1119  CG  ASP A 508     6528   4746   5615    221     -2    356       C  
ATOM   1120  OD1 ASP A 508      34.506  83.499  25.190  1.00 45.53           O  
ANISOU 1120  OD1 ASP A 508     6693   4840   5765    258    -21    403       O  
ATOM   1121  OD2 ASP A 508      36.213  82.244  25.804  1.00 46.76           O  
ANISOU 1121  OD2 ASP A 508     6843   5044   5878    179     49    332       O  
ATOM   1122  N   ASN A 509      33.895  79.432  28.856  1.00 31.03           N  
ANISOU 1122  N   ASN A 509     4636   3165   3988    162     -1    235       N  
ATOM   1123  CA  ASN A 509      33.232  78.203  29.310  1.00 31.76           C  
ANISOU 1123  CA  ASN A 509     4685   3294   4086    137    -26    220       C  
ATOM   1124  C   ASN A 509      33.123  78.078  30.840  1.00 31.60           C  
ANISOU 1124  C   ASN A 509     4624   3289   4093    114     16    194       C  
ATOM   1125  O   ASN A 509      32.723  77.025  31.358  1.00 32.88           O  
ANISOU 1125  O   ASN A 509     4761   3477   4255     81      6    186       O  
ATOM   1126  CB  ASN A 509      33.964  77.000  28.738  1.00 32.04           C  
ANISOU 1126  CB  ASN A 509     4764   3335   4075    109    -43    213       C  
ATOM   1127  CG  ASN A 509      33.681  76.776  27.273  1.00 32.07           C  
ANISOU 1127  CG  ASN A 509     4809   3337   4036    116    -93    229       C  
ATOM   1128  OD1 ASN A 509      32.997  77.557  26.619  1.00 34.69           O  
ANISOU 1128  OD1 ASN A 509     5139   3669   4370    141   -128    257       O  
ATOM   1129  ND2 ASN A 509      34.251  75.708  26.736  1.00 32.36           N  
ANISOU 1129  ND2 ASN A 509     4891   3371   4031     94    -97    211       N  
ATOM   1130  N   ILE A 510      33.481  79.150  31.556  1.00 30.69           N  
ANISOU 1130  N   ILE A 510     4512   3154   3994    122     66    179       N  
ATOM   1131  CA  ILE A 510      33.386  79.187  33.009  1.00 30.53           C  
ANISOU 1131  CA  ILE A 510     4468   3149   3981     94    112    149       C  
ATOM   1132  C   ILE A 510      32.227  80.114  33.402  1.00 30.95           C  
ANISOU 1132  C   ILE A 510     4479   3193   4087    130    145    134       C  
ATOM   1133  O   ILE A 510      32.216  81.320  33.097  1.00 33.26           O  
ANISOU 1133  O   ILE A 510     4789   3439   4408    171    164    134       O  
ATOM   1134  CB  ILE A 510      34.700  79.687  33.651  1.00 31.65           C  
ANISOU 1134  CB  ILE A 510     4650   3280   4096     65    147    131       C  
ATOM   1135  CG1 ILE A 510      35.920  78.942  33.068  1.00 30.84           C  
ANISOU 1135  CG1 ILE A 510     4573   3183   3960     50    119    149       C  
ATOM   1136  CG2 ILE A 510      34.651  79.495  35.147  1.00 32.99           C  
ANISOU 1136  CG2 ILE A 510     4809   3477   4247     22    180    102       C  
ATOM   1137  CD1 ILE A 510      35.921  77.458  33.324  1.00 32.47           C  
ANISOU 1137  CD1 ILE A 510     4768   3417   4149     30     90    159       C  
ATOM   1138  N   LEU A 511      31.247  79.540  34.065  1.00 32.16           N  
ANISOU 1138  N   LEU A 511     4575   3384   4258    115    157    123       N  
ATOM   1139  CA  LEU A 511      30.091  80.273  34.548  1.00 35.23           C  
ANISOU 1139  CA  LEU A 511     4904   3773   4706    151    203    103       C  
ATOM   1140  C   LEU A 511      30.238  80.453  36.051  1.00 33.42           C  
ANISOU 1140  C   LEU A 511     4686   3555   4453    110    283     54       C  
ATOM   1141  O   LEU A 511      30.913  79.660  36.688  1.00 33.60           O  
ANISOU 1141  O   LEU A 511     4743   3606   4416     47    281     52       O  
ATOM   1142  CB  LEU A 511      28.830  79.419  34.320  1.00 39.91           C  
ANISOU 1142  CB  LEU A 511     5412   4416   5335    147    170    120       C  
ATOM   1143  CG  LEU A 511      28.108  79.404  32.981  1.00 45.76           C  
ANISOU 1143  CG  LEU A 511     6110   5161   6114    191     91    162       C  
ATOM   1144  CD1 LEU A 511      29.012  79.740  31.817  1.00 49.88           C  
ANISOU 1144  CD1 LEU A 511     6710   5641   6598    214     38    191       C  
ATOM   1145  CD2 LEU A 511      27.405  78.082  32.771  1.00 44.18           C  
ANISOU 1145  CD2 LEU A 511     5859   5015   5910    137     41    175       C  
ATOM   1146  N   LEU A 512      29.560  81.453  36.620  1.00 32.44           N  
ANISOU 1146  N   LEU A 512     4538   3412   4376    148    354     16       N  
ATOM   1147  CA  LEU A 512      29.393  81.557  38.071  1.00 32.24           C  
ANISOU 1147  CA  LEU A 512     4518   3409   4321    104    443    -38       C  
ATOM   1148  C   LEU A 512      27.977  81.201  38.532  1.00 34.42           C  
ANISOU 1148  C   LEU A 512     4699   3734   4644    112    492    -50       C  
ATOM   1149  O   LEU A 512      26.964  81.570  37.892  1.00 33.12           O  
ANISOU 1149  O   LEU A 512     4451   3564   4569    183    487    -37       O  
ATOM   1150  CB  LEU A 512      29.706  82.966  38.537  1.00 33.54           C  
ANISOU 1150  CB  LEU A 512     4736   3509   4497    131    513    -92       C  
ATOM   1151  CG  LEU A 512      31.136  83.449  38.253  1.00 33.25           C  
ANISOU 1151  CG  LEU A 512     4790   3427   4415    104    479    -88       C  
ATOM   1152  CD1 LEU A 512      31.306  84.840  38.829  1.00 32.93           C  
ANISOU 1152  CD1 LEU A 512     4807   3317   4388    115    557   -151       C  
ATOM   1153  CD2 LEU A 512      32.194  82.506  38.799  1.00 32.96           C  
ANISOU 1153  CD2 LEU A 512     4793   3443   4288     17    443    -78       C  
ATOM   1154  N   ASP A 513      27.890  80.510  39.660  1.00 34.68           N  
ANISOU 1154  N   ASP A 513     4739   3817   4618     36    542    -71       N  
ATOM   1155  CA  ASP A 513      26.574  80.315  40.272  1.00 35.77           C  
ANISOU 1155  CA  ASP A 513     4787   4004   4797     32    619    -94       C  
ATOM   1156  C   ASP A 513      26.162  81.590  41.042  1.00 38.14           C  
ANISOU 1156  C   ASP A 513     5087   4274   5128     77    739   -169       C  
ATOM   1157  O   ASP A 513      26.909  82.586  41.065  1.00 36.68           O  
ANISOU 1157  O   ASP A 513     4981   4023   4931    104    752   -201       O  
ATOM   1158  CB  ASP A 513      26.558  79.036  41.102  1.00 35.85           C  
ANISOU 1158  CB  ASP A 513     4812   4079   4731    -71    628    -78       C  
ATOM   1159  CG  ASP A 513      27.330  79.140  42.408  1.00 35.98           C  
ANISOU 1159  CG  ASP A 513     4928   4103   4637   -142    686   -115       C  
ATOM   1160  OD1 ASP A 513      27.745  80.232  42.866  1.00 37.62           O  
ANISOU 1160  OD1 ASP A 513     5191   4276   4826   -122    740   -172       O  
ATOM   1161  OD2 ASP A 513      27.450  78.091  43.027  1.00 35.76           O  
ANISOU 1161  OD2 ASP A 513     4929   4119   4539   -224    678    -87       O  
ATOM   1162  N   LYS A 514      24.971  81.573  41.629  1.00 39.97           N  
ANISOU 1162  N   LYS A 514     5229   4549   5407     85    832   -200       N  
ATOM   1163  CA  LYS A 514      24.467  82.719  42.368  1.00 43.07           C  
ANISOU 1163  CA  LYS A 514     5615   4911   5839    136    965   -281       C  
ATOM   1164  C   LYS A 514      25.391  83.215  43.484  1.00 42.36           C  
ANISOU 1164  C   LYS A 514     5664   4794   5635     73   1034   -349       C  
ATOM   1165  O   LYS A 514      25.329  84.383  43.834  1.00 43.15           O  
ANISOU 1165  O   LYS A 514     5799   4832   5764    123   1121   -420       O  
ATOM   1166  CB  LYS A 514      23.081  82.424  42.937  1.00 47.64           C  
ANISOU 1166  CB  LYS A 514     6067   5559   6474    138   1069   -305       C  
ATOM   1167  CG  LYS A 514      23.006  81.225  43.860  1.00 49.21           C  
ANISOU 1167  CG  LYS A 514     6281   5844   6571      8   1103   -298       C  
ATOM   1168  CD  LYS A 514      21.560  80.947  44.237  1.00 54.66           C  
ANISOU 1168  CD  LYS A 514     6825   6607   7337      9   1206   -315       C  
ATOM   1169  CE  LYS A 514      21.394  79.538  44.781  1.00 57.07           C  
ANISOU 1169  CE  LYS A 514     7129   6993   7559   -123   1204   -274       C  
ATOM   1170  NZ  LYS A 514      22.049  79.447  46.110  1.00 58.43           N  
ANISOU 1170  NZ  LYS A 514     7442   7180   7578   -220   1286   -315       N  
ATOM   1171  N   ASP A 515      26.262  82.353  44.013  1.00 39.94           N  
ANISOU 1171  N   ASP A 515     5441   4531   5203    -35    989   -327       N  
ATOM   1172  CA  ASP A 515      27.134  82.742  45.131  1.00 39.04           C  
ANISOU 1172  CA  ASP A 515     5455   4410   4966   -111   1037   -386       C  
ATOM   1173  C   ASP A 515      28.553  83.123  44.703  1.00 36.18           C  
ANISOU 1173  C   ASP A 515     5187   3994   4564   -124    941   -370       C  
ATOM   1174  O   ASP A 515      29.329  83.588  45.524  1.00 35.84           O  
ANISOU 1174  O   ASP A 515     5245   3941   4428   -186    966   -422       O  
ATOM   1175  CB  ASP A 515      27.221  81.611  46.133  1.00 40.73           C  
ANISOU 1175  CB  ASP A 515     5705   4710   5059   -228   1048   -366       C  
ATOM   1176  CG  ASP A 515      25.878  81.298  46.769  1.00 44.36           C  
ANISOU 1176  CG  ASP A 515     6085   5228   5539   -241   1170   -393       C  
ATOM   1177  OD1 ASP A 515      25.224  82.231  47.222  1.00 45.47           O  
ANISOU 1177  OD1 ASP A 515     6208   5350   5718   -198   1298   -477       O  
ATOM   1178  OD2 ASP A 515      25.478  80.133  46.775  1.00 49.27           O  
ANISOU 1178  OD2 ASP A 515     6660   5911   6148   -294   1142   -332       O  
ATOM   1179  N   GLY A 516      28.886  82.909  43.438  1.00 33.77           N  
ANISOU 1179  N   GLY A 516     4847   3662   4320    -73    833   -301       N  
ATOM   1180  CA  GLY A 516      30.253  83.163  42.929  1.00 33.06           C  
ANISOU 1180  CA  GLY A 516     4829   3532   4198    -89    745   -278       C  
ATOM   1181  C   GLY A 516      31.167  81.972  42.770  1.00 33.23           C  
ANISOU 1181  C   GLY A 516     4869   3602   4154   -150    641   -209       C  
ATOM   1182  O   GLY A 516      32.354  82.131  42.442  1.00 31.53           O  
ANISOU 1182  O   GLY A 516     4701   3365   3911   -168    577   -192       O  
ATOM   1183  N   HIS A 517      30.628  80.761  42.951  1.00 32.84           N  
ANISOU 1183  N   HIS A 517     4777   3613   4087   -179    626   -167       N  
ATOM   1184  CA  HIS A 517      31.415  79.543  42.711  1.00 32.99           C  
ANISOU 1184  CA  HIS A 517     4812   3662   4061   -221    528    -96       C  
ATOM   1185  C   HIS A 517      31.409  79.228  41.230  1.00 33.04           C  
ANISOU 1185  C   HIS A 517     4770   3637   4145   -157    453    -46       C  
ATOM   1186  O   HIS A 517      30.433  79.537  40.543  1.00 32.73           O  
ANISOU 1186  O   HIS A 517     4667   3583   4186    -97    470    -49       O  
ATOM   1187  CB  HIS A 517      30.845  78.377  43.510  1.00 33.87           C  
ANISOU 1187  CB  HIS A 517     4914   3832   4120   -286    545    -69       C  
ATOM   1188  CG  HIS A 517      30.991  78.550  44.980  1.00 33.79           C  
ANISOU 1188  CG  HIS A 517     4972   3861   4004   -364    609   -108       C  
ATOM   1189  ND1 HIS A 517      32.198  78.394  45.624  1.00 32.66           N  
ANISOU 1189  ND1 HIS A 517     4910   3735   3764   -425    554    -92       N  
ATOM   1190  CD2 HIS A 517      30.089  78.882  45.935  1.00 35.75           C  
ANISOU 1190  CD2 HIS A 517     5220   4138   4222   -395    723   -163       C  
ATOM   1191  CE1 HIS A 517      32.038  78.626  46.911  1.00 35.73           C  
ANISOU 1191  CE1 HIS A 517     5357   4163   4054   -497    623   -135       C  
ATOM   1192  NE2 HIS A 517      30.765  78.913  47.127  1.00 36.43           N  
ANISOU 1192  NE2 HIS A 517     5403   4259   4179   -481    735   -182       N  
ATOM   1193  N   ILE A 518      32.489  78.619  40.740  1.00 31.61           N  
ANISOU 1193  N   ILE A 518     4618   3452   3939   -168    371     -1       N  
ATOM   1194  CA  ILE A 518      32.611  78.384  39.324  1.00 32.39           C  
ANISOU 1194  CA  ILE A 518     4690   3521   4094   -114    309     35       C  
ATOM   1195  C   ILE A 518      31.876  77.131  38.869  1.00 32.11           C  
ANISOU 1195  C   ILE A 518     4615   3505   4079   -119    273     75       C  
ATOM   1196  O   ILE A 518      31.660  76.176  39.642  1.00 31.12           O  
ANISOU 1196  O   ILE A 518     4496   3412   3916   -175    278     92       O  
ATOM   1197  CB  ILE A 518      34.067  78.342  38.815  1.00 34.23           C  
ANISOU 1197  CB  ILE A 518     4964   3735   4305   -114    252     57       C  
ATOM   1198  CG1 ILE A 518      34.734  77.033  39.116  1.00 35.04           C  
ANISOU 1198  CG1 ILE A 518     5082   3864   4365   -151    200    100       C  
ATOM   1199  CG2 ILE A 518      34.903  79.482  39.340  1.00 34.70           C  
ANISOU 1199  CG2 ILE A 518     5064   3780   4338   -133    279     19       C  
ATOM   1200  CD1 ILE A 518      34.820  76.183  37.889  1.00 35.86           C  
ANISOU 1200  CD1 ILE A 518     5172   3946   4504   -115    148    137       C  
ATOM   1201  N   LYS A 519      31.499  77.153  37.601  1.00 30.92           N  
ANISOU 1201  N   LYS A 519     4432   3333   3983    -69    234     91       N  
ATOM   1202  CA  LYS A 519      30.892  76.010  36.947  1.00 31.90           C  
ANISOU 1202  CA  LYS A 519     4526   3468   4126    -80    187    123       C  
ATOM   1203  C   LYS A 519      31.447  75.887  35.548  1.00 31.09           C  
ANISOU 1203  C   LYS A 519     4446   3333   4032    -42    122    144       C  
ATOM   1204  O   LYS A 519      31.290  76.794  34.723  1.00 32.77           O  
ANISOU 1204  O   LYS A 519     4648   3527   4276      8    114    141       O  
ATOM   1205  CB  LYS A 519      29.372  76.192  36.868  1.00 32.32           C  
ANISOU 1205  CB  LYS A 519     4494   3546   4237    -69    211    113       C  
ATOM   1206  CG  LYS A 519      28.652  76.067  38.201  1.00 32.00           C  
ANISOU 1206  CG  LYS A 519     4424   3547   4186   -117    289     92       C  
ATOM   1207  CD  LYS A 519      28.293  74.636  38.503  1.00 31.87           C  
ANISOU 1207  CD  LYS A 519     4405   3556   4148   -193    272    122       C  
ATOM   1208  CE  LYS A 519      27.438  74.481  39.769  1.00 33.81           C  
ANISOU 1208  CE  LYS A 519     4617   3850   4379   -252    359    106       C  
ATOM   1209  NZ  LYS A 519      27.051  73.052  39.870  1.00 33.12           N  
ANISOU 1209  NZ  LYS A 519     4530   3774   4278   -331    334    146       N  
ATOM   1210  N   ILE A 520      32.090  74.757  35.269  1.00 29.84           N  
ANISOU 1210  N   ILE A 520     4326   3164   3847    -65     81    166       N  
ATOM   1211  CA  ILE A 520      32.609  74.500  33.956  1.00 29.64           C  
ANISOU 1211  CA  ILE A 520     4330   3111   3821    -36     34    177       C  
ATOM   1212  C   ILE A 520      31.472  73.980  33.078  1.00 29.69           C  
ANISOU 1212  C   ILE A 520     4306   3123   3849    -42     -7    182       C  
ATOM   1213  O   ILE A 520      30.693  73.115  33.498  1.00 31.76           O  
ANISOU 1213  O   ILE A 520     4543   3401   4122    -90    -12    186       O  
ATOM   1214  CB  ILE A 520      33.716  73.435  34.005  1.00 31.15           C  
ANISOU 1214  CB  ILE A 520     4571   3280   3982    -50     15    191       C  
ATOM   1215  CG1 ILE A 520      34.892  73.941  34.832  1.00 31.93           C  
ANISOU 1215  CG1 ILE A 520     4685   3385   4060    -48     39    192       C  
ATOM   1216  CG2 ILE A 520      34.201  73.104  32.602  1.00 31.11           C  
ANISOU 1216  CG2 ILE A 520     4601   3246   3973    -21    -16    191       C  
ATOM   1217  CD1 ILE A 520      35.993  72.924  35.021  1.00 33.84           C  
ANISOU 1217  CD1 ILE A 520     4957   3612   4287    -51     16    215       C  
ATOM   1218  N   ALA A 521      31.356  74.543  31.888  1.00 30.27           N  
ANISOU 1218  N   ALA A 521     4383   3188   3929     -3    -39    185       N  
ATOM   1219  CA  ALA A 521      30.281  74.230  30.944  1.00 30.57           C  
ANISOU 1219  CA  ALA A 521     4390   3241   3982    -10    -97    193       C  
ATOM   1220  C   ALA A 521      30.835  73.784  29.586  1.00 31.98           C  
ANISOU 1220  C   ALA A 521     4638   3396   4116     -5   -145    194       C  
ATOM   1221  O   ALA A 521      31.974  74.089  29.243  1.00 33.36           O  
ANISOU 1221  O   ALA A 521     4870   3545   4260     20   -124    193       O  
ATOM   1222  CB  ALA A 521      29.375  75.444  30.751  1.00 33.20           C  
ANISOU 1222  CB  ALA A 521     4657   3594   4361     36   -101    202       C  
ATOM   1223  N   ASP A 522      29.973  73.115  28.814  1.00 31.66           N  
ANISOU 1223  N   ASP A 522     4589   3370   4071    -38   -208    194       N  
ATOM   1224  CA  ASP A 522      30.207  72.689  27.434  1.00 32.41           C  
ANISOU 1224  CA  ASP A 522     4753   3450   4111    -46   -260    188       C  
ATOM   1225  C   ASP A 522      31.193  71.540  27.350  1.00 33.04           C  
ANISOU 1225  C   ASP A 522     4915   3482   4154    -69   -237    161       C  
ATOM   1226  O   ASP A 522      32.418  71.733  27.246  1.00 31.37           O  
ANISOU 1226  O   ASP A 522     4754   3244   3920    -34   -192    156       O  
ATOM   1227  CB  ASP A 522      30.642  73.805  26.496  1.00 34.71           C  
ANISOU 1227  CB  ASP A 522     5079   3738   4369      7   -269    207       C  
ATOM   1228  CG  ASP A 522      30.549  73.385  25.058  1.00 35.29           C  
ANISOU 1228  CG  ASP A 522     5221   3813   4374    -14   -332    202       C  
ATOM   1229  OD1 ASP A 522      30.251  72.206  24.773  1.00 34.94           O  
ANISOU 1229  OD1 ASP A 522     5203   3764   4307    -70   -365    174       O  
ATOM   1230  OD2 ASP A 522      30.744  74.223  24.202  1.00 37.81           O  
ANISOU 1230  OD2 ASP A 522     5575   4134   4654     17   -350    227       O  
ATOM   1231  N   PHE A 523      30.655  70.331  27.393  1.00 32.82           N  
ANISOU 1231  N   PHE A 523     4898   3441   4129   -130   -265    144       N  
ATOM   1232  CA  PHE A 523      31.521  69.158  27.387  1.00 32.52           C  
ANISOU 1232  CA  PHE A 523     4941   3342   4072   -144   -240    120       C  
ATOM   1233  C   PHE A 523      31.620  68.469  26.030  1.00 33.22           C  
ANISOU 1233  C   PHE A 523     5118   3400   4103   -167   -274     82       C  
ATOM   1234  O   PHE A 523      32.138  67.357  25.943  1.00 33.67           O  
ANISOU 1234  O   PHE A 523     5246   3393   4151   -183   -254     53       O  
ATOM   1235  CB  PHE A 523      31.094  68.226  28.502  1.00 32.70           C  
ANISOU 1235  CB  PHE A 523     4941   3346   4134   -196   -229    128       C  
ATOM   1236  CG  PHE A 523      31.244  68.847  29.871  1.00 33.28           C  
ANISOU 1236  CG  PHE A 523     4955   3448   4242   -175   -182    158       C  
ATOM   1237  CD1 PHE A 523      30.164  69.471  30.482  1.00 34.26           C  
ANISOU 1237  CD1 PHE A 523     4989   3628   4398   -196   -181    172       C  
ATOM   1238  CD2 PHE A 523      32.474  68.918  30.488  1.00 32.44           C  
ANISOU 1238  CD2 PHE A 523     4875   3318   4133   -133   -138    169       C  
ATOM   1239  CE1 PHE A 523      30.306  70.087  31.711  1.00 34.62           C  
ANISOU 1239  CE1 PHE A 523     4993   3698   4460   -181   -129    188       C  
ATOM   1240  CE2 PHE A 523      32.621  69.545  31.725  1.00 32.11           C  
ANISOU 1240  CE2 PHE A 523     4788   3306   4105   -125   -102    191       C  
ATOM   1241  CZ  PHE A 523      31.530  70.106  32.341  1.00 31.62           C  
ANISOU 1241  CZ  PHE A 523     4656   3293   4063   -152    -93    197       C  
ATOM   1242  N   GLY A 524      31.195  69.160  24.967  1.00 33.92           N  
ANISOU 1242  N   GLY A 524     5212   3527   4147   -164   -321     84       N  
ATOM   1243  CA  GLY A 524      31.209  68.579  23.625  1.00 34.98           C  
ANISOU 1243  CA  GLY A 524     5442   3643   4205   -198   -359     44       C  
ATOM   1244  C   GLY A 524      32.578  68.227  23.053  1.00 37.65           C  
ANISOU 1244  C   GLY A 524     5881   3926   4495   -160   -290      7       C  
ATOM   1245  O   GLY A 524      32.684  67.326  22.221  1.00 37.26           O  
ANISOU 1245  O   GLY A 524     5927   3837   4393   -196   -296    -44       O  
ATOM   1246  N   MET A 525      33.629  68.907  23.506  1.00 36.21           N  
ANISOU 1246  N   MET A 525     5678   3742   4337    -93   -221     28       N  
ATOM   1247  CA AMET A 525      34.979  68.627  23.005  0.50 36.52           C  
ANISOU 1247  CA AMET A 525     5788   3740   4346    -51   -145     -4       C  
ATOM   1248  CA BMET A 525      34.986  68.641  23.033  0.50 38.46           C  
ANISOU 1248  CA BMET A 525     6032   3986   4593    -51   -144     -3       C  
ATOM   1249  C   MET A 525      35.706  67.491  23.736  1.00 36.08           C  
ANISOU 1249  C   MET A 525     5745   3616   4345    -32    -95    -25       C  
ATOM   1250  O   MET A 525      36.817  67.114  23.338  1.00 34.06           O  
ANISOU 1250  O   MET A 525     5538   3321   4081     10    -28    -56       O  
ATOM   1251  CB AMET A 525      35.853  69.888  23.056  0.50 35.39           C  
ANISOU 1251  CB AMET A 525     5611   3629   4204      2    -94     28       C  
ATOM   1252  CB BMET A 525      35.821  69.908  23.183  0.50 39.86           C  
ANISOU 1252  CB BMET A 525     6169   4196   4777      3    -95     32       C  
ATOM   1253  CG AMET A 525      36.894  69.933  21.950  0.50 37.03           C  
ANISOU 1253  CG AMET A 525     5898   3825   4346     25    -29     -2       C  
ATOM   1254  CG BMET A 525      35.512  70.905  22.104  0.50 45.55           C  
ANISOU 1254  CG BMET A 525     6921   4958   5426     -2   -123     50       C  
ATOM   1255  SD AMET A 525      36.128  70.292  20.348  0.50 42.13           S  
ANISOU 1255  SD AMET A 525     6635   4502   4868    -21    -88    -10       S  
ATOM   1256  SD BMET A 525      36.695  70.623  20.782  0.50 51.39           S  
ANISOU 1256  SD BMET A 525     7773   5675   6077      8    -46      3       S  
ATOM   1257  CE AMET A 525      36.057  72.101  20.481  0.50 38.64           C  
ANISOU 1257  CE AMET A 525     6133   4113   4434      6    -99     67       C  
ATOM   1258  CE BMET A 525      38.127  71.329  21.570  0.50 43.12           C  
ANISOU 1258  CE BMET A 525     6658   4628   5094     67     50     26       C  
ATOM   1259  N   CYS A 526      35.107  66.941  24.791  1.00 35.07           N  
ANISOU 1259  N   CYS A 526     5574   3473   4275    -60   -123     -5       N  
ATOM   1260  CA  CYS A 526      35.816  65.967  25.652  1.00 33.72           C  
ANISOU 1260  CA  CYS A 526     5413   3237   4162    -34    -85     -3       C  
ATOM   1261  C   CYS A 526      36.227  64.714  24.916  1.00 34.02           C  
ANISOU 1261  C   CYS A 526     5554   3186   4186    -32    -58    -60       C  
ATOM   1262  O   CYS A 526      35.547  64.307  23.986  1.00 33.39           O  
ANISOU 1262  O   CYS A 526     5543   3090   4052    -88    -90   -106       O  
ATOM   1263  CB  CYS A 526      34.956  65.543  26.843  1.00 33.78           C  
ANISOU 1263  CB  CYS A 526     5376   3241   4217    -83   -121     33       C  
ATOM   1264  SG  CYS A 526      34.765  66.785  28.115  1.00 35.27           S  
ANISOU 1264  SG  CYS A 526     5451   3511   4437    -71   -121     93       S  
ATOM   1265  N   LYS A 527      37.344  64.117  25.315  1.00 33.42           N  
ANISOU 1265  N   LYS A 527     5490   3050   4159     32     -2    -60       N  
ATOM   1266  CA  LYS A 527      37.672  62.763  24.894  1.00 35.25           C  
ANISOU 1266  CA  LYS A 527     5818   3171   4404     43     27   -111       C  
ATOM   1267  C   LYS A 527      37.451  61.823  26.072  1.00 34.38           C  
ANISOU 1267  C   LYS A 527     5704   2992   4364     31      4    -69       C  
ATOM   1268  O   LYS A 527      37.957  62.071  27.137  1.00 34.04           O  
ANISOU 1268  O   LYS A 527     5591   2970   4371     73      7     -7       O  
ATOM   1269  CB  LYS A 527      39.120  62.662  24.433  1.00 36.83           C  
ANISOU 1269  CB  LYS A 527     6031   3339   4621    140    115   -141       C  
ATOM   1270  CG  LYS A 527      39.452  61.333  23.777  1.00 39.92           C  
ANISOU 1270  CG  LYS A 527     6536   3608   5021    161    163   -212       C  
ATOM   1271  CD  LYS A 527      38.827  61.225  22.394  1.00 43.39           C  
ANISOU 1271  CD  LYS A 527     7083   4044   5358     92    161   -295       C  
ATOM   1272  CE  LYS A 527      39.041  59.824  21.831  1.00 47.20           C  
ANISOU 1272  CE  LYS A 527     7696   4389   5848    100    209   -378       C  
ATOM   1273  NZ  LYS A 527      38.783  59.836  20.384  1.00 49.85           N  
ANISOU 1273  NZ  LYS A 527     8141   4731   6066     47    228   -469       N  
ATOM   1274  N   GLU A 528      36.682  60.764  25.872  1.00 35.86           N  
ANISOU 1274  N   GLU A 528     5975   3101   4549    -36    -22   -101       N  
ATOM   1275  CA  GLU A 528      36.413  59.777  26.913  1.00 36.60           C  
ANISOU 1275  CA  GLU A 528     6088   3115   4704    -62    -41    -57       C  
ATOM   1276  C   GLU A 528      37.419  58.626  26.864  1.00 37.61           C  
ANISOU 1276  C   GLU A 528     6296   3104   4889     16     11    -76       C  
ATOM   1277  O   GLU A 528      38.213  58.508  25.935  1.00 36.05           O  
ANISOU 1277  O   GLU A 528     6143   2871   4681     81     69   -139       O  
ATOM   1278  CB  GLU A 528      35.015  59.208  26.731  1.00 37.61           C  
ANISOU 1278  CB  GLU A 528     6262   3221   4807   -190    -96    -80       C  
ATOM   1279  CG  GLU A 528      33.908  60.248  26.758  1.00 37.90           C  
ANISOU 1279  CG  GLU A 528     6207   3387   4803   -263   -151    -61       C  
ATOM   1280  CD  GLU A 528      32.661  59.725  26.068  1.00 39.73           C  
ANISOU 1280  CD  GLU A 528     6486   3609   4999   -385   -207   -108       C  
ATOM   1281  OE1 GLU A 528      32.716  59.508  24.869  1.00 38.88           O  
ANISOU 1281  OE1 GLU A 528     6458   3477   4837   -399   -210   -181       O  
ATOM   1282  OE2 GLU A 528      31.631  59.496  26.724  1.00 41.61           O  
ANISOU 1282  OE2 GLU A 528     6682   3866   5261   -475   -246    -76       O  
ATOM   1283  N   ASN A 529      37.369  57.775  27.881  1.00 40.02           N  
ANISOU 1283  N   ASN A 529     6621   3328   5254     11     -5    -18       N  
ATOM   1284  CA  ASN A 529      38.197  56.557  27.939  1.00 41.51           C  
ANISOU 1284  CA  ASN A 529     6894   3363   5514     88     34    -23       C  
ATOM   1285  C   ASN A 529      39.711  56.808  27.931  1.00 40.61           C  
ANISOU 1285  C   ASN A 529     6725   3253   5451    238     90    -11       C  
ATOM   1286  O   ASN A 529      40.447  56.026  27.339  1.00 39.76           O  
ANISOU 1286  O   ASN A 529     6685   3034   5386    317    149    -62       O  
ATOM   1287  CB  ASN A 529      37.849  55.630  26.767  1.00 45.07           C  
ANISOU 1287  CB  ASN A 529     7484   3698   5942     45     61   -128       C  
ATOM   1288  CG  ASN A 529      36.364  55.341  26.679  1.00 47.00           C  
ANISOU 1288  CG  ASN A 529     7774   3942   6139   -114      0   -146       C  
ATOM   1289  OD1 ASN A 529      35.738  55.551  25.636  1.00 49.82           O  
ANISOU 1289  OD1 ASN A 529     8169   4337   6424   -188    -13   -225       O  
ATOM   1290  ND2 ASN A 529      35.784  54.918  27.787  1.00 44.97           N  
ANISOU 1290  ND2 ASN A 529     7507   3658   5920   -175    -39    -68       N  
ATOM   1291  N   MET A 530      40.165  57.870  28.593  1.00 37.13           N  
ANISOU 1291  N   MET A 530     6160   2937   5010    273     74     51       N  
ATOM   1292  CA  MET A 530      41.571  58.259  28.573  1.00 39.22           C  
ANISOU 1292  CA  MET A 530     6347   3232   5322    398    120     63       C  
ATOM   1293  C   MET A 530      42.386  57.807  29.804  1.00 41.66           C  
ANISOU 1293  C   MET A 530     6605   3505   5716    479     91    162       C  
ATOM   1294  O   MET A 530      43.477  58.310  30.056  1.00 42.04           O  
ANISOU 1294  O   MET A 530     6554   3613   5804    566    105    193       O  
ATOM   1295  CB  MET A 530      41.671  59.769  28.386  1.00 37.68           C  
ANISOU 1295  CB  MET A 530     6051   3194   5070    381    121     60       C  
ATOM   1296  CG  MET A 530      41.144  60.196  27.021  1.00 38.34           C  
ANISOU 1296  CG  MET A 530     6188   3307   5073    330    153    -29       C  
ATOM   1297  SD  MET A 530      42.311  59.687  25.736  1.00 41.28           S  
ANISOU 1297  SD  MET A 530     6613   3608   5462    430    264   -120       S  
ATOM   1298  CE  MET A 530      43.591  60.889  26.032  1.00 40.51           C  
ANISOU 1298  CE  MET A 530     6363   3631   5395    509    300    -75       C  
ATOM   1299  N   LEU A 531      41.871  56.836  30.551  1.00 40.11           N  
ANISOU 1299  N   LEU A 531     6480   3211   5548    446     48    216       N  
ATOM   1300  CA  LEU A 531      42.617  56.266  31.666  1.00 41.37           C  
ANISOU 1300  CA  LEU A 531     6615   3321   5783    524     12    319       C  
ATOM   1301  C   LEU A 531      43.754  55.371  31.176  1.00 40.35           C  
ANISOU 1301  C   LEU A 531     6509   3066   5755    669     67    298       C  
ATOM   1302  O   LEU A 531      43.719  54.825  30.064  1.00 39.23           O  
ANISOU 1302  O   LEU A 531     6452   2831   5623    688    136    199       O  
ATOM   1303  CB  LEU A 531      41.675  55.453  32.573  1.00 43.97           C  
ANISOU 1303  CB  LEU A 531     7030   3571   6104    436    -43    389       C  
ATOM   1304  CG  LEU A 531      41.050  56.061  33.842  1.00 47.44           C  
ANISOU 1304  CG  LEU A 531     7420   4119   6485    343   -110    478       C  
ATOM   1305  CD1 LEU A 531      41.245  57.547  34.000  1.00 44.44           C  
ANISOU 1305  CD1 LEU A 531     6915   3917   6051    334   -116    473       C  
ATOM   1306  CD2 LEU A 531      39.593  55.646  34.087  1.00 48.67           C  
ANISOU 1306  CD2 LEU A 531     7657   4242   6592    196   -127    480       C  
ATOM   1307  N   GLY A 532      44.759  55.220  32.017  1.00 39.01           N  
ANISOU 1307  N   GLY A 532     6263   2896   5661    773     34    391       N  
ATOM   1308  CA  GLY A 532      45.818  54.265  31.754  1.00 41.68           C  
ANISOU 1308  CA  GLY A 532     6612   3104   6119    926     77    392       C  
ATOM   1309  C   GLY A 532      46.760  54.789  30.681  1.00 42.00           C  
ANISOU 1309  C   GLY A 532     6572   3199   6187   1016    172    301       C  
ATOM   1310  O   GLY A 532      46.996  55.999  30.560  1.00 42.29           O  
ANISOU 1310  O   GLY A 532     6498   3395   6172    987    176    287       O  
ATOM   1311  N   ASP A 533      47.293  53.866  29.907  1.00 44.95           N  
ANISOU 1311  N   ASP A 533     7006   3432   6641   1121    256    236       N  
ATOM   1312  CA  ASP A 533      48.241  54.170  28.846  1.00 47.79           C  
ANISOU 1312  CA  ASP A 533     7301   3822   7035   1216    370    143       C  
ATOM   1313  C   ASP A 533      47.423  54.409  27.579  1.00 47.64           C  
ANISOU 1313  C   ASP A 533     7392   3805   6902   1112    441      7       C  
ATOM   1314  O   ASP A 533      47.311  53.537  26.705  1.00 54.34           O  
ANISOU 1314  O   ASP A 533     8368   4513   7762   1135    520    -89       O  
ATOM   1315  CB  ASP A 533      49.184  52.988  28.673  1.00 49.53           C  
ANISOU 1315  CB  ASP A 533     7539   3877   7401   1387    434    136       C  
ATOM   1316  CG  ASP A 533      50.347  53.286  27.758  1.00 52.09           C  
ANISOU 1316  CG  ASP A 533     7763   4244   7783   1506    559     56       C  
ATOM   1317  OD1 ASP A 533      50.459  54.415  27.257  1.00 55.90           O  
ANISOU 1317  OD1 ASP A 533     8166   4884   8187   1449    595     12       O  
ATOM   1318  OD2 ASP A 533      51.168  52.382  27.545  1.00 57.28           O  
ANISOU 1318  OD2 ASP A 533     8418   4773   8570   1661    629     40       O  
ATOM   1319  N   ALA A 534      46.791  55.560  27.546  1.00 45.58           N  
ANISOU 1319  N   ALA A 534     7092   3696   6530    992    402      6       N  
ATOM   1320  CA  ALA A 534      45.910  55.964  26.468  1.00 45.49           C  
ANISOU 1320  CA  ALA A 534     7170   3716   6397    880    437    -96       C  
ATOM   1321  C   ALA A 534      46.277  57.382  26.012  1.00 43.30           C  
ANISOU 1321  C   ALA A 534     6784   3611   6055    859    467   -114       C  
ATOM   1322  O   ALA A 534      46.681  58.225  26.810  1.00 40.26           O  
ANISOU 1322  O   ALA A 534     6268   3341   5687    866    419    -34       O  
ATOM   1323  CB  ALA A 534      44.459  55.934  26.922  1.00 45.85           C  
ANISOU 1323  CB  ALA A 534     7291   3761   6366    732    342    -68       C  
ATOM   1324  N   LYS A 535      46.135  57.611  24.716  1.00 43.45           N  
ANISOU 1324  N   LYS A 535     6872   3642   5995    826    547   -221       N  
ATOM   1325  CA  LYS A 535      46.370  58.893  24.103  1.00 44.56           C  
ANISOU 1325  CA  LYS A 535     6945   3926   6059    792    583   -243       C  
ATOM   1326  C   LYS A 535      45.429  58.997  22.926  1.00 42.82           C  
ANISOU 1326  C   LYS A 535     6858   3703   5707    690    601   -335       C  
ATOM   1327  O   LYS A 535      44.891  57.991  22.433  1.00 39.60           O  
ANISOU 1327  O   LYS A 535     6588   3177   5280    665    613   -403       O  
ATOM   1328  CB  LYS A 535      47.821  59.039  23.649  1.00 49.78           C  
ANISOU 1328  CB  LYS A 535     7515   4612   6786    910    700   -271       C  
ATOM   1329  CG  LYS A 535      48.820  58.915  24.786  1.00 55.62           C  
ANISOU 1329  CG  LYS A 535     8106   5363   7663   1016    669   -176       C  
ATOM   1330  CD  LYS A 535      50.119  59.631  24.514  1.00 62.49           C  
ANISOU 1330  CD  LYS A 535     8828   6333   8582   1088    754   -178       C  
ATOM   1331  CE  LYS A 535      51.026  59.541  25.727  1.00 66.77           C  
ANISOU 1331  CE  LYS A 535     9212   6901   9255   1179    694    -73       C  
ATOM   1332  NZ  LYS A 535      52.404  59.965  25.357  1.00 70.92           N  
ANISOU 1332  NZ  LYS A 535     9585   7503   9855   1266    793    -88       N  
ATOM   1333  N   THR A 536      45.211  60.228  22.495  1.00 40.81           N  
ANISOU 1333  N   THR A 536     6567   3577   5361    624    594   -333       N  
ATOM   1334  CA  THR A 536      44.359  60.477  21.366  1.00 40.72           C  
ANISOU 1334  CA  THR A 536     6670   3585   5216    527    596   -404       C  
ATOM   1335  C   THR A 536      45.094  61.504  20.480  1.00 42.09           C  
ANISOU 1335  C   THR A 536     6807   3858   5326    539    684   -431       C  
ATOM   1336  O   THR A 536      46.146  62.026  20.856  1.00 40.47           O  
ANISOU 1336  O   THR A 536     6477   3708   5189    609    733   -391       O  
ATOM   1337  CB  THR A 536      42.975  60.934  21.835  1.00 39.80           C  
ANISOU 1337  CB  THR A 536     6560   3519   5043    413    467   -354       C  
ATOM   1338  OG1 THR A 536      42.030  60.797  20.762  1.00 39.83           O  
ANISOU 1338  OG1 THR A 536     6690   3512   4929    319    448   -425       O  
ATOM   1339  CG2 THR A 536      43.013  62.381  22.327  1.00 38.99           C  
ANISOU 1339  CG2 THR A 536     6335   3551   4926    394    428   -277       C  
ATOM   1340  N   ASN A 537      44.541  61.780  19.313  1.00 42.46           N  
ANISOU 1340  N   ASN A 537     6962   3929   5239    463    700   -494       N  
ATOM   1341  CA  ASN A 537      45.286  62.516  18.299  1.00 44.73           C  
ANISOU 1341  CA  ASN A 537     7252   4286   5454    471    807   -532       C  
ATOM   1342  C   ASN A 537      44.484  63.542  17.503  1.00 43.74           C  
ANISOU 1342  C   ASN A 537     7188   4252   5178    365    758   -524       C  
ATOM   1343  O   ASN A 537      44.921  63.941  16.438  1.00 45.61           O  
ANISOU 1343  O   ASN A 537     7480   4528   5321    351    847   -570       O  
ATOM   1344  CB  ASN A 537      45.883  61.497  17.345  1.00 47.43           C  
ANISOU 1344  CB  ASN A 537     7702   4536   5780    522    938   -647       C  
ATOM   1345  CG  ASN A 537      44.821  60.774  16.546  1.00 49.93           C  
ANISOU 1345  CG  ASN A 537     8202   4785   5984    434    900   -729       C  
ATOM   1346  OD1 ASN A 537      43.627  60.851  16.841  1.00 52.28           O  
ANISOU 1346  OD1 ASN A 537     8527   5093   6241    344    766   -694       O  
ATOM   1347  ND2 ASN A 537      45.248  60.076  15.524  1.00 55.75           N  
ANISOU 1347  ND2 ASN A 537     9059   5454   6667    454   1020   -844       N  
ATOM   1348  N   GLU A 538      43.314  63.952  17.981  1.00 41.85           N  
ANISOU 1348  N   GLU A 538     6940   4046   4915    291    622   -466       N  
ATOM   1349  CA  GLU A 538      42.521  64.923  17.241  1.00 42.76           C  
ANISOU 1349  CA  GLU A 538     7104   4242   4899    203    563   -448       C  
ATOM   1350  C   GLU A 538      43.012  66.364  17.453  1.00 40.30           C  
ANISOU 1350  C   GLU A 538     6691   4027   4593    212    577   -371       C  
ATOM   1351  O   GLU A 538      43.277  66.808  18.561  1.00 39.04           O  
ANISOU 1351  O   GLU A 538     6407   3891   4534    246    550   -304       O  
ATOM   1352  CB  GLU A 538      41.033  64.855  17.593  1.00 42.46           C  
ANISOU 1352  CB  GLU A 538     7084   4207   4840    123    414   -416       C  
ATOM   1353  CG  GLU A 538      40.392  63.521  17.267  1.00 45.29           C  
ANISOU 1353  CG  GLU A 538     7557   4473   5175     81    388   -493       C  
ATOM   1354  CD  GLU A 538      40.496  62.534  18.411  1.00 45.54           C  
ANISOU 1354  CD  GLU A 538     7543   4416   5343    127    380   -482       C  
ATOM   1355  OE1 GLU A 538      41.103  62.875  19.449  1.00 42.18           O  
ANISOU 1355  OE1 GLU A 538     6996   4009   5022    194    392   -415       O  
ATOM   1356  OE2 GLU A 538      39.985  61.405  18.266  1.00 45.64           O  
ANISOU 1356  OE2 GLU A 538     7650   4336   5353     89    360   -540       O  
ATOM   1357  N   PHE A 539      43.108  67.086  16.356  1.00 41.76           N  
ANISOU 1357  N   PHE A 539     6943   4264   4657    172    617   -382       N  
ATOM   1358  CA  PHE A 539      43.448  68.499  16.389  1.00 43.18           C  
ANISOU 1358  CA  PHE A 539     7057   4525   4824    162    627   -309       C  
ATOM   1359  C   PHE A 539      42.193  69.261  16.770  1.00 43.34           C  
ANISOU 1359  C   PHE A 539     7061   4580   4824    109    483   -236       C  
ATOM   1360  O   PHE A 539      41.238  69.281  16.008  1.00 45.01           O  
ANISOU 1360  O   PHE A 539     7368   4803   4931     50    412   -243       O  
ATOM   1361  CB  PHE A 539      43.956  68.991  15.024  1.00 44.51           C  
ANISOU 1361  CB  PHE A 539     7322   4731   4859    130    724   -338       C  
ATOM   1362  CG  PHE A 539      44.418  70.420  15.053  1.00 45.73           C  
ANISOU 1362  CG  PHE A 539     7414   4953   5007    116    748   -260       C  
ATOM   1363  CD1 PHE A 539      45.754  70.726  15.281  1.00 49.05           C  
ANISOU 1363  CD1 PHE A 539     7742   5394   5499    158    872   -257       C  
ATOM   1364  CD2 PHE A 539      43.506  71.455  14.937  1.00 49.84           C  
ANISOU 1364  CD2 PHE A 539     7959   5511   5466     61    643   -186       C  
ATOM   1365  CE1 PHE A 539      46.182  72.045  15.337  1.00 48.75           C  
ANISOU 1365  CE1 PHE A 539     7651   5410   5459    129    894   -188       C  
ATOM   1366  CE2 PHE A 539      43.915  72.781  15.008  1.00 50.35           C  
ANISOU 1366  CE2 PHE A 539     7978   5618   5533     47    666   -112       C  
ATOM   1367  CZ  PHE A 539      45.254  73.074  15.199  1.00 50.18           C  
ANISOU 1367  CZ  PHE A 539     7877   5613   5573     73    793   -116       C  
ATOM   1368  N   CYS A 540      42.176  69.869  17.943  1.00 40.46           N  
ANISOU 1368  N   CYS A 540     6576   4235   4561    131    439   -169       N  
ATOM   1369  CA  CYS A 540      40.996  70.625  18.346  1.00 41.85           C  
ANISOU 1369  CA  CYS A 540     6727   4440   4732     93    319   -106       C  
ATOM   1370  C   CYS A 540      41.334  71.554  19.485  1.00 39.98           C  
ANISOU 1370  C   CYS A 540     6369   4229   4589    117    315    -42       C  
ATOM   1371  O   CYS A 540      42.425  71.476  20.047  1.00 41.33           O  
ANISOU 1371  O   CYS A 540     6471   4397   4833    157    386    -46       O  
ATOM   1372  CB  CYS A 540      39.858  69.682  18.748  1.00 43.17           C  
ANISOU 1372  CB  CYS A 540     6907   4575   4920     69    223   -124       C  
ATOM   1373  SG  CYS A 540      40.224  68.681  20.196  1.00 43.13           S  
ANISOU 1373  SG  CYS A 540     6815   4515   5055    117    234   -131       S  
ATOM   1374  N   GLY A 541      40.404  72.448  19.801  1.00 40.37           N  
ANISOU 1374  N   GLY A 541     6395   4304   4638     93    231     13       N  
ATOM   1375  CA  GLY A 541      40.587  73.464  20.846  1.00 38.81           C  
ANISOU 1375  CA  GLY A 541     6103   4125   4517    106    225     66       C  
ATOM   1376  C   GLY A 541      40.177  74.823  20.291  1.00 40.65           C  
ANISOU 1376  C   GLY A 541     6366   4380   4698     84    200    119       C  
ATOM   1377  O   GLY A 541      39.618  74.912  19.203  1.00 43.69           O  
ANISOU 1377  O   GLY A 541     6837   4773   4990     60    167    125       O  
ATOM   1378  N   THR A 542      40.422  75.857  21.070  1.00 37.80           N  
ANISOU 1378  N   THR A 542     5941   4025   4396     90    209    159       N  
ATOM   1379  CA  THR A 542      40.210  77.238  20.671  1.00 38.88           C  
ANISOU 1379  CA  THR A 542     6106   4162   4503     76    199    215       C  
ATOM   1380  C   THR A 542      41.630  77.808  20.528  1.00 37.36           C  
ANISOU 1380  C   THR A 542     5907   3975   4313     63    304    216       C  
ATOM   1381  O   THR A 542      42.457  77.614  21.420  1.00 37.51           O  
ANISOU 1381  O   THR A 542     5845   4000   4406     71    346    196       O  
ATOM   1382  CB  THR A 542      39.388  77.969  21.749  1.00 39.49           C  
ANISOU 1382  CB  THR A 542     6119   4230   4655     89    140    247       C  
ATOM   1383  OG1 THR A 542      38.084  77.365  21.818  1.00 43.69           O  
ANISOU 1383  OG1 THR A 542     6642   4767   5188     96     52    244       O  
ATOM   1384  CG2 THR A 542      39.243  79.445  21.451  1.00 39.72           C  
ANISOU 1384  CG2 THR A 542     6178   4238   4674     85    138    305       C  
ATOM   1385  N   PRO A 543      41.922  78.458  19.401  1.00 38.68           N  
ANISOU 1385  N   PRO A 543     6154   4143   4396     36    344    243       N  
ATOM   1386  CA  PRO A 543      43.304  78.754  19.035  1.00 38.12           C  
ANISOU 1386  CA  PRO A 543     6081   4085   4314     12    460    236       C  
ATOM   1387  C   PRO A 543      44.229  79.348  20.124  1.00 36.97           C  
ANISOU 1387  C   PRO A 543     5833   3944   4270      3    506    240       C  
ATOM   1388  O   PRO A 543      45.362  78.875  20.259  1.00 34.64           O  
ANISOU 1388  O   PRO A 543     5476   3674   4009      4    584    206       O  
ATOM   1389  CB  PRO A 543      43.135  79.689  17.845  1.00 41.70           C  
ANISOU 1389  CB  PRO A 543     6647   4533   4664    -24    471    290       C  
ATOM   1390  CG  PRO A 543      41.903  79.163  17.158  1.00 41.11           C  
ANISOU 1390  CG  PRO A 543     6649   4458   4509    -14    375    293       C  
ATOM   1391  CD  PRO A 543      40.999  78.738  18.272  1.00 40.18           C  
ANISOU 1391  CD  PRO A 543     6450   4332   4484     22    283    280       C  
ATOM   1392  N   ASP A 544      43.776  80.329  20.908  1.00 35.11           N  
ANISOU 1392  N   ASP A 544     5572   3683   4084     -5    457    277       N  
ATOM   1393  CA  ASP A 544      44.644  80.913  21.954  1.00 34.82           C  
ANISOU 1393  CA  ASP A 544     5448   3650   4130    -30    493    274       C  
ATOM   1394  C   ASP A 544      45.094  79.926  23.032  1.00 33.33           C  
ANISOU 1394  C   ASP A 544     5155   3493   4016     -4    483    231       C  
ATOM   1395  O   ASP A 544      46.134  80.145  23.690  1.00 30.45           O  
ANISOU 1395  O   ASP A 544     4709   3152   3707    -29    522    222       O  
ATOM   1396  CB  ASP A 544      43.950  82.051  22.659  1.00 37.39           C  
ANISOU 1396  CB  ASP A 544     5780   3933   4493    -40    442    307       C  
ATOM   1397  CG  ASP A 544      43.988  83.369  21.861  1.00 41.43           C  
ANISOU 1397  CG  ASP A 544     6378   4400   4963    -79    472    362       C  
ATOM   1398  OD1 ASP A 544      45.035  83.769  21.319  1.00 45.06           O  
ANISOU 1398  OD1 ASP A 544     6851   4869   5400   -130    556    372       O  
ATOM   1399  OD2 ASP A 544      42.952  84.028  21.841  1.00 44.53           O  
ANISOU 1399  OD2 ASP A 544     6819   4745   5353    -57    413    399       O  
ATOM   1400  N   TYR A 545      44.287  78.877  23.248  1.00 31.11           N  
ANISOU 1400  N   TYR A 545     4876   3209   3735     39    424    210       N  
ATOM   1401  CA  TYR A 545      44.485  77.945  24.361  1.00 32.47           C  
ANISOU 1401  CA  TYR A 545     4966   3397   3973     66    397    184       C  
ATOM   1402  C   TYR A 545      45.115  76.608  23.981  1.00 31.48           C  
ANISOU 1402  C   TYR A 545     4825   3282   3852    104    434    148       C  
ATOM   1403  O   TYR A 545      45.374  75.797  24.851  1.00 33.73           O  
ANISOU 1403  O   TYR A 545     5048   3573   4195    132    412    137       O  
ATOM   1404  CB  TYR A 545      43.119  77.613  25.003  1.00 31.58           C  
ANISOU 1404  CB  TYR A 545     4865   3266   3868     83    309    186       C  
ATOM   1405  CG  TYR A 545      42.419  78.804  25.622  1.00 33.26           C  
ANISOU 1405  CG  TYR A 545     5078   3462   4096     63    275    212       C  
ATOM   1406  CD1 TYR A 545      41.591  79.626  24.855  1.00 33.39           C  
ANISOU 1406  CD1 TYR A 545     5160   3451   4074     62    256    241       C  
ATOM   1407  CD2 TYR A 545      42.549  79.100  26.965  1.00 33.47           C  
ANISOU 1407  CD2 TYR A 545     5045   3496   4174     48    260    206       C  
ATOM   1408  CE1 TYR A 545      40.938  80.723  25.416  1.00 34.71           C  
ANISOU 1408  CE1 TYR A 545     5328   3589   4270     59    233    261       C  
ATOM   1409  CE2 TYR A 545      41.879  80.182  27.525  1.00 33.58           C  
ANISOU 1409  CE2 TYR A 545     5070   3485   4203     34    243    217       C  
ATOM   1410  CZ  TYR A 545      41.081  80.993  26.739  1.00 33.89           C  
ANISOU 1410  CZ  TYR A 545     5169   3487   4220     45    233    243       C  
ATOM   1411  OH  TYR A 545      40.392  82.074  27.299  1.00 34.70           O  
ANISOU 1411  OH  TYR A 545     5281   3552   4352     46    223    251       O  
ATOM   1412  N   ILE A 546      45.319  76.373  22.698  1.00 31.91           N  
ANISOU 1412  N   ILE A 546     4946   3334   3844    107    491    131       N  
ATOM   1413  CA AILE A 546      45.733  75.061  22.219  0.50 34.25           C  
ANISOU 1413  CA AILE A 546     5251   3624   4138    149    534     85       C  
ATOM   1414  CA BILE A 546      45.761  75.062  22.181  0.50 32.25           C  
ANISOU 1414  CA BILE A 546     4999   3371   3883    149    537     84       C  
ATOM   1415  C   ILE A 546      47.196  74.754  22.583  1.00 34.32           C  
ANISOU 1415  C   ILE A 546     5155   3660   4223    176    609     71       C  
ATOM   1416  O   ILE A 546      48.079  75.590  22.434  1.00 33.45           O  
ANISOU 1416  O   ILE A 546     5000   3585   4124    144    672     85       O  
ATOM   1417  CB AILE A 546      45.446  74.920  20.713  0.50 36.46           C  
ANISOU 1417  CB AILE A 546     5649   3893   4309    136    575     62       C  
ATOM   1418  CB BILE A 546      45.678  74.999  20.647  0.50 31.83           C  
ANISOU 1418  CB BILE A 546     5056   3313   3724    135    594     62       C  
ATOM   1419  CG1AILE A 546      45.419  73.444  20.317  0.50 37.85           C  
ANISOU 1419  CG1AILE A 546     5864   4040   4476    178    593      2       C  
ATOM   1420  CG1BILE A 546      44.224  75.001  20.176  0.50 30.24           C  
ANISOU 1420  CG1BILE A 546     4954   3089   3446    116    504     72       C  
ATOM   1421  CG2AILE A 546      46.433  75.726  19.874  0.50 38.24           C  
ANISOU 1421  CG2AILE A 546     5886   4148   4494    104    681     70       C  
ATOM   1422  CG2BILE A 546      46.365  73.751  20.092  0.50 32.42           C  
ANISOU 1422  CG2BILE A 546     5141   3375   3800    179    673      0       C  
ATOM   1423  CD1AILE A 546      45.095  73.228  18.854  0.50 40.84           C  
ANISOU 1423  CD1AILE A 546     6374   4412   4731    155    628    -31       C  
ATOM   1424  CD1BILE A 546      44.105  75.004  18.669  0.50 30.75           C  
ANISOU 1424  CD1BILE A 546     5139   3156   3386     90    543     57       C  
ATOM   1425  N   ALA A 547      47.421  73.547  23.090  1.00 33.30           N  
ANISOU 1425  N   ALA A 547     4984   3513   4154    234    598     48       N  
ATOM   1426  CA  ALA A 547      48.727  73.131  23.589  1.00 32.95           C  
ANISOU 1426  CA  ALA A 547     4821   3494   4201    277    646     44       C  
ATOM   1427  C   ALA A 547      49.730  72.884  22.473  1.00 34.09           C  
ANISOU 1427  C   ALA A 547     4962   3653   4338    302    777      4       C  
ATOM   1428  O   ALA A 547      49.371  72.464  21.393  1.00 32.79           O  
ANISOU 1428  O   ALA A 547     4903   3458   4098    308    824    -37       O  
ATOM   1429  CB  ALA A 547      48.588  71.884  24.440  1.00 32.56           C  
ANISOU 1429  CB  ALA A 547     4742   3409   4219    340    588     42       C  
ATOM   1430  N   PRO A 548      51.002  73.163  22.736  1.00 34.47           N  
ANISOU 1430  N   PRO A 548     4883   3752   4461    310    837     13       N  
ATOM   1431  CA  PRO A 548      51.993  72.993  21.691  1.00 35.40           C  
ANISOU 1431  CA  PRO A 548     4981   3892   4577    331    979    -26       C  
ATOM   1432  C   PRO A 548      52.108  71.566  21.206  1.00 35.56           C  
ANISOU 1432  C   PRO A 548     5035   3860   4616    423   1033    -85       C  
ATOM   1433  O   PRO A 548      52.428  71.371  20.050  1.00 36.03           O  
ANISOU 1433  O   PRO A 548     5153   3916   4621    430   1152   -137       O  
ATOM   1434  CB  PRO A 548      53.300  73.444  22.350  1.00 36.95           C  
ANISOU 1434  CB  PRO A 548     5000   4159   4879    327   1010      0       C  
ATOM   1435  CG  PRO A 548      53.050  73.362  23.805  1.00 37.05           C  
ANISOU 1435  CG  PRO A 548     4944   4174   4959    335    874     45       C  
ATOM   1436  CD  PRO A 548      51.589  73.712  23.959  1.00 34.92           C  
ANISOU 1436  CD  PRO A 548     4808   3858   4601    289    781     58       C  
ATOM   1437  N   GLU A 549      51.848  70.574  22.055  1.00 35.57           N  
ANISOU 1437  N   GLU A 549     5012   3813   4688    490    954    -80       N  
ATOM   1438  CA  GLU A 549      51.924  69.163  21.585  1.00 37.49           C  
ANISOU 1438  CA  GLU A 549     5305   3983   4956    581   1008   -140       C  
ATOM   1439  C   GLU A 549      50.833  68.861  20.542  1.00 36.70           C  
ANISOU 1439  C   GLU A 549     5392   3826   4724    544   1016   -193       C  
ATOM   1440  O   GLU A 549      51.049  68.054  19.630  1.00 37.19           O  
ANISOU 1440  O   GLU A 549     5526   3841   4760    586   1113   -266       O  
ATOM   1441  CB  GLU A 549      51.944  68.132  22.742  1.00 37.50           C  
ANISOU 1441  CB  GLU A 549     5244   3933   5068    661    921   -111       C  
ATOM   1442  CG  GLU A 549      50.740  68.185  23.702  1.00 35.90           C  
ANISOU 1442  CG  GLU A 549     5094   3706   4838    613    770    -62       C  
ATOM   1443  CD  GLU A 549      50.931  69.161  24.862  1.00 35.73           C  
ANISOU 1443  CD  GLU A 549     4964   3760   4850    565    686     10       C  
ATOM   1444  OE1 GLU A 549      51.708  70.148  24.722  1.00 36.22           O  
ANISOU 1444  OE1 GLU A 549     4943   3898   4920    528    734     21       O  
ATOM   1445  OE2 GLU A 549      50.298  68.951  25.921  1.00 33.98           O  
ANISOU 1445  OE2 GLU A 549     4746   3521   4641    555    575     53       O  
ATOM   1446  N   ILE A 550      49.696  69.543  20.643  1.00 35.02           N  
ANISOU 1446  N   ILE A 550     5256   3620   4427    463    918   -160       N  
ATOM   1447  CA  ILE A 550      48.664  69.440  19.629  1.00 35.43           C  
ANISOU 1447  CA  ILE A 550     5471   3640   4348    414    908   -198       C  
ATOM   1448  C   ILE A 550      49.118  70.106  18.331  1.00 37.12           C  
ANISOU 1448  C   ILE A 550     5744   3896   4461    372   1023   -226       C  
ATOM   1449  O   ILE A 550      48.986  69.535  17.225  1.00 37.49           O  
ANISOU 1449  O   ILE A 550     5912   3913   4418    370   1092   -295       O  
ATOM   1450  CB  ILE A 550      47.340  70.065  20.104  1.00 36.14           C  
ANISOU 1450  CB  ILE A 550     5604   3736   4391    347    770   -146       C  
ATOM   1451  CG1 ILE A 550      46.737  69.207  21.225  1.00 35.57           C  
ANISOU 1451  CG1 ILE A 550     5506   3614   4393    378    670   -131       C  
ATOM   1452  CG2 ILE A 550      46.385  70.175  18.922  1.00 37.19           C  
ANISOU 1452  CG2 ILE A 550     5888   3859   4382    290    757   -175       C  
ATOM   1453  CD1 ILE A 550      45.549  69.831  21.935  1.00 35.67           C  
ANISOU 1453  CD1 ILE A 550     5523   3642   4385    321    548    -78       C  
ATOM   1454  N   LEU A 551      49.674  71.312  18.455  1.00 36.57           N  
ANISOU 1454  N   LEU A 551     5601   3894   4400    330   1050   -175       N  
ATOM   1455  CA  LEU A 551      50.208  72.007  17.279  1.00 39.04           C  
ANISOU 1455  CA  LEU A 551     5964   4249   4618    282   1170   -189       C  
ATOM   1456  C   LEU A 551      51.252  71.184  16.543  1.00 40.14           C  
ANISOU 1456  C   LEU A 551     6091   4385   4773    339   1331   -267       C  
ATOM   1457  O   LEU A 551      51.327  71.268  15.331  1.00 40.40           O  
ANISOU 1457  O   LEU A 551     6234   4427   4687    303   1430   -308       O  
ATOM   1458  CB  LEU A 551      50.807  73.376  17.644  1.00 38.08           C  
ANISOU 1458  CB  LEU A 551     5748   4191   4527    225   1184   -122       C  
ATOM   1459  CG  LEU A 551      49.771  74.347  18.193  1.00 38.06           C  
ANISOU 1459  CG  LEU A 551     5779   4183   4495    167   1048    -53       C  
ATOM   1460  CD1 LEU A 551      50.405  75.706  18.470  1.00 38.06           C  
ANISOU 1460  CD1 LEU A 551     5709   4230   4523    103   1075      2       C  
ATOM   1461  CD2 LEU A 551      48.571  74.465  17.239  1.00 38.56           C  
ANISOU 1461  CD2 LEU A 551     6014   4221   4416    126    999    -53       C  
ATOM   1462  N   LEU A 552      52.047  70.409  17.278  1.00 40.86           N  
ANISOU 1462  N   LEU A 552     6051   4464   5010    429   1358   -283       N  
ATOM   1463  CA  LEU A 552      53.083  69.588  16.678  1.00 43.94           C  
ANISOU 1463  CA  LEU A 552     6406   4843   5443    505   1518   -358       C  
ATOM   1464  C   LEU A 552      52.563  68.212  16.248  1.00 43.90           C  
ANISOU 1464  C   LEU A 552     6527   4741   5412    566   1528   -441       C  
ATOM   1465  O   LEU A 552      53.347  67.373  15.842  1.00 43.57           O  
ANISOU 1465  O   LEU A 552     6464   4668   5423    648   1658   -513       O  
ATOM   1466  CB  LEU A 552      54.271  69.429  17.639  1.00 46.07           C  
ANISOU 1466  CB  LEU A 552     6460   5147   5896    584   1542   -330       C  
ATOM   1467  CG  LEU A 552      55.024  70.703  18.054  1.00 47.06           C  
ANISOU 1467  CG  LEU A 552     6442   5372   6064    520   1551   -262       C  
ATOM   1468  CD1 LEU A 552      55.865  70.457  19.300  1.00 46.77           C  
ANISOU 1468  CD1 LEU A 552     6198   5365   6205    589   1501   -219       C  
ATOM   1469  CD2 LEU A 552      55.881  71.218  16.905  1.00 48.14           C  
ANISOU 1469  CD2 LEU A 552     6575   5567   6145    479   1736   -298       C  
ATOM   1470  N   GLY A 553      51.253  67.982  16.340  1.00 42.68           N  
ANISOU 1470  N   GLY A 553     6497   4535   5183    524   1397   -435       N  
ATOM   1471  CA  GLY A 553      50.653  66.731  15.844  1.00 43.23           C  
ANISOU 1471  CA  GLY A 553     6708   4508   5208    553   1400   -518       C  
ATOM   1472  C   GLY A 553      51.025  65.488  16.639  1.00 42.73           C  
ANISOU 1472  C   GLY A 553     6576   4358   5299    668   1396   -540       C  
ATOM   1473  O   GLY A 553      50.985  64.374  16.113  1.00 42.76           O  
ANISOU 1473  O   GLY A 553     6680   4271   5295    715   1459   -628       O  
ATOM   1474  N   GLN A 554      51.416  65.660  17.898  1.00 42.45           N  
ANISOU 1474  N   GLN A 554     6380   4346   5402    713   1323   -460       N  
ATOM   1475  CA  GLN A 554      51.762  64.517  18.750  1.00 44.03           C  
ANISOU 1475  CA  GLN A 554     6513   4463   5750    825   1300   -457       C  
ATOM   1476  C   GLN A 554      50.504  63.903  19.371  1.00 42.72           C  
ANISOU 1476  C   GLN A 554     6443   4218   5569    795   1152   -435       C  
ATOM   1477  O   GLN A 554      49.527  64.604  19.682  1.00 40.32           O  
ANISOU 1477  O   GLN A 554     6172   3955   5193    701   1036   -385       O  
ATOM   1478  CB  GLN A 554      52.705  64.936  19.871  1.00 45.07           C  
ANISOU 1478  CB  GLN A 554     6435   4661   6026    878   1268   -372       C  
ATOM   1479  CG  GLN A 554      53.973  65.627  19.404  1.00 47.87           C  
ANISOU 1479  CG  GLN A 554     6663   5110   6414    893   1404   -381       C  
ATOM   1480  CD  GLN A 554      54.802  64.708  18.569  1.00 51.86           C  
ANISOU 1480  CD  GLN A 554     7174   5563   6967    995   1574   -473       C  
ATOM   1481  OE1 GLN A 554      55.320  63.718  19.074  1.00 55.54           O  
ANISOU 1481  OE1 GLN A 554     7568   5961   7571   1119   1583   -477       O  
ATOM   1482  NE2 GLN A 554      54.903  64.995  17.267  1.00 54.14           N  
ANISOU 1482  NE2 GLN A 554     7559   5875   7135    948   1715   -550       N  
ATOM   1483  N   LYS A 555      50.541  62.600  19.604  1.00 42.83           N  
ANISOU 1483  N   LYS A 555     6494   4115   5663    878   1158   -469       N  
ATOM   1484  CA  LYS A 555      49.475  61.955  20.359  1.00 43.16           C  
ANISOU 1484  CA  LYS A 555     6605   4079   5715    850   1022   -436       C  
ATOM   1485  C   LYS A 555      49.543  62.534  21.760  1.00 40.81           C  
ANISOU 1485  C   LYS A 555     6164   3846   5494    849    906   -319       C  
ATOM   1486  O   LYS A 555      50.631  62.782  22.264  1.00 40.61           O  
ANISOU 1486  O   LYS A 555     5989   3870   5568    919    935   -276       O  
ATOM   1487  CB  LYS A 555      49.689  60.467  20.424  1.00 47.20           C  
ANISOU 1487  CB  LYS A 555     7174   4442   6317    948   1061   -483       C  
ATOM   1488  CG  LYS A 555      49.796  59.804  19.077  1.00 52.48           C  
ANISOU 1488  CG  LYS A 555     7984   5035   6920    963   1197   -615       C  
ATOM   1489  CD  LYS A 555      50.112  58.331  19.251  1.00 58.25           C  
ANISOU 1489  CD  LYS A 555     8764   5599   7766   1075   1241   -659       C  
ATOM   1490  CE  LYS A 555      48.868  57.488  19.058  1.00 62.82           C  
ANISOU 1490  CE  LYS A 555     9533   6060   8274    995   1172   -708       C  
ATOM   1491  NZ  LYS A 555      48.639  57.239  17.607  1.00 64.91           N  
ANISOU 1491  NZ  LYS A 555     9967   6290   8406    944   1279   -847       N  
ATOM   1492  N   TYR A 556      48.400  62.751  22.399  1.00 38.12           N  
ANISOU 1492  N   TYR A 556     5864   3510   5107    766    777   -269       N  
ATOM   1493  CA  TYR A 556      48.408  63.471  23.666  1.00 37.06           C  
ANISOU 1493  CA  TYR A 556     5611   3452   5018    745    676   -168       C  
ATOM   1494  C   TYR A 556      47.393  62.936  24.679  1.00 36.45           C  
ANISOU 1494  C   TYR A 556     5575   3322   4951    710    553   -117       C  
ATOM   1495  O   TYR A 556      46.460  62.219  24.334  1.00 34.81           O  
ANISOU 1495  O   TYR A 556     5492   3035   4700    672    532   -156       O  
ATOM   1496  CB  TYR A 556      48.169  64.971  23.408  1.00 35.68           C  
ANISOU 1496  CB  TYR A 556     5407   3394   4755    656    665   -150       C  
ATOM   1497  CG  TYR A 556      46.821  65.252  22.768  1.00 34.60           C  
ANISOU 1497  CG  TYR A 556     5398   3252   4493    558    621   -178       C  
ATOM   1498  CD1 TYR A 556      45.669  65.403  23.547  1.00 34.26           C  
ANISOU 1498  CD1 TYR A 556     5372   3212   4430    495    503   -131       C  
ATOM   1499  CD2 TYR A 556      46.691  65.337  21.398  1.00 36.09           C  
ANISOU 1499  CD2 TYR A 556     5688   3438   4584    529    694   -249       C  
ATOM   1500  CE1 TYR A 556      44.436  65.632  22.962  1.00 33.49           C  
ANISOU 1500  CE1 TYR A 556     5371   3118   4235    413    456   -152       C  
ATOM   1501  CE2 TYR A 556      45.460  65.570  20.803  1.00 35.47           C  
ANISOU 1501  CE2 TYR A 556     5721   3363   4392    441    636   -267       C  
ATOM   1502  CZ  TYR A 556      44.339  65.709  21.588  1.00 34.94           C  
ANISOU 1502  CZ  TYR A 556     5650   3301   4324    387    515   -217       C  
ATOM   1503  OH  TYR A 556      43.123  65.952  20.988  1.00 34.90           O  
ANISOU 1503  OH  TYR A 556     5732   3307   4218    305    451   -230       O  
ATOM   1504  N   ASN A 557      47.584  63.327  25.932  1.00 37.93           N  
ANISOU 1504  N   ASN A 557     5659   3561   5190    711    475    -29       N  
ATOM   1505  CA  ASN A 557      46.646  63.006  27.005  1.00 37.00           C  
ANISOU 1505  CA  ASN A 557     5570   3416   5070    664    365     29       C  
ATOM   1506  C   ASN A 557      46.196  64.289  27.712  1.00 37.16           C  
ANISOU 1506  C   ASN A 557     5529   3547   5040    581    298     80       C  
ATOM   1507  O   ASN A 557      46.102  65.352  27.086  1.00 36.34           O  
ANISOU 1507  O   ASN A 557     5416   3513   4875    535    327     54       O  
ATOM   1508  CB  ASN A 557      47.274  61.959  27.963  1.00 38.93           C  
ANISOU 1508  CB  ASN A 557     5777   3590   5425    752    332     88       C  
ATOM   1509  CG  ASN A 557      48.562  62.446  28.613  1.00 39.45           C  
ANISOU 1509  CG  ASN A 557     5686   3735   5567    818    327    145       C  
ATOM   1510  OD1 ASN A 557      48.895  63.671  28.657  1.00 36.54           O  
ANISOU 1510  OD1 ASN A 557     5231   3483   5167    775    330    154       O  
ATOM   1511  ND2 ASN A 557      49.286  61.506  29.157  1.00 40.46           N  
ANISOU 1511  ND2 ASN A 557     5775   3799   5798    919    313    190       N  
ATOM   1512  N   HIS A 558      45.867  64.178  28.998  1.00 35.22           N  
ANISOU 1512  N   HIS A 558     5256   3309   4815    560    212    151       N  
ATOM   1513  CA  HIS A 558      45.372  65.281  29.807  1.00 34.60           C  
ANISOU 1513  CA  HIS A 558     5134   3321   4691    483    153    192       C  
ATOM   1514  C   HIS A 558      46.343  66.460  29.970  1.00 33.46           C  
ANISOU 1514  C   HIS A 558     4879   3275   4556    485    171    207       C  
ATOM   1515  O   HIS A 558      45.950  67.532  30.442  1.00 32.96           O  
ANISOU 1515  O   HIS A 558     4793   3280   4449    418    140    223       O  
ATOM   1516  CB  HIS A 558      44.929  64.748  31.191  1.00 35.85           C  
ANISOU 1516  CB  HIS A 558     5296   3461   4864    461     70    263       C  
ATOM   1517  CG  HIS A 558      46.056  64.245  32.035  1.00 36.87           C  
ANISOU 1517  CG  HIS A 558     5353   3585   5068    535     40    326       C  
ATOM   1518  ND1 HIS A 558      46.714  63.066  31.779  1.00 42.58           N  
ANISOU 1518  ND1 HIS A 558     6090   4217   5871    631     63    330       N  
ATOM   1519  CD2 HIS A 558      46.684  64.799  33.095  1.00 39.33           C  
ANISOU 1519  CD2 HIS A 558     5574   3975   5391    530    -13    388       C  
ATOM   1520  CE1 HIS A 558      47.681  62.894  32.665  1.00 42.04           C  
ANISOU 1520  CE1 HIS A 558     5933   4173   5866    690     16    402       C  
ATOM   1521  NE2 HIS A 558      47.671  63.924  33.485  1.00 41.69           N  
ANISOU 1521  NE2 HIS A 558     5827   4236   5775    622    -35    439       N  
ATOM   1522  N   SER A 559      47.592  66.279  29.553  1.00 33.55           N  
ANISOU 1522  N   SER A 559     4824   3292   4631    560    228    197       N  
ATOM   1523  CA  SER A 559      48.570  67.383  29.495  1.00 33.75           C  
ANISOU 1523  CA  SER A 559     4743   3411   4669    552    259    201       C  
ATOM   1524  C   SER A 559      47.995  68.627  28.850  1.00 33.21           C  
ANISOU 1524  C   SER A 559     4711   3388   4516    470    288    168       C  
ATOM   1525  O   SER A 559      48.253  69.733  29.302  1.00 34.25           O  
ANISOU 1525  O   SER A 559     4784   3592   4637    419    271    189       O  
ATOM   1526  CB  SER A 559      49.816  66.949  28.707  1.00 33.98           C  
ANISOU 1526  CB  SER A 559     4708   3431   4769    640    351    171       C  
ATOM   1527  OG  SER A 559      49.479  66.766  27.335  1.00 34.51           O  
ANISOU 1527  OG  SER A 559     4870   3453   4787    643    441     96       O  
ATOM   1528  N   VAL A 560      47.192  68.447  27.808  1.00 33.86           N  
ANISOU 1528  N   VAL A 560     4899   3426   4540    454    324    119       N  
ATOM   1529  CA  VAL A 560      46.674  69.588  27.037  1.00 33.50           C  
ANISOU 1529  CA  VAL A 560     4896   3418   4415    389    350     96       C  
ATOM   1530  C   VAL A 560      45.791  70.490  27.864  1.00 33.19           C  
ANISOU 1530  C   VAL A 560     4855   3411   4342    321    277    130       C  
ATOM   1531  O   VAL A 560      45.813  71.720  27.663  1.00 32.21           O  
ANISOU 1531  O   VAL A 560     4719   3331   4186    276    293    133       O  
ATOM   1532  CB  VAL A 560      45.964  69.154  25.714  1.00 33.37           C  
ANISOU 1532  CB  VAL A 560     4997   3351   4330    383    388     40       C  
ATOM   1533  CG1 VAL A 560      46.899  68.267  24.888  1.00 34.40           C  
ANISOU 1533  CG1 VAL A 560     5136   3443   4491    453    480     -7       C  
ATOM   1534  CG2 VAL A 560      44.638  68.434  25.997  1.00 33.06           C  
ANISOU 1534  CG2 VAL A 560     5035   3260   4266    357    314     40       C  
ATOM   1535  N   ASP A 561      45.064  69.925  28.824  1.00 32.19           N  
ANISOU 1535  N   ASP A 561     4741   3262   4225    312    207    156       N  
ATOM   1536  CA  ASP A 561      44.206  70.725  29.685  1.00 30.95           C  
ANISOU 1536  CA  ASP A 561     4582   3137   4039    251    152    180       C  
ATOM   1537  C   ASP A 561      45.029  71.609  30.620  1.00 29.92           C  
ANISOU 1537  C   ASP A 561     4369   3068   3930    230    140    209       C  
ATOM   1538  O   ASP A 561      44.597  72.721  30.939  1.00 28.12           O  
ANISOU 1538  O   ASP A 561     4141   2869   3671    178    130    210       O  
ATOM   1539  CB  ASP A 561      43.258  69.864  30.554  1.00 31.19           C  
ANISOU 1539  CB  ASP A 561     4644   3134   4070    237     92    202       C  
ATOM   1540  CG  ASP A 561      42.084  69.265  29.771  1.00 31.59           C  
ANISOU 1540  CG  ASP A 561     4777   3137   4089    220     87    173       C  
ATOM   1541  OD1 ASP A 561      41.755  69.705  28.662  1.00 31.42           O  
ANISOU 1541  OD1 ASP A 561     4792   3116   4027    211    112    140       O  
ATOM   1542  OD2 ASP A 561      41.504  68.281  30.269  1.00 32.77           O  
ANISOU 1542  OD2 ASP A 561     4957   3243   4249    212     53    186       O  
ATOM   1543  N   TRP A 562      46.185  71.120  31.080  1.00 29.11           N  
ANISOU 1543  N   TRP A 562     4196   2982   3883    270    136    232       N  
ATOM   1544  CA  TRP A 562      47.062  71.939  31.929  1.00 30.56           C  
ANISOU 1544  CA  TRP A 562     4292   3232   4084    239    114    257       C  
ATOM   1545  C   TRP A 562      47.742  73.128  31.214  1.00 31.02           C  
ANISOU 1545  C   TRP A 562     4315   3331   4140    207    175    233       C  
ATOM   1546  O   TRP A 562      47.972  74.167  31.818  1.00 30.21           O  
ANISOU 1546  O   TRP A 562     4179   3272   4026    146    158    240       O  
ATOM   1547  CB  TRP A 562      48.075  71.061  32.689  1.00 30.48           C  
ANISOU 1547  CB  TRP A 562     4204   3237   4138    290     73    300       C  
ATOM   1548  CG  TRP A 562      47.351  70.166  33.627  1.00 32.09           C  
ANISOU 1548  CG  TRP A 562     4456   3407   4330    294      4    338       C  
ATOM   1549  CD1 TRP A 562      47.275  68.787  33.567  1.00 34.06           C  
ANISOU 1549  CD1 TRP A 562     4737   3587   4617    360     -7    357       C  
ATOM   1550  CD2 TRP A 562      46.500  70.562  34.724  1.00 32.36           C  
ANISOU 1550  CD2 TRP A 562     4526   3462   4306    224    -50    357       C  
ATOM   1551  NE1 TRP A 562      46.450  68.320  34.561  1.00 33.76           N  
ANISOU 1551  NE1 TRP A 562     4751   3529   4545    327    -70    396       N  
ATOM   1552  CE2 TRP A 562      45.959  69.376  35.283  1.00 33.24           C  
ANISOU 1552  CE2 TRP A 562     4686   3524   4418    244    -93    395       C  
ATOM   1553  CE3 TRP A 562      46.156  71.796  35.292  1.00 31.17           C  
ANISOU 1553  CE3 TRP A 562     4377   3362   4103    144    -59    343       C  
ATOM   1554  CZ2 TRP A 562      45.099  69.383  36.405  1.00 33.53           C  
ANISOU 1554  CZ2 TRP A 562     4767   3572   4398    182   -140    422       C  
ATOM   1555  CZ3 TRP A 562      45.269  71.801  36.416  1.00 33.19           C  
ANISOU 1555  CZ3 TRP A 562     4679   3627   4305     91   -102    360       C  
ATOM   1556  CH2 TRP A 562      44.751  70.598  36.935  1.00 32.91           C  
ANISOU 1556  CH2 TRP A 562     4685   3552   4265    109   -139    400       C  
ATOM   1557  N   TRP A 563      48.064  72.988  29.936  1.00 32.95           N  
ANISOU 1557  N   TRP A 563     4574   3556   4388    240    251    204       N  
ATOM   1558  CA  TRP A 563      48.467  74.163  29.141  1.00 32.60           C  
ANISOU 1558  CA  TRP A 563     4525   3538   4321    196    316    186       C  
ATOM   1559  C   TRP A 563      47.333  75.176  29.010  1.00 31.80           C  
ANISOU 1559  C   TRP A 563     4508   3419   4156    139    302    181       C  
ATOM   1560  O   TRP A 563      47.499  76.368  29.296  1.00 30.66           O  
ANISOU 1560  O   TRP A 563     4350   3296   4002     80    306    187       O  
ATOM   1561  CB  TRP A 563      48.953  73.746  27.758  1.00 32.09           C  
ANISOU 1561  CB  TRP A 563     4478   3457   4255    239    409    156       C  
ATOM   1562  CG  TRP A 563      49.518  74.881  26.974  1.00 33.27           C  
ANISOU 1562  CG  TRP A 563     4619   3638   4382    188    484    148       C  
ATOM   1563  CD1 TRP A 563      48.823  75.735  26.175  1.00 31.36           C  
ANISOU 1563  CD1 TRP A 563     4472   3376   4066    143    508    142       C  
ATOM   1564  CD2 TRP A 563      50.906  75.269  26.865  1.00 32.78           C  
ANISOU 1564  CD2 TRP A 563     4449   3633   4372    175    547    150       C  
ATOM   1565  NE1 TRP A 563      49.675  76.641  25.602  1.00 32.39           N  
ANISOU 1565  NE1 TRP A 563     4575   3538   4193     97    584    145       N  
ATOM   1566  CE2 TRP A 563      50.957  76.375  25.995  1.00 33.10           C  
ANISOU 1566  CE2 TRP A 563     4537   3679   4360    110    614    145       C  
ATOM   1567  CE3 TRP A 563      52.096  74.794  27.416  1.00 33.54           C  
ANISOU 1567  CE3 TRP A 563     4407   3777   4557    210    549    162       C  
ATOM   1568  CZ2 TRP A 563      52.160  77.022  25.657  1.00 33.36           C  
ANISOU 1568  CZ2 TRP A 563     4486   3764   4425     67    695    147       C  
ATOM   1569  CZ3 TRP A 563      53.289  75.424  27.078  1.00 34.33           C  
ANISOU 1569  CZ3 TRP A 563     4408   3937   4697    174    623    161       C  
ATOM   1570  CH2 TRP A 563      53.315  76.525  26.200  1.00 33.96           C  
ANISOU 1570  CH2 TRP A 563     4413   3895   4594     98    701    151       C  
ATOM   1571  N   SER A 564      46.178  74.719  28.546  1.00 30.52           N  
ANISOU 1571  N   SER A 564     4430   3211   3952    157    286    170       N  
ATOM   1572  CA  SER A 564      45.027  75.604  28.472  1.00 30.33           C  
ANISOU 1572  CA  SER A 564     4470   3171   3883    118    263    172       C  
ATOM   1573  C   SER A 564      44.736  76.312  29.795  1.00 28.79           C  
ANISOU 1573  C   SER A 564     4247   2993   3699     77    218    186       C  
ATOM   1574  O   SER A 564      44.365  77.489  29.816  1.00 29.56           O  
ANISOU 1574  O   SER A 564     4369   3083   3779     39    225    185       O  
ATOM   1575  CB  SER A 564      43.800  74.832  27.997  1.00 30.04           C  
ANISOU 1575  CB  SER A 564     4504   3096   3813    140    233    162       C  
ATOM   1576  OG  SER A 564      44.087  74.231  26.746  1.00 35.02           O  
ANISOU 1576  OG  SER A 564     5177   3709   4419    168    278    140       O  
ATOM   1577  N   PHE A 565      44.865  75.580  30.899  1.00 29.50           N  
ANISOU 1577  N   PHE A 565     4296   3099   3812     84    172    197       N  
ATOM   1578  CA  PHE A 565      44.670  76.142  32.225  1.00 28.73           C  
ANISOU 1578  CA  PHE A 565     4180   3025   3709     38    133    204       C  
ATOM   1579  C   PHE A 565      45.628  77.295  32.509  1.00 28.75           C  
ANISOU 1579  C   PHE A 565     4141   3061   3721    -14    151    199       C  
ATOM   1580  O   PHE A 565      45.236  78.324  33.021  1.00 30.40           O  
ANISOU 1580  O   PHE A 565     4374   3264   3910    -63    150    185       O  
ATOM   1581  CB  PHE A 565      44.824  75.038  33.271  1.00 30.18           C  
ANISOU 1581  CB  PHE A 565     4334   3225   3906     52     79    229       C  
ATOM   1582  CG  PHE A 565      44.701  75.513  34.679  1.00 31.02           C  
ANISOU 1582  CG  PHE A 565     4431   3366   3989     -2     38    236       C  
ATOM   1583  CD1 PHE A 565      43.456  75.775  35.231  1.00 30.82           C  
ANISOU 1583  CD1 PHE A 565     4455   3325   3927    -29     32    224       C  
ATOM   1584  CD2 PHE A 565      45.827  75.687  35.464  1.00 30.47           C  
ANISOU 1584  CD2 PHE A 565     4299   3347   3930    -31      6    252       C  
ATOM   1585  CE1 PHE A 565      43.336  76.186  36.558  1.00 31.75           C  
ANISOU 1585  CE1 PHE A 565     4577   3476   4010    -84      7    221       C  
ATOM   1586  CE2 PHE A 565      45.718  76.116  36.784  1.00 31.36           C  
ANISOU 1586  CE2 PHE A 565     4417   3495   4001    -93    -35    254       C  
ATOM   1587  CZ  PHE A 565      44.472  76.387  37.330  1.00 32.20           C  
ANISOU 1587  CZ  PHE A 565     4590   3583   4062   -121    -27    234       C  
ATOM   1588  N   GLY A 566      46.887  77.099  32.176  1.00 28.55           N  
ANISOU 1588  N   GLY A 566     4050   3066   3730     -5    172    207       N  
ATOM   1589  CA  GLY A 566      47.872  78.164  32.159  1.00 29.83           C  
ANISOU 1589  CA  GLY A 566     4167   3260   3907    -64    201    201       C  
ATOM   1590  C   GLY A 566      47.435  79.390  31.393  1.00 28.49           C  
ANISOU 1590  C   GLY A 566     4065   3049   3710   -101    253    186       C  
ATOM   1591  O   GLY A 566      47.584  80.481  31.896  1.00 28.54           O  
ANISOU 1591  O   GLY A 566     4077   3054   3711   -169    254    175       O  
ATOM   1592  N   VAL A 567      46.933  79.197  30.166  1.00 28.65           N  
ANISOU 1592  N   VAL A 567     4142   3032   3710    -59    293    187       N  
ATOM   1593  CA  VAL A 567      46.521  80.295  29.321  1.00 29.10           C  
ANISOU 1593  CA  VAL A 567     4271   3046   3737    -86    335    188       C  
ATOM   1594  C   VAL A 567      45.367  81.038  30.022  1.00 29.71           C  
ANISOU 1594  C   VAL A 567     4402   3084   3801   -101    299    182       C  
ATOM   1595  O   VAL A 567      45.380  82.260  30.125  1.00 27.85           O  
ANISOU 1595  O   VAL A 567     4198   2817   3566   -148    319    179       O  
ATOM   1596  CB  VAL A 567      46.119  79.810  27.905  1.00 28.81           C  
ANISOU 1596  CB  VAL A 567     4294   2985   3664    -38    368    195       C  
ATOM   1597  CG1 VAL A 567      45.510  80.956  27.108  1.00 28.98           C  
ANISOU 1597  CG1 VAL A 567     4403   2960   3648    -61    390    212       C  
ATOM   1598  CG2 VAL A 567      47.343  79.227  27.176  1.00 29.52           C  
ANISOU 1598  CG2 VAL A 567     4335   3111   3768    -26    431    189       C  
ATOM   1599  N   LEU A 568      44.404  80.271  30.527  1.00 28.97           N  
ANISOU 1599  N   LEU A 568     4317   2988   3701    -62    252    179       N  
ATOM   1600  CA  LEU A 568      43.258  80.820  31.213  1.00 30.47           C  
ANISOU 1600  CA  LEU A 568     4542   3148   3885    -66    229    168       C  
ATOM   1601  C   LEU A 568      43.655  81.650  32.469  1.00 31.11           C  
ANISOU 1601  C   LEU A 568     4608   3238   3972   -129    227    145       C  
ATOM   1602  O   LEU A 568      43.212  82.783  32.627  1.00 30.92           O  
ANISOU 1602  O   LEU A 568     4629   3168   3950   -152    249    129       O  
ATOM   1603  CB  LEU A 568      42.295  79.699  31.569  1.00 31.19           C  
ANISOU 1603  CB  LEU A 568     4630   3249   3971    -26    188    169       C  
ATOM   1604  CG  LEU A 568      40.909  80.064  32.132  1.00 30.87           C  
ANISOU 1604  CG  LEU A 568     4613   3186   3929    -18    174    159       C  
ATOM   1605  CD1 LEU A 568      39.942  78.896  31.982  1.00 32.15           C  
ANISOU 1605  CD1 LEU A 568     4772   3355   4086     16    141    167       C  
ATOM   1606  CD2 LEU A 568      40.998  80.425  33.590  1.00 33.71           C  
ANISOU 1606  CD2 LEU A 568     4959   3564   4285    -63    172    134       C  
ATOM   1607  N   LEU A 569      44.558  81.107  33.285  1.00 30.55           N  
ANISOU 1607  N   LEU A 569     4478   3223   3906   -158    200    143       N  
ATOM   1608  CA  LEU A 569      45.046  81.805  34.471  1.00 31.45           C  
ANISOU 1608  CA  LEU A 569     4579   3359   4011   -232    186    118       C  
ATOM   1609  C   LEU A 569      45.789  83.081  34.110  1.00 31.19           C  
ANISOU 1609  C   LEU A 569     4558   3300   3990   -296    228    104       C  
ATOM   1610  O   LEU A 569      45.606  84.114  34.754  1.00 30.13           O  
ANISOU 1610  O   LEU A 569     4467   3134   3846   -352    239     71       O  
ATOM   1611  CB  LEU A 569      45.999  80.911  35.245  1.00 33.68           C  
ANISOU 1611  CB  LEU A 569     4787   3715   4295   -248    134    134       C  
ATOM   1612  CG  LEU A 569      46.138  80.972  36.757  1.00 36.61           C  
ANISOU 1612  CG  LEU A 569     5150   4129   4630   -309     83    120       C  
ATOM   1613  CD1 LEU A 569      47.524  80.560  37.217  1.00 38.70           C  
ANISOU 1613  CD1 LEU A 569     5325   4470   4910   -342     30    144       C  
ATOM   1614  CD2 LEU A 569      45.615  82.190  37.479  1.00 36.74           C  
ANISOU 1614  CD2 LEU A 569     5233   4113   4612   -375    105     69       C  
ATOM   1615  N   TYR A 570      46.645  82.993  33.087  1.00 31.48           N  
ANISOU 1615  N   TYR A 570     4560   3349   4049   -292    258    128       N  
ATOM   1616  CA  TYR A 570      47.363  84.154  32.587  1.00 31.86           C  
ANISOU 1616  CA  TYR A 570     4622   3371   4110   -359    308    124       C  
ATOM   1617  C   TYR A 570      46.398  85.247  32.167  1.00 31.92           C  
ANISOU 1617  C   TYR A 570     4734   3283   4108   -355    343    119       C  
ATOM   1618  O   TYR A 570      46.574  86.428  32.515  1.00 30.83           O  
ANISOU 1618  O   TYR A 570     4638   3098   3976   -426    365     96       O  
ATOM   1619  CB  TYR A 570      48.286  83.764  31.432  1.00 31.12           C  
ANISOU 1619  CB  TYR A 570     4479   3307   4035   -346    351    152       C  
ATOM   1620  CG  TYR A 570      49.111  84.881  30.892  1.00 30.75           C  
ANISOU 1620  CG  TYR A 570     4439   3242   4001   -428    411    155       C  
ATOM   1621  CD1 TYR A 570      48.554  85.886  30.104  1.00 31.28           C  
ANISOU 1621  CD1 TYR A 570     4610   3223   4050   -439    458    168       C  
ATOM   1622  CD2 TYR A 570      50.484  84.921  31.116  1.00 31.94           C  
ANISOU 1622  CD2 TYR A 570     4488   3462   4186   -497    420    153       C  
ATOM   1623  CE1 TYR A 570      49.331  86.905  29.594  1.00 31.50           C  
ANISOU 1623  CE1 TYR A 570     4654   3224   4087   -524    518    178       C  
ATOM   1624  CE2 TYR A 570      51.256  85.950  30.631  1.00 33.35           C  
ANISOU 1624  CE2 TYR A 570     4668   3624   4377   -589    481    156       C  
ATOM   1625  CZ  TYR A 570      50.692  86.930  29.865  1.00 33.68           C  
ANISOU 1625  CZ  TYR A 570     4828   3572   4396   -606    533    169       C  
ATOM   1626  OH  TYR A 570      51.532  87.920  29.386  1.00 33.68           O  
ANISOU 1626  OH  TYR A 570     4834   3553   4410   -709    598    179       O  
ATOM   1627  N   GLU A 571      45.350  84.861  31.458  1.00 31.77           N  
ANISOU 1627  N   GLU A 571     4759   3232   4079   -274    342    140       N  
ATOM   1628  CA  GLU A 571      44.340  85.828  31.058  1.00 32.30           C  
ANISOU 1628  CA  GLU A 571     4914   3211   4146   -250    362    146       C  
ATOM   1629  C   GLU A 571      43.632  86.458  32.267  1.00 31.09           C  
ANISOU 1629  C   GLU A 571     4790   3021   4003   -265    353    103       C  
ATOM   1630  O   GLU A 571      43.421  87.677  32.301  1.00 30.67           O  
ANISOU 1630  O   GLU A 571     4802   2885   3966   -289    386     90       O  
ATOM   1631  CB  GLU A 571      43.324  85.206  30.104  1.00 33.95           C  
ANISOU 1631  CB  GLU A 571     5148   3409   4340   -163    344    180       C  
ATOM   1632  CG  GLU A 571      43.858  84.897  28.714  1.00 35.40           C  
ANISOU 1632  CG  GLU A 571     5345   3606   4499   -153    369    218       C  
ATOM   1633  CD  GLU A 571      42.810  84.195  27.863  1.00 39.13           C  
ANISOU 1633  CD  GLU A 571     5847   4076   4944    -79    337    243       C  
ATOM   1634  OE1 GLU A 571      41.838  83.680  28.455  1.00 41.62           O  
ANISOU 1634  OE1 GLU A 571     6144   4399   5270    -38    293    229       O  
ATOM   1635  OE2 GLU A 571      42.965  84.138  26.626  1.00 41.51           O  
ANISOU 1635  OE2 GLU A 571     6191   4373   5207    -70    356    274       O  
ATOM   1636  N   MET A 572      43.305  85.653  33.263  1.00 29.30           N  
ANISOU 1636  N   MET A 572     4521   2846   3763   -253    317     78       N  
ATOM   1637  CA  MET A 572      42.654  86.177  34.470  1.00 30.25           C  
ANISOU 1637  CA  MET A 572     4672   2942   3879   -273    322     28       C  
ATOM   1638  C   MET A 572      43.517  87.208  35.201  1.00 32.68           C  
ANISOU 1638  C   MET A 572     5005   3228   4181   -374    342    -15       C  
ATOM   1639  O   MET A 572      43.006  88.242  35.632  1.00 35.11           O  
ANISOU 1639  O   MET A 572     5380   3459   4498   -390    379    -57       O  
ATOM   1640  CB  MET A 572      42.276  85.071  35.436  1.00 30.15           C  
ANISOU 1640  CB  MET A 572     4615   2999   3838   -260    283     16       C  
ATOM   1641  CG  MET A 572      41.187  84.171  34.895  1.00 32.13           C  
ANISOU 1641  CG  MET A 572     4852   3256   4097   -174    267     47       C  
ATOM   1642  SD  MET A 572      40.423  83.213  36.214  1.00 32.68           S  
ANISOU 1642  SD  MET A 572     4898   3382   4137   -174    243     26       S  
ATOM   1643  CE  MET A 572      41.729  82.110  36.728  1.00 34.34           C  
ANISOU 1643  CE  MET A 572     5056   3675   4316   -218    187     50       C  
ATOM   1644  N   LEU A 573      44.812  86.915  35.335  1.00 32.33           N  
ANISOU 1644  N   LEU A 573     4904   3251   4127   -443    318     -9       N  
ATOM   1645  CA  LEU A 573      45.734  87.796  36.044  1.00 33.22           C  
ANISOU 1645  CA  LEU A 573     5028   3363   4232   -559    323    -51       C  
ATOM   1646  C   LEU A 573      46.190  89.011  35.263  1.00 33.66           C  
ANISOU 1646  C   LEU A 573     5135   3334   4318   -609    376    -47       C  
ATOM   1647  O   LEU A 573      46.328  90.079  35.819  1.00 34.25           O  
ANISOU 1647  O   LEU A 573     5271   3349   4392   -688    400    -96       O  
ATOM   1648  CB  LEU A 573      46.964  87.008  36.467  1.00 33.58           C  
ANISOU 1648  CB  LEU A 573     4972   3520   4264   -612    266    -37       C  
ATOM   1649  CG  LEU A 573      46.634  85.989  37.543  1.00 34.93           C  
ANISOU 1649  CG  LEU A 573     5113   3764   4394   -591    206    -42       C  
ATOM   1650  CD1 LEU A 573      47.710  84.918  37.630  1.00 35.80           C  
ANISOU 1650  CD1 LEU A 573     5111   3978   4510   -594    144      1       C  
ATOM   1651  CD2 LEU A 573      46.422  86.651  38.881  1.00 36.47           C  
ANISOU 1651  CD2 LEU A 573     5366   3952   4537   -672    197   -107       C  
ATOM   1652  N   ILE A 574      46.421  88.846  33.971  1.00 33.73           N  
ANISOU 1652  N   ILE A 574     5130   3337   4349   -570    399      8       N  
ATOM   1653  CA  ILE A 574      47.055  89.864  33.177  1.00 34.35           C  
ANISOU 1653  CA  ILE A 574     5250   3352   4449   -633    451     26       C  
ATOM   1654  C   ILE A 574      46.099  90.574  32.233  1.00 34.23           C  
ANISOU 1654  C   ILE A 574     5336   3221   4448   -566    492     60       C  
ATOM   1655  O   ILE A 574      46.342  91.718  31.879  1.00 32.52           O  
ANISOU 1655  O   ILE A 574     5194   2912   4249   -623    537     66       O  
ATOM   1656  CB  ILE A 574      48.320  89.288  32.498  1.00 35.46           C  
ANISOU 1656  CB  ILE A 574     5295   3581   4597   -670    457     63       C  
ATOM   1657  CG1 ILE A 574      49.280  88.881  33.622  1.00 38.13           C  
ANISOU 1657  CG1 ILE A 574     5534   4020   4933   -747    406     29       C  
ATOM   1658  CG2 ILE A 574      48.993  90.349  31.589  1.00 34.69           C  
ANISOU 1658  CG2 ILE A 574     5242   3420   4516   -748    525     88       C  
ATOM   1659  CD1 ILE A 574      50.236  87.794  33.253  1.00 41.57           C  
ANISOU 1659  CD1 ILE A 574     5841   4568   5386   -728    389     63       C  
ATOM   1660  N   GLY A 575      44.970  89.967  31.880  1.00 32.74           N  
ANISOU 1660  N   GLY A 575     5157   3029   4255   -451    471     85       N  
ATOM   1661  CA  GLY A 575      43.992  90.704  31.073  1.00 33.67           C  
ANISOU 1661  CA  GLY A 575     5365   3038   4390   -382    493    123       C  
ATOM   1662  C   GLY A 575      44.208  90.654  29.575  1.00 36.23           C  
ANISOU 1662  C   GLY A 575     5714   3354   4697   -361    508    199       C  
ATOM   1663  O   GLY A 575      43.506  91.324  28.808  1.00 36.93           O  
ANISOU 1663  O   GLY A 575     5884   3353   4793   -312    517    246       O  
ATOM   1664  N   GLN A 576      45.190  89.872  29.149  1.00 35.16           N  
ANISOU 1664  N   GLN A 576     5510   3311   4536   -396    513    212       N  
ATOM   1665  CA  GLN A 576      45.347  89.536  27.759  1.00 36.56           C  
ANISOU 1665  CA  GLN A 576     5706   3504   4678   -369    532    272       C  
ATOM   1666  C   GLN A 576      45.949  88.136  27.679  1.00 35.51           C  
ANISOU 1666  C   GLN A 576     5473   3491   4527   -355    520    260       C  
ATOM   1667  O   GLN A 576      46.402  87.562  28.678  1.00 34.69           O  
ANISOU 1667  O   GLN A 576     5285   3452   4443   -375    495    218       O  
ATOM   1668  CB  GLN A 576      46.236  90.582  27.017  1.00 40.72           C  
ANISOU 1668  CB  GLN A 576     6292   3977   5201   -460    600    308       C  
ATOM   1669  CG  GLN A 576      47.695  90.571  27.456  1.00 43.89           C  
ANISOU 1669  CG  GLN A 576     6611   4445   5619   -572    636    275       C  
ATOM   1670  CD  GLN A 576      48.607  91.520  26.667  1.00 48.46           C  
ANISOU 1670  CD  GLN A 576     7237   4980   6194   -674    714    313       C  
ATOM   1671  OE1 GLN A 576      49.407  92.212  27.247  1.00 49.97           O  
ANISOU 1671  OE1 GLN A 576     7409   5159   6417   -784    738    284       O  
ATOM   1672  NE2 GLN A 576      48.497  91.524  25.346  1.00 51.66           N  
ANISOU 1672  NE2 GLN A 576     7705   5368   6552   -649    751    377       N  
ATOM   1673  N   SER A 577      45.924  87.586  26.478  1.00 35.04           N  
ANISOU 1673  N   SER A 577     5432   3454   4426   -316    534    299       N  
ATOM   1674  CA  SER A 577      46.412  86.243  26.216  1.00 35.78           C  
ANISOU 1674  CA  SER A 577     5450   3640   4503   -287    534    287       C  
ATOM   1675  C   SER A 577      47.942  86.225  26.202  1.00 32.83           C  
ANISOU 1675  C   SER A 577     4998   3324   4149   -363    595    275       C  
ATOM   1676  O   SER A 577      48.564  87.235  25.881  1.00 32.89           O  
ANISOU 1676  O   SER A 577     5035   3300   4159   -442    650    293       O  
ATOM   1677  CB  SER A 577      45.870  85.779  24.857  1.00 39.86           C  
ANISOU 1677  CB  SER A 577     6032   4153   4958   -232    539    324       C  
ATOM   1678  OG  SER A 577      44.457  85.678  24.918  1.00 42.58           O  
ANISOU 1678  OG  SER A 577     6421   4461   5294   -162    471    335       O  
ATOM   1679  N   PRO A 578      48.551  85.088  26.578  1.00 32.01           N  
ANISOU 1679  N   PRO A 578     4790   3305   4068   -339    584    249       N  
ATOM   1680  CA  PRO A 578      50.015  85.005  26.617  1.00 31.92           C  
ANISOU 1680  CA  PRO A 578     4674   3360   4091   -399    636    240       C  
ATOM   1681  C   PRO A 578      50.673  84.929  25.229  1.00 31.98           C  
ANISOU 1681  C   PRO A 578     4695   3386   4068   -410    733    261       C  
ATOM   1682  O   PRO A 578      51.783  85.374  25.056  1.00 30.31           O  
ANISOU 1682  O   PRO A 578     4425   3208   3881   -487    799    264       O  
ATOM   1683  CB  PRO A 578      50.261  83.738  27.429  1.00 32.39           C  
ANISOU 1683  CB  PRO A 578     4628   3491   4188   -344    584    215       C  
ATOM   1684  CG  PRO A 578      49.059  82.913  27.217  1.00 31.96           C  
ANISOU 1684  CG  PRO A 578     4636   3409   4099   -251    540    215       C  
ATOM   1685  CD  PRO A 578      47.926  83.892  27.168  1.00 31.43           C  
ANISOU 1685  CD  PRO A 578     4678   3261   4000   -260    518    228       C  
ATOM   1686  N   PHE A 579      49.972  84.368  24.253  1.00 31.85           N  
ANISOU 1686  N   PHE A 579     4757   3351   3991   -342    742    274       N  
ATOM   1687  CA  PHE A 579      50.493  84.195  22.906  1.00 33.17           C  
ANISOU 1687  CA  PHE A 579     4956   3538   4106   -350    838    288       C  
ATOM   1688  C   PHE A 579      49.649  85.007  21.902  1.00 35.69           C  
ANISOU 1688  C   PHE A 579     5433   3785   4340   -362    845    337       C  
ATOM   1689  O   PHE A 579      48.442  85.204  22.110  1.00 34.72           O  
ANISOU 1689  O   PHE A 579     5382   3606   4201   -320    762    353       O  
ATOM   1690  CB  PHE A 579      50.552  82.694  22.594  1.00 32.73           C  
ANISOU 1690  CB  PHE A 579     4858   3530   4044   -263    845    254       C  
ATOM   1691  CG  PHE A 579      51.292  81.908  23.626  1.00 32.51           C  
ANISOU 1691  CG  PHE A 579     4683   3562   4107   -236    821    222       C  
ATOM   1692  CD1 PHE A 579      52.662  82.023  23.736  1.00 34.89           C  
ANISOU 1692  CD1 PHE A 579     4862   3926   4468   -282    889    215       C  
ATOM   1693  CD2 PHE A 579      50.619  81.084  24.531  1.00 33.60           C  
ANISOU 1693  CD2 PHE A 579     4798   3695   4272   -170    725    206       C  
ATOM   1694  CE1 PHE A 579      53.368  81.337  24.705  1.00 34.39           C  
ANISOU 1694  CE1 PHE A 579     4653   3921   4491   -254    852    197       C  
ATOM   1695  CE2 PHE A 579      51.322  80.383  25.500  1.00 34.19           C  
ANISOU 1695  CE2 PHE A 579     4744   3821   4424   -146    693    191       C  
ATOM   1696  CZ  PHE A 579      52.715  80.514  25.575  1.00 33.86           C  
ANISOU 1696  CZ  PHE A 579     4577   3844   4443   -184    752    189       C  
ATOM   1697  N   HIS A 580      50.294  85.500  20.844  1.00 38.05           N  
ANISOU 1697  N   HIS A 580     5780   4086   4588   -422    943    366       N  
ATOM   1698  CA  HIS A 580      49.704  86.498  19.939  1.00 41.66           C  
ANISOU 1698  CA  HIS A 580     6390   4470   4966   -455    952    430       C  
ATOM   1699  C   HIS A 580      50.095  86.292  18.507  1.00 40.80           C  
ANISOU 1699  C   HIS A 580     6355   4390   4756   -477   1047    452       C  
ATOM   1700  O   HIS A 580      51.204  85.859  18.216  1.00 38.62           O  
ANISOU 1700  O   HIS A 580     6002   4183   4489   -508   1150    421       O  
ATOM   1701  CB  HIS A 580      50.191  87.925  20.302  1.00 44.86           C  
ANISOU 1701  CB  HIS A 580     6811   4819   5413   -557    983    463       C  
ATOM   1702  CG  HIS A 580      49.806  88.343  21.672  1.00 48.86           C  
ANISOU 1702  CG  HIS A 580     7275   5286   6004   -553    902    438       C  
ATOM   1703  ND1 HIS A 580      50.693  88.324  22.728  1.00 52.58           N  
ANISOU 1703  ND1 HIS A 580     7617   5803   6556   -606    907    392       N  
ATOM   1704  CD2 HIS A 580      48.609  88.720  22.185  1.00 52.15           C  
ANISOU 1704  CD2 HIS A 580     7753   5628   6432   -500    812    448       C  
ATOM   1705  CE1 HIS A 580      50.060  88.700  23.829  1.00 53.23           C  
ANISOU 1705  CE1 HIS A 580     7703   5838   6683   -593    828    371       C  
ATOM   1706  NE2 HIS A 580      48.795  88.947  23.527  1.00 50.86           N  
ANISOU 1706  NE2 HIS A 580     7513   5462   6346   -526    778    402       N  
ATOM   1707  N   GLY A 581      49.205  86.701  17.614  1.00 40.74           N  
ANISOU 1707  N   GLY A 581     6497   4329   4651   -466   1015    510       N  
ATOM   1708  CA  GLY A 581      49.516  86.757  16.194  1.00 42.49           C  
ANISOU 1708  CA  GLY A 581     6826   4568   4750   -508   1104    545       C  
ATOM   1709  C   GLY A 581      48.408  87.431  15.417  1.00 43.45           C  
ANISOU 1709  C   GLY A 581     7116   4618   4773   -498   1032    629       C  
ATOM   1710  O   GLY A 581      47.267  87.370  15.813  1.00 42.78           O  
ANISOU 1710  O   GLY A 581     7049   4495   4708   -427    908    640       O  
ATOM   1711  N   GLN A 582      48.745  88.059  14.303  1.00 47.37           N  
ANISOU 1711  N   GLN A 582     7732   5101   5164   -570   1108    693       N  
ATOM   1712  CA  GLN A 582      47.726  88.652  13.440  1.00 52.38           C  
ANISOU 1712  CA  GLN A 582     8536   5674   5690   -558   1032    788       C  
ATOM   1713  C   GLN A 582      46.950  87.613  12.601  1.00 53.25           C  
ANISOU 1713  C   GLN A 582     8714   5836   5679   -499    971    772       C  
ATOM   1714  O   GLN A 582      45.879  87.912  12.098  1.00 55.28           O  
ANISOU 1714  O   GLN A 582     9082   6055   5867   -466    862    842       O  
ATOM   1715  CB  GLN A 582      48.350  89.711  12.545  1.00 55.97           C  
ANISOU 1715  CB  GLN A 582     9112   6091   6062   -665   1130    874       C  
ATOM   1716  CG  GLN A 582      48.942  90.880  13.323  1.00 60.28           C  
ANISOU 1716  CG  GLN A 582     9618   6562   6722   -736   1171    900       C  
ATOM   1717  CD  GLN A 582      47.895  91.743  14.005  1.00 64.52           C  
ANISOU 1717  CD  GLN A 582    10196   6983   7335   -681   1043    951       C  
ATOM   1718  OE1 GLN A 582      47.870  91.846  15.225  1.00 71.36           O  
ANISOU 1718  OE1 GLN A 582    10955   7825   8332   -658   1008    897       O  
ATOM   1719  NE2 GLN A 582      47.023  92.363  13.217  1.00 68.67           N  
ANISOU 1719  NE2 GLN A 582    10878   7435   7777   -658    974   1056       N  
ATOM   1720  N   ASP A 583      47.480  86.405  12.444  1.00 51.27           N  
ANISOU 1720  N   ASP A 583     8401   5669   5408   -485   1038    680       N  
ATOM   1721  CA  ASP A 583      46.708  85.301  11.862  1.00 50.44           C  
ANISOU 1721  CA  ASP A 583     8348   5605   5210   -429    971    642       C  
ATOM   1722  C   ASP A 583      47.043  84.061  12.654  1.00 48.32           C  
ANISOU 1722  C   ASP A 583     7935   5384   5039   -373    990    529       C  
ATOM   1723  O   ASP A 583      47.912  84.128  13.518  1.00 45.38           O  
ANISOU 1723  O   ASP A 583     7432   5022   4788   -381   1054    494       O  
ATOM   1724  CB  ASP A 583      47.029  85.124  10.361  1.00 51.43           C  
ANISOU 1724  CB  ASP A 583     8621   5772   5146   -489   1059    657       C  
ATOM   1725  CG  ASP A 583      48.517  84.878  10.086  1.00 51.77           C  
ANISOU 1725  CG  ASP A 583     8613   5871   5186   -549   1258    600       C  
ATOM   1726  OD1 ASP A 583      49.322  84.655  11.014  1.00 50.73           O  
ANISOU 1726  OD1 ASP A 583     8318   5757   5200   -536   1319    541       O  
ATOM   1727  OD2 ASP A 583      48.891  84.916   8.919  1.00 54.78           O  
ANISOU 1727  OD2 ASP A 583     9115   6283   5416   -611   1355    616       O  
ATOM   1728  N   GLU A 584      46.379  82.942  12.365  1.00 48.90           N  
ANISOU 1728  N   GLU A 584     8034   5484   5059   -322    930    476       N  
ATOM   1729  CA  GLU A 584      46.624  81.698  13.100  1.00 48.19           C  
ANISOU 1729  CA  GLU A 584     7823   5423   5062   -264    940    376       C  
ATOM   1730  C   GLU A 584      48.069  81.197  12.973  1.00 44.84           C  
ANISOU 1730  C   GLU A 584     7326   5046   4665   -281   1110    309       C  
ATOM   1731  O   GLU A 584      48.635  80.741  13.943  1.00 41.92           O  
ANISOU 1731  O   GLU A 584     6811   4688   4426   -243   1130    262       O  
ATOM   1732  CB  GLU A 584      45.663  80.579  12.671  1.00 50.65           C  
ANISOU 1732  CB  GLU A 584     8199   5745   5300   -222    854    330       C  
ATOM   1733  CG  GLU A 584      44.438  80.448  13.554  1.00 53.34           C  
ANISOU 1733  CG  GLU A 584     8490   6055   5719   -169    693    344       C  
ATOM   1734  CD  GLU A 584      43.603  79.221  13.235  1.00 54.53           C  
ANISOU 1734  CD  GLU A 584     8682   6219   5815   -141    618    287       C  
ATOM   1735  OE1 GLU A 584      42.442  79.187  13.690  1.00 58.79           O  
ANISOU 1735  OE1 GLU A 584     9202   6742   6390   -113    482    310       O  
ATOM   1736  OE2 GLU A 584      44.101  78.305  12.534  1.00 55.35           O  
ANISOU 1736  OE2 GLU A 584     8837   6346   5845   -151    700    215       O  
ATOM   1737  N   GLU A 585      48.630  81.287  11.780  1.00 44.05           N  
ANISOU 1737  N   GLU A 585     7325   4975   4437   -336   1228    310       N  
ATOM   1738  CA  GLU A 585      50.025  80.911  11.530  1.00 46.08           C  
ANISOU 1738  CA  GLU A 585     7509   5282   4716   -355   1411    250       C  
ATOM   1739  C   GLU A 585      50.979  81.626  12.487  1.00 43.68           C  
ANISOU 1739  C   GLU A 585     7046   4985   4562   -381   1461    271       C  
ATOM   1740  O   GLU A 585      51.819  80.996  13.106  1.00 41.41           O  
ANISOU 1740  O   GLU A 585     6608   4733   4391   -344   1523    210       O  
ATOM   1741  CB  GLU A 585      50.410  81.188  10.071  1.00 49.48           C  
ANISOU 1741  CB  GLU A 585     8089   5741   4969   -432   1537    265       C  
ATOM   1742  CG  GLU A 585      51.825  80.744   9.668  1.00 54.39           C  
ANISOU 1742  CG  GLU A 585     8639   6422   5602   -450   1749    194       C  
ATOM   1743  CD  GLU A 585      52.249  81.217   8.272  1.00 58.96           C  
ANISOU 1743  CD  GLU A 585     9369   7034   5998   -546   1891    221       C  
ATOM   1744  OE1 GLU A 585      51.516  81.999   7.638  1.00 64.76           O  
ANISOU 1744  OE1 GLU A 585    10267   7741   6597   -604   1818    310       O  
ATOM   1745  OE2 GLU A 585      53.335  80.823   7.788  1.00 60.70           O  
ANISOU 1745  OE2 GLU A 585     9546   7308   6208   -563   2082    157       O  
ATOM   1746  N   GLU A 586      50.828  82.934  12.655  1.00 41.48           N  
ANISOU 1746  N   GLU A 586     6800   4670   4287   -445   1424    359       N  
ATOM   1747  CA  GLU A 586      51.680  83.652  13.588  1.00 40.22           C  
ANISOU 1747  CA  GLU A 586     6502   4514   4265   -487   1460    374       C  
ATOM   1748  C   GLU A 586      51.372  83.274  15.040  1.00 38.77           C  
ANISOU 1748  C   GLU A 586     6183   4316   4228   -417   1343    342       C  
ATOM   1749  O   GLU A 586      52.290  83.127  15.856  1.00 37.38           O  
ANISOU 1749  O   GLU A 586     5849   4178   4174   -419   1383    309       O  
ATOM   1750  CB  GLU A 586      51.559  85.172  13.381  1.00 41.59           C  
ANISOU 1750  CB  GLU A 586     6767   4631   4403   -579   1453    473       C  
ATOM   1751  CG  GLU A 586      52.442  85.981  14.319  1.00 43.28           C  
ANISOU 1751  CG  GLU A 586     6851   4841   4750   -643   1489    483       C  
ATOM   1752  CD  GLU A 586      52.381  87.488  14.070  1.00 46.43           C  
ANISOU 1752  CD  GLU A 586     7356   5166   5116   -743   1496    578       C  
ATOM   1753  OE1 GLU A 586      51.460  87.945  13.368  1.00 45.35           O  
ANISOU 1753  OE1 GLU A 586     7388   4970   4873   -739   1437    647       O  
ATOM   1754  OE2 GLU A 586      53.248  88.218  14.608  1.00 49.03           O  
ANISOU 1754  OE2 GLU A 586     7600   5494   5534   -827   1553    585       O  
ATOM   1755  N   LEU A 587      50.087  83.115  15.366  1.00 36.81           N  
ANISOU 1755  N   LEU A 587     5994   4022   3968   -360   1197    356       N  
ATOM   1756  CA  LEU A 587      49.689  82.720  16.702  1.00 37.41           C  
ANISOU 1756  CA  LEU A 587     5961   4086   4163   -299   1092    328       C  
ATOM   1757  C   LEU A 587      50.263  81.350  17.094  1.00 36.98           C  
ANISOU 1757  C   LEU A 587     5792   4083   4176   -233   1124    248       C  
ATOM   1758  O   LEU A 587      50.760  81.179  18.198  1.00 33.94           O  
ANISOU 1758  O   LEU A 587     5269   3716   3908   -216   1105    228       O  
ATOM   1759  CB  LEU A 587      48.150  82.706  16.840  1.00 37.28           C  
ANISOU 1759  CB  LEU A 587     6030   4019   4114   -250    945    354       C  
ATOM   1760  CG  LEU A 587      47.576  82.104  18.112  1.00 36.79           C  
ANISOU 1760  CG  LEU A 587     5873   3950   4152   -185    842    320       C  
ATOM   1761  CD1 LEU A 587      48.108  82.872  19.306  1.00 36.21           C  
ANISOU 1761  CD1 LEU A 587     5698   3868   4189   -218    838    329       C  
ATOM   1762  CD2 LEU A 587      46.030  82.108  18.122  1.00 37.71           C  
ANISOU 1762  CD2 LEU A 587     6066   4025   4234   -144    711    347       C  
ATOM   1763  N   PHE A 588      50.161  80.391  16.190  1.00 37.32           N  
ANISOU 1763  N   PHE A 588     5899   4141   4138   -197   1169    205       N  
ATOM   1764  CA  PHE A 588      50.657  79.047  16.458  1.00 38.76           C  
ANISOU 1764  CA  PHE A 588     5991   4349   4383   -124   1206    129       C  
ATOM   1765  C   PHE A 588      52.187  79.048  16.603  1.00 38.90           C  
ANISOU 1765  C   PHE A 588     5868   4424   4488   -138   1339    106       C  
ATOM   1766  O   PHE A 588      52.721  78.332  17.453  1.00 36.95           O  
ANISOU 1766  O   PHE A 588     5482   4198   4359    -79   1331     73       O  
ATOM   1767  CB  PHE A 588      50.208  78.069  15.372  1.00 38.64           C  
ANISOU 1767  CB  PHE A 588     6099   4327   4256    -92   1235     78       C  
ATOM   1768  CG  PHE A 588      48.714  77.775  15.365  1.00 38.54           C  
ANISOU 1768  CG  PHE A 588     6188   4270   4182    -70   1088     89       C  
ATOM   1769  CD1 PHE A 588      47.892  78.101  16.425  1.00 39.28           C  
ANISOU 1769  CD1 PHE A 588     6239   4336   4349    -55    953    127       C  
ATOM   1770  CD2 PHE A 588      48.151  77.084  14.287  1.00 42.32           C  
ANISOU 1770  CD2 PHE A 588     6805   4742   4533    -68   1092     51       C  
ATOM   1771  CE1 PHE A 588      46.542  77.779  16.415  1.00 38.84           C  
ANISOU 1771  CE1 PHE A 588     6256   4251   4250    -35    828    134       C  
ATOM   1772  CE2 PHE A 588      46.804  76.760  14.265  1.00 40.63           C  
ANISOU 1772  CE2 PHE A 588     6668   4497   4270    -57    953     58       C  
ATOM   1773  CZ  PHE A 588      45.997  77.110  15.333  1.00 38.68           C  
ANISOU 1773  CZ  PHE A 588     6358   4227   4108    -38    823    103       C  
ATOM   1774  N   HIS A 589      52.874  79.842  15.782  1.00 39.10           N  
ANISOU 1774  N   HIS A 589     5924   4477   4455   -217   1458    129       N  
ATOM   1775  CA  HIS A 589      54.296  80.115  16.003  1.00 39.80           C  
ANISOU 1775  CA  HIS A 589     5859   4626   4636   -254   1577    122       C  
ATOM   1776  C   HIS A 589      54.602  80.677  17.403  1.00 39.51           C  
ANISOU 1776  C   HIS A 589     5678   4598   4736   -275   1491    151       C  
ATOM   1777  O   HIS A 589      55.561  80.243  18.058  1.00 39.48           O  
ANISOU 1777  O   HIS A 589     5500   4646   4851   -248   1521    124       O  
ATOM   1778  CB  HIS A 589      54.816  81.069  14.948  1.00 41.84           C  
ANISOU 1778  CB  HIS A 589     6193   4904   4800   -360   1707    158       C  
ATOM   1779  CG  HIS A 589      56.243  81.462  15.143  1.00 43.52           C  
ANISOU 1779  CG  HIS A 589     6241   5184   5108   -418   1832    155       C  
ATOM   1780  ND1 HIS A 589      56.614  82.616  15.795  1.00 44.24           N  
ANISOU 1780  ND1 HIS A 589     6267   5275   5264   -513   1806    208       N  
ATOM   1781  CD2 HIS A 589      57.393  80.845  14.778  1.00 44.91           C  
ANISOU 1781  CD2 HIS A 589     6297   5431   5334   -398   1986    101       C  
ATOM   1782  CE1 HIS A 589      57.934  82.689  15.826  1.00 45.52           C  
ANISOU 1782  CE1 HIS A 589     6270   5514   5510   -557   1929    191       C  
ATOM   1783  NE2 HIS A 589      58.426  81.626  15.217  1.00 45.38           N  
ANISOU 1783  NE2 HIS A 589     6209   5544   5490   -482   2043    129       N  
ATOM   1784  N   SER A 590      53.801  81.648  17.857  1.00 37.15           N  
ANISOU 1784  N   SER A 590     5450   4246   4416   -324   1385    205       N  
ATOM   1785  CA  SER A 590      53.978  82.213  19.176  1.00 36.92           C  
ANISOU 1785  CA  SER A 590     5314   4217   4495   -353   1301    223       C  
ATOM   1786  C   SER A 590      53.818  81.154  20.276  1.00 37.11           C  
ANISOU 1786  C   SER A 590     5234   4255   4609   -259   1205    187       C  
ATOM   1787  O   SER A 590      54.674  81.026  21.144  1.00 38.28           O  
ANISOU 1787  O   SER A 590     5226   4453   4862   -262   1198    177       O  
ATOM   1788  CB  SER A 590      53.000  83.385  19.374  1.00 37.18           C  
ANISOU 1788  CB  SER A 590     5469   4174   4483   -406   1214    278       C  
ATOM   1789  OG  SER A 590      53.057  83.886  20.689  1.00 37.14           O  
ANISOU 1789  OG  SER A 590     5380   4160   4569   -433   1131    282       O  
ATOM   1790  N   ILE A 591      52.735  80.383  20.211  1.00 35.57           N  
ANISOU 1790  N   ILE A 591     5125   4018   4369   -182   1129    172       N  
ATOM   1791  CA  ILE A 591      52.489  79.299  21.130  1.00 35.91           C  
ANISOU 1791  CA  ILE A 591     5098   4063   4483    -96   1046    144       C  
ATOM   1792  C   ILE A 591      53.672  78.308  21.153  1.00 37.07           C  
ANISOU 1792  C   ILE A 591     5106   4264   4711    -38   1124    105       C  
ATOM   1793  O   ILE A 591      54.104  77.872  22.235  1.00 36.31           O  
ANISOU 1793  O   ILE A 591     4883   4196   4718     -2   1066    105       O  
ATOM   1794  CB  ILE A 591      51.196  78.552  20.771  1.00 35.23           C  
ANISOU 1794  CB  ILE A 591     5137   3924   4324    -35    979    130       C  
ATOM   1795  CG1 ILE A 591      49.973  79.449  21.042  1.00 34.40           C  
ANISOU 1795  CG1 ILE A 591     5128   3770   4173    -71    878    172       C  
ATOM   1796  CG2 ILE A 591      51.087  77.260  21.570  1.00 35.50           C  
ANISOU 1796  CG2 ILE A 591     5104   3954   4430     51    919     99       C  
ATOM   1797  CD1 ILE A 591      48.662  78.939  20.470  1.00 34.30           C  
ANISOU 1797  CD1 ILE A 591     5238   3715   4077    -32    816    167       C  
ATOM   1798  N   ARG A 592      54.194  77.983  19.980  1.00 38.40           N  
ANISOU 1798  N   ARG A 592     5303   4450   4836    -28   1257     75       N  
ATOM   1799  CA  ARG A 592      55.310  77.017  19.899  1.00 40.53           C  
ANISOU 1799  CA  ARG A 592     5440   4765   5194     42   1350     32       C  
ATOM   1800  C   ARG A 592      56.628  77.582  20.389  1.00 42.44           C  
ANISOU 1800  C   ARG A 592     5497   5085   5541     -4   1401     50       C  
ATOM   1801  O   ARG A 592      57.436  76.819  20.889  1.00 42.87           O  
ANISOU 1801  O   ARG A 592     5398   5180   5710     67   1412     34       O  
ATOM   1802  CB  ARG A 592      55.498  76.466  18.488  1.00 40.64           C  
ANISOU 1802  CB  ARG A 592     5540   4774   5127     69   1496    -19       C  
ATOM   1803  CG  ARG A 592      54.384  75.536  18.028  1.00 40.79           C  
ANISOU 1803  CG  ARG A 592     5713   4722   5060    130   1448    -57       C  
ATOM   1804  CD  ARG A 592      54.696  74.885  16.689  1.00 43.00           C  
ANISOU 1804  CD  ARG A 592     6076   5000   5260    156   1600   -124       C  
ATOM   1805  NE  ARG A 592      54.538  75.812  15.571  1.00 45.10           N  
ANISOU 1805  NE  ARG A 592     6473   5281   5379     58   1673   -105       N  
ATOM   1806  CZ  ARG A 592      55.518  76.443  14.931  1.00 48.06           C  
ANISOU 1806  CZ  ARG A 592     6808   5713   5736     -3   1822   -101       C  
ATOM   1807  NH1 ARG A 592      56.797  76.233  15.249  1.00 50.08           N  
ANISOU 1807  NH1 ARG A 592     6878   6027   6123     26   1925   -122       N  
ATOM   1808  NH2 ARG A 592      55.218  77.292  13.945  1.00 47.58           N  
ANISOU 1808  NH2 ARG A 592     6895   5655   5528    -98   1869    -70       N  
ATOM   1809  N   MET A 593      56.860  78.892  20.244  1.00 42.07           N  
ANISOU 1809  N   MET A 593     5462   5059   5463   -124   1430     87       N  
ATOM   1810  CA  MET A 593      58.228  79.428  20.348  1.00 43.62           C  
ANISOU 1810  CA  MET A 593     5489   5337   5745   -191   1519     96       C  
ATOM   1811  C   MET A 593      58.496  80.502  21.400  1.00 44.34           C  
ANISOU 1811  C   MET A 593     5500   5452   5893   -295   1431    138       C  
ATOM   1812  O   MET A 593      59.632  80.638  21.858  1.00 43.07           O  
ANISOU 1812  O   MET A 593     5155   5371   5837   -330   1458    141       O  
ATOM   1813  CB  MET A 593      58.661  80.014  19.002  1.00 44.92           C  
ANISOU 1813  CB  MET A 593     5722   5520   5826   -268   1688     93       C  
ATOM   1814  CG  MET A 593      58.753  79.009  17.865  1.00 47.75           C  
ANISOU 1814  CG  MET A 593     6136   5877   6129   -185   1818     37       C  
ATOM   1815  SD  MET A 593      59.872  77.624  18.210  1.00 50.54           S  
ANISOU 1815  SD  MET A 593     6268   6290   6643    -48   1885    -19       S  
ATOM   1816  CE  MET A 593      61.437  78.489  18.238  1.00 52.51           C  
ANISOU 1816  CE  MET A 593     6302   6655   6994   -152   2008      1       C  
ATOM   1817  N   ASP A 594      57.515  81.319  21.748  1.00 42.09           N  
ANISOU 1817  N   ASP A 594     5346   5101   5543   -351   1334    167       N  
ATOM   1818  CA  ASP A 594      57.849  82.471  22.570  1.00 43.60           C  
ANISOU 1818  CA  ASP A 594     5484   5304   5775   -469   1282    196       C  
ATOM   1819  C   ASP A 594      57.632  82.300  24.076  1.00 41.86           C  
ANISOU 1819  C   ASP A 594     5190   5091   5620   -450   1127    197       C  
ATOM   1820  O   ASP A 594      56.870  81.452  24.522  1.00 40.75           O  
ANISOU 1820  O   ASP A 594     5086   4922   5473   -351   1040    188       O  
ATOM   1821  CB  ASP A 594      57.139  83.703  22.018  1.00 45.87           C  
ANISOU 1821  CB  ASP A 594     5951   5513   5964   -562   1297    229       C  
ATOM   1822  CG  ASP A 594      57.719  84.138  20.648  1.00 47.15           C  
ANISOU 1822  CG  ASP A 594     6157   5688   6066   -628   1462    242       C  
ATOM   1823  OD1 ASP A 594      58.898  83.820  20.299  1.00 46.46           O  
ANISOU 1823  OD1 ASP A 594     5930   5686   6034   -642   1577    223       O  
ATOM   1824  OD2 ASP A 594      56.986  84.795  19.914  1.00 46.00           O  
ANISOU 1824  OD2 ASP A 594     6189   5472   5818   -664   1477    275       O  
ATOM   1825  N   ASN A 595      58.358  83.090  24.852  1.00 42.88           N  
ANISOU 1825  N   ASN A 595     5216   5265   5810   -555   1096    207       N  
ATOM   1826  CA  ASN A 595      58.230  83.068  26.312  1.00 44.82           C  
ANISOU 1826  CA  ASN A 595     5402   5526   6100   -562    949    208       C  
ATOM   1827  C   ASN A 595      57.153  84.064  26.683  1.00 41.95           C  
ANISOU 1827  C   ASN A 595     5204   5070   5664   -625    886    213       C  
ATOM   1828  O   ASN A 595      57.223  85.187  26.243  1.00 42.56           O  
ANISOU 1828  O   ASN A 595     5350   5106   5711   -729    943    224       O  
ATOM   1829  CB  ASN A 595      59.534  83.505  26.957  1.00 47.76           C  
ANISOU 1829  CB  ASN A 595     5588   5995   6563   -662    940    211       C  
ATOM   1830  CG  ASN A 595      60.720  82.801  26.357  1.00 53.38           C  
ANISOU 1830  CG  ASN A 595     6124   6801   7357   -617   1040    209       C  
ATOM   1831  OD1 ASN A 595      60.904  81.603  26.554  1.00 53.72           O  
ANISOU 1831  OD1 ASN A 595     6076   6879   7455   -489   1013    205       O  
ATOM   1832  ND2 ASN A 595      61.503  83.532  25.570  1.00 58.79           N  
ANISOU 1832  ND2 ASN A 595     6767   7518   8053   -719   1168    211       N  
ATOM   1833  N   PRO A 596      56.169  83.660  27.478  1.00 40.60           N  
ANISOU 1833  N   PRO A 596     5096   4859   5469   -561    777    207       N  
ATOM   1834  CA  PRO A 596      55.130  84.611  27.928  1.00 40.79           C  
ANISOU 1834  CA  PRO A 596     5265   4796   5438   -610    722    205       C  
ATOM   1835  C   PRO A 596      55.682  85.817  28.682  1.00 39.88           C  
ANISOU 1835  C   PRO A 596     5122   4683   5345   -754    700    196       C  
ATOM   1836  O   PRO A 596      56.711  85.711  29.368  1.00 39.10           O  
ANISOU 1836  O   PRO A 596     4876   4673   5306   -808    668    189       O  
ATOM   1837  CB  PRO A 596      54.262  83.763  28.844  1.00 39.31           C  
ANISOU 1837  CB  PRO A 596     5094   4600   5240   -521    614    196       C  
ATOM   1838  CG  PRO A 596      54.437  82.367  28.317  1.00 38.95           C  
ANISOU 1838  CG  PRO A 596     4990   4592   5215   -403    636    200       C  
ATOM   1839  CD  PRO A 596      55.843  82.273  27.852  1.00 40.53           C  
ANISOU 1839  CD  PRO A 596     5049   4870   5478   -431    715    202       C  
ATOM   1840  N   PHE A 597      55.017  86.967  28.541  1.00 38.27           N  
ANISOU 1840  N   PHE A 597     5062   4380   5097   -817    716    198       N  
ATOM   1841  CA  PHE A 597      55.463  88.177  29.233  1.00 37.66           C  
ANISOU 1841  CA  PHE A 597     4989   4282   5038   -962    701    180       C  
ATOM   1842  C   PHE A 597      54.873  88.196  30.637  1.00 36.92           C  
ANISOU 1842  C   PHE A 597     4917   4176   4933   -962    590    144       C  
ATOM   1843  O   PHE A 597      53.660  88.090  30.816  1.00 36.05           O  
ANISOU 1843  O   PHE A 597     4917   3997   4782   -884    557    138       O  
ATOM   1844  CB  PHE A 597      55.091  89.458  28.454  1.00 37.15           C  
ANISOU 1844  CB  PHE A 597     5076   4099   4939  -1032    777    199       C  
ATOM   1845  CG  PHE A 597      55.263  90.728  29.236  1.00 37.64           C  
ANISOU 1845  CG  PHE A 597     5185   4100   5013  -1171    757    171       C  
ATOM   1846  CD1 PHE A 597      56.516  91.142  29.637  1.00 39.75           C  
ANISOU 1846  CD1 PHE A 597     5337   4436   5328  -1312    765    154       C  
ATOM   1847  CD2 PHE A 597      54.170  91.528  29.562  1.00 37.63           C  
ANISOU 1847  CD2 PHE A 597     5344   3970   4981  -1164    733    157       C  
ATOM   1848  CE1 PHE A 597      56.681  92.318  30.349  1.00 40.02           C  
ANISOU 1848  CE1 PHE A 597     5427   4407   5369  -1455    746    119       C  
ATOM   1849  CE2 PHE A 597      54.330  92.708  30.253  1.00 37.24           C  
ANISOU 1849  CE2 PHE A 597     5355   3849   4944  -1291    726    121       C  
ATOM   1850  CZ  PHE A 597      55.585  93.097  30.661  1.00 39.75           C  
ANISOU 1850  CZ  PHE A 597     5570   4232   5299  -1443    730     99       C  
ATOM   1851  N   TYR A 598      55.742  88.375  31.625  1.00 37.25           N  
ANISOU 1851  N   TYR A 598     4854   4290   5007  -1059    533    120       N  
ATOM   1852  CA  TYR A 598      55.329  88.507  33.021  1.00 37.61           C  
ANISOU 1852  CA  TYR A 598     4928   4335   5027  -1089    431     81       C  
ATOM   1853  C   TYR A 598      55.695  89.906  33.516  1.00 37.49           C  
ANISOU 1853  C   TYR A 598     4965   4270   5009  -1257    437     41       C  
ATOM   1854  O   TYR A 598      56.864  90.188  33.730  1.00 37.84           O  
ANISOU 1854  O   TYR A 598     4895   4389   5091  -1375    428     36       O  
ATOM   1855  CB  TYR A 598      56.042  87.467  33.899  1.00 38.06           C  
ANISOU 1855  CB  TYR A 598     4825   4525   5110  -1069    336     87       C  
ATOM   1856  CG  TYR A 598      55.790  86.055  33.474  1.00 37.13           C  
ANISOU 1856  CG  TYR A 598     4655   4445   5005   -909    331    123       C  
ATOM   1857  CD1 TYR A 598      56.821  85.264  32.962  1.00 38.81           C  
ANISOU 1857  CD1 TYR A 598     4710   4749   5284   -868    355    154       C  
ATOM   1858  CD2 TYR A 598      54.509  85.518  33.536  1.00 36.31           C  
ANISOU 1858  CD2 TYR A 598     4661   4280   4855   -800    312    123       C  
ATOM   1859  CE1 TYR A 598      56.578  83.963  32.559  1.00 38.60           C  
ANISOU 1859  CE1 TYR A 598     4652   4740   5274   -720    358    179       C  
ATOM   1860  CE2 TYR A 598      54.258  84.228  33.132  1.00 36.61           C  
ANISOU 1860  CE2 TYR A 598     4664   4340   4904   -667    309    151       C  
ATOM   1861  CZ  TYR A 598      55.289  83.457  32.649  1.00 36.46           C  
ANISOU 1861  CZ  TYR A 598     4505   4400   4948   -626    332    177       C  
ATOM   1862  OH  TYR A 598      55.020  82.173  32.246  1.00 36.74           O  
ANISOU 1862  OH  TYR A 598     4523   4440   4997   -492    335    197       O  
ATOM   1863  N   PRO A 599      54.700  90.788  33.689  1.00 37.74           N  
ANISOU 1863  N   PRO A 599     5165   4172   5002  -1269    454     12       N  
ATOM   1864  CA  PRO A 599      54.974  92.143  34.149  1.00 39.78           C  
ANISOU 1864  CA  PRO A 599     5498   4356   5258  -1427    467    -33       C  
ATOM   1865  C   PRO A 599      55.579  92.130  35.533  1.00 40.56           C  
ANISOU 1865  C   PRO A 599     5525   4542   5343  -1532    369    -85       C  
ATOM   1866  O   PRO A 599      55.261  91.251  36.322  1.00 39.21           O  
ANISOU 1866  O   PRO A 599     5315   4440   5141  -1461    288    -91       O  
ATOM   1867  CB  PRO A 599      53.581  92.790  34.271  1.00 40.44           C  
ANISOU 1867  CB  PRO A 599     5769   4288   5306  -1369    489    -60       C  
ATOM   1868  CG  PRO A 599      52.625  91.866  33.637  1.00 38.18           C  
ANISOU 1868  CG  PRO A 599     5500   4000   5008  -1193    496    -16       C  
ATOM   1869  CD  PRO A 599      53.262  90.523  33.523  1.00 37.13           C  
ANISOU 1869  CD  PRO A 599     5209   4011   4888  -1134    458     17       C  
ATOM   1870  N   ARG A 600      56.364  93.148  35.834  1.00 42.29           N  
ANISOU 1870  N   ARG A 600     5745   4745   5575  -1708    375   -121       N  
ATOM   1871  CA  ARG A 600      57.078  93.224  37.090  1.00 45.38           C  
ANISOU 1871  CA  ARG A 600     6063   5230   5947  -1837    274   -171       C  
ATOM   1872  C   ARG A 600      56.142  93.250  38.308  1.00 44.39           C  
ANISOU 1872  C   ARG A 600     6056   5067   5743  -1818    209   -234       C  
ATOM   1873  O   ARG A 600      56.454  92.686  39.346  1.00 44.82           O  
ANISOU 1873  O   ARG A 600     6037   5233   5757  -1847    103   -250       O  
ATOM   1874  CB  ARG A 600      57.967  94.471  37.078  1.00 50.51           C  
ANISOU 1874  CB  ARG A 600     6723   5843   6623  -2046    305   -206       C  
ATOM   1875  CG  ARG A 600      59.022  94.461  38.159  1.00 55.27           C  
ANISOU 1875  CG  ARG A 600     7200   6580   7219  -2201    192   -243       C  
ATOM   1876  CD  ARG A 600      59.395  95.881  38.493  1.00 64.09           C  
ANISOU 1876  CD  ARG A 600     8415   7607   8329  -2414    213   -313       C  
ATOM   1877  NE  ARG A 600      60.284  95.930  39.645  1.00 69.89           N  
ANISOU 1877  NE  ARG A 600     9050   8467   9037  -2577     88   -360       N  
ATOM   1878  CZ  ARG A 600      61.424  96.601  39.681  1.00 75.63           C  
ANISOU 1878  CZ  ARG A 600     9688   9241   9804  -2779     74   -377       C  
ATOM   1879  NH1 ARG A 600      61.820  97.315  38.631  1.00 77.90           N  
ANISOU 1879  NH1 ARG A 600     9984   9453  10161  -2850    192   -352       N  
ATOM   1880  NH2 ARG A 600      62.164  96.577  40.787  1.00 78.72           N  
ANISOU 1880  NH2 ARG A 600     9987   9759  10161  -2923    -60   -418       N  
ATOM   1881  N   TRP A 601      54.989  93.887  38.181  1.00 43.65           N  
ANISOU 1881  N   TRP A 601     6141   4819   5625  -1767    275   -266       N  
ATOM   1882  CA  TRP A 601      54.011  93.899  39.280  1.00 44.64           C  
ANISOU 1882  CA  TRP A 601     6377   4906   5677  -1736    239   -330       C  
ATOM   1883  C   TRP A 601      53.443  92.525  39.656  1.00 42.79           C  
ANISOU 1883  C   TRP A 601     6082   4766   5408  -1590    178   -295       C  
ATOM   1884  O   TRP A 601      52.837  92.384  40.712  1.00 43.97           O  
ANISOU 1884  O   TRP A 601     6295   4923   5487  -1587    136   -343       O  
ATOM   1885  CB  TRP A 601      52.866  94.885  39.005  1.00 43.18           C  
ANISOU 1885  CB  TRP A 601     6383   4529   5493  -1694    334   -369       C  
ATOM   1886  CG  TRP A 601      52.097  94.631  37.779  1.00 41.16           C  
ANISOU 1886  CG  TRP A 601     6153   4204   5281  -1536    404   -299       C  
ATOM   1887  CD1 TRP A 601      52.238  95.261  36.583  1.00 41.13           C  
ANISOU 1887  CD1 TRP A 601     6188   4109   5329  -1539    482   -252       C  
ATOM   1888  CD2 TRP A 601      51.040  93.661  37.608  1.00 39.64           C  
ANISOU 1888  CD2 TRP A 601     5956   4030   5076  -1358    396   -263       C  
ATOM   1889  NE1 TRP A 601      51.335  94.750  35.677  1.00 40.92           N  
ANISOU 1889  NE1 TRP A 601     6182   4048   5315  -1372    515   -190       N  
ATOM   1890  CE2 TRP A 601      50.582  93.777  36.287  1.00 38.35           C  
ANISOU 1890  CE2 TRP A 601     5827   3787   4955  -1262    463   -200       C  
ATOM   1891  CE3 TRP A 601      50.432  92.731  38.454  1.00 38.71           C  
ANISOU 1891  CE3 TRP A 601     5812   3986   4908  -1283    338   -278       C  
ATOM   1892  CZ2 TRP A 601      49.557  92.987  35.782  1.00 37.56           C  
ANISOU 1892  CZ2 TRP A 601     5729   3686   4854  -1098    467   -156       C  
ATOM   1893  CZ3 TRP A 601      49.398  91.931  37.948  1.00 36.94           C  
ANISOU 1893  CZ3 TRP A 601     5590   3755   4691  -1119    352   -233       C  
ATOM   1894  CH2 TRP A 601      48.984  92.066  36.624  1.00 37.28           C  
ANISOU 1894  CH2 TRP A 601     5659   3723   4780  -1031    412   -175       C  
ATOM   1895  N   LEU A 602      53.643  91.504  38.836  1.00 41.59           N  
ANISOU 1895  N   LEU A 602     5816   4686   5300  -1477    176   -214       N  
ATOM   1896  CA  LEU A 602      52.959  90.229  39.060  1.00 41.56           C  
ANISOU 1896  CA  LEU A 602     5779   4739   5270  -1332    133   -178       C  
ATOM   1897  C   LEU A 602      53.530  89.503  40.276  1.00 42.88           C  
ANISOU 1897  C   LEU A 602     5859   5041   5389  -1379     12   -180       C  
ATOM   1898  O   LEU A 602      54.717  89.399  40.396  1.00 43.34           O  
ANISOU 1898  O   LEU A 602     5792   5198   5475  -1460    -43   -161       O  
ATOM   1899  CB  LEU A 602      53.066  89.313  37.839  1.00 41.32           C  
ANISOU 1899  CB  LEU A 602     5661   4739   5299  -1205    166    -99       C  
ATOM   1900  CG  LEU A 602      52.349  87.960  37.933  1.00 39.87           C  
ANISOU 1900  CG  LEU A 602     5452   4597   5097  -1056    128    -61       C  
ATOM   1901  CD1 LEU A 602      50.848  88.151  38.108  1.00 39.38           C  
ANISOU 1901  CD1 LEU A 602     5529   4436   4994   -985    163    -90       C  
ATOM   1902  CD2 LEU A 602      52.631  87.115  36.707  1.00 40.60           C  
ANISOU 1902  CD2 LEU A 602     5461   4717   5246   -952    165      2       C  
ATOM   1903  N   GLU A 603      52.657  89.013  41.158  1.00 43.24           N  
ANISOU 1903  N   GLU A 603     5970   5093   5364  -1328    -25   -198       N  
ATOM   1904  CA  GLU A 603      53.046  88.285  42.383  1.00 45.97           C  
ANISOU 1904  CA  GLU A 603     6260   5561   5643  -1367   -145   -190       C  
ATOM   1905  C   GLU A 603      53.965  87.114  42.007  1.00 44.55           C  
ANISOU 1905  C   GLU A 603     5903   5499   5524  -1302   -212   -100       C  
ATOM   1906  O   GLU A 603      53.685  86.393  41.059  1.00 41.27           O  
ANISOU 1906  O   GLU A 603     5450   5063   5167  -1169   -165    -48       O  
ATOM   1907  CB  GLU A 603      51.757  87.820  43.104  1.00 50.21           C  
ANISOU 1907  CB  GLU A 603     6905   6068   6101  -1292   -142   -209       C  
ATOM   1908  CG  GLU A 603      51.847  86.618  44.054  1.00 55.02           C  
ANISOU 1908  CG  GLU A 603     7463   6793   6648  -1266   -251   -161       C  
ATOM   1909  CD  GLU A 603      52.867  86.830  45.150  1.00 59.01           C  
ANISOU 1909  CD  GLU A 603     7927   7404   7087  -1414   -367   -177       C  
ATOM   1910  OE1 GLU A 603      52.877  87.953  45.703  1.00 64.87           O  
ANISOU 1910  OE1 GLU A 603     8764   8109   7773  -1547   -350   -266       O  
ATOM   1911  OE2 GLU A 603      53.653  85.893  45.433  1.00 58.15           O  
ANISOU 1911  OE2 GLU A 603     7695   7412   6987  -1398   -477   -102       O  
ATOM   1912  N   LYS A 604      55.070  86.938  42.730  1.00 46.21           N  
ANISOU 1912  N   LYS A 604     6003   5830   5724  -1395   -323    -84       N  
ATOM   1913  CA  LYS A 604      56.083  85.964  42.332  1.00 46.68           C  
ANISOU 1913  CA  LYS A 604     5874   5996   5864  -1334   -380      0       C  
ATOM   1914  C   LYS A 604      55.560  84.526  42.311  1.00 44.71           C  
ANISOU 1914  C   LYS A 604     5603   5766   5619  -1167   -409     68       C  
ATOM   1915  O   LYS A 604      55.947  83.746  41.458  1.00 43.42           O  
ANISOU 1915  O   LYS A 604     5333   5621   5543  -1060   -386    125       O  
ATOM   1916  CB  LYS A 604      57.342  86.065  43.203  1.00 51.22           C  
ANISOU 1916  CB  LYS A 604     6324   6706   6430  -1465   -511      9       C  
ATOM   1917  CG  LYS A 604      57.138  85.756  44.673  1.00 55.46           C  
ANISOU 1917  CG  LYS A 604     6916   7309   6847  -1518   -640      5       C  
ATOM   1918  CD  LYS A 604      58.457  85.835  45.438  1.00 61.83           C  
ANISOU 1918  CD  LYS A 604     7581   8261   7648  -1648   -787     25       C  
ATOM   1919  CE  LYS A 604      58.288  85.416  46.892  1.00 66.68           C  
ANISOU 1919  CE  LYS A 604     8253   8953   8127  -1698   -929     37       C  
ATOM   1920  NZ  LYS A 604      57.329  86.297  47.626  1.00 69.36           N  
ANISOU 1920  NZ  LYS A 604     8811   9211   8330  -1798   -884    -66       N  
ATOM   1921  N   GLU A 605      54.675  84.170  43.234  1.00 43.51           N  
ANISOU 1921  N   GLU A 605     5558   5602   5371  -1150   -451     60       N  
ATOM   1922  CA  GLU A 605      54.135  82.824  43.244  1.00 44.16           C  
ANISOU 1922  CA  GLU A 605     5632   5690   5454  -1008   -475    127       C  
ATOM   1923  C   GLU A 605      53.183  82.599  42.070  1.00 40.69           C  
ANISOU 1923  C   GLU A 605     5252   5144   5064   -885   -353    125       C  
ATOM   1924  O   GLU A 605      53.124  81.491  41.571  1.00 39.94           O  
ANISOU 1924  O   GLU A 605     5105   5050   5017   -763   -354    183       O  
ATOM   1925  CB  GLU A 605      53.461  82.470  44.580  1.00 46.16           C  
ANISOU 1925  CB  GLU A 605     5986   5968   5585  -1036   -549    126       C  
ATOM   1926  CG  GLU A 605      54.380  82.549  45.803  1.00 50.13           C  
ANISOU 1926  CG  GLU A 605     6439   6590   6018  -1157   -693    140       C  
ATOM   1927  CD  GLU A 605      55.660  81.682  45.723  1.00 53.56           C  
ANISOU 1927  CD  GLU A 605     6682   7134   6535  -1114   -804    236       C  
ATOM   1928  OE1 GLU A 605      55.802  80.798  44.820  1.00 51.87           O  
ANISOU 1928  OE1 GLU A 605     6380   6901   6428   -972   -770    296       O  
ATOM   1929  OE2 GLU A 605      56.548  81.901  46.595  1.00 59.27           O  
ANISOU 1929  OE2 GLU A 605     7340   7964   7215  -1226   -930    248       O  
ATOM   1930  N   ALA A 606      52.470  83.640  41.626  1.00 37.89           N  
ANISOU 1930  N   ALA A 606     5006   4693   4697   -917   -255     59       N  
ATOM   1931  CA  ALA A 606      51.632  83.541  40.429  1.00 36.55           C  
ANISOU 1931  CA  ALA A 606     4884   4429   4572   -810   -151     62       C  
ATOM   1932  C   ALA A 606      52.491  83.348  39.169  1.00 35.93           C  
ANISOU 1932  C   ALA A 606     4699   4362   4588   -766   -107     97       C  
ATOM   1933  O   ALA A 606      52.223  82.457  38.354  1.00 35.86           O  
ANISOU 1933  O   ALA A 606     4669   4335   4619   -649    -75    135       O  
ATOM   1934  CB  ALA A 606      50.750  84.777  40.288  1.00 36.34           C  
ANISOU 1934  CB  ALA A 606     4990   4298   4517   -854    -67     -7       C  
ATOM   1935  N   LYS A 607      53.525  84.173  39.015  1.00 38.26           N  
ANISOU 1935  N   LYS A 607     4930   4688   4916   -867   -100     81       N  
ATOM   1936  CA  LYS A 607      54.501  83.971  37.935  1.00 39.22           C  
ANISOU 1936  CA  LYS A 607     4930   4843   5126   -840    -54    115       C  
ATOM   1937  C   LYS A 607      55.062  82.539  37.933  1.00 38.92           C  
ANISOU 1937  C   LYS A 607     4764   4885   5139   -734   -110    178       C  
ATOM   1938  O   LYS A 607      55.114  81.884  36.893  1.00 37.62           O  
ANISOU 1938  O   LYS A 607     4562   4701   5028   -632    -45    204       O  
ATOM   1939  CB  LYS A 607      55.666  84.952  38.061  1.00 41.31           C  
ANISOU 1939  CB  LYS A 607     5117   5158   5419   -987    -60     94       C  
ATOM   1940  CG  LYS A 607      56.809  84.642  37.104  1.00 43.95           C  
ANISOU 1940  CG  LYS A 607     5295   5554   5850   -966    -15    132       C  
ATOM   1941  CD  LYS A 607      57.874  85.739  37.068  1.00 48.06           C  
ANISOU 1941  CD  LYS A 607     5744   6112   6403  -1126      0    108       C  
ATOM   1942  CE  LYS A 607      58.946  85.385  36.046  1.00 49.90           C  
ANISOU 1942  CE  LYS A 607     5814   6410   6735  -1097     68    145       C  
ATOM   1943  NZ  LYS A 607      60.105  86.309  36.113  1.00 55.13           N  
ANISOU 1943  NZ  LYS A 607     6370   7134   7441  -1262     72    130       N  
ATOM   1944  N   ASP A 608      55.464  82.066  39.114  1.00 40.86           N  
ANISOU 1944  N   ASP A 608     4950   5212   5360   -760   -230    203       N  
ATOM   1945  CA  ASP A 608      56.091  80.745  39.249  1.00 41.53           C  
ANISOU 1945  CA  ASP A 608     4907   5368   5502   -659   -299    272       C  
ATOM   1946  C   ASP A 608      55.147  79.623  38.813  1.00 38.77           C  
ANISOU 1946  C   ASP A 608     4627   4949   5152   -512   -266    299       C  
ATOM   1947  O   ASP A 608      55.551  78.675  38.143  1.00 38.63           O  
ANISOU 1947  O   ASP A 608     4528   4937   5211   -401   -243    337       O  
ATOM   1948  CB  ASP A 608      56.517  80.496  40.694  1.00 43.44           C  
ANISOU 1948  CB  ASP A 608     5106   5703   5697   -718   -449    303       C  
ATOM   1949  CG  ASP A 608      57.324  79.237  40.824  1.00 44.90           C  
ANISOU 1949  CG  ASP A 608     5142   5961   5957   -615   -529    386       C  
ATOM   1950  OD1 ASP A 608      58.492  79.260  40.423  1.00 46.65           O  
ANISOU 1950  OD1 ASP A 608     5197   6252   6273   -618   -531    406       O  
ATOM   1951  OD2 ASP A 608      56.770  78.213  41.257  1.00 42.71           O  
ANISOU 1951  OD2 ASP A 608     4913   5662   5653   -524   -580    433       O  
ATOM   1952  N   LEU A 609      53.885  79.732  39.184  1.00 37.46           N  
ANISOU 1952  N   LEU A 609     4611   4716   4904   -513   -259    274       N  
ATOM   1953  CA  LEU A 609      52.915  78.711  38.782  1.00 36.09           C  
ANISOU 1953  CA  LEU A 609     4507   4477   4729   -393   -230    295       C  
ATOM   1954  C   LEU A 609      52.792  78.703  37.265  1.00 35.24           C  
ANISOU 1954  C   LEU A 609     4404   4310   4675   -326   -116    278       C  
ATOM   1955  O   LEU A 609      52.801  77.649  36.642  1.00 36.46           O  
ANISOU 1955  O   LEU A 609     4533   4444   4876   -219    -95    306       O  
ATOM   1956  CB  LEU A 609      51.559  78.971  39.410  1.00 35.58           C  
ANISOU 1956  CB  LEU A 609     4587   4358   4571   -420   -229    264       C  
ATOM   1957  CG  LEU A 609      50.430  78.058  38.945  1.00 33.92           C  
ANISOU 1957  CG  LEU A 609     4451   4077   4357   -318   -193    278       C  
ATOM   1958  CD1 LEU A 609      50.784  76.601  39.149  1.00 36.22           C  
ANISOU 1958  CD1 LEU A 609     4686   4390   4685   -231   -254    345       C  
ATOM   1959  CD2 LEU A 609      49.184  78.357  39.720  1.00 35.15           C  
ANISOU 1959  CD2 LEU A 609     4724   4201   4429   -357   -193    249       C  
ATOM   1960  N   LEU A 610      52.657  79.892  36.691  1.00 34.91           N  
ANISOU 1960  N   LEU A 610     4409   4232   4621   -393    -42    233       N  
ATOM   1961  CA  LEU A 610      52.539  80.046  35.247  1.00 34.63           C  
ANISOU 1961  CA  LEU A 610     4396   4144   4617   -349     63    221       C  
ATOM   1962  C   LEU A 610      53.771  79.480  34.540  1.00 35.48           C  
ANISOU 1962  C   LEU A 610     4368   4305   4806   -304     96    245       C  
ATOM   1963  O   LEU A 610      53.613  78.734  33.594  1.00 37.46           O  
ANISOU 1963  O   LEU A 610     4628   4524   5081   -211    154    251       O  
ATOM   1964  CB  LEU A 610      52.239  81.502  34.866  1.00 34.18           C  
ANISOU 1964  CB  LEU A 610     4419   4036   4529   -438    126    180       C  
ATOM   1965  CG  LEU A 610      50.859  82.070  35.292  1.00 34.53           C  
ANISOU 1965  CG  LEU A 610     4603   4005   4508   -452    123    150       C  
ATOM   1966  CD1 LEU A 610      50.766  83.583  35.049  1.00 35.30           C  
ANISOU 1966  CD1 LEU A 610     4772   4047   4593   -542    178    114       C  
ATOM   1967  CD2 LEU A 610      49.696  81.366  34.588  1.00 33.23           C  
ANISOU 1967  CD2 LEU A 610     4512   3781   4330   -348    152    160       C  
ATOM   1968  N   VAL A 611      54.974  79.757  35.045  1.00 38.57           N  
ANISOU 1968  N   VAL A 611     4629   4782   5241   -367     55    258       N  
ATOM   1969  CA  VAL A 611      56.208  79.200  34.452  1.00 40.05           C  
ANISOU 1969  CA  VAL A 611     4660   5033   5524   -318     90    282       C  
ATOM   1970  C   VAL A 611      56.148  77.663  34.432  1.00 40.64           C  
ANISOU 1970  C   VAL A 611     4699   5099   5640   -172     62    319       C  
ATOM   1971  O   VAL A 611      56.522  77.018  33.446  1.00 39.37           O  
ANISOU 1971  O   VAL A 611     4492   4927   5538    -83    144    319       O  
ATOM   1972  CB  VAL A 611      57.494  79.727  35.165  1.00 43.05           C  
ANISOU 1972  CB  VAL A 611     4884   5521   5951   -418     27    295       C  
ATOM   1973  CG1 VAL A 611      58.759  78.943  34.768  1.00 44.83           C  
ANISOU 1973  CG1 VAL A 611     4914   5825   6292   -344     44    330       C  
ATOM   1974  CG2 VAL A 611      57.711  81.215  34.865  1.00 43.52           C  
ANISOU 1974  CG2 VAL A 611     4974   5573   5989   -563     87    254       C  
ATOM   1975  N   LYS A 612      55.606  77.077  35.491  1.00 40.19           N  
ANISOU 1975  N   LYS A 612     4685   5039   5547   -149    -43    347       N  
ATOM   1976  CA  LYS A 612      55.532  75.623  35.579  1.00 41.20           C  
ANISOU 1976  CA  LYS A 612     4794   5144   5714    -19    -77    390       C  
ATOM   1977  C   LYS A 612      54.439  74.991  34.751  1.00 38.79           C  
ANISOU 1977  C   LYS A 612     4619   4737   5382     60     -7    368       C  
ATOM   1978  O   LYS A 612      54.502  73.787  34.476  1.00 37.55           O  
ANISOU 1978  O   LYS A 612     4447   4545   5274    172     -2    390       O  
ATOM   1979  CB  LYS A 612      55.390  75.197  37.023  1.00 43.87           C  
ANISOU 1979  CB  LYS A 612     5135   5515   6016    -33   -218    439       C  
ATOM   1980  CG  LYS A 612      56.686  75.376  37.784  1.00 46.15           C  
ANISOU 1980  CG  LYS A 612     5261   5917   6354    -77   -310    480       C  
ATOM   1981  CD  LYS A 612      56.470  75.057  39.251  1.00 48.85           C  
ANISOU 1981  CD  LYS A 612     5633   6296   6630   -110   -457    531       C  
ATOM   1982  CE  LYS A 612      57.797  74.813  39.962  1.00 51.07           C  
ANISOU 1982  CE  LYS A 612     5736   6691   6976   -113   -574    595       C  
ATOM   1983  NZ  LYS A 612      58.311  76.070  40.534  1.00 53.03           N  
ANISOU 1983  NZ  LYS A 612     5942   7026   7179   -275   -622    564       N  
ATOM   1984  N   LEU A 613      53.426  75.780  34.377  1.00 35.77           N  
ANISOU 1984  N   LEU A 613     4364   4303   4924      4     39    325       N  
ATOM   1985  CA  LEU A 613      52.366  75.292  33.491  1.00 33.80           C  
ANISOU 1985  CA  LEU A 613     4232   3965   4643     65    100    302       C  
ATOM   1986  C   LEU A 613      52.809  75.457  32.033  1.00 33.40           C  
ANISOU 1986  C   LEU A 613     4168   3901   4620     91    218    271       C  
ATOM   1987  O   LEU A 613      52.465  74.651  31.181  1.00 33.64           O  
ANISOU 1987  O   LEU A 613     4248   3879   4654    168    270    257       O  
ATOM   1988  CB  LEU A 613      51.068  76.076  33.722  1.00 33.24           C  
ANISOU 1988  CB  LEU A 613     4291   3852   4487      1     93    277       C  
ATOM   1989  CG  LEU A 613      50.385  75.795  35.067  1.00 32.60           C  
ANISOU 1989  CG  LEU A 613     4250   3774   4361    -20      0    299       C  
ATOM   1990  CD1 LEU A 613      49.313  76.840  35.346  1.00 32.63           C  
ANISOU 1990  CD1 LEU A 613     4354   3749   4295    -92     10    264       C  
ATOM   1991  CD2 LEU A 613      49.798  74.393  35.074  1.00 33.47           C  
ANISOU 1991  CD2 LEU A 613     4399   3837   4479     65    -22    325       C  
ATOM   1992  N   PHE A 614      53.591  76.492  31.737  1.00 33.31           N  
ANISOU 1992  N   PHE A 614     4095   3937   4622     18    265    259       N  
ATOM   1993  CA  PHE A 614      53.994  76.738  30.355  1.00 34.81           C  
ANISOU 1993  CA  PHE A 614     4285   4119   4823     26    387    233       C  
ATOM   1994  C   PHE A 614      55.297  76.004  30.027  1.00 37.26           C  
ANISOU 1994  C   PHE A 614     4445   4481   5229     93    434    241       C  
ATOM   1995  O   PHE A 614      56.171  76.548  29.392  1.00 41.07           O  
ANISOU 1995  O   PHE A 614     4853   5008   5743     55    519    230       O  
ATOM   1996  CB  PHE A 614      54.102  78.245  30.057  1.00 34.63           C  
ANISOU 1996  CB  PHE A 614     4288   4103   4763    -90    433    219       C  
ATOM   1997  CG  PHE A 614      52.761  78.954  29.997  1.00 33.23           C  
ANISOU 1997  CG  PHE A 614     4269   3854   4502   -128    419    207       C  
ATOM   1998  CD1 PHE A 614      51.713  78.436  29.241  1.00 32.25           C  
ANISOU 1998  CD1 PHE A 614     4258   3666   4330    -64    441    198       C  
ATOM   1999  CD2 PHE A 614      52.553  80.131  30.699  1.00 33.89           C  
ANISOU 1999  CD2 PHE A 614     4383   3933   4559   -226    383    203       C  
ATOM   2000  CE1 PHE A 614      50.484  79.087  29.196  1.00 31.90           C  
ANISOU 2000  CE1 PHE A 614     4335   3562   4222    -90    421    193       C  
ATOM   2001  CE2 PHE A 614      51.336  80.799  30.637  1.00 33.20           C  
ANISOU 2001  CE2 PHE A 614     4429   3774   4410   -245    378    192       C  
ATOM   2002  CZ  PHE A 614      50.305  80.276  29.884  1.00 31.42           C  
ANISOU 2002  CZ  PHE A 614     4296   3494   4147   -173    394    191       C  
ATOM   2003  N   VAL A 615      55.387  74.747  30.429  1.00 38.09           N  
ANISOU 2003  N   VAL A 615     4511   4576   5385    196    387    262       N  
ATOM   2004  CA  VAL A 615      56.488  73.883  30.043  1.00 38.65           C  
ANISOU 2004  CA  VAL A 615     4449   4676   5559    292    440    267       C  
ATOM   2005  C   VAL A 615      56.038  73.127  28.803  1.00 37.60           C  
ANISOU 2005  C   VAL A 615     4416   4463   5405    374    547    223       C  
ATOM   2006  O   VAL A 615      54.954  72.529  28.790  1.00 34.32           O  
ANISOU 2006  O   VAL A 615     4133   3969   4936    408    513    215       O  
ATOM   2007  CB  VAL A 615      56.855  72.962  31.220  1.00 41.25           C  
ANISOU 2007  CB  VAL A 615     4688   5026   5959    362    319    323       C  
ATOM   2008  CG1 VAL A 615      57.857  71.873  30.786  1.00 42.77           C  
ANISOU 2008  CG1 VAL A 615     4754   5223   6274    496    375    330       C  
ATOM   2009  CG2 VAL A 615      57.465  73.828  32.332  1.00 41.12           C  
ANISOU 2009  CG2 VAL A 615     4565   5108   5951    260    219    360       C  
ATOM   2010  N   ARG A 616      56.833  73.179  27.742  1.00 37.51           N  
ANISOU 2010  N   ARG A 616     4347   4475   5428    395    680    189       N  
ATOM   2011  CA  ARG A 616      56.383  72.628  26.466  1.00 39.58           C  
ANISOU 2011  CA  ARG A 616     4727   4666   5641    448    792    135       C  
ATOM   2012  C   ARG A 616      56.438  71.093  26.384  1.00 41.37           C  
ANISOU 2012  C   ARG A 616     4956   4829   5934    590    802    121       C  
ATOM   2013  O   ARG A 616      55.566  70.488  25.754  1.00 40.98           O  
ANISOU 2013  O   ARG A 616     5055   4693   5820    621    828     82       O  
ATOM   2014  CB  ARG A 616      57.105  73.290  25.288  1.00 40.42           C  
ANISOU 2014  CB  ARG A 616     4804   4816   5734    405    946     99       C  
ATOM   2015  CG  ARG A 616      56.750  74.788  25.183  1.00 40.82           C  
ANISOU 2015  CG  ARG A 616     4918   4892   5698    262    941    112       C  
ATOM   2016  CD  ARG A 616      56.999  75.368  23.795  1.00 41.34           C  
ANISOU 2016  CD  ARG A 616     5039   4965   5700    212   1094     79       C  
ATOM   2017  NE  ARG A 616      56.321  76.654  23.684  1.00 40.64           N  
ANISOU 2017  NE  ARG A 616     5061   4862   5516     94   1068     99       N  
ATOM   2018  CZ  ARG A 616      56.823  77.814  24.090  1.00 41.64           C  
ANISOU 2018  CZ  ARG A 616     5123   5036   5660    -13   1059    127       C  
ATOM   2019  NH1 ARG A 616      58.043  77.880  24.635  1.00 44.17           N  
ANISOU 2019  NH1 ARG A 616     5255   5439   6088    -29   1068    138       N  
ATOM   2020  NH2 ARG A 616      56.115  78.923  23.951  1.00 41.03           N  
ANISOU 2020  NH2 ARG A 616     5168   4922   5500   -106   1038    144       N  
ATOM   2021  N   GLU A 617      57.435  70.486  27.015  1.00 42.45           N  
ANISOU 2021  N   GLU A 617     4930   5000   6196    671    775    154       N  
ATOM   2022  CA  GLU A 617      57.472  69.027  27.206  1.00 45.71           C  
ANISOU 2022  CA  GLU A 617     5343   5337   6688    812    757    159       C  
ATOM   2023  C   GLU A 617      56.342  68.576  28.156  1.00 42.08           C  
ANISOU 2023  C   GLU A 617     4998   4809   6178    804    612    200       C  
ATOM   2024  O   GLU A 617      56.376  68.865  29.363  1.00 40.37           O  
ANISOU 2024  O   GLU A 617     4723   4641   5974    766    484    266       O  
ATOM   2025  CB  GLU A 617      58.821  68.575  27.771  1.00 49.01           C  
ANISOU 2025  CB  GLU A 617     5544   5814   7263    905    742    203       C  
ATOM   2026  CG  GLU A 617      58.832  67.105  28.222  1.00 55.93           C  
ANISOU 2026  CG  GLU A 617     6421   6599   8229   1055    691    231       C  
ATOM   2027  CD  GLU A 617      58.255  66.107  27.191  1.00 59.63           C  
ANISOU 2027  CD  GLU A 617     7047   6934   8673   1136    800    156       C  
ATOM   2028  OE1 GLU A 617      58.732  66.112  26.015  1.00 59.55           O  
ANISOU 2028  OE1 GLU A 617     7028   6925   8671   1165    964     80       O  
ATOM   2029  OE2 GLU A 617      57.332  65.303  27.563  1.00 58.78           O  
ANISOU 2029  OE2 GLU A 617     7076   6721   8535   1164    724    169       O  
ATOM   2030  N   PRO A 618      55.342  67.870  27.617  1.00 41.22           N  
ANISOU 2030  N   PRO A 618     5056   4595   6008    831    635    160       N  
ATOM   2031  CA  PRO A 618      54.144  67.640  28.450  1.00 40.95           C  
ANISOU 2031  CA  PRO A 618     5136   4510   5912    791    510    195       C  
ATOM   2032  C   PRO A 618      54.380  66.812  29.697  1.00 40.74           C  
ANISOU 2032  C   PRO A 618     5049   4464   5964    857    395    271       C  
ATOM   2033  O   PRO A 618      53.716  67.024  30.711  1.00 37.23           O  
ANISOU 2033  O   PRO A 618     4643   4030   5470    795    281    321       O  
ATOM   2034  CB  PRO A 618      53.180  66.897  27.525  1.00 41.23           C  
ANISOU 2034  CB  PRO A 618     5341   4436   5885    812    566    133       C  
ATOM   2035  CG  PRO A 618      53.876  66.702  26.232  1.00 44.20           C  
ANISOU 2035  CG  PRO A 618     5707   4802   6282    865    718     61       C  
ATOM   2036  CD  PRO A 618      55.177  67.430  26.224  1.00 41.83           C  
ANISOU 2036  CD  PRO A 618     5234   4608   6051    867    773     76       C  
ATOM   2037  N   GLU A 619      55.308  65.869  29.633  1.00 43.08           N  
ANISOU 2037  N   GLU A 619     5256   4730   6380    984    426    283       N  
ATOM   2038  CA  GLU A 619      55.577  65.042  30.806  1.00 47.75           C  
ANISOU 2038  CA  GLU A 619     5794   5298   7050   1056    307    371       C  
ATOM   2039  C   GLU A 619      56.282  65.813  31.924  1.00 46.93           C  
ANISOU 2039  C   GLU A 619     5539   5322   6969   1005    197    448       C  
ATOM   2040  O   GLU A 619      56.370  65.334  33.040  1.00 48.71           O  
ANISOU 2040  O   GLU A 619     5736   5547   7224   1032     72    533       O  
ATOM   2041  CB  GLU A 619      56.323  63.752  30.411  1.00 52.88           C  
ANISOU 2041  CB  GLU A 619     6398   5859   7834   1224    369    367       C  
ATOM   2042  CG  GLU A 619      55.435  62.784  29.611  1.00 57.45           C  
ANISOU 2042  CG  GLU A 619     7164   6286   8379   1262    440    299       C  
ATOM   2043  CD  GLU A 619      54.171  62.330  30.382  1.00 62.57           C  
ANISOU 2043  CD  GLU A 619     7963   6857   8951   1205    327    343       C  
ATOM   2044  OE1 GLU A 619      54.274  62.042  31.595  1.00 69.78           O  
ANISOU 2044  OE1 GLU A 619     8835   7778   9898   1220    202    442       O  
ATOM   2045  OE2 GLU A 619      53.066  62.245  29.793  1.00 63.28           O  
ANISOU 2045  OE2 GLU A 619     8212   6883   8947   1140    360    282       O  
ATOM   2046  N   LYS A 620      56.763  67.024  31.639  1.00 45.62           N  
ANISOU 2046  N   LYS A 620     5288   5264   6780    920    239    420       N  
ATOM   2047  CA  LYS A 620      57.404  67.839  32.657  1.00 44.98           C  
ANISOU 2047  CA  LYS A 620     5075   5305   6710    847    135    480       C  
ATOM   2048  C   LYS A 620      56.508  68.957  33.141  1.00 42.15           C  
ANISOU 2048  C   LYS A 620     4814   4983   6218    693     81    471       C  
ATOM   2049  O   LYS A 620      56.954  69.799  33.909  1.00 42.14           O  
ANISOU 2049  O   LYS A 620     4727   5079   6203    607      6    501       O  
ATOM   2050  CB  LYS A 620      58.706  68.434  32.123  1.00 48.11           C  
ANISOU 2050  CB  LYS A 620     5285   5801   7191    850    215    460       C  
ATOM   2051  CG  LYS A 620      59.762  67.384  31.796  1.00 52.29           C  
ANISOU 2051  CG  LYS A 620     5676   6314   7878   1015    266    475       C  
ATOM   2052  CD  LYS A 620      60.892  68.000  30.986  1.00 56.06           C  
ANISOU 2052  CD  LYS A 620     5987   6884   8430   1009    391    433       C  
ATOM   2053  CE  LYS A 620      62.083  68.348  31.851  1.00 60.09           C  
ANISOU 2053  CE  LYS A 620     6263   7528   9040    998    294    504       C  
ATOM   2054  NZ  LYS A 620      62.955  67.149  31.998  1.00 64.40           N  
ANISOU 2054  NZ  LYS A 620     6662   8053   9751   1182    282    552       N  
ATOM   2055  N   ARG A 621      55.250  68.964  32.708  1.00 41.14           N  
ANISOU 2055  N   ARG A 621     4859   4775   5994    657    116    427       N  
ATOM   2056  CA  ARG A 621      54.331  70.066  33.022  1.00 39.58           C  
ANISOU 2056  CA  ARG A 621     4756   4602   5681    524     87    409       C  
ATOM   2057  C   ARG A 621      53.598  69.834  34.344  1.00 39.98           C  
ANISOU 2057  C   ARG A 621     4870   4645   5676    487    -40    463       C  
ATOM   2058  O   ARG A 621      53.119  68.738  34.620  1.00 39.93           O  
ANISOU 2058  O   ARG A 621     4928   4564   5678    551    -76    494       O  
ATOM   2059  CB  ARG A 621      53.323  70.234  31.869  1.00 38.12           C  
ANISOU 2059  CB  ARG A 621     4713   4346   5425    505    183    340       C  
ATOM   2060  CG  ARG A 621      52.369  71.417  31.979  1.00 37.58           C  
ANISOU 2060  CG  ARG A 621     4734   4291   5252    388    171    318       C  
ATOM   2061  CD  ARG A 621      51.494  71.553  30.736  1.00 35.95           C  
ANISOU 2061  CD  ARG A 621     4649   4024   4985    381    257    261       C  
ATOM   2062  NE  ARG A 621      52.313  71.565  29.516  1.00 36.51           N  
ANISOU 2062  NE  ARG A 621     4679   4102   5090    418    372    223       N  
ATOM   2063  CZ  ARG A 621      51.967  71.071  28.336  1.00 35.91           C  
ANISOU 2063  CZ  ARG A 621     4688   3968   4987    458    455    176       C  
ATOM   2064  NH1 ARG A 621      50.784  70.496  28.136  1.00 36.62           N  
ANISOU 2064  NH1 ARG A 621     4906   3984   5022    465    430    160       N  
ATOM   2065  NH2 ARG A 621      52.834  71.130  27.342  1.00 37.92           N  
ANISOU 2065  NH2 ARG A 621     4896   4241   5268    485    568    142       N  
ATOM   2066  N   LEU A 622      53.500  70.870  35.164  1.00 39.93           N  
ANISOU 2066  N   LEU A 622     4855   4709   5607    377   -101    472       N  
ATOM   2067  CA  LEU A 622      52.826  70.754  36.443  1.00 38.89           C  
ANISOU 2067  CA  LEU A 622     4789   4582   5406    328   -208    517       C  
ATOM   2068  C   LEU A 622      51.352  70.441  36.138  1.00 37.56           C  
ANISOU 2068  C   LEU A 622     4777   4322   5170    322   -172    487       C  
ATOM   2069  O   LEU A 622      50.771  70.955  35.170  1.00 34.09           O  
ANISOU 2069  O   LEU A 622     4398   3852   4703    301    -87    425       O  
ATOM   2070  CB  LEU A 622      52.941  72.068  37.205  1.00 41.72           C  
ANISOU 2070  CB  LEU A 622     5127   5026   5700    200   -253    506       C  
ATOM   2071  CG  LEU A 622      53.102  72.192  38.733  1.00 44.62           C  
ANISOU 2071  CG  LEU A 622     5478   5460   6013    133   -383    560       C  
ATOM   2072  CD1 LEU A 622      52.155  73.256  39.241  1.00 44.23           C  
ANISOU 2072  CD1 LEU A 622     5535   5416   5851     13   -378    513       C  
ATOM   2073  CD2 LEU A 622      52.993  70.942  39.587  1.00 43.98           C  
ANISOU 2073  CD2 LEU A 622     5418   5356   5933    195   -477    643       C  
ATOM   2074  N   GLY A 623      50.752  69.574  36.943  1.00 38.46           N  
ANISOU 2074  N   GLY A 623     4956   4397   5259    337   -240    535       N  
ATOM   2075  CA  GLY A 623      49.423  69.043  36.629  1.00 37.19           C  
ANISOU 2075  CA  GLY A 623     4927   4149   5055    338   -208    513       C  
ATOM   2076  C   GLY A 623      49.548  67.659  36.024  1.00 39.50           C  
ANISOU 2076  C   GLY A 623     5239   4349   5418    446   -184    528       C  
ATOM   2077  O   GLY A 623      48.736  66.782  36.321  1.00 41.34           O  
ANISOU 2077  O   GLY A 623     5562   4510   5633    454   -208    552       O  
ATOM   2078  N   VAL A 624      50.535  67.474  35.156  1.00 39.36           N  
ANISOU 2078  N   VAL A 624     5142   4327   5483    525   -127    507       N  
ATOM   2079  CA  VAL A 624      50.929  66.166  34.689  1.00 42.31           C  
ANISOU 2079  CA  VAL A 624     5516   4613   5943    643   -103    519       C  
ATOM   2080  C   VAL A 624      51.891  65.562  35.701  1.00 43.88           C  
ANISOU 2080  C   VAL A 624     5622   4836   6213    707   -197    612       C  
ATOM   2081  O   VAL A 624      51.737  64.412  36.068  1.00 46.43           O  
ANISOU 2081  O   VAL A 624     5994   5075   6571    772   -238    665       O  
ATOM   2082  CB  VAL A 624      51.626  66.223  33.308  1.00 43.79           C  
ANISOU 2082  CB  VAL A 624     5656   4791   6190    707     14    451       C  
ATOM   2083  CG1 VAL A 624      52.102  64.843  32.881  1.00 45.55           C  
ANISOU 2083  CG1 VAL A 624     5880   4915   6512    840     49    456       C  
ATOM   2084  CG2 VAL A 624      50.671  66.821  32.277  1.00 44.26           C  
ANISOU 2084  CG2 VAL A 624     5819   4831   6167    641     94    370       C  
ATOM   2085  N   ARG A 625      52.881  66.348  36.110  1.00 46.60           N  
ANISOU 2085  N   ARG A 625     5831   5292   6580    685   -234    635       N  
ATOM   2086  CA AARG A 625      53.907  65.972  37.097  0.50 49.30           C  
ANISOU 2086  CA AARG A 625     6056   5688   6987    735   -343    729       C  
ATOM   2087  CA BARG A 625      53.856  65.911  37.112  0.50 48.90           C  
ANISOU 2087  CA BARG A 625     6012   5630   6934    737   -344    731       C  
ATOM   2088  C   ARG A 625      53.605  66.698  38.398  1.00 47.91           C  
ANISOU 2088  C   ARG A 625     5897   5599   6707    613   -455    774       C  
ATOM   2089  O   ARG A 625      52.848  67.678  38.397  1.00 46.17           O  
ANISOU 2089  O   ARG A 625     5744   5408   6388    501   -425    717       O  
ATOM   2090  CB AARG A 625      55.298  66.428  36.624  0.50 51.77           C  
ANISOU 2090  CB AARG A 625     6185   6085   7398    779   -307    716       C  
ATOM   2091  CB BARG A 625      55.288  66.090  36.573  0.50 50.96           C  
ANISOU 2091  CB BARG A 625     6092   5955   7314    811   -305    724       C  
ATOM   2092  CG AARG A 625      56.295  65.330  36.310  0.50 55.66           C  
ANISOU 2092  CG AARG A 625     6573   6534   8041    942   -294    754       C  
ATOM   2093  CG BARG A 625      56.248  66.879  37.455  0.50 53.65           C  
ANISOU 2093  CG BARG A 625     6282   6437   7662    752   -405    774       C  
ATOM   2094  CD AARG A 625      57.732  65.863  36.357  0.50 58.98           C  
ANISOU 2094  CD AARG A 625     6774   7079   8556    962   -308    774       C  
ATOM   2095  CD BARG A 625      57.379  67.477  36.640  0.50 55.84           C  
ANISOU 2095  CD BARG A 625     6395   6791   8030    771   -322    730       C  
ATOM   2096  NE AARG A 625      57.792  67.325  36.486  0.50 58.82           N  
ANISOU 2096  NE AARG A 625     6715   7176   8455    810   -311    735       N  
ATOM   2097  NE BARG A 625      57.469  68.926  36.823  0.50 56.76           N  
ANISOU 2097  NE BARG A 625     6478   7013   8072    621   -328    692       N  
ATOM   2098  CZ AARG A 625      58.870  68.067  36.230  0.50 59.69           C  
ANISOU 2098  CZ AARG A 625     6655   7394   8627    784   -284    719       C  
ATOM   2099  CZ BARG A 625      57.087  69.569  37.923  0.50 56.33           C  
ANISOU 2099  CZ BARG A 625     6469   7016   7916    502   -435    719       C  
ATOM   2100  NH1AARG A 625      58.827  69.382  36.389  0.50 58.88           N  
ANISOU 2100  NH1AARG A 625     6545   7378   8446    634   -288    684       N  
ATOM   2101  NH1BARG A 625      57.189  70.890  37.992  0.50 54.72           N  
ANISOU 2101  NH1BARG A 625     6246   6890   7655    369   -425    673       N  
ATOM   2102  NH2AARG A 625      59.991  67.500  35.813  0.50 62.52           N  
ANISOU 2102  NH2AARG A 625     6849   7772   9134    907   -246    738       N  
ATOM   2103  NH2BARG A 625      56.610  68.889  38.957  0.50 57.42           N  
ANISOU 2103  NH2BARG A 625     6681   7127   8006    513   -548    790       N  
ATOM   2104  N   GLY A 626      54.220  66.242  39.489  1.00 45.91           N  
ANISOU 2104  N   GLY A 626     5584   5386   6474    638   -582    874       N  
ATOM   2105  CA  GLY A 626      54.134  66.905  40.789  1.00 48.18           C  
ANISOU 2105  CA  GLY A 626     5880   5770   6655    521   -698    919       C  
ATOM   2106  C   GLY A 626      52.730  67.011  41.366  1.00 46.88           C  
ANISOU 2106  C   GLY A 626     5888   5568   6355    424   -700    907       C  
ATOM   2107  O   GLY A 626      51.854  66.236  41.025  1.00 46.96           O  
ANISOU 2107  O   GLY A 626     6008   5472   6362    460   -652    902       O  
ATOM   2108  N   ASP A 627      52.526  67.958  42.272  1.00 46.33           N  
ANISOU 2108  N   ASP A 627     5839   5588   6174    296   -754    901       N  
ATOM   2109  CA  ASP A 627      51.219  68.124  42.902  1.00 43.27           C  
ANISOU 2109  CA  ASP A 627     5603   5178   5658    202   -747    886       C  
ATOM   2110  C   ASP A 627      50.837  69.598  42.872  1.00 39.43           C  
ANISOU 2110  C   ASP A 627     5133   4751   5094     83   -693    791       C  
ATOM   2111  O   ASP A 627      51.251  70.388  43.710  1.00 37.32           O  
ANISOU 2111  O   ASP A 627     4840   4578   4762     -6   -758    793       O  
ATOM   2112  CB  ASP A 627      51.222  67.586  44.342  1.00 45.88           C  
ANISOU 2112  CB  ASP A 627     5981   5542   5908    165   -876    990       C  
ATOM   2113  CG  ASP A 627      49.831  67.609  44.965  1.00 46.34           C  
ANISOU 2113  CG  ASP A 627     6196   5571   5838     74   -847    976       C  
ATOM   2114  OD1 ASP A 627      48.891  68.250  44.398  1.00 46.47           O  
ANISOU 2114  OD1 ASP A 627     6268   5561   5827     28   -739    881       O  
ATOM   2115  OD2 ASP A 627      49.689  67.005  46.027  1.00 47.03           O  
ANISOU 2115  OD2 ASP A 627     6347   5666   5854     47   -933   1065       O  
ATOM   2116  N   ILE A 628      50.033  69.959  41.885  1.00 37.79           N  
ANISOU 2116  N   ILE A 628     4977   4485   4895     85   -577    709       N  
ATOM   2117  CA  ILE A 628      49.646  71.342  41.695  1.00 36.74           C  
ANISOU 2117  CA  ILE A 628     4863   4385   4709     -6   -516    622       C  
ATOM   2118  C   ILE A 628      48.925  71.939  42.913  1.00 35.42           C  
ANISOU 2118  C   ILE A 628     4783   4259   4415   -120   -548    612       C  
ATOM   2119  O   ILE A 628      49.088  73.120  43.211  1.00 35.66           O  
ANISOU 2119  O   ILE A 628     4807   4344   4399   -207   -542    560       O  
ATOM   2120  CB  ILE A 628      48.830  71.505  40.386  1.00 35.47           C  
ANISOU 2120  CB  ILE A 628     4749   4147   4580     27   -397    552       C  
ATOM   2121  CG1 ILE A 628      48.615  72.983  40.073  1.00 35.07           C  
ANISOU 2121  CG1 ILE A 628     4706   4123   4496    -50   -337    473       C  
ATOM   2122  CG2 ILE A 628      47.501  70.783  40.472  1.00 33.84           C  
ANISOU 2122  CG2 ILE A 628     4653   3869   4335     34   -375    557       C  
ATOM   2123  CD1 ILE A 628      48.098  73.229  38.672  1.00 35.23           C  
ANISOU 2123  CD1 ILE A 628     4751   4080   4553    -11   -236    418       C  
ATOM   2124  N   ARG A 629      48.168  71.127  43.643  1.00 36.00           N  
ANISOU 2124  N   ARG A 629     4942   4305   4430   -125   -578    661       N  
ATOM   2125  CA  ARG A 629      47.506  71.593  44.863  1.00 36.58           C  
ANISOU 2125  CA  ARG A 629     5102   4423   4373   -234   -600    654       C  
ATOM   2126  C   ARG A 629      48.490  72.112  45.929  1.00 39.78           C  
ANISOU 2126  C   ARG A 629     5468   4933   4713   -310   -704    681       C  
ATOM   2127  O   ARG A 629      48.128  72.976  46.736  1.00 40.43           O  
ANISOU 2127  O   ARG A 629     5613   5062   4686   -419   -699    633       O  
ATOM   2128  CB  ARG A 629      46.651  70.481  45.485  1.00 36.26           C  
ANISOU 2128  CB  ARG A 629     5154   4340   4281   -229   -616    719       C  
ATOM   2129  CG  ARG A 629      45.495  70.033  44.640  1.00 36.08           C  
ANISOU 2129  CG  ARG A 629     5183   4226   4299   -189   -521    685       C  
ATOM   2130  CD  ARG A 629      44.645  69.033  45.408  1.00 36.97           C  
ANISOU 2130  CD  ARG A 629     5390   4305   4351   -215   -535    749       C  
ATOM   2131  NE  ARG A 629      43.638  68.456  44.534  1.00 36.04           N  
ANISOU 2131  NE  ARG A 629     5307   4099   4287   -178   -458    724       N  
ATOM   2132  CZ  ARG A 629      42.572  67.774  44.952  1.00 37.77           C  
ANISOU 2132  CZ  ARG A 629     5607   4281   4462   -217   -432    750       C  
ATOM   2133  NH1 ARG A 629      42.349  67.588  46.252  1.00 38.63           N  
ANISOU 2133  NH1 ARG A 629     5780   4431   4464   -294   -469    805       N  
ATOM   2134  NH2 ARG A 629      41.699  67.300  44.058  1.00 36.93           N  
ANISOU 2134  NH2 ARG A 629     5519   4099   4412   -191   -369    720       N  
ATOM   2135  N   GLN A 630      49.725  71.615  45.910  1.00 41.57           N  
ANISOU 2135  N   GLN A 630     5590   5196   5007   -255   -796    751       N  
ATOM   2136  CA  GLN A 630      50.762  72.051  46.865  1.00 44.73           C  
ANISOU 2136  CA  GLN A 630     5932   5707   5356   -328   -917    785       C  
ATOM   2137  C   GLN A 630      51.558  73.268  46.404  1.00 43.83           C  
ANISOU 2137  C   GLN A 630     5723   5647   5282   -379   -896    710       C  
ATOM   2138  O   GLN A 630      52.465  73.706  47.096  1.00 44.38           O  
ANISOU 2138  O   GLN A 630     5731   5813   5318   -451   -996    729       O  
ATOM   2139  CB  GLN A 630      51.724  70.900  47.184  1.00 48.55           C  
ANISOU 2139  CB  GLN A 630     6334   6213   5899   -243  -1043    912       C  
ATOM   2140  CG  GLN A 630      51.016  69.746  47.886  1.00 54.45           C  
ANISOU 2140  CG  GLN A 630     7193   6910   6584   -218  -1084   1002       C  
ATOM   2141  CD  GLN A 630      51.953  68.632  48.323  1.00 61.76           C  
ANISOU 2141  CD  GLN A 630     8052   7849   7562   -132  -1223   1142       C  
ATOM   2142  OE1 GLN A 630      53.179  68.733  48.206  1.00 67.51           O  
ANISOU 2142  OE1 GLN A 630     8635   8641   8372    -92  -1301   1174       O  
ATOM   2143  NE2 GLN A 630      51.374  67.554  48.826  1.00 66.55           N  
ANISOU 2143  NE2 GLN A 630     8763   8393   8130   -103  -1253   1230       N  
ATOM   2144  N   HIS A 631      51.224  73.843  45.263  1.00 40.34           N  
ANISOU 2144  N   HIS A 631     5273   5146   4905   -354   -773    629       N  
ATOM   2145  CA  HIS A 631      51.912  75.071  44.852  1.00 40.66           C  
ANISOU 2145  CA  HIS A 631     5245   5229   4976   -420   -744    560       C  
ATOM   2146  C   HIS A 631      51.634  76.207  45.838  1.00 41.46           C  
ANISOU 2146  C   HIS A 631     5426   5375   4949   -569   -760    497       C  
ATOM   2147  O   HIS A 631      50.471  76.387  46.258  1.00 39.98           O  
ANISOU 2147  O   HIS A 631     5370   5147   4673   -604   -707    458       O  
ATOM   2148  CB  HIS A 631      51.527  75.518  43.426  1.00 39.23           C  
ANISOU 2148  CB  HIS A 631     5063   4969   4874   -371   -606    491       C  
ATOM   2149  CG  HIS A 631      52.500  76.500  42.857  1.00 39.39           C  
ANISOU 2149  CG  HIS A 631     4986   5029   4952   -417   -582    449       C  
ATOM   2150  ND1 HIS A 631      52.436  77.850  43.128  1.00 38.40           N  
ANISOU 2150  ND1 HIS A 631     4903   4917   4769   -540   -556    375       N  
ATOM   2151  CD2 HIS A 631      53.623  76.317  42.117  1.00 40.94           C  
ANISOU 2151  CD2 HIS A 631     5040   5256   5258   -367   -580    473       C  
ATOM   2152  CE1 HIS A 631      53.462  78.459  42.556  1.00 40.79           C  
ANISOU 2152  CE1 HIS A 631     5099   5256   5143   -572   -542    359       C  
ATOM   2153  NE2 HIS A 631      54.191  77.555  41.925  1.00 40.18           N  
ANISOU 2153  NE2 HIS A 631     4902   5195   5166   -468   -553    417       N  
ATOM   2154  N   PRO A 632      52.682  76.982  46.199  1.00 41.88           N  
ANISOU 2154  N   PRO A 632     5402   5512   4995   -662   -827    481       N  
ATOM   2155  CA  PRO A 632      52.542  78.071  47.182  1.00 43.37           C  
ANISOU 2155  CA  PRO A 632     5675   5744   5057   -817   -849    412       C  
ATOM   2156  C   PRO A 632      51.491  79.131  46.874  1.00 40.98           C  
ANISOU 2156  C   PRO A 632     5493   5356   4718   -862   -712    301       C  
ATOM   2157  O   PRO A 632      50.968  79.731  47.789  1.00 40.01           O  
ANISOU 2157  O   PRO A 632     5482   5243   4477   -961   -708    245       O  
ATOM   2158  CB  PRO A 632      53.948  78.692  47.232  1.00 44.64           C  
ANISOU 2158  CB  PRO A 632     5704   5995   5259   -896   -929    410       C  
ATOM   2159  CG  PRO A 632      54.871  77.588  46.840  1.00 45.92           C  
ANISOU 2159  CG  PRO A 632     5709   6200   5536   -780  -1004    516       C  
ATOM   2160  CD  PRO A 632      54.103  76.765  45.837  1.00 44.28           C  
ANISOU 2160  CD  PRO A 632     5531   5886   5406   -630   -898    532       C  
ATOM   2161  N   LEU A 633      51.160  79.365  45.612  1.00 41.30           N  
ANISOU 2161  N   LEU A 633     5518   5315   4857   -789   -600    269       N  
ATOM   2162  CA  LEU A 633      50.034  80.248  45.302  1.00 40.03           C  
ANISOU 2162  CA  LEU A 633     5472   5065   4671   -807   -477    181       C  
ATOM   2163  C   LEU A 633      48.789  79.847  46.089  1.00 39.65           C  
ANISOU 2163  C   LEU A 633     5542   4994   4527   -802   -455    174       C  
ATOM   2164  O   LEU A 633      47.992  80.705  46.448  1.00 41.38           O  
ANISOU 2164  O   LEU A 633     5861   5174   4686   -858   -384     94       O  
ATOM   2165  CB  LEU A 633      49.680  80.212  43.799  1.00 39.06           C  
ANISOU 2165  CB  LEU A 633     5324   4859   4659   -702   -375    176       C  
ATOM   2166  CG  LEU A 633      48.647  81.258  43.357  1.00 39.52           C  
ANISOU 2166  CG  LEU A 633     5481   4824   4709   -715   -259     94       C  
ATOM   2167  CD1 LEU A 633      49.167  82.673  43.631  1.00 41.00           C  
ANISOU 2167  CD1 LEU A 633     5693   5010   4875   -836   -245     22       C  
ATOM   2168  CD2 LEU A 633      48.295  81.109  41.886  1.00 40.72           C  
ANISOU 2168  CD2 LEU A 633     5611   4904   4954   -613   -180    105       C  
ATOM   2169  N   PHE A 634      48.616  78.543  46.305  1.00 37.85           N  
ANISOU 2169  N   PHE A 634     5301   4783   4296   -731   -506    258       N  
ATOM   2170  CA  PHE A 634      47.421  77.993  46.924  1.00 38.71           C  
ANISOU 2170  CA  PHE A 634     5511   4869   4327   -722   -476    266       C  
ATOM   2171  C   PHE A 634      47.600  77.666  48.406  1.00 41.19           C  
ANISOU 2171  C   PHE A 634     5880   5264   4505   -809   -571    303       C  
ATOM   2172  O   PHE A 634      46.758  77.007  48.984  1.00 41.19           O  
ANISOU 2172  O   PHE A 634     5956   5257   4437   -804   -558    332       O  
ATOM   2173  CB  PHE A 634      46.983  76.728  46.174  1.00 37.61           C  
ANISOU 2173  CB  PHE A 634     5344   4679   4264   -598   -461    335       C  
ATOM   2174  CG  PHE A 634      46.706  76.954  44.703  1.00 36.44           C  
ANISOU 2174  CG  PHE A 634     5159   4456   4229   -517   -371    302       C  
ATOM   2175  CD1 PHE A 634      45.706  77.824  44.292  1.00 35.80           C  
ANISOU 2175  CD1 PHE A 634     5137   4315   4148   -525   -267    224       C  
ATOM   2176  CD2 PHE A 634      47.431  76.290  43.736  1.00 35.72           C  
ANISOU 2176  CD2 PHE A 634     4978   4351   4241   -429   -390    349       C  
ATOM   2177  CE1 PHE A 634      45.438  78.031  42.936  1.00 34.36           C  
ANISOU 2177  CE1 PHE A 634     4929   4068   4056   -454   -198    204       C  
ATOM   2178  CE2 PHE A 634      47.177  76.502  42.391  1.00 33.86           C  
ANISOU 2178  CE2 PHE A 634     4725   4053   4088   -366   -307    318       C  
ATOM   2179  CZ  PHE A 634      46.185  77.371  41.986  1.00 32.25           C  
ANISOU 2179  CZ  PHE A 634     4585   3796   3873   -381   -218    250       C  
ATOM   2180  N   ARG A 635      48.666  78.167  49.027  1.00 44.64           N  
ANISOU 2180  N   ARG A 635     6283   5782   4896   -899   -665    300       N  
ATOM   2181  CA  ARG A 635      49.008  77.766  50.390  1.00 47.65           C  
ANISOU 2181  CA  ARG A 635     6707   6253   5142   -982   -784    353       C  
ATOM   2182  C   ARG A 635      47.916  78.075  51.416  1.00 48.67           C  
ANISOU 2182  C   ARG A 635     6993   6382   5117  -1067   -723    296       C  
ATOM   2183  O   ARG A 635      47.828  77.401  52.422  1.00 53.27           O  
ANISOU 2183  O   ARG A 635     7637   7019   5584  -1107   -795    360       O  
ATOM   2184  CB  ARG A 635      50.338  78.398  50.825  1.00 52.08           C  
ANISOU 2184  CB  ARG A 635     7199   6909   5680  -1080   -900    348       C  
ATOM   2185  CG  ARG A 635      50.280  79.910  50.938  1.00 54.29           C  
ANISOU 2185  CG  ARG A 635     7536   7174   5915  -1199   -832    215       C  
ATOM   2186  CD  ARG A 635      51.615  80.507  51.356  1.00 60.98           C  
ANISOU 2186  CD  ARG A 635     8309   8116   6741  -1314   -953    208       C  
ATOM   2187  NE  ARG A 635      51.630  81.917  50.983  1.00 66.66           N  
ANISOU 2187  NE  ARG A 635     9059   8784   7481  -1396   -863     84       N  
ATOM   2188  CZ  ARG A 635      52.429  82.470  50.071  1.00 76.11           C  
ANISOU 2188  CZ  ARG A 635    10147   9969   8802  -1396   -850     68       C  
ATOM   2189  NH1 ARG A 635      53.365  81.764  49.433  1.00 81.02           N  
ANISOU 2189  NH1 ARG A 635    10603  10639   9541  -1318   -920    160       N  
ATOM   2190  NH2 ARG A 635      52.321  83.768  49.821  1.00 79.89           N  
ANISOU 2190  NH2 ARG A 635    10683  10384   9285  -1479   -762    -42       N  
ATOM   2191  N   GLU A 636      47.081  79.075  51.165  1.00 49.38           N  
ANISOU 2191  N   GLU A 636     7150   6406   5205  -1091   -587    180       N  
ATOM   2192  CA  GLU A 636      45.992  79.403  52.081  1.00 51.58           C  
ANISOU 2192  CA  GLU A 636     7568   6679   5351  -1161   -503    113       C  
ATOM   2193  C   GLU A 636      44.734  78.567  51.829  1.00 51.35           C  
ANISOU 2193  C   GLU A 636     7568   6595   5347  -1074   -413    145       C  
ATOM   2194  O   GLU A 636      43.785  78.696  52.582  1.00 52.58           O  
ANISOU 2194  O   GLU A 636     7825   6751   5400  -1124   -334    100       O  
ATOM   2195  CB  GLU A 636      45.593  80.880  51.986  1.00 55.71           C  
ANISOU 2195  CB  GLU A 636     8152   7147   5869  -1217   -387    -31       C  
ATOM   2196  CG  GLU A 636      46.742  81.882  51.855  1.00 61.02           C  
ANISOU 2196  CG  GLU A 636     8784   7838   6561  -1296   -444    -81       C  
ATOM   2197  CD  GLU A 636      47.308  82.349  53.172  1.00 66.70           C  
ANISOU 2197  CD  GLU A 636     9582   8644   7114  -1457   -525   -122       C  
ATOM   2198  OE1 GLU A 636      47.711  83.539  53.240  1.00 74.86           O  
ANISOU 2198  OE1 GLU A 636    10647   9659   8135  -1551   -506   -222       O  
ATOM   2199  OE2 GLU A 636      47.368  81.543  54.127  1.00 69.36           O  
ANISOU 2199  OE2 GLU A 636     9958   9064   7329  -1496   -612    -53       O  
ATOM   2200  N   ILE A 637      44.717  77.729  50.788  1.00 46.60           N  
ANISOU 2200  N   ILE A 637     6880   5947   4878   -953   -419    217       N  
ATOM   2201  CA  ILE A 637      43.528  76.969  50.424  1.00 45.05           C  
ANISOU 2201  CA  ILE A 637     6704   5693   4719   -880   -337    241       C  
ATOM   2202  C   ILE A 637      43.467  75.630  51.155  1.00 45.28           C  
ANISOU 2202  C   ILE A 637     6767   5758   4678   -884   -411    355       C  
ATOM   2203  O   ILE A 637      44.396  74.815  51.084  1.00 46.62           O  
ANISOU 2203  O   ILE A 637     6880   5950   4880   -846   -529    454       O  
ATOM   2204  CB  ILE A 637      43.498  76.668  48.902  1.00 44.91           C  
ANISOU 2204  CB  ILE A 637     6592   5601   4869   -756   -308    259       C  
ATOM   2205  CG1 ILE A 637      43.589  77.955  48.072  1.00 45.49           C  
ANISOU 2205  CG1 ILE A 637     6635   5631   5016   -746   -239    165       C  
ATOM   2206  CG2 ILE A 637      42.263  75.835  48.527  1.00 43.49           C  
ANISOU 2206  CG2 ILE A 637     6431   5367   4726   -694   -236    284       C  
ATOM   2207  CD1 ILE A 637      42.287  78.704  47.914  1.00 46.94           C  
ANISOU 2207  CD1 ILE A 637     6873   5757   5205   -740   -105     77       C  
ATOM   2208  N   ASN A 638      42.375  75.396  51.867  1.00 45.54           N  
ANISOU 2208  N   ASN A 638     6890   5792   4618   -929   -337    344       N  
ATOM   2209  CA  ASN A 638      42.076  74.068  52.338  1.00 45.49           C  
ANISOU 2209  CA  ASN A 638     6922   5792   4567   -923   -378    455       C  
ATOM   2210  C   ASN A 638      41.194  73.445  51.272  1.00 42.00           C  
ANISOU 2210  C   ASN A 638     6436   5265   4255   -827   -300    465       C  
ATOM   2211  O   ASN A 638      40.060  73.895  51.066  1.00 41.90           O  
ANISOU 2211  O   ASN A 638     6439   5222   4257   -831   -174    388       O  
ATOM   2212  CB  ASN A 638      41.380  74.079  53.699  1.00 47.65           C  
ANISOU 2212  CB  ASN A 638     7321   6121   4662  -1038   -335    444       C  
ATOM   2213  CG  ASN A 638      41.063  72.681  54.178  1.00 48.49           C  
ANISOU 2213  CG  ASN A 638     7478   6226   4720  -1041   -376    571       C  
ATOM   2214  OD1 ASN A 638      40.404  71.907  53.489  1.00 47.87           O  
ANISOU 2214  OD1 ASN A 638     7369   6078   4740   -972   -329    607       O  
ATOM   2215  ND2 ASN A 638      41.568  72.336  55.340  1.00 54.08           N  
ANISOU 2215  ND2 ASN A 638     8265   7006   5276  -1124   -472    645       N  
ATOM   2216  N   TRP A 639      41.720  72.440  50.577  1.00 40.23           N  
ANISOU 2216  N   TRP A 639     6154   5000   4130   -741   -375    554       N  
ATOM   2217  CA  TRP A 639      41.068  71.910  49.358  1.00 40.29           C  
ANISOU 2217  CA  TRP A 639     6114   4923   4272   -649   -314    552       C  
ATOM   2218  C   TRP A 639      39.757  71.159  49.652  1.00 40.42           C  
ANISOU 2218  C   TRP A 639     6190   4910   4256   -677   -241    574       C  
ATOM   2219  O   TRP A 639      38.817  71.163  48.834  1.00 36.90           O  
ANISOU 2219  O   TRP A 639     5715   4414   3891   -640   -155    529       O  
ATOM   2220  CB  TRP A 639      42.037  71.019  48.572  1.00 39.34           C  
ANISOU 2220  CB  TRP A 639     5926   4761   4259   -552   -405    632       C  
ATOM   2221  CG  TRP A 639      43.195  71.820  48.032  1.00 39.31           C  
ANISOU 2221  CG  TRP A 639     5839   4783   4314   -520   -448    596       C  
ATOM   2222  CD1 TRP A 639      44.379  72.086  48.662  1.00 39.58           C  
ANISOU 2222  CD1 TRP A 639     5845   4888   4304   -553   -550    628       C  
ATOM   2223  CD2 TRP A 639      43.264  72.470  46.752  1.00 36.41           C  
ANISOU 2223  CD2 TRP A 639     5402   4376   4056   -459   -390    526       C  
ATOM   2224  NE1 TRP A 639      45.183  72.861  47.844  1.00 38.38           N  
ANISOU 2224  NE1 TRP A 639     5603   4741   4236   -520   -550    578       N  
ATOM   2225  CE2 TRP A 639      44.509  73.137  46.686  1.00 36.79           C  
ANISOU 2225  CE2 TRP A 639     5384   4470   4122   -465   -448    515       C  
ATOM   2226  CE3 TRP A 639      42.378  72.578  45.669  1.00 34.55           C  
ANISOU 2226  CE3 TRP A 639     5155   4074   3896   -409   -298    473       C  
ATOM   2227  CZ2 TRP A 639      44.911  73.866  45.557  1.00 36.76           C  
ANISOU 2227  CZ2 TRP A 639     5311   4443   4211   -422   -406    458       C  
ATOM   2228  CZ3 TRP A 639      42.768  73.313  44.558  1.00 34.35           C  
ANISOU 2228  CZ3 TRP A 639     5070   4027   3955   -363   -266    420       C  
ATOM   2229  CH2 TRP A 639      44.026  73.944  44.506  1.00 34.92           C  
ANISOU 2229  CH2 TRP A 639     5084   4141   4043   -370   -314    413       C  
ATOM   2230  N   GLU A 640      39.701  70.547  50.832  1.00 43.26           N  
ANISOU 2230  N   GLU A 640     6632   5307   4494   -751   -277    646       N  
ATOM   2231  CA  GLU A 640      38.523  69.816  51.286  1.00 45.68           C  
ANISOU 2231  CA  GLU A 640     7004   5597   4753   -801   -206    677       C  
ATOM   2232  C   GLU A 640      37.379  70.785  51.562  1.00 43.16           C  
ANISOU 2232  C   GLU A 640     6699   5309   4389   -860    -63    565       C  
ATOM   2233  O   GLU A 640      36.260  70.578  51.111  1.00 41.91           O  
ANISOU 2233  O   GLU A 640     6517   5116   4290   -850     30    537       O  
ATOM   2234  CB  GLU A 640      38.854  69.026  52.560  1.00 51.03           C  
ANISOU 2234  CB  GLU A 640     7780   6314   5292   -876   -283    789       C  
ATOM   2235  CG  GLU A 640      39.840  67.880  52.335  1.00 55.86           C  
ANISOU 2235  CG  GLU A 640     8381   6879   5962   -805   -421    919       C  
ATOM   2236  CD  GLU A 640      41.249  68.334  51.933  1.00 58.36           C  
ANISOU 2236  CD  GLU A 640     8614   7219   6338   -736   -528    918       C  
ATOM   2237  OE1 GLU A 640      41.827  69.276  52.566  1.00 59.71           O  
ANISOU 2237  OE1 GLU A 640     8788   7476   6420   -794   -564    877       O  
ATOM   2238  OE2 GLU A 640      41.779  67.744  50.960  1.00 60.32           O  
ANISOU 2238  OE2 GLU A 640     8793   7399   6724   -628   -571    953       O  
ATOM   2239  N   GLU A 641      37.686  71.864  52.272  1.00 42.99           N  
ANISOU 2239  N   GLU A 641     6709   5351   4272   -917    -48    495       N  
ATOM   2240  CA  GLU A 641      36.716  72.945  52.469  1.00 43.59           C  
ANISOU 2240  CA  GLU A 641     6793   5445   4323   -954     94    372       C  
ATOM   2241  C   GLU A 641      36.273  73.555  51.140  1.00 39.96           C  
ANISOU 2241  C   GLU A 641     6234   4923   4024   -858    155    298       C  
ATOM   2242  O   GLU A 641      35.085  73.815  50.922  1.00 38.64           O  
ANISOU 2242  O   GLU A 641     6041   4742   3899   -850    272    240       O  
ATOM   2243  CB  GLU A 641      37.301  74.032  53.382  1.00 45.72           C  
ANISOU 2243  CB  GLU A 641     7125   5777   4467  -1030     90    302       C  
ATOM   2244  CG  GLU A 641      37.381  73.599  54.836  1.00 49.82           C  
ANISOU 2244  CG  GLU A 641     7763   6372   4794  -1147     64    354       C  
ATOM   2245  CD  GLU A 641      37.922  74.685  55.756  1.00 53.82           C  
ANISOU 2245  CD  GLU A 641     8344   6944   5161  -1238     58    273       C  
ATOM   2246  OE1 GLU A 641      38.518  75.653  55.274  1.00 54.89           O  
ANISOU 2246  OE1 GLU A 641     8435   7063   5355  -1210     40    198       O  
ATOM   2247  OE2 GLU A 641      37.758  74.564  56.981  1.00 58.99           O  
ANISOU 2247  OE2 GLU A 641     9111   7664   5635  -1348     73    283       O  
ATOM   2248  N   LEU A 642      37.229  73.798  50.255  1.00 37.86           N  
ANISOU 2248  N   LEU A 642     5910   4628   3847   -787     76    302       N  
ATOM   2249  CA  LEU A 642      36.904  74.366  48.939  1.00 36.91           C  
ANISOU 2249  CA  LEU A 642     5707   4449   3867   -699    121    244       C  
ATOM   2250  C   LEU A 642      35.897  73.503  48.177  1.00 36.99           C  
ANISOU 2250  C   LEU A 642     5675   4414   3965   -654    158    275       C  
ATOM   2251  O   LEU A 642      34.905  74.014  47.620  1.00 34.61           O  
ANISOU 2251  O   LEU A 642     5328   4090   3730   -623    245    213       O  
ATOM   2252  CB  LEU A 642      38.166  74.538  48.085  1.00 36.04           C  
ANISOU 2252  CB  LEU A 642     5545   4317   3831   -638     28    262       C  
ATOM   2253  CG  LEU A 642      38.019  75.331  46.784  1.00 34.47           C  
ANISOU 2253  CG  LEU A 642     5281   4065   3751   -561     70    201       C  
ATOM   2254  CD1 LEU A 642      37.827  76.813  47.032  1.00 34.51           C  
ANISOU 2254  CD1 LEU A 642     5303   4071   3735   -589    144    100       C  
ATOM   2255  CD2 LEU A 642      39.251  75.122  45.908  1.00 36.02           C  
ANISOU 2255  CD2 LEU A 642     5425   4243   4017   -504    -16    242       C  
ATOM   2256  N   GLU A 643      36.154  72.202  48.166  1.00 36.78           N  
ANISOU 2256  N   GLU A 643     5663   4370   3940   -651     88    371       N  
ATOM   2257  CA  GLU A 643      35.312  71.281  47.456  1.00 41.14           C  
ANISOU 2257  CA  GLU A 643     6186   4873   4570   -623    109    402       C  
ATOM   2258  C   GLU A 643      33.906  71.217  48.047  1.00 41.42           C  
ANISOU 2258  C   GLU A 643     6233   4934   4568   -689    217    377       C  
ATOM   2259  O   GLU A 643      32.976  70.966  47.323  1.00 42.32           O  
ANISOU 2259  O   GLU A 643     6294   5019   4764   -668    260    362       O  
ATOM   2260  CB  GLU A 643      35.926  69.876  47.394  1.00 45.94           C  
ANISOU 2260  CB  GLU A 643     6824   5441   5188   -609     15    509       C  
ATOM   2261  CG  GLU A 643      35.402  69.114  46.181  1.00 52.32           C  
ANISOU 2261  CG  GLU A 643     7591   6176   6109   -555     19    518       C  
ATOM   2262  CD  GLU A 643      35.864  67.682  46.107  1.00 59.88           C  
ANISOU 2262  CD  GLU A 643     8592   7071   7086   -541    -55    615       C  
ATOM   2263  OE1 GLU A 643      37.097  67.439  46.185  1.00 63.37           O  
ANISOU 2263  OE1 GLU A 643     9043   7505   7529   -496   -140    664       O  
ATOM   2264  OE2 GLU A 643      34.975  66.808  45.959  1.00 67.08           O  
ANISOU 2264  OE2 GLU A 643     9523   7941   8022   -573    -26    640       O  
ATOM   2265  N   ARG A 644      33.751  71.460  49.345  1.00 42.59           N  
ANISOU 2265  N   ARG A 644     6449   5142   4592   -775    261    370       N  
ATOM   2266  CA  ARG A 644      32.420  71.480  49.963  1.00 43.29           C  
ANISOU 2266  CA  ARG A 644     6542   5264   4642   -841    385    338       C  
ATOM   2267  C   ARG A 644      31.787  72.880  49.904  1.00 42.61           C  
ANISOU 2267  C   ARG A 644     6408   5198   4581   -819    496    217       C  
ATOM   2268  O   ARG A 644      30.782  73.100  50.531  1.00 39.32           O  
ANISOU 2268  O   ARG A 644     5990   4819   4129   -869    613    174       O  
ATOM   2269  CB  ARG A 644      32.501  71.007  51.432  1.00 46.76           C  
ANISOU 2269  CB  ARG A 644     7090   5757   4917   -952    395    390       C  
ATOM   2270  CG  ARG A 644      33.006  69.577  51.612  1.00 49.10           C  
ANISOU 2270  CG  ARG A 644     7445   6023   5186   -976    292    523       C  
ATOM   2271  CD  ARG A 644      32.685  68.989  52.985  1.00 53.91           C  
ANISOU 2271  CD  ARG A 644     8163   6680   5638  -1096    326    586       C  
ATOM   2272  NE  ARG A 644      33.382  69.687  54.061  1.00 57.98           N  
ANISOU 2272  NE  ARG A 644     8759   7267   6001  -1152    305    567       N  
ATOM   2273  CZ  ARG A 644      34.640  69.444  54.449  1.00 63.01           C  
ANISOU 2273  CZ  ARG A 644     9453   7916   6572  -1151    165    642       C  
ATOM   2274  NH1 ARG A 644      35.383  68.500  53.864  1.00 67.35           N  
ANISOU 2274  NH1 ARG A 644     9985   8404   7201  -1084     40    743       N  
ATOM   2275  NH2 ARG A 644      35.169  70.150  55.440  1.00 61.62           N  
ANISOU 2275  NH2 ARG A 644     9348   7815   6248  -1218    149    613       N  
ATOM   2276  N   LYS A 645      32.388  73.816  49.156  1.00 41.75           N  
ANISOU 2276  N   LYS A 645     6261   5060   4539   -743    464    165       N  
ATOM   2277  CA  LYS A 645      31.888  75.185  49.028  1.00 44.49           C  
ANISOU 2277  CA  LYS A 645     6573   5404   4924   -709    559     57       C  
ATOM   2278  C   LYS A 645      31.786  75.916  50.386  1.00 46.49           C  
ANISOU 2278  C   LYS A 645     6907   5709   5047   -788    648    -10       C  
ATOM   2279  O   LYS A 645      30.878  76.707  50.608  1.00 48.86           O  
ANISOU 2279  O   LYS A 645     7184   6013   5366   -780    774    -95       O  
ATOM   2280  CB  LYS A 645      30.539  75.238  48.295  1.00 46.72           C  
ANISOU 2280  CB  LYS A 645     6756   5669   5324   -659    640     28       C  
ATOM   2281  CG  LYS A 645      30.558  74.687  46.871  1.00 47.94           C  
ANISOU 2281  CG  LYS A 645     6838   5774   5600   -584    557     76       C  
ATOM   2282  CD  LYS A 645      29.183  74.162  46.479  1.00 53.33           C  
ANISOU 2282  CD  LYS A 645     7436   6465   6359   -584    612     83       C  
ATOM   2283  CE  LYS A 645      28.428  75.121  45.589  1.00 56.90           C  
ANISOU 2283  CE  LYS A 645     7790   6898   6928   -498    654     23       C  
ATOM   2284  NZ  LYS A 645      28.781  74.837  44.154  1.00 58.14           N  
ANISOU 2284  NZ  LYS A 645     7911   7007   7171   -431    549     60       N  
ATOM   2285  N   GLU A 646      32.737  75.656  51.272  1.00 45.98           N  
ANISOU 2285  N   GLU A 646     6936   5681   4851   -862    579     27       N  
ATOM   2286  CA  GLU A 646      32.763  76.292  52.568  1.00 49.38           C  
ANISOU 2286  CA  GLU A 646     7463   6165   5133   -952    647    -36       C  
ATOM   2287  C   GLU A 646      33.693  77.496  52.591  1.00 48.61           C  
ANISOU 2287  C   GLU A 646     7398   6053   5015   -948    616   -111       C  
ATOM   2288  O   GLU A 646      33.795  78.145  53.610  1.00 49.42           O  
ANISOU 2288  O   GLU A 646     7591   6192   4993  -1026    668   -180       O  
ATOM   2289  CB  GLU A 646      33.131  75.263  53.650  1.00 50.57           C  
ANISOU 2289  CB  GLU A 646     7710   6376   5128  -1055    589     55       C  
ATOM   2290  CG  GLU A 646      32.031  74.215  53.817  1.00 52.09           C  
ANISOU 2290  CG  GLU A 646     7888   6580   5324  -1086    657    113       C  
ATOM   2291  CD  GLU A 646      32.449  72.956  54.591  1.00 55.09           C  
ANISOU 2291  CD  GLU A 646     8357   6992   5583  -1168    573    240       C  
ATOM   2292  OE1 GLU A 646      33.594  72.871  55.085  1.00 56.84           O  
ANISOU 2292  OE1 GLU A 646     8650   7237   5710  -1200    454    290       O  
ATOM   2293  OE2 GLU A 646      31.619  72.026  54.681  1.00 55.69           O  
ANISOU 2293  OE2 GLU A 646     8426   7065   5666  -1203    621    298       O  
ATOM   2294  N   ILE A 647      34.368  77.795  51.481  1.00 46.05           N  
ANISOU 2294  N   ILE A 647     7011   5676   4809   -867    536   -101       N  
ATOM   2295  CA  ILE A 647      35.185  79.011  51.381  1.00 46.16           C  
ANISOU 2295  CA  ILE A 647     7047   5665   4824   -866    518   -176       C  
ATOM   2296  C   ILE A 647      34.379  80.032  50.572  1.00 46.94           C  
ANISOU 2296  C   ILE A 647     7090   5691   5051   -780    624   -261       C  
ATOM   2297  O   ILE A 647      33.899  79.722  49.479  1.00 44.70           O  
ANISOU 2297  O   ILE A 647     6717   5369   4897   -690    619   -225       O  
ATOM   2298  CB  ILE A 647      36.568  78.728  50.733  1.00 47.91           C  
ANISOU 2298  CB  ILE A 647     7237   5881   5085   -843    365   -105       C  
ATOM   2299  CG1 ILE A 647      37.335  77.690  51.574  1.00 50.60           C  
ANISOU 2299  CG1 ILE A 647     7625   6291   5309   -914    252     -9       C  
ATOM   2300  CG2 ILE A 647      37.406  80.018  50.599  1.00 47.76           C  
ANISOU 2300  CG2 ILE A 647     7236   5836   5074   -858    351   -182       C  
ATOM   2301  CD1 ILE A 647      38.688  77.266  51.026  1.00 48.87           C  
ANISOU 2301  CD1 ILE A 647     7357   6076   5135   -884    104     69       C  
ATOM   2302  N   ASP A 648      34.190  81.231  51.122  1.00 46.45           N  
ANISOU 2302  N   ASP A 648     7087   5609   4952   -807    719   -374       N  
ATOM   2303  CA  ASP A 648      33.394  82.267  50.452  1.00 46.97           C  
ANISOU 2303  CA  ASP A 648     7108   5596   5142   -717    825   -454       C  
ATOM   2304  C   ASP A 648      34.138  82.804  49.217  1.00 44.12           C  
ANISOU 2304  C   ASP A 648     6702   5163   4895   -647    745   -435       C  
ATOM   2305  O   ASP A 648      35.318  83.091  49.300  1.00 43.20           O  
ANISOU 2305  O   ASP A 648     6630   5050   4734   -697    664   -433       O  
ATOM   2306  CB  ASP A 648      33.080  83.405  51.419  1.00 51.17           C  
ANISOU 2306  CB  ASP A 648     7731   6110   5602   -765    953   -585       C  
ATOM   2307  CG  ASP A 648      32.042  83.018  52.456  1.00 54.37           C  
ANISOU 2307  CG  ASP A 648     8163   6575   5920   -812   1076   -619       C  
ATOM   2308  OD1 ASP A 648      31.299  82.046  52.252  1.00 59.65           O  
ANISOU 2308  OD1 ASP A 648     8757   7281   6626   -787   1086   -549       O  
ATOM   2309  OD2 ASP A 648      31.941  83.710  53.468  1.00 61.23           O  
ANISOU 2309  OD2 ASP A 648     9130   7450   6683   -880   1173   -721       O  
ATOM   2310  N   PRO A 649      33.462  82.885  48.051  1.00 41.05           N  
ANISOU 2310  N   PRO A 649     6224   4720   4650   -536    763   -414       N  
ATOM   2311  CA  PRO A 649      34.128  83.477  46.882  1.00 38.53           C  
ANISOU 2311  CA  PRO A 649     5878   4332   4426   -476    702   -397       C  
ATOM   2312  C   PRO A 649      34.449  84.948  47.131  1.00 38.75           C  
ANISOU 2312  C   PRO A 649     5980   4289   4454   -492    761   -494       C  
ATOM   2313  O   PRO A 649      33.618  85.639  47.703  1.00 36.87           O  
ANISOU 2313  O   PRO A 649     5773   4020   4215   -482    879   -579       O  
ATOM   2314  CB  PRO A 649      33.081  83.333  45.763  1.00 38.89           C  
ANISOU 2314  CB  PRO A 649     5828   4341   4607   -362    724   -364       C  
ATOM   2315  CG  PRO A 649      32.179  82.229  46.221  1.00 39.73           C  
ANISOU 2315  CG  PRO A 649     5892   4516   4687   -379    751   -330       C  
ATOM   2316  CD  PRO A 649      32.105  82.415  47.716  1.00 41.29           C  
ANISOU 2316  CD  PRO A 649     6171   4757   4759   -470    829   -396       C  
ATOM   2317  N   PRO A 650      35.644  85.420  46.721  1.00 36.66           N  
ANISOU 2317  N   PRO A 650     5742   3995   4191   -521    686   -486       N  
ATOM   2318  CA  PRO A 650      35.966  86.837  46.937  1.00 38.58           C  
ANISOU 2318  CA  PRO A 650     6064   4156   4436   -550    742   -580       C  
ATOM   2319  C   PRO A 650      35.083  87.787  46.146  1.00 38.06           C  
ANISOU 2319  C   PRO A 650     5980   3977   4500   -438    828   -613       C  
ATOM   2320  O   PRO A 650      34.892  88.918  46.566  1.00 40.74           O  
ANISOU 2320  O   PRO A 650     6394   4237   4845   -446    917   -708       O  
ATOM   2321  CB  PRO A 650      37.428  86.957  46.482  1.00 38.81           C  
ANISOU 2321  CB  PRO A 650     6098   4188   4457   -605    633   -541       C  
ATOM   2322  CG  PRO A 650      37.965  85.581  46.573  1.00 38.28           C  
ANISOU 2322  CG  PRO A 650     5978   4228   4339   -632    527   -449       C  
ATOM   2323  CD  PRO A 650      36.831  84.629  46.360  1.00 37.24           C  
ANISOU 2323  CD  PRO A 650     5786   4121   4240   -556    555   -401       C  
ATOM   2324  N   PHE A 651      34.523  87.328  45.027  1.00 36.21           N  
ANISOU 2324  N   PHE A 651     5654   3733   4369   -334    800   -536       N  
ATOM   2325  CA  PHE A 651      33.542  88.106  44.264  1.00 35.12           C  
ANISOU 2325  CA  PHE A 651     5484   3501   4358   -216    866   -548       C  
ATOM   2326  C   PHE A 651      32.153  87.504  44.402  1.00 35.90           C  
ANISOU 2326  C   PHE A 651     5498   3642   4497   -148    924   -539       C  
ATOM   2327  O   PHE A 651      31.960  86.326  44.073  1.00 34.57           O  
ANISOU 2327  O   PHE A 651     5258   3553   4324   -144    860   -464       O  
ATOM   2328  CB  PHE A 651      33.955  88.139  42.784  1.00 34.77           C  
ANISOU 2328  CB  PHE A 651     5398   3414   4396   -154    782   -462       C  
ATOM   2329  CG  PHE A 651      32.931  88.779  41.884  1.00 34.10           C  
ANISOU 2329  CG  PHE A 651     5271   3244   4438    -26    821   -446       C  
ATOM   2330  CD1 PHE A 651      32.845  90.167  41.775  1.00 33.48           C  
ANISOU 2330  CD1 PHE A 651     5258   3040   4423     13    886   -498       C  
ATOM   2331  CD2 PHE A 651      32.024  87.984  41.170  1.00 34.20           C  
ANISOU 2331  CD2 PHE A 651     5180   3303   4511     52    787   -377       C  
ATOM   2332  CE1 PHE A 651      31.904  90.770  40.947  1.00 34.12           C  
ANISOU 2332  CE1 PHE A 651     5299   3038   4626    142    911   -470       C  
ATOM   2333  CE2 PHE A 651      31.056  88.570  40.353  1.00 35.12           C  
ANISOU 2333  CE2 PHE A 651     5247   3351   4744    172    807   -354       C  
ATOM   2334  CZ  PHE A 651      30.986  89.974  40.251  1.00 35.91           C  
ANISOU 2334  CZ  PHE A 651     5409   3324   4909    224    868   -397       C  
ATOM   2335  N   ARG A 652      31.185  88.291  44.879  1.00 36.85           N  
ANISOU 2335  N   ARG A 652     5626   3710   4663    -97   1048   -619       N  
ATOM   2336  CA  ARG A 652      29.793  87.851  44.917  1.00 40.15           C  
ANISOU 2336  CA  ARG A 652     5941   4167   5145    -23   1113   -612       C  
ATOM   2337  C   ARG A 652      28.955  88.491  43.834  1.00 39.49           C  
ANISOU 2337  C   ARG A 652     5779   4003   5220    119   1123   -584       C  
ATOM   2338  O   ARG A 652      28.720  89.696  43.862  1.00 41.34           O  
ANISOU 2338  O   ARG A 652     6054   4129   5521    182   1201   -645       O  
ATOM   2339  CB  ARG A 652      29.142  88.175  46.252  1.00 46.04           C  
ANISOU 2339  CB  ARG A 652     6725   4928   5840    -55   1261   -720       C  
ATOM   2340  CG  ARG A 652      29.796  87.448  47.407  1.00 54.35           C  
ANISOU 2340  CG  ARG A 652     7853   6076   6719   -200   1250   -739       C  
ATOM   2341  CD  ARG A 652      28.879  87.374  48.620  1.00 63.84           C  
ANISOU 2341  CD  ARG A 652     9064   7328   7862   -232   1397   -821       C  
ATOM   2342  NE  ARG A 652      29.408  86.447  49.626  1.00 70.87           N  
ANISOU 2342  NE  ARG A 652    10019   8325   8580   -370   1366   -806       N  
ATOM   2343  CZ  ARG A 652      29.494  85.119  49.477  1.00 71.92           C  
ANISOU 2343  CZ  ARG A 652    10100   8548   8678   -408   1274   -703       C  
ATOM   2344  NH1 ARG A 652      29.083  84.507  48.360  1.00 67.32           N  
ANISOU 2344  NH1 ARG A 652     9398   7967   8211   -329   1205   -613       N  
ATOM   2345  NH2 ARG A 652      29.989  84.388  50.472  1.00 74.90           N  
ANISOU 2345  NH2 ARG A 652    10552   9010   8896   -531   1249   -689       N  
ATOM   2346  N   PRO A 653      28.433  87.685  42.910  1.00 39.44           N  
ANISOU 2346  N   PRO A 653     5663   4046   5276    173   1046   -492       N  
ATOM   2347  CA  PRO A 653      27.594  88.303  41.889  1.00 40.99           C  
ANISOU 2347  CA  PRO A 653     5780   4174   5617    309   1041   -456       C  
ATOM   2348  C   PRO A 653      26.414  89.038  42.510  1.00 41.42           C  
ANISOU 2348  C   PRO A 653     5787   4191   5757    391   1183   -533       C  
ATOM   2349  O   PRO A 653      25.976  88.692  43.604  1.00 39.50           O  
ANISOU 2349  O   PRO A 653     5532   4012   5461    341   1280   -598       O  
ATOM   2350  CB  PRO A 653      27.100  87.108  41.068  1.00 41.00           C  
ANISOU 2350  CB  PRO A 653     5667   4265   5645    323    942   -361       C  
ATOM   2351  CG  PRO A 653      28.091  86.011  41.317  1.00 39.74           C  
ANISOU 2351  CG  PRO A 653     5557   4181   5360    204    870   -332       C  
ATOM   2352  CD  PRO A 653      28.573  86.231  42.716  1.00 38.83           C  
ANISOU 2352  CD  PRO A 653     5533   4077   5143    114    955   -416       C  
ATOM   2353  N   LYS A 654      25.965  90.082  41.838  1.00 42.77           N  
ANISOU 2353  N   LYS A 654     5939   4254   6054    516   1199   -527       N  
ATOM   2354  CA  LYS A 654      24.795  90.818  42.232  1.00 48.97           C  
ANISOU 2354  CA  LYS A 654     6658   4992   6954    626   1328   -588       C  
ATOM   2355  C   LYS A 654      23.625  90.098  41.604  1.00 49.30           C  
ANISOU 2355  C   LYS A 654     6517   5120   7093    702   1283   -513       C  
ATOM   2356  O   LYS A 654      23.502  90.107  40.387  1.00 48.49           O  
ANISOU 2356  O   LYS A 654     6361   4998   7062    772   1166   -417       O  
ATOM   2357  CB  LYS A 654      24.824  92.233  41.665  1.00 54.11           C  
ANISOU 2357  CB  LYS A 654     7367   5476   7715    741   1346   -595       C  
ATOM   2358  CG  LYS A 654      26.029  93.076  42.026  1.00 57.63           C  
ANISOU 2358  CG  LYS A 654     7997   5814   8083    665   1370   -657       C  
ATOM   2359  CD  LYS A 654      25.706  94.567  41.876  1.00 60.59           C  
ANISOU 2359  CD  LYS A 654     8428   6007   8583    787   1453   -701       C  
ATOM   2360  CE  LYS A 654      24.885  95.046  43.059  1.00 63.93           C  
ANISOU 2360  CE  LYS A 654     8845   6403   9040    827   1638   -834       C  
ATOM   2361  NZ  LYS A 654      24.536  96.486  42.967  1.00 68.97           N  
ANISOU 2361  NZ  LYS A 654     9544   6849   9812    957   1732   -885       N  
ATOM   2362  N   VAL A 655      22.799  89.447  42.414  1.00 51.66           N  
ANISOU 2362  N   VAL A 655     6722   5519   7384    673   1371   -553       N  
ATOM   2363  CA  VAL A 655      21.570  88.800  41.913  1.00 55.42           C  
ANISOU 2363  CA  VAL A 655     7005   6084   7966    736   1342   -492       C  
ATOM   2364  C   VAL A 655      20.410  89.114  42.840  1.00 57.99           C  
ANISOU 2364  C   VAL A 655     7230   6433   8370    792   1519   -578       C  
ATOM   2365  O   VAL A 655      20.526  88.979  44.059  1.00 59.17           O  
ANISOU 2365  O   VAL A 655     7443   6615   8422    705   1647   -669       O  
ATOM   2366  CB  VAL A 655      21.701  87.259  41.769  1.00 54.64           C  
ANISOU 2366  CB  VAL A 655     6863   6120   7776    616   1244   -426       C  
ATOM   2367  CG1 VAL A 655      22.776  86.904  40.754  1.00 55.05           C  
ANISOU 2367  CG1 VAL A 655     6997   6151   7765    577   1077   -343       C  
ATOM   2368  CG2 VAL A 655      22.007  86.597  43.105  1.00 54.49           C  
ANISOU 2368  CG2 VAL A 655     6912   6173   7618    479   1337   -492       C  
ATOM   2369  N   LYS A 656      19.294  89.521  42.247  1.00 60.26           N  
ANISOU 2369  N   LYS A 656     7356   6707   8831    937   1524   -545       N  
ATOM   2370  CA  LYS A 656      18.116  89.951  42.985  1.00 64.14           C  
ANISOU 2370  CA  LYS A 656     7724   7211   9434   1022   1699   -624       C  
ATOM   2371  C   LYS A 656      17.055  88.858  43.129  1.00 63.81           C  
ANISOU 2371  C   LYS A 656     7485   7330   9428    983   1714   -594       C  
ATOM   2372  O   LYS A 656      16.171  88.980  43.969  1.00 67.33           O  
ANISOU 2372  O   LYS A 656     7833   7817   9930   1010   1884   -671       O  
ATOM   2373  CB  LYS A 656      17.513  91.184  42.296  1.00 68.70           C  
ANISOU 2373  CB  LYS A 656     8232   7665  10204   1224   1705   -607       C  
ATOM   2374  CG  LYS A 656      18.365  92.446  42.444  1.00 71.82           C  
ANISOU 2374  CG  LYS A 656     8824   7881  10583   1267   1753   -668       C  
ATOM   2375  CD  LYS A 656      18.138  93.500  41.356  1.00 75.10           C  
ANISOU 2375  CD  LYS A 656     9216   8157  11158   1444   1678   -596       C  
ATOM   2376  CE  LYS A 656      16.668  93.857  41.149  1.00 78.31           C  
ANISOU 2376  CE  LYS A 656     9401   8572  11778   1625   1733   -579       C  
ATOM   2377  NZ  LYS A 656      16.060  93.142  39.988  1.00 79.83           N  
ANISOU 2377  NZ  LYS A 656     9416   8872  12043   1661   1549   -435       N  
ATOM   2378  N   SER A 657      17.127  87.797  42.324  1.00 59.74           N  
ANISOU 2378  N   SER A 657     6913   6902   8882    914   1548   -489       N  
ATOM   2379  CA  SER A 657      16.126  86.718  42.391  1.00 59.33           C  
ANISOU 2379  CA  SER A 657     6676   6998   8867    860   1550   -456       C  
ATOM   2380  C   SER A 657      16.664  85.458  41.727  1.00 56.33           C  
ANISOU 2380  C   SER A 657     6328   6688   8384    733   1374   -364       C  
ATOM   2381  O   SER A 657      17.726  85.505  41.090  1.00 53.82           O  
ANISOU 2381  O   SER A 657     6150   6306   7990    714   1250   -322       O  
ATOM   2382  CB  SER A 657      14.823  87.149  41.702  1.00 58.71           C  
ANISOU 2382  CB  SER A 657     6366   6938   9002   1016   1535   -414       C  
ATOM   2383  OG  SER A 657      14.991  87.203  40.290  1.00 58.07           O  
ANISOU 2383  OG  SER A 657     6266   6826   8969   1077   1329   -303       O  
ATOM   2384  N   PRO A 658      15.937  84.327  41.858  1.00 56.63           N  
ANISOU 2384  N   PRO A 658     6237   6854   8425    643   1370   -336       N  
ATOM   2385  CA  PRO A 658      16.385  83.125  41.160  1.00 55.87           C  
ANISOU 2385  CA  PRO A 658     6172   6809   8246    530   1204   -253       C  
ATOM   2386  C   PRO A 658      16.296  83.234  39.629  1.00 54.09           C  
ANISOU 2386  C   PRO A 658     5888   6562   8100    610   1014   -161       C  
ATOM   2387  O   PRO A 658      16.991  82.497  38.946  1.00 51.87           O  
ANISOU 2387  O   PRO A 658     5692   6285   7732    535    875   -104       O  
ATOM   2388  CB  PRO A 658      15.442  82.018  41.693  1.00 57.37           C  
ANISOU 2388  CB  PRO A 658     6223   7129   8444    421   1263   -251       C  
ATOM   2389  CG  PRO A 658      14.886  82.566  42.968  1.00 60.23           C  
ANISOU 2389  CG  PRO A 658     6547   7507   8828    440   1485   -348       C  
ATOM   2390  CD  PRO A 658      14.769  84.048  42.716  1.00 60.40           C  
ANISOU 2390  CD  PRO A 658     6553   7429   8967    622   1527   -385       C  
ATOM   2391  N   PHE A 659      15.471  84.146  39.110  1.00 54.80           N  
ANISOU 2391  N   PHE A 659     5842   6628   8349    762   1009   -145       N  
ATOM   2392  CA  PHE A 659      15.307  84.325  37.656  1.00 56.76           C  
ANISOU 2392  CA  PHE A 659     6035   6862   8669    843    823    -49       C  
ATOM   2393  C   PHE A 659      16.042  85.542  37.082  1.00 55.58           C  
ANISOU 2393  C   PHE A 659     6014   6572   8530    962    781    -31       C  
ATOM   2394  O   PHE A 659      16.002  85.784  35.873  1.00 56.89           O  
ANISOU 2394  O   PHE A 659     6162   6715   8738   1030    628     53       O  
ATOM   2395  CB  PHE A 659      13.822  84.393  37.259  1.00 60.42           C  
ANISOU 2395  CB  PHE A 659     6237   7407   9310    929    801    -11       C  
ATOM   2396  CG  PHE A 659      13.022  85.426  38.011  1.00 64.54           C  
ANISOU 2396  CG  PHE A 659     6644   7901   9976   1065    972    -75       C  
ATOM   2397  CD1 PHE A 659      13.011  86.758  37.608  1.00 66.09           C  
ANISOU 2397  CD1 PHE A 659     6853   7979  10277   1245    970    -64       C  
ATOM   2398  CD2 PHE A 659      12.256  85.057  39.116  1.00 66.94           C  
ANISOU 2398  CD2 PHE A 659     6827   8291  10313   1015   1145   -148       C  
ATOM   2399  CE1 PHE A 659      12.266  87.703  38.301  1.00 67.97           C  
ANISOU 2399  CE1 PHE A 659     6987   8178  10658   1381   1139   -130       C  
ATOM   2400  CE2 PHE A 659      11.506  85.996  39.804  1.00 68.39           C  
ANISOU 2400  CE2 PHE A 659     6901   8449  10632   1146   1320   -216       C  
ATOM   2401  CZ  PHE A 659      11.508  87.320  39.395  1.00 69.53           C  
ANISOU 2401  CZ  PHE A 659     7059   8468  10889   1335   1317   -211       C  
ATOM   2402  N   ASP A 660      16.701  86.302  37.947  1.00 54.70           N  
ANISOU 2402  N   ASP A 660     6039   6369   8376    979    914   -111       N  
ATOM   2403  CA  ASP A 660      17.422  87.508  37.546  1.00 53.27           C  
ANISOU 2403  CA  ASP A 660     5992   6042   8206   1077    898   -106       C  
ATOM   2404  C   ASP A 660      18.401  87.112  36.454  1.00 50.32           C  
ANISOU 2404  C   ASP A 660     5739   5651   7730   1018    724    -24       C  
ATOM   2405  O   ASP A 660      19.150  86.148  36.604  1.00 50.63           O  
ANISOU 2405  O   ASP A 660     5863   5738   7634    881    690    -28       O  
ATOM   2406  CB  ASP A 660      18.126  88.089  38.783  1.00 54.15           C  
ANISOU 2406  CB  ASP A 660     6253   6077   8243   1043   1065   -219       C  
ATOM   2407  CG  ASP A 660      19.152  89.192  38.462  1.00 53.92           C  
ANISOU 2407  CG  ASP A 660     6404   5894   8189   1093   1048   -222       C  
ATOM   2408  OD1 ASP A 660      19.173  90.181  39.198  1.00 53.45           O  
ANISOU 2408  OD1 ASP A 660     6403   5738   8165   1151   1185   -307       O  
ATOM   2409  OD2 ASP A 660      19.986  89.049  37.550  1.00 53.44           O  
ANISOU 2409  OD2 ASP A 660     6436   5805   8060   1059    910   -151       O  
ATOM   2410  N   CYS A 661      18.375  87.829  35.342  1.00 51.53           N  
ANISOU 2410  N   CYS A 661     5895   5734   7947   1125    615     52       N  
ATOM   2411  CA  CYS A 661      19.317  87.576  34.254  1.00 50.91           C  
ANISOU 2411  CA  CYS A 661     5941   5632   7768   1076    465    127       C  
ATOM   2412  C   CYS A 661      20.162  88.805  33.885  1.00 50.69           C  
ANISOU 2412  C   CYS A 661     6069   5453   7736   1146    466    142       C  
ATOM   2413  O   CYS A 661      20.682  88.896  32.763  1.00 49.21           O  
ANISOU 2413  O   CYS A 661     5957   5234   7506   1149    340    223       O  
ATOM   2414  CB  CYS A 661      18.554  87.066  33.042  1.00 52.50           C  
ANISOU 2414  CB  CYS A 661     6018   5912   8016   1102    299    228       C  
ATOM   2415  SG  CYS A 661      17.359  88.268  32.481  1.00 59.14           S  
ANISOU 2415  SG  CYS A 661     6711   6702   9054   1307    267    292       S  
ATOM   2416  N   SER A 662      20.363  89.704  34.848  1.00 49.17           N  
ANISOU 2416  N   SER A 662     5940   5167   7574   1184    614     57       N  
ATOM   2417  CA  SER A 662      21.168  90.911  34.638  1.00 49.95           C  
ANISOU 2417  CA  SER A 662     6196   5109   7672   1235    634     57       C  
ATOM   2418  C   SER A 662      22.696  90.686  34.438  1.00 47.42           C  
ANISOU 2418  C   SER A 662     6059   4762   7196   1108    592     59       C  
ATOM   2419  O   SER A 662      23.394  91.599  33.987  1.00 45.46           O  
ANISOU 2419  O   SER A 662     5936   4393   6943   1135    579     83       O  
ATOM   2420  CB  SER A 662      20.952  91.882  35.808  1.00 52.98           C  
ANISOU 2420  CB  SER A 662     6605   5398   8125   1295    814    -52       C  
ATOM   2421  OG  SER A 662      21.487  91.331  37.002  1.00 54.41           O  
ANISOU 2421  OG  SER A 662     6846   5633   8194   1163    919   -155       O  
ATOM   2422  N   ASN A 663      23.226  89.509  34.765  1.00 45.39           N  
ANISOU 2422  N   ASN A 663     5815   4609   6818    972    575     36       N  
ATOM   2423  CA  ASN A 663      24.683  89.258  34.582  1.00 43.53           C  
ANISOU 2423  CA  ASN A 663     5732   4358   6450    860    537     39       C  
ATOM   2424  C   ASN A 663      25.074  88.643  33.223  1.00 44.01           C  
ANISOU 2424  C   ASN A 663     5810   4457   6455    833    387    138       C  
ATOM   2425  O   ASN A 663      26.123  87.995  33.083  1.00 44.68           O  
ANISOU 2425  O   ASN A 663     5974   4572   6427    731    354    139       O  
ATOM   2426  CB  ASN A 663      25.227  88.409  35.715  1.00 43.50           C  
ANISOU 2426  CB  ASN A 663     5756   4428   6342    734    602    -37       C  
ATOM   2427  CG  ASN A 663      25.202  89.131  37.038  1.00 45.41           C  
ANISOU 2427  CG  ASN A 663     6039   4618   6596    733    751   -142       C  
ATOM   2428  OD1 ASN A 663      25.717  90.229  37.153  1.00 46.20           O  
ANISOU 2428  OD1 ASN A 663     6241   4603   6710    758    799   -174       O  
ATOM   2429  ND2 ASN A 663      24.617  88.510  38.048  1.00 45.74           N  
ANISOU 2429  ND2 ASN A 663     6012   4744   6624    692    830   -200       N  
ATOM   2430  N   PHE A 664      24.230  88.862  32.230  1.00 45.21           N  
ANISOU 2430  N   PHE A 664     5885   4608   6683    927    300    219       N  
ATOM   2431  CA  PHE A 664      24.438  88.352  30.894  1.00 46.42           C  
ANISOU 2431  CA  PHE A 664     6057   4799   6780    907    158    310       C  
ATOM   2432  C   PHE A 664      24.400  89.517  29.914  1.00 51.53           C  
ANISOU 2432  C   PHE A 664     6759   5340   7477   1008    104    392       C  
ATOM   2433  O   PHE A 664      23.814  90.579  30.191  1.00 48.83           O  
ANISOU 2433  O   PHE A 664     6392   4910   7250   1120    156    391       O  
ATOM   2434  CB  PHE A 664      23.348  87.344  30.554  1.00 45.60           C  
ANISOU 2434  CB  PHE A 664     5804   4817   6705    906     77    342       C  
ATOM   2435  CG  PHE A 664      23.364  86.123  31.433  1.00 44.07           C  
ANISOU 2435  CG  PHE A 664     5565   4720   6457    798    124    276       C  
ATOM   2436  CD1 PHE A 664      24.375  85.168  31.296  1.00 42.88           C  
ANISOU 2436  CD1 PHE A 664     5505   4605   6182    683     93    267       C  
ATOM   2437  CD2 PHE A 664      22.394  85.937  32.418  1.00 44.64           C  
ANISOU 2437  CD2 PHE A 664     5510   4843   6605    813    206    224       C  
ATOM   2438  CE1 PHE A 664      24.397  84.039  32.111  1.00 42.47           C  
ANISOU 2438  CE1 PHE A 664     5422   4629   6083    589    131    218       C  
ATOM   2439  CE2 PHE A 664      22.417  84.815  33.235  1.00 43.05           C  
ANISOU 2439  CE2 PHE A 664     5283   4726   6347    705    251    173       C  
ATOM   2440  CZ  PHE A 664      23.416  83.864  33.080  1.00 41.80           C  
ANISOU 2440  CZ  PHE A 664     5222   4593   6066    595    207    174       C  
ATOM   2441  N   ASP A 665      25.033  89.309  28.768  1.00 55.89           N  
ANISOU 2441  N   ASP A 665     7397   5897   7942    969      3    465       N  
ATOM   2442  CA  ASP A 665      25.129  90.340  27.743  1.00 59.20           C  
ANISOU 2442  CA  ASP A 665     7894   6217   8380   1044    -56    558       C  
ATOM   2443  C   ASP A 665      23.746  90.747  27.230  1.00 61.72           C  
ANISOU 2443  C   ASP A 665     8091   6539   8819   1179   -137    635       C  
ATOM   2444  O   ASP A 665      22.926  89.893  26.907  1.00 59.68           O  
ANISOU 2444  O   ASP A 665     7709   6397   8567   1174   -223    659       O  
ATOM   2445  CB  ASP A 665      26.017  89.850  26.605  1.00 61.89           C  
ANISOU 2445  CB  ASP A 665     8341   6588   8586    961   -143    617       C  
ATOM   2446  CG  ASP A 665      26.566  90.988  25.779  1.00 64.64           C  
ANISOU 2446  CG  ASP A 665     8822   6815   8920    998   -162    697       C  
ATOM   2447  OD1 ASP A 665      25.761  91.777  25.252  1.00 66.28           O  
ANISOU 2447  OD1 ASP A 665     9007   6965   9210   1112   -220    778       O  
ATOM   2448  OD2 ASP A 665      27.801  91.096  25.675  1.00 67.81           O  
ANISOU 2448  OD2 ASP A 665     9350   7180   9235    913   -117    681       O  
ATOM   2449  N   LYS A 666      23.503  92.058  27.132  1.00 64.15           N  
ANISOU 2449  N   LYS A 666     8433   6714   9224   1297   -114    677       N  
ATOM   2450  CA  LYS A 666      22.175  92.587  26.753  1.00 67.24           C  
ANISOU 2450  CA  LYS A 666     8696   7093   9757   1450   -183    753       C  
ATOM   2451  C   LYS A 666      21.901  92.374  25.267  1.00 66.14           C  
ANISOU 2451  C   LYS A 666     8561   7004   9564   1464   -368    889       C  
ATOM   2452  O   LYS A 666      20.748  92.348  24.831  1.00 64.49           O  
ANISOU 2452  O   LYS A 666     8210   6849   9442   1556   -470    958       O  
ATOM   2453  CB  LYS A 666      22.017  94.093  27.067  1.00 73.11           C  
ANISOU 2453  CB  LYS A 666     9488   7658  10630   1586   -103    762       C  
ATOM   2454  CG  LYS A 666      22.987  94.700  28.076  1.00 77.06           C  
ANISOU 2454  CG  LYS A 666    10122   8043  11113   1533     60    654       C  
ATOM   2455  CD  LYS A 666      22.985  93.982  29.418  1.00 77.74           C  
ANISOU 2455  CD  LYS A 666    10138   8213  11185   1457    182    512       C  
ATOM   2456  CE  LYS A 666      24.403  93.818  29.950  1.00 78.64           C  
ANISOU 2456  CE  LYS A 666    10403   8306  11168   1307    258    433       C  
ATOM   2457  NZ  LYS A 666      24.426  93.049  31.227  1.00 77.66           N  
ANISOU 2457  NZ  LYS A 666    10221   8273  11013   1225    359    311       N  
ATOM   2458  N   GLU A 667      22.970  92.238  24.493  1.00 66.67           N  
ANISOU 2458  N   GLU A 667     8789   7057   9484   1369   -409    926       N  
ATOM   2459  CA  GLU A 667      22.868  91.913  23.071  1.00 71.69           C  
ANISOU 2459  CA  GLU A 667     9460   7752  10026   1350   -575   1043       C  
ATOM   2460  C   GLU A 667      21.919  90.729  22.820  1.00 68.04           C  
ANISOU 2460  C   GLU A 667     8837   7457   9556   1322   -685   1045       C  
ATOM   2461  O   GLU A 667      21.156  90.732  21.869  1.00 67.85           O  
ANISOU 2461  O   GLU A 667     8759   7481   9538   1372   -837   1148       O  
ATOM   2462  CB  GLU A 667      24.269  91.575  22.541  1.00 75.64           C  
ANISOU 2462  CB  GLU A 667    10139   8247  10351   1214   -559   1036       C  
ATOM   2463  CG  GLU A 667      24.359  91.284  21.051  1.00 81.56           C  
ANISOU 2463  CG  GLU A 667    10966   9048  10971   1177   -708   1145       C  
ATOM   2464  CD  GLU A 667      25.781  90.970  20.615  1.00 84.19           C  
ANISOU 2464  CD  GLU A 667    11469   9376  11142   1046   -660   1123       C  
ATOM   2465  OE1 GLU A 667      26.495  90.249  21.353  1.00 82.97           O  
ANISOU 2465  OE1 GLU A 667    11312   9260  10950    954   -562   1013       O  
ATOM   2466  OE2 GLU A 667      26.187  91.452  19.536  1.00 87.09           O  
ANISOU 2466  OE2 GLU A 667    11967   9701  11421   1036   -718   1221       O  
ATOM   2467  N   PHE A 668      21.982  89.717  23.680  1.00 66.45           N  
ANISOU 2467  N   PHE A 668     8564   7343   9338   1233   -612    934       N  
ATOM   2468  CA  PHE A 668      21.178  88.499  23.519  1.00 65.06           C  
ANISOU 2468  CA  PHE A 668     8250   7320   9150   1178   -701    923       C  
ATOM   2469  C   PHE A 668      19.814  88.636  24.201  1.00 64.70           C  
ANISOU 2469  C   PHE A 668     7989   7316   9277   1276   -689    911       C  
ATOM   2470  O   PHE A 668      18.792  88.227  23.651  1.00 62.70           O  
ANISOU 2470  O   PHE A 668     7598   7161   9063   1296   -818    967       O  
ATOM   2471  CB  PHE A 668      21.913  87.291  24.117  1.00 63.93           C  
ANISOU 2471  CB  PHE A 668     8142   7242   8907   1031   -626    816       C  
ATOM   2472  CG  PHE A 668      23.304  87.052  23.562  1.00 62.97           C  
ANISOU 2472  CG  PHE A 668     8209   7088   8626    935   -615    812       C  
ATOM   2473  CD1 PHE A 668      24.410  86.970  24.420  1.00 62.50           C  
ANISOU 2473  CD1 PHE A 668     8234   6984   8528    871   -479    726       C  
ATOM   2474  CD2 PHE A 668      23.509  86.853  22.204  1.00 63.51           C  
ANISOU 2474  CD2 PHE A 668     8364   7183   8581    901   -739    890       C  
ATOM   2475  CE1 PHE A 668      25.681  86.723  23.930  1.00 59.52           C  
ANISOU 2475  CE1 PHE A 668     8006   6588   8021    786   -463    720       C  
ATOM   2476  CE2 PHE A 668      24.779  86.600  21.708  1.00 60.96           C  
ANISOU 2476  CE2 PHE A 668     8205   6838   8117    812   -710    878       C  
ATOM   2477  CZ  PHE A 668      25.865  86.533  22.572  1.00 61.42           C  
ANISOU 2477  CZ  PHE A 668     8327   6852   8156    759   -571    794       C  
ATOM   2478  N   LEU A 669      19.803  89.227  25.399  1.00 64.34           N  
ANISOU 2478  N   LEU A 669     7912   7198   9334   1333   -532    835       N  
ATOM   2479  CA  LEU A 669      18.582  89.324  26.223  1.00 62.65           C  
ANISOU 2479  CA  LEU A 669     7493   7024   9285   1420   -477    800       C  
ATOM   2480  C   LEU A 669      17.447  90.036  25.514  1.00 67.32           C  
ANISOU 2480  C   LEU A 669     7955   7612  10011   1573   -595    911       C  
ATOM   2481  O   LEU A 669      16.275  89.779  25.787  1.00 67.56           O  
ANISOU 2481  O   LEU A 669     7775   7731  10163   1624   -614    909       O  
ATOM   2482  CB  LEU A 669      18.880  90.051  27.544  1.00 61.78           C  
ANISOU 2482  CB  LEU A 669     7414   6812   9248   1464   -279    699       C  
ATOM   2483  CG  LEU A 669      19.837  89.333  28.511  1.00 58.28           C  
ANISOU 2483  CG  LEU A 669     7062   6389   8693   1320   -155    583       C  
ATOM   2484  CD1 LEU A 669      20.221  90.222  29.688  1.00 57.08           C  
ANISOU 2484  CD1 LEU A 669     6972   6123   8592   1359     23    492       C  
ATOM   2485  CD2 LEU A 669      19.212  88.032  28.995  1.00 57.00           C  
ANISOU 2485  CD2 LEU A 669     6757   6375   8522   1230   -153    534       C  
ATOM   2486  N   ASN A 670      17.803  90.938  24.609  1.00 69.81           N  
ANISOU 2486  N   ASN A 670     8392   7824  10306   1645   -674   1012       N  
ATOM   2487  CA  ASN A 670      16.818  91.695  23.852  1.00 74.29           C  
ANISOU 2487  CA  ASN A 670     8859   8372  10994   1801   -804   1139       C  
ATOM   2488  C   ASN A 670      16.083  90.904  22.763  1.00 75.17           C  
ANISOU 2488  C   ASN A 670     8865   8636  11059   1762  -1018   1232       C  
ATOM   2489  O   ASN A 670      15.047  91.360  22.277  1.00 77.09           O  
ANISOU 2489  O   ASN A 670     8965   8901  11424   1890  -1137   1332       O  
ATOM   2490  CB  ASN A 670      17.477  92.943  23.259  1.00 75.73           C  
ANISOU 2490  CB  ASN A 670     9229   8382  11162   1884   -816   1226       C  
ATOM   2491  CG  ASN A 670      17.743  94.006  24.312  1.00 79.32           C  
ANISOU 2491  CG  ASN A 670     9733   8671  11733   1976   -626   1152       C  
ATOM   2492  OD1 ASN A 670      16.869  94.318  25.122  1.00 84.53           O  
ANISOU 2492  OD1 ASN A 670    10233   9322  12561   2087   -542   1104       O  
ATOM   2493  ND2 ASN A 670      18.945  94.566  24.310  1.00 78.68           N  
ANISOU 2493  ND2 ASN A 670     9872   8461  11562   1925   -552   1136       N  
ATOM   2494  N   GLU A 671      16.598  89.731  22.397  1.00 73.32           N  
ANISOU 2494  N   GLU A 671     8697   8505  10656   1589  -1069   1198       N  
ATOM   2495  CA  GLU A 671      15.975  88.906  21.354  1.00 75.45           C  
ANISOU 2495  CA  GLU A 671     8891   8917  10857   1525  -1271   1270       C  
ATOM   2496  C   GLU A 671      14.787  88.122  21.879  1.00 75.48           C  
ANISOU 2496  C   GLU A 671     8641   9062  10973   1508  -1289   1226       C  
ATOM   2497  O   GLU A 671      14.869  87.508  22.947  1.00 76.13           O  
ANISOU 2497  O   GLU A 671     8673   9174  11077   1438  -1144   1107       O  
ATOM   2498  CB  GLU A 671      16.969  87.894  20.787  1.00 74.97           C  
ANISOU 2498  CB  GLU A 671     9004   8903  10576   1343  -1303   1234       C  
ATOM   2499  CG  GLU A 671      17.864  88.412  19.681  1.00 75.63           C  
ANISOU 2499  CG  GLU A 671     9310   8911  10514   1332  -1375   1321       C  
ATOM   2500  CD  GLU A 671      18.434  87.285  18.846  1.00 75.64           C  
ANISOU 2500  CD  GLU A 671     9428   9000  10311   1165  -1456   1303       C  
ATOM   2501  OE1 GLU A 671      17.644  86.487  18.307  1.00 77.75           O  
ANISOU 2501  OE1 GLU A 671     9593   9395  10551   1108  -1599   1324       O  
ATOM   2502  OE2 GLU A 671      19.672  87.187  18.741  1.00 76.54           O  
ANISOU 2502  OE2 GLU A 671     9732   9055  10294   1087  -1372   1264       O  
ATOM   2503  N   LYS A 672      13.705  88.103  21.106  1.00 74.78           N  
ANISOU 2503  N   LYS A 672     8395   9068  10948   1560  -1473   1327       N  
ATOM   2504  CA  LYS A 672      12.562  87.259  21.425  1.00 76.16           C  
ANISOU 2504  CA  LYS A 672     8321   9399  11217   1518  -1517   1295       C  
ATOM   2505  C   LYS A 672      12.967  85.800  21.286  1.00 72.09           C  
ANISOU 2505  C   LYS A 672     7872   8984  10535   1301  -1541   1219       C  
ATOM   2506  O   LYS A 672      13.469  85.397  20.241  1.00 71.71           O  
ANISOU 2506  O   LYS A 672     7972   8955  10316   1209  -1671   1261       O  
ATOM   2507  CB  LYS A 672      11.391  87.546  20.506  1.00 79.95           C  
ANISOU 2507  CB  LYS A 672     8624   9966  11787   1608  -1736   1430       C  
ATOM   2508  CG  LYS A 672      10.777  88.906  20.743  1.00 84.84           C  
ANISOU 2508  CG  LYS A 672     9129  10493  12613   1841  -1711   1504       C  
ATOM   2509  CD  LYS A 672       9.604  89.129  19.809  1.00 89.29           C  
ANISOU 2509  CD  LYS A 672     9501  11155  13268   1933  -1949   1649       C  
ATOM   2510  CE  LYS A 672       9.226  90.595  19.715  1.00 91.01           C  
ANISOU 2510  CE  LYS A 672     9676  11245  13658   2178  -1960   1760       C  
ATOM   2511  NZ  LYS A 672       8.592  90.848  18.400  1.00 94.65           N  
ANISOU 2511  NZ  LYS A 672    10082  11772  14108   2238  -2241   1937       N  
ATOM   2512  N   PRO A 673      12.777  85.009  22.350  1.00 69.30           N  
ANISOU 2512  N   PRO A 673     7420   8684  10226   1218  -1408   1105       N  
ATOM   2513  CA  PRO A 673      13.107  83.585  22.264  1.00 65.91           C  
ANISOU 2513  CA  PRO A 673     7050   8337   9654   1016  -1428   1035       C  
ATOM   2514  C   PRO A 673      12.382  82.901  21.103  1.00 65.50           C  
ANISOU 2514  C   PRO A 673     6924   8414   9547    933  -1659   1102       C  
ATOM   2515  O   PRO A 673      11.171  83.021  20.982  1.00 65.09           O  
ANISOU 2515  O   PRO A 673     6642   8457   9629    986  -1758   1156       O  
ATOM   2516  CB  PRO A 673      12.633  83.044  23.609  1.00 64.94           C  
ANISOU 2516  CB  PRO A 673     6775   8260   9639    974  -1266    933       C  
ATOM   2517  CG  PRO A 673      12.822  84.201  24.529  1.00 65.87           C  
ANISOU 2517  CG  PRO A 673     6892   8265   9871   1126  -1094    910       C  
ATOM   2518  CD  PRO A 673      12.413  85.397  23.724  1.00 68.27           C  
ANISOU 2518  CD  PRO A 673     7159   8521  10257   1297  -1211   1029       C  
ATOM   2519  N   ARG A 674      13.143  82.217  20.253  1.00 63.02           N  
ANISOU 2519  N   ARG A 674     6805   8104   9035    804  -1741   1097       N  
ATOM   2520  CA  ARG A 674      12.592  81.529  19.099  1.00 63.91           C  
ANISOU 2520  CA  ARG A 674     6892   8332   9059    702  -1960   1147       C  
ATOM   2521  C   ARG A 674      13.535  80.394  18.692  1.00 60.32           C  
ANISOU 2521  C   ARG A 674     6650   7872   8397    522  -1955   1071       C  
ATOM   2522  O   ARG A 674      14.759  80.550  18.709  1.00 58.66           O  
ANISOU 2522  O   ARG A 674     6653   7556   8078    519  -1851   1039       O  
ATOM   2523  CB  ARG A 674      12.422  82.526  17.942  1.00 67.23           C  
ANISOU 2523  CB  ARG A 674     7352   8739   9453    815  -2135   1289       C  
ATOM   2524  CG  ARG A 674      11.519  82.062  16.810  1.00 71.82           C  
ANISOU 2524  CG  ARG A 674     7842   9460   9983    744  -2390   1365       C  
ATOM   2525  CD  ARG A 674      11.583  83.023  15.620  1.00 75.21           C  
ANISOU 2525  CD  ARG A 674     8371   9862  10341    843  -2560   1511       C  
ATOM   2526  NE  ARG A 674      12.977  83.275  15.265  1.00 74.15           N  
ANISOU 2526  NE  ARG A 674     8535   9605  10032    822  -2474   1498       N  
ATOM   2527  CZ  ARG A 674      13.659  82.650  14.305  1.00 76.34           C  
ANISOU 2527  CZ  ARG A 674     9023   9900  10082    684  -2549   1486       C  
ATOM   2528  NH1 ARG A 674      13.079  81.749  13.513  1.00 78.78           N  
ANISOU 2528  NH1 ARG A 674     9300  10338  10292    549  -2728   1487       N  
ATOM   2529  NH2 ARG A 674      14.938  82.953  14.120  1.00 75.46           N  
ANISOU 2529  NH2 ARG A 674     9156   9675   9840    679  -2439   1469       N  
ATOM   2530  N   LEU A 675      12.954  79.251  18.351  1.00 59.84           N  
ANISOU 2530  N   LEU A 675     6523   7920   8291    371  -2061   1038       N  
ATOM   2531  CA  LEU A 675      13.693  78.137  17.764  1.00 58.89           C  
ANISOU 2531  CA  LEU A 675     6601   7798   7976    200  -2087    971       C  
ATOM   2532  C   LEU A 675      13.533  78.253  16.279  1.00 58.85           C  
ANISOU 2532  C   LEU A 675     6679   7846   7836    172  -2304   1054       C  
ATOM   2533  O   LEU A 675      12.430  78.423  15.812  1.00 61.87           O  
ANISOU 2533  O   LEU A 675     6892   8332   8282    187  -2475   1129       O  
ATOM   2534  CB  LEU A 675      13.089  76.805  18.199  1.00 59.89           C  
ANISOU 2534  CB  LEU A 675     6621   8005   8127     39  -2086    887       C  
ATOM   2535  CG  LEU A 675      13.249  76.449  19.675  1.00 57.81           C  
ANISOU 2535  CG  LEU A 675     6296   7700   7969     29  -1873    800       C  
ATOM   2536  CD1 LEU A 675      12.417  75.225  20.017  1.00 58.66           C  
ANISOU 2536  CD1 LEU A 675     6269   7899   8119   -129  -1898    743       C  
ATOM   2537  CD2 LEU A 675      14.710  76.223  19.980  1.00 57.14           C  
ANISOU 2537  CD2 LEU A 675     6451   7493   7767     10  -1723    733       C  
HETATM 2538  N   SEP A 676      14.604  78.152  15.516  1.00 57.36           N  
ANISOU 2538  N   SEP A 676     6742   7595   7456    126  -2302   1043       N  
HETATM 2539  CA  SEP A 676      14.426  78.353  14.106  1.00 60.95           C  
ANISOU 2539  CA  SEP A 676     7284   8103   7770    102  -2506   1129       C  
HETATM 2540  CB  SEP A 676      15.568  79.061  13.422  1.00 62.35           C  
ANISOU 2540  CB  SEP A 676     7705   8185   7800    154  -2472   1172       C  
HETATM 2541  OG  SEP A 676      16.886  79.052  13.953  1.00 59.77           O  
ANISOU 2541  OG  SEP A 676     7543   7739   7426    160  -2263   1096       O  
HETATM 2542  C   SEP A 676      14.028  77.113  13.370  1.00 61.38           C  
ANISOU 2542  C   SEP A 676     7366   8255   7698    -87  -2646   1077       C  
HETATM 2543  O   SEP A 676      14.082  75.995  13.892  1.00 58.57           O  
ANISOU 2543  O   SEP A 676     7005   7905   7344   -211  -2569    964       O  
HETATM 2544  P   SEP A 676      17.679  80.215  13.139  1.00 64.09           P  
ANISOU 2544  P   SEP A 676     8273   8207   7867    252  -2273   1196       P  
HETATM 2545  O1P SEP A 676      18.644  79.523  12.203  1.00 65.01           O  
ANISOU 2545  O1P SEP A 676     8635   8316   7749    123  -2269   1144       O  
HETATM 2546  O2P SEP A 676      18.288  81.045  14.233  1.00 59.29           O  
ANISOU 2546  O2P SEP A 676     7651   7485   7392    374  -2078   1183       O  
HETATM 2547  O3P SEP A 676      16.588  80.908  12.370  1.00 61.71           O  
ANISOU 2547  O3P SEP A 676     7867   7982   7597    320  -2490   1336       O  
ATOM   2548  N   PHE A 677      13.574  77.329  12.147  1.00 61.53           N  
ANISOU 2548  N   PHE A 677     7416   8353   7608   -110  -2863   1165       N  
ATOM   2549  CA  PHE A 677      13.206  76.244  11.279  1.00 63.78           C  
ANISOU 2549  CA  PHE A 677     7754   8733   7746   -299  -3019   1120       C  
ATOM   2550  C   PHE A 677      14.422  75.389  10.950  1.00 60.12           C  
ANISOU 2550  C   PHE A 677     7569   8190   7083   -421  -2907   1003       C  
ATOM   2551  O   PHE A 677      15.562  75.836  11.047  1.00 58.84           O  
ANISOU 2551  O   PHE A 677     7573   7917   6863   -350  -2757    993       O  
ATOM   2552  CB  PHE A 677      12.588  76.787   9.991  1.00 68.82           C  
ANISOU 2552  CB  PHE A 677     8397   9467   8283   -290  -3279   1250       C  
ATOM   2553  CG  PHE A 677      11.259  77.459  10.191  1.00 73.58           C  
ANISOU 2553  CG  PHE A 677     8703  10169   9084   -184  -3425   1366       C  
ATOM   2554  CD1 PHE A 677      11.044  78.763   9.753  1.00 77.69           C  
ANISOU 2554  CD1 PHE A 677     9192  10682   9643    -13  -3525   1524       C  
ATOM   2555  CD2 PHE A 677      10.210  76.776  10.795  1.00 76.19           C  
ANISOU 2555  CD2 PHE A 677     8781  10598   9567   -256  -3463   1321       C  
ATOM   2556  CE1 PHE A 677       9.804  79.372   9.917  1.00 80.80           C  
ANISOU 2556  CE1 PHE A 677     9300  11164  10233     98  -3663   1634       C  
ATOM   2557  CE2 PHE A 677       8.977  77.376  10.963  1.00 79.89           C  
ANISOU 2557  CE2 PHE A 677     8957  11167  10229   -155  -3593   1425       C  
ATOM   2558  CZ  PHE A 677       8.769  78.676  10.524  1.00 81.71           C  
ANISOU 2558  CZ  PHE A 677     9150  11389  10506     29  -3695   1581       C  
ATOM   2559  N   ALA A 678      14.145  74.147  10.584  1.00 59.87           N  
ANISOU 2559  N   ALA A 678     7575   8214   6959   -606  -2978    912       N  
ATOM   2560  CA  ALA A 678      15.140  73.214  10.105  1.00 58.68           C  
ANISOU 2560  CA  ALA A 678     7683   7997   6613   -734  -2900    796       C  
ATOM   2561  C   ALA A 678      14.952  72.964   8.615  1.00 60.20           C  
ANISOU 2561  C   ALA A 678     8025   8269   6579   -852  -3103    816       C  
ATOM   2562  O   ALA A 678      13.849  73.089   8.082  1.00 61.42           O  
ANISOU 2562  O   ALA A 678     8047   8548   6741   -891  -3325    890       O  
ATOM   2563  CB  ALA A 678      15.018  71.897  10.861  1.00 58.34           C  
ANISOU 2563  CB  ALA A 678     7599   7935   6632   -865  -2809    662       C  
ATOM   2564  N   ASP A 679      16.042  72.579   7.963  1.00 59.55           N  
ANISOU 2564  N   ASP A 679     8215   8115   6294   -914  -3023    743       N  
ATOM   2565  CA  ASP A 679      16.032  72.123   6.577  1.00 62.10           C  
ANISOU 2565  CA  ASP A 679     8729   8498   6368  -1056  -3176    723       C  
ATOM   2566  C   ASP A 679      15.398  70.729   6.478  1.00 64.69           C  
ANISOU 2566  C   ASP A 679     9039   8875   6664  -1258  -3256    603       C  
ATOM   2567  O   ASP A 679      16.049  69.726   6.757  1.00 64.94           O  
ANISOU 2567  O   ASP A 679     9195   8818   6660  -1343  -3107    462       O  
ATOM   2568  CB  ASP A 679      17.473  72.125   6.055  1.00 60.53           C  
ANISOU 2568  CB  ASP A 679     8819   8196   5982  -1051  -3017    666       C  
ATOM   2569  CG  ASP A 679      17.608  71.598   4.650  1.00 62.09           C  
ANISOU 2569  CG  ASP A 679     9249   8442   5900  -1203  -3135    623       C  
ATOM   2570  OD1 ASP A 679      16.710  70.896   4.141  1.00 64.95           O  
ANISOU 2570  OD1 ASP A 679     9580   8898   6197  -1352  -3318    591       O  
ATOM   2571  OD2 ASP A 679      18.653  71.887   4.046  1.00 62.34           O  
ANISOU 2571  OD2 ASP A 679     9501   8416   5769  -1182  -3035    615       O  
ATOM   2572  N   ARG A 680      14.135  70.688   6.070  1.00 68.60           N  
ANISOU 2572  N   ARG A 680     9377   9509   7177  -1333  -3494    662       N  
ATOM   2573  CA  ARG A 680      13.361  69.444   5.993  1.00 73.57           C  
ANISOU 2573  CA  ARG A 680     9955  10200   7796  -1537  -3596    561       C  
ATOM   2574  C   ARG A 680      14.007  68.338   5.168  1.00 74.47           C  
ANISOU 2574  C   ARG A 680    10360  10262   7670  -1718  -3572    413       C  
ATOM   2575  O   ARG A 680      13.893  67.165   5.511  1.00 75.32           O  
ANISOU 2575  O   ARG A 680    10484  10330   7802  -1859  -3520    283       O  
ATOM   2576  CB  ARG A 680      11.999  69.702   5.370  1.00 79.38           C  
ANISOU 2576  CB  ARG A 680    10511  11112   8538  -1598  -3892    663       C  
ATOM   2577  CG  ARG A 680      11.022  70.511   6.201  1.00 83.10           C  
ANISOU 2577  CG  ARG A 680    10640  11657   9276  -1458  -3945    787       C  
ATOM   2578  CD  ARG A 680       9.669  70.488   5.498  1.00 89.94           C  
ANISOU 2578  CD  ARG A 680    11330  12707  10135  -1557  -4252    865       C  
ATOM   2579  NE  ARG A 680       8.920  71.735   5.649  1.00 94.11           N  
ANISOU 2579  NE  ARG A 680    11610  13318  10828  -1372  -4369   1043       N  
ATOM   2580  CZ  ARG A 680       7.900  72.109   4.875  1.00 97.95           C  
ANISOU 2580  CZ  ARG A 680    11959  13963  11295  -1393  -4655   1162       C  
ATOM   2581  NH1 ARG A 680       7.483  71.341   3.873  1.00101.30           N  
ANISOU 2581  NH1 ARG A 680    12471  14491  11527  -1607  -4866   1121       N  
ATOM   2582  NH2 ARG A 680       7.291  73.270   5.103  1.00 99.97           N  
ANISOU 2582  NH2 ARG A 680    11987  14270  11725  -1196  -4735   1325       N  
ATOM   2583  N   ALA A 681      14.637  68.706   4.057  1.00 75.35           N  
ANISOU 2583  N   ALA A 681    10706  10375   7549  -1719  -3611    434       N  
ATOM   2584  CA  ALA A 681      15.241  67.720   3.158  1.00 75.57           C  
ANISOU 2584  CA  ALA A 681    11025  10359   7329  -1888  -3588    290       C  
ATOM   2585  C   ALA A 681      16.318  66.928   3.903  1.00 72.99           C  
ANISOU 2585  C   ALA A 681    10817   9863   7051  -1877  -3306    144       C  
ATOM   2586  O   ALA A 681      16.428  65.708   3.784  1.00 72.68           O  
ANISOU 2586  O   ALA A 681    10900   9768   6946  -2031  -3266     -6       O  
ATOM   2587  CB  ALA A 681      15.839  68.411   1.940  1.00 75.85           C  
ANISOU 2587  CB  ALA A 681    11288  10419   7112  -1865  -3641    350       C  
ATOM   2588  N   LEU A 682      17.102  67.651   4.679  1.00 69.61           N  
ANISOU 2588  N   LEU A 682    10350   9350   6747  -1691  -3118    193       N  
ATOM   2589  CA  LEU A 682      18.156  67.060   5.481  1.00 69.00           C  
ANISOU 2589  CA  LEU A 682    10356   9120   6740  -1650  -2856     81       C  
ATOM   2590  C   LEU A 682      17.605  66.225   6.639  1.00 68.11           C  
ANISOU 2590  C   LEU A 682    10071   8973   6834  -1698  -2808     21       C  
ATOM   2591  O   LEU A 682      18.101  65.130   6.923  1.00 67.54           O  
ANISOU 2591  O   LEU A 682    10111   8793   6756  -1776  -2679   -112       O  
ATOM   2592  CB  LEU A 682      19.038  68.177   6.020  1.00 65.67           C  
ANISOU 2592  CB  LEU A 682     9912   8637   6400  -1444  -2697    168       C  
ATOM   2593  CG  LEU A 682      20.535  67.955   5.983  1.00 64.76           C  
ANISOU 2593  CG  LEU A 682    10009   8393   6202  -1399  -2466     80       C  
ATOM   2594  CD1 LEU A 682      21.030  67.429   4.646  1.00 65.92           C  
ANISOU 2594  CD1 LEU A 682    10430   8538   6076  -1519  -2485     -6       C  
ATOM   2595  CD2 LEU A 682      21.216  69.272   6.335  1.00 63.44           C  
ANISOU 2595  CD2 LEU A 682     9802   8199   6100  -1213  -2364    194       C  
ATOM   2596  N   ILE A 683      16.577  66.748   7.298  1.00 67.71           N  
ANISOU 2596  N   ILE A 683     9749   9010   6967  -1650  -2906    122       N  
ATOM   2597  CA  ILE A 683      15.964  66.060   8.427  1.00 67.44           C  
ANISOU 2597  CA  ILE A 683     9533   8959   7132  -1697  -2860     82       C  
ATOM   2598  C   ILE A 683      15.379  64.746   7.920  1.00 69.43           C  
ANISOU 2598  C   ILE A 683     9854   9228   7295  -1929  -2967    -32       C  
ATOM   2599  O   ILE A 683      15.708  63.680   8.426  1.00 68.58           O  
ANISOU 2599  O   ILE A 683     9822   9011   7222  -2010  -2841   -147       O  
ATOM   2600  CB  ILE A 683      14.859  66.923   9.084  1.00 68.14           C  
ANISOU 2600  CB  ILE A 683     9308   9160   7421  -1609  -2959    213       C  
ATOM   2601  CG1 ILE A 683      15.447  68.208   9.695  1.00 66.18           C  
ANISOU 2601  CG1 ILE A 683     8997   8872   7274  -1380  -2835    314       C  
ATOM   2602  CG2 ILE A 683      14.105  66.137  10.144  1.00 68.57           C  
ANISOU 2602  CG2 ILE A 683     9173   9217   7661  -1691  -2924    168       C  
ATOM   2603  CD1 ILE A 683      16.457  67.988  10.798  1.00 63.40           C  
ANISOU 2603  CD1 ILE A 683     8693   8380   7015  -1300  -2580    252       C  
ATOM   2604  N   ASN A 684      14.543  64.835   6.889  1.00 72.38           N  
ANISOU 2604  N   ASN A 684    10217   9734   7550  -2039  -3205      2       N  
ATOM   2605  CA  ASN A 684      13.893  63.661   6.304  1.00 74.69           C  
ANISOU 2605  CA  ASN A 684    10574  10059   7743  -2279  -3338   -103       C  
ATOM   2606  C   ASN A 684      14.838  62.619   5.723  1.00 74.69           C  
ANISOU 2606  C   ASN A 684    10896   9927   7557  -2391  -3227   -268       C  
ATOM   2607  O   ASN A 684      14.448  61.470   5.565  1.00 75.59           O  
ANISOU 2607  O   ASN A 684    11073  10013   7633  -2585  -3271   -383       O  
ATOM   2608  CB  ASN A 684      12.927  64.088   5.197  1.00 78.72           C  
ANISOU 2608  CB  ASN A 684    11030  10747   8131  -2366  -3629    -24       C  
ATOM   2609  CG  ASN A 684      11.756  64.885   5.718  1.00 79.98           C  
ANISOU 2609  CG  ASN A 684    10846  11049   8493  -2291  -3770    122       C  
ATOM   2610  OD1 ASN A 684      11.200  65.712   5.007  1.00 83.08           O  
ANISOU 2610  OD1 ASN A 684    11163  11574   8829  -2254  -3971    242       O  
ATOM   2611  ND2 ASN A 684      11.384  64.652   6.968  1.00 79.71           N  
ANISOU 2611  ND2 ASN A 684    10602  10987   8696  -2262  -3661    118       N  
ATOM   2612  N   SER A 685      16.061  63.017   5.393  1.00 74.24           N  
ANISOU 2612  N   SER A 685    11037   9785   7385  -2273  -3082   -281       N  
ATOM   2613  CA  SER A 685      17.008  62.125   4.732  1.00 75.91           C  
ANISOU 2613  CA  SER A 685    11556   9875   7409  -2359  -2968   -436       C  
ATOM   2614  C   SER A 685      18.059  61.532   5.657  1.00 73.67           C  
ANISOU 2614  C   SER A 685    11345   9408   7235  -2278  -2698   -523       C  
ATOM   2615  O   SER A 685      18.665  60.521   5.323  1.00 74.59           O  
ANISOU 2615  O   SER A 685    11681   9407   7252  -2366  -2598   -669       O  
ATOM   2616  CB  SER A 685      17.712  62.867   3.602  1.00 76.56           C  
ANISOU 2616  CB  SER A 685    11833   9990   7265  -2302  -2982   -404       C  
ATOM   2617  OG  SER A 685      16.783  63.190   2.592  1.00 80.69           O  
ANISOU 2617  OG  SER A 685    12342  10672   7642  -2412  -3246   -342       O  
ATOM   2618  N   MET A 686      18.297  62.158   6.800  1.00 73.17           N  
ANISOU 2618  N   MET A 686    11107   9318   7373  -2108  -2579   -436       N  
ATOM   2619  CA  MET A 686      19.314  61.653   7.705  1.00 73.18           C  
ANISOU 2619  CA  MET A 686    11169   9156   7478  -2023  -2338   -503       C  
ATOM   2620  C   MET A 686      18.772  60.475   8.495  1.00 72.19           C  
ANISOU 2620  C   MET A 686    10982   8961   7483  -2145  -2317   -578       C  
ATOM   2621  O   MET A 686      17.566  60.308   8.663  1.00 69.60           O  
ANISOU 2621  O   MET A 686    10489   8726   7226  -2257  -2469   -546       O  
ATOM   2622  CB  MET A 686      19.830  62.748   8.648  1.00 71.81           C  
ANISOU 2622  CB  MET A 686    10850   8978   7456  -1808  -2218   -388       C  
ATOM   2623  CG  MET A 686      18.824  63.245   9.670  1.00 73.12           C  
ANISOU 2623  CG  MET A 686    10726   9226   7830  -1767  -2283   -281       C  
ATOM   2624  SD  MET A 686      19.427  64.627  10.669  1.00 75.85           S  
ANISOU 2624  SD  MET A 686    10928   9564   8327  -1521  -2149   -157       S  
ATOM   2625  CE  MET A 686      17.962  64.915  11.653  1.00 76.54           C  
ANISOU 2625  CE  MET A 686    10693   9759   8630  -1530  -2251    -68       C  
ATOM   2626  N   ASP A 687      19.693  59.665   8.985  1.00 73.52           N  
ANISOU 2626  N   ASP A 687    11282   8964   7687  -2121  -2126   -672       N  
ATOM   2627  CA  ASP A 687      19.358  58.566   9.865  1.00 73.30           C  
ANISOU 2627  CA  ASP A 687    11215   8839   7794  -2213  -2073   -731       C  
ATOM   2628  C   ASP A 687      19.082  59.128  11.258  1.00 72.46           C  
ANISOU 2628  C   ASP A 687    10861   8762   7909  -2098  -2016   -617       C  
ATOM   2629  O   ASP A 687      20.001  59.625  11.910  1.00 69.14           O  
ANISOU 2629  O   ASP A 687    10432   8282   7555  -1928  -1863   -577       O  
ATOM   2630  CB  ASP A 687      20.547  57.614   9.918  1.00 73.31           C  
ANISOU 2630  CB  ASP A 687    11445   8644   7763  -2193  -1881   -854       C  
ATOM   2631  CG  ASP A 687      20.310  56.431  10.818  1.00 73.33           C  
ANISOU 2631  CG  ASP A 687    11441   8520   7901  -2282  -1815   -910       C  
ATOM   2632  OD1 ASP A 687      19.164  56.233  11.273  1.00 72.77           O  
ANISOU 2632  OD1 ASP A 687    11207   8518   7925  -2398  -1925   -872       O  
ATOM   2633  OD2 ASP A 687      21.284  55.697  11.063  1.00 75.05           O  
ANISOU 2633  OD2 ASP A 687    11816   8567   8132  -2235  -1651   -989       O  
ATOM   2634  N   GLN A 688      17.839  59.043  11.734  1.00 74.40           N  
ANISOU 2634  N   GLN A 688    10903   9098   8266  -2195  -2131   -570       N  
ATOM   2635  CA  GLN A 688      17.537  59.526  13.100  1.00 72.75           C  
ANISOU 2635  CA  GLN A 688    10463   8915   8261  -2096  -2060   -473       C  
ATOM   2636  C   GLN A 688      18.270  58.724  14.192  1.00 73.11           C  
ANISOU 2636  C   GLN A 688    10574   8794   8409  -2065  -1866   -516       C  
ATOM   2637  O   GLN A 688      18.724  59.292  15.213  1.00 69.18           O  
ANISOU 2637  O   GLN A 688     9982   8278   8025  -1915  -1745   -448       O  
ATOM   2638  CB  GLN A 688      16.025  59.594  13.377  1.00 74.02           C  
ANISOU 2638  CB  GLN A 688    10378   9217   8527  -2208  -2212   -415       C  
ATOM   2639  CG  GLN A 688      15.336  60.827  12.774  1.00 72.49           C  
ANISOU 2639  CG  GLN A 688    10026   9203   8311  -2146  -2379   -310       C  
ATOM   2640  CD  GLN A 688      15.800  62.158  13.376  1.00 69.25           C  
ANISOU 2640  CD  GLN A 688     9505   8820   7986  -1915  -2290   -201       C  
ATOM   2641  OE1 GLN A 688      16.644  62.203  14.291  1.00 64.94           O  
ANISOU 2641  OE1 GLN A 688     8989   8170   7514  -1802  -2105   -203       O  
ATOM   2642  NE2 GLN A 688      15.238  63.252  12.872  1.00 66.83           N  
ANISOU 2642  NE2 GLN A 688     9070   8649   7670  -1845  -2427   -103       N  
ATOM   2643  N   ASN A 689      18.439  57.423  13.963  1.00 70.70           N  
ANISOU 2643  N   ASN A 689    10445   8361   8056  -2201  -1836   -630       N  
ATOM   2644  CA  ASN A 689      19.294  56.626  14.848  1.00 68.60           C  
ANISOU 2644  CA  ASN A 689    10280   7916   7867  -2156  -1655   -670       C  
ATOM   2645  C   ASN A 689      20.626  57.253  15.215  1.00 63.91           C  
ANISOU 2645  C   ASN A 689     9738   7261   7282  -1941  -1500   -638       C  
ATOM   2646  O   ASN A 689      21.225  56.843  16.187  1.00 63.32           O  
ANISOU 2646  O   ASN A 689     9680   7074   7304  -1877  -1365   -632       O  
ATOM   2647  CB  ASN A 689      19.544  55.229  14.276  1.00 70.26           C  
ANISOU 2647  CB  ASN A 689    10727   7972   7995  -2301  -1634   -809       C  
ATOM   2648  CG  ASN A 689      18.430  54.282  14.606  1.00 72.27           C  
ANISOU 2648  CG  ASN A 689    10925   8214   8319  -2511  -1709   -836       C  
ATOM   2649  OD1 ASN A 689      17.723  54.487  15.584  1.00 75.33           O  
ANISOU 2649  OD1 ASN A 689    11108   8668   8847  -2523  -1715   -751       O  
ATOM   2650  ND2 ASN A 689      18.262  53.245  13.801  1.00 75.05           N  
ANISOU 2650  ND2 ASN A 689    11459   8482   8573  -2684  -1761   -958       N  
ATOM   2651  N   MET A 690      21.098  58.228  14.446  1.00 63.47           N  
ANISOU 2651  N   MET A 690     9710   7278   7126  -1837  -1523   -614       N  
ATOM   2652  CA  MET A 690      22.282  59.004  14.842  1.00 63.43           C  
ANISOU 2652  CA  MET A 690     9715   7240   7142  -1637  -1385   -568       C  
ATOM   2653  C   MET A 690      22.264  59.509  16.281  1.00 57.34           C  
ANISOU 2653  C   MET A 690     8763   6483   6540  -1533  -1308   -472       C  
ATOM   2654  O   MET A 690      23.309  59.575  16.927  1.00 56.84           O  
ANISOU 2654  O   MET A 690     8738   6336   6523  -1411  -1168   -463       O  
ATOM   2655  CB  MET A 690      22.439  60.217  13.943  1.00 67.76           C  
ANISOU 2655  CB  MET A 690    10258   7903   7583  -1557  -1450   -519       C  
ATOM   2656  CG  MET A 690      23.684  60.189  13.086  1.00 70.37           C  
ANISOU 2656  CG  MET A 690    10798   8161   7777  -1494  -1357   -586       C  
ATOM   2657  SD  MET A 690      23.578  61.397  11.770  1.00 76.88           S  
ANISOU 2657  SD  MET A 690    11650   9126   8434  -1469  -1473   -536       S  
ATOM   2658  CE  MET A 690      22.507  62.646  12.488  1.00 74.26           C  
ANISOU 2658  CE  MET A 690    11035   8943   8237  -1407  -1587   -380       C  
ATOM   2659  N   PHE A 691      21.090  59.891  16.769  1.00 54.85           N  
ANISOU 2659  N   PHE A 691     8248   6280   6312  -1582  -1399   -403       N  
ATOM   2660  CA  PHE A 691      20.961  60.396  18.138  1.00 54.19           C  
ANISOU 2660  CA  PHE A 691     7990   6219   6377  -1496  -1323   -319       C  
ATOM   2661  C   PHE A 691      20.310  59.380  19.083  1.00 53.37           C  
ANISOU 2661  C   PHE A 691     7832   6066   6379  -1616  -1297   -331       C  
ATOM   2662  O   PHE A 691      19.658  59.760  20.053  1.00 48.96           O  
ANISOU 2662  O   PHE A 691     7092   5575   5933  -1606  -1283   -262       O  
ATOM   2663  CB  PHE A 691      20.169  61.704  18.118  1.00 54.16           C  
ANISOU 2663  CB  PHE A 691     7787   6375   6413  -1435  -1414   -226       C  
ATOM   2664  CG  PHE A 691      20.764  62.742  17.204  1.00 53.47           C  
ANISOU 2664  CG  PHE A 691     7759   6331   6224  -1323  -1443   -201       C  
ATOM   2665  CD1 PHE A 691      20.192  63.007  15.960  1.00 55.95           C  
ANISOU 2665  CD1 PHE A 691     8093   6734   6428  -1385  -1598   -201       C  
ATOM   2666  CD2 PHE A 691      21.925  63.413  17.563  1.00 51.81           C  
ANISOU 2666  CD2 PHE A 691     7595   6070   6017  -1167  -1317   -176       C  
ATOM   2667  CE1 PHE A 691      20.752  63.956  15.119  1.00 54.39           C  
ANISOU 2667  CE1 PHE A 691     7966   6572   6128  -1289  -1620   -168       C  
ATOM   2668  CE2 PHE A 691      22.489  64.363  16.723  1.00 51.97           C  
ANISOU 2668  CE2 PHE A 691     7677   6125   5944  -1077  -1335   -148       C  
ATOM   2669  CZ  PHE A 691      21.901  64.631  15.502  1.00 51.22           C  
ANISOU 2669  CZ  PHE A 691     7609   6114   5738  -1136  -1483   -142       C  
ATOM   2670  N   ARG A 692      20.483  58.087  18.803  1.00 55.52           N  
ANISOU 2670  N   ARG A 692     8268   6216   6611  -1734  -1283   -418       N  
ATOM   2671  CA  ARG A 692      19.917  57.072  19.691  1.00 57.41           C  
ANISOU 2671  CA  ARG A 692     8477   6388   6945  -1858  -1251   -424       C  
ATOM   2672  C   ARG A 692      20.597  57.152  21.061  1.00 52.59           C  
ANISOU 2672  C   ARG A 692     7836   5710   6433  -1742  -1104   -365       C  
ATOM   2673  O   ARG A 692      21.798  57.459  21.182  1.00 48.00           O  
ANISOU 2673  O   ARG A 692     7341   5064   5831  -1593  -1011   -361       O  
ATOM   2674  CB  ARG A 692      19.955  55.649  19.093  1.00 65.87           C  
ANISOU 2674  CB  ARG A 692     9748   7322   7958  -2013  -1266   -532       C  
ATOM   2675  CG  ARG A 692      21.113  54.743  19.500  1.00 71.56           C  
ANISOU 2675  CG  ARG A 692    10659   7840   8689  -1959  -1124   -577       C  
ATOM   2676  CD  ARG A 692      20.863  53.292  19.049  1.00 79.19           C  
ANISOU 2676  CD  ARG A 692    11800   8664   9625  -2138  -1144   -680       C  
ATOM   2677  NE  ARG A 692      20.175  52.467  20.061  1.00 87.03           N  
ANISOU 2677  NE  ARG A 692    12741   9597  10729  -2265  -1122   -649       N  
ATOM   2678  CZ  ARG A 692      20.770  51.670  20.964  1.00 92.00           C  
ANISOU 2678  CZ  ARG A 692    13464  10061  11431  -2237  -1004   -635       C  
ATOM   2679  NH1 ARG A 692      22.097  51.551  21.025  1.00 92.76           N  
ANISOU 2679  NH1 ARG A 692    13698  10031  11514  -2077   -897   -650       N  
ATOM   2680  NH2 ARG A 692      20.028  50.974  21.827  1.00 94.32           N  
ANISOU 2680  NH2 ARG A 692    13707  10315  11812  -2372   -994   -598       N  
ATOM   2681  N   ASN A 693      19.773  56.940  22.076  1.00 51.35           N  
ANISOU 2681  N   ASN A 693     7543   5585   6380  -1817  -1089   -315       N  
ATOM   2682  CA  ASN A 693      20.146  57.049  23.475  1.00 49.13           C  
ANISOU 2682  CA  ASN A 693     7209   5270   6188  -1738   -967   -249       C  
ATOM   2683  C   ASN A 693      20.517  58.455  23.914  1.00 45.25           C  
ANISOU 2683  C   ASN A 693     6596   4877   5718  -1562   -926   -180       C  
ATOM   2684  O   ASN A 693      21.117  58.611  24.968  1.00 43.25           O  
ANISOU 2684  O   ASN A 693     6337   4584   5510  -1476   -821   -136       O  
ATOM   2685  CB  ASN A 693      21.285  56.087  23.813  1.00 50.63           C  
ANISOU 2685  CB  ASN A 693     7598   5271   6368  -1704   -864   -278       C  
ATOM   2686  CG  ASN A 693      20.981  54.671  23.397  1.00 54.10           C  
ANISOU 2686  CG  ASN A 693     8180   5584   6791  -1872   -892   -352       C  
ATOM   2687  OD1 ASN A 693      19.855  54.199  23.533  1.00 58.15           O  
ANISOU 2687  OD1 ASN A 693     8619   6133   7342  -2040   -947   -352       O  
ATOM   2688  ND2 ASN A 693      21.985  53.982  22.893  1.00 56.49           N  
ANISOU 2688  ND2 ASN A 693     8688   5733   7043  -1831   -847   -418       N  
ATOM   2689  N   PHE A 694      20.145  59.471  23.141  1.00 43.28           N  
ANISOU 2689  N   PHE A 694     6256   4751   5436  -1515  -1013   -169       N  
ATOM   2690  CA  PHE A 694      20.349  60.855  23.593  1.00 41.68           C  
ANISOU 2690  CA  PHE A 694     5929   4638   5267  -1359   -977   -102       C  
ATOM   2691  C   PHE A 694      19.528  61.136  24.824  1.00 41.32           C  
ANISOU 2691  C   PHE A 694     5702   4663   5333  -1377   -930    -44       C  
ATOM   2692  O   PHE A 694      19.993  61.835  25.715  1.00 37.62           O  
ANISOU 2692  O   PHE A 694     5188   4202   4902  -1263   -838      0       O  
ATOM   2693  CB  PHE A 694      19.975  61.875  22.526  1.00 42.46           C  
ANISOU 2693  CB  PHE A 694     5962   4849   5318  -1312  -1088    -88       C  
ATOM   2694  CG  PHE A 694      20.239  63.299  22.931  1.00 40.60           C  
ANISOU 2694  CG  PHE A 694     5624   4681   5120  -1149  -1047    -23       C  
ATOM   2695  CD1 PHE A 694      21.539  63.789  22.976  1.00 39.27           C  
ANISOU 2695  CD1 PHE A 694     5562   4449   4909  -1018   -964    -21       C  
ATOM   2696  CD2 PHE A 694      19.193  64.153  23.254  1.00 40.67           C  
ANISOU 2696  CD2 PHE A 694     5426   4813   5212  -1129  -1089     32       C  
ATOM   2697  CE1 PHE A 694      21.787  65.090  23.356  1.00 38.80           C  
ANISOU 2697  CE1 PHE A 694     5418   4440   4883   -883   -925     33       C  
ATOM   2698  CE2 PHE A 694      19.431  65.460  23.594  1.00 39.79           C  
ANISOU 2698  CE2 PHE A 694     5235   4745   5136   -979  -1048     84       C  
ATOM   2699  CZ  PHE A 694      20.733  65.934  23.663  1.00 38.45           C  
ANISOU 2699  CZ  PHE A 694     5186   4503   4918   -862   -966     84       C  
HETATM 2700  N   SEP A 695      18.313  60.607  24.877  1.00 40.77           N  
ANISOU 2700  N   SEP A 695     5526   4650   5312  -1525   -989    -46       N  
HETATM 2701  CA  SEP A 695      17.398  60.968  25.935  1.00 43.62           C  
ANISOU 2701  CA  SEP A 695     5689   5102   5779  -1545   -943      5       C  
HETATM 2702  CB  SEP A 695      15.979  60.473  25.674  1.00 45.31           C  
ANISOU 2702  CB  SEP A 695     5764   5405   6045  -1717  -1035     -1       C  
HETATM 2703  OG  SEP A 695      15.385  61.413  24.789  1.00 46.70           O  
ANISOU 2703  OG  SEP A 695     5813   5708   6221  -1667  -1156     14       O  
HETATM 2704  C   SEP A 695      17.838  60.422  27.266  1.00 44.96           C  
ANISOU 2704  C   SEP A 695     5910   5189   5984  -1555   -804     25       C  
HETATM 2705  O   SEP A 695      18.299  59.284  27.365  1.00 45.81           O  
ANISOU 2705  O   SEP A 695     6173   5169   6061  -1633   -776     -1       O  
HETATM 2706  P   SEP A 695      14.021  60.990  24.020  1.00 53.02           P  
ANISOU 2706  P   SEP A 695     6482   6616   7047  -1838  -1312      0       P  
HETATM 2707  O1P SEP A 695      13.554  62.200  23.210  1.00 51.87           O  
ANISOU 2707  O1P SEP A 695     6199   6604   6905  -1735  -1434     41       O  
HETATM 2708  O2P SEP A 695      14.491  59.792  23.258  1.00 54.20           O  
ANISOU 2708  O2P SEP A 695     6855   6646   7092  -1963  -1359    -75       O  
HETATM 2709  O3P SEP A 695      13.138  60.724  25.190  1.00 52.21           O  
ANISOU 2709  O3P SEP A 695     6206   6565   7065  -1922  -1230     29       O  
ATOM   2710  N   PHE A 696      17.638  61.215  28.306  1.00 44.90           N  
ANISOU 2710  N   PHE A 696     5771   5248   6038  -1481   -719     74       N  
ATOM   2711  CA  PHE A 696      18.046  60.839  29.650  1.00 48.17           C  
ANISOU 2711  CA  PHE A 696     6230   5601   6472  -1485   -588    104       C  
ATOM   2712  C   PHE A 696      17.276  61.702  30.633  1.00 47.22           C  
ANISOU 2712  C   PHE A 696     5913   5599   6426  -1454   -515    145       C  
ATOM   2713  O   PHE A 696      17.081  62.907  30.417  1.00 43.31           O  
ANISOU 2713  O   PHE A 696     5303   5195   5959  -1339   -531    155       O  
ATOM   2714  CB  PHE A 696      19.561  61.064  29.795  1.00 52.57           C  
ANISOU 2714  CB  PHE A 696     6947   6060   6966  -1345   -534    105       C  
ATOM   2715  CG  PHE A 696      20.103  60.766  31.164  1.00 61.64           C  
ANISOU 2715  CG  PHE A 696     8149   7150   8120  -1334   -416    144       C  
ATOM   2716  CD1 PHE A 696      20.662  59.531  31.451  1.00 65.61           C  
ANISOU 2716  CD1 PHE A 696     8811   7519   8599  -1400   -390    146       C  
ATOM   2717  CD2 PHE A 696      20.081  61.738  32.156  1.00 65.26           C  
ANISOU 2717  CD2 PHE A 696     8509   7683   8604  -1253   -334    180       C  
ATOM   2718  CE1 PHE A 696      21.172  59.263  32.709  1.00 70.18           C  
ANISOU 2718  CE1 PHE A 696     9444   8046   9173  -1388   -296    195       C  
ATOM   2719  CE2 PHE A 696      20.577  61.471  33.413  1.00 68.85           C  
ANISOU 2719  CE2 PHE A 696     9022   8092   9045  -1252   -236    218       C  
ATOM   2720  CZ  PHE A 696      21.121  60.234  33.693  1.00 69.03           C  
ANISOU 2720  CZ  PHE A 696     9198   7990   9039  -1320   -223    232       C  
ATOM   2721  N   MET A 697      16.814  61.096  31.713  1.00 49.27           N  
ANISOU 2721  N   MET A 697     6141   5856   6722  -1557   -427    168       N  
ATOM   2722  CA  MET A 697      16.190  61.878  32.766  1.00 51.89           C  
ANISOU 2722  CA  MET A 697     6308   6292   7116  -1525   -327    199       C  
ATOM   2723  C   MET A 697      16.573  61.492  34.186  1.00 50.58           C  
ANISOU 2723  C   MET A 697     6213   6076   6928  -1554   -191    232       C  
ATOM   2724  O   MET A 697      16.469  60.319  34.571  1.00 52.72           O  
ANISOU 2724  O   MET A 697     6566   6277   7186  -1693   -167    246       O  
ATOM   2725  CB  MET A 697      14.681  61.824  32.660  1.00 54.81           C  
ANISOU 2725  CB  MET A 697     6466   6784   7575  -1640   -355    199       C  
ATOM   2726  CG  MET A 697      14.088  62.949  33.480  1.00 58.27           C  
ANISOU 2726  CG  MET A 697     6715   7339   8084  -1554   -259    218       C  
ATOM   2727  SD  MET A 697      12.369  63.106  33.139  1.00 71.94           S  
ANISOU 2727  SD  MET A 697     8160   9231   9941  -1645   -309    219       S  
ATOM   2728  CE  MET A 697      12.246  64.829  32.692  1.00 71.84           C  
ANISOU 2728  CE  MET A 697     8000   9310   9985  -1425   -342    224       C  
ATOM   2729  N   ASN A 698      16.929  62.480  34.992  1.00 49.91           N  
ANISOU 2729  N   ASN A 698     6095   6031   6838  -1436   -101    247       N  
ATOM   2730  CA AASN A 698      17.306  62.174  36.368  0.50 50.41           C  
ANISOU 2730  CA AASN A 698     6232   6058   6861  -1466     22    281       C  
ATOM   2731  CA BASN A 698      17.294  62.227  36.390  0.50 51.86           C  
ANISOU 2731  CA BASN A 698     6410   6246   7046  -1462     25    281       C  
ATOM   2732  C   ASN A 698      16.048  62.044  37.237  1.00 52.19           C  
ANISOU 2732  C   ASN A 698     6304   6380   7144  -1585    117    296       C  
ATOM   2733  O   ASN A 698      14.992  62.562  36.875  1.00 51.90           O  
ANISOU 2733  O   ASN A 698     6073   6454   7190  -1592    102    277       O  
ATOM   2734  CB AASN A 698      18.387  63.138  36.907  0.50 48.37           C  
ANISOU 2734  CB AASN A 698     6041   5784   6550  -1309     75    286       C  
ATOM   2735  CB BASN A 698      18.137  63.365  36.948  0.50 51.95           C  
ANISOU 2735  CB BASN A 698     6448   6268   7020  -1304     85    282       C  
ATOM   2736  CG AASN A 698      17.831  64.357  37.621  0.50 48.20           C  
ANISOU 2736  CG AASN A 698     5871   5874   6567  -1240    169    276       C  
ATOM   2737  CG BASN A 698      19.522  63.394  36.352  0.50 52.27           C  
ANISOU 2737  CG BASN A 698     6650   6210   6998  -1200     19    276       C  
ATOM   2738  OD1AASN A 698      16.652  64.668  37.543  0.50 47.65           O  
ANISOU 2738  OD1AASN A 698     5623   5903   6577  -1274    186    264       O  
ATOM   2739  OD1BASN A 698      19.944  64.397  35.794  0.50 55.60           O  
ANISOU 2739  OD1BASN A 698     7051   6652   7420  -1073    -13    256       O  
ATOM   2740  ND2AASN A 698      18.717  65.072  38.321  0.50 47.55           N  
ANISOU 2740  ND2AASN A 698     5861   5775   6430  -1140    232    278       N  
ATOM   2741  ND2BASN A 698      20.237  62.285  36.464  0.50 53.98           N  
ANISOU 2741  ND2BASN A 698     7029   6315   7166  -1254      5    298       N  
ATOM   2742  N   PRO A 699      16.155  61.299  38.364  1.00 53.50           N  
ANISOU 2742  N   PRO A 699     6557   6504   7266  -1684    214    335       N  
ATOM   2743  CA  PRO A 699      14.974  61.031  39.208  1.00 55.41           C  
ANISOU 2743  CA  PRO A 699     6667   6832   7552  -1822    320    352       C  
ATOM   2744  C   PRO A 699      14.241  62.280  39.720  1.00 52.49           C  
ANISOU 2744  C   PRO A 699     6098   6606   7240  -1746    418    329       C  
ATOM   2745  O   PRO A 699      13.016  62.283  39.778  1.00 51.09           O  
ANISOU 2745  O   PRO A 699     5732   6532   7147  -1831    458    321       O  
ATOM   2746  CB  PRO A 699      15.558  60.242  40.396  1.00 58.38           C  
ANISOU 2746  CB  PRO A 699     7216   7125   7839  -1899    410    408       C  
ATOM   2747  CG  PRO A 699      16.820  59.634  39.882  1.00 57.62           C  
ANISOU 2747  CG  PRO A 699     7331   6878   7682  -1848    314    422       C  
ATOM   2748  CD  PRO A 699      17.364  60.629  38.893  1.00 55.10           C  
ANISOU 2748  CD  PRO A 699     6981   6576   7377  -1676    227    373       C  
ATOM   2749  N   GLY A 700      14.995  63.315  40.076  1.00 50.78           N  
ANISOU 2749  N   GLY A 700     5921   6390   6981  -1589    458    316       N  
ATOM   2750  CA  GLY A 700      14.422  64.562  40.609  1.00 51.91           C  
ANISOU 2750  CA  GLY A 700     5903   6645   7173  -1499    563    285       C  
ATOM   2751  C   GLY A 700      13.597  65.275  39.549  1.00 51.23           C  
ANISOU 2751  C   GLY A 700     5617   6640   7207  -1427    483    254       C  
ATOM   2752  O   GLY A 700      12.482  65.722  39.801  1.00 51.07           O  
ANISOU 2752  O   GLY A 700     5392   6731   7281  -1438    555    239       O  
ATOM   2753  N   MET A 701      14.142  65.356  38.344  1.00 48.82           N  
ANISOU 2753  N   MET A 701     5370   6281   6898  -1355    332    249       N  
ATOM   2754  CA  MET A 701      13.379  65.887  37.237  1.00 50.08           C  
ANISOU 2754  CA  MET A 701     5360   6512   7156  -1304    227    234       C  
ATOM   2755  C   MET A 701      12.112  65.055  37.002  1.00 51.27           C  
ANISOU 2755  C   MET A 701     5355   6737   7385  -1469    198    242       C  
ATOM   2756  O   MET A 701      11.010  65.616  36.909  1.00 51.68           O  
ANISOU 2756  O   MET A 701     5177   6909   7551  -1452    212    235       O  
ATOM   2757  CB  MET A 701      14.221  65.960  35.965  1.00 49.48           C  
ANISOU 2757  CB  MET A 701     5402   6360   7035  -1225     70    231       C  
ATOM   2758  CG  MET A 701      13.578  66.834  34.882  1.00 50.63           C  
ANISOU 2758  CG  MET A 701     5389   6583   7266  -1132    -37    225       C  
ATOM   2759  SD  MET A 701      13.614  68.580  35.307  1.00 51.91           S  
ANISOU 2759  SD  MET A 701     5454   6786   7482   -925     49    215       S  
ATOM   2760  CE  MET A 701      12.662  69.225  33.935  1.00 54.92           C  
ANISOU 2760  CE  MET A 701     5641   7253   7970   -856   -108    231       C  
ATOM   2761  N   GLU A 702      12.252  63.726  36.938  1.00 51.50           N  
ANISOU 2761  N   GLU A 702     5505   6697   7365  -1630    163    256       N  
ATOM   2762  CA  GLU A 702      11.086  62.857  36.709  1.00 54.79           C  
ANISOU 2762  CA  GLU A 702     5789   7176   7853  -1813    131    261       C  
ATOM   2763  C   GLU A 702       9.986  63.093  37.747  1.00 55.92           C  
ANISOU 2763  C   GLU A 702     5728   7440   8077  -1874    286    267       C  
ATOM   2764  O   GLU A 702       8.801  63.073  37.411  1.00 56.02           O  
ANISOU 2764  O   GLU A 702     5517   7566   8199  -1946    258    262       O  
ATOM   2765  CB  GLU A 702      11.445  61.360  36.692  1.00 57.01           C  
ANISOU 2765  CB  GLU A 702     6256   7339   8064  -1986    100    276       C  
ATOM   2766  CG  GLU A 702      10.196  60.461  36.783  1.00 61.67           C  
ANISOU 2766  CG  GLU A 702     6709   7993   8727  -2204    110    284       C  
ATOM   2767  CD  GLU A 702      10.467  58.981  36.670  1.00 65.13           C  
ANISOU 2767  CD  GLU A 702     7334   8301   9109  -2384     71    296       C  
ATOM   2768  OE1 GLU A 702      11.628  58.590  36.490  1.00 70.73           O  
ANISOU 2768  OE1 GLU A 702     8279   8867   9728  -2332     33    298       O  
ATOM   2769  OE2 GLU A 702       9.509  58.184  36.763  1.00 73.41           O  
ANISOU 2769  OE2 GLU A 702     8293   9387  10212  -2580     81    303       O  
ATOM   2770  N   ARG A 703      10.373  63.279  39.006  1.00 55.74           N  
ANISOU 2770  N   ARG A 703     5781   7401   7997  -1854    450    275       N  
ATOM   2771  CA  ARG A 703       9.404  63.629  40.044  1.00 58.52           C  
ANISOU 2771  CA  ARG A 703     5950   7870   8413  -1895    623    271       C  
ATOM   2772  C   ARG A 703       8.661  64.931  39.730  1.00 58.31           C  
ANISOU 2772  C   ARG A 703     5677   7964   8512  -1743    632    239       C  
ATOM   2773  O   ARG A 703       7.451  64.984  39.872  1.00 59.33           O  
ANISOU 2773  O   ARG A 703     5569   8216   8757  -1805    689    234       O  
ATOM   2774  CB  ARG A 703      10.083  63.748  41.413  1.00 60.87           C  
ANISOU 2774  CB  ARG A 703     6399   8125   8601  -1880    790    280       C  
ATOM   2775  CG  ARG A 703       9.128  64.142  42.531  1.00 63.22           C  
ANISOU 2775  CG  ARG A 703     6528   8543   8947  -1921    992    266       C  
ATOM   2776  CD  ARG A 703       9.785  64.001  43.890  1.00 64.60           C  
ANISOU 2776  CD  ARG A 703     6887   8673   8984  -1955   1145    282       C  
ATOM   2777  NE  ARG A 703       9.776  62.603  44.317  1.00 67.44           N  
ANISOU 2777  NE  ARG A 703     7371   8977   9275  -2164   1162    339       N  
ATOM   2778  CZ  ARG A 703      10.838  61.804  44.386  1.00 67.96           C  
ANISOU 2778  CZ  ARG A 703     7692   8904   9223  -2202   1093    385       C  
ATOM   2779  NH1 ARG A 703      12.065  62.239  44.071  1.00 68.57           N  
ANISOU 2779  NH1 ARG A 703     7928   8893   9232  -2050   1003    379       N  
ATOM   2780  NH2 ARG A 703      10.666  60.547  44.793  1.00 69.37           N  
ANISOU 2780  NH2 ARG A 703     7966   9032   9359  -2397   1118    441       N  
ATOM   2781  N   LEU A 704       9.380  65.981  39.336  1.00 57.92           N  
ANISOU 2781  N   LEU A 704     5681   7877   8446  -1545    584    222       N  
ATOM   2782  CA  LEU A 704       8.744  67.280  39.025  1.00 61.48           C  
ANISOU 2782  CA  LEU A 704     5918   8420   9020  -1380    589    199       C  
ATOM   2783  C   LEU A 704       7.723  67.171  37.882  1.00 64.93           C  
ANISOU 2783  C   LEU A 704     6140   8946   9584  -1410    437    212       C  
ATOM   2784  O   LEU A 704       6.610  67.714  37.973  1.00 64.98           O  
ANISOU 2784  O   LEU A 704     5883   9075   9730  -1377    486    206       O  
ATOM   2785  CB  LEU A 704       9.795  68.339  38.681  1.00 61.49           C  
ANISOU 2785  CB  LEU A 704     6049   8342   8973  -1178    543    185       C  
ATOM   2786  CG  LEU A 704       9.316  69.753  38.312  1.00 62.64           C  
ANISOU 2786  CG  LEU A 704     6017   8545   9237   -985    539    169       C  
ATOM   2787  CD1 LEU A 704       8.639  70.443  39.485  1.00 64.47           C  
ANISOU 2787  CD1 LEU A 704     6105   8850   9539   -940    751    132       C  
ATOM   2788  CD2 LEU A 704      10.484  70.589  37.820  1.00 61.56           C  
ANISOU 2788  CD2 LEU A 704     6051   8307   9033   -823    468    165       C  
ATOM   2789  N   ILE A 705       8.112  66.461  36.822  1.00 66.24           N  
ANISOU 2789  N   ILE A 705     6417   9052   9698  -1475    255    230       N  
ATOM   2790  CA  ILE A 705       7.235  66.219  35.666  1.00 69.28           C  
ANISOU 2790  CA  ILE A 705     6632   9517  10172  -1532     83    243       C  
ATOM   2791  C   ILE A 705       5.975  65.463  36.067  1.00 72.17           C  
ANISOU 2791  C   ILE A 705     6793   9994  10632  -1722    139    248       C  
ATOM   2792  O   ILE A 705       4.863  65.896  35.760  1.00 71.77           O  
ANISOU 2792  O   ILE A 705     6467  10077  10723  -1704    106    254       O  
ATOM   2793  CB  ILE A 705       7.931  65.396  34.543  1.00 68.21           C  
ANISOU 2793  CB  ILE A 705     6694   9286   9936  -1605   -104    248       C  
ATOM   2794  CG1 ILE A 705       9.251  66.030  34.102  1.00 66.50           C  
ANISOU 2794  CG1 ILE A 705     6689   8957   9619  -1437   -154    244       C  
ATOM   2795  CG2 ILE A 705       7.009  65.236  33.330  1.00 69.84           C  
ANISOU 2795  CG2 ILE A 705     6728   9586  10221  -1665   -292    258       C  
ATOM   2796  CD1 ILE A 705       9.158  67.503  33.812  1.00 68.73           C  
ANISOU 2796  CD1 ILE A 705     6855   9288   9969  -1224   -169    250       C  
ATOM   2797  N   SER A 706       6.157  64.325  36.735  1.00 75.78           N  
ANISOU 2797  N   SER A 706     7383  10394  11015  -1905    218    251       N  
ATOM   2798  CA  SER A 706       5.036  63.439  37.071  1.00 80.95           C  
ANISOU 2798  CA  SER A 706     7875  11138  11744  -2123    267    259       C  
ATOM   2799  C   SER A 706       4.107  64.061  38.107  1.00 82.95           C  
ANISOU 2799  C   SER A 706     7887  11522  12107  -2098    465    252       C  
ATOM   2800  O   SER A 706       2.924  63.734  38.153  1.00 85.00           O  
ANISOU 2800  O   SER A 706     7906  11907  12483  -2226    487    257       O  
ATOM   2801  CB  SER A 706       5.543  62.086  37.568  1.00 82.50           C  
ANISOU 2801  CB  SER A 706     8303  11217  11826  -2319    311    272       C  
ATOM   2802  OG  SER A 706       6.432  62.258  38.660  1.00 86.30           O  
ANISOU 2802  OG  SER A 706     8972  11615  12203  -2254    466    278       O  
ATOM   2803  N   HIS A 707       4.645  64.959  38.928  1.00 83.96           N  
ANISOU 2803  N   HIS A 707     8078  11623  12197  -1937    612    235       N  
ATOM   2804  CA  HIS A 707       3.838  65.701  39.892  1.00 88.22           C  
ANISOU 2804  CA  HIS A 707     8403  12279  12835  -1881    814    213       C  
ATOM   2805  C   HIS A 707       2.857  66.664  39.209  1.00 90.95           C  
ANISOU 2805  C   HIS A 707     8435  12754  13365  -1744    748    207       C  
ATOM   2806  O   HIS A 707       1.728  66.804  39.667  1.00 91.90           O  
ANISOU 2806  O   HIS A 707     8288  13010  13619  -1783    865    198       O  
ATOM   2807  CB  HIS A 707       4.723  66.464  40.888  1.00 87.54           C  
ANISOU 2807  CB  HIS A 707     8488  12122  12650  -1741    976    187       C  
ATOM   2808  CG  HIS A 707       3.986  66.929  42.103  1.00 91.21           C  
ANISOU 2808  CG  HIS A 707     8796  12686  13172  -1739   1224    156       C  
ATOM   2809  ND1 HIS A 707       3.473  68.203  42.223  1.00 93.95           N  
ANISOU 2809  ND1 HIS A 707     8945  13108  13641  -1549   1308    117       N  
ATOM   2810  CD2 HIS A 707       3.646  66.278  43.241  1.00 93.41           C  
ANISOU 2810  CD2 HIS A 707     9088  13000  13403  -1905   1414    157       C  
ATOM   2811  CE1 HIS A 707       2.860  68.321  43.388  1.00 95.50           C  
ANISOU 2811  CE1 HIS A 707     9039  13384  13862  -1596   1548     85       C  
ATOM   2812  NE2 HIS A 707       2.951  67.168  44.025  1.00 95.73           N  
ANISOU 2812  NE2 HIS A 707     9194  13396  13783  -1816   1616    111       N  
ATOM   2813  N   HIS A 708       3.284  67.315  38.123  1.00 92.26           N  
ANISOU 2813  N   HIS A 708     8632  12881  13540  -1585    565    216       N  
ATOM   2814  CA  HIS A 708       2.409  68.230  37.363  1.00 97.33           C  
ANISOU 2814  CA  HIS A 708     8993  13635  14353  -1443    469    227       C  
ATOM   2815  C   HIS A 708       1.805  67.591  36.097  1.00 99.67           C  
ANISOU 2815  C   HIS A 708     9170  13996  14703  -1557    228    262       C  
ATOM   2816  O   HIS A 708       1.509  68.294  35.123  1.00100.85           O  
ANISOU 2816  O   HIS A 708     9190  14191  14934  -1425     66    287       O  
ATOM   2817  CB  HIS A 708       3.160  69.526  37.002  1.00 97.33           C  
ANISOU 2817  CB  HIS A 708     9082  13557  14339  -1181    427    223       C  
ATOM   2818  CG  HIS A 708       3.213  70.522  38.120  1.00101.81           C  
ANISOU 2818  CG  HIS A 708     9624  14120  14939  -1033    657    181       C  
ATOM   2819  ND1 HIS A 708       2.373  71.616  38.185  1.00105.00           N  
ANISOU 2819  ND1 HIS A 708     9768  14609  15517   -863    721    171       N  
ATOM   2820  CD2 HIS A 708       3.998  70.584  39.223  1.00102.12           C  
ANISOU 2820  CD2 HIS A 708     9867  14077  14857  -1032    839    143       C  
ATOM   2821  CE1 HIS A 708       2.637  72.307  39.280  1.00105.22           C  
ANISOU 2821  CE1 HIS A 708     9850  14601  15527   -767    942    119       C  
ATOM   2822  NE2 HIS A 708       3.618  71.702  39.928  1.00103.77           N  
ANISOU 2822  NE2 HIS A 708     9947  14321  15158   -873   1012    102       N  
ATOM   2823  N   HIS A 709       1.595  66.274  36.126  1.00 98.06           N  
ANISOU 2823  N   HIS A 709     9012  13794  14452  -1807    203    266       N  
ATOM   2824  CA  HIS A 709       1.083  65.539  34.961  1.00 98.38           C  
ANISOU 2824  CA  HIS A 709     8975  13884  14518  -1950    -24    288       C  
ATOM   2825  C   HIS A 709      -0.444  65.580  34.904  1.00 97.71           C  
ANISOU 2825  C   HIS A 709     8501  13993  14629  -2022    -31    302       C  
ATOM   2826  O   HIS A 709      -1.116  65.304  35.891  1.00 95.85           O  
ANISOU 2826  O   HIS A 709     8121  13833  14463  -2125    157    290       O  
ATOM   2827  CB  HIS A 709       1.601  64.090  34.970  1.00 98.55           C  
ANISOU 2827  CB  HIS A 709     9244  13798  14402  -2188    -53    281       C  
ATOM   2828  CG  HIS A 709       0.723  63.121  34.238  1.00102.54           C  
ANISOU 2828  CG  HIS A 709     9618  14381  14960  -2415   -204    288       C  
ATOM   2829  ND1 HIS A 709       0.532  63.166  32.873  1.00104.22           N  
ANISOU 2829  ND1 HIS A 709     9782  14630  15184  -2409   -456    298       N  
ATOM   2830  CD2 HIS A 709      -0.018  62.079  34.686  1.00105.84           C  
ANISOU 2830  CD2 HIS A 709     9948  14848  15416  -2667   -140    287       C  
ATOM   2831  CE1 HIS A 709      -0.293  62.198  32.513  1.00105.66           C  
ANISOU 2831  CE1 HIS A 709     9849  14883  15411  -2648   -546    296       C  
ATOM   2832  NE2 HIS A 709      -0.639  61.522  33.594  1.00106.18           N  
ANISOU 2832  NE2 HIS A 709     9888  14955  15499  -2810   -356    290       N  
TER    2833      HIS A 709                                                      
ATOM   2834  N   LEU B 375      36.051  57.795  -7.713  1.00113.59           N  
ANISOU 2834  N   LEU B 375    19032  10967  13157   4611  -1387    458       N  
ATOM   2835  CA  LEU B 375      35.095  56.993  -6.899  1.00112.11           C  
ANISOU 2835  CA  LEU B 375    19197  10507  12893   4341  -1557    489       C  
ATOM   2836  C   LEU B 375      33.977  56.463  -7.791  1.00110.80           C  
ANISOU 2836  C   LEU B 375    19428  10077  12592   4118  -1574    362       C  
ATOM   2837  O   LEU B 375      34.022  56.595  -9.015  1.00109.17           O  
ANISOU 2837  O   LEU B 375    19278   9868  12331   4219  -1465    244       O  
ATOM   2838  CB  LEU B 375      34.486  57.851  -5.782  1.00109.89           C  
ANISOU 2838  CB  LEU B 375    18628  10435  12687   3979  -1649    578       C  
ATOM   2839  CG  LEU B 375      35.421  58.696  -4.916  1.00109.25           C  
ANISOU 2839  CG  LEU B 375    18102  10665  12740   4098  -1658    691       C  
ATOM   2840  CD1 LEU B 375      34.616  59.700  -4.105  1.00107.19           C  
ANISOU 2840  CD1 LEU B 375    17598  10608  12521   3708  -1720    732       C  
ATOM   2841  CD2 LEU B 375      36.260  57.817  -4.003  1.00111.04           C  
ANISOU 2841  CD2 LEU B 375    18459  10758  12971   4371  -1755    807       C  
ATOM   2842  N   LYS B 376      32.972  55.871  -7.157  1.00109.87           N  
ANISOU 2842  N   LYS B 376    19585   9740  12420   3805  -1719    396       N  
ATOM   2843  CA  LYS B 376      31.766  55.416  -7.836  1.00108.72           C  
ANISOU 2843  CA  LYS B 376    19783   9356  12169   3505  -1781    303       C  
ATOM   2844  C   LYS B 376      30.615  56.343  -7.471  1.00102.93           C  
ANISOU 2844  C   LYS B 376    18784   8828  11495   3040  -1822    332       C  
ATOM   2845  O   LYS B 376      30.595  56.914  -6.383  1.00 99.71           O  
ANISOU 2845  O   LYS B 376    18094   8618  11171   2921  -1844    444       O  
ATOM   2846  CB  LYS B 376      31.427  53.987  -7.398  1.00112.45           C  
ANISOU 2846  CB  LYS B 376    20775   9405  12543   3471  -1920    339       C  
ATOM   2847  CG  LYS B 376      31.767  52.903  -8.410  1.00116.30           C  
ANISOU 2847  CG  LYS B 376    21749   9541  12896   3751  -1910    224       C  
ATOM   2848  CD  LYS B 376      32.033  51.576  -7.714  1.00120.11           C  
ANISOU 2848  CD  LYS B 376    22660   9658  13316   3898  -2019    299       C  
ATOM   2849  CE  LYS B 376      32.130  50.429  -8.709  1.00124.68           C  
ANISOU 2849  CE  LYS B 376    23811   9824  13736   4111  -2036    173       C  
ATOM   2850  NZ  LYS B 376      30.794  50.011  -9.219  1.00125.58           N  
ANISOU 2850  NZ  LYS B 376    24279   9677  13757   3684  -2172     97       N  
ATOM   2851  N   ILE B 377      29.666  56.496  -8.390  1.00100.79           N  
ANISOU 2851  N   ILE B 377    18610   8509  11174   2791  -1834    233       N  
ATOM   2852  CA  ILE B 377      28.385  57.149  -8.084  1.00 97.11           C  
ANISOU 2852  CA  ILE B 377    17968   8175  10755   2332  -1891    268       C  
ATOM   2853  C   ILE B 377      27.570  56.276  -7.119  1.00 97.39           C  
ANISOU 2853  C   ILE B 377    18264   7973  10766   2057  -2030    376       C  
ATOM   2854  O   ILE B 377      26.815  56.778  -6.287  1.00 93.73           O  
ANISOU 2854  O   ILE B 377    17590   7658  10362   1756  -2055    474       O  
ATOM   2855  CB  ILE B 377      27.569  57.443  -9.368  1.00 96.25           C  
ANISOU 2855  CB  ILE B 377    17919   8055  10597   2143  -1894    141       C  
ATOM   2856  CG1 ILE B 377      26.301  58.250  -9.059  1.00 93.31           C  
ANISOU 2856  CG1 ILE B 377    17288   7869  10295   1702  -1937    191       C  
ATOM   2857  CG2 ILE B 377      27.183  56.158 -10.088  1.00 99.94           C  
ANISOU 2857  CG2 ILE B 377    18936   8107  10927   2121  -2004     61       C  
ATOM   2858  CD1 ILE B 377      26.560  59.602  -8.434  1.00 89.14           C  
ANISOU 2858  CD1 ILE B 377    16248   7734   9885   1700  -1836    251       C  
ATOM   2859  N   GLU B 378      27.751  54.964  -7.225  1.00 99.50           N  
ANISOU 2859  N   GLU B 378    19001   7866  10938   2177  -2112    365       N  
ATOM   2860  CA  GLU B 378      27.055  54.022  -6.359  1.00100.71           C  
ANISOU 2860  CA  GLU B 378    19449   7753  11060   1932  -2245    478       C  
ATOM   2861  C   GLU B 378      27.523  54.108  -4.899  1.00 98.61           C  
ANISOU 2861  C   GLU B 378    19020   7599  10845   2001  -2239    636       C  
ATOM   2862  O   GLU B 378      26.886  53.543  -4.015  1.00 98.51           O  
ANISOU 2862  O   GLU B 378    19174   7438  10816   1762  -2326    759       O  
ATOM   2863  CB  GLU B 378      27.197  52.594  -6.903  1.00105.44           C  
ANISOU 2863  CB  GLU B 378    20632   7894  11536   2066  -2340    418       C  
ATOM   2864  CG  GLU B 378      26.406  52.339  -8.187  1.00107.45           C  
ANISOU 2864  CG  GLU B 378    21143   7967  11713   1877  -2407    281       C  
ATOM   2865  CD  GLU B 378      27.192  52.598  -9.467  1.00108.36           C  
ANISOU 2865  CD  GLU B 378    21280   8126  11764   2231  -2300    111       C  
ATOM   2866  OE1 GLU B 378      28.337  52.114  -9.576  1.00113.25           O  
ANISOU 2866  OE1 GLU B 378    22055   8640  12334   2672  -2230     79       O  
ATOM   2867  OE2 GLU B 378      26.654  53.255 -10.383  1.00105.97           O  
ANISOU 2867  OE2 GLU B 378    20852   7955  11453   2076  -2284     15       O  
ATOM   2868  N   ASP B 379      28.621  54.822  -4.652  1.00 96.18           N  
ANISOU 2868  N   ASP B 379    18390   7554  10597   2313  -2144    642       N  
ATOM   2869  CA  ASP B 379      29.045  55.153  -3.287  1.00 95.57           C  
ANISOU 2869  CA  ASP B 379    18096   7644  10570   2354  -2151    784       C  
ATOM   2870  C   ASP B 379      28.119  56.165  -2.605  1.00 91.54           C  
ANISOU 2870  C   ASP B 379    17259   7405  10116   1987  -2132    853       C  
ATOM   2871  O   ASP B 379      28.203  56.362  -1.390  1.00 91.82           O  
ANISOU 2871  O   ASP B 379    17185   7540  10161   1946  -2153    977       O  
ATOM   2872  CB  ASP B 379      30.464  55.735  -3.281  1.00 95.63           C  
ANISOU 2872  CB  ASP B 379    17810   7881  10642   2763  -2074    771       C  
ATOM   2873  CG  ASP B 379      31.498  54.779  -3.843  1.00 98.85           C  
ANISOU 2873  CG  ASP B 379    18497   8058  11004   3187  -2066    725       C  
ATOM   2874  OD1 ASP B 379      31.250  53.556  -3.867  1.00102.14           O  
ANISOU 2874  OD1 ASP B 379    19375   8104  11326   3195  -2149    731       O  
ATOM   2875  OD2 ASP B 379      32.572  55.260  -4.256  1.00 99.07           O  
ANISOU 2875  OD2 ASP B 379    18277   8273  11090   3519  -1973    689       O  
ATOM   2876  N   PHE B 380      27.263  56.819  -3.383  1.00 87.83           N  
ANISOU 2876  N   PHE B 380    16640   7055   9673   1743  -2090    773       N  
ATOM   2877  CA  PHE B 380      26.365  57.839  -2.858  1.00 84.36           C  
ANISOU 2877  CA  PHE B 380    15879   6882   9290   1425  -2052    829       C  
ATOM   2878  C   PHE B 380      24.924  57.384  -2.933  1.00 85.61           C  
ANISOU 2878  C   PHE B 380    16210   6889   9427   1017  -2111    870       C  
ATOM   2879  O   PHE B 380      24.555  56.651  -3.840  1.00 88.77           O  
ANISOU 2879  O   PHE B 380    16893   7047   9787    952  -2175    798       O  
ATOM   2880  CB  PHE B 380      26.517  59.121  -3.660  1.00 80.44           C  
ANISOU 2880  CB  PHE B 380    15008   6689   8863   1469  -1954    723       C  
ATOM   2881  CG  PHE B 380      27.854  59.760  -3.501  1.00 79.21           C  
ANISOU 2881  CG  PHE B 380    14602   6736   8756   1811  -1894    709       C  
ATOM   2882  CD1 PHE B 380      28.059  60.725  -2.527  1.00 77.44           C  
ANISOU 2882  CD1 PHE B 380    14058   6780   8585   1784  -1870    782       C  
ATOM   2883  CD2 PHE B 380      28.915  59.384  -4.306  1.00 80.48           C  
ANISOU 2883  CD2 PHE B 380    14852   6818   8908   2160  -1863    630       C  
ATOM   2884  CE1 PHE B 380      29.300  61.315  -2.369  1.00 76.77           C  
ANISOU 2884  CE1 PHE B 380    13732   6878   8558   2071  -1841    781       C  
ATOM   2885  CE2 PHE B 380      30.160  59.969  -4.156  1.00 80.04           C  
ANISOU 2885  CE2 PHE B 380    14527   6964   8917   2464  -1809    640       C  
ATOM   2886  CZ  PHE B 380      30.353  60.937  -3.187  1.00 78.01           C  
ANISOU 2886  CZ  PHE B 380    13940   6973   8728   2405  -1811    718       C  
ATOM   2887  N   GLU B 381      24.119  57.821  -1.973  1.00 83.36           N  
ANISOU 2887  N   GLU B 381    15757   6748   9167    746  -2089    991       N  
ATOM   2888  CA  GLU B 381      22.679  57.661  -2.049  1.00 83.41           C  
ANISOU 2888  CA  GLU B 381    15800   6702   9186    335  -2118   1048       C  
ATOM   2889  C   GLU B 381      22.128  59.022  -2.422  1.00 81.13           C  
ANISOU 2889  C   GLU B 381    15097   6752   8976    205  -2028   1000       C  
ATOM   2890  O   GLU B 381      22.336  60.004  -1.711  1.00 77.56           O  
ANISOU 2890  O   GLU B 381    14344   6572   8554    256  -1940   1037       O  
ATOM   2891  CB  GLU B 381      22.120  57.172  -0.714  1.00 85.76           C  
ANISOU 2891  CB  GLU B 381    16201   6928   9454    132  -2131   1237       C  
ATOM   2892  CG  GLU B 381      20.645  57.469  -0.457  1.00 86.08           C  
ANISOU 2892  CG  GLU B 381    16092   7072   9539   -288  -2098   1341       C  
ATOM   2893  CD  GLU B 381      19.723  56.337  -0.831  1.00 89.30           C  
ANISOU 2893  CD  GLU B 381    16815   7174   9940   -586  -2211   1398       C  
ATOM   2894  OE1 GLU B 381      19.771  55.888  -1.990  1.00 89.90           O  
ANISOU 2894  OE1 GLU B 381    17080   7066  10011   -564  -2305   1273       O  
ATOM   2895  OE2 GLU B 381      18.944  55.907   0.047  1.00 91.87           O  
ANISOU 2895  OE2 GLU B 381    17207   7440  10259   -849  -2207   1573       O  
ATOM   2896  N   LEU B 382      21.449  59.092  -3.560  1.00 80.27           N  
ANISOU 2896  N   LEU B 382    14991   6615   8893     48  -2062    914       N  
ATOM   2897  CA  LEU B 382      20.826  60.330  -3.984  1.00 78.44           C  
ANISOU 2897  CA  LEU B 382    14387   6681   8734    -86  -1990    875       C  
ATOM   2898  C   LEU B 382      19.484  60.436  -3.283  1.00 78.59           C  
ANISOU 2898  C   LEU B 382    14288   6776   8796   -459  -1978   1022       C  
ATOM   2899  O   LEU B 382      18.622  59.585  -3.478  1.00 80.65           O  
ANISOU 2899  O   LEU B 382    14754   6833   9056   -723  -2072   1080       O  
ATOM   2900  CB  LEU B 382      20.664  60.351  -5.498  1.00 78.95           C  
ANISOU 2900  CB  LEU B 382    14514   6686   8796    -91  -2043    729       C  
ATOM   2901  CG  LEU B 382      21.958  60.073  -6.279  1.00 80.07           C  
ANISOU 2901  CG  LEU B 382    14824   6719   8879    286  -2037    592       C  
ATOM   2902  CD1 LEU B 382      21.704  60.173  -7.778  1.00 79.90           C  
ANISOU 2902  CD1 LEU B 382    14873   6653   8830    269  -2077    451       C  
ATOM   2903  CD2 LEU B 382      23.083  61.017  -5.858  1.00 77.70           C  
ANISOU 2903  CD2 LEU B 382    14232   6676   8613    586  -1917    577       C  
ATOM   2904  N   HIS B 383      19.323  61.460  -2.446  1.00 75.92           N  
ANISOU 2904  N   HIS B 383    13629   6724   8493   -476  -1861   1088       N  
ATOM   2905  CA  HIS B 383      18.136  61.593  -1.599  1.00 75.24           C  
ANISOU 2905  CA  HIS B 383    13416   6735   8436   -781  -1808   1249       C  
ATOM   2906  C   HIS B 383      17.091  62.517  -2.187  1.00 74.62           C  
ANISOU 2906  C   HIS B 383    13024   6881   8446   -986  -1763   1237       C  
ATOM   2907  O   HIS B 383      15.904  62.362  -1.919  1.00 74.41           O  
ANISOU 2907  O   HIS B 383    12928   6878   8465  -1287  -1754   1364       O  
ATOM   2908  CB  HIS B 383      18.513  62.113  -0.209  1.00 73.89           C  
ANISOU 2908  CB  HIS B 383    13122   6727   8223   -672  -1699   1342       C  
ATOM   2909  CG  HIS B 383      19.072  61.064   0.695  1.00 74.97           C  
ANISOU 2909  CG  HIS B 383    13571   6640   8272   -589  -1746   1434       C  
ATOM   2910  ND1 HIS B 383      18.278  60.282   1.505  1.00 77.14           N  
ANISOU 2910  ND1 HIS B 383    14007   6787   8515   -831  -1745   1608       N  
ATOM   2911  CD2 HIS B 383      20.345  60.661   0.913  1.00 74.93           C  
ANISOU 2911  CD2 HIS B 383    13743   6517   8208   -289  -1798   1388       C  
ATOM   2912  CE1 HIS B 383      19.040  59.445   2.187  1.00 78.68           C  
ANISOU 2912  CE1 HIS B 383    14488   6783   8624   -681  -1798   1660       C  
ATOM   2913  NE2 HIS B 383      20.298  59.656   1.846  1.00 77.29           N  
ANISOU 2913  NE2 HIS B 383    14321   6612   8434   -345  -1836   1528       N  
ATOM   2914  N   LYS B 384      17.521  63.503  -2.958  1.00 74.21           N  
ANISOU 2914  N   LYS B 384    12767   7004   8424   -821  -1731   1100       N  
ATOM   2915  CA  LYS B 384      16.581  64.470  -3.480  1.00 74.86           C  
ANISOU 2915  CA  LYS B 384    12543   7311   8587   -983  -1688   1091       C  
ATOM   2916  C   LYS B 384      17.177  65.243  -4.630  1.00 73.60           C  
ANISOU 2916  C   LYS B 384    12272   7248   8441   -794  -1695    923       C  
ATOM   2917  O   LYS B 384      18.359  65.566  -4.615  1.00 72.87           O  
ANISOU 2917  O   LYS B 384    12182   7188   8315   -510  -1658    839       O  
ATOM   2918  CB  LYS B 384      16.165  65.445  -2.378  1.00 75.22           C  
ANISOU 2918  CB  LYS B 384    12301   7623   8653  -1016  -1537   1193       C  
ATOM   2919  CG  LYS B 384      14.768  66.010  -2.566  1.00 77.17           C  
ANISOU 2919  CG  LYS B 384    12284   8046   8989  -1279  -1492   1271       C  
ATOM   2920  CD  LYS B 384      14.673  67.448  -2.079  1.00 75.39           C  
ANISOU 2920  CD  LYS B 384    11733   8127   8785  -1180  -1339   1271       C  
ATOM   2921  CE  LYS B 384      13.245  67.955  -2.178  1.00 76.39           C  
ANISOU 2921  CE  LYS B 384    11590   8430   9003  -1421  -1280   1371       C  
ATOM   2922  NZ  LYS B 384      13.125  69.342  -1.665  1.00 74.91           N  
ANISOU 2922  NZ  LYS B 384    11118   8520   8823  -1305  -1123   1371       N  
ATOM   2923  N   MET B 385      16.344  65.535  -5.622  1.00 75.04           N  
ANISOU 2923  N   MET B 385    12352   7482   8677   -960  -1746    886       N  
ATOM   2924  CA  MET B 385      16.691  66.471  -6.692  1.00 76.01           C  
ANISOU 2924  CA  MET B 385    12320   7743   8814   -817  -1732    749       C  
ATOM   2925  C   MET B 385      16.456  67.880  -6.165  1.00 71.45           C  
ANISOU 2925  C   MET B 385    11375   7478   8295   -791  -1597    782       C  
ATOM   2926  O   MET B 385      15.324  68.226  -5.828  1.00 71.16           O  
ANISOU 2926  O   MET B 385    11150   7567   8318  -1004  -1564    884       O  
ATOM   2927  CB  MET B 385      15.820  66.205  -7.935  1.00 81.19           C  
ANISOU 2927  CB  MET B 385    13034   8321   9491  -1018  -1862    707       C  
ATOM   2928  CG  MET B 385      15.478  67.426  -8.797  1.00 83.04           C  
ANISOU 2928  CG  MET B 385    12993   8784   9773  -1009  -1836    641       C  
ATOM   2929  SD  MET B 385      16.655  67.744 -10.118  1.00 88.43           S  
ANISOU 2929  SD  MET B 385    13786   9433  10377   -711  -1842    449       S  
ATOM   2930  CE  MET B 385      16.275  66.337 -11.164  1.00 87.78           C  
ANISOU 2930  CE  MET B 385    14115   9018  10217   -855  -2046    393       C  
ATOM   2931  N   LEU B 386      17.512  68.689  -6.109  1.00 68.32           N  
ANISOU 2931  N   LEU B 386    10876   7200   7882   -529  -1520    702       N  
ATOM   2932  CA  LEU B 386      17.419  70.050  -5.573  1.00 66.42           C  
ANISOU 2932  CA  LEU B 386    10329   7225   7681   -482  -1402    721       C  
ATOM   2933  C   LEU B 386      17.122  71.096  -6.633  1.00 65.63           C  
ANISOU 2933  C   LEU B 386    10023   7281   7629   -478  -1391    643       C  
ATOM   2934  O   LEU B 386      16.617  72.157  -6.318  1.00 63.18           O  
ANISOU 2934  O   LEU B 386     9467   7172   7363   -510  -1310    675       O  
ATOM   2935  CB  LEU B 386      18.714  70.440  -4.861  1.00 64.65           C  
ANISOU 2935  CB  LEU B 386    10096   7047   7421   -228  -1346    690       C  
ATOM   2936  CG  LEU B 386      19.115  69.591  -3.653  1.00 65.77           C  
ANISOU 2936  CG  LEU B 386    10421   7065   7504   -196  -1354    775       C  
ATOM   2937  CD1 LEU B 386      20.466  70.062  -3.140  1.00 64.66           C  
ANISOU 2937  CD1 LEU B 386    10244   6983   7338     63  -1333    734       C  
ATOM   2938  CD2 LEU B 386      18.069  69.650  -2.543  1.00 66.37           C  
ANISOU 2938  CD2 LEU B 386    10430   7213   7574   -389  -1288    913       C  
ATOM   2939  N   GLY B 387      17.467  70.813  -7.882  1.00 68.89           N  
ANISOU 2939  N   GLY B 387    10556   7595   8021   -419  -1468    540       N  
ATOM   2940  CA  GLY B 387      17.255  71.768  -8.964  1.00 66.68           C  
ANISOU 2940  CA  GLY B 387    10115   7450   7771   -402  -1465    466       C  
ATOM   2941  C   GLY B 387      17.834  71.272 -10.269  1.00 68.77           C  
ANISOU 2941  C   GLY B 387    10584   7570   7974   -298  -1539    351       C  
ATOM   2942  O   GLY B 387      18.709  70.398 -10.289  1.00 71.65           O  
ANISOU 2942  O   GLY B 387    11185   7760   8277   -159  -1560    311       O  
ATOM   2943  N   LYS B 388      17.341  71.830 -11.363  1.00 68.98           N  
ANISOU 2943  N   LYS B 388    10533   7668   8007   -351  -1576    301       N  
ATOM   2944  CA  LYS B 388      17.774  71.436 -12.693  1.00 70.10           C  
ANISOU 2944  CA  LYS B 388    10885   7681   8067   -258  -1642    190       C  
ATOM   2945  C   LYS B 388      17.642  72.589 -13.685  1.00 68.44           C  
ANISOU 2945  C   LYS B 388    10502   7638   7863   -218  -1618    136       C  
ATOM   2946  O   LYS B 388      16.826  73.489 -13.492  1.00 64.84           O  
ANISOU 2946  O   LYS B 388     9794   7359   7483   -336  -1601    193       O  
ATOM   2947  CB  LYS B 388      16.945  70.247 -13.170  1.00 75.03           C  
ANISOU 2947  CB  LYS B 388    11768   8088   8650   -468  -1807    194       C  
ATOM   2948  CG  LYS B 388      15.487  70.274 -12.714  1.00 76.26           C  
ANISOU 2948  CG  LYS B 388    11766   8311   8897   -781  -1878    313       C  
ATOM   2949  CD  LYS B 388      14.555  69.486 -13.632  1.00 79.00           C  
ANISOU 2949  CD  LYS B 388    12301   8497   9218  -1015  -2077    304       C  
ATOM   2950  CE  LYS B 388      15.197  68.229 -14.198  1.00 80.80           C  
ANISOU 2950  CE  LYS B 388    12959   8419   9321   -939  -2175    210       C  
ATOM   2951  NZ  LYS B 388      14.199  67.167 -14.486  1.00 85.08           N  
ANISOU 2951  NZ  LYS B 388    13717   8752   9857  -1238  -2383    251       N  
ATOM   2952  N   GLY B 389      18.445  72.551 -14.746  1.00 69.06           N  
ANISOU 2952  N   GLY B 389    10727   7656   7855    -39  -1606     35       N  
ATOM   2953  CA  GLY B 389      18.398  73.581 -15.786  1.00 67.00           C  
ANISOU 2953  CA  GLY B 389    10346   7532   7579     10  -1582    -13       C  
ATOM   2954  C   GLY B 389      19.575  73.469 -16.726  1.00 66.16           C  
ANISOU 2954  C   GLY B 389    10407   7362   7367    262  -1516   -109       C  
ATOM   2955  O   GLY B 389      20.080  72.377 -16.943  1.00 66.01           O  
ANISOU 2955  O   GLY B 389    10672   7146   7263    353  -1542   -158       O  
ATOM   2956  N   SER B 390      20.034  74.594 -17.262  1.00 64.43           N  
ANISOU 2956  N   SER B 390    10019   7306   7154    384  -1418   -128       N  
ATOM   2957  CA  SER B 390      21.152  74.570 -18.202  1.00 66.57           C  
ANISOU 2957  CA  SER B 390    10420   7544   7326    628  -1325   -201       C  
ATOM   2958  C   SER B 390      22.415  73.983 -17.558  1.00 66.64           C  
ANISOU 2958  C   SER B 390    10485   7492   7344    842  -1226   -197       C  
ATOM   2959  O   SER B 390      23.252  73.387 -18.248  1.00 66.69           O  
ANISOU 2959  O   SER B 390    10697   7391   7250   1045  -1171   -256       O  
ATOM   2960  CB  SER B 390      21.449  75.967 -18.742  1.00 66.64           C  
ANISOU 2960  CB  SER B 390    10202   7755   7361    704  -1224   -193       C  
ATOM   2961  OG  SER B 390      22.265  76.676 -17.836  1.00 69.60           O  
ANISOU 2961  OG  SER B 390    10335   8267   7843    804  -1105   -139       O  
ATOM   2962  N   PHE B 391      22.526  74.132 -16.235  1.00 65.08           N  
ANISOU 2962  N   PHE B 391    10111   7358   7255    805  -1207   -125       N  
ATOM   2963  CA  PHE B 391      23.682  73.653 -15.476  1.00 64.19           C  
ANISOU 2963  CA  PHE B 391    10014   7206   7167    994  -1138   -103       C  
ATOM   2964  C   PHE B 391      23.716  72.146 -15.287  1.00 66.43           C  
ANISOU 2964  C   PHE B 391    10612   7246   7381   1019  -1211   -123       C  
ATOM   2965  O   PHE B 391      24.758  71.617 -14.911  1.00 69.36           O  
ANISOU 2965  O   PHE B 391    11045   7558   7750   1223  -1156   -115       O  
ATOM   2966  CB  PHE B 391      23.748  74.326 -14.092  1.00 61.81           C  
ANISOU 2966  CB  PHE B 391     9451   7045   6986    937  -1116    -19       C  
ATOM   2967  CG  PHE B 391      22.447  74.276 -13.322  1.00 61.44           C  
ANISOU 2967  CG  PHE B 391     9371   6996   6977    680  -1205     31       C  
ATOM   2968  CD1 PHE B 391      21.568  75.348 -13.350  1.00 59.75           C  
ANISOU 2968  CD1 PHE B 391     8949   6937   6814    531  -1205     55       C  
ATOM   2969  CD2 PHE B 391      22.102  73.162 -12.570  1.00 62.84           C  
ANISOU 2969  CD2 PHE B 391     9720   7018   7139    595  -1277     66       C  
ATOM   2970  CE1 PHE B 391      20.370  75.313 -12.653  1.00 58.85           C  
ANISOU 2970  CE1 PHE B 391     8778   6841   6741    315  -1262    116       C  
ATOM   2971  CE2 PHE B 391      20.903  73.120 -11.868  1.00 62.70           C  
ANISOU 2971  CE2 PHE B 391     9651   7014   7159    356  -1336    132       C  
ATOM   2972  CZ  PHE B 391      20.037  74.203 -11.908  1.00 60.22           C  
ANISOU 2972  CZ  PHE B 391     9105   6873   6901    222  -1321    160       C  
ATOM   2973  N   GLY B 392      22.585  71.468 -15.494  1.00 65.52           N  
ANISOU 2973  N   GLY B 392    10687   6987   7219    806  -1345   -138       N  
ATOM   2974  CA  GLY B 392      22.483  70.016 -15.302  1.00 66.40           C  
ANISOU 2974  CA  GLY B 392    11129   6836   7264    787  -1439   -151       C  
ATOM   2975  C   GLY B 392      21.443  69.672 -14.246  1.00 66.28           C  
ANISOU 2975  C   GLY B 392    11081   6784   7317    515  -1539    -63       C  
ATOM   2976  O   GLY B 392      20.340  70.231 -14.264  1.00 63.76           O  
ANISOU 2976  O   GLY B 392    10607   6569   7049    282  -1594    -27       O  
ATOM   2977  N   LYS B 393      21.796  68.750 -13.340  1.00 65.55           N  
ANISOU 2977  N   LYS B 393    11133   6548   7225    555  -1557    -20       N  
ATOM   2978  CA  LYS B 393      20.969  68.394 -12.176  1.00 65.88           C  
ANISOU 2978  CA  LYS B 393    11144   6560   7326    325  -1620     85       C  
ATOM   2979  C   LYS B 393      21.803  68.360 -10.899  1.00 63.96           C  
ANISOU 2979  C   LYS B 393    10820   6357   7123    467  -1548    154       C  
ATOM   2980  O   LYS B 393      22.894  67.786 -10.874  1.00 62.56           O  
ANISOU 2980  O   LYS B 393    10790   6073   6904    708  -1520    126       O  
ATOM   2981  CB  LYS B 393      20.343  67.011 -12.339  1.00 70.79           C  
ANISOU 2981  CB  LYS B 393    12118   6893   7884    168  -1764     86       C  
ATOM   2982  CG  LYS B 393      19.165  66.953 -13.296  1.00 73.83           C  
ANISOU 2982  CG  LYS B 393    12572   7231   8248    -81  -1893     57       C  
ATOM   2983  CD  LYS B 393      18.714  65.516 -13.496  1.00 77.35           C  
ANISOU 2983  CD  LYS B 393    13412   7354   8622   -225  -2055     50       C  
ATOM   2984  CE  LYS B 393      17.634  65.419 -14.563  1.00 79.62           C  
ANISOU 2984  CE  LYS B 393    13794   7577   8878   -469  -2218     12       C  
ATOM   2985  NZ  LYS B 393      17.355  64.006 -14.936  1.00 82.71           N  
ANISOU 2985  NZ  LYS B 393    14631   7617   9177   -585  -2394    -20       N  
ATOM   2986  N   VAL B 394      21.262  68.944  -9.833  1.00 62.12           N  
ANISOU 2986  N   VAL B 394    10367   6272   6963    322  -1523    248       N  
ATOM   2987  CA  VAL B 394      21.915  68.928  -8.530  1.00 60.67           C  
ANISOU 2987  CA  VAL B 394    10126   6124   6802    421  -1479    321       C  
ATOM   2988  C   VAL B 394      21.097  68.105  -7.549  1.00 61.14           C  
ANISOU 2988  C   VAL B 394    10315   6062   6852    215  -1537    426       C  
ATOM   2989  O   VAL B 394      19.904  68.367  -7.366  1.00 62.13           O  
ANISOU 2989  O   VAL B 394    10335   6257   7013    -33  -1548    485       O  
ATOM   2990  CB  VAL B 394      22.089  70.347  -8.001  1.00 58.12           C  
ANISOU 2990  CB  VAL B 394     9468   6070   6545    452  -1391    343       C  
ATOM   2991  CG1 VAL B 394      22.657  70.324  -6.586  1.00 58.36           C  
ANISOU 2991  CG1 VAL B 394     9464   6129   6581    526  -1373    422       C  
ATOM   2992  CG2 VAL B 394      22.986  71.132  -8.944  1.00 57.52           C  
ANISOU 2992  CG2 VAL B 394     9266   6105   6483    651  -1330    258       C  
ATOM   2993  N   PHE B 395      21.741  67.110  -6.936  1.00 60.61           N  
ANISOU 2993  N   PHE B 395    10470   5816   6740    325  -1570    459       N  
ATOM   2994  CA  PHE B 395      21.099  66.245  -5.966  1.00 62.03           C  
ANISOU 2994  CA  PHE B 395    10807   5858   6900    148  -1619    572       C  
ATOM   2995  C   PHE B 395      21.689  66.455  -4.567  1.00 61.82           C  
ANISOU 2995  C   PHE B 395    10705   5912   6869    251  -1571    657       C  
ATOM   2996  O   PHE B 395      22.878  66.741  -4.440  1.00 59.53           O  
ANISOU 2996  O   PHE B 395    10362   5676   6578    507  -1547    620       O  
ATOM   2997  CB  PHE B 395      21.331  64.787  -6.343  1.00 65.55           C  
ANISOU 2997  CB  PHE B 395    11642   5985   7278    186  -1718    551       C  
ATOM   2998  CG  PHE B 395      20.801  64.411  -7.696  1.00 67.02           C  
ANISOU 2998  CG  PHE B 395    11985   6041   7438     88  -1796    461       C  
ATOM   2999  CD1 PHE B 395      21.624  64.461  -8.816  1.00 67.21           C  
ANISOU 2999  CD1 PHE B 395    12089   6028   7417    326  -1781    330       C  
ATOM   3000  CD2 PHE B 395      19.483  63.988  -7.848  1.00 68.65           C  
ANISOU 3000  CD2 PHE B 395    12264   6158   7659   -243  -1888    515       C  
ATOM   3001  CE1 PHE B 395      21.141  64.092 -10.065  1.00 68.57           C  
ANISOU 3001  CE1 PHE B 395    12450   6065   7536    243  -1863    240       C  
ATOM   3002  CE2 PHE B 395      18.994  63.619  -9.099  1.00 69.83           C  
ANISOU 3002  CE2 PHE B 395    12583   6174   7775   -346  -1994    429       C  
ATOM   3003  CZ  PHE B 395      19.826  63.675 -10.204  1.00 69.36           C  
ANISOU 3003  CZ  PHE B 395    12638   6067   7648    -97  -1984    285       C  
ATOM   3004  N   LEU B 396      20.849  66.299  -3.539  1.00 62.62           N  
ANISOU 3004  N   LEU B 396    10804   6023   6964     48  -1561    779       N  
ATOM   3005  CA  LEU B 396      21.310  66.100  -2.154  1.00 63.81           C  
ANISOU 3005  CA  LEU B 396    11006   6167   7069    121  -1545    876       C  
ATOM   3006  C   LEU B 396      21.691  64.634  -2.000  1.00 66.77           C  
ANISOU 3006  C   LEU B 396    11738   6246   7384    174  -1635    912       C  
ATOM   3007  O   LEU B 396      20.855  63.739  -2.174  1.00 69.39           O  
ANISOU 3007  O   LEU B 396    12267   6394   7703    -33  -1689    961       O  
ATOM   3008  CB  LEU B 396      20.218  66.454  -1.133  1.00 63.73           C  
ANISOU 3008  CB  LEU B 396    10885   6273   7054   -108  -1477   1001       C  
ATOM   3009  CG  LEU B 396      20.527  66.184   0.357  1.00 64.93           C  
ANISOU 3009  CG  LEU B 396    11135   6406   7129    -63  -1460   1116       C  
ATOM   3010  CD1 LEU B 396      21.681  67.051   0.851  1.00 63.31           C  
ANISOU 3010  CD1 LEU B 396    10797   6349   6907    186  -1448   1067       C  
ATOM   3011  CD2 LEU B 396      19.295  66.386   1.229  1.00 64.82           C  
ANISOU 3011  CD2 LEU B 396    11045   6486   7096   -306  -1368   1251       C  
ATOM   3012  N   ALA B 397      22.949  64.399  -1.643  1.00 66.46           N  
ANISOU 3012  N   ALA B 397    11777   6158   7315    448  -1660    897       N  
ATOM   3013  CA  ALA B 397      23.532  63.075  -1.688  1.00 67.40           C  
ANISOU 3013  CA  ALA B 397    12233   5993   7380    579  -1744    907       C  
ATOM   3014  C   ALA B 397      24.252  62.730  -0.385  1.00 68.98           C  
ANISOU 3014  C   ALA B 397    12524   6156   7529    719  -1772   1008       C  
ATOM   3015  O   ALA B 397      25.011  63.540   0.143  1.00 65.86           O  
ANISOU 3015  O   ALA B 397    11924   5950   7149    879  -1749   1007       O  
ATOM   3016  CB  ALA B 397      24.498  62.992  -2.853  1.00 67.21           C  
ANISOU 3016  CB  ALA B 397    12242   5921   7372    843  -1753    775       C  
ATOM   3017  N   GLU B 398      24.007  61.518   0.110  1.00 71.51           N  
ANISOU 3017  N   GLU B 398    13164   6220   7785    650  -1838   1099       N  
ATOM   3018  CA  GLU B 398      24.677  60.999   1.302  1.00 74.47           C  
ANISOU 3018  CA  GLU B 398    13688   6512   8093    789  -1885   1205       C  
ATOM   3019  C   GLU B 398      25.805  60.089   0.865  1.00 77.75           C  
ANISOU 3019  C   GLU B 398    14333   6713   8492   1094  -1963   1158       C  
ATOM   3020  O   GLU B 398      25.604  59.252  -0.009  1.00 79.67           O  
ANISOU 3020  O   GLU B 398    14815   6727   8726   1080  -1999   1104       O  
ATOM   3021  CB  GLU B 398      23.688  60.199   2.152  1.00 75.90           C  
ANISOU 3021  CB  GLU B 398    14098   6532   8208    524  -1900   1355       C  
ATOM   3022  CG  GLU B 398      24.177  59.888   3.559  1.00 76.56           C  
ANISOU 3022  CG  GLU B 398    14304   6581   8202    620  -1932   1486       C  
ATOM   3023  CD  GLU B 398      23.290  58.913   4.298  1.00 77.99           C  
ANISOU 3023  CD  GLU B 398    14765   6558   8309    376  -1945   1645       C  
ATOM   3024  OE1 GLU B 398      22.094  58.801   3.969  1.00 77.80           O  
ANISOU 3024  OE1 GLU B 398    14734   6510   8316     71  -1901   1680       O  
ATOM   3025  OE2 GLU B 398      23.798  58.259   5.225  1.00 80.75           O  
ANISOU 3025  OE2 GLU B 398    15336   6773   8571    488  -2004   1748       O  
ATOM   3026  N   PHE B 399      26.981  60.212   1.474  1.00 80.13           N  
ANISOU 3026  N   PHE B 399    14578   7077   8788   1373  -1996   1183       N  
ATOM   3027  CA  PHE B 399      28.088  59.324   1.105  1.00 85.36           C  
ANISOU 3027  CA  PHE B 399    15444   7546   9443   1699  -2060   1156       C  
ATOM   3028  C   PHE B 399      27.876  57.893   1.627  1.00 90.76           C  
ANISOU 3028  C   PHE B 399    16559   7887  10036   1671  -2147   1255       C  
ATOM   3029  O   PHE B 399      28.767  57.048   1.523  1.00 95.52           O  
ANISOU 3029  O   PHE B 399    17377   8298  10617   1954  -2209   1256       O  
ATOM   3030  CB  PHE B 399      29.441  59.898   1.539  1.00 85.43           C  
ANISOU 3030  CB  PHE B 399    15224   7739   9494   2010  -2083   1165       C  
ATOM   3031  CG  PHE B 399      30.629  59.062   1.115  1.00 88.30           C  
ANISOU 3031  CG  PHE B 399    15740   7941   9869   2381  -2128   1146       C  
ATOM   3032  CD1 PHE B 399      31.611  58.718   2.033  1.00 89.64           C  
ANISOU 3032  CD1 PHE B 399    15945   8088  10024   2622  -2220   1245       C  
ATOM   3033  CD2 PHE B 399      30.762  58.612  -0.196  1.00 89.10           C  
ANISOU 3033  CD2 PHE B 399    15960   7909   9983   2506  -2079   1033       C  
ATOM   3034  CE1 PHE B 399      32.702  57.954   1.654  1.00 91.95           C  
ANISOU 3034  CE1 PHE B 399    16358   8242  10334   2988  -2254   1239       C  
ATOM   3035  CE2 PHE B 399      31.853  57.847  -0.579  1.00 90.69           C  
ANISOU 3035  CE2 PHE B 399    16308   7964  10187   2879  -2097   1018       C  
ATOM   3036  CZ  PHE B 399      32.822  57.518   0.348  1.00 92.91           C  
ANISOU 3036  CZ  PHE B 399    16594   8236  10471   3125  -2180   1125       C  
ATOM   3037  N   LYS B 400      26.689  57.626   2.174  1.00 93.48           N  
ANISOU 3037  N   LYS B 400    17028   8156  10333   1334  -2146   1347       N  
ATOM   3038  CA  LYS B 400      26.178  56.264   2.355  1.00 97.95           C  
ANISOU 3038  CA  LYS B 400    18021   8368  10828   1211  -2220   1430       C  
ATOM   3039  C   LYS B 400      26.820  55.622   3.567  1.00101.16           C  
ANISOU 3039  C   LYS B 400    18626   8653  11154   1369  -2295   1567       C  
ATOM   3040  O   LYS B 400      26.132  55.200   4.499  1.00103.83           O  
ANISOU 3040  O   LYS B 400    19127   8899  11422   1150  -2308   1711       O  
ATOM   3041  CB  LYS B 400      26.411  55.420   1.096  1.00100.41           C  
ANISOU 3041  CB  LYS B 400    18595   8414  11141   1337  -2265   1313       C  
ATOM   3042  CG  LYS B 400      25.330  54.388   0.819  1.00103.36           C  
ANISOU 3042  CG  LYS B 400    19326   8472  11472   1036  -2328   1352       C  
ATOM   3043  CD  LYS B 400      25.543  53.719  -0.531  1.00104.55           C  
ANISOU 3043  CD  LYS B 400    19735   8378  11610   1161  -2375   1206       C  
ATOM   3044  CE  LYS B 400      24.227  53.473  -1.245  1.00104.94           C  
ANISOU 3044  CE  LYS B 400    19900   8303  11667    769  -2416   1180       C  
ATOM   3045  NZ  LYS B 400      24.461  52.868  -2.581  1.00106.44           N  
ANISOU 3045  NZ  LYS B 400    20372   8250  11820    903  -2473   1023       N  
ATOM   3046  N   LYS B 401      28.146  55.555   3.552  1.00102.03           N  
ANISOU 3046  N   LYS B 401    18715   8774  11278   1754  -2341   1533       N  
ATOM   3047  CA  LYS B 401      28.890  55.173   4.732  1.00105.91           C  
ANISOU 3047  CA  LYS B 401    19319   9216  11704   1940  -2426   1661       C  
ATOM   3048  C   LYS B 401      28.706  56.272   5.783  1.00102.74           C  
ANISOU 3048  C   LYS B 401    18628   9121  11284   1813  -2394   1730       C  
ATOM   3049  O   LYS B 401      27.843  56.171   6.657  1.00105.53           O  
ANISOU 3049  O   LYS B 401    19086   9452  11556   1554  -2375   1849       O  
ATOM   3050  CB  LYS B 401      30.382  54.968   4.398  1.00108.80           C  
ANISOU 3050  CB  LYS B 401    19657   9568  12114   2395  -2483   1610       C  
ATOM   3051  CG  LYS B 401      31.110  53.970   5.289  1.00111.74           C  
ANISOU 3051  CG  LYS B 401    20322   9721  12411   2625  -2607   1740       C  
ATOM   3052  CD  LYS B 401      31.498  52.708   4.535  1.00115.48           C  
ANISOU 3052  CD  LYS B 401    21166   9842  12869   2852  -2647   1701       C  
ATOM   3053  CE  LYS B 401      30.287  51.966   3.989  1.00117.16           C  
ANISOU 3053  CE  LYS B 401    21710   9772  13030   2537  -2629   1677       C  
ATOM   3054  NZ  LYS B 401      30.646  50.583   3.564  1.00120.89           N  
ANISOU 3054  NZ  LYS B 401    22649   9833  13448   2748  -2704   1670       N  
ATOM   3055  N   THR B 402      29.458  57.356   5.628  1.00 97.96           N  
ANISOU 3055  N   THR B 402    17662   8803  10755   1981  -2376   1653       N  
ATOM   3056  CA  THR B 402      29.756  58.269   6.722  1.00 95.00           C  
ANISOU 3056  CA  THR B 402    17072   8676  10348   1986  -2402   1717       C  
ATOM   3057  C   THR B 402      28.572  59.086   7.207  1.00 91.26           C  
ANISOU 3057  C   THR B 402    16471   8371   9831   1646  -2301   1744       C  
ATOM   3058  O   THR B 402      28.701  59.822   8.179  1.00 89.62           O  
ANISOU 3058  O   THR B 402    16140   8345   9566   1633  -2317   1796       O  
ATOM   3059  CB  THR B 402      30.862  59.262   6.313  1.00 93.49           C  
ANISOU 3059  CB  THR B 402    16514   8740  10267   2228  -2418   1625       C  
ATOM   3060  OG1 THR B 402      30.460  59.947   5.123  1.00 92.28           O  
ANISOU 3060  OG1 THR B 402    16138   8712  10210   2133  -2301   1488       O  
ATOM   3061  CG2 THR B 402      32.178  58.538   6.059  1.00 95.66           C  
ANISOU 3061  CG2 THR B 402    16864   8896  10586   2610  -2515   1632       C  
ATOM   3062  N   ASN B 403      27.429  58.980   6.536  1.00 89.20           N  
ANISOU 3062  N   ASN B 403    16239   8056   9594   1382  -2202   1710       N  
ATOM   3063  CA  ASN B 403      26.298  59.846   6.837  1.00 87.66           C  
ANISOU 3063  CA  ASN B 403    15865   8055   9385   1085  -2085   1729       C  
ATOM   3064  C   ASN B 403      26.634  61.328   6.576  1.00 83.07           C  
ANISOU 3064  C   ASN B 403    14890   7795   8877   1148  -2037   1619       C  
ATOM   3065  O   ASN B 403      25.971  62.219   7.109  1.00 82.91           O  
ANISOU 3065  O   ASN B 403    14711   7966   8824    982  -1954   1641       O  
ATOM   3066  CB  ASN B 403      25.847  59.643   8.295  1.00 89.86           C  
ANISOU 3066  CB  ASN B 403    16308   8314   9520    959  -2079   1898       C  
ATOM   3067  CG  ASN B 403      24.335  59.608   8.453  1.00 91.28           C  
ANISOU 3067  CG  ASN B 403    16512   8496   9672    598  -1949   1979       C  
ATOM   3068  OD1 ASN B 403      23.582  60.221   7.684  1.00 89.37           O  
ANISOU 3068  OD1 ASN B 403    16053   8384   9519    432  -1854   1904       O  
ATOM   3069  ND2 ASN B 403      23.882  58.878   9.460  1.00 94.25           N  
ANISOU 3069  ND2 ASN B 403    17150   8734   9927    477  -1943   2148       N  
ATOM   3070  N   GLN B 404      27.659  61.578   5.756  1.00 79.92           N  
ANISOU 3070  N   GLN B 404    14344   7447   8574   1392  -2081   1509       N  
ATOM   3071  CA  GLN B 404      28.050  62.929   5.367  1.00 76.96           C  
ANISOU 3071  CA  GLN B 404    13604   7350   8284   1450  -2043   1407       C  
ATOM   3072  C   GLN B 404      27.268  63.292   4.111  1.00 73.76           C  
ANISOU 3072  C   GLN B 404    13069   6992   7962   1297  -1936   1300       C  
ATOM   3073  O   GLN B 404      27.149  62.474   3.197  1.00 73.72           O  
ANISOU 3073  O   GLN B 404    13221   6804   7985   1311  -1938   1256       O  
ATOM   3074  CB  GLN B 404      29.551  62.988   5.070  1.00 78.79           C  
ANISOU 3074  CB  GLN B 404    13725   7622   8590   1781  -2134   1364       C  
ATOM   3075  CG  GLN B 404      30.466  62.634   6.251  1.00 81.26           C  
ANISOU 3075  CG  GLN B 404    14142   7896   8834   1965  -2275   1473       C  
ATOM   3076  CD  GLN B 404      31.085  63.846   6.915  1.00 80.93           C  
ANISOU 3076  CD  GLN B 404    13832   8110   8805   2015  -2335   1472       C  
ATOM   3077  OE1 GLN B 404      32.192  63.777   7.434  1.00 85.42           O  
ANISOU 3077  OE1 GLN B 404    14369   8702   9383   2230  -2472   1522       O  
ATOM   3078  NE2 GLN B 404      30.388  64.968   6.880  1.00 80.69           N  
ANISOU 3078  NE2 GLN B 404    13610   8267   8781   1819  -2245   1417       N  
ATOM   3079  N   PHE B 405      26.734  64.507   4.066  1.00 69.70           N  
ANISOU 3079  N   PHE B 405    12292   6710   7479   1158  -1853   1256       N  
ATOM   3080  CA  PHE B 405      25.892  64.920   2.953  1.00 67.43           C  
ANISOU 3080  CA  PHE B 405    11875   6482   7264    997  -1761   1169       C  
ATOM   3081  C   PHE B 405      26.592  65.921   2.058  1.00 64.78           C  
ANISOU 3081  C   PHE B 405    11258   6328   7027   1140  -1739   1048       C  
ATOM   3082  O   PHE B 405      27.422  66.694   2.513  1.00 63.78           O  
ANISOU 3082  O   PHE B 405    10959   6355   6919   1276  -1771   1043       O  
ATOM   3083  CB  PHE B 405      24.563  65.471   3.454  1.00 66.41           C  
ANISOU 3083  CB  PHE B 405    11668   6463   7099    715  -1665   1224       C  
ATOM   3084  CG  PHE B 405      23.639  64.408   3.974  1.00 68.37           C  
ANISOU 3084  CG  PHE B 405    12176   6523   7276    517  -1658   1346       C  
ATOM   3085  CD1 PHE B 405      23.881  63.808   5.194  1.00 70.03           C  
ANISOU 3085  CD1 PHE B 405    12594   6635   7378    553  -1702   1468       C  
ATOM   3086  CD2 PHE B 405      22.537  63.999   3.235  1.00 69.03           C  
ANISOU 3086  CD2 PHE B 405    12300   6525   7401    285  -1618   1349       C  
ATOM   3087  CE1 PHE B 405      23.039  62.825   5.681  1.00 72.54           C  
ANISOU 3087  CE1 PHE B 405    13156   6775   7631    358  -1687   1598       C  
ATOM   3088  CE2 PHE B 405      21.689  63.015   3.714  1.00 70.99           C  
ANISOU 3088  CE2 PHE B 405    12776   6598   7598     76  -1618   1479       C  
ATOM   3089  CZ  PHE B 405      21.939  62.428   4.941  1.00 73.04           C  
ANISOU 3089  CZ  PHE B 405    13242   6759   7750    111  -1643   1607       C  
ATOM   3090  N   PHE B 406      26.251  65.879   0.772  1.00 62.94           N  
ANISOU 3090  N   PHE B 406    10994   6066   6853   1100  -1693    958       N  
ATOM   3091  CA  PHE B 406      26.837  66.752  -0.240  1.00 60.44           C  
ANISOU 3091  CA  PHE B 406    10435   5903   6624   1224  -1654    849       C  
ATOM   3092  C   PHE B 406      25.779  67.163  -1.249  1.00 58.77           C  
ANISOU 3092  C   PHE B 406    10144   5739   6445   1029  -1581    780       C  
ATOM   3093  O   PHE B 406      24.676  66.616  -1.249  1.00 58.65           O  
ANISOU 3093  O   PHE B 406    10270   5616   6397    812  -1578    816       O  
ATOM   3094  CB  PHE B 406      27.927  65.999  -0.994  1.00 61.67           C  
ANISOU 3094  CB  PHE B 406    10697   5930   6804   1494  -1688    804       C  
ATOM   3095  CG  PHE B 406      29.017  65.483  -0.117  1.00 62.20           C  
ANISOU 3095  CG  PHE B 406    10841   5939   6853   1715  -1774    879       C  
ATOM   3096  CD1 PHE B 406      28.925  64.225   0.451  1.00 64.15           C  
ANISOU 3096  CD1 PHE B 406    11406   5945   7022   1732  -1842    954       C  
ATOM   3097  CD2 PHE B 406      30.126  66.263   0.150  1.00 61.50           C  
ANISOU 3097  CD2 PHE B 406    10505   6033   6828   1897  -1800    884       C  
ATOM   3098  CE1 PHE B 406      29.929  63.752   1.266  1.00 65.62           C  
ANISOU 3098  CE1 PHE B 406    11666   6078   7188   1948  -1933   1031       C  
ATOM   3099  CE2 PHE B 406      31.133  65.796   0.967  1.00 63.42           C  
ANISOU 3099  CE2 PHE B 406    10801   6233   7061   2101  -1902    964       C  
ATOM   3100  CZ  PHE B 406      31.036  64.540   1.526  1.00 64.91           C  
ANISOU 3100  CZ  PHE B 406    11311   6186   7166   2137  -1968   1036       C  
ATOM   3101  N   ALA B 407      26.129  68.136  -2.091  1.00 56.18           N  
ANISOU 3101  N   ALA B 407     9582   5576   6185   1100  -1532    693       N  
ATOM   3102  CA  ALA B 407      25.352  68.466  -3.271  1.00 55.95           C  
ANISOU 3102  CA  ALA B 407     9493   5578   6185    974  -1481    616       C  
ATOM   3103  C   ALA B 407      26.163  68.007  -4.468  1.00 57.28           C  
ANISOU 3103  C   ALA B 407     9743   5654   6364   1180  -1478    532       C  
ATOM   3104  O   ALA B 407      27.276  68.492  -4.689  1.00 56.13           O  
ANISOU 3104  O   ALA B 407     9446   5615   6264   1396  -1452    505       O  
ATOM   3105  CB  ALA B 407      25.109  69.956  -3.356  1.00 54.03           C  
ANISOU 3105  CB  ALA B 407     8946   5584   5997    907  -1417    587       C  
ATOM   3106  N   ILE B 408      25.627  67.047  -5.218  1.00 59.17           N  
ANISOU 3106  N   ILE B 408    10232   5691   6558   1115  -1507    496       N  
ATOM   3107  CA  ILE B 408      26.283  66.579  -6.441  1.00 60.89           C  
ANISOU 3107  CA  ILE B 408    10576   5803   6755   1315  -1492    404       C  
ATOM   3108  C   ILE B 408      25.598  67.158  -7.683  1.00 59.96           C  
ANISOU 3108  C   ILE B 408    10387   5753   6640   1197  -1456    316       C  
ATOM   3109  O   ILE B 408      24.393  66.975  -7.874  1.00 58.83           O  
ANISOU 3109  O   ILE B 408    10324   5549   6478    941  -1502    319       O  
ATOM   3110  CB  ILE B 408      26.286  65.042  -6.544  1.00 63.46           C  
ANISOU 3110  CB  ILE B 408    11296   5812   7001   1364  -1565    406       C  
ATOM   3111  CG1 ILE B 408      26.964  64.427  -5.318  1.00 64.28           C  
ANISOU 3111  CG1 ILE B 408    11491   5836   7095   1493  -1611    502       C  
ATOM   3112  CG2 ILE B 408      26.997  64.607  -7.824  1.00 65.17           C  
ANISOU 3112  CG2 ILE B 408    11664   5921   7176   1607  -1530    301       C  
ATOM   3113  CD1 ILE B 408      27.012  62.916  -5.320  1.00 67.03           C  
ANISOU 3113  CD1 ILE B 408    12246   5855   7364   1556  -1687    516       C  
ATOM   3114  N   LYS B 409      26.379  67.858  -8.505  1.00 60.03           N  
ANISOU 3114  N   LYS B 409    10236   5895   6675   1382  -1377    252       N  
ATOM   3115  CA  LYS B 409      25.946  68.283  -9.837  1.00 60.68           C  
ANISOU 3115  CA  LYS B 409    10304   6015   6735   1333  -1342    163       C  
ATOM   3116  C   LYS B 409      26.309  67.207 -10.865  1.00 63.95           C  
ANISOU 3116  C   LYS B 409    11045   6200   7052   1498  -1350     83       C  
ATOM   3117  O   LYS B 409      27.493  66.865 -11.026  1.00 63.78           O  
ANISOU 3117  O   LYS B 409    11069   6144   7018   1795  -1289     71       O  
ATOM   3118  CB  LYS B 409      26.585  69.615 -10.240  1.00 59.73           C  
ANISOU 3118  CB  LYS B 409     9863   6148   6681   1442  -1240    143       C  
ATOM   3119  CG  LYS B 409      26.020  70.208 -11.531  1.00 59.28           C  
ANISOU 3119  CG  LYS B 409     9774   6153   6597   1364  -1207     67       C  
ATOM   3120  CD  LYS B 409      26.430  71.660 -11.754  1.00 57.73           C  
ANISOU 3120  CD  LYS B 409     9245   6212   6474   1405  -1116     71       C  
ATOM   3121  CE  LYS B 409      27.909  71.800 -12.081  1.00 58.91           C  
ANISOU 3121  CE  LYS B 409     9304   6428   6649   1700  -1017     72       C  
ATOM   3122  NZ  LYS B 409      28.292  73.210 -12.387  1.00 58.55           N  
ANISOU 3122  NZ  LYS B 409     8948   6617   6679   1713   -934     85       N  
ATOM   3123  N   ALA B 410      25.289  66.681 -11.548  1.00 65.69           N  
ANISOU 3123  N   ALA B 410    11493   6263   7201   1309  -1430     33       N  
ATOM   3124  CA  ALA B 410      25.477  65.662 -12.593  1.00 68.79           C  
ANISOU 3124  CA  ALA B 410    12254   6408   7473   1437  -1458    -59       C  
ATOM   3125  C   ALA B 410      25.250  66.252 -13.973  1.00 69.33           C  
ANISOU 3125  C   ALA B 410    12307   6548   7485   1437  -1421   -155       C  
ATOM   3126  O   ALA B 410      24.242  66.931 -14.203  1.00 67.10           O  
ANISOU 3126  O   ALA B 410    11886   6376   7233   1184  -1469   -152       O  
ATOM   3127  CB  ALA B 410      24.534  64.487 -12.372  1.00 71.31           C  
ANISOU 3127  CB  ALA B 410    12910   6448   7734   1215  -1611    -46       C  
ATOM   3128  N   LEU B 411      26.198  66.004 -14.877  1.00 71.31           N  
ANISOU 3128  N   LEU B 411    12699   6743   7653   1736  -1329   -230       N  
ATOM   3129  CA  LEU B 411      26.088  66.428 -16.269  1.00 73.18           C  
ANISOU 3129  CA  LEU B 411    12991   7016   7798   1777  -1283   -325       C  
ATOM   3130  C   LEU B 411      26.159  65.215 -17.185  1.00 76.46           C  
ANISOU 3130  C   LEU B 411    13889   7123   8037   1904  -1330   -429       C  
ATOM   3131  O   LEU B 411      26.946  64.287 -16.954  1.00 77.28           O  
ANISOU 3131  O   LEU B 411    14211   7055   8097   2145  -1298   -435       O  
ATOM   3132  CB  LEU B 411      27.222  67.376 -16.660  1.00 73.63           C  
ANISOU 3132  CB  LEU B 411    12771   7310   7894   2043  -1092   -318       C  
ATOM   3133  CG  LEU B 411      27.537  68.601 -15.811  1.00 72.74           C  
ANISOU 3133  CG  LEU B 411    12199   7491   7947   2000  -1026   -223       C  
ATOM   3134  CD1 LEU B 411      28.606  69.439 -16.511  1.00 73.27           C  
ANISOU 3134  CD1 LEU B 411    12053   7753   8032   2245   -847   -223       C  
ATOM   3135  CD2 LEU B 411      26.298  69.436 -15.558  1.00 71.84           C  
ANISOU 3135  CD2 LEU B 411    11902   7498   7893   1662  -1113   -198       C  
ATOM   3136  N   LYS B 412      25.342  65.243 -18.234  1.00 77.81           N  
ANISOU 3136  N   LYS B 412    14240   7222   8101   1753  -1414   -511       N  
ATOM   3137  CA  LYS B 412      25.363  64.218 -19.272  1.00 81.67           C  
ANISOU 3137  CA  LYS B 412    15219   7417   8392   1868  -1468   -630       C  
ATOM   3138  C   LYS B 412      26.440  64.568 -20.299  1.00 81.61           C  
ANISOU 3138  C   LYS B 412    15233   7495   8280   2234  -1265   -698       C  
ATOM   3139  O   LYS B 412      26.429  65.671 -20.859  1.00 76.31           O  
ANISOU 3139  O   LYS B 412    14307   7060   7626   2219  -1178   -696       O  
ATOM   3140  CB  LYS B 412      23.985  64.108 -19.931  1.00 83.16           C  
ANISOU 3140  CB  LYS B 412    15595   7494   8508   1524  -1676   -683       C  
ATOM   3141  CG  LYS B 412      23.014  63.241 -19.150  1.00 86.08           C  
ANISOU 3141  CG  LYS B 412    16122   7657   8925   1210  -1886   -631       C  
ATOM   3142  CD  LYS B 412      21.577  63.694 -19.328  1.00 87.96           C  
ANISOU 3142  CD  LYS B 412    16238   7966   9215    799  -2062   -602       C  
ATOM   3143  CE  LYS B 412      20.602  62.673 -18.758  1.00 91.54           C  
ANISOU 3143  CE  LYS B 412    16910   8176   9694    480  -2279   -551       C  
ATOM   3144  NZ  LYS B 412      19.243  63.270 -18.607  1.00 92.45           N  
ANISOU 3144  NZ  LYS B 412    16759   8442   9925     81  -2414   -469       N  
ATOM   3145  N   LYS B 413      27.366  63.631 -20.536  1.00 83.75           N  
ANISOU 3145  N   LYS B 413    15806   7572   8442   2569  -1179   -747       N  
ATOM   3146  CA  LYS B 413      28.489  63.871 -21.454  1.00 85.20           C  
ANISOU 3146  CA  LYS B 413    16006   7839   8526   2960   -948   -792       C  
ATOM   3147  C   LYS B 413      28.020  64.211 -22.880  1.00 87.40           C  
ANISOU 3147  C   LYS B 413    16481   8104   8622   2923   -951   -899       C  
ATOM   3148  O   LYS B 413      28.607  65.065 -23.545  1.00 87.35           O  
ANISOU 3148  O   LYS B 413    16278   8313   8595   3095   -762   -892       O  
ATOM   3149  CB  LYS B 413      29.455  62.681 -21.469  1.00 87.63           C  
ANISOU 3149  CB  LYS B 413    16651   7909   8734   3337   -864   -828       C  
ATOM   3150  CG  LYS B 413      30.423  62.656 -20.298  1.00 86.53           C  
ANISOU 3150  CG  LYS B 413    16215   7888   8773   3525   -768   -705       C  
ATOM   3151  CD  LYS B 413      31.190  61.343 -20.223  1.00 89.46           C  
ANISOU 3151  CD  LYS B 413    16961   7981   9049   3868   -730   -735       C  
ATOM   3152  CE  LYS B 413      32.329  61.427 -19.213  1.00 89.02           C  
ANISOU 3152  CE  LYS B 413    16569   8085   9167   4117   -613   -605       C  
ATOM   3153  NZ  LYS B 413      33.073  60.153 -19.039  1.00 91.06           N  
ANISOU 3153  NZ  LYS B 413    17169   8077   9350   4465   -584   -617       N  
ATOM   3154  N   ASP B 414      26.948  63.564 -23.329  1.00 90.25           N  
ANISOU 3154  N   ASP B 414    17224   8211   8853   2682  -1175   -986       N  
ATOM   3155  CA  ASP B 414      26.411  63.791 -24.675  1.00 91.86           C  
ANISOU 3155  CA  ASP B 414    17668   8370   8863   2624  -1227  -1093       C  
ATOM   3156  C   ASP B 414      25.903  65.223 -24.875  1.00 88.60           C  
ANISOU 3156  C   ASP B 414    16831   8280   8552   2415  -1213  -1035       C  
ATOM   3157  O   ASP B 414      26.086  65.795 -25.950  1.00 88.31           O  
ANISOU 3157  O   ASP B 414    16832   8335   8384   2531  -1113  -1084       O  
ATOM   3158  CB  ASP B 414      25.309  62.767 -25.005  1.00 94.98           C  
ANISOU 3158  CB  ASP B 414    18550   8415   9120   2361  -1520  -1186       C  
ATOM   3159  CG  ASP B 414      24.033  62.983 -24.196  1.00 94.88           C  
ANISOU 3159  CG  ASP B 414    18314   8448   9285   1887  -1758  -1102       C  
ATOM   3160  OD1 ASP B 414      24.117  63.398 -23.021  1.00 94.75           O  
ANISOU 3160  OD1 ASP B 414    17896   8615   9487   1808  -1708   -979       O  
ATOM   3161  OD2 ASP B 414      22.937  62.736 -24.736  1.00 97.26           O  
ANISOU 3161  OD2 ASP B 414    18843   8605   9503   1595  -1996  -1154       O  
ATOM   3162  N   VAL B 415      25.283  65.800 -23.842  1.00 85.52           N  
ANISOU 3162  N   VAL B 415    16056   8054   8382   2125  -1303   -929       N  
ATOM   3163  CA  VAL B 415      24.757  67.169 -23.920  1.00 82.02           C  
ANISOU 3163  CA  VAL B 415    15208   7905   8048   1929  -1297   -868       C  
ATOM   3164  C   VAL B 415      25.883  68.204 -23.824  1.00 81.60           C  
ANISOU 3164  C   VAL B 415    14771   8143   8088   2177  -1031   -798       C  
ATOM   3165  O   VAL B 415      25.801  69.282 -24.420  1.00 79.62           O  
ANISOU 3165  O   VAL B 415    14318   8095   7837   2151   -962   -782       O  
ATOM   3166  CB  VAL B 415      23.690  67.421 -22.833  1.00 78.99           C  
ANISOU 3166  CB  VAL B 415    14562   7593   7858   1554  -1470   -776       C  
ATOM   3167  CG1 VAL B 415      23.278  68.883 -22.799  1.00 75.61           C  
ANISOU 3167  CG1 VAL B 415    13698   7476   7554   1407  -1432   -706       C  
ATOM   3168  CG2 VAL B 415      22.476  66.534 -23.083  1.00 80.26           C  
ANISOU 3168  CG2 VAL B 415    15060   7496   7937   1262  -1743   -826       C  
ATOM   3169  N   VAL B 416      26.927  67.874 -23.066  1.00 83.27           N  
ANISOU 3169  N   VAL B 416    14883   8370   8386   2409   -895   -747       N  
ATOM   3170  CA  VAL B 416      28.115  68.727 -22.970  1.00 83.53           C  
ANISOU 3170  CA  VAL B 416    14562   8660   8515   2656   -652   -670       C  
ATOM   3171  C   VAL B 416      28.822  68.819 -24.326  1.00 86.62           C  
ANISOU 3171  C   VAL B 416    15127   9062   8721   2947   -464   -730       C  
ATOM   3172  O   VAL B 416      29.146  69.915 -24.789  1.00 84.42           O  
ANISOU 3172  O   VAL B 416    14584   9017   8472   2986   -325   -683       O  
ATOM   3173  CB  VAL B 416      29.101  68.199 -21.906  1.00 83.87           C  
ANISOU 3173  CB  VAL B 416    14494   8694   8678   2857   -574   -600       C  
ATOM   3174  CG1 VAL B 416      30.448  68.908 -22.007  1.00 84.24           C  
ANISOU 3174  CG1 VAL B 416    14223   8979   8802   3150   -323   -522       C  
ATOM   3175  CG2 VAL B 416      28.511  68.368 -20.510  1.00 82.00           C  
ANISOU 3175  CG2 VAL B 416    14020   8508   8627   2583   -721   -518       C  
ATOM   3176  N   LEU B 417      29.076  67.661 -24.933  1.00 91.50           N  
ANISOU 3176  N   LEU B 417    16205   9418   9143   3157   -453   -829       N  
ATOM   3177  CA  LEU B 417      29.601  67.588 -26.300  1.00 97.94           C  
ANISOU 3177  CA  LEU B 417    17288  10195   9730   3435   -285   -906       C  
ATOM   3178  C   LEU B 417      28.693  68.359 -27.244  1.00 99.23           C  
ANISOU 3178  C   LEU B 417    17493  10423   9785   3214   -372   -950       C  
ATOM   3179  O   LEU B 417      29.148  69.238 -27.975  1.00101.08           O  
ANISOU 3179  O   LEU B 417    17576  10852   9976   3336   -190   -919       O  
ATOM   3180  CB  LEU B 417      29.686  66.131 -26.796  1.00101.93           C  
ANISOU 3180  CB  LEU B 417    18380  10342  10007   3632   -328  -1032       C  
ATOM   3181  CG  LEU B 417      30.924  65.235 -26.587  1.00106.17           C  
ANISOU 3181  CG  LEU B 417    19052  10773  10514   4057   -140  -1027       C  
ATOM   3182  CD1 LEU B 417      32.190  66.042 -26.366  1.00106.03           C  
ANISOU 3182  CD1 LEU B 417    18560  11075  10650   4323    149   -895       C  
ATOM   3183  CD2 LEU B 417      30.764  64.227 -25.455  1.00106.71           C  
ANISOU 3183  CD2 LEU B 417    19233  10629  10680   3988   -305  -1016       C  
ATOM   3184  N   MET B 418      27.405  68.026 -27.195  1.00102.72           N  
ANISOU 3184  N   MET B 418    18129  10705  10195   2882   -657  -1008       N  
ATOM   3185  CA  MET B 418      26.371  68.619 -28.052  1.00105.32           C  
ANISOU 3185  CA  MET B 418    18532  11062  10422   2639   -804  -1051       C  
ATOM   3186  C   MET B 418      26.357  70.148 -28.065  1.00101.03           C  
ANISOU 3186  C   MET B 418    17517  10852  10016   2548   -706   -951       C  
ATOM   3187  O   MET B 418      26.231  70.754 -29.130  1.00103.53           O  
ANISOU 3187  O   MET B 418    17904  11239  10190   2574   -663   -977       O  
ATOM   3188  CB  MET B 418      25.003  68.106 -27.603  1.00109.60           C  
ANISOU 3188  CB  MET B 418    19199  11434  11007   2253  -1134  -1077       C  
ATOM   3189  CG  MET B 418      23.807  68.700 -28.319  1.00113.18           C  
ANISOU 3189  CG  MET B 418    19673  11928  11400   1961  -1334  -1100       C  
ATOM   3190  SD  MET B 418      22.285  68.083 -27.580  1.00119.19           S  
ANISOU 3190  SD  MET B 418    20480  12530  12276   1503  -1699  -1085       S  
ATOM   3191  CE  MET B 418      22.307  66.389 -28.166  1.00118.52           C  
ANISOU 3191  CE  MET B 418    21093  12003  11936   1591  -1842  -1233       C  
ATOM   3192  N   ASP B 419      26.472  70.772 -26.896  1.00 94.65           N  
ANISOU 3192  N   ASP B 419    16257  10236   9469   2441   -680   -837       N  
ATOM   3193  CA  ASP B 419      26.466  72.234 -26.811  1.00 90.54           C  
ANISOU 3193  CA  ASP B 419    15302  10010   9088   2348   -599   -740       C  
ATOM   3194  C   ASP B 419      27.895  72.761 -26.773  1.00 89.68           C  
ANISOU 3194  C   ASP B 419    14942  10087   9045   2645   -306   -661       C  
ATOM   3195  O   ASP B 419      28.142  73.868 -26.291  1.00 87.50           O  
ANISOU 3195  O   ASP B 419    14253  10046   8946   2582   -231   -558       O  
ATOM   3196  CB  ASP B 419      25.687  72.705 -25.577  1.00 88.68           C  
ANISOU 3196  CB  ASP B 419    14732   9874   9086   2046   -749   -663       C  
ATOM   3197  CG  ASP B 419      24.394  71.933 -25.366  1.00 89.26           C  
ANISOU 3197  CG  ASP B 419    15029   9752   9133   1765  -1025   -714       C  
ATOM   3198  OD1 ASP B 419      23.939  71.253 -26.303  1.00 92.92           O  
ANISOU 3198  OD1 ASP B 419    15886  10021   9399   1749  -1140   -812       O  
ATOM   3199  OD2 ASP B 419      23.832  71.990 -24.257  1.00 89.41           O  
ANISOU 3199  OD2 ASP B 419    14836   9808   9325   1555  -1129   -651       O  
ATOM   3200  N   ASP B 420      28.832  71.951 -27.268  1.00 92.15           N  
ANISOU 3200  N   ASP B 420    15505  10288   9218   2970   -146   -705       N  
ATOM   3201  CA  ASP B 420      30.251  72.294 -27.302  1.00 93.04           C  
ANISOU 3201  CA  ASP B 420    15390  10571   9389   3282    143   -619       C  
ATOM   3202  C   ASP B 420      30.762  72.891 -25.974  1.00 89.64           C  
ANISOU 3202  C   ASP B 420    14471  10336   9251   3221    171   -488       C  
ATOM   3203  O   ASP B 420      31.482  73.895 -25.964  1.00 87.05           O  
ANISOU 3203  O   ASP B 420    13790  10245   9039   3282    334   -381       O  
ATOM   3204  CB  ASP B 420      30.502  73.256 -28.466  1.00 94.02           C  
ANISOU 3204  CB  ASP B 420    15464  10856   9403   3363    314   -592       C  
ATOM   3205  CG  ASP B 420      31.849  73.051 -29.096  1.00 97.43           C  
ANISOU 3205  CG  ASP B 420    15931  11343   9744   3762    625   -557       C  
ATOM   3206  OD1 ASP B 420      32.726  73.919 -28.921  1.00 98.34           O  
ANISOU 3206  OD1 ASP B 420    15648  11703  10011   3849    820   -424       O  
ATOM   3207  OD2 ASP B 420      32.036  72.008 -29.754  1.00100.64           O  
ANISOU 3207  OD2 ASP B 420    16766  11544   9928   3991    675   -658       O  
ATOM   3208  N   ASP B 421      30.386  72.264 -24.861  1.00 86.36           N  
ANISOU 3208  N   ASP B 421    14057   9810   8944   3091      2   -493       N  
ATOM   3209  CA  ASP B 421      30.730  72.766 -23.522  1.00 83.74           C  
ANISOU 3209  CA  ASP B 421    13317   9635   8864   3005    -14   -381       C  
ATOM   3210  C   ASP B 421      31.884  72.028 -22.859  1.00 80.00           C  
ANISOU 3210  C   ASP B 421    12795   9134   8464   3275     85   -332       C  
ATOM   3211  O   ASP B 421      32.111  72.187 -21.655  1.00 75.54           O  
ANISOU 3211  O   ASP B 421    11969   8647   8084   3203     25   -252       O  
ATOM   3212  CB  ASP B 421      29.510  72.682 -22.600  1.00 83.91           C  
ANISOU 3212  CB  ASP B 421    13330   9582   8967   2667   -264   -396       C  
ATOM   3213  CG  ASP B 421      28.638  73.902 -22.681  1.00 85.05           C  
ANISOU 3213  CG  ASP B 421    13257   9883   9175   2396   -338   -370       C  
ATOM   3214  OD1 ASP B 421      29.183  75.024 -22.781  1.00 86.29           O  
ANISOU 3214  OD1 ASP B 421    13110  10254   9419   2431   -211   -295       O  
ATOM   3215  OD2 ASP B 421      27.401  73.734 -22.633  1.00 85.28           O  
ANISOU 3215  OD2 ASP B 421    13414   9817   9171   2145   -526   -416       O  
ATOM   3216  N   VAL B 422      32.622  71.240 -23.633  1.00 80.59           N  
ANISOU 3216  N   VAL B 422    13126   9104   8391   3598    238   -373       N  
ATOM   3217  CA  VAL B 422      33.642  70.373 -23.055  1.00 81.28           C  
ANISOU 3217  CA  VAL B 422    13219   9131   8532   3882    319   -333       C  
ATOM   3218  C   VAL B 422      34.640  71.208 -22.281  1.00 79.45           C  
ANISOU 3218  C   VAL B 422    12477   9172   8538   3941    422   -178       C  
ATOM   3219  O   VAL B 422      34.910  70.929 -21.115  1.00 78.55           O  
ANISOU 3219  O   VAL B 422    12216   9056   8570   3925    330   -118       O  
ATOM   3220  CB  VAL B 422      34.395  69.544 -24.114  1.00 84.92           C  
ANISOU 3220  CB  VAL B 422    14003   9469   8792   4275    518   -390       C  
ATOM   3221  CG1 VAL B 422      35.567  68.789 -23.487  1.00 85.99           C  
ANISOU 3221  CG1 VAL B 422    14067   9587   9016   4604    625   -320       C  
ATOM   3222  CG2 VAL B 422      33.449  68.564 -24.782  1.00 87.02           C  
ANISOU 3222  CG2 VAL B 422    14832   9417   8812   4220    378   -553       C  
ATOM   3223  N   GLU B 423      35.170  72.241 -22.925  1.00 78.02           N  
ANISOU 3223  N   GLU B 423    12035   9216   8390   3994    598   -107       N  
ATOM   3224  CA  GLU B 423      36.175  73.073 -22.289  1.00 77.54           C  
ANISOU 3224  CA  GLU B 423    11488   9414   8558   4039    690     48       C  
ATOM   3225  C   GLU B 423      35.628  73.758 -21.031  1.00 74.81           C  
ANISOU 3225  C   GLU B 423    10880   9145   8398   3709    478     93       C  
ATOM   3226  O   GLU B 423      36.336  73.838 -20.025  1.00 72.73           O  
ANISOU 3226  O   GLU B 423    10344   8976   8311   3746    447    192       O  
ATOM   3227  CB  GLU B 423      36.734  74.103 -23.272  1.00 77.89           C  
ANISOU 3227  CB  GLU B 423    11321   9674   8598   4111    911    123       C  
ATOM   3228  CG  GLU B 423      37.930  74.891 -22.755  1.00 78.11           C  
ANISOU 3228  CG  GLU B 423    10849   9965   8862   4183   1025    302       C  
ATOM   3229  CD  GLU B 423      39.057  74.009 -22.246  1.00 81.17           C  
ANISOU 3229  CD  GLU B 423    11155  10352   9335   4497   1105    374       C  
ATOM   3230  OE1 GLU B 423      39.253  72.890 -22.764  1.00 84.19           O  
ANISOU 3230  OE1 GLU B 423    11863  10569   9556   4781   1202    303       O  
ATOM   3231  OE2 GLU B 423      39.758  74.437 -21.310  1.00 81.36           O  
ANISOU 3231  OE2 GLU B 423    10794  10533   9584   4467   1061    504       O  
ATOM   3232  N   CYS B 424      34.379  74.225 -21.081  1.00 71.60           N  
ANISOU 3232  N   CYS B 424    10565   8695   7945   3402    329     23       N  
ATOM   3233  CA  CYS B 424      33.756  74.894 -19.928  1.00 70.23           C  
ANISOU 3233  CA  CYS B 424    10175   8587   7922   3101    146     57       C  
ATOM   3234  C   CYS B 424      33.794  74.013 -18.683  1.00 68.93           C  
ANISOU 3234  C   CYS B 424    10060   8305   7823   3103      8     66       C  
ATOM   3235  O   CYS B 424      34.128  74.472 -17.590  1.00 67.25           O  
ANISOU 3235  O   CYS B 424     9576   8202   7772   3026    -60    149       O  
ATOM   3236  CB  CYS B 424      32.296  75.260 -20.223  1.00 68.27           C  
ANISOU 3236  CB  CYS B 424    10077   8273   7588   2810      9    -26       C  
ATOM   3237  SG  CYS B 424      32.093  76.623 -21.376  1.00 70.45           S  
ANISOU 3237  SG  CYS B 424    10225   8715   7825   2728    115    -11       S  
ATOM   3238  N   THR B 425      33.431  72.751 -18.873  1.00 70.80           N  
ANISOU 3238  N   THR B 425    10672   8306   7921   3187    -39    -21       N  
ATOM   3239  CA  THR B 425      33.413  71.759 -17.805  1.00 70.39           C  
ANISOU 3239  CA  THR B 425    10741   8102   7901   3201   -166    -15       C  
ATOM   3240  C   THR B 425      34.805  71.514 -17.242  1.00 71.06           C  
ANISOU 3240  C   THR B 425    10624   8270   8103   3476    -81     86       C  
ATOM   3241  O   THR B 425      34.982  71.420 -16.028  1.00 70.81           O  
ANISOU 3241  O   THR B 425    10463   8254   8187   3422   -196    151       O  
ATOM   3242  CB  THR B 425      32.821  70.439 -18.330  1.00 72.30           C  
ANISOU 3242  CB  THR B 425    11464   8050   7955   3255   -222   -130       C  
ATOM   3243  OG1 THR B 425      31.466  70.668 -18.737  1.00 72.44           O  
ANISOU 3243  OG1 THR B 425    11636   7998   7888   2961   -341   -209       O  
ATOM   3244  CG2 THR B 425      32.834  69.372 -17.270  1.00 73.56           C  
ANISOU 3244  CG2 THR B 425    11776   8032   8139   3279   -346   -115       C  
ATOM   3245  N   MET B 426      35.788  71.399 -18.128  1.00 71.96           N  
ANISOU 3245  N   MET B 426    10716   8443   8182   3780    120    108       N  
ATOM   3246  CA  MET B 426      37.175  71.207 -17.716  1.00 73.12           C  
ANISOU 3246  CA  MET B 426    10626   8699   8455   4067    220    225       C  
ATOM   3247  C   MET B 426      37.714  72.459 -17.029  1.00 70.56           C  
ANISOU 3247  C   MET B 426     9816   8647   8345   3936    200    356       C  
ATOM   3248  O   MET B 426      38.461  72.361 -16.056  1.00 69.13           O  
ANISOU 3248  O   MET B 426     9422   8535   8309   4010    137    455       O  
ATOM   3249  CB  MET B 426      38.060  70.853 -18.918  1.00 75.26           C  
ANISOU 3249  CB  MET B 426    10973   8989   8634   4431    474    228       C  
ATOM   3250  CG  MET B 426      37.663  69.573 -19.636  1.00 77.19           C  
ANISOU 3250  CG  MET B 426    11740   8942   8647   4605    498     93       C  
ATOM   3251  SD  MET B 426      37.662  68.142 -18.549  1.00 78.18           S  
ANISOU 3251  SD  MET B 426    12128   8806   8772   4703    328     77       S  
ATOM   3252  CE  MET B 426      39.407  68.019 -18.154  1.00 80.31           C  
ANISOU 3252  CE  MET B 426    12043   9258   9212   5110    489    242       C  
ATOM   3253  N   VAL B 427      37.332  73.630 -17.537  1.00 69.01           N  
ANISOU 3253  N   VAL B 427     9461   8593   8164   3739    238    356       N  
ATOM   3254  CA  VAL B 427      37.684  74.891 -16.881  1.00 67.71           C  
ANISOU 3254  CA  VAL B 427     8882   8653   8190   3564    189    466       C  
ATOM   3255  C   VAL B 427      37.096  74.879 -15.472  1.00 64.44           C  
ANISOU 3255  C   VAL B 427     8460   8180   7842   3338    -47    460       C  
ATOM   3256  O   VAL B 427      37.770  75.233 -14.509  1.00 63.19           O  
ANISOU 3256  O   VAL B 427     8036   8135   7838   3324   -128    561       O  
ATOM   3257  CB  VAL B 427      37.180  76.131 -17.659  1.00 67.92           C  
ANISOU 3257  CB  VAL B 427     8807   8799   8200   3368    250    454       C  
ATOM   3258  CG1 VAL B 427      37.234  77.386 -16.786  1.00 66.84           C  
ANISOU 3258  CG1 VAL B 427     8331   8827   8238   3124    136    537       C  
ATOM   3259  CG2 VAL B 427      37.984  76.338 -18.939  1.00 70.14           C  
ANISOU 3259  CG2 VAL B 427     9018   9189   8440   3594    505    501       C  
ATOM   3260  N   GLU B 428      35.845  74.454 -15.359  1.00 63.05           N  
ANISOU 3260  N   GLU B 428     8581   7829   7545   3162   -160    350       N  
ATOM   3261  CA  GLU B 428      35.168  74.453 -14.069  1.00 62.26           C  
ANISOU 3261  CA  GLU B 428     8495   7675   7486   2941   -358    349       C  
ATOM   3262  C   GLU B 428      35.919  73.565 -13.074  1.00 62.99           C  
ANISOU 3262  C   GLU B 428     8593   7705   7634   3106   -433    412       C  
ATOM   3263  O   GLU B 428      36.194  73.978 -11.938  1.00 63.41           O  
ANISOU 3263  O   GLU B 428     8454   7841   7798   3018   -553    485       O  
ATOM   3264  CB  GLU B 428      33.706  74.011 -14.221  1.00 61.58           C  
ANISOU 3264  CB  GLU B 428     8725   7409   7261   2741   -445    237       C  
ATOM   3265  CG  GLU B 428      32.983  73.941 -12.886  1.00 62.52           C  
ANISOU 3265  CG  GLU B 428     8866   7475   7411   2527   -620    249       C  
ATOM   3266  CD  GLU B 428      31.481  73.843 -13.008  1.00 61.48           C  
ANISOU 3266  CD  GLU B 428     8941   7233   7185   2278   -698    170       C  
ATOM   3267  OE1 GLU B 428      30.953  74.020 -14.119  1.00 63.69           O  
ANISOU 3267  OE1 GLU B 428     9314   7497   7385   2238   -642    105       O  
ATOM   3268  OE2 GLU B 428      30.825  73.572 -11.988  1.00 60.17           O  
ANISOU 3268  OE2 GLU B 428     8839   6999   7021   2122   -817    183       O  
ATOM   3269  N   LYS B 429      36.262  72.358 -13.514  1.00 64.03           N  
ANISOU 3269  N   LYS B 429     8965   7682   7679   3357   -367    382       N  
ATOM   3270  CA  LYS B 429      37.027  71.417 -12.700  1.00 65.35           C  
ANISOU 3270  CA  LYS B 429     9167   7773   7889   3563   -426    446       C  
ATOM   3271  C   LYS B 429      38.325  72.041 -12.198  1.00 65.41           C  
ANISOU 3271  C   LYS B 429     8764   8005   8080   3687   -412    587       C  
ATOM   3272  O   LYS B 429      38.613  72.007 -10.998  1.00 64.69           O  
ANISOU 3272  O   LYS B 429     8566   7936   8076   3647   -565    658       O  
ATOM   3273  CB  LYS B 429      37.315  70.142 -13.503  1.00 68.60           C  
ANISOU 3273  CB  LYS B 429     9895   7994   8174   3862   -317    391       C  
ATOM   3274  CG  LYS B 429      38.289  69.156 -12.850  1.00 72.37           C  
ANISOU 3274  CG  LYS B 429    10398   8400   8699   4153   -342    468       C  
ATOM   3275  CD  LYS B 429      39.709  69.294 -13.399  1.00 75.41           C  
ANISOU 3275  CD  LYS B 429    10513   8959   9181   4495   -158    565       C  
ATOM   3276  CE  LYS B 429      40.701  68.453 -12.621  1.00 79.13           C  
ANISOU 3276  CE  LYS B 429    10938   9395   9732   4777   -207    665       C  
ATOM   3277  NZ  LYS B 429      42.101  68.783 -13.008  1.00 82.25           N  
ANISOU 3277  NZ  LYS B 429    10961  10020  10267   5072    -41    796       N  
ATOM   3278  N   ARG B 430      39.115  72.599 -13.111  1.00 65.98           N  
ANISOU 3278  N   ARG B 430     8611   8246   8212   3834   -234    636       N  
ATOM   3279  CA  ARG B 430      40.422  73.144 -12.741  1.00 67.69           C  
ANISOU 3279  CA  ARG B 430     8413   8684   8620   3958   -213    790       C  
ATOM   3280  C   ARG B 430      40.289  74.308 -11.763  1.00 65.37           C  
ANISOU 3280  C   ARG B 430     7852   8531   8454   3659   -386    846       C  
ATOM   3281  O   ARG B 430      40.989  74.364 -10.761  1.00 65.92           O  
ANISOU 3281  O   ARG B 430     7723   8674   8649   3680   -521    947       O  
ATOM   3282  CB  ARG B 430      41.214  73.561 -13.980  1.00 70.05           C  
ANISOU 3282  CB  ARG B 430     8519   9143   8953   4148     33    844       C  
ATOM   3283  CG  ARG B 430      41.714  72.377 -14.793  1.00 73.40           C  
ANISOU 3283  CG  ARG B 430     9159   9455   9272   4531    216    822       C  
ATOM   3284  CD  ARG B 430      42.671  72.807 -15.889  1.00 76.23           C  
ANISOU 3284  CD  ARG B 430     9277  10007   9680   4754    483    911       C  
ATOM   3285  NE  ARG B 430      42.026  73.680 -16.871  1.00 75.14           N  
ANISOU 3285  NE  ARG B 430     9174   9919   9455   4570    590    848       N  
ATOM   3286  CZ  ARG B 430      41.424  73.279 -17.992  1.00 76.53           C  
ANISOU 3286  CZ  ARG B 430     9697   9959   9419   4644    724    724       C  
ATOM   3287  NH1 ARG B 430      41.343  71.997 -18.322  1.00 79.27           N  
ANISOU 3287  NH1 ARG B 430    10419  10091   9607   4893    773    636       N  
ATOM   3288  NH2 ARG B 430      40.879  74.180 -18.797  1.00 76.03           N  
ANISOU 3288  NH2 ARG B 430     9628   9965   9294   4463    795    687       N  
ATOM   3289  N   VAL B 431      39.370  75.223 -12.035  1.00 61.30           N  
ANISOU 3289  N   VAL B 431     7354   8039   7895   3385   -395    777       N  
ATOM   3290  CA  VAL B 431      39.129  76.334 -11.120  1.00 59.47           C  
ANISOU 3290  CA  VAL B 431     6930   7909   7757   3105   -557    811       C  
ATOM   3291  C   VAL B 431      38.661  75.842  -9.743  1.00 59.50           C  
ANISOU 3291  C   VAL B 431     7084   7792   7728   3002   -768    794       C  
ATOM   3292  O   VAL B 431      39.190  76.292  -8.711  1.00 59.64           O  
ANISOU 3292  O   VAL B 431     6909   7898   7854   2938   -919    876       O  
ATOM   3293  CB  VAL B 431      38.109  77.340 -11.693  1.00 56.02           C  
ANISOU 3293  CB  VAL B 431     6528   7495   7261   2854   -521    732       C  
ATOM   3294  CG1 VAL B 431      37.726  78.382 -10.645  1.00 53.64           C  
ANISOU 3294  CG1 VAL B 431     6100   7253   7024   2580   -695    747       C  
ATOM   3295  CG2 VAL B 431      38.689  78.015 -12.930  1.00 56.67           C  
ANISOU 3295  CG2 VAL B 431     6422   7722   7387   2933   -326    778       C  
ATOM   3296  N   LEU B 432      37.692  74.924  -9.725  1.00 59.28           N  
ANISOU 3296  N   LEU B 432     7409   7563   7552   2980   -785    695       N  
ATOM   3297  CA  LEU B 432      37.223  74.344  -8.460  1.00 60.47           C  
ANISOU 3297  CA  LEU B 432     7731   7587   7656   2893   -961    691       C  
ATOM   3298  C   LEU B 432      38.365  73.660  -7.669  1.00 64.04           C  
ANISOU 3298  C   LEU B 432     8101   8042   8186   3113  -1049    796       C  
ATOM   3299  O   LEU B 432      38.303  73.582  -6.443  1.00 63.85           O  
ANISOU 3299  O   LEU B 432     8103   7989   8166   3028  -1221    834       O  
ATOM   3300  CB  LEU B 432      36.067  73.359  -8.681  1.00 59.81           C  
ANISOU 3300  CB  LEU B 432     8034   7278   7410   2841   -952    587       C  
ATOM   3301  CG  LEU B 432      34.691  73.985  -8.937  1.00 57.97           C  
ANISOU 3301  CG  LEU B 432     7893   7029   7103   2558   -951    501       C  
ATOM   3302  CD1 LEU B 432      33.692  72.910  -9.332  1.00 58.09           C  
ANISOU 3302  CD1 LEU B 432     8269   6826   6977   2525   -943    416       C  
ATOM   3303  CD2 LEU B 432      34.201  74.768  -7.727  1.00 56.11           C  
ANISOU 3303  CD2 LEU B 432     7566   6857   6896   2327  -1085    527       C  
ATOM   3304  N   SER B 433      39.402  73.197  -8.366  1.00 67.89           N  
ANISOU 3304  N   SER B 433     8488   8574   8733   3403   -928    851       N  
ATOM   3305  CA  SER B 433      40.580  72.612  -7.708  1.00 72.15           C  
ANISOU 3305  CA  SER B 433     8896   9145   9370   3642  -1003    969       C  
ATOM   3306  C   SER B 433      41.353  73.603  -6.843  1.00 74.76           C  
ANISOU 3306  C   SER B 433     8860   9677   9865   3542  -1153   1088       C  
ATOM   3307  O   SER B 433      42.064  73.192  -5.930  1.00 76.68           O  
ANISOU 3307  O   SER B 433     9031   9929  10174   3653  -1300   1182       O  
ATOM   3308  CB  SER B 433      41.540  72.029  -8.742  1.00 73.65           C  
ANISOU 3308  CB  SER B 433     9015   9369   9597   3992   -807   1012       C  
ATOM   3309  OG  SER B 433      40.886  71.044  -9.498  1.00 73.33           O  
ANISOU 3309  OG  SER B 433     9357   9114   9389   4100   -694    898       O  
ATOM   3310  N   LEU B 434      41.234  74.889  -7.171  1.00 76.06           N  
ANISOU 3310  N   LEU B 434     8809   9994  10095   3339  -1123   1086       N  
ATOM   3311  CA  LEU B 434      41.853  75.985  -6.427  1.00 78.38           C  
ANISOU 3311  CA  LEU B 434     8781  10461  10536   3188  -1279   1183       C  
ATOM   3312  C   LEU B 434      40.894  76.562  -5.403  1.00 76.44           C  
ANISOU 3312  C   LEU B 434     8681  10153  10210   2891  -1457   1118       C  
ATOM   3313  O   LEU B 434      41.314  77.259  -4.490  1.00 79.04           O  
ANISOU 3313  O   LEU B 434     8845  10568  10618   2769  -1642   1183       O  
ATOM   3314  CB  LEU B 434      42.243  77.116  -7.390  1.00 80.71           C  
ANISOU 3314  CB  LEU B 434     8783  10940  10942   3122  -1142   1222       C  
ATOM   3315  CG  LEU B 434      43.497  76.908  -8.244  1.00 83.82           C  
ANISOU 3315  CG  LEU B 434     8897  11479  11470   3396   -975   1344       C  
ATOM   3316  CD1 LEU B 434      43.554  75.518  -8.863  1.00 86.98           C  
ANISOU 3316  CD1 LEU B 434     9528  11750  11769   3716   -815   1305       C  
ATOM   3317  CD2 LEU B 434      43.582  77.971  -9.327  1.00 83.66           C  
ANISOU 3317  CD2 LEU B 434     8675  11602  11507   3302   -802   1362       C  
ATOM   3318  N   ALA B 435      39.611  76.262  -5.558  1.00 74.27           N  
ANISOU 3318  N   ALA B 435     8717   9727   9773   2779  -1403    993       N  
ATOM   3319  CA  ALA B 435      38.546  76.980  -4.868  1.00 73.92           C  
ANISOU 3319  CA  ALA B 435     8791   9646   9646   2497  -1501    923       C  
ATOM   3320  C   ALA B 435      38.424  76.674  -3.380  1.00 74.62           C  
ANISOU 3320  C   ALA B 435     9010   9661   9679   2435  -1707    949       C  
ATOM   3321  O   ALA B 435      38.016  77.541  -2.610  1.00 72.81           O  
ANISOU 3321  O   ALA B 435     8776   9463   9425   2231  -1821    934       O  
ATOM   3322  CB  ALA B 435      37.216  76.708  -5.550  1.00 72.47           C  
ANISOU 3322  CB  ALA B 435     8868   9341   9324   2405  -1372    801       C  
ATOM   3323  N   TRP B 436      38.755  75.448  -2.976  1.00 75.72           N  
ANISOU 3323  N   TRP B 436     9293   9694   9783   2619  -1753    988       N  
ATOM   3324  CA  TRP B 436      38.704  75.066  -1.560  1.00 76.75           C  
ANISOU 3324  CA  TRP B 436     9568   9747   9846   2582  -1950   1027       C  
ATOM   3325  C   TRP B 436      39.510  76.033  -0.688  1.00 75.67           C  
ANISOU 3325  C   TRP B 436     9191   9753   9806   2503  -2147   1107       C  
ATOM   3326  O   TRP B 436      39.274  76.146   0.506  1.00 76.75           O  
ANISOU 3326  O   TRP B 436     9452   9847   9861   2396  -2317   1118       O  
ATOM   3327  CB  TRP B 436      39.233  73.643  -1.367  1.00 80.72           C  
ANISOU 3327  CB  TRP B 436    10211  10130  10329   2837  -1976   1083       C  
ATOM   3328  CG  TRP B 436      40.675  73.507  -1.744  1.00 84.15           C  
ANISOU 3328  CG  TRP B 436    10359  10685  10927   3088  -1977   1190       C  
ATOM   3329  CD1 TRP B 436      41.171  73.163  -2.967  1.00 85.36           C  
ANISOU 3329  CD1 TRP B 436    10412  10872  11149   3297  -1787   1194       C  
ATOM   3330  CD2 TRP B 436      41.810  73.740  -0.901  1.00 86.71           C  
ANISOU 3330  CD2 TRP B 436    10449  11125  11370   3158  -2175   1318       C  
ATOM   3331  NE1 TRP B 436      42.546  73.158  -2.937  1.00 88.33           N  
ANISOU 3331  NE1 TRP B 436    10483  11390  11689   3504  -1833   1326       N  
ATOM   3332  CE2 TRP B 436      42.965  73.508  -1.681  1.00 89.07           C  
ANISOU 3332  CE2 TRP B 436    10477  11538  11826   3415  -2083   1407       C  
ATOM   3333  CE3 TRP B 436      41.964  74.114   0.441  1.00 88.06           C  
ANISOU 3333  CE3 TRP B 436    10620  11316  11523   3033  -2426   1370       C  
ATOM   3334  CZ2 TRP B 436      44.257  73.634  -1.164  1.00 92.00           C  
ANISOU 3334  CZ2 TRP B 436    10542  12053  12360   3541  -2242   1558       C  
ATOM   3335  CZ3 TRP B 436      43.254  74.242   0.954  1.00 90.29           C  
ANISOU 3335  CZ3 TRP B 436    10627  11726  11952   3149  -2607   1509       C  
ATOM   3336  CH2 TRP B 436      44.379  74.006   0.150  1.00 91.96           C  
ANISOU 3336  CH2 TRP B 436    10536  12061  12343   3394  -2517   1606       C  
ATOM   3337  N   GLU B 437      40.464  76.720  -1.308  1.00 75.15           N  
ANISOU 3337  N   GLU B 437     8792   9852   9908   2551  -2123   1169       N  
ATOM   3338  CA  GLU B 437      41.342  77.660  -0.625  1.00 75.70           C  
ANISOU 3338  CA  GLU B 437     8601  10061  10098   2464  -2321   1259       C  
ATOM   3339  C   GLU B 437      40.613  78.903  -0.107  1.00 71.69           C  
ANISOU 3339  C   GLU B 437     8146   9565   9528   2174  -2406   1189       C  
ATOM   3340  O   GLU B 437      41.087  79.561   0.819  1.00 70.63           O  
ANISOU 3340  O   GLU B 437     7929   9480   9424   2068  -2627   1239       O  
ATOM   3341  CB  GLU B 437      42.458  78.084  -1.587  1.00 79.25           C  
ANISOU 3341  CB  GLU B 437     8668  10687  10754   2570  -2235   1352       C  
ATOM   3342  CG  GLU B 437      43.798  78.373  -0.933  1.00 83.86           C  
ANISOU 3342  CG  GLU B 437     8945  11408  11508   2614  -2452   1505       C  
ATOM   3343  CD  GLU B 437      44.915  78.495  -1.957  1.00 87.67           C  
ANISOU 3343  CD  GLU B 437     9045  12067  12199   2774  -2319   1623       C  
ATOM   3344  OE1 GLU B 437      44.919  77.719  -2.938  1.00 90.44           O  
ANISOU 3344  OE1 GLU B 437     9430  12395  12538   2994  -2082   1608       O  
ATOM   3345  OE2 GLU B 437      45.786  79.371  -1.792  1.00 89.10           O  
ANISOU 3345  OE2 GLU B 437     8896  12404  12551   2677  -2449   1735       O  
ATOM   3346  N   HIS B 438      39.468  79.234  -0.702  1.00 67.25           N  
ANISOU 3346  N   HIS B 438     7728   8952   8873   2053  -2240   1076       N  
ATOM   3347  CA  HIS B 438      38.778  80.457  -0.341  1.00 63.96           C  
ANISOU 3347  CA  HIS B 438     7350   8547   8402   1810  -2289   1011       C  
ATOM   3348  C   HIS B 438      37.423  80.219   0.324  1.00 61.06           C  
ANISOU 3348  C   HIS B 438     7316   8047   7835   1705  -2272    918       C  
ATOM   3349  O   HIS B 438      36.650  79.377  -0.123  1.00 62.13           O  
ANISOU 3349  O   HIS B 438     7624   8091   7889   1757  -2127    869       O  
ATOM   3350  CB  HIS B 438      38.601  81.345  -1.566  1.00 62.81           C  
ANISOU 3350  CB  HIS B 438     7043   8485   8336   1736  -2122    976       C  
ATOM   3351  CG  HIS B 438      38.495  82.788  -1.219  1.00 61.83           C  
ANISOU 3351  CG  HIS B 438     6847   8410   8233   1523  -2223    959       C  
ATOM   3352  ND1 HIS B 438      37.288  83.404  -0.990  1.00 60.01           N  
ANISOU 3352  ND1 HIS B 438     6813   8113   7873   1366  -2188    856       N  
ATOM   3353  CD2 HIS B 438      39.447  83.717  -0.980  1.00 63.29           C  
ANISOU 3353  CD2 HIS B 438     6802   8694   8552   1440  -2375   1036       C  
ATOM   3354  CE1 HIS B 438      37.497  84.666  -0.668  1.00 61.90           C  
ANISOU 3354  CE1 HIS B 438     6969   8395   8154   1212  -2303    859       C  
ATOM   3355  NE2 HIS B 438      38.801  84.877  -0.638  1.00 62.91           N  
ANISOU 3355  NE2 HIS B 438     6845   8616   8441   1237  -2430    967       N  
ATOM   3356  N   PRO B 439      37.114  80.981   1.384  1.00 60.23           N  
ANISOU 3356  N   PRO B 439     7307   7928   7648   1552  -2419    897       N  
ATOM   3357  CA  PRO B 439      35.824  80.814   2.075  1.00 58.44           C  
ANISOU 3357  CA  PRO B 439     7381   7594   7229   1460  -2381    825       C  
ATOM   3358  C   PRO B 439      34.562  81.170   1.280  1.00 55.02           C  
ANISOU 3358  C   PRO B 439     7014   7144   6745   1363  -2174    732       C  
ATOM   3359  O   PRO B 439      33.492  80.653   1.585  1.00 52.75           O  
ANISOU 3359  O   PRO B 439     6944   6772   6326   1327  -2096    695       O  
ATOM   3360  CB  PRO B 439      35.946  81.773   3.272  1.00 60.56           C  
ANISOU 3360  CB  PRO B 439     7709   7871   7429   1334  -2579    823       C  
ATOM   3361  CG  PRO B 439      37.007  82.753   2.875  1.00 62.26           C  
ANISOU 3361  CG  PRO B 439     7638   8199   7817   1295  -2682    865       C  
ATOM   3362  CD  PRO B 439      37.996  81.913   2.118  1.00 62.19           C  
ANISOU 3362  CD  PRO B 439     7416   8249   7965   1471  -2645    951       C  
ATOM   3363  N   PHE B 440      34.673  82.049   0.288  1.00 52.90           N  
ANISOU 3363  N   PHE B 440     6556   6959   6582   1316  -2092    708       N  
ATOM   3364  CA  PHE B 440      33.486  82.590  -0.386  1.00 50.67           C  
ANISOU 3364  CA  PHE B 440     6327   6672   6253   1213  -1930    626       C  
ATOM   3365  C   PHE B 440      33.257  82.033  -1.797  1.00 50.30           C  
ANISOU 3365  C   PHE B 440     6226   6628   6256   1286  -1750    606       C  
ATOM   3366  O   PHE B 440      32.464  82.585  -2.581  1.00 48.60           O  
ANISOU 3366  O   PHE B 440     6000   6431   6032   1210  -1629    550       O  
ATOM   3367  CB  PHE B 440      33.540  84.125  -0.382  1.00 51.16           C  
ANISOU 3367  CB  PHE B 440     6282   6798   6356   1085  -1977    602       C  
ATOM   3368  CG  PHE B 440      33.633  84.729   1.000  1.00 52.64           C  
ANISOU 3368  CG  PHE B 440     6582   6957   6460   1005  -2158    602       C  
ATOM   3369  CD1 PHE B 440      32.858  84.234   2.056  1.00 53.94           C  
ANISOU 3369  CD1 PHE B 440     6999   7041   6455    997  -2175    580       C  
ATOM   3370  CD2 PHE B 440      34.490  85.788   1.252  1.00 54.04           C  
ANISOU 3370  CD2 PHE B 440     6631   7182   6719    933  -2315    628       C  
ATOM   3371  CE1 PHE B 440      32.941  84.780   3.325  1.00 54.80           C  
ANISOU 3371  CE1 PHE B 440     7247   7116   6457    940  -2336    575       C  
ATOM   3372  CE2 PHE B 440      34.584  86.337   2.524  1.00 56.74           C  
ANISOU 3372  CE2 PHE B 440     7115   7478   6963    859  -2502    618       C  
ATOM   3373  CZ  PHE B 440      33.806  85.839   3.560  1.00 56.25           C  
ANISOU 3373  CZ  PHE B 440     7324   7335   6711    872  -2509    586       C  
ATOM   3374  N   LEU B 441      33.924  80.920  -2.106  1.00 49.89           N  
ANISOU 3374  N   LEU B 441     6163   6550   6243   1444  -1737    650       N  
ATOM   3375  CA  LEU B 441      33.693  80.173  -3.327  1.00 48.91           C  
ANISOU 3375  CA  LEU B 441     6063   6392   6126   1537  -1578    623       C  
ATOM   3376  C   LEU B 441      33.156  78.802  -2.949  1.00 49.35           C  
ANISOU 3376  C   LEU B 441     6367   6307   6077   1592  -1573    616       C  
ATOM   3377  O   LEU B 441      33.534  78.256  -1.910  1.00 52.17           O  
ANISOU 3377  O   LEU B 441     6805   6615   6401   1641  -1692    666       O  
ATOM   3378  CB  LEU B 441      34.986  80.031  -4.115  1.00 50.75           C  
ANISOU 3378  CB  LEU B 441     6087   6704   6490   1702  -1545    685       C  
ATOM   3379  CG  LEU B 441      35.834  81.282  -4.373  1.00 51.94           C  
ANISOU 3379  CG  LEU B 441     5957   7000   6776   1655  -1575    734       C  
ATOM   3380  CD1 LEU B 441      37.131  80.895  -5.076  1.00 54.77           C  
ANISOU 3380  CD1 LEU B 441     6104   7441   7264   1847  -1522    821       C  
ATOM   3381  CD2 LEU B 441      35.067  82.321  -5.182  1.00 50.75           C  
ANISOU 3381  CD2 LEU B 441     5778   6887   6616   1516  -1468    673       C  
ATOM   3382  N   THR B 442      32.295  78.221  -3.780  1.00 48.51           N  
ANISOU 3382  N   THR B 442     6392   6124   5914   1580  -1452    561       N  
ATOM   3383  CA  THR B 442      31.800  76.869  -3.510  1.00 50.57           C  
ANISOU 3383  CA  THR B 442     6900   6229   6083   1617  -1453    560       C  
ATOM   3384  C   THR B 442      32.982  75.861  -3.464  1.00 52.31           C  
ANISOU 3384  C   THR B 442     7134   6397   6343   1844  -1497    618       C  
ATOM   3385  O   THR B 442      33.858  75.866  -4.337  1.00 51.28           O  
ANISOU 3385  O   THR B 442     6861   6324   6297   1996  -1436    629       O  
ATOM   3386  CB  THR B 442      30.787  76.387  -4.561  1.00 50.35           C  
ANISOU 3386  CB  THR B 442     7006   6120   6002   1563  -1337    494       C  
ATOM   3387  OG1 THR B 442      31.349  76.543  -5.876  1.00 49.55           O  
ANISOU 3387  OG1 THR B 442     6796   6070   5962   1676  -1244    467       O  
ATOM   3388  CG2 THR B 442      29.468  77.144  -4.445  1.00 49.06           C  
ANISOU 3388  CG2 THR B 442     6854   5992   5792   1349  -1306    455       C  
ATOM   3389  N   HIS B 443      33.018  75.022  -2.434  1.00 54.40           N  
ANISOU 3389  N   HIS B 443     7565   6557   6544   1877  -1595    664       N  
ATOM   3390  CA  HIS B 443      34.086  74.033  -2.329  1.00 57.29           C  
ANISOU 3390  CA  HIS B 443     7959   6862   6944   2108  -1645    726       C  
ATOM   3391  C   HIS B 443      33.689  72.736  -2.995  1.00 57.16           C  
ANISOU 3391  C   HIS B 443     8192   6665   6861   2198  -1566    692       C  
ATOM   3392  O   HIS B 443      32.599  72.224  -2.776  1.00 55.49           O  
ANISOU 3392  O   HIS B 443     8208   6325   6547   2060  -1559    664       O  
ATOM   3393  CB  HIS B 443      34.493  73.812  -0.879  1.00 60.43           C  
ANISOU 3393  CB  HIS B 443     8413   7238   7310   2123  -1814    804       C  
ATOM   3394  CG  HIS B 443      35.059  75.037  -0.238  1.00 62.16           C  
ANISOU 3394  CG  HIS B 443     8406   7616   7593   2053  -1925    837       C  
ATOM   3395  ND1 HIS B 443      35.263  75.149   1.120  1.00 64.49           N  
ANISOU 3395  ND1 HIS B 443     8759   7908   7834   2013  -2094    892       N  
ATOM   3396  CD2 HIS B 443      35.457  76.212  -0.778  1.00 61.45           C  
ANISOU 3396  CD2 HIS B 443     8055   7682   7610   2005  -1900    824       C  
ATOM   3397  CE1 HIS B 443      35.762  76.342   1.389  1.00 65.03           C  
ANISOU 3397  CE1 HIS B 443     8619   8116   7971   1939  -2182    903       C  
ATOM   3398  NE2 HIS B 443      35.879  77.009   0.256  1.00 63.05           N  
ANISOU 3398  NE2 HIS B 443     8168   7961   7826   1926  -2065    866       N  
ATOM   3399  N   MET B 444      34.585  72.249  -3.845  1.00 58.88           N  
ANISOU 3399  N   MET B 444     8358   6875   7136   2430  -1502    699       N  
ATOM   3400  CA  MET B 444      34.447  70.952  -4.471  1.00 60.77           C  
ANISOU 3400  CA  MET B 444     8859   6921   7307   2569  -1441    667       C  
ATOM   3401  C   MET B 444      35.282  69.958  -3.678  1.00 63.81           C  
ANISOU 3401  C   MET B 444     9343   7208   7693   2777  -1541    751       C  
ATOM   3402  O   MET B 444      36.485  70.162  -3.490  1.00 64.59           O  
ANISOU 3402  O   MET B 444     9222   7423   7895   2962  -1579    825       O  
ATOM   3403  CB  MET B 444      34.938  71.017  -5.913  1.00 61.65           C  
ANISOU 3403  CB  MET B 444     8884   7079   7460   2732  -1291    622       C  
ATOM   3404  CG  MET B 444      34.824  69.714  -6.688  1.00 63.77           C  
ANISOU 3404  CG  MET B 444     9458   7131   7637   2896  -1223    571       C  
ATOM   3405  SD  MET B 444      36.385  68.810  -6.708  1.00 68.88           S  
ANISOU 3405  SD  MET B 444    10081   7746   8343   3310  -1205    650       S  
ATOM   3406  CE  MET B 444      37.349  69.825  -7.826  1.00 68.08           C  
ANISOU 3406  CE  MET B 444     9610   7897   8361   3456  -1040    664       C  
ATOM   3407  N   PHE B 445      34.647  68.886  -3.221  1.00 64.27           N  
ANISOU 3407  N   PHE B 445     9725   7050   7643   2742  -1590    751       N  
ATOM   3408  CA  PHE B 445      35.356  67.829  -2.502  1.00 66.78           C  
ANISOU 3408  CA  PHE B 445    10191   7238   7944   2948  -1687    832       C  
ATOM   3409  C   PHE B 445      36.023  66.861  -3.474  1.00 69.91           C  
ANISOU 3409  C   PHE B 445    10705   7511   8345   3247  -1599    812       C  
ATOM   3410  O   PHE B 445      37.181  66.431  -3.281  1.00 70.63           O  
ANISOU 3410  O   PHE B 445    10721   7615   8500   3531  -1632    888       O  
ATOM   3411  CB  PHE B 445      34.392  67.066  -1.588  1.00 67.02           C  
ANISOU 3411  CB  PHE B 445    10542   7073   7849   2781  -1771    854       C  
ATOM   3412  CG  PHE B 445      34.076  67.782  -0.294  1.00 65.46           C  
ANISOU 3412  CG  PHE B 445    10263   6980   7628   2587  -1877    911       C  
ATOM   3413  CD1 PHE B 445      32.966  68.599  -0.189  1.00 62.95           C  
ANISOU 3413  CD1 PHE B 445     9908   6737   7272   2304  -1835    867       C  
ATOM   3414  CD2 PHE B 445      34.878  67.601   0.826  1.00 67.48           C  
ANISOU 3414  CD2 PHE B 445    10502   7249   7887   2704  -2023   1012       C  
ATOM   3415  CE1 PHE B 445      32.667  69.239   1.001  1.00 62.44           C  
ANISOU 3415  CE1 PHE B 445     9804   6757   7163   2152  -1915    914       C  
ATOM   3416  CE2 PHE B 445      34.587  68.237   2.023  1.00 66.01           C  
ANISOU 3416  CE2 PHE B 445    10287   7143   7648   2535  -2125   1058       C  
ATOM   3417  CZ  PHE B 445      33.479  69.056   2.110  1.00 64.31           C  
ANISOU 3417  CZ  PHE B 445    10051   6997   7384   2265  -2061   1005       C  
ATOM   3418  N   CYS B 446      35.281  66.489  -4.510  1.00 70.04           N  
ANISOU 3418  N   CYS B 446    10922   7401   8289   3195  -1492    713       N  
ATOM   3419  CA  CYS B 446      35.825  65.609  -5.514  1.00 73.08           C  
ANISOU 3419  CA  CYS B 446    11465   7652   8647   3479  -1395    674       C  
ATOM   3420  C   CYS B 446      35.004  65.618  -6.788  1.00 72.64           C  
ANISOU 3420  C   CYS B 446    11561   7523   8515   3378  -1280    550       C  
ATOM   3421  O   CYS B 446      33.869  66.087  -6.829  1.00 70.69           O  
ANISOU 3421  O   CYS B 446    11343   7286   8229   3072  -1297    500       O  
ATOM   3422  CB  CYS B 446      35.933  64.177  -4.983  1.00 75.63           C  
ANISOU 3422  CB  CYS B 446    12142   7700   8891   3630  -1479    712       C  
ATOM   3423  SG  CYS B 446      34.433  63.206  -5.214  1.00 76.12           S  
ANISOU 3423  SG  CYS B 446    12685   7441   8793   3384  -1509    630       S  
ATOM   3424  N   THR B 447      35.613  65.036  -7.809  1.00 74.80           N  
ANISOU 3424  N   THR B 447    11945   7714   8759   3659  -1167    506       N  
ATOM   3425  CA  THR B 447      35.123  65.074  -9.155  1.00 74.28           C  
ANISOU 3425  CA  THR B 447    12010   7598   8612   3637  -1048    391       C  
ATOM   3426  C   THR B 447      35.507  63.722  -9.772  1.00 78.93           C  
ANISOU 3426  C   THR B 447    12974   7919   9096   3936  -1001    345       C  
ATOM   3427  O   THR B 447      36.621  63.223  -9.568  1.00 77.44           O  
ANISOU 3427  O   THR B 447    12750   7723   8951   4269   -969    412       O  
ATOM   3428  CB  THR B 447      35.764  66.285  -9.851  1.00 74.01           C  
ANISOU 3428  CB  THR B 447    11589   7854   8675   3706   -912    398       C  
ATOM   3429  OG1 THR B 447      34.751  67.196 -10.313  1.00 72.57           O  
ANISOU 3429  OG1 THR B 447    11339   7761   8471   3402   -898    331       O  
ATOM   3430  CG2 THR B 447      36.678  65.896 -10.948  1.00 75.76           C  
ANISOU 3430  CG2 THR B 447    11848   8065   8872   4061   -742    375       C  
ATOM   3431  N   PHE B 448      34.563  63.111 -10.477  1.00 80.48           N  
ANISOU 3431  N   PHE B 448    13539   7885   9153   3813  -1013    237       N  
ATOM   3432  CA  PHE B 448      34.807  61.841 -11.153  1.00 84.72           C  
ANISOU 3432  CA  PHE B 448    14497   8130   9561   4075   -978    171       C  
ATOM   3433  C   PHE B 448      33.785  61.652 -12.272  1.00 84.69           C  
ANISOU 3433  C   PHE B 448    14799   7964   9412   3901   -971     33       C  
ATOM   3434  O   PHE B 448      32.760  62.338 -12.305  1.00 81.06           O  
ANISOU 3434  O   PHE B 448    14246   7590   8962   3547  -1030      7       O  
ATOM   3435  CB  PHE B 448      34.734  60.675 -10.161  1.00 87.27           C  
ANISOU 3435  CB  PHE B 448    15117   8190   9850   4100  -1122    227       C  
ATOM   3436  CG  PHE B 448      33.393  60.529  -9.510  1.00 87.27           C  
ANISOU 3436  CG  PHE B 448    15278   8064   9813   3679  -1281    229       C  
ATOM   3437  CD1 PHE B 448      32.398  59.759 -10.102  1.00 88.84           C  
ANISOU 3437  CD1 PHE B 448    15894   7979   9880   3507  -1345    137       C  
ATOM   3438  CD2 PHE B 448      33.111  61.184  -8.320  1.00 86.27           C  
ANISOU 3438  CD2 PHE B 448    14885   8109   9782   3449  -1366    328       C  
ATOM   3439  CE1 PHE B 448      31.151  59.639  -9.513  1.00 88.29           C  
ANISOU 3439  CE1 PHE B 448    15933   7815   9796   3107  -1483    161       C  
ATOM   3440  CE2 PHE B 448      31.867  61.062  -7.724  1.00 85.90           C  
ANISOU 3440  CE2 PHE B 448    14969   7967   9702   3075  -1482    345       C  
ATOM   3441  CZ  PHE B 448      30.885  60.292  -8.323  1.00 86.75           C  
ANISOU 3441  CZ  PHE B 448    15451   7808   9699   2899  -1536    270       C  
ATOM   3442  N   GLN B 449      34.061  60.710 -13.171  1.00 87.96           N  
ANISOU 3442  N   GLN B 449    15590   8140   9688   4158   -910    -52       N  
ATOM   3443  CA  GLN B 449      33.198  60.479 -14.332  1.00 88.16           C  
ANISOU 3443  CA  GLN B 449    15946   7994   9554   4027   -917   -192       C  
ATOM   3444  C   GLN B 449      32.830  59.005 -14.478  1.00 91.82           C  
ANISOU 3444  C   GLN B 449    16992   8032   9863   4073  -1027   -261       C  
ATOM   3445  O   GLN B 449      33.634  58.125 -14.161  1.00 93.35           O  
ANISOU 3445  O   GLN B 449    17365   8065  10037   4390  -1005   -229       O  
ATOM   3446  CB  GLN B 449      33.886  60.974 -15.611  1.00 87.97           C  
ANISOU 3446  CB  GLN B 449    15838   8110   9473   4298   -706   -256       C  
ATOM   3447  CG  GLN B 449      35.019  60.089 -16.116  1.00 91.14           C  
ANISOU 3447  CG  GLN B 449    16470   8369   9790   4794   -561   -277       C  
ATOM   3448  CD  GLN B 449      36.009  60.846 -16.986  1.00 91.09           C  
ANISOU 3448  CD  GLN B 449    16176   8629   9804   5093   -309   -265       C  
ATOM   3449  OE1 GLN B 449      35.647  61.401 -18.025  1.00 90.59           O  
ANISOU 3449  OE1 GLN B 449    16135   8636   9650   5019   -227   -346       O  
ATOM   3450  NE2 GLN B 449      37.266  60.872 -16.563  1.00 92.58           N  
ANISOU 3450  NE2 GLN B 449    16087   8973  10116   5430   -187   -151       N  
ATOM   3451  N   THR B 450      31.599  58.754 -14.927  1.00 92.24           N  
ANISOU 3451  N   THR B 450    17331   7902   9814   3746  -1160   -347       N  
ATOM   3452  CA  THR B 450      31.206  57.444 -15.443  1.00 95.48           C  
ANISOU 3452  CA  THR B 450    18342   7891  10045   3777  -1263   -445       C  
ATOM   3453  C   THR B 450      31.326  57.532 -16.959  1.00 97.51           C  
ANISOU 3453  C   THR B 450    18801   8109  10139   3946  -1153   -588       C  
ATOM   3454  O   THR B 450      31.695  58.582 -17.493  1.00 94.32           O  
ANISOU 3454  O   THR B 450    18053   8009   9775   4025   -997   -591       O  
ATOM   3455  CB  THR B 450      29.766  57.033 -15.041  1.00 94.76           C  
ANISOU 3455  CB  THR B 450    18467   7599   9938   3294  -1500   -441       C  
ATOM   3456  OG1 THR B 450      28.802  57.854 -15.713  1.00 93.18           O  
ANISOU 3456  OG1 THR B 450    18133   7541   9729   2974  -1540   -496       O  
ATOM   3457  CG2 THR B 450      29.568  57.133 -13.530  1.00 93.19           C  
ANISOU 3457  CG2 THR B 450    18023   7491   9894   3098  -1583   -287       C  
ATOM   3458  N   LYS B 451      31.023  56.438 -17.652  1.00101.27           N  
ANISOU 3458  N   LYS B 451    19853   8203  10419   4003  -1236   -705       N  
ATOM   3459  CA  LYS B 451      31.039  56.447 -19.110  1.00103.54           C  
ANISOU 3459  CA  LYS B 451    20410   8416  10512   4149  -1153   -854       C  
ATOM   3460  C   LYS B 451      30.065  57.488 -19.667  1.00103.09           C  
ANISOU 3460  C   LYS B 451    20137   8564  10468   3776  -1211   -887       C  
ATOM   3461  O   LYS B 451      30.327  58.104 -20.701  1.00104.13           O  
ANISOU 3461  O   LYS B 451    20211   8840  10511   3915  -1070   -956       O  
ATOM   3462  CB  LYS B 451      30.701  55.062 -19.663  1.00107.97           C  
ANISOU 3462  CB  LYS B 451    21682   8489  10852   4203  -1289   -979       C  
ATOM   3463  CG  LYS B 451      30.966  54.932 -21.152  1.00109.60           C  
ANISOU 3463  CG  LYS B 451    22238   8586  10818   4465  -1174  -1140       C  
ATOM   3464  CD  LYS B 451      31.020  53.482 -21.594  1.00113.75           C  
ANISOU 3464  CD  LYS B 451    23487   8616  11117   4665  -1261  -1260       C  
ATOM   3465  CE  LYS B 451      31.616  53.367 -22.987  1.00115.94           C  
ANISOU 3465  CE  LYS B 451    24089   8816  11145   5063  -1073  -1407       C  
ATOM   3466  NZ  LYS B 451      31.700  51.950 -23.429  1.00120.50           N  
ANISOU 3466  NZ  LYS B 451    25415   8886  11482   5288  -1154  -1536       N  
ATOM   3467  N   GLU B 452      28.960  57.706 -18.961  1.00101.54           N  
ANISOU 3467  N   GLU B 452    19804   8392  10382   3315  -1408   -825       N  
ATOM   3468  CA  GLU B 452      27.888  58.554 -19.457  1.00 99.35           C  
ANISOU 3468  CA  GLU B 452    19368   8266  10115   2941  -1501   -852       C  
ATOM   3469  C   GLU B 452      27.828  59.933 -18.808  1.00 93.92           C  
ANISOU 3469  C   GLU B 452    18048   8001   9637   2784  -1424   -737       C  
ATOM   3470  O   GLU B 452      27.291  60.870 -19.400  1.00 90.53           O  
ANISOU 3470  O   GLU B 452    17418   7765   9212   2609  -1420   -761       O  
ATOM   3471  CB  GLU B 452      26.561  57.846 -19.236  1.00102.08           C  
ANISOU 3471  CB  GLU B 452    20009   8341  10434   2513  -1782   -861       C  
ATOM   3472  CG  GLU B 452      26.492  56.491 -19.911  1.00109.27           C  
ANISOU 3472  CG  GLU B 452    21591   8796  11128   2612  -1901   -984       C  
ATOM   3473  CD  GLU B 452      25.277  55.696 -19.493  1.00113.10           C  
ANISOU 3473  CD  GLU B 452    22352   8999  11621   2176  -2190   -958       C  
ATOM   3474  OE1 GLU B 452      24.735  55.969 -18.401  1.00113.77           O  
ANISOU 3474  OE1 GLU B 452    22119   9217  11890   1886  -2255   -819       O  
ATOM   3475  OE2 GLU B 452      24.867  54.796 -20.256  1.00117.33           O  
ANISOU 3475  OE2 GLU B 452    23431   9175  11974   2122  -2351  -1073       O  
ATOM   3476  N   ASN B 453      28.375  60.060 -17.602  1.00 91.28           N  
ANISOU 3476  N   ASN B 453    17423   7795   9462   2851  -1372   -614       N  
ATOM   3477  CA  ASN B 453      28.187  61.271 -16.810  1.00 86.30           C  
ANISOU 3477  CA  ASN B 453    16252   7515   9023   2656  -1342   -504       C  
ATOM   3478  C   ASN B 453      29.447  61.841 -16.180  1.00 84.97           C  
ANISOU 3478  C   ASN B 453    15706   7596   8983   2946  -1169   -414       C  
ATOM   3479  O   ASN B 453      30.433  61.128 -15.965  1.00 86.19           O  
ANISOU 3479  O   ASN B 453    15988   7641   9118   3276  -1100   -397       O  
ATOM   3480  CB  ASN B 453      27.169  61.002 -15.706  1.00 84.86           C  
ANISOU 3480  CB  ASN B 453    16052   7261   8930   2281  -1524   -418       C  
ATOM   3481  CG  ASN B 453      25.750  61.008 -16.217  1.00 83.80           C  
ANISOU 3481  CG  ASN B 453    16051   7040   8749   1888  -1691   -462       C  
ATOM   3482  OD1 ASN B 453      25.216  62.050 -16.571  1.00 81.21           O  
ANISOU 3482  OD1 ASN B 453    15442   6944   8469   1717  -1677   -463       O  
ATOM   3483  ND2 ASN B 453      25.131  59.845 -16.254  1.00 86.87           N  
ANISOU 3483  ND2 ASN B 453    16867   7089   9049   1740  -1862   -489       N  
ATOM   3484  N   LEU B 454      29.375  63.141 -15.887  1.00 81.60           N  
ANISOU 3484  N   LEU B 454    14814   7499   8688   2812  -1114   -352       N  
ATOM   3485  CA  LEU B 454      30.388  63.863 -15.126  1.00 79.77           C  
ANISOU 3485  CA  LEU B 454    14169   7532   8609   2983  -1000   -248       C  
ATOM   3486  C   LEU B 454      29.760  64.318 -13.809  1.00 76.44           C  
ANISOU 3486  C   LEU B 454    13503   7221   8317   2682  -1114   -148       C  
ATOM   3487  O   LEU B 454      28.626  64.803 -13.801  1.00 74.13           O  
ANISOU 3487  O   LEU B 454    13149   6977   8037   2352  -1196   -156       O  
ATOM   3488  CB  LEU B 454      30.865  65.079 -15.911  1.00 78.99           C  
ANISOU 3488  CB  LEU B 454    13749   7717   8545   3075   -839   -257       C  
ATOM   3489  CG  LEU B 454      31.479  64.771 -17.279  1.00 81.91           C  
ANISOU 3489  CG  LEU B 454    14337   8015   8769   3379   -691   -348       C  
ATOM   3490  CD1 LEU B 454      31.320  65.960 -18.216  1.00 81.12           C  
ANISOU 3490  CD1 LEU B 454    14020   8141   8660   3309   -590   -375       C  
ATOM   3491  CD2 LEU B 454      32.944  64.376 -17.140  1.00 84.35           C  
ANISOU 3491  CD2 LEU B 454    14584   8352   9112   3806   -536   -294       C  
ATOM   3492  N   PHE B 455      30.491  64.161 -12.706  1.00 73.64           N  
ANISOU 3492  N   PHE B 455    13016   6910   8054   2808  -1116    -51       N  
ATOM   3493  CA  PHE B 455      29.956  64.477 -11.385  1.00 70.57           C  
ANISOU 3493  CA  PHE B 455    12454   6600   7758   2556  -1219     44       C  
ATOM   3494  C   PHE B 455      30.886  65.396 -10.610  1.00 68.30           C  
ANISOU 3494  C   PHE B 455    11760   6585   7606   2673  -1161    135       C  
ATOM   3495  O   PHE B 455      32.069  65.098 -10.440  1.00 69.94           O  
ANISOU 3495  O   PHE B 455    11920   6806   7846   2977  -1110    177       O  
ATOM   3496  CB  PHE B 455      29.749  63.202 -10.579  1.00 72.51           C  
ANISOU 3496  CB  PHE B 455    13023   6570   7957   2535  -1339     87       C  
ATOM   3497  CG  PHE B 455      28.717  62.274 -11.151  1.00 73.73           C  
ANISOU 3497  CG  PHE B 455    13586   6434   7992   2349  -1438     16       C  
ATOM   3498  CD1 PHE B 455      27.369  62.507 -10.935  1.00 72.25           C  
ANISOU 3498  CD1 PHE B 455    13383   6250   7816   1955  -1536     32       C  
ATOM   3499  CD2 PHE B 455      29.090  61.156 -11.884  1.00 76.59           C  
ANISOU 3499  CD2 PHE B 455    14353   6514   8233   2569  -1441    -59       C  
ATOM   3500  CE1 PHE B 455      26.412  61.653 -11.442  1.00 73.51           C  
ANISOU 3500  CE1 PHE B 455    13900   6146   7883   1754  -1653    -16       C  
ATOM   3501  CE2 PHE B 455      28.132  60.296 -12.398  1.00 77.84           C  
ANISOU 3501  CE2 PHE B 455    14912   6383   8278   2374  -1563   -126       C  
ATOM   3502  CZ  PHE B 455      26.793  60.544 -12.175  1.00 76.56           C  
ANISOU 3502  CZ  PHE B 455    14709   6235   8145   1952  -1679   -100       C  
ATOM   3503  N   PHE B 456      30.340  66.511 -10.138  1.00 65.62           N  
ANISOU 3503  N   PHE B 456    11131   6457   7343   2430  -1179    169       N  
ATOM   3504  CA  PHE B 456      31.041  67.383  -9.209  1.00 63.54           C  
ANISOU 3504  CA  PHE B 456    10521   6422   7198   2471  -1171    258       C  
ATOM   3505  C   PHE B 456      30.436  67.137  -7.835  1.00 62.91           C  
ANISOU 3505  C   PHE B 456    10492   6287   7121   2275  -1293    333       C  
ATOM   3506  O   PHE B 456      29.235  67.339  -7.647  1.00 61.52           O  
ANISOU 3506  O   PHE B 456    10353   6098   6920   1988  -1335    325       O  
ATOM   3507  CB  PHE B 456      30.838  68.858  -9.568  1.00 61.70           C  
ANISOU 3507  CB  PHE B 456     9960   6448   7034   2338  -1109    244       C  
ATOM   3508  CG  PHE B 456      31.307  69.242 -10.950  1.00 62.02           C  
ANISOU 3508  CG  PHE B 456     9940   6562   7061   2492   -978    181       C  
ATOM   3509  CD1 PHE B 456      30.526  68.982 -12.061  1.00 61.79           C  
ANISOU 3509  CD1 PHE B 456    10128   6422   6928   2414   -956     86       C  
ATOM   3510  CD2 PHE B 456      32.517  69.919 -11.125  1.00 61.56           C  
ANISOU 3510  CD2 PHE B 456     9597   6697   7096   2699   -880    227       C  
ATOM   3511  CE1 PHE B 456      30.954  69.358 -13.326  1.00 62.51           C  
ANISOU 3511  CE1 PHE B 456    10184   6583   6984   2561   -828     32       C  
ATOM   3512  CE2 PHE B 456      32.951  70.287 -12.384  1.00 61.65           C  
ANISOU 3512  CE2 PHE B 456     9550   6785   7088   2840   -737    186       C  
ATOM   3513  CZ  PHE B 456      32.168  70.007 -13.486  1.00 61.90           C  
ANISOU 3513  CZ  PHE B 456     9828   6698   6993   2779   -705     85       C  
ATOM   3514  N   VAL B 457      31.250  66.718  -6.870  1.00 63.32           N  
ANISOU 3514  N   VAL B 457    10539   6315   7202   2431  -1346    415       N  
ATOM   3515  CA  VAL B 457      30.764  66.540  -5.509  1.00 62.35           C  
ANISOU 3515  CA  VAL B 457    10468   6155   7067   2263  -1452    497       C  
ATOM   3516  C   VAL B 457      31.113  67.779  -4.708  1.00 59.56           C  
ANISOU 3516  C   VAL B 457     9774   6057   6796   2212  -1466    551       C  
ATOM   3517  O   VAL B 457      32.287  68.002  -4.395  1.00 60.29           O  
ANISOU 3517  O   VAL B 457     9697   6252   6958   2419  -1482    600       O  
ATOM   3518  CB  VAL B 457      31.359  65.285  -4.856  1.00 64.93           C  
ANISOU 3518  CB  VAL B 457    11043   6275   7352   2450  -1528    560       C  
ATOM   3519  CG1 VAL B 457      30.797  65.099  -3.457  1.00 64.95           C  
ANISOU 3519  CG1 VAL B 457    11124   6234   7320   2264  -1629    653       C  
ATOM   3520  CG2 VAL B 457      31.048  64.079  -5.721  1.00 67.56           C  
ANISOU 3520  CG2 VAL B 457    11747   6328   7595   2511  -1519    495       C  
ATOM   3521  N   MET B 458      30.076  68.559  -4.390  1.00 56.87           N  
ANISOU 3521  N   MET B 458     9344   5813   6448   1937  -1466    545       N  
ATOM   3522  CA  MET B 458      30.191  69.875  -3.751  1.00 55.26           C  
ANISOU 3522  CA  MET B 458     8851   5839   6305   1853  -1473    573       C  
ATOM   3523  C   MET B 458      29.696  69.865  -2.303  1.00 55.39           C  
ANISOU 3523  C   MET B 458     8931   5844   6269   1707  -1553    650       C  
ATOM   3524  O   MET B 458      28.949  68.974  -1.875  1.00 56.10           O  
ANISOU 3524  O   MET B 458     9264   5769   6280   1601  -1579    684       O  
ATOM   3525  CB  MET B 458      29.312  70.907  -4.493  1.00 53.82           C  
ANISOU 3525  CB  MET B 458     8522   5784   6142   1665  -1396    507       C  
ATOM   3526  CG  MET B 458      29.407  70.890  -6.008  1.00 53.56           C  
ANISOU 3526  CG  MET B 458     8489   5740   6120   1744  -1310    424       C  
ATOM   3527  SD  MET B 458      31.047  71.267  -6.629  1.00 54.93           S  
ANISOU 3527  SD  MET B 458     8450   6037   6382   2046  -1249    428       S  
ATOM   3528  CE  MET B 458      31.286  72.912  -5.978  1.00 52.68           C  
ANISOU 3528  CE  MET B 458     7815   6009   6192   1937  -1269    467       C  
ATOM   3529  N   GLU B 459      30.083  70.897  -1.565  1.00 54.38           N  
ANISOU 3529  N   GLU B 459     8594   5890   6177   1692  -1588    680       N  
ATOM   3530  CA  GLU B 459      29.515  71.144  -0.251  1.00 54.22           C  
ANISOU 3530  CA  GLU B 459     8626   5889   6086   1544  -1641    739       C  
ATOM   3531  C   GLU B 459      28.062  71.521  -0.389  1.00 52.24           C  
ANISOU 3531  C   GLU B 459     8394   5659   5795   1299  -1558    712       C  
ATOM   3532  O   GLU B 459      27.696  72.261  -1.295  1.00 51.88           O  
ANISOU 3532  O   GLU B 459     8201   5709   5801   1236  -1485    645       O  
ATOM   3533  CB  GLU B 459      30.263  72.260   0.481  1.00 54.27           C  
ANISOU 3533  CB  GLU B 459     8422   6069   6130   1581  -1710    761       C  
ATOM   3534  CG  GLU B 459      30.108  73.636  -0.133  1.00 52.98           C  
ANISOU 3534  CG  GLU B 459     8013   6080   6036   1499  -1646    696       C  
ATOM   3535  CD  GLU B 459      30.935  74.690   0.572  1.00 53.11           C  
ANISOU 3535  CD  GLU B 459     7848   6238   6093   1529  -1741    719       C  
ATOM   3536  OE1 GLU B 459      31.427  75.612  -0.103  1.00 52.63           O  
ANISOU 3536  OE1 GLU B 459     7564   6303   6130   1550  -1719    685       O  
ATOM   3537  OE2 GLU B 459      31.087  74.605   1.801  1.00 57.04           O  
ANISOU 3537  OE2 GLU B 459     8439   6716   6518   1522  -1846    775       O  
ATOM   3538  N   TYR B 460      27.235  71.012   0.509  1.00 52.19           N  
ANISOU 3538  N   TYR B 460     8562   5567   5697   1164  -1566    777       N  
ATOM   3539  CA  TYR B 460      25.810  71.329   0.510  1.00 51.83           C  
ANISOU 3539  CA  TYR B 460     8514   5557   5621    930  -1480    779       C  
ATOM   3540  C   TYR B 460      25.570  72.685   1.153  1.00 50.96           C  
ANISOU 3540  C   TYR B 460     8226   5635   5500    866  -1447    775       C  
ATOM   3541  O   TYR B 460      25.979  72.893   2.284  1.00 51.12           O  
ANISOU 3541  O   TYR B 460     8283   5682   5458    910  -1502    823       O  
ATOM   3542  CB  TYR B 460      25.033  70.251   1.272  1.00 52.98           C  
ANISOU 3542  CB  TYR B 460     8905   5546   5676    807  -1485    873       C  
ATOM   3543  CG  TYR B 460      23.553  70.538   1.401  1.00 51.84           C  
ANISOU 3543  CG  TYR B 460     8730   5456   5510    564  -1390    908       C  
ATOM   3544  CD1 TYR B 460      22.756  70.702   0.272  1.00 50.63           C  
ANISOU 3544  CD1 TYR B 460     8487   5325   5423    443  -1338    854       C  
ATOM   3545  CD2 TYR B 460      22.947  70.636   2.654  1.00 51.79           C  
ANISOU 3545  CD2 TYR B 460     8781   5483   5413    463  -1349   1003       C  
ATOM   3546  CE1 TYR B 460      21.401  70.969   0.381  1.00 50.50           C  
ANISOU 3546  CE1 TYR B 460     8406   5375   5405    227  -1256    902       C  
ATOM   3547  CE2 TYR B 460      21.593  70.885   2.778  1.00 51.64           C  
ANISOU 3547  CE2 TYR B 460     8707   5530   5384    257  -1240   1053       C  
ATOM   3548  CZ  TYR B 460      20.820  71.054   1.634  1.00 51.74           C  
ANISOU 3548  CZ  TYR B 460     8596   5575   5485    138  -1198   1006       C  
ATOM   3549  OH  TYR B 460      19.476  71.300   1.753  1.00 51.54           O  
ANISOU 3549  OH  TYR B 460     8483   5630   5467    -60  -1097   1071       O  
ATOM   3550  N   LEU B 461      24.887  73.586   0.435  1.00 50.69           N  
ANISOU 3550  N   LEU B 461     8025   5717   5516    769  -1366    718       N  
ATOM   3551  CA  LEU B 461      24.568  74.930   0.913  1.00 51.22           C  
ANISOU 3551  CA  LEU B 461     7938   5947   5573    716  -1323    703       C  
ATOM   3552  C   LEU B 461      23.072  75.134   0.827  1.00 52.19           C  
ANISOU 3552  C   LEU B 461     8039   6111   5679    532  -1213    723       C  
ATOM   3553  O   LEU B 461      22.472  74.846  -0.207  1.00 54.54           O  
ANISOU 3553  O   LEU B 461     8306   6383   6032    455  -1179    698       O  
ATOM   3554  CB  LEU B 461      25.240  75.974   0.029  1.00 50.16           C  
ANISOU 3554  CB  LEU B 461     7594   5928   5536    795  -1327    621       C  
ATOM   3555  CG  LEU B 461      26.758  75.831  -0.056  1.00 51.54           C  
ANISOU 3555  CG  LEU B 461     7730   6091   5761    978  -1425    614       C  
ATOM   3556  CD1 LEU B 461      27.314  76.586  -1.249  1.00 50.49           C  
ANISOU 3556  CD1 LEU B 461     7398   6050   5736   1040  -1398    549       C  
ATOM   3557  CD2 LEU B 461      27.411  76.305   1.235  1.00 52.28           C  
ANISOU 3557  CD2 LEU B 461     7829   6228   5805   1024  -1521    654       C  
ATOM   3558  N   ASN B 462      22.455  75.663   1.873  1.00 50.57           N  
ANISOU 3558  N   ASN B 462     7842   5977   5395    468  -1157    771       N  
ATOM   3559  CA  ASN B 462      21.002  75.729   1.886  1.00 50.82           C  
ANISOU 3559  CA  ASN B 462     7839   6054   5414    304  -1038    819       C  
ATOM   3560  C   ASN B 462      20.445  77.092   2.268  1.00 49.96           C  
ANISOU 3560  C   ASN B 462     7593   6104   5282    292   -946    802       C  
ATOM   3561  O   ASN B 462      19.281  77.197   2.663  1.00 48.31           O  
ANISOU 3561  O   ASN B 462     7363   5952   5039    187   -830    867       O  
ATOM   3562  CB  ASN B 462      20.448  74.656   2.804  1.00 52.87           C  
ANISOU 3562  CB  ASN B 462     8288   6214   5586    214  -1011    936       C  
ATOM   3563  CG  ASN B 462      20.887  74.833   4.232  1.00 53.22           C  
ANISOU 3563  CG  ASN B 462     8456   6266   5498    290  -1023    984       C  
ATOM   3564  OD1 ASN B 462      21.513  75.823   4.582  1.00 53.09           O  
ANISOU 3564  OD1 ASN B 462     8382   6333   5457    394  -1057    926       O  
ATOM   3565  ND2 ASN B 462      20.565  73.862   5.065  1.00 55.51           N  
ANISOU 3565  ND2 ASN B 462     8936   6457   5697    231  -1007   1094       N  
ATOM   3566  N   GLY B 463      21.280  78.125   2.130  1.00 48.40           N  
ANISOU 3566  N   GLY B 463     7305   5975   5110    402   -997    720       N  
ATOM   3567  CA  GLY B 463      20.878  79.479   2.446  1.00 47.94           C  
ANISOU 3567  CA  GLY B 463     7148   6040   5025    412   -928    688       C  
ATOM   3568  C   GLY B 463      20.097  80.171   1.334  1.00 48.15           C  
ANISOU 3568  C   GLY B 463     6989   6155   5150    356   -853    648       C  
ATOM   3569  O   GLY B 463      19.498  81.204   1.586  1.00 49.02           O  
ANISOU 3569  O   GLY B 463     7026   6360   5237    359   -772    637       O  
ATOM   3570  N   GLY B 464      20.107  79.617   0.120  1.00 47.64           N  
ANISOU 3570  N   GLY B 464     6866   6051   5181    319   -885    625       N  
ATOM   3571  CA  GLY B 464      19.436  80.217  -1.031  1.00 47.82           C  
ANISOU 3571  CA  GLY B 464     6727   6150   5291    270   -841    587       C  
ATOM   3572  C   GLY B 464      20.370  81.140  -1.803  1.00 48.65           C  
ANISOU 3572  C   GLY B 464     6733   6293   5457    368   -894    499       C  
ATOM   3573  O   GLY B 464      21.465  81.439  -1.353  1.00 52.15           O  
ANISOU 3573  O   GLY B 464     7207   6723   5884    462   -959    473       O  
ATOM   3574  N   ASP B 465      19.957  81.607  -2.977  1.00 46.59           N  
ANISOU 3574  N   ASP B 465     6350   6083   5269    340   -873    462       N  
ATOM   3575  CA  ASP B 465      20.800  82.532  -3.741  1.00 46.28           C  
ANISOU 3575  CA  ASP B 465     6216   6083   5285    423   -906    394       C  
ATOM   3576  C   ASP B 465      20.267  83.966  -3.665  1.00 44.99           C  
ANISOU 3576  C   ASP B 465     5945   6020   5128    426   -850    376       C  
ATOM   3577  O   ASP B 465      19.108  84.188  -3.305  1.00 45.24           O  
ANISOU 3577  O   ASP B 465     5949   6103   5136    373   -773    413       O  
ATOM   3578  CB  ASP B 465      20.925  82.068  -5.186  1.00 47.45           C  
ANISOU 3578  CB  ASP B 465     6337   6200   5490    418   -929    361       C  
ATOM   3579  CG  ASP B 465      19.614  82.157  -5.933  1.00 48.23           C  
ANISOU 3579  CG  ASP B 465     6370   6341   5612    313   -889    373       C  
ATOM   3580  OD1 ASP B 465      19.095  81.106  -6.322  1.00 49.34           O  
ANISOU 3580  OD1 ASP B 465     6581   6414   5749    232   -913    395       O  
ATOM   3581  OD2 ASP B 465      19.101  83.277  -6.099  1.00 49.50           O  
ANISOU 3581  OD2 ASP B 465     6415   6596   5795    310   -847    365       O  
ATOM   3582  N   LEU B 466      21.114  84.933  -3.999  1.00 42.85           N  
ANISOU 3582  N   LEU B 466     5613   5774   4893    493   -886    328       N  
ATOM   3583  CA  LEU B 466      20.750  86.336  -3.829  1.00 42.88           C  
ANISOU 3583  CA  LEU B 466     5556   5842   4894    510   -849    307       C  
ATOM   3584  C   LEU B 466      19.624  86.796  -4.711  1.00 43.84           C  
ANISOU 3584  C   LEU B 466     5575   6026   5054    472   -781    310       C  
ATOM   3585  O   LEU B 466      18.886  87.696  -4.318  1.00 45.08           O  
ANISOU 3585  O   LEU B 466     5704   6235   5189    487   -720    315       O  
ATOM   3586  CB  LEU B 466      21.950  87.248  -4.043  1.00 42.79           C  
ANISOU 3586  CB  LEU B 466     5506   5827   4922    565   -918    266       C  
ATOM   3587  CG  LEU B 466      23.043  87.137  -2.985  1.00 43.53           C  
ANISOU 3587  CG  LEU B 466     5680   5876   4981    602  -1010    269       C  
ATOM   3588  CD1 LEU B 466      24.094  88.221  -3.209  1.00 44.19           C  
ANISOU 3588  CD1 LEU B 466     5698   5968   5122    624  -1086    243       C  
ATOM   3589  CD2 LEU B 466      22.467  87.216  -1.577  1.00 44.27           C  
ANISOU 3589  CD2 LEU B 466     5903   5958   4960    601   -989    283       C  
ATOM   3590  N   MET B 467      19.480  86.199  -5.898  1.00 44.98           N  
ANISOU 3590  N   MET B 467     5677   6164   5248    434   -797    308       N  
ATOM   3591  CA  MET B 467      18.319  86.493  -6.731  1.00 46.50           C  
ANISOU 3591  CA  MET B 467     5775   6416   5474    384   -758    323       C  
ATOM   3592  C   MET B 467      17.024  86.118  -5.990  1.00 48.63           C  
ANISOU 3592  C   MET B 467     6028   6726   5721    317   -693    390       C  
ATOM   3593  O   MET B 467      16.041  86.890  -5.974  1.00 48.36           O  
ANISOU 3593  O   MET B 467     5896   6774   5701    321   -629    417       O  
ATOM   3594  CB  MET B 467      18.371  85.764  -8.080  1.00 47.06           C  
ANISOU 3594  CB  MET B 467     5847   6456   5578    345   -807    308       C  
ATOM   3595  CG  MET B 467      17.138  86.030  -8.937  1.00 49.85           C  
ANISOU 3595  CG  MET B 467     6106   6870   5961    281   -800    331       C  
ATOM   3596  SD  MET B 467      16.978  87.793  -9.309  1.00 51.14           S  
ANISOU 3596  SD  MET B 467     6159   7117   6154    357   -764    314       S  
ATOM   3597  CE  MET B 467      18.162  87.930 -10.634  1.00 52.68           C  
ANISOU 3597  CE  MET B 467     6385   7270   6357    404   -813    261       C  
ATOM   3598  N   TYR B 468      17.005  84.932  -5.393  1.00 48.33           N  
ANISOU 3598  N   TYR B 468     6078   6632   5650    261   -701    428       N  
ATOM   3599  CA  TYR B 468      15.826  84.506  -4.640  1.00 49.37           C  
ANISOU 3599  CA  TYR B 468     6190   6805   5762    184   -626    513       C  
ATOM   3600  C   TYR B 468      15.540  85.475  -3.494  1.00 47.90           C  
ANISOU 3600  C   TYR B 468     5998   6684   5517    264   -526    529       C  
ATOM   3601  O   TYR B 468      14.385  85.815  -3.241  1.00 45.91           O  
ANISOU 3601  O   TYR B 468     5648   6522   5272    249   -427    591       O  
ATOM   3602  CB  TYR B 468      15.986  83.072  -4.133  1.00 51.56           C  
ANISOU 3602  CB  TYR B 468     6595   6989   6005    110   -656    558       C  
ATOM   3603  CG  TYR B 468      15.088  82.709  -2.972  1.00 54.69           C  
ANISOU 3603  CG  TYR B 468     7004   7419   6354     50   -559    658       C  
ATOM   3604  CD1 TYR B 468      13.792  82.260  -3.174  1.00 58.21           C  
ANISOU 3604  CD1 TYR B 468     7346   7920   6850    -80   -514    751       C  
ATOM   3605  CD2 TYR B 468      15.553  82.805  -1.669  1.00 57.03           C  
ANISOU 3605  CD2 TYR B 468     7418   7697   6554    122   -515    668       C  
ATOM   3606  CE1 TYR B 468      12.971  81.920  -2.101  1.00 61.83           C  
ANISOU 3606  CE1 TYR B 468     7799   8423   7269   -137   -401    863       C  
ATOM   3607  CE2 TYR B 468      14.752  82.469  -0.594  1.00 61.81           C  
ANISOU 3607  CE2 TYR B 468     8052   8335   7095     78   -406    767       C  
ATOM   3608  CZ  TYR B 468      13.464  82.026  -0.809  1.00 63.20           C  
ANISOU 3608  CZ  TYR B 468     8108   8575   7328    -49   -336    870       C  
ATOM   3609  OH  TYR B 468      12.695  81.692   0.286  1.00 68.28           O  
ANISOU 3609  OH  TYR B 468     8769   9262   7910    -91   -205    987       O  
ATOM   3610  N   HIS B 469      16.597  85.936  -2.827  1.00 47.84           N  
ANISOU 3610  N   HIS B 469     6096   6631   5450    355   -556    475       N  
ATOM   3611  CA  HIS B 469      16.452  86.794  -1.649  1.00 49.68           C  
ANISOU 3611  CA  HIS B 469     6389   6892   5594    438   -481    475       C  
ATOM   3612  C   HIS B 469      15.988  88.200  -1.978  1.00 50.63           C  
ANISOU 3612  C   HIS B 469     6422   7078   5735    512   -429    443       C  
ATOM   3613  O   HIS B 469      15.237  88.817  -1.209  1.00 50.04           O  
ANISOU 3613  O   HIS B 469     6358   7054   5598    576   -316    469       O  
ATOM   3614  CB  HIS B 469      17.757  86.840  -0.856  1.00 48.30           C  
ANISOU 3614  CB  HIS B 469     6368   6636   5348    496   -568    427       C  
ATOM   3615  CG  HIS B 469      17.987  85.591  -0.072  1.00 49.89           C  
ANISOU 3615  CG  HIS B 469     6690   6778   5487    456   -587    478       C  
ATOM   3616  ND1 HIS B 469      17.110  85.168   0.906  1.00 51.32           N  
ANISOU 3616  ND1 HIS B 469     6933   6983   5582    432   -477    557       N  
ATOM   3617  CD2 HIS B 469      18.942  84.634  -0.167  1.00 48.49           C  
ANISOU 3617  CD2 HIS B 469     6583   6517   5322    441   -692    474       C  
ATOM   3618  CE1 HIS B 469      17.531  84.012   1.395  1.00 52.44           C  
ANISOU 3618  CE1 HIS B 469     7192   7049   5682    392   -526    598       C  
ATOM   3619  NE2 HIS B 469      18.643  83.669   0.764  1.00 49.46           N  
ANISOU 3619  NE2 HIS B 469     6825   6603   5365    405   -660    546       N  
ATOM   3620  N   ILE B 470      16.442  88.705  -3.111  1.00 49.15           N  
ANISOU 3620  N   ILE B 470     6163   6883   5628    518   -502    392       N  
ATOM   3621  CA  ILE B 470      16.035  90.033  -3.542  1.00 51.47           C  
ANISOU 3621  CA  ILE B 470     6386   7222   5947    588   -466    366       C  
ATOM   3622  C   ILE B 470      14.594  90.060  -4.082  1.00 52.04           C  
ANISOU 3622  C   ILE B 470     6301   7395   6075    566   -382    432       C  
ATOM   3623  O   ILE B 470      13.922  91.077  -3.975  1.00 52.32           O  
ANISOU 3623  O   ILE B 470     6289   7484   6105    653   -306    439       O  
ATOM   3624  CB  ILE B 470      17.051  90.620  -4.540  1.00 51.69           C  
ANISOU 3624  CB  ILE B 470     6399   7206   6035    597   -568    303       C  
ATOM   3625  CG1 ILE B 470      17.159  92.135  -4.315  1.00 55.97           C  
ANISOU 3625  CG1 ILE B 470     6978   7733   6554    687   -557    261       C  
ATOM   3626  CG2 ILE B 470      16.699  90.251  -5.976  1.00 51.46           C  
ANISOU 3626  CG2 ILE B 470     6250   7210   6090    540   -595    318       C  
ATOM   3627  CD1 ILE B 470      18.387  92.768  -4.919  1.00 56.47           C  
ANISOU 3627  CD1 ILE B 470     7058   7735   6660    684   -660    211       C  
ATOM   3628  N   GLN B 471      14.140  88.945  -4.652  1.00 53.96           N  
ANISOU 3628  N   GLN B 471     6470   7659   6372    453   -407    484       N  
ATOM   3629  CA  GLN B 471      12.719  88.732  -4.979  1.00 58.67           C  
ANISOU 3629  CA  GLN B 471     6906   8359   7028    398   -345    573       C  
ATOM   3630  C   GLN B 471      11.852  89.052  -3.783  1.00 60.20           C  
ANISOU 3630  C   GLN B 471     7076   8628   7167    462   -189    641       C  
ATOM   3631  O   GLN B 471      10.858  89.761  -3.916  1.00 60.10           O  
ANISOU 3631  O   GLN B 471     6925   8715   7192    523   -105    689       O  
ATOM   3632  CB  GLN B 471      12.434  87.261  -5.349  1.00 60.90           C  
ANISOU 3632  CB  GLN B 471     7170   8620   7349    237   -403    628       C  
ATOM   3633  CG  GLN B 471      12.395  86.864  -6.808  1.00 63.08           C  
ANISOU 3633  CG  GLN B 471     7393   8877   7698    151   -526    610       C  
ATOM   3634  CD  GLN B 471      13.017  87.872  -7.740  1.00 66.56           C  
ANISOU 3634  CD  GLN B 471     7831   9306   8151    240   -578    530       C  
ATOM   3635  OE1 GLN B 471      12.343  88.795  -8.211  1.00 69.96           O  
ANISOU 3635  OE1 GLN B 471     8145   9815   8621    288   -558    547       O  
ATOM   3636  NE2 GLN B 471      14.298  87.689  -8.045  1.00 67.20           N  
ANISOU 3636  NE2 GLN B 471     8033   9293   8204    265   -644    453       N  
ATOM   3637  N   SER B 472      12.234  88.516  -2.618  1.00 62.87           N  
ANISOU 3637  N   SER B 472     7555   8920   7413    462   -145    652       N  
ATOM   3638  CA  SER B 472      11.412  88.596  -1.402  1.00 64.65           C  
ANISOU 3638  CA  SER B 472     7786   9215   7561    517     23    731       C  
ATOM   3639  C   SER B 472      11.320  90.014  -0.893  1.00 64.04           C  
ANISOU 3639  C   SER B 472     7758   9160   7413    700    113    683       C  
ATOM   3640  O   SER B 472      10.246  90.464  -0.526  1.00 65.63           O  
ANISOU 3640  O   SER B 472     7862   9466   7607    781    268    755       O  
ATOM   3641  CB  SER B 472      11.974  87.720  -0.267  1.00 66.97           C  
ANISOU 3641  CB  SER B 472     8265   9436   7745    483     34    747       C  
ATOM   3642  OG  SER B 472      13.048  86.921  -0.726  1.00 67.52           O  
ANISOU 3642  OG  SER B 472     8423   9393   7836    400   -126    693       O  
ATOM   3643  N   CYS B 473      12.450  90.715  -0.849  1.00 61.95           N  
ANISOU 3643  N   CYS B 473     7648   8791   7096    768     17    569       N  
ATOM   3644  CA  CYS B 473      12.483  92.035  -0.216  1.00 61.03           C  
ANISOU 3644  CA  CYS B 473     7646   8653   6887    935     82    512       C  
ATOM   3645  C   CYS B 473      12.670  93.205  -1.193  1.00 58.98           C  
ANISOU 3645  C   CYS B 473     7338   8371   6698    997     13    446       C  
ATOM   3646  O   CYS B 473      12.821  94.337  -0.748  1.00 57.06           O  
ANISOU 3646  O   CYS B 473     7222   8077   6380   1127     38    387       O  
ATOM   3647  CB  CYS B 473      13.581  92.059   0.842  1.00 62.01           C  
ANISOU 3647  CB  CYS B 473     8024   8662   6873    963     19    442       C  
ATOM   3648  SG  CYS B 473      15.217  91.746   0.179  1.00 60.03           S  
ANISOU 3648  SG  CYS B 473     7827   8297   6684    861   -213    359       S  
ATOM   3649  N   HIS B 474      12.649  92.939  -2.501  1.00 55.42           N  
ANISOU 3649  N   HIS B 474     6731   7947   6377    906    -73    457       N  
ATOM   3650  CA  HIS B 474      12.831  93.972  -3.542  1.00 56.06           C  
ANISOU 3650  CA  HIS B 474     6767   8007   6526    952   -141    409       C  
ATOM   3651  C   HIS B 474      14.261  94.517  -3.635  1.00 53.26           C  
ANISOU 3651  C   HIS B 474     6565   7524   6146    947   -270    313       C  
ATOM   3652  O   HIS B 474      14.864  94.507  -4.714  1.00 50.40           O  
ANISOU 3652  O   HIS B 474     6149   7137   5861    882   -372    291       O  
ATOM   3653  CB  HIS B 474      11.820  95.132  -3.411  1.00 60.22           C  
ANISOU 3653  CB  HIS B 474     7249   8588   7041   1112    -23    432       C  
ATOM   3654  CG  HIS B 474      11.989  96.198  -4.458  1.00 65.39           C  
ANISOU 3654  CG  HIS B 474     7879   9207   7758   1161    -97    393       C  
ATOM   3655  ND1 HIS B 474      11.723  95.982  -5.798  1.00 68.23           N  
ANISOU 3655  ND1 HIS B 474     8076   9619   8228   1087   -170    427       N  
ATOM   3656  CD2 HIS B 474      12.398  97.488  -4.364  1.00 67.38           C  
ANISOU 3656  CD2 HIS B 474     8270   9363   7966   1271   -115    326       C  
ATOM   3657  CE1 HIS B 474      11.963  97.089  -6.480  1.00 66.54           C  
ANISOU 3657  CE1 HIS B 474     7895   9352   8036   1155   -220    390       C  
ATOM   3658  NE2 HIS B 474      12.374  98.017  -5.634  1.00 67.37           N  
ANISOU 3658  NE2 HIS B 474     8179   9363   8055   1262   -189    331       N  
ATOM   3659  N   LYS B 475      14.801  95.021  -2.534  1.00 51.28           N  
ANISOU 3659  N   LYS B 475     6502   7194   5787   1013   -268    261       N  
ATOM   3660  CA  LYS B 475      16.194  95.453  -2.516  1.00 50.08           C  
ANISOU 3660  CA  LYS B 475     6478   6926   5623    980   -410    186       C  
ATOM   3661  C   LYS B 475      16.794  95.267  -1.134  1.00 49.70           C  
ANISOU 3661  C   LYS B 475     6626   6807   5448    994   -436    154       C  
ATOM   3662  O   LYS B 475      16.070  95.113  -0.162  1.00 51.05           O  
ANISOU 3662  O   LYS B 475     6871   7009   5515   1064   -320    178       O  
ATOM   3663  CB  LYS B 475      16.308  96.912  -2.941  1.00 52.40           C  
ANISOU 3663  CB  LYS B 475     6821   7156   5932   1052   -440    141       C  
ATOM   3664  CG  LYS B 475      15.896  97.907  -1.868  1.00 55.69           C  
ANISOU 3664  CG  LYS B 475     7422   7514   6222   1193   -369    103       C  
ATOM   3665  CD  LYS B 475      15.661  99.266  -2.470  1.00 59.32           C  
ANISOU 3665  CD  LYS B 475     7907   7920   6711   1279   -372     78       C  
ATOM   3666  CE  LYS B 475      15.507 100.305  -1.383  1.00 61.93           C  
ANISOU 3666  CE  LYS B 475     8485   8146   6900   1422   -331     18       C  
ATOM   3667  NZ  LYS B 475      14.444 101.228  -1.811  1.00 66.09           N  
ANISOU 3667  NZ  LYS B 475     8973   8696   7443   1576   -221     38       N  
ATOM   3668  N   PHE B 476      18.117  95.275  -1.056  1.00 46.66           N  
ANISOU 3668  N   PHE B 476     6320   6337   5070    930   -588    110       N  
ATOM   3669  CA  PHE B 476      18.795  95.109   0.218  1.00 47.51           C  
ANISOU 3669  CA  PHE B 476     6620   6374   5058    933   -655     81       C  
ATOM   3670  C   PHE B 476      19.094  96.459   0.884  1.00 48.90           C  
ANISOU 3670  C   PHE B 476     7001   6438   5137   1003   -710      9       C  
ATOM   3671  O   PHE B 476      19.387  97.441   0.214  1.00 49.22           O  
ANISOU 3671  O   PHE B 476     7028   6428   5244    998   -770    -21       O  
ATOM   3672  CB  PHE B 476      20.091  94.306   0.032  1.00 45.55           C  
ANISOU 3672  CB  PHE B 476     6336   6097   4872    829   -807     85       C  
ATOM   3673  CG  PHE B 476      19.891  92.908  -0.507  1.00 43.99           C  
ANISOU 3673  CG  PHE B 476     5998   5971   4743    771   -767    145       C  
ATOM   3674  CD1 PHE B 476      18.765  92.155  -0.192  1.00 44.69           C  
ANISOU 3674  CD1 PHE B 476     6064   6126   4788    782   -631    198       C  
ATOM   3675  CD2 PHE B 476      20.872  92.322  -1.295  1.00 43.74           C  
ANISOU 3675  CD2 PHE B 476     5867   5934   4815    704   -866    152       C  
ATOM   3676  CE1 PHE B 476      18.609  90.861  -0.686  1.00 44.27           C  
ANISOU 3676  CE1 PHE B 476     5912   6112   4796    709   -619    251       C  
ATOM   3677  CE2 PHE B 476      20.725  91.034  -1.787  1.00 43.11           C  
ANISOU 3677  CE2 PHE B 476     5703   5892   4782    661   -839    196       C  
ATOM   3678  CZ  PHE B 476      19.589  90.305  -1.486  1.00 43.76           C  
ANISOU 3678  CZ  PHE B 476     5785   6020   4822    654   -727    242       C  
ATOM   3679  N   ASP B 477      19.023  96.502   2.207  1.00 52.13           N  
ANISOU 3679  N   ASP B 477     7628   6799   5380   1065   -695    -15       N  
ATOM   3680  CA  ASP B 477      19.375  97.721   2.944  1.00 55.46           C  
ANISOU 3680  CA  ASP B 477     8302   7087   5682   1127   -775    -95       C  
ATOM   3681  C   ASP B 477      20.876  97.958   2.824  1.00 53.84           C  
ANISOU 3681  C   ASP B 477     8130   6787   5540   1000  -1020   -128       C  
ATOM   3682  O   ASP B 477      21.618  97.070   2.417  1.00 50.61           O  
ANISOU 3682  O   ASP B 477     7570   6425   5235    898  -1103    -86       O  
ATOM   3683  CB  ASP B 477      18.960  97.626   4.413  1.00 59.47           C  
ANISOU 3683  CB  ASP B 477     9063   7564   5968   1230   -701   -114       C  
ATOM   3684  CG  ASP B 477      19.682  96.509   5.151  1.00 63.31           C  
ANISOU 3684  CG  ASP B 477     9606   8051   6398   1151   -798    -87       C  
ATOM   3685  OD1 ASP B 477      20.798  96.752   5.663  1.00 65.13           O  
ANISOU 3685  OD1 ASP B 477     9989   8176   6581   1091  -1007   -134       O  
ATOM   3686  OD2 ASP B 477      19.131  95.384   5.197  1.00 65.81           O  
ANISOU 3686  OD2 ASP B 477     9810   8471   6722   1142   -677    -12       O  
ATOM   3687  N   LEU B 478      21.318  99.156   3.181  1.00 54.99           N  
ANISOU 3687  N   LEU B 478     8473   6795   5624   1009  -1136   -197       N  
ATOM   3688  CA  LEU B 478      22.679  99.577   2.877  1.00 55.10           C  
ANISOU 3688  CA  LEU B 478     8474   6725   5737    869  -1370   -210       C  
ATOM   3689  C   LEU B 478      23.755  98.657   3.481  1.00 54.38           C  
ANISOU 3689  C   LEU B 478     8379   6640   5642    774  -1534   -185       C  
ATOM   3690  O   LEU B 478      24.701  98.285   2.787  1.00 51.28           O  
ANISOU 3690  O   LEU B 478     7788   6285   5408    662  -1642   -139       O  
ATOM   3691  CB  LEU B 478      22.898 101.025   3.319  1.00 58.33           C  
ANISOU 3691  CB  LEU B 478     9144   6960   6059    883  -1483   -288       C  
ATOM   3692  CG  LEU B 478      24.297 101.612   3.095  1.00 60.25           C  
ANISOU 3692  CG  LEU B 478     9386   7100   6405    713  -1744   -291       C  
ATOM   3693  CD1 LEU B 478      24.591 101.688   1.604  1.00 59.16           C  
ANISOU 3693  CD1 LEU B 478     8954   7033   6490    627  -1722   -225       C  
ATOM   3694  CD2 LEU B 478      24.424 102.986   3.742  1.00 62.53           C  
ANISOU 3694  CD2 LEU B 478    10001   7185   6572    722  -1871   -376       C  
ATOM   3695  N   SER B 479      23.631  98.304   4.762  1.00 56.09           N  
ANISOU 3695  N   SER B 479     8817   6822   5673    829  -1548   -210       N  
ATOM   3696  CA  SER B 479      24.651  97.469   5.397  1.00 57.65           C  
ANISOU 3696  CA  SER B 479     9031   7017   5855    752  -1723   -182       C  
ATOM   3697  C   SER B 479      24.652  96.036   4.860  1.00 53.92           C  
ANISOU 3697  C   SER B 479     8314   6679   5493    732  -1640    -99       C  
ATOM   3698  O   SER B 479      25.720  95.449   4.688  1.00 51.75           O  
ANISOU 3698  O   SER B 479     7917   6422   5321    651  -1790    -58       O  
ATOM   3699  CB  SER B 479      24.533  97.487   6.928  1.00 63.23           C  
ANISOU 3699  CB  SER B 479    10075   7639   6310    819  -1773   -228       C  
ATOM   3700  OG  SER B 479      23.190  97.297   7.315  1.00 68.75           O  
ANISOU 3700  OG  SER B 479    10866   8387   6869    963  -1517   -229       O  
ATOM   3701  N   ARG B 480      23.470  95.490   4.553  1.00 51.96           N  
ANISOU 3701  N   ARG B 480     7987   6522   5233    807  -1408    -71       N  
ATOM   3702  CA  ARG B 480      23.374  94.156   3.958  1.00 49.97           C  
ANISOU 3702  CA  ARG B 480     7527   6374   5084    780  -1331      1       C  
ATOM   3703  C   ARG B 480      24.026  94.139   2.567  1.00 48.55           C  
ANISOU 3703  C   ARG B 480     7094   6236   5118    704  -1382     25       C  
ATOM   3704  O   ARG B 480      24.837  93.273   2.273  1.00 46.88           O  
ANISOU 3704  O   ARG B 480     6764   6052   4994    658  -1460     68       O  
ATOM   3705  CB  ARG B 480      21.914  93.679   3.899  1.00 48.90           C  
ANISOU 3705  CB  ARG B 480     7358   6321   4900    850  -1089     35       C  
ATOM   3706  CG  ARG B 480      21.708  92.279   3.336  1.00 48.54           C  
ANISOU 3706  CG  ARG B 480     7140   6358   4945    807  -1020    109       C  
ATOM   3707  CD  ARG B 480      20.243  91.846   3.369  1.00 48.55           C  
ANISOU 3707  CD  ARG B 480     7104   6439   4903    848   -801    157       C  
ATOM   3708  NE  ARG B 480      20.062  90.479   2.880  1.00 47.45           N  
ANISOU 3708  NE  ARG B 480     6834   6351   4842    783   -762    227       N  
ATOM   3709  CZ  ARG B 480      18.883  89.903   2.632  1.00 48.05           C  
ANISOU 3709  CZ  ARG B 480     6818   6504   4935    771   -603    290       C  
ATOM   3710  NH1 ARG B 480      17.734  90.565   2.796  1.00 50.31           N  
ANISOU 3710  NH1 ARG B 480     7090   6848   5177    834   -447    302       N  
ATOM   3711  NH2 ARG B 480      18.849  88.655   2.188  1.00 47.83           N  
ANISOU 3711  NH2 ARG B 480     6706   6491   4976    694   -606    346       N  
ATOM   3712  N   ALA B 481      23.679  95.109   1.724  1.00 48.69           N  
ANISOU 3712  N   ALA B 481     7040   6252   5207    706  -1330      2       N  
ATOM   3713  CA  ALA B 481      24.287  95.228   0.394  1.00 46.60           C  
ANISOU 3713  CA  ALA B 481     6559   6022   5123    640  -1365     28       C  
ATOM   3714  C   ALA B 481      25.801  95.409   0.467  1.00 45.93           C  
ANISOU 3714  C   ALA B 481     6439   5894   5116    554  -1570     42       C  
ATOM   3715  O   ALA B 481      26.542  94.830  -0.331  1.00 44.77           O  
ANISOU 3715  O   ALA B 481     6102   5804   5102    514  -1597     93       O  
ATOM   3716  CB  ALA B 481      23.674  96.405  -0.362  1.00 47.51           C  
ANISOU 3716  CB  ALA B 481     6654   6122   5275    660  -1292      3       C  
ATOM   3717  N   THR B 482      26.255  96.228   1.407  1.00 46.33           N  
ANISOU 3717  N   THR B 482     6673   5845   5085    528  -1717      2       N  
ATOM   3718  CA  THR B 482      27.683  96.499   1.552  1.00 48.16           C  
ANISOU 3718  CA  THR B 482     6862   6035   5400    424  -1942     27       C  
ATOM   3719  C   THR B 482      28.433  95.227   1.977  1.00 48.96           C  
ANISOU 3719  C   THR B 482     6893   6189   5519    424  -2024     80       C  
ATOM   3720  O   THR B 482      29.522  94.921   1.471  1.00 47.79           O  
ANISOU 3720  O   THR B 482     6551   6087   5520    369  -2121    143       O  
ATOM   3721  CB  THR B 482      27.918  97.620   2.579  1.00 51.33           C  
ANISOU 3721  CB  THR B 482     7522   6297   5684    388  -2108    -34       C  
ATOM   3722  OG1 THR B 482      27.308  98.830   2.114  1.00 50.10           O  
ANISOU 3722  OG1 THR B 482     7437   6075   5523    398  -2040    -79       O  
ATOM   3723  CG2 THR B 482      29.391  97.859   2.797  1.00 53.62           C  
ANISOU 3723  CG2 THR B 482     7756   6548   6069    256  -2371      4       C  
ATOM   3724  N   PHE B 483      27.836  94.490   2.905  1.00 49.09           N  
ANISOU 3724  N   PHE B 483     7067   6201   5383    497  -1974     64       N  
ATOM   3725  CA  PHE B 483      28.395  93.233   3.349  1.00 48.66           C  
ANISOU 3725  CA  PHE B 483     6980   6182   5325    515  -2037    117       C  
ATOM   3726  C   PHE B 483      28.583  92.240   2.185  1.00 46.74           C  
ANISOU 3726  C   PHE B 483     6485   6033   5237    532  -1937    177       C  
ATOM   3727  O   PHE B 483      29.685  91.713   1.980  1.00 46.92           O  
ANISOU 3727  O   PHE B 483     6368   6087   5370    518  -2047    234       O  
ATOM   3728  CB  PHE B 483      27.501  92.643   4.437  1.00 50.59           C  
ANISOU 3728  CB  PHE B 483     7449   6403   5367    590  -1954     99       C  
ATOM   3729  CG  PHE B 483      27.947  91.306   4.911  1.00 52.12           C  
ANISOU 3729  CG  PHE B 483     7642   6619   5542    616  -2006    158       C  
ATOM   3730  CD1 PHE B 483      28.963  91.198   5.849  1.00 53.97           C  
ANISOU 3730  CD1 PHE B 483     7974   6805   5726    597  -2235    176       C  
ATOM   3731  CD2 PHE B 483      27.365  90.154   4.416  1.00 51.54           C  
ANISOU 3731  CD2 PHE B 483     7479   6602   5499    657  -1845    200       C  
ATOM   3732  CE1 PHE B 483      29.389  89.962   6.285  1.00 55.45           C  
ANISOU 3732  CE1 PHE B 483     8166   7005   5894    637  -2290    238       C  
ATOM   3733  CE2 PHE B 483      27.793  88.915   4.849  1.00 52.05           C  
ANISOU 3733  CE2 PHE B 483     7566   6664   5543    687  -1898    258       C  
ATOM   3734  CZ  PHE B 483      28.807  88.824   5.775  1.00 54.03           C  
ANISOU 3734  CZ  PHE B 483     7910   6872   5746    686  -2115    278       C  
ATOM   3735  N   TYR B 484      27.522  91.989   1.418  1.00 44.90           N  
ANISOU 3735  N   TYR B 484     6200   5845   5012    568  -1733    168       N  
ATOM   3736  CA  TYR B 484      27.626  91.079   0.271  1.00 43.41           C  
ANISOU 3736  CA  TYR B 484     5819   5726   4946    586  -1642    211       C  
ATOM   3737  C   TYR B 484      28.667  91.587  -0.728  1.00 43.34           C  
ANISOU 3737  C   TYR B 484     5612   5750   5102    545  -1703    241       C  
ATOM   3738  O   TYR B 484      29.481  90.804  -1.213  1.00 43.12           O  
ANISOU 3738  O   TYR B 484     5446   5765   5170    570  -1723    293       O  
ATOM   3739  CB  TYR B 484      26.279  90.884  -0.439  1.00 42.83           C  
ANISOU 3739  CB  TYR B 484     5727   5689   4854    609  -1444    195       C  
ATOM   3740  CG  TYR B 484      25.211  90.214   0.387  1.00 42.27           C  
ANISOU 3740  CG  TYR B 484     5800   5610   4649    640  -1351    195       C  
ATOM   3741  CD1 TYR B 484      25.519  89.212   1.300  1.00 42.61           C  
ANISOU 3741  CD1 TYR B 484     5945   5626   4619    660  -1407    227       C  
ATOM   3742  CD2 TYR B 484      23.884  90.569   0.235  1.00 41.59           C  
ANISOU 3742  CD2 TYR B 484     5736   5550   4514    653  -1202    179       C  
ATOM   3743  CE1 TYR B 484      24.529  88.590   2.047  1.00 43.27           C  
ANISOU 3743  CE1 TYR B 484     6160   5703   4577    677  -1307    245       C  
ATOM   3744  CE2 TYR B 484      22.894  89.959   0.974  1.00 42.96           C  
ANISOU 3744  CE2 TYR B 484     6012   5733   4577    674  -1098    201       C  
ATOM   3745  CZ  TYR B 484      23.222  88.970   1.884  1.00 43.49           C  
ANISOU 3745  CZ  TYR B 484     6190   5768   4566    680  -1147    235       C  
ATOM   3746  OH  TYR B 484      22.217  88.398   2.607  1.00 44.18           O  
ANISOU 3746  OH  TYR B 484     6377   5865   4542    690  -1029    273       O  
ATOM   3747  N   ALA B 485      28.661  92.892  -1.007  1.00 43.23           N  
ANISOU 3747  N   ALA B 485     5593   5713   5119    489  -1726    216       N  
ATOM   3748  CA  ALA B 485      29.633  93.497  -1.924  1.00 42.96           C  
ANISOU 3748  CA  ALA B 485     5373   5708   5239    430  -1777    261       C  
ATOM   3749  C   ALA B 485      31.088  93.232  -1.494  1.00 44.57           C  
ANISOU 3749  C   ALA B 485     5478   5927   5530    396  -1958    325       C  
ATOM   3750  O   ALA B 485      31.928  92.878  -2.315  1.00 45.30           O  
ANISOU 3750  O   ALA B 485     5361   6091   5759    405  -1943    395       O  
ATOM   3751  CB  ALA B 485      29.391  94.997  -2.048  1.00 42.68           C  
ANISOU 3751  CB  ALA B 485     5400   5613   5203    362  -1802    227       C  
ATOM   3752  N   ALA B 486      31.385  93.405  -0.216  1.00 46.12           N  
ANISOU 3752  N   ALA B 486     5820   6059   5643    366  -2128    309       N  
ATOM   3753  CA  ALA B 486      32.761  93.175   0.262  1.00 48.90           C  
ANISOU 3753  CA  ALA B 486     6069   6428   6081    328  -2333    379       C  
ATOM   3754  C   ALA B 486      33.186  91.704   0.137  1.00 47.77           C  
ANISOU 3754  C   ALA B 486     5815   6356   5979    435  -2296    438       C  
ATOM   3755  O   ALA B 486      34.288  91.430  -0.307  1.00 49.86           O  
ANISOU 3755  O   ALA B 486     5860   6689   6393    442  -2353    523       O  
ATOM   3756  CB  ALA B 486      32.934  93.669   1.693  1.00 50.13           C  
ANISOU 3756  CB  ALA B 486     6445   6488   6113    273  -2547    343       C  
ATOM   3757  N   GLU B 487      32.312  90.773   0.511  1.00 47.07           N  
ANISOU 3757  N   GLU B 487     5876   6246   5762    520  -2193    400       N  
ATOM   3758  CA  GLU B 487      32.622  89.341   0.420  1.00 47.74           C  
ANISOU 3758  CA  GLU B 487     5904   6366   5868    626  -2157    449       C  
ATOM   3759  C   GLU B 487      32.848  88.955  -1.042  1.00 47.31           C  
ANISOU 3759  C   GLU B 487     5640   6385   5948    679  -2006    484       C  
ATOM   3760  O   GLU B 487      33.804  88.241  -1.366  1.00 46.32           O  
ANISOU 3760  O   GLU B 487     5363   6310   5925    755  -2031    555       O  
ATOM   3761  CB  GLU B 487      31.543  88.453   1.093  1.00 47.47           C  
ANISOU 3761  CB  GLU B 487     6091   6279   5666    682  -2071    410       C  
ATOM   3762  CG  GLU B 487      31.411  88.635   2.608  1.00 49.24           C  
ANISOU 3762  CG  GLU B 487     6545   6433   5730    660  -2209    389       C  
ATOM   3763  CD  GLU B 487      30.862  87.413   3.351  1.00 49.85           C  
ANISOU 3763  CD  GLU B 487     6796   6472   5673    730  -2164    403       C  
ATOM   3764  OE1 GLU B 487      31.281  87.188   4.514  1.00 52.02           O  
ANISOU 3764  OE1 GLU B 487     7213   6702   5849    742  -2320    424       O  
ATOM   3765  OE2 GLU B 487      30.034  86.663   2.800  1.00 49.10           O  
ANISOU 3765  OE2 GLU B 487     6706   6383   5566    765  -1987    400       O  
ATOM   3766  N   ILE B 488      32.005  89.475  -1.932  1.00 46.05           N  
ANISOU 3766  N   ILE B 488     5477   6234   5786    651  -1852    439       N  
ATOM   3767  CA  ILE B 488      32.177  89.243  -3.360  1.00 46.21           C  
ANISOU 3767  CA  ILE B 488     5331   6317   5907    696  -1710    466       C  
ATOM   3768  C   ILE B 488      33.515  89.783  -3.858  1.00 47.86           C  
ANISOU 3768  C   ILE B 488     5309   6595   6277    673  -1775    549       C  
ATOM   3769  O   ILE B 488      34.176  89.145  -4.665  1.00 49.47           O  
ANISOU 3769  O   ILE B 488     5361   6864   6570    763  -1699    606       O  
ATOM   3770  CB  ILE B 488      31.012  89.844  -4.178  1.00 44.60           C  
ANISOU 3770  CB  ILE B 488     5174   6107   5662    659  -1562    408       C  
ATOM   3771  CG1 ILE B 488      29.742  89.025  -3.930  1.00 43.72           C  
ANISOU 3771  CG1 ILE B 488     5229   5956   5426    693  -1470    355       C  
ATOM   3772  CG2 ILE B 488      31.332  89.826  -5.674  1.00 44.65           C  
ANISOU 3772  CG2 ILE B 488     5022   6178   5764    694  -1438    441       C  
ATOM   3773  CD1 ILE B 488      28.449  89.660  -4.427  1.00 42.33           C  
ANISOU 3773  CD1 ILE B 488     5108   5776   5198    652  -1357    304       C  
ATOM   3774  N   ILE B 489      33.916  90.955  -3.378  1.00 48.93           N  
ANISOU 3774  N   ILE B 489     5423   6716   6451    554  -1914    561       N  
ATOM   3775  CA  ILE B 489      35.206  91.527  -3.768  1.00 49.81           C  
ANISOU 3775  CA  ILE B 489     5297   6896   6732    498  -1996    661       C  
ATOM   3776  C   ILE B 489      36.372  90.598  -3.417  1.00 51.83           C  
ANISOU 3776  C   ILE B 489     5402   7215   7077    583  -2091    752       C  
ATOM   3777  O   ILE B 489      37.295  90.389  -4.219  1.00 52.94           O  
ANISOU 3777  O   ILE B 489     5299   7453   7361    636  -2032    848       O  
ATOM   3778  CB  ILE B 489      35.401  92.889  -3.101  1.00 50.53           C  
ANISOU 3778  CB  ILE B 489     5439   6926   6833    333  -2174    654       C  
ATOM   3779  CG1 ILE B 489      34.558  93.941  -3.826  1.00 49.86           C  
ANISOU 3779  CG1 ILE B 489     5423   6801   6720    265  -2059    602       C  
ATOM   3780  CG2 ILE B 489      36.868  93.302  -3.114  1.00 53.08           C  
ANISOU 3780  CG2 ILE B 489     5516   7314   7337    249  -2330    778       C  
ATOM   3781  CD1 ILE B 489      34.354  95.192  -3.003  1.00 51.40           C  
ANISOU 3781  CD1 ILE B 489     5784   6885   6857    133  -2218    553       C  
ATOM   3782  N   LEU B 490      36.327  90.040  -2.216  1.00 52.69           N  
ANISOU 3782  N   LEU B 490     5655   7269   7095    609  -2230    728       N  
ATOM   3783  CA  LEU B 490      37.372  89.112  -1.766  1.00 54.75           C  
ANISOU 3783  CA  LEU B 490     5797   7578   7426    706  -2342    816       C  
ATOM   3784  C   LEU B 490      37.418  87.866  -2.646  1.00 54.54           C  
ANISOU 3784  C   LEU B 490     5699   7597   7425    891  -2150    840       C  
ATOM   3785  O   LEU B 490      38.493  87.404  -3.027  1.00 56.68           O  
ANISOU 3785  O   LEU B 490     5747   7957   7831    990  -2151    942       O  
ATOM   3786  CB  LEU B 490      37.133  88.726  -0.313  1.00 55.34           C  
ANISOU 3786  CB  LEU B 490     6098   7568   7360    705  -2515    778       C  
ATOM   3787  CG  LEU B 490      37.321  89.868   0.702  1.00 57.18           C  
ANISOU 3787  CG  LEU B 490     6425   7743   7555    541  -2751    760       C  
ATOM   3788  CD1 LEU B 490      36.717  89.477   2.045  1.00 57.58           C  
ANISOU 3788  CD1 LEU B 490     6780   7694   7401    559  -2855    695       C  
ATOM   3789  CD2 LEU B 490      38.794  90.249   0.858  1.00 58.14           C  
ANISOU 3789  CD2 LEU B 490     6292   7938   7858    473  -2970    882       C  
ATOM   3790  N   GLY B 491      36.247  87.336  -2.991  1.00 53.40           N  
ANISOU 3790  N   GLY B 491     5745   7391   7151    940  -1987    749       N  
ATOM   3791  CA  GLY B 491      36.178  86.185  -3.879  1.00 53.48           C  
ANISOU 3791  CA  GLY B 491     5742   7414   7162   1102  -1813    754       C  
ATOM   3792  C   GLY B 491      36.767  86.478  -5.242  1.00 53.56           C  
ANISOU 3792  C   GLY B 491     5531   7521   7296   1147  -1668    809       C  
ATOM   3793  O   GLY B 491      37.589  85.708  -5.759  1.00 53.92           O  
ANISOU 3793  O   GLY B 491     5443   7623   7419   1303  -1601    879       O  
ATOM   3794  N   LEU B 492      36.348  87.602  -5.818  1.00 52.29           N  
ANISOU 3794  N   LEU B 492     5343   7376   7147   1022  -1611    783       N  
ATOM   3795  CA  LEU B 492      36.812  88.016  -7.150  1.00 52.59           C  
ANISOU 3795  CA  LEU B 492     5194   7503   7283   1045  -1459    840       C  
ATOM   3796  C   LEU B 492      38.317  88.235  -7.184  1.00 54.11           C  
ANISOU 3796  C   LEU B 492     5091   7811   7658   1066  -1523    982       C  
ATOM   3797  O   LEU B 492      39.002  87.705  -8.063  1.00 55.79           O  
ANISOU 3797  O   LEU B 492     5145   8108   7942   1212  -1380   1056       O  
ATOM   3798  CB  LEU B 492      36.115  89.314  -7.588  1.00 50.60           C  
ANISOU 3798  CB  LEU B 492     4980   7234   7011    889  -1424    798       C  
ATOM   3799  CG  LEU B 492      34.678  89.150  -8.078  1.00 49.54           C  
ANISOU 3799  CG  LEU B 492     5060   7030   6732    893  -1300    686       C  
ATOM   3800  CD1 LEU B 492      34.150  90.518  -8.483  1.00 49.42           C  
ANISOU 3800  CD1 LEU B 492     5053   7005   6716    756  -1282    666       C  
ATOM   3801  CD2 LEU B 492      34.550  88.146  -9.226  1.00 48.68           C  
ANISOU 3801  CD2 LEU B 492     4970   6940   6587   1044  -1118    677       C  
ATOM   3802  N   GLN B 493      38.814  89.035  -6.245  1.00 53.80           N  
ANISOU 3802  N   GLN B 493     4979   7775   7688    921  -1735   1025       N  
ATOM   3803  CA  GLN B 493      40.234  89.361  -6.180  1.00 56.47           C  
ANISOU 3803  CA  GLN B 493     5009   8226   8218    897  -1837   1177       C  
ATOM   3804  C   GLN B 493      41.104  88.125  -5.973  1.00 59.10           C  
ANISOU 3804  C   GLN B 493     5215   8624   8614   1099  -1848   1257       C  
ATOM   3805  O   GLN B 493      42.215  88.055  -6.501  1.00 60.86           O  
ANISOU 3805  O   GLN B 493     5141   8979   9001   1174  -1797   1396       O  
ATOM   3806  CB  GLN B 493      40.494  90.374  -5.066  1.00 57.41           C  
ANISOU 3806  CB  GLN B 493     5134   8304   8374    686  -2111   1191       C  
ATOM   3807  CG  GLN B 493      40.074  91.773  -5.452  1.00 56.46           C  
ANISOU 3807  CG  GLN B 493     5048   8145   8259    492  -2102   1165       C  
ATOM   3808  CD  GLN B 493      40.381  92.803  -4.394  1.00 58.63           C  
ANISOU 3808  CD  GLN B 493     5359   8355   8563    283  -2384   1175       C  
ATOM   3809  OE1 GLN B 493      40.466  92.502  -3.203  1.00 59.58           O  
ANISOU 3809  OE1 GLN B 493     5594   8421   8622    275  -2587   1146       O  
ATOM   3810  NE2 GLN B 493      40.542  94.041  -4.826  1.00 60.82           N  
ANISOU 3810  NE2 GLN B 493     5563   8623   8920    109  -2404   1216       N  
ATOM   3811  N   PHE B 494      40.595  87.157  -5.209  1.00 58.84           N  
ANISOU 3811  N   PHE B 494     5404   8499   8452   1194  -1905   1180       N  
ATOM   3812  CA  PHE B 494      41.263  85.880  -5.081  1.00 60.57           C  
ANISOU 3812  CA  PHE B 494     5560   8749   8704   1415  -1895   1241       C  
ATOM   3813  C   PHE B 494      41.439  85.247  -6.456  1.00 61.57           C  
ANISOU 3813  C   PHE B 494     5603   8935   8856   1610  -1620   1265       C  
ATOM   3814  O   PHE B 494      42.553  84.879  -6.851  1.00 63.49           O  
ANISOU 3814  O   PHE B 494     5588   9296   9237   1762  -1565   1393       O  
ATOM   3815  CB  PHE B 494      40.491  84.928  -4.171  1.00 59.43           C  
ANISOU 3815  CB  PHE B 494     5721   8468   8388   1476  -1967   1145       C  
ATOM   3816  CG  PHE B 494      41.080  83.542  -4.123  1.00 61.12           C  
ANISOU 3816  CG  PHE B 494     5919   8685   8620   1722  -1941   1200       C  
ATOM   3817  CD1 PHE B 494      42.341  83.327  -3.568  1.00 64.26           C  
ANISOU 3817  CD1 PHE B 494     6085   9171   9159   1804  -2100   1335       C  
ATOM   3818  CD2 PHE B 494      40.397  82.458  -4.653  1.00 59.87           C  
ANISOU 3818  CD2 PHE B 494     5973   8434   8340   1875  -1768   1123       C  
ATOM   3819  CE1 PHE B 494      42.902  82.054  -3.545  1.00 65.35           C  
ANISOU 3819  CE1 PHE B 494     6207   9307   9315   2059  -2071   1392       C  
ATOM   3820  CE2 PHE B 494      40.952  81.185  -4.630  1.00 62.46           C  
ANISOU 3820  CE2 PHE B 494     6313   8740   8677   2116  -1744   1171       C  
ATOM   3821  CZ  PHE B 494      42.202  80.979  -4.069  1.00 63.80           C  
ANISOU 3821  CZ  PHE B 494     6254   8999   8985   2221  -1888   1305       C  
ATOM   3822  N   LEU B 495      40.338  85.132  -7.186  1.00 59.04           N  
ANISOU 3822  N   LEU B 495     5500   8536   8396   1611  -1449   1148       N  
ATOM   3823  CA  LEU B 495      40.356  84.546  -8.529  1.00 59.70           C  
ANISOU 3823  CA  LEU B 495     5576   8649   8458   1789  -1192   1147       C  
ATOM   3824  C   LEU B 495      41.338  85.281  -9.443  1.00 61.78           C  
ANISOU 3824  C   LEU B 495     5521   9072   8879   1797  -1076   1277       C  
ATOM   3825  O   LEU B 495      42.206  84.661 -10.097  1.00 64.83           O  
ANISOU 3825  O   LEU B 495     5743   9549   9337   2010   -931   1369       O  
ATOM   3826  CB  LEU B 495      38.946  84.579  -9.127  1.00 58.03           C  
ANISOU 3826  CB  LEU B 495     5641   8329   8076   1726  -1076   1003       C  
ATOM   3827  CG  LEU B 495      37.915  83.648  -8.483  1.00 56.54           C  
ANISOU 3827  CG  LEU B 495     5763   7988   7730   1742  -1131    889       C  
ATOM   3828  CD1 LEU B 495      36.504  84.027  -8.917  1.00 54.88           C  
ANISOU 3828  CD1 LEU B 495     5760   7700   7389   1612  -1064    771       C  
ATOM   3829  CD2 LEU B 495      38.227  82.199  -8.840  1.00 58.70           C  
ANISOU 3829  CD2 LEU B 495     6125   8214   7963   1989  -1037    892       C  
ATOM   3830  N   HIS B 496      41.233  86.605  -9.443  1.00 60.15           N  
ANISOU 3830  N   HIS B 496     5227   8898   8728   1569  -1137   1296       N  
ATOM   3831  CA  HIS B 496      42.110  87.441 -10.242  1.00 62.59           C  
ANISOU 3831  CA  HIS B 496     5237   9350   9191   1526  -1041   1434       C  
ATOM   3832  C   HIS B 496      43.577  87.205  -9.889  1.00 66.11           C  
ANISOU 3832  C   HIS B 496     5341   9938   9837   1613  -1114   1611       C  
ATOM   3833  O   HIS B 496      44.417  87.136 -10.782  1.00 69.56           O  
ANISOU 3833  O   HIS B 496     5533  10514  10382   1738   -931   1739       O  
ATOM   3834  CB  HIS B 496      41.743  88.921 -10.090  1.00 61.78           C  
ANISOU 3834  CB  HIS B 496     5131   9225   9116   1243  -1147   1426       C  
ATOM   3835  CG  HIS B 496      40.358  89.251 -10.563  1.00 59.30           C  
ANISOU 3835  CG  HIS B 496     5103   8798   8628   1174  -1058   1277       C  
ATOM   3836  ND1 HIS B 496      39.697  90.400 -10.186  1.00 58.44           N  
ANISOU 3836  ND1 HIS B 496     5097   8615   8489    952  -1175   1222       N  
ATOM   3837  CD2 HIS B 496      39.500  88.569 -11.359  1.00 57.52           C  
ANISOU 3837  CD2 HIS B 496     5086   8516   8251   1300   -880   1176       C  
ATOM   3838  CE1 HIS B 496      38.499  90.422 -10.745  1.00 56.62           C  
ANISOU 3838  CE1 HIS B 496     5098   8305   8108    956  -1062   1104       C  
ATOM   3839  NE2 HIS B 496      38.357  89.325 -11.469  1.00 56.33           N  
ANISOU 3839  NE2 HIS B 496     5124   8278   7997   1152   -892   1075       N  
ATOM   3840  N   SER B 497      43.883  87.036  -8.602  1.00 67.21           N  
ANISOU 3840  N   SER B 497     5465  10050  10020   1564  -1373   1626       N  
ATOM   3841  CA  SER B 497      45.270  86.789  -8.164  1.00 69.46           C  
ANISOU 3841  CA  SER B 497     5413  10473  10504   1643  -1485   1803       C  
ATOM   3842  C   SER B 497      45.837  85.469  -8.713  1.00 71.17           C  
ANISOU 3842  C   SER B 497     5551  10754  10734   1986  -1293   1858       C  
ATOM   3843  O   SER B 497      47.050  85.331  -8.923  1.00 76.65           O  
ANISOU 3843  O   SER B 497     5894  11613  11614   2108  -1256   2036       O  
ATOM   3844  CB  SER B 497      45.349  86.760  -6.638  1.00 69.73           C  
ANISOU 3844  CB  SER B 497     5516  10440  10539   1537  -1819   1786       C  
ATOM   3845  OG  SER B 497      44.876  85.517  -6.125  1.00 69.05           O  
ANISOU 3845  OG  SER B 497     5684  10245  10307   1723  -1832   1691       O  
ATOM   3846  N   LYS B 498      44.953  84.499  -8.909  1.00 69.17           N  
ANISOU 3846  N   LYS B 498     5631  10364  10286   2142  -1180   1710       N  
ATOM   3847  CA  LYS B 498      45.297  83.216  -9.505  1.00 69.43           C  
ANISOU 3847  CA  LYS B 498     5689  10407  10285   2475   -986   1727       C  
ATOM   3848  C   LYS B 498      45.294  83.256 -11.032  1.00 69.71           C  
ANISOU 3848  C   LYS B 498     5697  10504  10286   2600   -660   1736       C  
ATOM   3849  O   LYS B 498      45.656  82.274 -11.673  1.00 70.59           O  
ANISOU 3849  O   LYS B 498     5828  10629  10363   2895   -467   1755       O  
ATOM   3850  CB  LYS B 498      44.312  82.142  -9.026  1.00 67.70           C  
ANISOU 3850  CB  LYS B 498     5875   9986   9861   2563  -1029   1564       C  
ATOM   3851  CG  LYS B 498      44.306  81.934  -7.515  1.00 67.74           C  
ANISOU 3851  CG  LYS B 498     5950   9921   9866   2480  -1327   1558       C  
ATOM   3852  CD  LYS B 498      45.639  81.388  -7.024  1.00 70.79           C  
ANISOU 3852  CD  LYS B 498     6059  10419  10419   2668  -1426   1721       C  
ATOM   3853  CE  LYS B 498      45.814  81.541  -5.520  1.00 71.16           C  
ANISOU 3853  CE  LYS B 498     6108  10433  10494   2531  -1764   1748       C  
ATOM   3854  NZ  LYS B 498      47.166  81.063  -5.110  1.00 74.75           N  
ANISOU 3854  NZ  LYS B 498     6253  11016  11130   2714  -1874   1927       N  
ATOM   3855  N   GLY B 499      44.883  84.379 -11.618  1.00 67.96           N  
ANISOU 3855  N   GLY B 499     5454  10308  10058   2389   -598   1722       N  
ATOM   3856  CA  GLY B 499      44.887  84.527 -13.064  1.00 67.87           C  
ANISOU 3856  CA  GLY B 499     5425  10360  10002   2488   -299   1741       C  
ATOM   3857  C   GLY B 499      43.641  83.925 -13.672  1.00 66.41           C  
ANISOU 3857  C   GLY B 499     5655  10006   9571   2555   -180   1550       C  
ATOM   3858  O   GLY B 499      43.685  83.344 -14.768  1.00 67.37           O  
ANISOU 3858  O   GLY B 499     5864  10132   9598   2772     65   1536       O  
ATOM   3859  N   ILE B 500      42.523  84.095 -12.958  1.00 62.88           N  
ANISOU 3859  N   ILE B 500     5464   9409   9015   2363   -359   1407       N  
ATOM   3860  CA  ILE B 500      41.238  83.589 -13.384  1.00 60.85           C  
ANISOU 3860  CA  ILE B 500     5584   8991   8543   2373   -297   1234       C  
ATOM   3861  C   ILE B 500      40.246  84.756 -13.424  1.00 57.96           C  
ANISOU 3861  C   ILE B 500     5307   8585   8127   2095   -361   1162       C  
ATOM   3862  O   ILE B 500      40.108  85.495 -12.445  1.00 55.89           O  
ANISOU 3862  O   ILE B 500     4991   8314   7928   1892   -560   1165       O  
ATOM   3863  CB  ILE B 500      40.695  82.530 -12.409  1.00 60.93           C  
ANISOU 3863  CB  ILE B 500     5839   8848   8461   2423   -447   1135       C  
ATOM   3864  CG1 ILE B 500      41.682  81.370 -12.256  1.00 63.18           C  
ANISOU 3864  CG1 ILE B 500     6050   9154   8798   2709   -409   1210       C  
ATOM   3865  CG2 ILE B 500      39.328  82.024 -12.862  1.00 58.95           C  
ANISOU 3865  CG2 ILE B 500     5959   8433   8003   2400   -395    970       C  
ATOM   3866  CD1 ILE B 500      41.438  80.572 -11.000  1.00 63.18           C  
ANISOU 3866  CD1 ILE B 500     6208   9033   8763   2718   -612   1165       C  
ATOM   3867  N   VAL B 501      39.589  84.911 -14.567  1.00 56.88           N  
ANISOU 3867  N   VAL B 501     5318   8421   7870   2104   -196   1099       N  
ATOM   3868  CA  VAL B 501      38.524  85.896 -14.754  1.00 55.10           C  
ANISOU 3868  CA  VAL B 501     5213   8146   7575   1881   -237   1023       C  
ATOM   3869  C   VAL B 501      37.214  85.122 -14.855  1.00 53.38           C  
ANISOU 3869  C   VAL B 501     5338   7772   7168   1896   -248    863       C  
ATOM   3870  O   VAL B 501      37.115  84.147 -15.594  1.00 53.99           O  
ANISOU 3870  O   VAL B 501     5575   7800   7138   2074   -123    817       O  
ATOM   3871  CB  VAL B 501      38.751  86.741 -16.018  1.00 55.94           C  
ANISOU 3871  CB  VAL B 501     5219   8345   7690   1864    -55   1091       C  
ATOM   3872  CG1 VAL B 501      37.633  87.770 -16.195  1.00 53.95           C  
ANISOU 3872  CG1 VAL B 501     5098   8032   7366   1649   -111   1017       C  
ATOM   3873  CG2 VAL B 501      40.097  87.439 -15.941  1.00 58.66           C  
ANISOU 3873  CG2 VAL B 501     5200   8849   8237   1840    -36   1273       C  
ATOM   3874  N   TYR B 502      36.217  85.573 -14.106  1.00 52.29           N  
ANISOU 3874  N   TYR B 502     5316   7558   6993   1706   -400    784       N  
ATOM   3875  CA  TYR B 502      35.017  84.791 -13.828  1.00 50.98           C  
ANISOU 3875  CA  TYR B 502     5430   7253   6686   1689   -456    657       C  
ATOM   3876  C   TYR B 502      33.973  84.915 -14.946  1.00 50.01           C  
ANISOU 3876  C   TYR B 502     5485   7084   6431   1655   -361    578       C  
ATOM   3877  O   TYR B 502      33.376  83.916 -15.353  1.00 50.17           O  
ANISOU 3877  O   TYR B 502     5725   7006   6330   1732   -329    499       O  
ATOM   3878  CB  TYR B 502      34.448  85.202 -12.451  1.00 50.10           C  
ANISOU 3878  CB  TYR B 502     5346   7097   6593   1518   -646    626       C  
ATOM   3879  CG  TYR B 502      33.166  84.486 -12.059  1.00 49.33           C  
ANISOU 3879  CG  TYR B 502     5503   6872   6365   1472   -699    519       C  
ATOM   3880  CD1 TYR B 502      33.171  83.144 -11.712  1.00 50.42           C  
ANISOU 3880  CD1 TYR B 502     5784   6922   6450   1586   -718    494       C  
ATOM   3881  CD2 TYR B 502      31.960  85.148 -12.042  1.00 49.61           C  
ANISOU 3881  CD2 TYR B 502     5630   6877   6342   1318   -728    457       C  
ATOM   3882  CE1 TYR B 502      32.004  82.480 -11.369  1.00 50.16           C  
ANISOU 3882  CE1 TYR B 502     5974   6773   6309   1521   -766    415       C  
ATOM   3883  CE2 TYR B 502      30.779  84.487 -11.700  1.00 50.11           C  
ANISOU 3883  CE2 TYR B 502     5893   6843   6304   1266   -769    382       C  
ATOM   3884  CZ  TYR B 502      30.804  83.160 -11.364  1.00 49.71           C  
ANISOU 3884  CZ  TYR B 502     5977   6706   6205   1355   -789    365       C  
ATOM   3885  OH  TYR B 502      29.621  82.530 -11.019  1.00 50.18           O  
ANISOU 3885  OH  TYR B 502     6222   6668   6174   1276   -831    308       O  
ATOM   3886  N   ARG B 503      33.741  86.144 -15.408  1.00 50.03           N  
ANISOU 3886  N   ARG B 503     5406   7145   6457   1531   -338    600       N  
ATOM   3887  CA  ARG B 503      32.927  86.427 -16.617  1.00 50.05           C  
ANISOU 3887  CA  ARG B 503     5542   7128   6346   1511   -245    551       C  
ATOM   3888  C   ARG B 503      31.405  86.224 -16.531  1.00 48.39           C  
ANISOU 3888  C   ARG B 503     5548   6816   6022   1407   -328    441       C  
ATOM   3889  O   ARG B 503      30.688  86.604 -17.454  1.00 48.28           O  
ANISOU 3889  O   ARG B 503     5624   6793   5925   1369   -286    410       O  
ATOM   3890  CB  ARG B 503      33.482  85.676 -17.832  1.00 53.05           C  
ANISOU 3890  CB  ARG B 503     5987   7521   6648   1711    -70    564       C  
ATOM   3891  CG  ARG B 503      34.979  85.905 -18.052  1.00 55.19           C  
ANISOU 3891  CG  ARG B 503     6010   7919   7038   1829     49    697       C  
ATOM   3892  CD  ARG B 503      35.406  85.617 -19.487  1.00 57.98           C  
ANISOU 3892  CD  ARG B 503     6420   8311   7297   2007    267    724       C  
ATOM   3893  NE  ARG B 503      35.410  84.188 -19.792  1.00 59.07           N  
ANISOU 3893  NE  ARG B 503     6770   8357   7314   2213    326    652       N  
ATOM   3894  CZ  ARG B 503      35.823  83.640 -20.932  1.00 61.43           C  
ANISOU 3894  CZ  ARG B 503     7177   8661   7500   2422    517    656       C  
ATOM   3895  NH1 ARG B 503      36.292  84.384 -21.923  1.00 62.52           N  
ANISOU 3895  NH1 ARG B 503     7217   8909   7628   2457    688    741       N  
ATOM   3896  NH2 ARG B 503      35.788  82.313 -21.065  1.00 63.60           N  
ANISOU 3896  NH2 ARG B 503     7680   8820   7662   2605    542    579       N  
ATOM   3897  N   ASP B 504      30.882  85.665 -15.447  1.00 47.51           N  
ANISOU 3897  N   ASP B 504     5511   6633   5905   1357   -447    394       N  
ATOM   3898  CA  ASP B 504      29.428  85.459 -15.378  1.00 45.84           C  
ANISOU 3898  CA  ASP B 504     5471   6342   5602   1251   -514    312       C  
ATOM   3899  C   ASP B 504      28.837  85.874 -14.036  1.00 45.00           C  
ANISOU 3899  C   ASP B 504     5336   6223   5536   1120   -634    303       C  
ATOM   3900  O   ASP B 504      27.906  85.262 -13.524  1.00 44.17           O  
ANISOU 3900  O   ASP B 504     5355   6050   5377   1065   -694    257       O  
ATOM   3901  CB  ASP B 504      29.103  84.007 -15.718  1.00 48.05           C  
ANISOU 3901  CB  ASP B 504     5960   6517   5779   1337   -506    253       C  
ATOM   3902  CG  ASP B 504      27.676  83.822 -16.183  1.00 49.36           C  
ANISOU 3902  CG  ASP B 504     6290   6616   5846   1231   -553    185       C  
ATOM   3903  OD1 ASP B 504      27.094  84.772 -16.741  1.00 51.37           O  
ANISOU 3903  OD1 ASP B 504     6505   6922   6091   1151   -546    185       O  
ATOM   3904  OD2 ASP B 504      27.134  82.725 -15.966  1.00 52.70           O  
ANISOU 3904  OD2 ASP B 504     6879   6936   6209   1222   -607    140       O  
ATOM   3905  N   LEU B 505      29.393  86.926 -13.452  1.00 45.99           N  
ANISOU 3905  N   LEU B 505     5307   6412   5754   1067   -669    353       N  
ATOM   3906  CA  LEU B 505      28.899  87.403 -12.181  1.00 45.10           C  
ANISOU 3906  CA  LEU B 505     5194   6281   5659    962   -775    341       C  
ATOM   3907  C   LEU B 505      27.456  87.884 -12.358  1.00 44.48           C  
ANISOU 3907  C   LEU B 505     5198   6183   5518    866   -778    292       C  
ATOM   3908  O   LEU B 505      27.136  88.632 -13.299  1.00 43.64           O  
ANISOU 3908  O   LEU B 505     5069   6107   5404    844   -730    294       O  
ATOM   3909  CB  LEU B 505      29.800  88.496 -11.636  1.00 46.73           C  
ANISOU 3909  CB  LEU B 505     5246   6540   5966    917   -827    399       C  
ATOM   3910  CG  LEU B 505      29.601  88.853 -10.171  1.00 47.24           C  
ANISOU 3910  CG  LEU B 505     5338   6574   6035    839   -951    387       C  
ATOM   3911  CD1 LEU B 505      30.045  87.738  -9.236  1.00 48.23           C  
ANISOU 3911  CD1 LEU B 505     5506   6665   6150    900  -1016    394       C  
ATOM   3912  CD2 LEU B 505      30.342  90.129  -9.858  1.00 48.41           C  
ANISOU 3912  CD2 LEU B 505     5366   6755   6271    766  -1017    434       C  
ATOM   3913  N   LYS B 506      26.592  87.367 -11.493  1.00 42.31           N  
ANISOU 3913  N   LYS B 506     5017   5861   5197    821   -829    260       N  
ATOM   3914  CA  LYS B 506      25.184  87.730 -11.432  1.00 42.22           C  
ANISOU 3914  CA  LYS B 506     5055   5845   5139    737   -834    230       C  
ATOM   3915  C   LYS B 506      24.569  87.216 -10.114  1.00 41.83           C  
ANISOU 3915  C   LYS B 506     5076   5759   5057    694   -881    224       C  
ATOM   3916  O   LYS B 506      25.142  86.327  -9.463  1.00 40.27           O  
ANISOU 3916  O   LYS B 506     4926   5521   4854    732   -913    234       O  
ATOM   3917  CB  LYS B 506      24.421  87.153 -12.620  1.00 43.43           C  
ANISOU 3917  CB  LYS B 506     5280   5983   5239    734   -798    205       C  
ATOM   3918  CG  LYS B 506      24.589  85.658 -12.820  1.00 45.70           C  
ANISOU 3918  CG  LYS B 506     5684   6199   5479    782   -801    188       C  
ATOM   3919  CD  LYS B 506      23.936  85.264 -14.119  1.00 47.99           C  
ANISOU 3919  CD  LYS B 506     6063   6464   5704    773   -785    157       C  
ATOM   3920  CE  LYS B 506      23.948  83.773 -14.349  1.00 51.13           C  
ANISOU 3920  CE  LYS B 506     6625   6760   6041    808   -804    129       C  
ATOM   3921  NZ  LYS B 506      23.112  83.498 -15.540  1.00 54.89           N  
ANISOU 3921  NZ  LYS B 506     7209   7203   6443    766   -823     94       N  
ATOM   3922  N   LEU B 507      23.410  87.769  -9.739  1.00 40.97           N  
ANISOU 3922  N   LEU B 507     4974   5667   4923    628   -875    216       N  
ATOM   3923  CA  LEU B 507      22.764  87.457  -8.457  1.00 42.19           C  
ANISOU 3923  CA  LEU B 507     5189   5802   5036    592   -891    223       C  
ATOM   3924  C   LEU B 507      22.523  85.964  -8.301  1.00 42.29           C  
ANISOU 3924  C   LEU B 507     5295   5759   5013    578   -900    232       C  
ATOM   3925  O   LEU B 507      22.723  85.407  -7.211  1.00 42.28           O  
ANISOU 3925  O   LEU B 507     5360   5720   4981    581   -926    250       O  
ATOM   3926  CB  LEU B 507      21.418  88.173  -8.320  1.00 42.79           C  
ANISOU 3926  CB  LEU B 507     5242   5920   5093    544   -851    225       C  
ATOM   3927  CG  LEU B 507      21.484  89.680  -8.145  1.00 44.35           C  
ANISOU 3927  CG  LEU B 507     5395   6147   5309    564   -846    215       C  
ATOM   3928  CD1 LEU B 507      20.085  90.270  -8.301  1.00 47.37           C  
ANISOU 3928  CD1 LEU B 507     5743   6576   5679    548   -792    224       C  
ATOM   3929  CD2 LEU B 507      22.088  90.037  -6.806  1.00 45.08           C  
ANISOU 3929  CD2 LEU B 507     5544   6209   5372    582   -887    210       C  
ATOM   3930  N   ASP B 508      22.161  85.330  -9.408  1.00 42.45           N  
ANISOU 3930  N   ASP B 508     5340   5760   5029    563   -888    220       N  
ATOM   3931  CA  ASP B 508      21.795  83.922  -9.437  1.00 44.67           C  
ANISOU 3931  CA  ASP B 508     5736   5962   5272    530   -909    225       C  
ATOM   3932  C   ASP B 508      22.979  83.023  -9.092  1.00 43.62           C  
ANISOU 3932  C   ASP B 508     5681   5757   5132    619   -936    227       C  
ATOM   3933  O   ASP B 508      22.778  81.896  -8.673  1.00 45.76           O  
ANISOU 3933  O   ASP B 508     6072   5946   5369    597   -961    241       O  
ATOM   3934  CB  ASP B 508      21.253  83.505 -10.813  1.00 48.02           C  
ANISOU 3934  CB  ASP B 508     6199   6364   5680    498   -915    202       C  
ATOM   3935  CG  ASP B 508      20.263  84.504 -11.394  1.00 50.06           C  
ANISOU 3935  CG  ASP B 508     6359   6705   5956    438   -902    205       C  
ATOM   3936  OD1 ASP B 508      19.094  84.117 -11.567  1.00 52.38           O  
ANISOU 3936  OD1 ASP B 508     6661   6997   6241    337   -929    224       O  
ATOM   3937  OD2 ASP B 508      20.658  85.672 -11.661  1.00 51.91           O  
ANISOU 3937  OD2 ASP B 508     6502   7002   6217    488   -873    198       O  
ATOM   3938  N   ASN B 509      24.201  83.510  -9.280  1.00 42.30           N  
ANISOU 3938  N   ASN B 509     5444   5622   5006    717   -931    223       N  
ATOM   3939  CA  ASN B 509      25.382  82.692  -9.045  1.00 42.88           C  
ANISOU 3939  CA  ASN B 509     5559   5644   5088    826   -955    237       C  
ATOM   3940  C   ASN B 509      25.996  82.926  -7.679  1.00 43.83           C  
ANISOU 3940  C   ASN B 509     5651   5777   5225    842  -1012    271       C  
ATOM   3941  O   ASN B 509      27.045  82.339  -7.368  1.00 44.57           O  
ANISOU 3941  O   ASN B 509     5754   5842   5339    941  -1049    295       O  
ATOM   3942  CB  ASN B 509      26.426  82.951 -10.124  1.00 43.41           C  
ANISOU 3942  CB  ASN B 509     5548   5749   5198    935   -909    232       C  
ATOM   3943  CG  ASN B 509      26.074  82.301 -11.427  1.00 43.81           C  
ANISOU 3943  CG  ASN B 509     5699   5750   5197    963   -863    195       C  
ATOM   3944  OD1 ASN B 509      25.006  81.720 -11.575  1.00 46.07           O  
ANISOU 3944  OD1 ASN B 509     6104   5973   5427    877   -887    171       O  
ATOM   3945  ND2 ASN B 509      26.958  82.414 -12.393  1.00 44.98           N  
ANISOU 3945  ND2 ASN B 509     5804   5926   5357   1077   -799    196       N  
ATOM   3946  N   ILE B 510      25.348  83.770  -6.865  1.00 43.31           N  
ANISOU 3946  N   ILE B 510     5561   5751   5143    759  -1024    274       N  
ATOM   3947  CA  ILE B 510      25.785  84.030  -5.494  1.00 44.91           C  
ANISOU 3947  CA  ILE B 510     5781   5953   5328    763  -1092    298       C  
ATOM   3948  C   ILE B 510      24.859  83.270  -4.531  1.00 45.06           C  
ANISOU 3948  C   ILE B 510     5940   5918   5262    707  -1088    318       C  
ATOM   3949  O   ILE B 510      23.732  83.696  -4.250  1.00 43.28           O  
ANISOU 3949  O   ILE B 510     5725   5720   4997    629  -1038    317       O  
ATOM   3950  CB  ILE B 510      25.764  85.534  -5.120  1.00 44.77           C  
ANISOU 3950  CB  ILE B 510     5685   5998   5326    723  -1107    286       C  
ATOM   3951  CG1 ILE B 510      26.391  86.424  -6.197  1.00 43.94           C  
ANISOU 3951  CG1 ILE B 510     5441   5947   5305    741  -1090    278       C  
ATOM   3952  CG2 ILE B 510      26.494  85.750  -3.799  1.00 45.41           C  
ANISOU 3952  CG2 ILE B 510     5806   6064   5383    739  -1209    306       C  
ATOM   3953  CD1 ILE B 510      27.824  86.087  -6.531  1.00 45.57           C  
ANISOU 3953  CD1 ILE B 510     5562   6164   5585    824  -1127    312       C  
ATOM   3954  N   LEU B 511      25.339  82.133  -4.057  1.00 44.22           N  
ANISOU 3954  N   LEU B 511     5935   5736   5130    754  -1134    347       N  
ATOM   3955  CA  LEU B 511      24.626  81.339  -3.059  1.00 45.35           C  
ANISOU 3955  CA  LEU B 511     6224   5817   5188    701  -1134    384       C  
ATOM   3956  C   LEU B 511      24.908  81.881  -1.654  1.00 43.84           C  
ANISOU 3956  C   LEU B 511     6075   5643   4936    710  -1188    406       C  
ATOM   3957  O   LEU B 511      25.897  82.559  -1.441  1.00 44.75           O  
ANISOU 3957  O   LEU B 511     6124   5792   5085    765  -1264    396       O  
ATOM   3958  CB  LEU B 511      25.069  79.879  -3.163  1.00 47.13           C  
ANISOU 3958  CB  LEU B 511     6573   5931   5402    758  -1170    409       C  
ATOM   3959  CG  LEU B 511      24.415  78.981  -4.224  1.00 50.27           C  
ANISOU 3959  CG  LEU B 511     7038   6257   5805    716  -1128    394       C  
ATOM   3960  CD1 LEU B 511      24.153  79.669  -5.551  1.00 51.31           C  
ANISOU 3960  CD1 LEU B 511     7052   6454   5988    699  -1078    341       C  
ATOM   3961  CD2 LEU B 511      25.227  77.704  -4.417  1.00 51.74           C  
ANISOU 3961  CD2 LEU B 511     7353   6319   5985    824  -1174    403       C  
ATOM   3962  N   LEU B 512      24.044  81.577  -0.693  1.00 44.49           N  
ANISOU 3962  N   LEU B 512     6276   5704   4924    650  -1153    443       N  
ATOM   3963  CA  LEU B 512      24.350  81.816   0.725  1.00 45.43           C  
ANISOU 3963  CA  LEU B 512     6500   5813   4947    674  -1211    469       C  
ATOM   3964  C   LEU B 512      24.519  80.494   1.447  1.00 45.73           C  
ANISOU 3964  C   LEU B 512     6702   5755   4918    691  -1252    532       C  
ATOM   3965  O   LEU B 512      23.775  79.547   1.194  1.00 45.64           O  
ANISOU 3965  O   LEU B 512     6755   5689   4896    633  -1189    567       O  
ATOM   3966  CB  LEU B 512      23.232  82.642   1.392  1.00 46.06           C  
ANISOU 3966  CB  LEU B 512     6610   5948   4942    616  -1116    469       C  
ATOM   3967  CG  LEU B 512      23.037  84.090   0.895  1.00 44.82           C  
ANISOU 3967  CG  LEU B 512     6328   5871   4830    614  -1083    409       C  
ATOM   3968  CD1 LEU B 512      21.974  84.815   1.709  1.00 45.20           C  
ANISOU 3968  CD1 LEU B 512     6438   5960   4775    597   -981    415       C  
ATOM   3969  CD2 LEU B 512      24.337  84.864   0.951  1.00 44.92           C  
ANISOU 3969  CD2 LEU B 512     6299   5884   4884    668  -1215    370       C  
ATOM   3970  N   ASP B 513      25.500  80.414   2.341  1.00 46.50           N  
ANISOU 3970  N   ASP B 513     6874   5823   4970    765  -1373    553       N  
ATOM   3971  CA  ASP B 513      25.555  79.287   3.282  1.00 47.63           C  
ANISOU 3971  CA  ASP B 513     7208   5872   5015    783  -1414    624       C  
ATOM   3972  C   ASP B 513      24.502  79.509   4.371  1.00 47.89           C  
ANISOU 3972  C   ASP B 513     7375   5917   4902    710  -1328    661       C  
ATOM   3973  O   ASP B 513      23.867  80.561   4.408  1.00 45.77           O  
ANISOU 3973  O   ASP B 513     7046   5729   4613    671  -1249    624       O  
ATOM   3974  CB  ASP B 513      26.976  79.066   3.845  1.00 48.89           C  
ANISOU 3974  CB  ASP B 513     7400   5998   5178    897  -1588    646       C  
ATOM   3975  CG  ASP B 513      27.442  80.160   4.814  1.00 50.08           C  
ANISOU 3975  CG  ASP B 513     7566   6200   5259    906  -1692    629       C  
ATOM   3976  OD1 ASP B 513      26.620  80.863   5.445  1.00 49.50           O  
ANISOU 3976  OD1 ASP B 513     7571   6156   5078    844  -1624    613       O  
ATOM   3977  OD2 ASP B 513      28.672  80.277   4.981  1.00 51.35           O  
ANISOU 3977  OD2 ASP B 513     7670   6367   5472    982  -1853    638       O  
ATOM   3978  N   LYS B 514      24.331  78.522   5.254  1.00 49.53           N  
ANISOU 3978  N   LYS B 514     7773   6043   5003    703  -1335    740       N  
ATOM   3979  CA  LYS B 514      23.323  78.598   6.326  1.00 49.92           C  
ANISOU 3979  CA  LYS B 514     7963   6105   4898    641  -1227    798       C  
ATOM   3980  C   LYS B 514      23.496  79.775   7.321  1.00 49.73           C  
ANISOU 3980  C   LYS B 514     8005   6139   4751    688  -1256    763       C  
ATOM   3981  O   LYS B 514      22.547  80.145   8.023  1.00 51.23           O  
ANISOU 3981  O   LYS B 514     8278   6368   4816    656  -1123    790       O  
ATOM   3982  CB  LYS B 514      23.265  77.278   7.095  1.00 51.10           C  
ANISOU 3982  CB  LYS B 514     8324   6142   4950    630  -1242    902       C  
ATOM   3983  CG  LYS B 514      24.549  76.854   7.804  1.00 51.79           C  
ANISOU 3983  CG  LYS B 514     8543   6152   4982    745  -1431    922       C  
ATOM   3984  CD  LYS B 514      24.243  75.693   8.746  1.00 53.97           C  
ANISOU 3984  CD  LYS B 514     9064   6318   5122    723  -1417   1038       C  
ATOM   3985  CE  LYS B 514      25.483  74.961   9.261  1.00 54.66           C  
ANISOU 3985  CE  LYS B 514     9284   6305   5178    845  -1614   1077       C  
ATOM   3986  NZ  LYS B 514      26.280  75.783  10.198  1.00 54.88           N  
ANISOU 3986  NZ  LYS B 514     9365   6379   5107    927  -1758   1053       N  
ATOM   3987  N   ASP B 515      24.684  80.360   7.384  1.00 48.70           N  
ANISOU 3987  N   ASP B 515     7841   6011   4650    763  -1426    707       N  
ATOM   3988  CA  ASP B 515      24.907  81.508   8.259  1.00 49.57           C  
ANISOU 3988  CA  ASP B 515     8036   6152   4644    793  -1488    663       C  
ATOM   3989  C   ASP B 515      24.622  82.817   7.569  1.00 48.60           C  
ANISOU 3989  C   ASP B 515     7757   6108   4600    773  -1432    576       C  
ATOM   3990  O   ASP B 515      24.397  83.819   8.234  1.00 48.25           O  
ANISOU 3990  O   ASP B 515     7808   6081   4443    788  -1424    535       O  
ATOM   3991  CB  ASP B 515      26.340  81.528   8.779  1.00 50.32           C  
ANISOU 3991  CB  ASP B 515     8183   6206   4731    862  -1734    659       C  
ATOM   3992  CG  ASP B 515      26.649  80.352   9.665  1.00 52.48           C  
ANISOU 3992  CG  ASP B 515     8652   6394   4893    902  -1811    749       C  
ATOM   3993  OD1 ASP B 515      25.778  79.947  10.437  1.00 53.40           O  
ANISOU 3993  OD1 ASP B 515     8955   6483   4850    877  -1693    805       O  
ATOM   3994  OD2 ASP B 515      27.769  79.829   9.609  1.00 52.34           O  
ANISOU 3994  OD2 ASP B 515     8601   6339   4946    966  -1987    775       O  
ATOM   3995  N   GLY B 516      24.648  82.819   6.237  1.00 47.37           N  
ANISOU 3995  N   GLY B 516     7385   5988   4624    748  -1397    548       N  
ATOM   3996  CA  GLY B 516      24.458  84.036   5.495  1.00 47.09           C  
ANISOU 3996  CA  GLY B 516     7202   6018   4672    732  -1356    475       C  
ATOM   3997  C   GLY B 516      25.704  84.589   4.848  1.00 46.30           C  
ANISOU 3997  C   GLY B 516     6958   5928   4706    754  -1510    431       C  
ATOM   3998  O   GLY B 516      25.651  85.697   4.307  1.00 47.08           O  
ANISOU 3998  O   GLY B 516     6954   6067   4864    735  -1495    376       O  
ATOM   3999  N   HIS B 517      26.800  83.834   4.864  1.00 46.60           N  
ANISOU 3999  N   HIS B 517     6976   5931   4797    796  -1649    467       N  
ATOM   4000  CA  HIS B 517      28.002  84.213   4.111  1.00 47.57           C  
ANISOU 4000  CA  HIS B 517     6913   6083   5077    819  -1769    452       C  
ATOM   4001  C   HIS B 517      27.863  83.772   2.668  1.00 47.92           C  
ANISOU 4001  C   HIS B 517     6786   6156   5262    825  -1659    448       C  
ATOM   4002  O   HIS B 517      27.214  82.761   2.385  1.00 48.43           O  
ANISOU 4002  O   HIS B 517     6902   6188   5310    825  -1560    472       O  
ATOM   4003  CB  HIS B 517      29.266  83.591   4.695  1.00 49.40           C  
ANISOU 4003  CB  HIS B 517     7166   6282   5322    884  -1960    506       C  
ATOM   4004  CG  HIS B 517      29.616  84.103   6.058  1.00 49.49           C  
ANISOU 4004  CG  HIS B 517     7346   6262   5196    876  -2120    507       C  
ATOM   4005  ND1 HIS B 517      30.160  85.353   6.264  1.00 50.07           N  
ANISOU 4005  ND1 HIS B 517     7383   6354   5287    832  -2250    466       N  
ATOM   4006  CD2 HIS B 517      29.493  83.539   7.286  1.00 50.80           C  
ANISOU 4006  CD2 HIS B 517     7743   6367   5192    901  -2179    545       C  
ATOM   4007  CE1 HIS B 517      30.361  85.535   7.560  1.00 51.25           C  
ANISOU 4007  CE1 HIS B 517     7742   6451   5276    832  -2394    469       C  
ATOM   4008  NE2 HIS B 517      29.959  84.452   8.201  1.00 50.80           N  
ANISOU 4008  NE2 HIS B 517     7850   6351   5097    880  -2347    518       N  
ATOM   4009  N   ILE B 518      28.481  84.512   1.751  1.00 46.93           N  
ANISOU 4009  N   ILE B 518     6475   6085   5269    824  -1682    423       N  
ATOM   4010  CA  ILE B 518      28.325  84.206   0.336  1.00 46.77           C  
ANISOU 4010  CA  ILE B 518     6317   6094   5358    837  -1569    413       C  
ATOM   4011  C   ILE B 518      29.210  83.058  -0.172  1.00 47.22           C  
ANISOU 4011  C   ILE B 518     6323   6128   5491    933  -1599    456       C  
ATOM   4012  O   ILE B 518      30.263  82.718   0.417  1.00 47.43           O  
ANISOU 4012  O   ILE B 518     6342   6142   5536   1002  -1731    501       O  
ATOM   4013  CB  ILE B 518      28.538  85.444  -0.559  1.00 47.69           C  
ANISOU 4013  CB  ILE B 518     6268   6277   5573    802  -1549    378       C  
ATOM   4014  CG1 ILE B 518      30.009  85.780  -0.672  1.00 48.30           C  
ANISOU 4014  CG1 ILE B 518     6200   6389   5763    836  -1679    413       C  
ATOM   4015  CG2 ILE B 518      27.755  86.637  -0.023  1.00 48.20           C  
ANISOU 4015  CG2 ILE B 518     6404   6348   5562    732  -1531    334       C  
ATOM   4016  CD1 ILE B 518      30.418  86.074  -2.083  1.00 49.22           C  
ANISOU 4016  CD1 ILE B 518     6126   6565   6010    853  -1604    418       C  
ATOM   4017  N   LYS B 519      28.726  82.434  -1.241  1.00 46.02           N  
ANISOU 4017  N   LYS B 519     6152   5962   5371    947  -1481    441       N  
ATOM   4018  CA  LYS B 519      29.471  81.426  -1.977  1.00 46.56           C  
ANISOU 4018  CA  LYS B 519     6185   6000   5504   1059  -1475    465       C  
ATOM   4019  C   LYS B 519      29.206  81.610  -3.466  1.00 46.71           C  
ANISOU 4019  C   LYS B 519     6108   6052   5584   1060  -1357    426       C  
ATOM   4020  O   LYS B 519      28.103  81.324  -3.966  1.00 45.41           O  
ANISOU 4020  O   LYS B 519     6024   5855   5375    995  -1270    393       O  
ATOM   4021  CB  LYS B 519      29.053  80.019  -1.552  1.00 47.93           C  
ANISOU 4021  CB  LYS B 519     6552   6060   5596   1087  -1470    490       C  
ATOM   4022  CG  LYS B 519      29.432  79.632  -0.129  1.00 48.58           C  
ANISOU 4022  CG  LYS B 519     6755   6097   5605   1112  -1590    543       C  
ATOM   4023  CD  LYS B 519      30.883  79.231  -0.051  1.00 49.31           C  
ANISOU 4023  CD  LYS B 519     6769   6192   5774   1259  -1702    592       C  
ATOM   4024  CE  LYS B 519      31.223  78.621   1.310  1.00 50.31           C  
ANISOU 4024  CE  LYS B 519     7048   6254   5814   1299  -1835    653       C  
ATOM   4025  NZ  LYS B 519      32.548  77.991   1.188  1.00 50.15           N  
ANISOU 4025  NZ  LYS B 519     6942   6228   5882   1468  -1928    710       N  
ATOM   4026  N   ILE B 520      30.223  82.094  -4.167  1.00 47.25           N  
ANISOU 4026  N   ILE B 520     6004   6190   5756   1128  -1359    440       N  
ATOM   4027  CA  ILE B 520      30.184  82.198  -5.621  1.00 46.99           C  
ANISOU 4027  CA  ILE B 520     5893   6190   5770   1159  -1245    414       C  
ATOM   4028  C   ILE B 520      30.229  80.797  -6.237  1.00 47.15           C  
ANISOU 4028  C   ILE B 520     6032   6123   5759   1270  -1191    408       C  
ATOM   4029  O   ILE B 520      31.139  79.994  -5.918  1.00 46.01           O  
ANISOU 4029  O   ILE B 520     5900   5944   5637   1403  -1236    451       O  
ATOM   4030  CB  ILE B 520      31.368  83.031  -6.142  1.00 48.56           C  
ANISOU 4030  CB  ILE B 520     5873   6491   6087   1209  -1248    453       C  
ATOM   4031  CG1 ILE B 520      31.324  84.441  -5.541  1.00 48.73           C  
ANISOU 4031  CG1 ILE B 520     5811   6569   6133   1083  -1322    454       C  
ATOM   4032  CG2 ILE B 520      31.344  83.070  -7.659  1.00 48.89           C  
ANISOU 4032  CG2 ILE B 520     5860   6563   6152   1257  -1112    434       C  
ATOM   4033  CD1 ILE B 520      32.542  85.290  -5.839  1.00 50.08           C  
ANISOU 4033  CD1 ILE B 520     5763   6831   6433   1095  -1361    514       C  
ATOM   4034  N   ALA B 521      29.245  80.522  -7.099  1.00 44.63           N  
ANISOU 4034  N   ALA B 521     5809   5760   5387   1220  -1109    357       N  
ATOM   4035  CA  ALA B 521      29.081  79.250  -7.773  1.00 46.44           C  
ANISOU 4035  CA  ALA B 521     6200   5878   5566   1296  -1068    335       C  
ATOM   4036  C   ALA B 521      29.171  79.350  -9.310  1.00 47.41           C  
ANISOU 4036  C   ALA B 521     6300   6022   5692   1357   -967    296       C  
ATOM   4037  O   ALA B 521      29.049  80.429  -9.898  1.00 47.91           O  
ANISOU 4037  O   ALA B 521     6233   6183   5787   1303   -922    286       O  
ATOM   4038  CB  ALA B 521      27.750  78.628  -7.375  1.00 46.86           C  
ANISOU 4038  CB  ALA B 521     6436   5834   5534   1161  -1089    315       C  
ATOM   4039  N   ASP B 522      29.333  78.187  -9.938  1.00 48.78           N  
ANISOU 4039  N   ASP B 522     6636   6085   5814   1472   -935    273       N  
ATOM   4040  CA  ASP B 522      29.434  78.030 -11.391  1.00 49.83           C  
ANISOU 4040  CA  ASP B 522     6819   6205   5909   1560   -839    230       C  
ATOM   4041  C   ASP B 522      30.634  78.722 -12.045  1.00 50.79           C  
ANISOU 4041  C   ASP B 522     6738   6454   6103   1703   -745    267       C  
ATOM   4042  O   ASP B 522      30.520  79.856 -12.525  1.00 49.81           O  
ANISOU 4042  O   ASP B 522     6470   6441   6014   1628   -704    271       O  
ATOM   4043  CB  ASP B 522      28.148  78.500 -12.101  1.00 48.96           C  
ANISOU 4043  CB  ASP B 522     6761   6097   5745   1392   -831    176       C  
ATOM   4044  CG  ASP B 522      28.099  78.050 -13.547  1.00 49.73           C  
ANISOU 4044  CG  ASP B 522     7000   6133   5759   1475   -762    120       C  
ATOM   4045  OD1 ASP B 522      29.099  77.481 -14.041  1.00 50.70           O  
ANISOU 4045  OD1 ASP B 522     7170   6225   5866   1678   -691    122       O  
ATOM   4046  OD2 ASP B 522      27.064  78.263 -14.191  1.00 51.48           O  
ANISOU 4046  OD2 ASP B 522     7291   6340   5926   1347   -779     78       O  
ATOM   4047  N   PHE B 523      31.755  78.016 -12.128  1.00 52.49           N  
ANISOU 4047  N   PHE B 523     6948   6651   6341   1915   -704    303       N  
ATOM   4048  CA  PHE B 523      32.963  78.571 -12.734  1.00 53.83           C  
ANISOU 4048  CA  PHE B 523     6902   6955   6594   2064   -598    363       C  
ATOM   4049  C   PHE B 523      33.168  78.141 -14.178  1.00 54.65           C  
ANISOU 4049  C   PHE B 523     7119   7030   6615   2225   -446    327       C  
ATOM   4050  O   PHE B 523      34.242  78.342 -14.726  1.00 56.16           O  
ANISOU 4050  O   PHE B 523     7155   7322   6861   2394   -326    388       O  
ATOM   4051  CB  PHE B 523      34.158  78.242 -11.843  1.00 55.87           C  
ANISOU 4051  CB  PHE B 523     7019   7253   6953   2204   -645    451       C  
ATOM   4052  CG  PHE B 523      33.975  78.756 -10.454  1.00 55.02           C  
ANISOU 4052  CG  PHE B 523     6826   7175   6904   2044   -802    483       C  
ATOM   4053  CD1 PHE B 523      33.363  77.975  -9.494  1.00 54.94           C  
ANISOU 4053  CD1 PHE B 523     7007   7038   6829   1989   -911    459       C  
ATOM   4054  CD2 PHE B 523      34.320  80.059 -10.137  1.00 55.41           C  
ANISOU 4054  CD2 PHE B 523     6633   7366   7055   1931   -840    533       C  
ATOM   4055  CE1 PHE B 523      33.153  78.463  -8.214  1.00 54.44           C  
ANISOU 4055  CE1 PHE B 523     6894   6999   6789   1850  -1043    486       C  
ATOM   4056  CE2 PHE B 523      34.107  80.560  -8.863  1.00 53.80           C  
ANISOU 4056  CE2 PHE B 523     6393   7171   6875   1787   -990    549       C  
ATOM   4057  CZ  PHE B 523      33.520  79.758  -7.901  1.00 53.79           C  
ANISOU 4057  CZ  PHE B 523     6587   7053   6795   1755  -1084    524       C  
ATOM   4058  N   GLY B 524      32.117  77.608 -14.800  1.00 54.53           N  
ANISOU 4058  N   GLY B 524     7368   6883   6465   2163   -452    234       N  
ATOM   4059  CA  GLY B 524      32.176  77.126 -16.175  1.00 58.61           C  
ANISOU 4059  CA  GLY B 524     8065   7340   6863   2307   -330    180       C  
ATOM   4060  C   GLY B 524      32.562  78.142 -17.246  1.00 60.48           C  
ANISOU 4060  C   GLY B 524     8151   7723   7106   2343   -190    208       C  
ATOM   4061  O   GLY B 524      33.029  77.753 -18.321  1.00 63.97           O  
ANISOU 4061  O   GLY B 524     8701   8145   7457   2533    -49    192       O  
ATOM   4062  N   MET B 525      32.379  79.431 -16.961  1.00 58.12           N  
ANISOU 4062  N   MET B 525     7621   7560   6901   2170   -220    253       N  
ATOM   4063  CA  MET B 525      32.676  80.477 -17.920  1.00 59.09           C  
ANISOU 4063  CA  MET B 525     7604   7813   7034   2172    -99    292       C  
ATOM   4064  C   MET B 525      34.002  81.177 -17.655  1.00 58.67           C  
ANISOU 4064  C   MET B 525     7229   7924   7137   2251    -21    418       C  
ATOM   4065  O   MET B 525      34.389  82.061 -18.412  1.00 55.62           O  
ANISOU 4065  O   MET B 525     6703   7653   6775   2253     91    475       O  
ATOM   4066  CB  MET B 525      31.546  81.508 -17.930  1.00 60.76           C  
ANISOU 4066  CB  MET B 525     7794   8051   7240   1927   -183    263       C  
ATOM   4067  CG  MET B 525      31.532  82.333 -19.203  1.00 65.02           C  
ANISOU 4067  CG  MET B 525     8313   8667   7724   1933    -66    277       C  
ATOM   4068  SD  MET B 525      29.976  82.169 -20.073  1.00 73.72           S  
ANISOU 4068  SD  MET B 525     9696   9658   8654   1811   -136    167       S  
ATOM   4069  CE  MET B 525      28.956  83.266 -19.114  1.00 66.21           C  
ANISOU 4069  CE  MET B 525     8595   8757   7805   1550   -285    178       C  
ATOM   4070  N   CYS B 526      34.710  80.781 -16.602  1.00 56.91           N  
ANISOU 4070  N   CYS B 526     6887   7713   7021   2311    -88    471       N  
ATOM   4071  CA  CYS B 526      35.999  81.386 -16.305  1.00 58.64           C  
ANISOU 4071  CA  CYS B 526     6782   8091   7405   2375    -44    603       C  
ATOM   4072  C   CYS B 526      36.994  81.233 -17.451  1.00 60.56           C  
ANISOU 4072  C   CYS B 526     6945   8421   7641   2607    179    672       C  
ATOM   4073  O   CYS B 526      36.841  80.367 -18.309  1.00 61.83           O  
ANISOU 4073  O   CYS B 526     7343   8492   7655   2778    292    607       O  
ATOM   4074  CB  CYS B 526      36.641  80.747 -15.070  1.00 59.75           C  
ANISOU 4074  CB  CYS B 526     6842   8216   7641   2445   -161    650       C  
ATOM   4075  SG  CYS B 526      35.865  81.129 -13.496  1.00 57.73           S  
ANISOU 4075  SG  CYS B 526     6599   7909   7424   2192   -408    618       S  
ATOM   4076  N   LYS B 527      38.012  82.084 -17.433  1.00 61.22           N  
ANISOU 4076  N   LYS B 527     6701   8678   7882   2608    238    809       N  
ATOM   4077  CA  LYS B 527      39.158  81.989 -18.332  1.00 64.61           C  
ANISOU 4077  CA  LYS B 527     6971   9230   8345   2837    465    918       C  
ATOM   4078  C   LYS B 527      40.414  81.959 -17.478  1.00 66.95           C  
ANISOU 4078  C   LYS B 527     6940   9650   8848   2917    422   1062       C  
ATOM   4079  O   LYS B 527      40.499  82.691 -16.493  1.00 64.96           O  
ANISOU 4079  O   LYS B 527     6501   9445   8733   2714    240   1110       O  
ATOM   4080  CB  LYS B 527      39.201  83.196 -19.255  1.00 64.94           C  
ANISOU 4080  CB  LYS B 527     6887   9388   8397   2730    590    982       C  
ATOM   4081  CG  LYS B 527      40.235  83.089 -20.360  1.00 66.68           C  
ANISOU 4081  CG  LYS B 527     6987   9734   8615   2971    867   1094       C  
ATOM   4082  CD  LYS B 527      39.881  81.995 -21.345  1.00 67.72           C  
ANISOU 4082  CD  LYS B 527     7471   9743   8515   3209   1018    983       C  
ATOM   4083  CE  LYS B 527      40.871  81.943 -22.500  1.00 70.02           C  
ANISOU 4083  CE  LYS B 527     7667  10163   8773   3467   1326   1093       C  
ATOM   4084  NZ  LYS B 527      40.326  81.129 -23.614  1.00 70.17           N  
ANISOU 4084  NZ  LYS B 527     8096  10044   8520   3653   1462    964       N  
ATOM   4085  N   GLU B 528      41.408  81.173 -17.897  1.00 72.55           N  
ANISOU 4085  N   GLU B 528     7573  10415   9577   3216    589   1137       N  
ATOM   4086  CA  GLU B 528      42.403  80.640 -16.974  1.00 76.20           C  
ANISOU 4086  CA  GLU B 528     7822  10935  10196   3352    511   1238       C  
ATOM   4087  C   GLU B 528      43.841  81.135 -16.965  1.00 81.66           C  
ANISOU 4087  C   GLU B 528     8060  11856  11109   3439    597   1451       C  
ATOM   4088  O   GLU B 528      44.642  80.618 -16.177  1.00 84.21           O  
ANISOU 4088  O   GLU B 528     8208  12224  11561   3564    510   1538       O  
ATOM   4089  CB  GLU B 528      42.474  79.129 -17.181  1.00 78.60           C  
ANISOU 4089  CB  GLU B 528     8388  11104  10371   3665    594   1169       C  
ATOM   4090  CG  GLU B 528      41.627  78.360 -16.202  1.00 76.70           C  
ANISOU 4090  CG  GLU B 528     8427  10662  10051   3587    371   1042       C  
ATOM   4091  CD  GLU B 528      41.715  76.891 -16.480  1.00 79.46           C  
ANISOU 4091  CD  GLU B 528     9061  10857  10271   3891    454    978       C  
ATOM   4092  OE1 GLU B 528      41.214  76.474 -17.544  1.00 79.63           O  
ANISOU 4092  OE1 GLU B 528     9371  10774  10107   3989    600    878       O  
ATOM   4093  OE2 GLU B 528      42.305  76.163 -15.655  1.00 82.29           O  
ANISOU 4093  OE2 GLU B 528     9367  11190  10706   4039    366   1030       O  
ATOM   4094  N   ASN B 529      44.231  82.087 -17.792  1.00 83.05           N  
ANISOU 4094  N   ASN B 529     8028  12183  11343   3379    758   1555       N  
ATOM   4095  CA  ASN B 529      45.656  82.431 -17.777  1.00 87.21           C  
ANISOU 4095  CA  ASN B 529     8100  12937  12099   3472    847   1781       C  
ATOM   4096  C   ASN B 529      45.902  83.919 -17.851  1.00 88.16           C  
ANISOU 4096  C   ASN B 529     7929  13198  12369   3183    815   1904       C  
ATOM   4097  O   ASN B 529      46.802  84.386 -18.542  1.00 90.57           O  
ANISOU 4097  O   ASN B 529     7937  13687  12787   3245   1013   2080       O  
ATOM   4098  CB  ASN B 529      46.401  81.655 -18.865  1.00 89.81           C  
ANISOU 4098  CB  ASN B 529     8409  13343  12369   3855   1178   1850       C  
ATOM   4099  CG  ASN B 529      46.614  80.198 -18.488  1.00 91.84           C  
ANISOU 4099  CG  ASN B 529     8831  13494  12568   4169   1171   1794       C  
ATOM   4100  OD1 ASN B 529      45.969  79.304 -19.031  1.00 93.00           O  
ANISOU 4100  OD1 ASN B 529     9380  13467  12488   4339   1263   1639       O  
ATOM   4101  ND2 ASN B 529      47.500  79.957 -17.530  1.00 92.42           N  
ANISOU 4101  ND2 ASN B 529     8611  13660  12843   4236   1037   1920       N  
ATOM   4102  N   MET B 530      45.119  84.650 -17.070  1.00 85.24           N  
ANISOU 4102  N   MET B 530     7646  12736  12005   2867    560   1820       N  
ATOM   4103  CA  MET B 530      45.129  86.095 -17.114  1.00 85.25           C  
ANISOU 4103  CA  MET B 530     7465  12812  12113   2567    499   1900       C  
ATOM   4104  C   MET B 530      46.066  86.661 -16.065  1.00 85.48           C  
ANISOU 4104  C   MET B 530     7124  12956  12398   2413    284   2056       C  
ATOM   4105  O   MET B 530      45.641  87.364 -15.153  1.00 85.07           O  
ANISOU 4105  O   MET B 530     7106  12831  12385   2144     22   2009       O  
ATOM   4106  CB  MET B 530      43.717  86.618 -16.895  1.00 81.72           C  
ANISOU 4106  CB  MET B 530     7341  12192  11516   2328    350   1719       C  
ATOM   4107  CG  MET B 530      42.725  86.061 -17.892  1.00 82.45           C  
ANISOU 4107  CG  MET B 530     7801  12166  11360   2450    517   1565       C  
ATOM   4108  SD  MET B 530      43.011  86.739 -19.534  1.00 84.48           S  
ANISOU 4108  SD  MET B 530     7992  12539  11566   2500    830   1665       S  
ATOM   4109  CE  MET B 530      42.692  85.281 -20.507  1.00 83.46           C  
ANISOU 4109  CE  MET B 530     8203  12317  11190   2851   1053   1543       C  
ATOM   4110  N   LEU B 531      47.347  86.352 -16.194  1.00 88.10           N  
ANISOU 4110  N   LEU B 531     7104  13466  12901   2591    391   2247       N  
ATOM   4111  CA  LEU B 531      48.350  86.998 -15.374  1.00 89.06           C  
ANISOU 4111  CA  LEU B 531     6821  13727  13291   2427    195   2432       C  
ATOM   4112  C   LEU B 531      48.876  88.169 -16.177  1.00 90.53           C  
ANISOU 4112  C   LEU B 531     6729  14062  13604   2263    337   2606       C  
ATOM   4113  O   LEU B 531      48.853  88.134 -17.405  1.00 91.93           O  
ANISOU 4113  O   LEU B 531     6946  14292  13689   2402    649   2632       O  
ATOM   4114  CB  LEU B 531      49.477  86.033 -15.007  1.00 91.97           C  
ANISOU 4114  CB  LEU B 531     6918  14223  13803   2703    210   2567       C  
ATOM   4115  CG  LEU B 531      49.109  84.973 -13.965  1.00 91.36           C  
ANISOU 4115  CG  LEU B 531     7073  13998  13640   2823      3   2431       C  
ATOM   4116  CD1 LEU B 531      48.208  83.902 -14.561  1.00 90.01           C  
ANISOU 4116  CD1 LEU B 531     7337  13660  13201   3064    183   2236       C  
ATOM   4117  CD2 LEU B 531      50.358  84.329 -13.376  1.00 94.32           C  
ANISOU 4117  CD2 LEU B 531     7103  14518  14216   3023    -67   2607       C  
ATOM   4118  N   GLY B 532      49.309  89.216 -15.480  1.00 91.26           N  
ANISOU 4118  N   GLY B 532     6574  14207  13894   1956    100   2720       N  
ATOM   4119  CA  GLY B 532      49.990  90.359 -16.095  1.00 92.62           C  
ANISOU 4119  CA  GLY B 532     6425  14528  14237   1765    196   2928       C  
ATOM   4120  C   GLY B 532      49.316  90.951 -17.320  1.00 90.69           C  
ANISOU 4120  C   GLY B 532     6380  14242  13834   1721    446   2883       C  
ATOM   4121  O   GLY B 532      48.198  91.448 -17.242  1.00 87.96           O  
ANISOU 4121  O   GLY B 532     6370  13718  13332   1551    341   2709       O  
ATOM   4122  N   ASP B 533      49.998  90.877 -18.461  1.00 92.86           N  
ANISOU 4122  N   ASP B 533     6452  14687  14143   1892    784   3048       N  
ATOM   4123  CA  ASP B 533      49.548  91.533 -19.699  1.00 91.58           C  
ANISOU 4123  CA  ASP B 533     6432  14515  13847   1844   1035   3054       C  
ATOM   4124  C   ASP B 533      48.362  90.872 -20.396  1.00 86.12           C  
ANISOU 4124  C   ASP B 533     6226  13662  12832   2033   1183   2815       C  
ATOM   4125  O   ASP B 533      47.759  91.482 -21.272  1.00 86.28           O  
ANISOU 4125  O   ASP B 533     6435  13632  12713   1954   1315   2781       O  
ATOM   4126  CB  ASP B 533      50.704  91.597 -20.709  1.00 96.83           C  
ANISOU 4126  CB  ASP B 533     6726  15426  14637   1992   1377   3321       C  
ATOM   4127  CG  ASP B 533      51.317  92.976 -20.814  1.00100.09           C  
ANISOU 4127  CG  ASP B 533     6812  15946  15269   1657   1336   3551       C  
ATOM   4128  OD1 ASP B 533      52.452  93.161 -20.310  1.00106.10           O  
ANISOU 4128  OD1 ASP B 533     7117  16880  16316   1580   1250   3775       O  
ATOM   4129  OD2 ASP B 533      50.668  93.872 -21.406  1.00 99.74           O  
ANISOU 4129  OD2 ASP B 533     6968  15811  15117   1467   1381   3515       O  
ATOM   4130  N   ALA B 534      48.035  89.639 -20.021  1.00 81.82           N  
ANISOU 4130  N   ALA B 534     5887  13032  12168   2273   1150   2659       N  
ATOM   4131  CA  ALA B 534      47.212  88.784 -20.865  1.00 79.24           C  
ANISOU 4131  CA  ALA B 534     5959  12591  11554   2518   1346   2481       C  
ATOM   4132  C   ALA B 534      45.779  89.306 -21.051  1.00 75.28           C  
ANISOU 4132  C   ALA B 534     5854  11895  10851   2323   1242   2282       C  
ATOM   4133  O   ALA B 534      45.261  90.055 -20.223  1.00 72.37           O  
ANISOU 4133  O   ALA B 534     5517  11438  10541   2041    974   2225       O  
ATOM   4134  CB  ALA B 534      47.190  87.364 -20.321  1.00 78.45           C  
ANISOU 4134  CB  ALA B 534     5997  12420  11390   2789   1298   2366       C  
ATOM   4135  N   LYS B 535      45.171  88.890 -22.156  1.00 75.14           N  
ANISOU 4135  N   LYS B 535     6138  11817  10594   2491   1459   2183       N  
ATOM   4136  CA  LYS B 535      43.815  89.301 -22.542  1.00 74.39           C  
ANISOU 4136  CA  LYS B 535     6413  11556  10293   2349   1394   2009       C  
ATOM   4137  C   LYS B 535      43.171  88.144 -23.289  1.00 73.40           C  
ANISOU 4137  C   LYS B 535     6662  11324   9902   2614   1535   1846       C  
ATOM   4138  O   LYS B 535      43.878  87.252 -23.769  1.00 75.14           O  
ANISOU 4138  O   LYS B 535     6850  11613  10085   2911   1748   1895       O  
ATOM   4139  CB  LYS B 535      43.863  90.520 -23.464  1.00 75.58           C  
ANISOU 4139  CB  LYS B 535     6497  11775  10443   2195   1531   2130       C  
ATOM   4140  CG  LYS B 535      43.910  91.880 -22.773  1.00 76.22           C  
ANISOU 4140  CG  LYS B 535     6384  11860  10713   1843   1317   2215       C  
ATOM   4141  CD  LYS B 535      45.315  92.267 -22.344  1.00 80.11           C  
ANISOU 4141  CD  LYS B 535     6411  12535  11491   1779   1321   2455       C  
ATOM   4142  CE  LYS B 535      45.694  93.687 -22.737  1.00 81.72           C  
ANISOU 4142  CE  LYS B 535     6419  12809  11821   1519   1352   2638       C  
ATOM   4143  NZ  LYS B 535      44.678  94.684 -22.310  1.00 78.17           N  
ANISOU 4143  NZ  LYS B 535     6184  12186  11330   1231   1109   2522       N  
ATOM   4144  N   THR B 536      41.841  88.159 -23.383  1.00 69.74           N  
ANISOU 4144  N   THR B 536     6552  10688   9255   2511   1413   1658       N  
ATOM   4145  CA  THR B 536      41.104  87.153 -24.156  1.00 68.98           C  
ANISOU 4145  CA  THR B 536     6846  10468   8894   2713   1510   1496       C  
ATOM   4146  C   THR B 536      39.954  87.834 -24.923  1.00 67.85           C  
ANISOU 4146  C   THR B 536     6970  10234   8574   2562   1489   1405       C  
ATOM   4147  O   THR B 536      39.755  89.037 -24.783  1.00 67.03           O  
ANISOU 4147  O   THR B 536     6747  10159   8560   2321   1404   1466       O  
ATOM   4148  CB  THR B 536      40.600  86.008 -23.254  1.00 67.05           C  
ANISOU 4148  CB  THR B 536     6787  10079   8610   2781   1327   1338       C  
ATOM   4149  OG1 THR B 536      40.152  84.909 -24.057  1.00 66.48           O  
ANISOU 4149  OG1 THR B 536     7069   9890   8297   3009   1442   1210       O  
ATOM   4150  CG2 THR B 536      39.470  86.480 -22.334  1.00 64.34           C  
ANISOU 4150  CG2 THR B 536     6549   9614   8282   2500   1036   1220       C  
ATOM   4151  N   ASN B 537      39.214  87.074 -25.731  1.00 67.78           N  
ANISOU 4151  N   ASN B 537     7327  10109   8315   2703   1553   1265       N  
ATOM   4152  CA  ASN B 537      38.307  87.676 -26.715  1.00 68.00           C  
ANISOU 4152  CA  ASN B 537     7594  10081   8160   2611   1576   1212       C  
ATOM   4153  C   ASN B 537      36.997  86.930 -26.996  1.00 66.25           C  
ANISOU 4153  C   ASN B 537     7785   9674   7710   2623   1449   1005       C  
ATOM   4154  O   ASN B 537      36.404  87.124 -28.051  1.00 68.27           O  
ANISOU 4154  O   ASN B 537     8279   9888   7771   2633   1510    963       O  
ATOM   4155  CB  ASN B 537      39.064  87.871 -28.038  1.00 70.89           C  
ANISOU 4155  CB  ASN B 537     7948  10563   8423   2788   1893   1338       C  
ATOM   4156  CG  ASN B 537      39.333  86.563 -28.759  1.00 73.48           C  
ANISOU 4156  CG  ASN B 537     8520  10848   8551   3120   2081   1270       C  
ATOM   4157  OD1 ASN B 537      38.782  85.511 -28.416  1.00 73.11           O  
ANISOU 4157  OD1 ASN B 537     8713  10654   8411   3199   1956   1109       O  
ATOM   4158  ND2 ASN B 537      40.189  86.621 -29.766  1.00 76.79           N  
ANISOU 4158  ND2 ASN B 537     8890  11388   8896   3320   2390   1398       N  
ATOM   4159  N   GLU B 538      36.543  86.081 -26.082  1.00 64.16           N  
ANISOU 4159  N   GLU B 538     7611   9298   7468   2614   1268    885       N  
ATOM   4160  CA  GLU B 538      35.302  85.355 -26.311  1.00 63.39           C  
ANISOU 4160  CA  GLU B 538     7883   9025   7177   2597   1134    706       C  
ATOM   4161  C   GLU B 538      34.118  86.263 -25.955  1.00 60.46           C  
ANISOU 4161  C   GLU B 538     7526   8611   6833   2314    921    658       C  
ATOM   4162  O   GLU B 538      34.155  86.978 -24.958  1.00 57.73           O  
ANISOU 4162  O   GLU B 538     6948   8312   6675   2146    802    706       O  
ATOM   4163  CB  GLU B 538      35.236  84.065 -25.499  1.00 63.75           C  
ANISOU 4163  CB  GLU B 538     8035   8957   7229   2689   1029    609       C  
ATOM   4164  CG  GLU B 538      36.280  83.019 -25.876  1.00 68.56           C  
ANISOU 4164  CG  GLU B 538     8690   9574   7783   3007   1229    635       C  
ATOM   4165  CD  GLU B 538      37.636  83.218 -25.204  1.00 69.45           C  
ANISOU 4165  CD  GLU B 538     8412   9848   8126   3094   1325    794       C  
ATOM   4166  OE1 GLU B 538      37.791  84.129 -24.366  1.00 68.38           O  
ANISOU 4166  OE1 GLU B 538     7983   9804   8193   2891   1212    878       O  
ATOM   4167  OE2 GLU B 538      38.561  82.449 -25.517  1.00 74.84           O  
ANISOU 4167  OE2 GLU B 538     9086  10565   8785   3375   1510    840       O  
ATOM   4168  N   PHE B 539      33.091  86.239 -26.804  1.00 60.47           N  
ANISOU 4168  N   PHE B 539     7807   8524   6641   2277    875    566       N  
ATOM   4169  CA  PHE B 539      31.859  86.937 -26.545  1.00 59.59           C  
ANISOU 4169  CA  PHE B 539     7736   8365   6537   2047    675    514       C  
ATOM   4170  C   PHE B 539      31.069  86.091 -25.582  1.00 59.08           C  
ANISOU 4170  C   PHE B 539     7764   8186   6497   1974    475    398       C  
ATOM   4171  O   PHE B 539      30.736  84.948 -25.865  1.00 59.93           O  
ANISOU 4171  O   PHE B 539     8122   8180   6469   2067    449    299       O  
ATOM   4172  CB  PHE B 539      31.026  87.181 -27.791  1.00 59.99           C  
ANISOU 4172  CB  PHE B 539     8042   8371   6380   2033    675    469       C  
ATOM   4173  CG  PHE B 539      29.786  87.956 -27.500  1.00 59.45           C  
ANISOU 4173  CG  PHE B 539     7973   8270   6343   1812    472    434       C  
ATOM   4174  CD1 PHE B 539      29.830  89.339 -27.412  1.00 58.84           C  
ANISOU 4174  CD1 PHE B 539     7706   8275   6374   1688    476    533       C  
ATOM   4175  CD2 PHE B 539      28.583  87.305 -27.245  1.00 59.61           C  
ANISOU 4175  CD2 PHE B 539     8171   8178   6300   1727    276    313       C  
ATOM   4176  CE1 PHE B 539      28.688  90.057 -27.112  1.00 58.33           C  
ANISOU 4176  CE1 PHE B 539     7642   8179   6339   1515    299    503       C  
ATOM   4177  CE2 PHE B 539      27.443  88.018 -26.934  1.00 57.86           C  
ANISOU 4177  CE2 PHE B 539     7915   7946   6122   1543    103    296       C  
ATOM   4178  CZ  PHE B 539      27.496  89.394 -26.862  1.00 56.73           C  
ANISOU 4178  CZ  PHE B 539     7591   7885   6077   1451    119    387       C  
ATOM   4179  N   CYS B 540      30.687  86.697 -24.476  1.00 56.97           N  
ANISOU 4179  N   CYS B 540     7320   7936   6388   1797    330    410       N  
ATOM   4180  CA  CYS B 540      30.582  85.953 -23.294  1.00 56.82           C  
ANISOU 4180  CA  CYS B 540     7275   7860   6452   1772    213    362       C  
ATOM   4181  C   CYS B 540      29.916  86.648 -22.100  1.00 54.32           C  
ANISOU 4181  C   CYS B 540     6819   7548   6269   1569     45    360       C  
ATOM   4182  O   CYS B 540      30.253  87.785 -21.801  1.00 55.31           O  
ANISOU 4182  O   CYS B 540     6748   7757   6510   1485     52    439       O  
ATOM   4183  CB  CYS B 540      32.039  85.741 -22.971  1.00 61.97           C  
ANISOU 4183  CB  CYS B 540     7738   8594   7214   1919    345    452       C  
ATOM   4184  SG  CYS B 540      32.210  84.587 -21.709  1.00 57.76           S  
ANISOU 4184  SG  CYS B 540     7210   7984   6751   1964    239    406       S  
ATOM   4185  N   GLY B 541      29.019  85.951 -21.393  1.00 52.69           N  
ANISOU 4185  N   GLY B 541     6723   7249   6046   1496    -98    277       N  
ATOM   4186  CA  GLY B 541      28.380  86.491 -20.186  1.00 50.84           C  
ANISOU 4186  CA  GLY B 541     6377   7019   5920   1332   -236    274       C  
ATOM   4187  C   GLY B 541      26.854  86.428 -20.168  1.00 49.42           C  
ANISOU 4187  C   GLY B 541     6324   6776   5675   1201   -364    205       C  
ATOM   4188  O   GLY B 541      26.250  85.713 -20.958  1.00 52.48           O  
ANISOU 4188  O   GLY B 541     6906   7093   5937   1220   -385    147       O  
ATOM   4189  N   THR B 542      26.239  87.153 -19.238  1.00 46.11           N  
ANISOU 4189  N   THR B 542     5796   6380   5342   1072   -452    215       N  
ATOM   4190  CA  THR B 542      24.781  87.218 -19.137  1.00 45.76           C  
ANISOU 4190  CA  THR B 542     5817   6306   5263    951   -560    175       C  
ATOM   4191  C   THR B 542      24.339  88.640 -19.509  1.00 43.26           C  
ANISOU 4191  C   THR B 542     5413   6053   4971    890   -561    212       C  
ATOM   4192  O   THR B 542      24.943  89.594 -19.031  1.00 42.04           O  
ANISOU 4192  O   THR B 542     5122   5945   4904    880   -530    261       O  
ATOM   4193  CB  THR B 542      24.308  86.855 -17.717  1.00 46.33           C  
ANISOU 4193  CB  THR B 542     5851   6351   5399    874   -643    162       C  
ATOM   4194  OG1 THR B 542      24.692  85.507 -17.447  1.00 46.01           O  
ANISOU 4194  OG1 THR B 542     5918   6235   5328    934   -648    133       O  
ATOM   4195  CG2 THR B 542      22.785  86.988 -17.598  1.00 47.16           C  
ANISOU 4195  CG2 THR B 542     5981   6449   5486    753   -733    143       C  
ATOM   4196  N   PRO B 543      23.305  88.776 -20.373  1.00 42.61           N  
ANISOU 4196  N   PRO B 543     5420   5962   4808    848   -610    192       N  
ATOM   4197  CA  PRO B 543      23.022  90.066 -21.009  1.00 42.50           C  
ANISOU 4197  CA  PRO B 543     5356   5998   4793    826   -598    235       C  
ATOM   4198  C   PRO B 543      23.075  91.291 -20.092  1.00 41.76           C  
ANISOU 4198  C   PRO B 543     5107   5942   4815    777   -603    278       C  
ATOM   4199  O   PRO B 543      23.865  92.210 -20.362  1.00 42.03           O  
ANISOU 4199  O   PRO B 543     5077   6005   4885    797   -537    333       O  
ATOM   4200  CB  PRO B 543      21.626  89.843 -21.618  1.00 43.01           C  
ANISOU 4200  CB  PRO B 543     5517   6043   4781    765   -705    204       C  
ATOM   4201  CG  PRO B 543      21.674  88.417 -22.050  1.00 43.67           C  
ANISOU 4201  CG  PRO B 543     5769   6056   4768    793   -727    147       C  
ATOM   4202  CD  PRO B 543      22.505  87.696 -21.004  1.00 43.57           C  
ANISOU 4202  CD  PRO B 543     5716   6015   4820    830   -682    136       C  
ATOM   4203  N   ASP B 544      22.322  91.295 -18.992  1.00 40.26           N  
ANISOU 4203  N   ASP B 544     4870   5746   4681    715   -674    258       N  
ATOM   4204  CA  ASP B 544      22.300  92.488 -18.113  1.00 40.37           C  
ANISOU 4204  CA  ASP B 544     4781   5776   4779    683   -683    287       C  
ATOM   4205  C   ASP B 544      23.637  92.932 -17.565  1.00 38.90           C  
ANISOU 4205  C   ASP B 544     4522   5592   4666    697   -640    319       C  
ATOM   4206  O   ASP B 544      23.811  94.116 -17.256  1.00 37.53           O  
ANISOU 4206  O   ASP B 544     4296   5417   4546    668   -647    351       O  
ATOM   4207  CB  ASP B 544      21.343  92.307 -16.939  1.00 41.87           C  
ANISOU 4207  CB  ASP B 544     4949   5962   4998    637   -740    261       C  
ATOM   4208  CG  ASP B 544      19.915  92.579 -17.328  1.00 44.93           C  
ANISOU 4208  CG  ASP B 544     5336   6373   5360    609   -788    265       C  
ATOM   4209  OD1 ASP B 544      19.614  93.712 -17.733  1.00 50.33           O  
ANISOU 4209  OD1 ASP B 544     5996   7074   6053    624   -787    294       O  
ATOM   4210  OD2 ASP B 544      19.096  91.670 -17.225  1.00 47.80           O  
ANISOU 4210  OD2 ASP B 544     5721   6739   5702    569   -832    249       O  
ATOM   4211  N   TYR B 545      24.555  91.984 -17.420  1.00 38.13           N  
ANISOU 4211  N   TYR B 545     4421   5491   4574    740   -608    315       N  
ATOM   4212  CA  TYR B 545      25.805  92.197 -16.701  1.00 38.46           C  
ANISOU 4212  CA  TYR B 545     4366   5543   4701    747   -595    352       C  
ATOM   4213  C   TYR B 545      27.028  92.350 -17.603  1.00 40.02           C  
ANISOU 4213  C   TYR B 545     4502   5782   4921    801   -500    418       C  
ATOM   4214  O   TYR B 545      28.114  92.668 -17.105  1.00 39.83           O  
ANISOU 4214  O   TYR B 545     4361   5782   4989    792   -496    472       O  
ATOM   4215  CB  TYR B 545      26.074  91.008 -15.766  1.00 39.33           C  
ANISOU 4215  CB  TYR B 545     4493   5630   4819    773   -628    321       C  
ATOM   4216  CG  TYR B 545      25.025  90.761 -14.718  1.00 37.43           C  
ANISOU 4216  CG  TYR B 545     4303   5357   4562    720   -702    275       C  
ATOM   4217  CD1 TYR B 545      23.893  90.020 -15.007  1.00 37.93           C  
ANISOU 4217  CD1 TYR B 545     4454   5399   4556    704   -718    237       C  
ATOM   4218  CD2 TYR B 545      25.179  91.255 -13.424  1.00 37.24           C  
ANISOU 4218  CD2 TYR B 545     4242   5321   4584    682   -758    279       C  
ATOM   4219  CE1 TYR B 545      22.920  89.779 -14.040  1.00 37.53           C  
ANISOU 4219  CE1 TYR B 545     4427   5334   4498    650   -765    217       C  
ATOM   4220  CE2 TYR B 545      24.210  91.030 -12.453  1.00 37.19           C  
ANISOU 4220  CE2 TYR B 545     4290   5293   4547    647   -799    247       C  
ATOM   4221  CZ  TYR B 545      23.091  90.281 -12.756  1.00 37.43           C  
ANISOU 4221  CZ  TYR B 545     4380   5319   4523    632   -791    223       C  
ATOM   4222  OH  TYR B 545      22.122  90.051 -11.775  1.00 38.35           O  
ANISOU 4222  OH  TYR B 545     4527   5428   4617    594   -812    213       O  
ATOM   4223  N   ILE B 546      26.857  92.138 -18.912  1.00 40.54           N  
ANISOU 4223  N   ILE B 546     4643   5860   4899    854   -427    421       N  
ATOM   4224  CA AILE B 546      27.982  92.092 -19.831  0.50 42.43           C  
ANISOU 4224  CA AILE B 546     4840   6146   5133    933   -302    487       C  
ATOM   4225  CA BILE B 546      27.993  92.100 -19.844  0.50 42.43           C  
ANISOU 4225  CA BILE B 546     4840   6147   5134    933   -300    488       C  
ATOM   4226  C   ILE B 546      28.659  93.470 -19.976  1.00 42.92           C  
ANISOU 4226  C   ILE B 546     4776   6248   5283    871   -267    585       C  
ATOM   4227  O   ILE B 546      27.996  94.485 -20.157  1.00 42.33           O  
ANISOU 4227  O   ILE B 546     4730   6151   5201    799   -306    593       O  
ATOM   4228  CB AILE B 546      27.527  91.495 -21.188  0.50 43.05           C  
ANISOU 4228  CB AILE B 546     5082   6214   5061   1012   -236    456       C  
ATOM   4229  CB BILE B 546      27.582  91.581 -21.247  0.50 43.06           C  
ANISOU 4229  CB BILE B 546     5076   6219   5064   1012   -229    463       C  
ATOM   4230  CG1AILE B 546      28.718  91.080 -22.037  0.50 44.57           C  
ANISOU 4230  CG1AILE B 546     5260   6451   5221   1139    -79    511       C  
ATOM   4231  CG1BILE B 546      27.339  90.077 -21.216  0.50 43.32           C  
ANISOU 4231  CG1BILE B 546     5241   6201   5017   1086   -246    383       C  
ATOM   4232  CG2AILE B 546      26.649  92.459 -21.962  0.50 42.49           C  
ANISOU 4232  CG2AILE B 546     5072   6139   4931    955   -260    467       C  
ATOM   4233  CG2BILE B 546      28.675  91.835 -22.272  0.50 44.10           C  
ANISOU 4233  CG2BILE B 546     5168   6411   5177   1096    -70    550       C  
ATOM   4234  CD1AILE B 546      28.337  90.090 -23.115  0.50 45.86           C  
ANISOU 4234  CD1AILE B 546     5638   6573   5211   1245    -31    450       C  
ATOM   4235  CD1BILE B 546      26.488  89.588 -22.373  0.50 44.02           C  
ANISOU 4235  CD1BILE B 546     5534   6246   4944   1115   -254    328       C  
ATOM   4236  N   ALA B 547      29.987  93.494 -19.870  1.00 44.65           N  
ANISOU 4236  N   ALA B 547     4849   6522   5594    896   -199    667       N  
ATOM   4237  CA  ALA B 547      30.756  94.747 -19.938  1.00 44.34           C  
ANISOU 4237  CA  ALA B 547     4670   6516   5660    809   -177    779       C  
ATOM   4238  C   ALA B 547      30.761  95.338 -21.343  1.00 44.98           C  
ANISOU 4238  C   ALA B 547     4797   6624   5668    828    -52    847       C  
ATOM   4239  O   ALA B 547      30.721  94.598 -22.336  1.00 45.01           O  
ANISOU 4239  O   ALA B 547     4896   6653   5553    947     58    833       O  
ATOM   4240  CB  ALA B 547      32.193  94.501 -19.484  1.00 45.43           C  
ANISOU 4240  CB  ALA B 547     4610   6722   5927    828   -142    868       C  
ATOM   4241  N   PRO B 548      30.852  96.675 -21.446  1.00 45.67           N  
ANISOU 4241  N   PRO B 548     4839   6696   5816    715    -72    924       N  
ATOM   4242  CA  PRO B 548      30.826  97.294 -22.782  1.00 47.27           C  
ANISOU 4242  CA  PRO B 548     5103   6918   5939    728     44   1001       C  
ATOM   4243  C   PRO B 548      31.981  96.868 -23.704  1.00 49.41           C  
ANISOU 4243  C   PRO B 548     5287   7288   6197    824    243   1107       C  
ATOM   4244  O   PRO B 548      31.768  96.704 -24.906  1.00 50.52           O  
ANISOU 4244  O   PRO B 548     5554   7447   6194    912    362   1121       O  
ATOM   4245  CB  PRO B 548      30.878  98.802 -22.493  1.00 47.29           C  
ANISOU 4245  CB  PRO B 548     5060   6868   6038    576    -27   1076       C  
ATOM   4246  CG  PRO B 548      31.321  98.930 -21.075  1.00 47.29           C  
ANISOU 4246  CG  PRO B 548     4942   6843   6182    486   -157   1061       C  
ATOM   4247  CD  PRO B 548      30.884  97.678 -20.369  1.00 45.38           C  
ANISOU 4247  CD  PRO B 548     4738   6604   5899    573   -211    937       C  
ATOM   4248  N   GLU B 549      33.180  96.694 -23.150  1.00 51.34           N  
ANISOU 4248  N   GLU B 549     5321   7600   6585    816    278   1188       N  
ATOM   4249  CA  GLU B 549      34.339  96.287 -23.952  1.00 53.78           C  
ANISOU 4249  CA  GLU B 549     5509   8023   6901    927    488   1308       C  
ATOM   4250  C   GLU B 549      34.130  94.923 -24.647  1.00 53.38           C  
ANISOU 4250  C   GLU B 549     5613   7987   6680   1140    605   1222       C  
ATOM   4251  O   GLU B 549      34.675  94.681 -25.732  1.00 55.64           O  
ANISOU 4251  O   GLU B 549     5917   8343   6879   1266    809   1297       O  
ATOM   4252  CB  GLU B 549      35.653  96.329 -23.138  1.00 55.87           C  
ANISOU 4252  CB  GLU B 549     5483   8368   7375    879    481   1421       C  
ATOM   4253  CG  GLU B 549      35.683  95.483 -21.868  1.00 56.41           C  
ANISOU 4253  CG  GLU B 549     5505   8414   7512    904    335   1327       C  
ATOM   4254  CD  GLU B 549      35.198  96.220 -20.613  1.00 55.81           C  
ANISOU 4254  CD  GLU B 549     5435   8245   7524    722     97   1270       C  
ATOM   4255  OE1 GLU B 549      34.316  97.112 -20.713  1.00 55.40           O  
ANISOU 4255  OE1 GLU B 549     5519   8107   7422    620     25   1231       O  
ATOM   4256  OE2 GLU B 549      35.701  95.895 -19.509  1.00 56.98           O  
ANISOU 4256  OE2 GLU B 549     5464   8401   7784    696    -19   1266       O  
ATOM   4257  N   ILE B 550      33.312  94.056 -24.054  1.00 51.40           N  
ANISOU 4257  N   ILE B 550     5497   7662   6370   1178    478   1069       N  
ATOM   4258  CA  ILE B 550      32.919  92.804 -24.702  1.00 52.14           C  
ANISOU 4258  CA  ILE B 550     5794   7727   6286   1350    545    970       C  
ATOM   4259  C   ILE B 550      31.927  93.077 -25.813  1.00 52.57           C  
ANISOU 4259  C   ILE B 550     6084   7734   6155   1352    557    926       C  
ATOM   4260  O   ILE B 550      32.041  92.515 -26.900  1.00 53.89           O  
ANISOU 4260  O   ILE B 550     6402   7911   6160   1495    695    921       O  
ATOM   4261  CB  ILE B 550      32.293  91.791 -23.714  1.00 51.87           C  
ANISOU 4261  CB  ILE B 550     5841   7615   6251   1362    391    832       C  
ATOM   4262  CG1 ILE B 550      33.347  91.294 -22.714  1.00 52.59           C  
ANISOU 4262  CG1 ILE B 550     5731   7754   6496   1403    386    876       C  
ATOM   4263  CG2 ILE B 550      31.691  90.605 -24.466  1.00 52.45           C  
ANISOU 4263  CG2 ILE B 550     6175   7625   6128   1501    426    723       C  
ATOM   4264  CD1 ILE B 550      32.750  90.473 -21.583  1.00 51.54           C  
ANISOU 4264  CD1 ILE B 550     5667   7539   6374   1386    222    760       C  
ATOM   4265  N   LEU B 551      30.941  93.935 -25.541  1.00 50.94           N  
ANISOU 4265  N   LEU B 551     5922   7470   5963   1206    407    893       N  
ATOM   4266  CA  LEU B 551      29.949  94.280 -26.550  1.00 49.80           C  
ANISOU 4266  CA  LEU B 551     5983   7282   5655   1201    387    862       C  
ATOM   4267  C   LEU B 551      30.594  94.951 -27.764  1.00 52.44           C  
ANISOU 4267  C   LEU B 551     6330   7676   5918   1243    569    991       C  
ATOM   4268  O   LEU B 551      30.148  94.741 -28.883  1.00 52.09           O  
ANISOU 4268  O   LEU B 551     6494   7614   5681   1321    620    969       O  
ATOM   4269  CB  LEU B 551      28.888  95.197 -25.970  1.00 47.62           C  
ANISOU 4269  CB  LEU B 551     5710   6948   5434   1055    208    829       C  
ATOM   4270  CG  LEU B 551      28.083  94.625 -24.817  1.00 44.94           C  
ANISOU 4270  CG  LEU B 551     5373   6555   5146   1011     42    713       C  
ATOM   4271  CD1 LEU B 551      27.166  95.722 -24.310  1.00 44.91           C  
ANISOU 4271  CD1 LEU B 551     5354   6508   5199    892    -91    707       C  
ATOM   4272  CD2 LEU B 551      27.309  93.391 -25.260  1.00 43.76           C  
ANISOU 4272  CD2 LEU B 551     5412   6366   4847   1088      2    604       C  
ATOM   4273  N   LEU B 552      31.643  95.743 -27.521  1.00 53.91           N  
ANISOU 4273  N   LEU B 552     6298   7928   6257   1180    656   1131       N  
ATOM   4274  CA  LEU B 552      32.458  96.357 -28.581  1.00 56.04           C  
ANISOU 4274  CA  LEU B 552     6533   8272   6487   1211    861   1288       C  
ATOM   4275  C   LEU B 552      33.508  95.420 -29.195  1.00 57.95           C  
ANISOU 4275  C   LEU B 552     6743   8607   6667   1401   1094   1341       C  
ATOM   4276  O   LEU B 552      34.376  95.873 -29.934  1.00 59.76           O  
ANISOU 4276  O   LEU B 552     6888   8924   6894   1434   1296   1496       O  
ATOM   4277  CB  LEU B 552      33.188  97.582 -28.015  1.00 57.19           C  
ANISOU 4277  CB  LEU B 552     6439   8446   6843   1041    849   1433       C  
ATOM   4278  CG  LEU B 552      32.285  98.756 -27.643  1.00 56.16           C  
ANISOU 4278  CG  LEU B 552     6368   8215   6754    874    666   1415       C  
ATOM   4279  CD1 LEU B 552      33.050  99.823 -26.880  1.00 56.31           C  
ANISOU 4279  CD1 LEU B 552     6172   8233   6989    698    617   1535       C  
ATOM   4280  CD2 LEU B 552      31.644  99.336 -28.897  1.00 57.93           C  
ANISOU 4280  CD2 LEU B 552     6800   8408   6801    895    718   1450       C  
ATOM   4281  N   GLY B 553      33.444  94.128 -28.875  1.00 57.95           N  
ANISOU 4281  N   GLY B 553     6811   8588   6620   1532   1075   1222       N  
ATOM   4282  CA  GLY B 553      34.380  93.133 -29.399  1.00 60.34           C  
ANISOU 4282  CA  GLY B 553     7112   8961   6852   1751   1292   1253       C  
ATOM   4283  C   GLY B 553      35.856  93.400 -29.144  1.00 62.59           C  
ANISOU 4283  C   GLY B 553     7068   9385   7325   1774   1461   1432       C  
ATOM   4284  O   GLY B 553      36.691  93.059 -29.978  1.00 64.64           O  
ANISOU 4284  O   GLY B 553     7311   9737   7511   1948   1713   1526       O  
ATOM   4285  N   GLN B 554      36.186  94.009 -28.005  1.00 62.34           N  
ANISOU 4285  N   GLN B 554     6779   9374   7534   1601   1324   1486       N  
ATOM   4286  CA  GLN B 554      37.579  94.330 -27.679  1.00 64.63           C  
ANISOU 4286  CA  GLN B 554     6722   9798   8033   1584   1441   1670       C  
ATOM   4287  C   GLN B 554      38.207  93.179 -26.909  1.00 65.51           C  
ANISOU 4287  C   GLN B 554     6708   9949   8233   1726   1435   1634       C  
ATOM   4288  O   GLN B 554      37.507  92.431 -26.216  1.00 63.60           O  
ANISOU 4288  O   GLN B 554     6605   9606   7952   1747   1267   1469       O  
ATOM   4289  CB  GLN B 554      37.673  95.609 -26.837  1.00 64.01           C  
ANISOU 4289  CB  GLN B 554     6446   9707   8167   1311   1268   1753       C  
ATOM   4290  CG  GLN B 554      37.096  96.844 -27.502  1.00 63.94           C  
ANISOU 4290  CG  GLN B 554     6555   9644   8095   1163   1258   1803       C  
ATOM   4291  CD  GLN B 554      37.792  97.170 -28.810  1.00 67.30           C  
ANISOU 4291  CD  GLN B 554     6953  10172   8442   1239   1538   1975       C  
ATOM   4292  OE1 GLN B 554      39.019  97.279 -28.864  1.00 69.01           O  
ANISOU 4292  OE1 GLN B 554     6896  10524   8801   1248   1697   2154       O  
ATOM   4293  NE2 GLN B 554      37.013  97.321 -29.874  1.00 67.92           N  
ANISOU 4293  NE2 GLN B 554     7314  10197   8294   1294   1602   1933       N  
ATOM   4294  N   LYS B 555      39.522  93.039 -27.037  1.00 67.81           N  
ANISOU 4294  N   LYS B 555     6730  10389   8645   1827   1623   1800       N  
ATOM   4295  CA  LYS B 555      40.285  92.148 -26.171  1.00 68.83           C  
ANISOU 4295  CA  LYS B 555     6666  10572   8912   1942   1597   1807       C  
ATOM   4296  C   LYS B 555      40.172  92.683 -24.758  1.00 65.96           C  
ANISOU 4296  C   LYS B 555     6145  10164   8751   1706   1307   1789       C  
ATOM   4297  O   LYS B 555      40.233  93.881 -24.555  1.00 65.93           O  
ANISOU 4297  O   LYS B 555     6017  10166   8864   1477   1223   1878       O  
ATOM   4298  CB  LYS B 555      41.755  92.099 -26.580  1.00 73.24           C  
ANISOU 4298  CB  LYS B 555     6907  11324   9596   2076   1852   2026       C  
ATOM   4299  CG  LYS B 555      42.032  91.114 -27.696  1.00 77.43           C  
ANISOU 4299  CG  LYS B 555     7598  11899   9923   2404   2147   2018       C  
ATOM   4300  CD  LYS B 555      43.512  90.788 -27.805  1.00 83.46           C  
ANISOU 4300  CD  LYS B 555     8011  12860  10837   2589   2384   2221       C  
ATOM   4301  CE  LYS B 555      43.714  89.351 -28.248  1.00 86.46           C  
ANISOU 4301  CE  LYS B 555     8571  13229  11049   2962   2567   2136       C  
ATOM   4302  NZ  LYS B 555      43.108  89.102 -29.587  1.00 88.31           N  
ANISOU 4302  NZ  LYS B 555     9197  13392  10962   3118   2759   2049       N  
ATOM   4303  N   TYR B 556      40.024  91.796 -23.785  1.00 64.40           N  
ANISOU 4303  N   TYR B 556     5974   9910   8584   1764   1156   1676       N  
ATOM   4304  CA  TYR B 556      39.715  92.219 -22.420  1.00 61.87           C  
ANISOU 4304  CA  TYR B 556     5586   9520   8400   1555    869   1625       C  
ATOM   4305  C   TYR B 556      40.377  91.341 -21.367  1.00 62.43           C  
ANISOU 4305  C   TYR B 556     5503   9621   8594   1644    774   1626       C  
ATOM   4306  O   TYR B 556      40.772  90.205 -21.641  1.00 64.39           O  
ANISOU 4306  O   TYR B 556     5775   9901   8786   1891    905   1614       O  
ATOM   4307  CB  TYR B 556      38.194  92.235 -22.224  1.00 57.40           C  
ANISOU 4307  CB  TYR B 556     5341   8788   7678   1470    708   1430       C  
ATOM   4308  CG  TYR B 556      37.546  90.884 -22.390  1.00 55.52           C  
ANISOU 4308  CG  TYR B 556     5361   8468   7265   1659    728   1273       C  
ATOM   4309  CD1 TYR B 556      37.500  89.988 -21.326  1.00 54.30           C  
ANISOU 4309  CD1 TYR B 556     5219   8262   7149   1705    589   1192       C  
ATOM   4310  CD2 TYR B 556      36.962  90.498 -23.600  1.00 55.09           C  
ANISOU 4310  CD2 TYR B 556     5560   8375   6997   1782    868   1208       C  
ATOM   4311  CE1 TYR B 556      36.908  88.749 -21.459  1.00 52.89           C  
ANISOU 4311  CE1 TYR B 556     5289   7989   6817   1858    596   1057       C  
ATOM   4312  CE2 TYR B 556      36.368  89.248 -23.742  1.00 54.44           C  
ANISOU 4312  CE2 TYR B 556     5734   8195   6753   1934    860   1063       C  
ATOM   4313  CZ  TYR B 556      36.342  88.380 -22.654  1.00 53.52           C  
ANISOU 4313  CZ  TYR B 556     5617   8023   6695   1965    724    991       C  
ATOM   4314  OH  TYR B 556      35.753  87.132 -22.733  1.00 53.23           O  
ANISOU 4314  OH  TYR B 556     5844   7871   6510   2093    700    855       O  
ATOM   4315  N   ASN B 557      40.478  91.890 -20.159  1.00 62.35           N  
ANISOU 4315  N   ASN B 557     5362   9588   8740   1449    537   1639       N  
ATOM   4316  CA  ASN B 557      41.062  91.201 -19.007  1.00 62.35           C  
ANISOU 4316  CA  ASN B 557     5221   9607   8861   1497    394   1644       C  
ATOM   4317  C   ASN B 557      40.040  91.175 -17.863  1.00 60.63           C  
ANISOU 4317  C   ASN B 557     5207   9237   8591   1368    134   1480       C  
ATOM   4318  O   ASN B 557      38.820  91.226 -18.109  1.00 58.10           O  
ANISOU 4318  O   ASN B 557     5161   8801   8109   1331    116   1340       O  
ATOM   4319  CB  ASN B 557      42.391  91.864 -18.603  1.00 64.57           C  
ANISOU 4319  CB  ASN B 557     5108  10031   9393   1392    353   1853       C  
ATOM   4320  CG  ASN B 557      42.250  93.341 -18.224  1.00 64.49           C  
ANISOU 4320  CG  ASN B 557     5037   9981   9482   1078    186   1901       C  
ATOM   4321  OD1 ASN B 557      41.154  93.866 -18.045  1.00 60.85           O  
ANISOU 4321  OD1 ASN B 557     4823   9382   8912    949     75   1770       O  
ATOM   4322  ND2 ASN B 557      43.385  94.015 -18.098  1.00 66.57           N  
ANISOU 4322  ND2 ASN B 557     4966  10366   9960    957    166   2100       N  
ATOM   4323  N   HIS B 558      40.519  91.094 -16.625  1.00 60.35           N  
ANISOU 4323  N   HIS B 558     5037   9205   8685   1303    -63   1504       N  
ATOM   4324  CA  HIS B 558      39.634  91.081 -15.454  1.00 58.60           C  
ANISOU 4324  CA  HIS B 558     5005   8849   8410   1189   -297   1364       C  
ATOM   4325  C   HIS B 558      38.681  92.282 -15.318  1.00 55.50           C  
ANISOU 4325  C   HIS B 558     4755   8360   7970    968   -401   1297       C  
ATOM   4326  O   HIS B 558      37.745  92.242 -14.514  1.00 52.65           O  
ANISOU 4326  O   HIS B 558     4591   7886   7525    904   -545   1169       O  
ATOM   4327  CB  HIS B 558      40.454  90.941 -14.167  1.00 59.74           C  
ANISOU 4327  CB  HIS B 558     4971   9023   8702   1145   -501   1425       C  
ATOM   4328  CG  HIS B 558      41.354  92.103 -13.894  1.00 63.41           C  
ANISOU 4328  CG  HIS B 558     5169   9565   9359    949   -606   1577       C  
ATOM   4329  ND1 HIS B 558      41.155  92.961 -12.835  1.00 64.02           N  
ANISOU 4329  ND1 HIS B 558     5283   9559   9479    725   -859   1548       N  
ATOM   4330  CD2 HIS B 558      42.467  92.539 -14.530  1.00 67.20           C  
ANISOU 4330  CD2 HIS B 558     5344  10191   9998    936   -496   1764       C  
ATOM   4331  CE1 HIS B 558      42.101  93.884 -12.835  1.00 67.01           C  
ANISOU 4331  CE1 HIS B 558     5405  10015  10037    567   -923   1706       C  
ATOM   4332  NE2 HIS B 558      42.914  93.647 -13.850  1.00 69.58           N  
ANISOU 4332  NE2 HIS B 558     5501  10489  10447    683   -703   1848       N  
ATOM   4333  N   SER B 559      38.921  93.337 -16.090  1.00 55.49           N  
ANISOU 4333  N   SER B 559     4660   8403   8020    862   -319   1392       N  
ATOM   4334  CA  SER B 559      38.095  94.538 -16.046  1.00 54.79           C  
ANISOU 4334  CA  SER B 559     4707   8217   7892    671   -407   1345       C  
ATOM   4335  C   SER B 559      36.596  94.242 -16.103  1.00 51.92           C  
ANISOU 4335  C   SER B 559     4649   7738   7340    710   -414   1169       C  
ATOM   4336  O   SER B 559      35.806  94.949 -15.479  1.00 52.24           O  
ANISOU 4336  O   SER B 559     4820   7680   7349    582   -553   1094       O  
ATOM   4337  CB  SER B 559      38.469  95.480 -17.197  1.00 56.40           C  
ANISOU 4337  CB  SER B 559     4812   8481   8137    605   -257   1472       C  
ATOM   4338  OG  SER B 559      38.199  94.883 -18.450  1.00 57.40           O  
ANISOU 4338  OG  SER B 559     5029   8648   8131    779    -26   1458       O  
ATOM   4339  N   VAL B 560      36.223  93.197 -16.841  1.00 51.04           N  
ANISOU 4339  N   VAL B 560     4650   7638   7104    889   -269   1110       N  
ATOM   4340  CA  VAL B 560      34.821  92.870 -17.111  1.00 49.57           C  
ANISOU 4340  CA  VAL B 560     4728   7357   6746    920   -265    966       C  
ATOM   4341  C   VAL B 560      34.082  92.430 -15.853  1.00 48.00           C  
ANISOU 4341  C   VAL B 560     4652   7071   6514    886   -434    851       C  
ATOM   4342  O   VAL B 560      32.897  92.701 -15.684  1.00 45.48           O  
ANISOU 4342  O   VAL B 560     4498   6673   6106    826   -491    758       O  
ATOM   4343  CB  VAL B 560      34.683  91.772 -18.210  1.00 50.06           C  
ANISOU 4343  CB  VAL B 560     4901   7439   6679   1113    -90    932       C  
ATOM   4344  CG1 VAL B 560      35.357  92.211 -19.508  1.00 51.18           C  
ANISOU 4344  CG1 VAL B 560     4952   7670   6822   1164    104   1047       C  
ATOM   4345  CG2 VAL B 560      35.245  90.431 -17.732  1.00 51.57           C  
ANISOU 4345  CG2 VAL B 560     5068   7641   6882   1268    -84    916       C  
ATOM   4346  N   ASP B 561      34.799  91.745 -14.967  1.00 48.27           N  
ANISOU 4346  N   ASP B 561     4595   7124   6619    932   -508    871       N  
ATOM   4347  CA  ASP B 561      34.214  91.304 -13.711  1.00 47.37           C  
ANISOU 4347  CA  ASP B 561     4597   6931   6468    903   -661    781       C  
ATOM   4348  C   ASP B 561      33.795  92.499 -12.857  1.00 46.53           C  
ANISOU 4348  C   ASP B 561     4522   6768   6387    728   -811    760       C  
ATOM   4349  O   ASP B 561      32.791  92.440 -12.149  1.00 47.02           O  
ANISOU 4349  O   ASP B 561     4748   6752   6364    694   -888    664       O  
ATOM   4350  CB  ASP B 561      35.214  90.427 -12.939  1.00 48.04           C  
ANISOU 4350  CB  ASP B 561     4569   7051   6630    990   -723    828       C  
ATOM   4351  CG  ASP B 561      35.225  88.965 -13.406  1.00 47.53           C  
ANISOU 4351  CG  ASP B 561     4587   6982   6490   1187   -612    795       C  
ATOM   4352  OD1 ASP B 561      34.337  88.525 -14.174  1.00 45.08           O  
ANISOU 4352  OD1 ASP B 561     4454   6621   6052   1238   -517    716       O  
ATOM   4353  OD2 ASP B 561      36.145  88.237 -12.968  1.00 47.82           O  
ANISOU 4353  OD2 ASP B 561     4518   7055   6595   1294   -635    851       O  
ATOM   4354  N   TRP B 562      34.576  93.576 -12.910  1.00 47.36           N  
ANISOU 4354  N   TRP B 562     4477   6908   6608    618   -850    855       N  
ATOM   4355  CA  TRP B 562      34.296  94.776 -12.115  1.00 47.01           C  
ANISOU 4355  CA  TRP B 562     4487   6786   6585    453  -1004    837       C  
ATOM   4356  C   TRP B 562      33.088  95.570 -12.653  1.00 46.07           C  
ANISOU 4356  C   TRP B 562     4532   6600   6372    411   -954    771       C  
ATOM   4357  O   TRP B 562      32.350  96.184 -11.884  1.00 47.46           O  
ANISOU 4357  O   TRP B 562     4845   6687   6498    341  -1057    701       O  
ATOM   4358  CB  TRP B 562      35.559  95.631 -11.990  1.00 48.07           C  
ANISOU 4358  CB  TRP B 562     4415   6964   6883    330  -1085    969       C  
ATOM   4359  CG  TRP B 562      36.614  94.925 -11.152  1.00 49.80           C  
ANISOU 4359  CG  TRP B 562     4481   7239   7198    360  -1194   1026       C  
ATOM   4360  CD1 TRP B 562      37.863  94.483 -11.562  1.00 51.87           C  
ANISOU 4360  CD1 TRP B 562     4486   7628   7593    422  -1133   1160       C  
ATOM   4361  CD2 TRP B 562      36.487  94.532  -9.784  1.00 49.51           C  
ANISOU 4361  CD2 TRP B 562     4543   7142   7125    351  -1374    959       C  
ATOM   4362  NE1 TRP B 562      38.517  93.866 -10.517  1.00 52.41           N  
ANISOU 4362  NE1 TRP B 562     4476   7715   7719    448  -1285   1181       N  
ATOM   4363  CE2 TRP B 562      37.701  93.881  -9.415  1.00 51.96           C  
ANISOU 4363  CE2 TRP B 562     4647   7540   7553    400  -1439   1058       C  
ATOM   4364  CE3 TRP B 562      35.475  94.678  -8.824  1.00 49.14           C  
ANISOU 4364  CE3 TRP B 562     4737   6980   6951    314  -1480    835       C  
ATOM   4365  CZ2 TRP B 562      37.921  93.382  -8.131  1.00 52.11           C  
ANISOU 4365  CZ2 TRP B 562     4711   7525   7560    406  -1625   1032       C  
ATOM   4366  CZ3 TRP B 562      35.694  94.171  -7.536  1.00 50.19           C  
ANISOU 4366  CZ3 TRP B 562     4925   7082   7062    321  -1645    808       C  
ATOM   4367  CH2 TRP B 562      36.907  93.531  -7.206  1.00 51.66           C  
ANISOU 4367  CH2 TRP B 562     4919   7348   7361    362  -1726    904       C  
ATOM   4368  N   TRP B 563      32.871  95.532 -13.960  1.00 46.45           N  
ANISOU 4368  N   TRP B 563     4576   6690   6383    469   -795    795       N  
ATOM   4369  CA  TRP B 563      31.624  96.063 -14.544  1.00 44.75           C  
ANISOU 4369  CA  TRP B 563     4519   6419   6063    460   -749    732       C  
ATOM   4370  C   TRP B 563      30.421  95.219 -14.112  1.00 42.89           C  
ANISOU 4370  C   TRP B 563     4440   6143   5711    529   -765    612       C  
ATOM   4371  O   TRP B 563      29.400  95.764 -13.717  1.00 41.71           O  
ANISOU 4371  O   TRP B 563     4408   5932   5507    491   -817    550       O  
ATOM   4372  CB  TRP B 563      31.690  96.103 -16.067  1.00 44.92           C  
ANISOU 4372  CB  TRP B 563     4519   6497   6053    515   -586    787       C  
ATOM   4373  CG  TRP B 563      30.431  96.720 -16.680  1.00 43.72           C  
ANISOU 4373  CG  TRP B 563     4522   6290   5800    504   -565    735       C  
ATOM   4374  CD1 TRP B 563      29.267  96.086 -16.948  1.00 42.41           C  
ANISOU 4374  CD1 TRP B 563     4489   6106   5516    575   -546    645       C  
ATOM   4375  CD2 TRP B 563      30.235  98.095 -17.038  1.00 43.79           C  
ANISOU 4375  CD2 TRP B 563     4559   6251   5826    413   -581    781       C  
ATOM   4376  NE1 TRP B 563      28.345  96.980 -17.481  1.00 43.16           N  
ANISOU 4376  NE1 TRP B 563     4677   6162   5559    545   -548    635       N  
ATOM   4377  CE2 TRP B 563      28.919  98.221 -17.527  1.00 42.45           C  
ANISOU 4377  CE2 TRP B 563     4537   6046   5546    455   -566    714       C  
ATOM   4378  CE3 TRP B 563      31.047  99.230 -16.993  1.00 44.61           C  
ANISOU 4378  CE3 TRP B 563     4581   6333   6035    293   -616    879       C  
ATOM   4379  CZ2 TRP B 563      28.406  99.430 -17.995  1.00 43.07           C  
ANISOU 4379  CZ2 TRP B 563     4687   6068   5608    406   -576    742       C  
ATOM   4380  CZ3 TRP B 563      30.539 100.426 -17.455  1.00 45.23           C  
ANISOU 4380  CZ3 TRP B 563     4750   6340   6093    230   -624    903       C  
ATOM   4381  CH2 TRP B 563      29.232 100.524 -17.945  1.00 43.50           C  
ANISOU 4381  CH2 TRP B 563     4684   6086   5756    299   -601    833       C  
ATOM   4382  N   SER B 564      30.552  93.891 -14.170  1.00 43.54           N  
ANISOU 4382  N   SER B 564     4523   6258   5759    633   -719    589       N  
ATOM   4383  CA  SER B 564      29.445  93.001 -13.767  1.00 44.17           C  
ANISOU 4383  CA  SER B 564     4745   6296   5738    677   -737    492       C  
ATOM   4384  C   SER B 564      29.160  93.189 -12.274  1.00 42.73           C  
ANISOU 4384  C   SER B 564     4612   6062   5559    618   -866    451       C  
ATOM   4385  O   SER B 564      28.007  93.189 -11.837  1.00 40.17           O  
ANISOU 4385  O   SER B 564     4402   5697   5161    605   -886    386       O  
ATOM   4386  CB  SER B 564      29.776  91.524 -14.083  1.00 46.43           C  
ANISOU 4386  CB  SER B 564     5046   6604   5991    794   -676    482       C  
ATOM   4387  OG  SER B 564      30.044  91.320 -15.467  1.00 47.10           O  
ANISOU 4387  OG  SER B 564     5121   6729   6045    869   -546    512       O  
ATOM   4388  N   PHE B 565      30.228  93.355 -11.499  1.00 41.66           N  
ANISOU 4388  N   PHE B 565     4387   5933   5506    586   -952    497       N  
ATOM   4389  CA  PHE B 565      30.115  93.726 -10.088  1.00 41.83           C  
ANISOU 4389  CA  PHE B 565     4475   5897   5520    523  -1090    464       C  
ATOM   4390  C   PHE B 565      29.316  95.012  -9.867  1.00 40.32           C  
ANISOU 4390  C   PHE B 565     4382   5643   5293    447  -1124    428       C  
ATOM   4391  O   PHE B 565      28.443  95.072  -8.994  1.00 41.44           O  
ANISOU 4391  O   PHE B 565     4657   5733   5354    449  -1162    362       O  
ATOM   4392  CB  PHE B 565      31.517  93.859  -9.472  1.00 43.33           C  
ANISOU 4392  CB  PHE B 565     4537   6109   5817    482  -1202    536       C  
ATOM   4393  CG  PHE B 565      31.512  94.232  -8.012  1.00 43.95           C  
ANISOU 4393  CG  PHE B 565     4711   6118   5869    415  -1368    502       C  
ATOM   4394  CD1 PHE B 565      31.220  93.294  -7.043  1.00 44.89           C  
ANISOU 4394  CD1 PHE B 565     4930   6214   5912    470  -1416    456       C  
ATOM   4395  CD2 PHE B 565      31.838  95.513  -7.606  1.00 45.86           C  
ANISOU 4395  CD2 PHE B 565     4964   6306   6152    296  -1484    518       C  
ATOM   4396  CE1 PHE B 565      31.232  93.638  -5.694  1.00 44.71           C  
ANISOU 4396  CE1 PHE B 565     5022   6126   5839    418  -1566    426       C  
ATOM   4397  CE2 PHE B 565      31.862  95.859  -6.261  1.00 45.88           C  
ANISOU 4397  CE2 PHE B 565     5092   6231   6107    241  -1649    478       C  
ATOM   4398  CZ  PHE B 565      31.535  94.923  -5.310  1.00 45.00           C  
ANISOU 4398  CZ  PHE B 565     5086   6107   5903    309  -1683    430       C  
ATOM   4399  N   GLY B 566      29.600  96.036 -10.656  1.00 41.16           N  
ANISOU 4399  N   GLY B 566     4432   5750   5455    393  -1100    476       N  
ATOM   4400  CA  GLY B 566      28.792  97.272 -10.638  1.00 40.90           C  
ANISOU 4400  CA  GLY B 566     4509   5645   5386    345  -1118    445       C  
ATOM   4401  C   GLY B 566      27.299  97.039 -10.861  1.00 39.35           C  
ANISOU 4401  C   GLY B 566     4421   5444   5086    416  -1040    377       C  
ATOM   4402  O   GLY B 566      26.459  97.573 -10.133  1.00 39.95           O  
ANISOU 4402  O   GLY B 566     4614   5460   5102    420  -1073    324       O  
ATOM   4403  N   VAL B 567      26.979  96.229 -11.862  1.00 39.05           N  
ANISOU 4403  N   VAL B 567     4343   5468   5025    475   -939    383       N  
ATOM   4404  CA  VAL B 567      25.594  95.893 -12.197  1.00 37.56           C  
ANISOU 4404  CA  VAL B 567     4226   5289   4755    526   -883    335       C  
ATOM   4405  C   VAL B 567      24.929  95.189 -11.025  1.00 38.22           C  
ANISOU 4405  C   VAL B 567     4379   5359   4784    545   -912    281       C  
ATOM   4406  O   VAL B 567      23.844  95.551 -10.614  1.00 37.05           O  
ANISOU 4406  O   VAL B 567     4297   5194   4586    560   -904    249       O  
ATOM   4407  CB  VAL B 567      25.503  95.013 -13.458  1.00 37.49           C  
ANISOU 4407  CB  VAL B 567     4186   5336   4722    573   -799    349       C  
ATOM   4408  CG1 VAL B 567      24.056  94.559 -13.742  1.00 37.83           C  
ANISOU 4408  CG1 VAL B 567     4293   5388   4689    599   -776    306       C  
ATOM   4409  CG2 VAL B 567      26.027  95.794 -14.666  1.00 39.15           C  
ANISOU 4409  CG2 VAL B 567     4349   5563   4961    562   -747    410       C  
ATOM   4410  N   LEU B 568      25.607  94.175 -10.498  1.00 39.59           N  
ANISOU 4410  N   LEU B 568     4533   5543   4966    556   -938    283       N  
ATOM   4411  CA  LEU B 568      25.095  93.411  -9.373  1.00 40.07           C  
ANISOU 4411  CA  LEU B 568     4669   5587   4969    570   -964    247       C  
ATOM   4412  C   LEU B 568      24.901  94.298  -8.118  1.00 38.72           C  
ANISOU 4412  C   LEU B 568     4586   5362   4764    548  -1029    221       C  
ATOM   4413  O   LEU B 568      23.883  94.203  -7.442  1.00 37.42           O  
ANISOU 4413  O   LEU B 568     4502   5189   4526    571  -1000    191       O  
ATOM   4414  CB  LEU B 568      26.028  92.227  -9.134  1.00 40.30           C  
ANISOU 4414  CB  LEU B 568     4668   5625   5019    595   -989    265       C  
ATOM   4415  CG  LEU B 568      25.670  91.154  -8.130  1.00 42.21           C  
ANISOU 4415  CG  LEU B 568     4992   5844   5199    613  -1011    245       C  
ATOM   4416  CD1 LEU B 568      26.522  89.918  -8.382  1.00 42.38           C  
ANISOU 4416  CD1 LEU B 568     4984   5872   5246    665  -1013    268       C  
ATOM   4417  CD2 LEU B 568      25.934  91.675  -6.725  1.00 43.34           C  
ANISOU 4417  CD2 LEU B 568     5201   5949   5315    590  -1102    235       C  
ATOM   4418  N   LEU B 569      25.843  95.194  -7.856  1.00 39.33           N  
ANISOU 4418  N   LEU B 569     4653   5401   4890    503  -1111    237       N  
ATOM   4419  CA  LEU B 569      25.740  96.110  -6.700  1.00 40.82           C  
ANISOU 4419  CA  LEU B 569     4967   5513   5029    481  -1193    202       C  
ATOM   4420  C   LEU B 569      24.567  97.077  -6.862  1.00 39.83           C  
ANISOU 4420  C   LEU B 569     4923   5356   4853    515  -1130    171       C  
ATOM   4421  O   LEU B 569      23.768  97.322  -5.930  1.00 39.50           O  
ANISOU 4421  O   LEU B 569     5009   5279   4720    561  -1117    128       O  
ATOM   4422  CB  LEU B 569      27.047  96.908  -6.527  1.00 43.20           C  
ANISOU 4422  CB  LEU B 569     5238   5768   5408    398  -1321    236       C  
ATOM   4423  CG  LEU B 569      27.501  97.366  -5.141  1.00 46.91           C  
ANISOU 4423  CG  LEU B 569     5838   6153   5831    356  -1471    207       C  
ATOM   4424  CD1 LEU B 569      28.253  98.687  -5.221  1.00 49.22           C  
ANISOU 4424  CD1 LEU B 569     6143   6366   6190    254  -1587    230       C  
ATOM   4425  CD2 LEU B 569      26.396  97.452  -4.097  1.00 48.02           C  
ANISOU 4425  CD2 LEU B 569     6176   6243   5825    422  -1444    135       C  
ATOM   4426  N   TYR B 570      24.481  97.655  -8.050  1.00 39.34           N  
ANISOU 4426  N   TYR B 570     4792   5309   4846    506  -1086    199       N  
ATOM   4427  CA  TYR B 570      23.356  98.526  -8.400  1.00 38.01           C  
ANISOU 4427  CA  TYR B 570     4680   5119   4641    556  -1025    183       C  
ATOM   4428  C   TYR B 570      22.041  97.788  -8.120  1.00 38.52           C  
ANISOU 4428  C   TYR B 570     4753   5244   4639    630   -937    161       C  
ATOM   4429  O   TYR B 570      21.128  98.335  -7.507  1.00 39.17           O  
ANISOU 4429  O   TYR B 570     4921   5302   4659    695   -901    135       O  
ATOM   4430  CB  TYR B 570      23.459  98.936  -9.869  1.00 37.04           C  
ANISOU 4430  CB  TYR B 570     4469   5022   4580    540   -986    231       C  
ATOM   4431  CG  TYR B 570      22.383  99.922 -10.326  1.00 36.82           C  
ANISOU 4431  CG  TYR B 570     4496   4968   4525    598   -942    228       C  
ATOM   4432  CD1 TYR B 570      21.083  99.507 -10.582  1.00 35.63           C  
ANISOU 4432  CD1 TYR B 570     4319   4883   4334    673   -867    220       C  
ATOM   4433  CD2 TYR B 570      22.680 101.263 -10.484  1.00 37.47           C  
ANISOU 4433  CD2 TYR B 570     4653   4955   4629    575   -986    241       C  
ATOM   4434  CE1 TYR B 570      20.104 100.411 -11.009  1.00 36.35           C  
ANISOU 4434  CE1 TYR B 570     4439   4960   4410    744   -834    229       C  
ATOM   4435  CE2 TYR B 570      21.725 102.170 -10.897  1.00 38.44           C  
ANISOU 4435  CE2 TYR B 570     4835   5043   4726    648   -950    243       C  
ATOM   4436  CZ  TYR B 570      20.436 101.747 -11.152  1.00 37.44           C  
ANISOU 4436  CZ  TYR B 570     4666   4997   4562    743   -872    238       C  
ATOM   4437  OH  TYR B 570      19.528 102.677 -11.556  1.00 37.91           O  
ANISOU 4437  OH  TYR B 570     4770   5027   4606    830   -845    250       O  
ATOM   4438  N   GLU B 571      21.950  96.534  -8.555  1.00 38.49           N  
ANISOU 4438  N   GLU B 571     4663   5314   4647    621   -900    178       N  
ATOM   4439  CA  GLU B 571      20.713  95.749  -8.341  1.00 37.18           C  
ANISOU 4439  CA  GLU B 571     4487   5205   4434    658   -828    176       C  
ATOM   4440  C   GLU B 571      20.400  95.550  -6.861  1.00 38.24           C  
ANISOU 4440  C   GLU B 571     4719   5318   4491    685   -820    153       C  
ATOM   4441  O   GLU B 571      19.236  95.706  -6.429  1.00 38.86           O  
ANISOU 4441  O   GLU B 571     4816   5425   4521    741   -743    156       O  
ATOM   4442  CB  GLU B 571      20.822  94.393  -9.067  1.00 38.01           C  
ANISOU 4442  CB  GLU B 571     4519   5362   4562    625   -816    196       C  
ATOM   4443  CG  GLU B 571      20.710  94.477 -10.602  1.00 37.79           C  
ANISOU 4443  CG  GLU B 571     4421   5366   4570    618   -799    217       C  
ATOM   4444  CD  GLU B 571      20.912  93.132 -11.297  1.00 38.75           C  
ANISOU 4444  CD  GLU B 571     4519   5512   4690    596   -796    223       C  
ATOM   4445  OE1 GLU B 571      21.515  92.215 -10.696  1.00 41.06           O  
ANISOU 4445  OE1 GLU B 571     4837   5786   4977    588   -814    216       O  
ATOM   4446  OE2 GLU B 571      20.488  92.978 -12.459  1.00 42.13           O  
ANISOU 4446  OE2 GLU B 571     4924   5968   5116    593   -783    233       O  
ATOM   4447  N   MET B 572      21.436  95.219  -6.071  1.00 37.21           N  
ANISOU 4447  N   MET B 572     4647   5144   4346    655   -895    140       N  
ATOM   4448  CA  MET B 572      21.262  95.045  -4.636  1.00 39.57           C  
ANISOU 4448  CA  MET B 572     5071   5412   4550    682   -901    119       C  
ATOM   4449  C   MET B 572      20.722  96.275  -3.960  1.00 40.49           C  
ANISOU 4449  C   MET B 572     5314   5476   4595    746   -880     85       C  
ATOM   4450  O   MET B 572      19.864  96.169  -3.097  1.00 42.24           O  
ANISOU 4450  O   MET B 572     5615   5711   4724    809   -800     79       O  
ATOM   4451  CB  MET B 572      22.562  94.619  -3.946  1.00 38.95           C  
ANISOU 4451  CB  MET B 572     5041   5289   4469    639  -1019    115       C  
ATOM   4452  CG  MET B 572      22.985  93.222  -4.362  1.00 39.44           C  
ANISOU 4452  CG  MET B 572     5014   5394   4577    613  -1021    149       C  
ATOM   4453  SD  MET B 572      24.126  92.410  -3.241  1.00 41.46           S  
ANISOU 4453  SD  MET B 572     5340   5611   4801    602  -1139    159       S  
ATOM   4454  CE  MET B 572      25.616  93.354  -3.517  1.00 43.20           C  
ANISOU 4454  CE  MET B 572     5496   5798   5117    554  -1278    166       C  
ATOM   4455  N   LEU B 573      21.237  97.435  -4.357  1.00 41.95           N  
ANISOU 4455  N   LEU B 573     5526   5594   4817    733   -944     67       N  
ATOM   4456  CA  LEU B 573      20.923  98.694  -3.699  1.00 43.26           C  
ANISOU 4456  CA  LEU B 573     5859   5669   4908    796   -951     23       C  
ATOM   4457  C   LEU B 573      19.589  99.291  -4.156  1.00 43.66           C  
ANISOU 4457  C   LEU B 573     5886   5754   4948    901   -823     30       C  
ATOM   4458  O   LEU B 573      18.883  99.912  -3.366  1.00 43.95           O  
ANISOU 4458  O   LEU B 573     6059   5750   4887   1007   -762      0       O  
ATOM   4459  CB  LEU B 573      22.036  99.702  -3.970  1.00 44.00           C  
ANISOU 4459  CB  LEU B 573     6000   5659   5057    720  -1088     11       C  
ATOM   4460  CG  LEU B 573      23.315  99.411  -3.192  1.00 44.25           C  
ANISOU 4460  CG  LEU B 573     6086   5640   5086    630  -1241      3       C  
ATOM   4461  CD1 LEU B 573      24.452 100.264  -3.729  1.00 45.51           C  
ANISOU 4461  CD1 LEU B 573     6214   5729   5346    521  -1373     25       C  
ATOM   4462  CD2 LEU B 573      23.092  99.660  -1.705  1.00 45.85           C  
ANISOU 4462  CD2 LEU B 573     6526   5762   5134    685  -1278    -55       C  
ATOM   4463  N   ILE B 574      19.255  99.100  -5.425  1.00 42.27           N  
ANISOU 4463  N   ILE B 574     5543   5651   4863    882   -785     74       N  
ATOM   4464  CA  ILE B 574      18.121  99.804  -6.039  1.00 42.61           C  
ANISOU 4464  CA  ILE B 574     5545   5724   4917    976   -699     93       C  
ATOM   4465  C   ILE B 574      16.949  98.886  -6.390  1.00 42.31           C  
ANISOU 4465  C   ILE B 574     5352   5823   4899   1003   -596    143       C  
ATOM   4466  O   ILE B 574      15.824  99.330  -6.425  1.00 43.68           O  
ANISOU 4466  O   ILE B 574     5492   6041   5062   1106   -509    166       O  
ATOM   4467  CB  ILE B 574      18.633 100.615  -7.263  1.00 44.05           C  
ANISOU 4467  CB  ILE B 574     5692   5863   5182    934   -761    110       C  
ATOM   4468  CG1 ILE B 574      19.568 101.714  -6.753  1.00 45.09           C  
ANISOU 4468  CG1 ILE B 574     5994   5844   5292    906   -861     71       C  
ATOM   4469  CG2 ILE B 574      17.478 101.232  -8.081  1.00 43.93           C  
ANISOU 4469  CG2 ILE B 574     5616   5887   5187   1030   -690    144       C  
ATOM   4470  CD1 ILE B 574      20.575 102.164  -7.767  1.00 47.44           C  
ANISOU 4470  CD1 ILE B 574     6242   6100   5682    800   -943    105       C  
ATOM   4471  N   GLY B 575      17.192  97.597  -6.594  1.00 41.86           N  
ANISOU 4471  N   GLY B 575     5203   5830   4872    913   -610    166       N  
ATOM   4472  CA  GLY B 575      16.102  96.655  -6.885  1.00 42.21           C  
ANISOU 4472  CA  GLY B 575     5112   5987   4937    906   -537    219       C  
ATOM   4473  C   GLY B 575      15.675  96.593  -8.336  1.00 40.96           C  
ANISOU 4473  C   GLY B 575     4820   5887   4856    877   -558    256       C  
ATOM   4474  O   GLY B 575      14.639  96.037  -8.639  1.00 43.15           O  
ANISOU 4474  O   GLY B 575     4982   6254   5158    868   -518    306       O  
ATOM   4475  N   GLN B 576      16.483  97.199  -9.204  1.00 40.61           N  
ANISOU 4475  N   GLN B 576     4797   5788   4845    855   -625    239       N  
ATOM   4476  CA  GLN B 576      16.327  97.232 -10.654  1.00 41.24           C  
ANISOU 4476  CA  GLN B 576     4793   5901   4973    829   -657    269       C  
ATOM   4477  C   GLN B 576      17.697  97.118 -11.254  1.00 37.45           C  
ANISOU 4477  C   GLN B 576     4347   5369   4512    761   -717    252       C  
ATOM   4478  O   GLN B 576      18.666  97.528 -10.627  1.00 36.66           O  
ANISOU 4478  O   GLN B 576     4322   5199   4408    749   -744    226       O  
ATOM   4479  CB  GLN B 576      15.923  98.653 -11.090  1.00 46.26           C  
ANISOU 4479  CB  GLN B 576     5451   6507   5617    916   -652    281       C  
ATOM   4480  CG  GLN B 576      14.510  98.924 -11.417  1.00 50.40           C  
ANISOU 4480  CG  GLN B 576     5882   7111   6158    997   -611    329       C  
ATOM   4481  CD  GLN B 576      14.438 100.073 -12.433  1.00 55.32           C  
ANISOU 4481  CD  GLN B 576     6523   7695   6798   1052   -646    351       C  
ATOM   4482  OE1 GLN B 576      14.026  99.867 -13.574  1.00 56.16           O  
ANISOU 4482  OE1 GLN B 576     6550   7858   6930   1030   -686    392       O  
ATOM   4483  NE2 GLN B 576      14.888 101.272 -12.032  1.00 54.07           N  
ANISOU 4483  NE2 GLN B 576     6495   7426   6620   1115   -644    324       N  
ATOM   4484  N   SER B 577      17.772  96.645 -12.485  1.00 36.53           N  
ANISOU 4484  N   SER B 577     4177   5286   4414    722   -738    273       N  
ATOM   4485  CA  SER B 577      18.997  96.660 -13.252  1.00 38.09           C  
ANISOU 4485  CA  SER B 577     4392   5450   4627    683   -765    275       C  
ATOM   4486  C   SER B 577      19.267  98.074 -13.785  1.00 38.79           C  
ANISOU 4486  C   SER B 577     4514   5491   4734    707   -773    297       C  
ATOM   4487  O   SER B 577      18.333  98.848 -14.012  1.00 37.80           O  
ANISOU 4487  O   SER B 577     4390   5368   4602    764   -766    313       O  
ATOM   4488  CB  SER B 577      18.907  95.644 -14.388  1.00 40.44           C  
ANISOU 4488  CB  SER B 577     4660   5792   4910    652   -772    286       C  
ATOM   4489  OG  SER B 577      18.900  94.330 -13.823  1.00 42.91           O  
ANISOU 4489  OG  SER B 577     4974   6117   5211    618   -774    266       O  
ATOM   4490  N   PRO B 578      20.545  98.427 -13.957  1.00 36.93           N  
ANISOU 4490  N   PRO B 578     4297   5208   4527    665   -789    308       N  
ATOM   4491  CA  PRO B 578      20.891  99.780 -14.404  1.00 37.72           C  
ANISOU 4491  CA  PRO B 578     4439   5245   4649    663   -802    341       C  
ATOM   4492  C   PRO B 578      20.644 100.014 -15.899  1.00 39.31           C  
ANISOU 4492  C   PRO B 578     4626   5475   4835    676   -781    390       C  
ATOM   4493  O   PRO B 578      20.373 101.137 -16.310  1.00 38.46           O  
ANISOU 4493  O   PRO B 578     4565   5318   4727    701   -789    422       O  
ATOM   4494  CB  PRO B 578      22.384  99.904 -14.054  1.00 38.13           C  
ANISOU 4494  CB  PRO B 578     4485   5252   4750    588   -831    355       C  
ATOM   4495  CG  PRO B 578      22.890  98.510 -13.975  1.00 37.40           C  
ANISOU 4495  CG  PRO B 578     4327   5224   4659    573   -815    344       C  
ATOM   4496  CD  PRO B 578      21.723  97.619 -13.613  1.00 36.90           C  
ANISOU 4496  CD  PRO B 578     4269   5205   4545    617   -799    301       C  
ATOM   4497  N   PHE B 579      20.699  98.959 -16.699  1.00 39.49           N  
ANISOU 4497  N   PHE B 579     4609   5564   4831    667   -759    395       N  
ATOM   4498  CA  PHE B 579      20.517  99.071 -18.151  1.00 39.35           C  
ANISOU 4498  CA  PHE B 579     4607   5572   4771    682   -745    438       C  
ATOM   4499  C   PHE B 579      19.300  98.252 -18.546  1.00 39.75           C  
ANISOU 4499  C   PHE B 579     4646   5684   4773    707   -774    417       C  
ATOM   4500  O   PHE B 579      18.989  97.266 -17.889  1.00 40.58           O  
ANISOU 4500  O   PHE B 579     4721   5816   4880    691   -783    378       O  
ATOM   4501  CB  PHE B 579      21.800  98.592 -18.827  1.00 37.77           C  
ANISOU 4501  CB  PHE B 579     4397   5386   4566    652   -693    466       C  
ATOM   4502  CG  PHE B 579      23.016  99.327 -18.337  1.00 37.18           C  
ANISOU 4502  CG  PHE B 579     4295   5265   4565    602   -681    503       C  
ATOM   4503  CD1 PHE B 579      23.140 100.681 -18.569  1.00 37.72           C  
ANISOU 4503  CD1 PHE B 579     4400   5272   4659    579   -691    555       C  
ATOM   4504  CD2 PHE B 579      24.008  98.676 -17.618  1.00 37.44           C  
ANISOU 4504  CD2 PHE B 579     4268   5309   4647    572   -675    492       C  
ATOM   4505  CE1 PHE B 579      24.240 101.383 -18.109  1.00 39.56           C  
ANISOU 4505  CE1 PHE B 579     4610   5451   4969    504   -703    598       C  
ATOM   4506  CE2 PHE B 579      25.102  99.363 -17.136  1.00 37.82           C  
ANISOU 4506  CE2 PHE B 579     4274   5320   4775    508   -693    535       C  
ATOM   4507  CZ  PHE B 579      25.219 100.723 -17.377  1.00 39.15           C  
ANISOU 4507  CZ  PHE B 579     4478   5423   4973    462   -711    589       C  
ATOM   4508  N   HIS B 580      18.628  98.674 -19.606  1.00 41.49           N  
ANISOU 4508  N   HIS B 580     4892   5920   4951    736   -799    453       N  
ATOM   4509  CA  HIS B 580      17.289  98.194 -19.949  1.00 42.54           C  
ANISOU 4509  CA  HIS B 580     4997   6109   5055    751   -861    451       C  
ATOM   4510  C   HIS B 580      17.101  98.153 -21.451  1.00 41.79           C  
ANISOU 4510  C   HIS B 580     4966   6031   4881    758   -899    484       C  
ATOM   4511  O   HIS B 580      17.678  98.950 -22.182  1.00 41.26           O  
ANISOU 4511  O   HIS B 580     4961   5931   4784    778   -869    527       O  
ATOM   4512  CB  HIS B 580      16.205  99.136 -19.375  1.00 45.74           C  
ANISOU 4512  CB  HIS B 580     5352   6521   5505    813   -882    473       C  
ATOM   4513  CG  HIS B 580      16.275  99.283 -17.888  1.00 49.67           C  
ANISOU 4513  CG  HIS B 580     5821   6995   6053    826   -840    438       C  
ATOM   4514  ND1 HIS B 580      15.717  98.363 -17.024  1.00 51.47           N  
ANISOU 4514  ND1 HIS B 580     5984   7273   6296    807   -834    412       N  
ATOM   4515  CD2 HIS B 580      16.863 100.227 -17.108  1.00 50.97           C  
ANISOU 4515  CD2 HIS B 580     6038   7084   6245    850   -809    428       C  
ATOM   4516  CE1 HIS B 580      15.953  98.732 -15.775  1.00 52.66           C  
ANISOU 4516  CE1 HIS B 580     6152   7386   6468    832   -790    385       C  
ATOM   4517  NE2 HIS B 580      16.656  99.853 -15.798  1.00 52.09           N  
ANISOU 4517  NE2 HIS B 580     6157   7232   6401    857   -784    388       N  
ATOM   4518  N   GLY B 581      16.247  97.239 -21.893  1.00 40.24           N  
ANISOU 4518  N   GLY B 581     4763   5881   4643    733   -974    471       N  
ATOM   4519  CA  GLY B 581      15.862  97.121 -23.282  1.00 41.60           C  
ANISOU 4519  CA  GLY B 581     5017   6068   4721    737  -1045    496       C  
ATOM   4520  C   GLY B 581      14.788  96.052 -23.407  1.00 43.39           C  
ANISOU 4520  C   GLY B 581     5213   6339   4932    680  -1159    478       C  
ATOM   4521  O   GLY B 581      14.716  95.136 -22.556  1.00 41.18           O  
ANISOU 4521  O   GLY B 581     4883   6065   4696    627  -1153    439       O  
ATOM   4522  N   GLN B 582      13.956  96.196 -24.427  1.00 45.49           N  
ANISOU 4522  N   GLN B 582     5511   6632   5140    682  -1274    515       N  
ATOM   4523  CA  GLN B 582      12.892  95.247 -24.751  1.00 50.62           C  
ANISOU 4523  CA  GLN B 582     6139   7321   5773    604  -1422    512       C  
ATOM   4524  C   GLN B 582      13.415  94.049 -25.511  1.00 50.53           C  
ANISOU 4524  C   GLN B 582     6305   7255   5639    548  -1459    453       C  
ATOM   4525  O   GLN B 582      12.723  93.057 -25.626  1.00 54.02           O  
ANISOU 4525  O   GLN B 582     6758   7698   6066    457  -1582    435       O  
ATOM   4526  CB  GLN B 582      11.818  95.913 -25.619  1.00 53.60           C  
ANISOU 4526  CB  GLN B 582     6488   7747   6130    630  -1559    582       C  
ATOM   4527  CG  GLN B 582      11.081  97.030 -24.915  1.00 57.49           C  
ANISOU 4527  CG  GLN B 582     6805   8295   6743    708  -1537    647       C  
ATOM   4528  CD  GLN B 582      10.423  96.538 -23.652  1.00 60.30           C  
ANISOU 4528  CD  GLN B 582     6980   8710   7221    668  -1514    647       C  
ATOM   4529  OE1 GLN B 582       9.346  95.955 -23.695  1.00 68.86           O  
ANISOU 4529  OE1 GLN B 582     7949   9866   8349    600  -1631    686       O  
ATOM   4530  NE2 GLN B 582      11.079  96.745 -22.519  1.00 62.55           N  
ANISOU 4530  NE2 GLN B 582     7241   8964   7559    700  -1368    613       N  
ATOM   4531  N   ASP B 583      14.602  94.183 -26.088  1.00 48.93           N  
ANISOU 4531  N   ASP B 583     6247   7000   5342    606  -1355    430       N  
ATOM   4532  CA  ASP B 583      15.310  93.072 -26.691  1.00 47.50           C  
ANISOU 4532  CA  ASP B 583     6250   6758   5038    596  -1340    368       C  
ATOM   4533  C   ASP B 583      16.776  93.299 -26.468  1.00 47.01           C  
ANISOU 4533  C   ASP B 583     6215   6669   4976    669  -1151    358       C  
ATOM   4534  O   ASP B 583      17.168  94.321 -25.890  1.00 43.40           O  
ANISOU 4534  O   ASP B 583     5643   6234   4612    702  -1062    401       O  
ATOM   4535  CB  ASP B 583      14.961  92.898 -28.180  1.00 49.61           C  
ANISOU 4535  CB  ASP B 583     6712   7002   5134    600  -1456    368       C  
ATOM   4536  CG  ASP B 583      15.324  94.104 -29.065  1.00 49.02           C  
ANISOU 4536  CG  ASP B 583     6701   6940   4984    688  -1398    431       C  
ATOM   4537  OD1 ASP B 583      16.036  95.051 -28.683  1.00 46.23           O  
ANISOU 4537  OD1 ASP B 583     6268   6597   4699    744  -1256    473       O  
ATOM   4538  OD2 ASP B 583      14.883  94.065 -30.216  1.00 52.92           O  
ANISOU 4538  OD2 ASP B 583     7348   7421   5335    693  -1512    442       O  
ATOM   4539  N   GLU B 584      17.585  92.345 -26.912  1.00 45.94           N  
ANISOU 4539  N   GLU B 584     6231   6484   4738    698  -1095    307       N  
ATOM   4540  CA  GLU B 584      19.003  92.383 -26.673  1.00 45.98           C  
ANISOU 4540  CA  GLU B 584     6233   6478   4757    771   -915    309       C  
ATOM   4541  C   GLU B 584      19.724  93.563 -27.358  1.00 43.68           C  
ANISOU 4541  C   GLU B 584     5948   6212   4434    837   -802    383       C  
ATOM   4542  O   GLU B 584      20.592  94.176 -26.761  1.00 42.79           O  
ANISOU 4542  O   GLU B 584     5720   6117   4421    853   -686    423       O  
ATOM   4543  CB  GLU B 584      19.640  91.050 -27.120  1.00 48.14           C  
ANISOU 4543  CB  GLU B 584     6684   6692   4914    817   -876    243       C  
ATOM   4544  CG  GLU B 584      20.530  90.451 -26.083  1.00 48.74           C  
ANISOU 4544  CG  GLU B 584     6679   6754   5083    841   -777    218       C  
ATOM   4545  CD  GLU B 584      20.982  89.039 -26.424  1.00 50.35           C  
ANISOU 4545  CD  GLU B 584     7070   6882   5177    897   -758    147       C  
ATOM   4546  OE1 GLU B 584      20.875  88.179 -25.541  1.00 54.57           O  
ANISOU 4546  OE1 GLU B 584     7583   7376   5775    858   -800    106       O  
ATOM   4547  OE2 GLU B 584      21.433  88.793 -27.556  1.00 51.19           O  
ANISOU 4547  OE2 GLU B 584     7362   6961   5126    989   -698    135       O  
ATOM   4548  N   GLU B 585      19.389  93.837 -28.609  1.00 44.47           N  
ANISOU 4548  N   GLU B 585     6196   6308   4392    865   -843    408       N  
ATOM   4549  CA  GLU B 585      19.931  94.999 -29.336  1.00 45.46           C  
ANISOU 4549  CA  GLU B 585     6346   6451   4474    916   -744    495       C  
ATOM   4550  C   GLU B 585      19.742  96.281 -28.488  1.00 44.54           C  
ANISOU 4550  C   GLU B 585     6044   6354   4523    878   -747    556       C  
ATOM   4551  O   GLU B 585      20.677  97.049 -28.314  1.00 41.79           O  
ANISOU 4551  O   GLU B 585     5635   6008   4235    891   -622    617       O  
ATOM   4552  CB  GLU B 585      19.269  95.146 -30.724  1.00 47.93           C  
ANISOU 4552  CB  GLU B 585     6854   6752   4602    941   -837    514       C  
ATOM   4553  CG  GLU B 585      19.984  96.087 -31.691  1.00 49.75           C  
ANISOU 4553  CG  GLU B 585     7174   6991   4735   1006   -708    608       C  
ATOM   4554  CD  GLU B 585      19.186  96.449 -32.955  1.00 51.17           C  
ANISOU 4554  CD  GLU B 585     7542   7159   4740   1027   -828    641       C  
ATOM   4555  OE1 GLU B 585      18.073  95.942 -33.189  1.00 53.36           O  
ANISOU 4555  OE1 GLU B 585     7884   7425   4963    988  -1029    591       O  
ATOM   4556  OE2 GLU B 585      19.674  97.266 -33.740  1.00 51.37           O  
ANISOU 4556  OE2 GLU B 585     7652   7187   4679   1076   -729    729       O  
ATOM   4557  N   GLU B 586      18.543  96.492 -27.946  1.00 44.48           N  
ANISOU 4557  N   GLU B 586     5950   6357   4590    834   -889    543       N  
ATOM   4558  CA  GLU B 586      18.270  97.708 -27.158  1.00 43.81           C  
ANISOU 4558  CA  GLU B 586     5727   6275   4640    826   -892    592       C  
ATOM   4559  C   GLU B 586      19.061  97.668 -25.850  1.00 41.80           C  
ANISOU 4559  C   GLU B 586     5348   6012   4520    802   -802    568       C  
ATOM   4560  O   GLU B 586      19.710  98.660 -25.460  1.00 40.06           O  
ANISOU 4560  O   GLU B 586     5078   5768   4374    800   -732    616       O  
ATOM   4561  CB  GLU B 586      16.758  97.873 -26.886  1.00 44.36           C  
ANISOU 4561  CB  GLU B 586     5724   6372   4755    812  -1048    590       C  
ATOM   4562  CG  GLU B 586      16.396  99.129 -26.083  1.00 44.36           C  
ANISOU 4562  CG  GLU B 586     5610   6365   4877    839  -1042    634       C  
ATOM   4563  CD  GLU B 586      14.903  99.371 -25.962  1.00 46.69           C  
ANISOU 4563  CD  GLU B 586     5822   6705   5213    860  -1175    655       C  
ATOM   4564  OE1 GLU B 586      14.089  98.482 -26.347  1.00 46.09           O  
ANISOU 4564  OE1 GLU B 586     5740   6674   5096    822  -1290    636       O  
ATOM   4565  OE2 GLU B 586      14.534 100.490 -25.529  1.00 48.00           O  
ANISOU 4565  OE2 GLU B 586     5930   6856   5451    918  -1169    698       O  
ATOM   4566  N   LEU B 587      19.038  96.516 -25.177  1.00 40.64           N  
ANISOU 4566  N   LEU B 587     5167   5873   4399    774   -817    498       N  
ATOM   4567  CA  LEU B 587      19.779  96.366 -23.933  1.00 40.34           C  
ANISOU 4567  CA  LEU B 587     5027   5827   4472    754   -751    474       C  
ATOM   4568  C   LEU B 587      21.280  96.649 -24.128  1.00 39.64           C  
ANISOU 4568  C   LEU B 587     4937   5730   4394    774   -619    516       C  
ATOM   4569  O   LEU B 587      21.878  97.343 -23.321  1.00 37.50           O  
ANISOU 4569  O   LEU B 587     4577   5445   4226    749   -584    543       O  
ATOM   4570  CB  LEU B 587      19.589  94.965 -23.334  1.00 40.98           C  
ANISOU 4570  CB  LEU B 587     5103   5909   4556    728   -784    402       C  
ATOM   4571  CG  LEU B 587      20.335  94.628 -22.049  1.00 40.55           C  
ANISOU 4571  CG  LEU B 587     4963   5845   4597    714   -732    378       C  
ATOM   4572  CD1 LEU B 587      20.053  95.628 -20.932  1.00 40.53           C  
ANISOU 4572  CD1 LEU B 587     4858   5840   4699    694   -746    394       C  
ATOM   4573  CD2 LEU B 587      19.966  93.214 -21.589  1.00 40.36           C  
ANISOU 4573  CD2 LEU B 587     4964   5810   4558    686   -779    316       C  
ATOM   4574  N   PHE B 588      21.864  96.119 -25.199  1.00 39.61           N  
ANISOU 4574  N   PHE B 588     5034   5735   4279    819   -549    527       N  
ATOM   4575  CA  PHE B 588      23.282  96.356 -25.497  1.00 41.26           C  
ANISOU 4575  CA  PHE B 588     5218   5958   4500    848   -401    589       C  
ATOM   4576  C   PHE B 588      23.591  97.833 -25.783  1.00 41.92           C  
ANISOU 4576  C   PHE B 588     5269   6033   4624    819   -362    689       C  
ATOM   4577  O   PHE B 588      24.570  98.371 -25.282  1.00 42.79           O  
ANISOU 4577  O   PHE B 588     5275   6144   4840    783   -295    746       O  
ATOM   4578  CB  PHE B 588      23.747  95.442 -26.638  1.00 42.57           C  
ANISOU 4578  CB  PHE B 588     5522   6138   4515    931   -315    581       C  
ATOM   4579  CG  PHE B 588      23.792  93.960 -26.263  1.00 44.11           C  
ANISOU 4579  CG  PHE B 588     5758   6317   4684    965   -331    490       C  
ATOM   4580  CD1 PHE B 588      23.667  93.537 -24.942  1.00 44.21           C  
ANISOU 4580  CD1 PHE B 588     5661   6319   4817    918   -393    442       C  
ATOM   4581  CD2 PHE B 588      24.016  93.000 -27.232  1.00 47.06           C  
ANISOU 4581  CD2 PHE B 588     6304   6675   4900   1053   -278    455       C  
ATOM   4582  CE1 PHE B 588      23.742  92.188 -24.609  1.00 45.96           C  
ANISOU 4582  CE1 PHE B 588     5936   6511   5012    948   -407    370       C  
ATOM   4583  CE2 PHE B 588      24.114  91.649 -26.896  1.00 47.42           C  
ANISOU 4583  CE2 PHE B 588     6416   6683   4919   1091   -293    374       C  
ATOM   4584  CZ  PHE B 588      23.963  91.248 -25.594  1.00 46.44           C  
ANISOU 4584  CZ  PHE B 588     6173   6545   4926   1034   -361    335       C  
ATOM   4585  N   HIS B 589      22.736  98.492 -26.554  1.00 41.21           N  
ANISOU 4585  N   HIS B 589     5273   5927   4457    827   -422    717       N  
ATOM   4586  CA  HIS B 589      22.830  99.951 -26.696  1.00 41.68           C  
ANISOU 4586  CA  HIS B 589     5322   5951   4561    796   -412    808       C  
ATOM   4587  C   HIS B 589      22.837 100.684 -25.343  1.00 40.04           C  
ANISOU 4587  C   HIS B 589     5000   5699   4513    736   -463    800       C  
ATOM   4588  O   HIS B 589      23.683 101.560 -25.098  1.00 39.92           O  
ANISOU 4588  O   HIS B 589     4939   5650   4579    682   -414    872       O  
ATOM   4589  CB  HIS B 589      21.681 100.467 -27.563  1.00 42.81           C  
ANISOU 4589  CB  HIS B 589     5583   6077   4603    829   -505    827       C  
ATOM   4590  CG  HIS B 589      21.658 101.959 -27.697  1.00 43.67           C  
ANISOU 4590  CG  HIS B 589     5709   6129   4752    810   -510    920       C  
ATOM   4591  ND1 HIS B 589      20.835 102.763 -26.933  1.00 42.72           N  
ANISOU 4591  ND1 HIS B 589     5551   5961   4719    806   -611    908       N  
ATOM   4592  CD2 HIS B 589      22.373 102.792 -28.489  1.00 45.22           C  
ANISOU 4592  CD2 HIS B 589     5968   6301   4911    798   -419   1032       C  
ATOM   4593  CE1 HIS B 589      21.045 104.029 -27.246  1.00 43.92           C  
ANISOU 4593  CE1 HIS B 589     5758   6044   4885    795   -595    999       C  
ATOM   4594  NE2 HIS B 589      21.963 104.075 -28.198  1.00 46.46           N  
ANISOU 4594  NE2 HIS B 589     6138   6379   5134    777   -484   1081       N  
ATOM   4595  N   SER B 590      21.912 100.302 -24.459  1.00 38.41           N  
ANISOU 4595  N   SER B 590     4756   5492   4345    740   -562    717       N  
ATOM   4596  CA  SER B 590      21.800 100.936 -23.142  1.00 38.05           C  
ANISOU 4596  CA  SER B 590     4639   5399   4418    705   -608    695       C  
ATOM   4597  C   SER B 590      23.088 100.753 -22.326  1.00 38.83           C  
ANISOU 4597  C   SER B 590     4652   5493   4608    648   -555    699       C  
ATOM   4598  O   SER B 590      23.619 101.720 -21.763  1.00 37.73           O  
ANISOU 4598  O   SER B 590     4491   5293   4551    593   -564    737       O  
ATOM   4599  CB  SER B 590      20.584 100.383 -22.383  1.00 37.57           C  
ANISOU 4599  CB  SER B 590     4548   5359   4366    732   -693    615       C  
ATOM   4600  OG  SER B 590      20.562 100.845 -21.048  1.00 38.49           O  
ANISOU 4600  OG  SER B 590     4617   5434   4572    716   -716    586       O  
ATOM   4601  N   ILE B 591      23.603  99.519 -22.298  1.00 38.53           N  
ANISOU 4601  N   ILE B 591     4576   5510   4553    663   -510    663       N  
ATOM   4602  CA  ILE B 591      24.864  99.252 -21.654  1.00 39.60           C  
ANISOU 4602  CA  ILE B 591     4614   5657   4774    625   -463    681       C  
ATOM   4603  C   ILE B 591      26.026 100.078 -22.227  1.00 41.33           C  
ANISOU 4603  C   ILE B 591     4789   5875   5037    580   -380    797       C  
ATOM   4604  O   ILE B 591      26.905 100.514 -21.473  1.00 41.50           O  
ANISOU 4604  O   ILE B 591     4717   5878   5172    506   -393    836       O  
ATOM   4605  CB  ILE B 591      25.232  97.755 -21.744  1.00 40.29           C  
ANISOU 4605  CB  ILE B 591     4686   5800   4821    679   -415    636       C  
ATOM   4606  CG1 ILE B 591      24.278  96.938 -20.865  1.00 39.98           C  
ANISOU 4606  CG1 ILE B 591     4665   5751   4774    687   -504    537       C  
ATOM   4607  CG2 ILE B 591      26.658  97.537 -21.272  1.00 40.73           C  
ANISOU 4607  CG2 ILE B 591     4621   5883   4969    662   -355    682       C  
ATOM   4608  CD1 ILE B 591      24.286  95.460 -21.163  1.00 40.89           C  
ANISOU 4608  CD1 ILE B 591     4826   5891   4819    741   -481    485       C  
ATOM   4609  N   ARG B 592      26.062 100.238 -23.546  1.00 42.40           N  
ANISOU 4609  N   ARG B 592     4991   6034   5081    616   -298    859       N  
ATOM   4610  CA  ARG B 592      27.141 101.001 -24.194  1.00 45.42           C  
ANISOU 4610  CA  ARG B 592     5331   6428   5498    570   -195    991       C  
ATOM   4611  C   ARG B 592      27.002 102.521 -24.017  1.00 46.49           C  
ANISOU 4611  C   ARG B 592     5496   6470   5696    478   -258   1057       C  
ATOM   4612  O   ARG B 592      28.002 103.218 -24.059  1.00 47.08           O  
ANISOU 4612  O   ARG B 592     5498   6532   5856    389   -211   1166       O  
ATOM   4613  CB  ARG B 592      27.212 100.685 -25.695  1.00 47.42           C  
ANISOU 4613  CB  ARG B 592     5678   6732   5605    650    -71   1043       C  
ATOM   4614  CG  ARG B 592      27.886  99.356 -26.016  1.00 48.98           C  
ANISOU 4614  CG  ARG B 592     5846   7011   5750    742     42   1021       C  
ATOM   4615  CD  ARG B 592      28.018  99.126 -27.510  1.00 50.40           C  
ANISOU 4615  CD  ARG B 592     6155   7232   5763    834    177   1073       C  
ATOM   4616  NE  ARG B 592      26.715  99.078 -28.161  1.00 52.11           N  
ANISOU 4616  NE  ARG B 592     6561   7408   5830    872     81   1006       N  
ATOM   4617  CZ  ARG B 592      26.191 100.038 -28.927  1.00 54.34           C  
ANISOU 4617  CZ  ARG B 592     6950   7655   6040    855     58   1067       C  
ATOM   4618  NH1 ARG B 592      26.853 101.167 -29.185  1.00 56.56           N  
ANISOU 4618  NH1 ARG B 592     7188   7926   6377    792    135   1201       N  
ATOM   4619  NH2 ARG B 592      24.982  99.862 -29.455  1.00 54.08           N  
ANISOU 4619  NH2 ARG B 592     7070   7596   5880    895    -54   1004       N  
ATOM   4620  N   MET B 593      25.782 103.029 -23.811  1.00 46.85           N  
ANISOU 4620  N   MET B 593     5645   6448   5707    500   -364    998       N  
ATOM   4621  CA  MET B 593      25.505 104.473 -24.002  1.00 49.07           C  
ANISOU 4621  CA  MET B 593     6012   6627   6004    455   -409   1066       C  
ATOM   4622  C   MET B 593      24.797 105.208 -22.850  1.00 48.22           C  
ANISOU 4622  C   MET B 593     5947   6415   5959    441   -538   1000       C  
ATOM   4623  O   MET B 593      25.000 106.405 -22.670  1.00 47.98           O  
ANISOU 4623  O   MET B 593     5976   6274   5981    375   -578   1057       O  
ATOM   4624  CB  MET B 593      24.646 104.661 -25.254  1.00 51.09           C  
ANISOU 4624  CB  MET B 593     6398   6889   6123    535   -395   1095       C  
ATOM   4625  CG  MET B 593      25.286 104.180 -26.557  1.00 54.66           C  
ANISOU 4625  CG  MET B 593     6873   7420   6473    563   -258   1172       C  
ATOM   4626  SD  MET B 593      26.861 104.968 -26.974  1.00 60.16           S  
ANISOU 4626  SD  MET B 593     7498   8113   7246    453   -119   1347       S  
ATOM   4627  CE  MET B 593      26.318 106.633 -27.339  1.00 60.24           C  
ANISOU 4627  CE  MET B 593     7655   7982   7249    403   -191   1437       C  
ATOM   4628  N   ASP B 594      23.943 104.514 -22.103  1.00 46.16           N  
ANISOU 4628  N   ASP B 594     5673   6181   5683    506   -596    887       N  
ATOM   4629  CA  ASP B 594      23.052 105.177 -21.133  1.00 47.64           C  
ANISOU 4629  CA  ASP B 594     5921   6282   5896    538   -691    824       C  
ATOM   4630  C   ASP B 594      23.841 105.598 -19.859  1.00 46.16           C  
ANISOU 4630  C   ASP B 594     5716   6015   5806    448   -742    805       C  
ATOM   4631  O   ASP B 594      24.803 104.946 -19.456  1.00 43.66           O  
ANISOU 4631  O   ASP B 594     5299   5746   5542    382   -725    804       O  
ATOM   4632  CB  ASP B 594      21.903 104.236 -20.689  1.00 46.76           C  
ANISOU 4632  CB  ASP B 594     5781   6243   5743    630   -721    725       C  
ATOM   4633  CG  ASP B 594      20.690 104.203 -21.633  1.00 49.61           C  
ANISOU 4633  CG  ASP B 594     6184   6644   6020    722   -740    735       C  
ATOM   4634  OD1 ASP B 594      20.625 104.916 -22.677  1.00 46.68           O  
ANISOU 4634  OD1 ASP B 594     5888   6243   5603    736   -733    812       O  
ATOM   4635  OD2 ASP B 594      19.738 103.428 -21.256  1.00 47.69           O  
ANISOU 4635  OD2 ASP B 594     5895   6465   5760    775   -772    670       O  
ATOM   4636  N   ASN B 595      23.392 106.674 -19.230  1.00 47.24           N  
ANISOU 4636  N   ASN B 595     5965   6025   5959    458   -814    786       N  
ATOM   4637  CA  ASN B 595      23.897 107.101 -17.921  1.00 50.36           C  
ANISOU 4637  CA  ASN B 595     6396   6320   6415    389   -892    744       C  
ATOM   4638  C   ASN B 595      23.027 106.449 -16.852  1.00 47.69           C  
ANISOU 4638  C   ASN B 595     6062   6017   6040    485   -913    628       C  
ATOM   4639  O   ASN B 595      21.811 106.667 -16.854  1.00 48.08           O  
ANISOU 4639  O   ASN B 595     6170   6060   6036    608   -907    593       O  
ATOM   4640  CB  ASN B 595      23.802 108.630 -17.801  1.00 53.20           C  
ANISOU 4640  CB  ASN B 595     6927   6499   6787    365   -959    776       C  
ATOM   4641  CG  ASN B 595      24.421 109.340 -18.989  1.00 57.38           C  
ANISOU 4641  CG  ASN B 595     7471   6990   7338    280   -926    908       C  
ATOM   4642  OD1 ASN B 595      23.726 109.732 -19.952  1.00 61.74           O  
ANISOU 4642  OD1 ASN B 595     8089   7538   7831    360   -890    953       O  
ATOM   4643  ND2 ASN B 595      25.736 109.463 -18.960  1.00 57.29           N  
ANISOU 4643  ND2 ASN B 595     7387   6966   7413    116   -934    984       N  
ATOM   4644  N   PRO B 596      23.618 105.641 -15.954  1.00 46.68           N  
ANISOU 4644  N   PRO B 596     5863   5931   5941    437   -933    581       N  
ATOM   4645  CA  PRO B 596      22.767 104.971 -14.974  1.00 45.53           C  
ANISOU 4645  CA  PRO B 596     5726   5822   5749    527   -937    486       C  
ATOM   4646  C   PRO B 596      22.036 105.953 -14.062  1.00 45.54           C  
ANISOU 4646  C   PRO B 596     5888   5701   5713    599   -982    432       C  
ATOM   4647  O   PRO B 596      22.591 106.960 -13.667  1.00 47.91           O  
ANISOU 4647  O   PRO B 596     6307   5860   6034    537  -1054    439       O  
ATOM   4648  CB  PRO B 596      23.745 104.085 -14.186  1.00 46.61           C  
ANISOU 4648  CB  PRO B 596     5784   6001   5923    449   -965    463       C  
ATOM   4649  CG  PRO B 596      24.972 103.970 -15.035  1.00 47.14           C  
ANISOU 4649  CG  PRO B 596     5743   6107   6058    348   -945    552       C  
ATOM   4650  CD  PRO B 596      25.029 105.216 -15.860  1.00 48.42           C  
ANISOU 4650  CD  PRO B 596     5975   6184   6235    313   -945    626       C  
ATOM   4651  N   PHE B 597      20.778 105.663 -13.759  1.00 43.65           N  
ANISOU 4651  N   PHE B 597     5654   5511   5418    733   -938    384       N  
ATOM   4652  CA  PHE B 597      19.973 106.507 -12.889  1.00 43.00           C  
ANISOU 4652  CA  PHE B 597     5720   5329   5286    846   -946    334       C  
ATOM   4653  C   PHE B 597      20.279 106.210 -11.421  1.00 43.01           C  
ANISOU 4653  C   PHE B 597     5793   5292   5253    832   -979    258       C  
ATOM   4654  O   PHE B 597      20.271 105.066 -11.004  1.00 41.60           O  
ANISOU 4654  O   PHE B 597     5516   5222   5067    820   -950    234       O  
ATOM   4655  CB  PHE B 597      18.483 106.276 -13.175  1.00 42.06           C  
ANISOU 4655  CB  PHE B 597     5541   5307   5133   1003   -871    335       C  
ATOM   4656  CG  PHE B 597      17.570 106.985 -12.222  1.00 42.90           C  
ANISOU 4656  CG  PHE B 597     5772   5341   5183   1158   -844    288       C  
ATOM   4657  CD1 PHE B 597      17.532 108.374 -12.179  1.00 43.57           C  
ANISOU 4657  CD1 PHE B 597     6044   5258   5249   1222   -878    288       C  
ATOM   4658  CD2 PHE B 597      16.767 106.266 -11.342  1.00 42.31           C  
ANISOU 4658  CD2 PHE B 597     5644   5359   5069   1247   -774    249       C  
ATOM   4659  CE1 PHE B 597      16.709 109.033 -11.282  1.00 45.22           C  
ANISOU 4659  CE1 PHE B 597     6395   5391   5393   1394   -838    239       C  
ATOM   4660  CE2 PHE B 597      15.942 106.922 -10.454  1.00 42.90           C  
ANISOU 4660  CE2 PHE B 597     5840   5378   5082   1412   -721    212       C  
ATOM   4661  CZ  PHE B 597      15.902 108.304 -10.427  1.00 44.50           C  
ANISOU 4661  CZ  PHE B 597     6237   5412   5258   1499   -749    202       C  
ATOM   4662  N   TYR B 598      20.550 107.247 -10.646  1.00 44.07           N  
ANISOU 4662  N   TYR B 598     6125   5261   5358    833  -1047    220       N  
ATOM   4663  CA  TYR B 598      20.732 107.125  -9.212  1.00 46.12           C  
ANISOU 4663  CA  TYR B 598     6508   5461   5553    841  -1089    141       C  
ATOM   4664  C   TYR B 598      19.647 107.915  -8.504  1.00 47.01           C  
ANISOU 4664  C   TYR B 598     6809   5484   5568   1026  -1040     84       C  
ATOM   4665  O   TYR B 598      19.654 109.136  -8.559  1.00 47.69           O  
ANISOU 4665  O   TYR B 598     7078   5404   5636   1057  -1088     78       O  
ATOM   4666  CB  TYR B 598      22.110 107.655  -8.802  1.00 47.08           C  
ANISOU 4666  CB  TYR B 598     6731   5446   5710    671  -1239    141       C  
ATOM   4667  CG  TYR B 598      23.242 106.983  -9.538  1.00 46.18           C  
ANISOU 4667  CG  TYR B 598     6413   5426   5705    506  -1271    216       C  
ATOM   4668  CD1 TYR B 598      23.962 107.657 -10.523  1.00 46.56           C  
ANISOU 4668  CD1 TYR B 598     6425   5426   5840    392  -1307    301       C  
ATOM   4669  CD2 TYR B 598      23.567 105.663  -9.279  1.00 45.61           C  
ANISOU 4669  CD2 TYR B 598     6188   5493   5647    479  -1249    211       C  
ATOM   4670  CE1 TYR B 598      24.988 107.037 -11.197  1.00 45.88           C  
ANISOU 4670  CE1 TYR B 598     6142   5439   5848    265  -1307    380       C  
ATOM   4671  CE2 TYR B 598      24.606 105.040  -9.940  1.00 45.01           C  
ANISOU 4671  CE2 TYR B 598     5931   5503   5666    362  -1262    281       C  
ATOM   4672  CZ  TYR B 598      25.301 105.726 -10.900  1.00 45.25           C  
ANISOU 4672  CZ  TYR B 598     5914   5498   5779    262  -1281    366       C  
ATOM   4673  OH  TYR B 598      26.318 105.090 -11.558  1.00 46.05           O  
ANISOU 4673  OH  TYR B 598     5826   5701   5970    169  -1265    445       O  
ATOM   4674  N   PRO B 599      18.723 107.231  -7.809  1.00 47.24           N  
ANISOU 4674  N   PRO B 599     6804   5614   5529   1155   -938     49       N  
ATOM   4675  CA  PRO B 599      17.682 108.025  -7.156  1.00 50.44           C  
ANISOU 4675  CA  PRO B 599     7381   5943   5837   1361   -864      6       C  
ATOM   4676  C   PRO B 599      18.236 108.940  -6.075  1.00 54.22           C  
ANISOU 4676  C   PRO B 599     8171   6207   6221   1363   -958    -74       C  
ATOM   4677  O   PRO B 599      19.296 108.670  -5.517  1.00 54.67           O  
ANISOU 4677  O   PRO B 599     8284   6213   6273   1208  -1075   -103       O  
ATOM   4678  CB  PRO B 599      16.763 106.988  -6.507  1.00 48.94           C  
ANISOU 4678  CB  PRO B 599     7078   5918   5597   1466   -731     -1       C  
ATOM   4679  CG  PRO B 599      17.279 105.661  -6.884  1.00 47.02           C  
ANISOU 4679  CG  PRO B 599     6620   5820   5425   1311   -751     34       C  
ATOM   4680  CD  PRO B 599      18.661 105.816  -7.441  1.00 45.77           C  
ANISOU 4680  CD  PRO B 599     6460   5587   5340   1124   -888     48       C  
ATOM   4681  N   ARG B 600      17.474 109.982  -5.773  1.00 59.52           N  
ANISOU 4681  N   ARG B 600     9046   6755   6812   1549   -909   -109       N  
ATOM   4682  CA  ARG B 600      17.841 111.014  -4.808  1.00 63.88           C  
ANISOU 4682  CA  ARG B 600     9955   7065   7249   1583  -1000   -196       C  
ATOM   4683  C   ARG B 600      18.198 110.414  -3.455  1.00 62.07           C  
ANISOU 4683  C   ARG B 600     9844   6831   6906   1558  -1027   -271       C  
ATOM   4684  O   ARG B 600      19.184 110.815  -2.831  1.00 62.38           O  
ANISOU 4684  O   ARG B 600    10096   6704   6901   1428  -1197   -325       O  
ATOM   4685  CB  ARG B 600      16.670 112.001  -4.640  1.00 69.32           C  
ANISOU 4685  CB  ARG B 600    10827   7661   7849   1862   -886   -222       C  
ATOM   4686  CG  ARG B 600      17.039 113.452  -4.852  1.00 77.33           C  
ANISOU 4686  CG  ARG B 600    12132   8403   8847   1861  -1005   -245       C  
ATOM   4687  CD  ARG B 600      15.949 114.212  -5.606  1.00 82.22           C  
ANISOU 4687  CD  ARG B 600    12745   9009   9484   2087   -896   -197       C  
ATOM   4688  NE  ARG B 600      14.678 114.241  -4.873  1.00 88.49           N  
ANISOU 4688  NE  ARG B 600    13596   9861  10165   2398   -708   -232       N  
ATOM   4689  CZ  ARG B 600      13.526 113.690  -5.269  1.00 92.31           C  
ANISOU 4689  CZ  ARG B 600    13804  10573  10694   2564   -536   -161       C  
ATOM   4690  NH1 ARG B 600      13.422 113.037  -6.427  1.00 92.14           N  
ANISOU 4690  NH1 ARG B 600    13449  10739  10818   2454   -538    -62       N  
ATOM   4691  NH2 ARG B 600      12.448 113.810  -4.494  1.00 95.33           N  
ANISOU 4691  NH2 ARG B 600    14250  10996  10972   2849   -360   -185       N  
ATOM   4692  N   TRP B 601      17.406 109.441  -3.010  1.00 59.77           N  
ANISOU 4692  N   TRP B 601     9416   6724   6569   1671   -871   -264       N  
ATOM   4693  CA  TRP B 601      17.589 108.864  -1.679  1.00 59.32           C  
ANISOU 4693  CA  TRP B 601     9493   6667   6378   1680   -870   -328       C  
ATOM   4694  C   TRP B 601      18.851 108.026  -1.510  1.00 57.30           C  
ANISOU 4694  C   TRP B 601     9153   6442   6176   1436  -1028   -321       C  
ATOM   4695  O   TRP B 601      19.151 107.625  -0.392  1.00 56.40           O  
ANISOU 4695  O   TRP B 601     9181   6302   5944   1427  -1067   -373       O  
ATOM   4696  CB  TRP B 601      16.376 108.017  -1.268  1.00 59.06           C  
ANISOU 4696  CB  TRP B 601     9322   6830   6288   1856   -646   -300       C  
ATOM   4697  CG  TRP B 601      16.055 106.909  -2.224  1.00 56.87           C  
ANISOU 4697  CG  TRP B 601     8664   6783   6160   1777   -576   -203       C  
ATOM   4698  CD1 TRP B 601      15.111 106.938  -3.209  1.00 55.71           C  
ANISOU 4698  CD1 TRP B 601     8303   6755   6109   1866   -469   -129       C  
ATOM   4699  CD2 TRP B 601      16.669 105.614  -2.294  1.00 53.92           C  
ANISOU 4699  CD2 TRP B 601     8102   6534   5850   1599   -623   -170       C  
ATOM   4700  NE1 TRP B 601      15.102 105.750  -3.888  1.00 53.50           N  
ANISOU 4700  NE1 TRP B 601     7731   6657   5939   1741   -456    -60       N  
ATOM   4701  CE2 TRP B 601      16.040 104.913  -3.342  1.00 53.80           C  
ANISOU 4701  CE2 TRP B 601     7785   6697   5958   1585   -540    -85       C  
ATOM   4702  CE3 TRP B 601      17.684 104.976  -1.573  1.00 54.70           C  
ANISOU 4702  CE3 TRP B 601     8268   6604   5910   1459   -738   -202       C  
ATOM   4703  CZ2 TRP B 601      16.393 103.604  -3.692  1.00 51.58           C  
ANISOU 4703  CZ2 TRP B 601     7293   6550   5755   1439   -559    -41       C  
ATOM   4704  CZ3 TRP B 601      18.040 103.668  -1.921  1.00 53.66           C  
ANISOU 4704  CZ3 TRP B 601     7904   6616   5865   1327   -749   -149       C  
ATOM   4705  CH2 TRP B 601      17.390 103.001  -2.970  1.00 52.81           C  
ANISOU 4705  CH2 TRP B 601     7523   6669   5871   1321   -655    -74       C  
ATOM   4706  N   LEU B 602      19.580 107.738  -2.588  1.00 55.21           N  
ANISOU 4706  N   LEU B 602     8661   6237   6078   1256  -1111   -253       N  
ATOM   4707  CA  LEU B 602      20.721 106.811  -2.488  1.00 54.44           C  
ANISOU 4707  CA  LEU B 602     8434   6202   6046   1055  -1232   -230       C  
ATOM   4708  C   LEU B 602      21.910 107.418  -1.733  1.00 57.25           C  
ANISOU 4708  C   LEU B 602     9018   6373   6363    915  -1455   -280       C  
ATOM   4709  O   LEU B 602      22.372 108.515  -2.054  1.00 56.92           O  
ANISOU 4709  O   LEU B 602     9102   6166   6355    843  -1571   -283       O  
ATOM   4710  CB  LEU B 602      21.190 106.364  -3.874  1.00 52.55           C  
ANISOU 4710  CB  LEU B 602     7901   6079   5986    924  -1239   -140       C  
ATOM   4711  CG  LEU B 602      22.307 105.313  -3.929  1.00 51.71           C  
ANISOU 4711  CG  LEU B 602     7619   6063   5963    754  -1329   -101       C  
ATOM   4712  CD1 LEU B 602      21.855 104.017  -3.276  1.00 51.18           C  
ANISOU 4712  CD1 LEU B 602     7478   6132   5833    816  -1239   -111       C  
ATOM   4713  CD2 LEU B 602      22.755 105.065  -5.365  1.00 50.88           C  
ANISOU 4713  CD2 LEU B 602     7267   6051   6015    655  -1317    -14       C  
ATOM   4714  N   GLU B 603      22.410 106.677  -0.748  1.00 59.18           N  
ANISOU 4714  N   GLU B 603     9308   6639   6535    865  -1528   -309       N  
ATOM   4715  CA  GLU B 603      23.611 107.048  -0.003  1.00 61.93           C  
ANISOU 4715  CA  GLU B 603     9835   6838   6856    708  -1772   -343       C  
ATOM   4716  C   GLU B 603      24.721 107.527  -0.952  1.00 60.36           C  
ANISOU 4716  C   GLU B 603     9493   6594   6843    495  -1926   -271       C  
ATOM   4717  O   GLU B 603      25.048 106.860  -1.928  1.00 57.49           O  
ANISOU 4717  O   GLU B 603     8823   6385   6633    421  -1876   -184       O  
ATOM   4718  CB  GLU B 603      24.056 105.836   0.826  1.00 63.80           C  
ANISOU 4718  CB  GLU B 603    10017   7178   7047    667  -1817   -342       C  
ATOM   4719  CG  GLU B 603      25.420 105.924   1.483  1.00 67.78           C  
ANISOU 4719  CG  GLU B 603    10611   7581   7559    481  -2092   -349       C  
ATOM   4720  CD  GLU B 603      25.510 107.031   2.508  1.00 72.76           C  
ANISOU 4720  CD  GLU B 603    11651   7973   8020    491  -2247   -448       C  
ATOM   4721  OE1 GLU B 603      24.586 107.142   3.354  1.00 74.35           O  
ANISOU 4721  OE1 GLU B 603    12106   8127   8016    682  -2132   -529       O  
ATOM   4722  OE2 GLU B 603      26.520 107.778   2.460  1.00 76.39           O  
ANISOU 4722  OE2 GLU B 603    12181   8291   8551    306  -2484   -439       O  
ATOM   4723  N   LYS B 604      25.273 108.698  -0.663  1.00 63.07           N  
ANISOU 4723  N   LYS B 604    10076   6721   7165    401  -2108   -304       N  
ATOM   4724  CA  LYS B 604      26.294 109.346  -1.498  1.00 64.13           C  
ANISOU 4724  CA  LYS B 604    10108   6786   7472    185  -2257   -223       C  
ATOM   4725  C   LYS B 604      27.480 108.454  -1.835  1.00 60.81           C  
ANISOU 4725  C   LYS B 604     9374   6515   7215      0  -2349   -126       C  
ATOM   4726  O   LYS B 604      27.978 108.465  -2.956  1.00 61.06           O  
ANISOU 4726  O   LYS B 604     9161   6621   7415   -107  -2324    -22       O  
ATOM   4727  CB  LYS B 604      26.828 110.579  -0.775  1.00 69.89           C  
ANISOU 4727  CB  LYS B 604    11184   7239   8129     79  -2493   -282       C  
ATOM   4728  CG  LYS B 604      25.854 111.749  -0.700  1.00 75.00           C  
ANISOU 4728  CG  LYS B 604    12156   7692   8648    245  -2424   -361       C  
ATOM   4729  CD  LYS B 604      26.069 112.613   0.543  1.00 79.63           C  
ANISOU 4729  CD  LYS B 604    13192   8006   9055    232  -2626   -476       C  
ATOM   4730  CE  LYS B 604      27.535 112.976   0.773  1.00 83.50           C  
ANISOU 4730  CE  LYS B 604    13712   8370   9643    -81  -2950   -436       C  
ATOM   4731  NZ  LYS B 604      27.830 113.311   2.200  1.00 87.23           N  
ANISOU 4731  NZ  LYS B 604    14581   8642   9919   -104  -3171   -553       N  
ATOM   4732  N   GLU B 605      27.949 107.699  -0.856  1.00 60.69           N  
ANISOU 4732  N   GLU B 605     9376   6540   7143    -29  -2452   -153       N  
ATOM   4733  CA  GLU B 605      29.098 106.815  -1.060  1.00 61.02           C  
ANISOU 4733  CA  GLU B 605     9127   6722   7335   -179  -2546    -58       C  
ATOM   4734  C   GLU B 605      28.762 105.603  -1.913  1.00 58.32           C  
ANISOU 4734  C   GLU B 605     8473   6612   7072    -87  -2328      0       C  
ATOM   4735  O   GLU B 605      29.616 105.099  -2.652  1.00 56.38           O  
ANISOU 4735  O   GLU B 605     7945   6486   6991   -189  -2339    102       O  
ATOM   4736  CB  GLU B 605      29.677 106.368   0.283  1.00 64.83           C  
ANISOU 4736  CB  GLU B 605     9742   7169   7722   -223  -2738   -103       C  
ATOM   4737  CG  GLU B 605      30.256 107.503   1.099  1.00 68.14           C  
ANISOU 4737  CG  GLU B 605    10463   7351   8076   -360  -3013   -152       C  
ATOM   4738  CD  GLU B 605      31.278 108.329   0.323  1.00 72.71           C  
ANISOU 4738  CD  GLU B 605    10906   7863   8857   -597  -3170    -49       C  
ATOM   4739  OE1 GLU B 605      31.937 107.805  -0.608  1.00 72.80           O  
ANISOU 4739  OE1 GLU B 605    10549   8041   9068   -685  -3120     77       O  
ATOM   4740  OE2 GLU B 605      31.426 109.522   0.646  1.00 78.94           O  
ANISOU 4740  OE2 GLU B 605    11969   8423   9599   -696  -3340    -91       O  
ATOM   4741  N   ALA B 606      27.512 105.154  -1.829  1.00 55.77           N  
ANISOU 4741  N   ALA B 606     8205   6350   6633    105  -2129    -57       N  
ATOM   4742  CA  ALA B 606      27.029 104.080  -2.678  1.00 52.87           C  
ANISOU 4742  CA  ALA B 606     7583   6176   6326    188  -1931     -9       C  
ATOM   4743  C   ALA B 606      27.038 104.550  -4.126  1.00 51.22           C  
ANISOU 4743  C   ALA B 606     7211   6000   6248    151  -1849     62       C  
ATOM   4744  O   ALA B 606      27.624 103.898  -5.005  1.00 48.72           O  
ANISOU 4744  O   ALA B 606     6643   5810   6057     94  -1808    145       O  
ATOM   4745  CB  ALA B 606      25.632 103.655  -2.248  1.00 53.14           C  
ANISOU 4745  CB  ALA B 606     7719   6254   6215    380  -1754    -75       C  
ATOM   4746  N   LYS B 607      26.413 105.701  -4.371  1.00 51.55           N  
ANISOU 4746  N   LYS B 607     7414   5920   6250    193  -1823     34       N  
ATOM   4747  CA  LYS B 607      26.473 106.341  -5.681  1.00 50.73           C  
ANISOU 4747  CA  LYS B 607     7206   5814   6254    147  -1771    108       C  
ATOM   4748  C   LYS B 607      27.905 106.509  -6.186  1.00 51.75           C  
ANISOU 4748  C   LYS B 607     7176   5945   6540    -58  -1896    209       C  
ATOM   4749  O   LYS B 607      28.188 106.273  -7.353  1.00 50.87           O  
ANISOU 4749  O   LYS B 607     6853   5938   6534    -93  -1806    299       O  
ATOM   4750  CB  LYS B 607      25.793 107.721  -5.635  1.00 53.73           C  
ANISOU 4750  CB  LYS B 607     7841   6011   6563    207  -1781     62       C  
ATOM   4751  CG  LYS B 607      25.856 108.470  -6.957  1.00 54.15           C  
ANISOU 4751  CG  LYS B 607     7818   6039   6716    157  -1740    147       C  
ATOM   4752  CD  LYS B 607      25.070 109.777  -6.941  1.00 56.88           C  
ANISOU 4752  CD  LYS B 607     8427   6200   6985    251  -1737    104       C  
ATOM   4753  CE  LYS B 607      25.204 110.477  -8.286  1.00 57.93           C  
ANISOU 4753  CE  LYS B 607     8487   6307   7217    190  -1705    204       C  
ATOM   4754  NZ  LYS B 607      24.455 111.759  -8.341  1.00 60.87           N  
ANISOU 4754  NZ  LYS B 607     9119   6486   7519    293  -1706    172       N  
ATOM   4755  N   ASP B 608      28.806 106.932  -5.309  1.00 54.11           N  
ANISOU 4755  N   ASP B 608     7578   6130   6849   -196  -2103    202       N  
ATOM   4756  CA  ASP B 608      30.169 107.239  -5.728  1.00 55.20           C  
ANISOU 4756  CA  ASP B 608     7555   6264   7154   -411  -2238    316       C  
ATOM   4757  C   ASP B 608      30.922 105.977  -6.169  1.00 53.72           C  
ANISOU 4757  C   ASP B 608     7041   6290   7080   -431  -2179    403       C  
ATOM   4758  O   ASP B 608      31.689 106.003  -7.121  1.00 55.00           O  
ANISOU 4758  O   ASP B 608     6981   6529   7386   -528  -2147    524       O  
ATOM   4759  CB  ASP B 608      30.924 107.939  -4.605  1.00 58.45           C  
ANISOU 4759  CB  ASP B 608     8156   6501   7547   -564  -2506    288       C  
ATOM   4760  CG  ASP B 608      32.321 108.343  -5.020  1.00 60.42           C  
ANISOU 4760  CG  ASP B 608     8219   6746   7989   -811  -2660    427       C  
ATOM   4761  OD1 ASP B 608      32.463 109.419  -5.615  1.00 63.57           O  
ANISOU 4761  OD1 ASP B 608     8677   7026   8450   -922  -2692    482       O  
ATOM   4762  OD2 ASP B 608      33.273 107.576  -4.772  1.00 59.40           O  
ANISOU 4762  OD2 ASP B 608     7873   6738   7955   -892  -2745    493       O  
ATOM   4763  N   LEU B 609      30.697 104.865  -5.487  1.00 52.53           N  
ANISOU 4763  N   LEU B 609     6870   6230   6856   -327  -2154    347       N  
ATOM   4764  CA  LEU B 609      31.329 103.619  -5.881  1.00 51.09           C  
ANISOU 4764  CA  LEU B 609     6413   6233   6766   -312  -2090    418       C  
ATOM   4765  C   LEU B 609      30.798 103.159  -7.228  1.00 48.70           C  
ANISOU 4765  C   LEU B 609     5960   6053   6491   -213  -1861    457       C  
ATOM   4766  O   LEU B 609      31.554 102.745  -8.105  1.00 46.66           O  
ANISOU 4766  O   LEU B 609     5470   5908   6351   -249  -1799    558       O  
ATOM   4767  CB  LEU B 609      31.071 102.532  -4.833  1.00 51.55           C  
ANISOU 4767  CB  LEU B 609     6527   6337   6721   -211  -2110    346       C  
ATOM   4768  CG  LEU B 609      31.593 101.135  -5.171  1.00 50.57           C  
ANISOU 4768  CG  LEU B 609     6160   6384   6668   -159  -2037    406       C  
ATOM   4769  CD1 LEU B 609      33.085 101.170  -5.494  1.00 52.79           C  
ANISOU 4769  CD1 LEU B 609     6203   6725   7129   -294  -2145    534       C  
ATOM   4770  CD2 LEU B 609      31.305 100.187  -4.019  1.00 51.51           C  
ANISOU 4770  CD2 LEU B 609     6386   6514   6672    -72  -2079    337       C  
ATOM   4771  N   LEU B 610      29.481 103.228  -7.376  1.00 47.69           N  
ANISOU 4771  N   LEU B 610     5969   5903   6248    -82  -1737    378       N  
ATOM   4772  CA  LEU B 610      28.844 102.827  -8.612  1.00 46.00           C  
ANISOU 4772  CA  LEU B 610     5648   5790   6039      8  -1548    404       C  
ATOM   4773  C   LEU B 610      29.394 103.690  -9.743  1.00 46.54           C  
ANISOU 4773  C   LEU B 610     5633   5842   6208    -86  -1528    505       C  
ATOM   4774  O   LEU B 610      29.791 103.186 -10.795  1.00 46.30           O  
ANISOU 4774  O   LEU B 610     5421   5926   6241    -81  -1420    583       O  
ATOM   4775  CB  LEU B 610      27.321 102.950  -8.479  1.00 44.96           C  
ANISOU 4775  CB  LEU B 610     5676   5628   5779    148  -1454    316       C  
ATOM   4776  CG  LEU B 610      26.671 101.899  -7.572  1.00 44.76           C  
ANISOU 4776  CG  LEU B 610     5694   5656   5657    250  -1421    242       C  
ATOM   4777  CD1 LEU B 610      25.210 102.218  -7.295  1.00 45.04           C  
ANISOU 4777  CD1 LEU B 610     5876   5656   5577    377  -1335    173       C  
ATOM   4778  CD2 LEU B 610      26.774 100.510  -8.181  1.00 44.03           C  
ANISOU 4778  CD2 LEU B 610     5421   5709   5597    289  -1326    275       C  
ATOM   4779  N   VAL B 611      29.440 104.995  -9.528  1.00 48.48           N  
ANISOU 4779  N   VAL B 611     6027   5933   6457   -173  -1628    506       N  
ATOM   4780  CA  VAL B 611      29.972 105.896 -10.555  1.00 50.15           C  
ANISOU 4780  CA  VAL B 611     6180   6110   6765   -283  -1615    616       C  
ATOM   4781  C   VAL B 611      31.400 105.496 -10.990  1.00 50.77           C  
ANISOU 4781  C   VAL B 611     5998   6298   6994   -411  -1630    748       C  
ATOM   4782  O   VAL B 611      31.746 105.583 -12.168  1.00 51.30           O  
ANISOU 4782  O   VAL B 611     5928   6437   7127   -436  -1515    854       O  
ATOM   4783  CB  VAL B 611      29.971 107.358 -10.062  1.00 52.94           C  
ANISOU 4783  CB  VAL B 611     6758   6247   7106   -385  -1762    600       C  
ATOM   4784  CG1 VAL B 611      30.808 108.250 -10.978  1.00 55.90           C  
ANISOU 4784  CG1 VAL B 611     7054   6578   7606   -553  -1782    741       C  
ATOM   4785  CG2 VAL B 611      28.551 107.892  -9.956  1.00 51.78           C  
ANISOU 4785  CG2 VAL B 611     6847   6004   6824   -228  -1701    499       C  
ATOM   4786  N   LYS B 612      32.218 105.035 -10.053  1.00 50.88           N  
ANISOU 4786  N   LYS B 612     5939   6332   7057   -478  -1764    749       N  
ATOM   4787  CA  LYS B 612      33.590 104.636 -10.387  1.00 53.10           C  
ANISOU 4787  CA  LYS B 612     5945   6733   7498   -583  -1781    887       C  
ATOM   4788  C   LYS B 612      33.703 103.260 -11.028  1.00 52.07           C  
ANISOU 4788  C   LYS B 612     5615   6793   7374   -440  -1606    913       C  
ATOM   4789  O   LYS B 612      34.679 102.969 -11.707  1.00 52.28           O  
ANISOU 4789  O   LYS B 612     5406   6938   7520   -477  -1539   1041       O  
ATOM   4790  CB  LYS B 612      34.475 104.727  -9.157  1.00 55.43           C  
ANISOU 4790  CB  LYS B 612     6230   6976   7854   -714  -2020    893       C  
ATOM   4791  CG  LYS B 612      34.869 106.162  -8.876  1.00 59.39           C  
ANISOU 4791  CG  LYS B 612     6856   7299   8410   -921  -2204    933       C  
ATOM   4792  CD  LYS B 612      35.234 106.390  -7.420  1.00 61.75           C  
ANISOU 4792  CD  LYS B 612     7300   7477   8683  -1020  -2475    869       C  
ATOM   4793  CE  LYS B 612      35.596 107.854  -7.215  1.00 64.45           C  
ANISOU 4793  CE  LYS B 612     7802   7613   9072  -1237  -2670    904       C  
ATOM   4794  NZ  LYS B 612      35.878 108.106  -5.780  1.00 67.64           N  
ANISOU 4794  NZ  LYS B 612     8403   7877   9418  -1329  -2951    824       N  
ATOM   4795  N   LEU B 613      32.704 102.415 -10.813  1.00 50.79           N  
ANISOU 4795  N   LEU B 613     5555   6659   7084   -276  -1527    796       N  
ATOM   4796  CA  LEU B 613      32.648 101.114 -11.479  1.00 50.44           C  
ANISOU 4796  CA  LEU B 613     5381   6762   7022   -135  -1364    804       C  
ATOM   4797  C   LEU B 613      32.092 101.206 -12.902  1.00 50.21           C  
ANISOU 4797  C   LEU B 613     5348   6775   6952    -66  -1178    831       C  
ATOM   4798  O   LEU B 613      32.570 100.495 -13.787  1.00 52.17           O  
ANISOU 4798  O   LEU B 613     5449   7141   7229     -4  -1045    898       O  
ATOM   4799  CB  LEU B 613      31.800 100.142 -10.661  1.00 49.52           C  
ANISOU 4799  CB  LEU B 613     5382   6646   6787    -12  -1370    679       C  
ATOM   4800  CG  LEU B 613      32.430  99.767  -9.317  1.00 49.37           C  
ANISOU 4800  CG  LEU B 613     5360   6607   6788    -51  -1538    661       C  
ATOM   4801  CD1 LEU B 613      31.352  99.285  -8.367  1.00 48.67           C  
ANISOU 4801  CD1 LEU B 613     5468   6469   6555     39  -1556    535       C  
ATOM   4802  CD2 LEU B 613      33.515  98.709  -9.505  1.00 50.32           C  
ANISOU 4802  CD2 LEU B 613     5256   6857   7006    -14  -1514    745       C  
ATOM   4803  N   PHE B 614      31.095 102.070 -13.124  1.00 48.81           N  
ANISOU 4803  N   PHE B 614     5343   6502   6699    -64  -1169    782       N  
ATOM   4804  CA  PHE B 614      30.528 102.266 -14.465  1.00 48.25           C  
ANISOU 4804  CA  PHE B 614     5290   6461   6581     -5  -1021    814       C  
ATOM   4805  C   PHE B 614      31.336 103.220 -15.354  1.00 50.91           C  
ANISOU 4805  C   PHE B 614     5548   6788   7006   -119   -987    953       C  
ATOM   4806  O   PHE B 614      30.776 104.008 -16.104  1.00 51.55           O  
ANISOU 4806  O   PHE B 614     5729   6814   7044   -119   -939    975       O  
ATOM   4807  CB  PHE B 614      29.054 102.713 -14.379  1.00 47.15           C  
ANISOU 4807  CB  PHE B 614     5350   6239   6326     69  -1023    715       C  
ATOM   4808  CG  PHE B 614      28.148 101.670 -13.796  1.00 45.15           C  
ANISOU 4808  CG  PHE B 614     5145   6024   5983    186  -1008    606       C  
ATOM   4809  CD1 PHE B 614      28.184 100.360 -14.256  1.00 46.03           C  
ANISOU 4809  CD1 PHE B 614     5167   6249   6072    266   -918    600       C  
ATOM   4810  CD2 PHE B 614      27.271 101.985 -12.783  1.00 45.98           C  
ANISOU 4810  CD2 PHE B 614     5396   6048   6024    219  -1077    515       C  
ATOM   4811  CE1 PHE B 614      27.344  99.391 -13.725  1.00 45.12           C  
ANISOU 4811  CE1 PHE B 614     5102   6158   5881    350   -911    512       C  
ATOM   4812  CE2 PHE B 614      26.432 101.022 -12.243  1.00 45.59           C  
ANISOU 4812  CE2 PHE B 614     5378   6044   5899    313  -1050    435       C  
ATOM   4813  CZ  PHE B 614      26.470  99.723 -12.711  1.00 43.90           C  
ANISOU 4813  CZ  PHE B 614     5068   5936   5674    366   -975    437       C  
ATOM   4814  N   VAL B 615      32.658 103.135 -15.278  1.00 52.06           N  
ANISOU 4814  N   VAL B 615     5505   6994   7281   -215  -1010   1062       N  
ATOM   4815  CA  VAL B 615      33.528 103.850 -16.193  1.00 53.48           C  
ANISOU 4815  CA  VAL B 615     5562   7199   7557   -324   -944   1223       C  
ATOM   4816  C   VAL B 615      33.770 102.917 -17.378  1.00 54.11           C  
ANISOU 4816  C   VAL B 615     5515   7437   7605   -195   -728   1282       C  
ATOM   4817  O   VAL B 615      34.209 101.773 -17.207  1.00 54.40           O  
ANISOU 4817  O   VAL B 615     5429   7582   7657   -101   -682   1271       O  
ATOM   4818  CB  VAL B 615      34.850 104.221 -15.494  1.00 55.11           C  
ANISOU 4818  CB  VAL B 615     5600   7405   7934   -502  -1081   1329       C  
ATOM   4819  CG1 VAL B 615      35.863 104.767 -16.495  1.00 56.83           C  
ANISOU 4819  CG1 VAL B 615     5630   7688   8271   -616   -980   1527       C  
ATOM   4820  CG2 VAL B 615      34.572 105.220 -14.373  1.00 54.95           C  
ANISOU 4820  CG2 VAL B 615     5765   7197   7914   -633  -1308   1259       C  
ATOM   4821  N   ARG B 616      33.473 103.391 -18.580  1.00 54.65           N  
ANISOU 4821  N   ARG B 616     5640   7508   7617   -175   -597   1343       N  
ATOM   4822  CA  ARG B 616      33.482 102.507 -19.747  1.00 55.22           C  
ANISOU 4822  CA  ARG B 616     5668   7707   7606    -26   -393   1371       C  
ATOM   4823  C   ARG B 616      34.885 102.192 -20.261  1.00 56.90           C  
ANISOU 4823  C   ARG B 616     5634   8057   7927    -40   -261   1533       C  
ATOM   4824  O   ARG B 616      35.105 101.123 -20.826  1.00 57.77           O  
ANISOU 4824  O   ARG B 616     5685   8281   7981    114   -112   1532       O  
ATOM   4825  CB  ARG B 616      32.584 103.054 -20.852  1.00 54.49           C  
ANISOU 4825  CB  ARG B 616     5749   7570   7385     18   -309   1371       C  
ATOM   4826  CG  ARG B 616      31.121 103.045 -20.424  1.00 52.46           C  
ANISOU 4826  CG  ARG B 616     5696   7220   7015     87   -409   1211       C  
ATOM   4827  CD  ARG B 616      30.181 102.925 -21.605  1.00 52.12           C  
ANISOU 4827  CD  ARG B 616     5791   7191   6820    199   -312   1190       C  
ATOM   4828  NE  ARG B 616      28.804 102.639 -21.185  1.00 50.45           N  
ANISOU 4828  NE  ARG B 616     5718   6931   6517    280   -399   1046       N  
ATOM   4829  CZ  ARG B 616      27.970 103.525 -20.646  1.00 49.38           C  
ANISOU 4829  CZ  ARG B 616     5697   6685   6379    251   -510    999       C  
ATOM   4830  NH1 ARG B 616      28.359 104.781 -20.435  1.00 51.84           N  
ANISOU 4830  NH1 ARG B 616     6037   6895   6765    137   -568   1069       N  
ATOM   4831  NH2 ARG B 616      26.731 103.164 -20.327  1.00 45.80           N  
ANISOU 4831  NH2 ARG B 616     5333   6218   5848    340   -561    887       N  
ATOM   4832  N   GLU B 617      35.823 103.103 -20.050  1.00 58.32           N  
ANISOU 4832  N   GLU B 617     5672   8223   8262   -221   -318   1674       N  
ATOM   4833  CA  GLU B 617      37.216 102.847 -20.408  1.00 63.16           C  
ANISOU 4833  CA  GLU B 617     6000   8984   9012   -248   -202   1852       C  
ATOM   4834  C   GLU B 617      37.816 101.879 -19.371  1.00 62.80           C  
ANISOU 4834  C   GLU B 617     5793   9011   9058   -202   -294   1813       C  
ATOM   4835  O   GLU B 617      38.073 102.272 -18.223  1.00 62.51           O  
ANISOU 4835  O   GLU B 617     5722   8903   9126   -344   -512   1796       O  
ATOM   4836  CB  GLU B 617      38.000 104.158 -20.472  1.00 66.68           C  
ANISOU 4836  CB  GLU B 617     6334   9387   9612   -489   -257   2031       C  
ATOM   4837  CG  GLU B 617      39.441 104.009 -20.942  1.00 73.07           C  
ANISOU 4837  CG  GLU B 617     6812  10369  10582   -534   -115   2253       C  
ATOM   4838  CD  GLU B 617      40.084 105.345 -21.292  1.00 77.87           C  
ANISOU 4838  CD  GLU B 617     7332  10932  11322   -782   -131   2452       C  
ATOM   4839  OE1 GLU B 617      39.391 106.222 -21.862  1.00 79.76           O  
ANISOU 4839  OE1 GLU B 617     7790  11047  11466   -836   -116   2448       O  
ATOM   4840  OE2 GLU B 617      41.290 105.523 -21.008  1.00 85.03           O  
ANISOU 4840  OE2 GLU B 617     7945  11926  12434   -928   -165   2626       O  
ATOM   4841  N   PRO B 618      38.036 100.610 -19.769  1.00 62.10           N  
ANISOU 4841  N   PRO B 618     5629   9049   8916      2   -137   1796       N  
ATOM   4842  CA  PRO B 618      38.373  99.582 -18.778  1.00 63.82           C  
ANISOU 4842  CA  PRO B 618     5754   9310   9183     83   -231   1732       C  
ATOM   4843  C   PRO B 618      39.519  99.986 -17.840  1.00 66.55           C  
ANISOU 4843  C   PRO B 618     5851   9689   9746    -83   -398   1851       C  
ATOM   4844  O   PRO B 618      39.445  99.741 -16.639  1.00 65.72           O  
ANISOU 4844  O   PRO B 618     5774   9527   9668   -117   -601   1764       O  
ATOM   4845  CB  PRO B 618      38.781  98.367 -19.629  1.00 64.34           C  
ANISOU 4845  CB  PRO B 618     5737   9517   9192    318      4   1763       C  
ATOM   4846  CG  PRO B 618      38.317  98.649 -21.010  1.00 63.32           C  
ANISOU 4846  CG  PRO B 618     5740   9394   8925    379    204   1787       C  
ATOM   4847  CD  PRO B 618      38.217 100.131 -21.149  1.00 63.29           C  
ANISOU 4847  CD  PRO B 618     5759   9310   8976    161    135   1868       C  
ATOM   4848  N   GLU B 619      40.552 100.624 -18.378  1.00 70.11           N  
ANISOU 4848  N   GLU B 619     6065  10227  10345   -198   -321   2057       N  
ATOM   4849  CA  GLU B 619      41.745 100.936 -17.583  1.00 73.12           C  
ANISOU 4849  CA  GLU B 619     6164  10664  10953   -364   -481   2199       C  
ATOM   4850  C   GLU B 619      41.544 102.007 -16.501  1.00 72.42           C  
ANISOU 4850  C   GLU B 619     6188  10403  10925   -619   -789   2154       C  
ATOM   4851  O   GLU B 619      42.385 102.137 -15.603  1.00 71.38           O  
ANISOU 4851  O   GLU B 619     5876  10289  10954   -757   -990   2227       O  
ATOM   4852  CB  GLU B 619      42.907 101.313 -18.507  1.00 78.01           C  
ANISOU 4852  CB  GLU B 619     6472  11439  11726   -426   -298   2455       C  
ATOM   4853  CG  GLU B 619      43.345 100.166 -19.415  1.00 81.46           C  
ANISOU 4853  CG  GLU B 619     6767  12062  12120   -149      2   2514       C  
ATOM   4854  CD  GLU B 619      43.580  98.858 -18.654  1.00 83.36           C  
ANISOU 4854  CD  GLU B 619     6935  12368  12370     41    -53   2431       C  
ATOM   4855  OE1 GLU B 619      44.534  98.804 -17.857  1.00 86.13           O  
ANISOU 4855  OE1 GLU B 619     7017  12791  12915    -40   -201   2536       O  
ATOM   4856  OE2 GLU B 619      42.804  97.885 -18.835  1.00 83.77           O  
ANISOU 4856  OE2 GLU B 619     7205  12387  12236    264     33   2264       O  
ATOM   4857  N   LYS B 620      40.447 102.760 -16.580  1.00 69.14           N  
ANISOU 4857  N   LYS B 620     6076   9818  10374   -673   -835   2036       N  
ATOM   4858  CA  LYS B 620      40.134 103.768 -15.569  1.00 69.76           C  
ANISOU 4858  CA  LYS B 620     6327   9707  10472   -877  -1111   1968       C  
ATOM   4859  C   LYS B 620      39.097 103.272 -14.570  1.00 66.85           C  
ANISOU 4859  C   LYS B 620     6217   9232   9951   -768  -1241   1740       C  
ATOM   4860  O   LYS B 620      38.704 104.003 -13.662  1.00 66.62           O  
ANISOU 4860  O   LYS B 620     6378   9036   9896   -890  -1455   1655       O  
ATOM   4861  CB  LYS B 620      39.643 105.054 -16.231  1.00 71.76           C  
ANISOU 4861  CB  LYS B 620     6753   9825  10686  -1007  -1086   2002       C  
ATOM   4862  CG  LYS B 620      40.723 105.811 -16.991  1.00 76.49           C  
ANISOU 4862  CG  LYS B 620     7114  10490  11457  -1191  -1013   2249       C  
ATOM   4863  CD  LYS B 620      40.175 107.115 -17.546  1.00 77.89           C  
ANISOU 4863  CD  LYS B 620     7509  10499  11584  -1325  -1016   2275       C  
ATOM   4864  CE  LYS B 620      41.266 107.996 -18.115  1.00 81.92           C  
ANISOU 4864  CE  LYS B 620     7802  11043  12280  -1562   -987   2532       C  
ATOM   4865  NZ  LYS B 620      40.653 109.094 -18.909  1.00 83.39           N  
ANISOU 4865  NZ  LYS B 620     8219  11080  12383  -1637   -927   2564       N  
ATOM   4866  N   ARG B 621      38.654 102.029 -14.732  1.00 64.59           N  
ANISOU 4866  N   ARG B 621     5950   9033   9557   -537  -1107   1646       N  
ATOM   4867  CA  ARG B 621      37.607 101.481 -13.883  1.00 61.75           C  
ANISOU 4867  CA  ARG B 621     5826   8587   9049   -429  -1194   1447       C  
ATOM   4868  C   ARG B 621      38.181 101.060 -12.541  1.00 61.45           C  
ANISOU 4868  C   ARG B 621     5723   8546   9077   -471  -1407   1425       C  
ATOM   4869  O   ARG B 621      39.207 100.386 -12.486  1.00 64.03           O  
ANISOU 4869  O   ARG B 621     5799   9005   9522   -439  -1399   1528       O  
ATOM   4870  CB  ARG B 621      36.948 100.277 -14.563  1.00 59.79           C  
ANISOU 4870  CB  ARG B 621     5628   8421   8668   -191   -989   1367       C  
ATOM   4871  CG  ARG B 621      35.652  99.807 -13.911  1.00 56.47           C  
ANISOU 4871  CG  ARG B 621     5462   7909   8084    -93  -1043   1176       C  
ATOM   4872  CD  ARG B 621      35.028  98.681 -14.721  1.00 55.12           C  
ANISOU 4872  CD  ARG B 621     5341   7809   7794    106   -854   1115       C  
ATOM   4873  NE  ARG B 621      34.765  99.117 -16.090  1.00 54.38           N  
ANISOU 4873  NE  ARG B 621     5270   7737   7654    127   -685   1167       N  
ATOM   4874  CZ  ARG B 621      34.754  98.337 -17.173  1.00 54.68           C  
ANISOU 4874  CZ  ARG B 621     5288   7863   7625    272   -495   1185       C  
ATOM   4875  NH1 ARG B 621      34.967  97.029 -17.087  1.00 54.65           N  
ANISOU 4875  NH1 ARG B 621     5245   7926   7593    420   -438   1149       N  
ATOM   4876  NH2 ARG B 621      34.509  98.875 -18.368  1.00 56.04           N  
ANISOU 4876  NH2 ARG B 621     5508   8043   7741    277   -362   1236       N  
ATOM   4877  N   LEU B 622      37.518 101.468 -11.465  1.00 61.20           N  
ANISOU 4877  N   LEU B 622     5924   8365   8962   -528  -1595   1297       N  
ATOM   4878  CA  LEU B 622      37.880 101.038 -10.105  1.00 60.77           C  
ANISOU 4878  CA  LEU B 622     5879   8288   8922   -551  -1809   1250       C  
ATOM   4879  C   LEU B 622      37.816  99.504 -10.034  1.00 59.22           C  
ANISOU 4879  C   LEU B 622     5618   8207   8674   -340  -1705   1207       C  
ATOM   4880  O   LEU B 622      36.868  98.868 -10.541  1.00 53.62           O  
ANISOU 4880  O   LEU B 622     5030   7508   7834   -180  -1535   1115       O  
ATOM   4881  CB  LEU B 622      36.897 101.632  -9.090  1.00 61.16           C  
ANISOU 4881  CB  LEU B 622     6256   8153   8829   -590  -1964   1093       C  
ATOM   4882  CG  LEU B 622      37.331 102.113  -7.699  1.00 63.06           C  
ANISOU 4882  CG  LEU B 622     6595   8280   9082   -734  -2260   1066       C  
ATOM   4883  CD1 LEU B 622      36.300 101.646  -6.688  1.00 60.41           C  
ANISOU 4883  CD1 LEU B 622     6535   7863   8554   -611  -2302    893       C  
ATOM   4884  CD2 LEU B 622      38.729 101.686  -7.273  1.00 65.62           C  
ANISOU 4884  CD2 LEU B 622     6647   8710   9574   -817  -2410   1195       C  
ATOM   4885  N   GLY B 623      38.830  98.907  -9.421  1.00 59.37           N  
ANISOU 4885  N   GLY B 623     5449   8307   8800   -342  -1819   1280       N  
ATOM   4886  CA  GLY B 623      38.983  97.465  -9.450  1.00 59.22           C  
ANISOU 4886  CA  GLY B 623     5344   8397   8758   -138  -1717   1271       C  
ATOM   4887  C   GLY B 623      40.112  97.098 -10.386  1.00 61.45           C  
ANISOU 4887  C   GLY B 623     5299   8850   9198    -83  -1571   1442       C  
ATOM   4888  O   GLY B 623      40.862  96.163 -10.103  1.00 63.41           O  
ANISOU 4888  O   GLY B 623     5376   9198   9516     26  -1586   1501       O  
ATOM   4889  N   VAL B 624      40.238  97.830 -11.497  1.00 61.73           N  
ANISOU 4889  N   VAL B 624     5249   8919   9283   -144  -1422   1530       N  
ATOM   4890  CA  VAL B 624      41.431  97.748 -12.366  1.00 64.51           C  
ANISOU 4890  CA  VAL B 624     5265   9440   9804   -128  -1282   1728       C  
ATOM   4891  C   VAL B 624      42.478  98.745 -11.879  1.00 67.72           C  
ANISOU 4891  C   VAL B 624     5458   9858  10413   -379  -1487   1883       C  
ATOM   4892  O   VAL B 624      43.650  98.408 -11.732  1.00 69.95           O  
ANISOU 4892  O   VAL B 624     5429  10278  10870   -380  -1526   2036       O  
ATOM   4893  CB  VAL B 624      41.096  98.038 -13.850  1.00 64.44           C  
ANISOU 4893  CB  VAL B 624     5274   9470   9740    -73  -1006   1768       C  
ATOM   4894  CG1 VAL B 624      42.311  97.794 -14.743  1.00 66.22           C  
ANISOU 4894  CG1 VAL B 624     5161   9886  10115    -12   -817   1974       C  
ATOM   4895  CG2 VAL B 624      39.924  97.186 -14.308  1.00 61.79           C  
ANISOU 4895  CG2 VAL B 624     5192   9092   9191    132   -851   1602       C  
ATOM   4896  N   ARG B 625      42.056  99.982 -11.648  1.00 69.49           N  
ANISOU 4896  N   ARG B 625     5848   9933  10619   -591  -1623   1850       N  
ATOM   4897  CA  ARG B 625      42.924 100.971 -11.015  1.00 72.67           C  
ANISOU 4897  CA  ARG B 625     6119  10296  11193   -863  -1879   1969       C  
ATOM   4898  C   ARG B 625      42.430 101.191  -9.601  1.00 70.64           C  
ANISOU 4898  C   ARG B 625     6129   9868  10841   -944  -2173   1814       C  
ATOM   4899  O   ARG B 625      41.297 100.801  -9.254  1.00 65.80           O  
ANISOU 4899  O   ARG B 625     5811   9160  10027   -808  -2142   1625       O  
ATOM   4900  CB  ARG B 625      42.930 102.298 -11.785  1.00 76.81           C  
ANISOU 4900  CB  ARG B 625     6657  10753  11774  -1063  -1835   2062       C  
ATOM   4901  CG  ARG B 625      41.567 102.968 -11.952  1.00 77.86           C  
ANISOU 4901  CG  ARG B 625     7175  10696  11710  -1060  -1802   1894       C  
ATOM   4902  CD  ARG B 625      41.699 104.445 -12.311  1.00 82.08           C  
ANISOU 4902  CD  ARG B 625     7759  11111  12317  -1310  -1870   1988       C  
ATOM   4903  NE  ARG B 625      42.242 105.226 -11.193  1.00 86.82           N  
ANISOU 4903  NE  ARG B 625     8388  11584  13016  -1561  -2209   2010       N  
ATOM   4904  CZ  ARG B 625      41.534 105.651 -10.144  1.00 86.83           C  
ANISOU 4904  CZ  ARG B 625     8720  11383  12888  -1606  -2428   1837       C  
ATOM   4905  NH1 ARG B 625      42.132 106.347  -9.183  1.00 88.79           N  
ANISOU 4905  NH1 ARG B 625     9000  11514  13222  -1841  -2746   1867       N  
ATOM   4906  NH2 ARG B 625      40.231 105.386 -10.048  1.00 87.35           N  
ANISOU 4906  NH2 ARG B 625     9087  11365  12736  -1418  -2333   1640       N  
ATOM   4907  N   GLY B 626      43.274 101.833  -8.803  1.00 70.25           N  
ANISOU 4907  N   GLY B 626     5980   9778  10931  -1171  -2459   1902       N  
ATOM   4908  CA  GLY B 626      42.931 102.233  -7.454  1.00 69.99           C  
ANISOU 4908  CA  GLY B 626     6222   9566  10805  -1281  -2765   1770       C  
ATOM   4909  C   GLY B 626      42.971 101.065  -6.502  1.00 70.09           C  
ANISOU 4909  C   GLY B 626     6252   9628  10751  -1121  -2861   1694       C  
ATOM   4910  O   GLY B 626      43.583 100.032  -6.782  1.00 69.39           O  
ANISOU 4910  O   GLY B 626     5896   9718  10748   -969  -2752   1783       O  
ATOM   4911  N   ASP B 627      42.313 101.238  -5.364  1.00 70.85           N  
ANISOU 4911  N   ASP B 627     6680   9557  10682  -1143  -3059   1532       N  
ATOM   4912  CA  ASP B 627      42.117 100.154  -4.407  1.00 70.00           C  
ANISOU 4912  CA  ASP B 627     6671   9465  10460   -982  -3136   1437       C  
ATOM   4913  C   ASP B 627      40.678 100.189  -3.911  1.00 66.99           C  
ANISOU 4913  C   ASP B 627     6710   8925   9817   -883  -3088   1222       C  
ATOM   4914  O   ASP B 627      40.314 100.996  -3.044  1.00 66.78           O  
ANISOU 4914  O   ASP B 627     6964   8724   9685  -1001  -3288   1128       O  
ATOM   4915  CB  ASP B 627      43.085 100.280  -3.241  1.00 73.44           C  
ANISOU 4915  CB  ASP B 627     7041   9880  10981  -1135  -3498   1500       C  
ATOM   4916  CG  ASP B 627      42.970  99.124  -2.255  1.00 74.12           C  
ANISOU 4916  CG  ASP B 627     7223   9987  10950   -964  -3583   1423       C  
ATOM   4917  OD1 ASP B 627      42.173  98.180  -2.473  1.00 72.88           O  
ANISOU 4917  OD1 ASP B 627     7170   9862  10658   -734  -3357   1328       O  
ATOM   4918  OD2 ASP B 627      43.690  99.165  -1.251  1.00 77.21           O  
ANISOU 4918  OD2 ASP B 627     7594  10358  11384  -1071  -3892   1465       O  
ATOM   4919  N   ILE B 628      39.865  99.297  -4.464  1.00 62.93           N  
ANISOU 4919  N   ILE B 628     6239   8472   9199   -663  -2822   1150       N  
ATOM   4920  CA  ILE B 628      38.444  99.279  -4.174  1.00 59.96           C  
ANISOU 4920  CA  ILE B 628     6204   7979   8598   -560  -2731    972       C  
ATOM   4921  C   ILE B 628      38.152  99.062  -2.687  1.00 59.26           C  
ANISOU 4921  C   ILE B 628     6371   7785   8358   -549  -2937    865       C  
ATOM   4922  O   ILE B 628      37.180  99.603  -2.159  1.00 56.21           O  
ANISOU 4922  O   ILE B 628     6295   7258   7801   -548  -2954    736       O  
ATOM   4923  CB  ILE B 628      37.709  98.226  -5.033  1.00 58.33           C  
ANISOU 4923  CB  ILE B 628     5967   7868   8325   -343  -2435    933       C  
ATOM   4924  CG1 ILE B 628      36.187  98.429  -4.928  1.00 56.29           C  
ANISOU 4924  CG1 ILE B 628     6019   7500   7868   -269  -2327    777       C  
ATOM   4925  CG2 ILE B 628      38.120  96.809  -4.625  1.00 58.22           C  
ANISOU 4925  CG2 ILE B 628     5853   7954   8314   -195  -2436    953       C  
ATOM   4926  CD1 ILE B 628      35.402  97.646  -5.958  1.00 54.07           C  
ANISOU 4926  CD1 ILE B 628     5712   7296   7535   -106  -2056    747       C  
ATOM   4927  N   ARG B 629      39.016  98.314  -2.000  1.00 60.71           N  
ANISOU 4927  N   ARG B 629     6429   8038   8598   -535  -3095    927       N  
ATOM   4928  CA  ARG B 629      38.856  98.094  -0.559  1.00 61.59           C  
ANISOU 4928  CA  ARG B 629     6789   8053   8558   -529  -3310    841       C  
ATOM   4929  C   ARG B 629      38.914  99.393   0.256  1.00 63.93           C  
ANISOU 4929  C   ARG B 629     7319   8174   8796   -725  -3572    792       C  
ATOM   4930  O   ARG B 629      38.389  99.468   1.372  1.00 63.20           O  
ANISOU 4930  O   ARG B 629     7546   7957   8507   -705  -3696    677       O  
ATOM   4931  CB  ARG B 629      39.913  97.117  -0.039  1.00 63.33           C  
ANISOU 4931  CB  ARG B 629     6806   8383   8872   -487  -3460    941       C  
ATOM   4932  CG  ARG B 629      39.817  95.715  -0.608  1.00 61.58           C  
ANISOU 4932  CG  ARG B 629     6433   8296   8666   -265  -3229    969       C  
ATOM   4933  CD  ARG B 629      40.774  94.779   0.124  1.00 63.33           C  
ANISOU 4933  CD  ARG B 629     6519   8594   8949   -202  -3408   1054       C  
ATOM   4934  NE  ARG B 629      40.983  93.519  -0.589  1.00 62.05           N  
ANISOU 4934  NE  ARG B 629     6156   8565   8853      3  -3199   1115       N  
ATOM   4935  CZ  ARG B 629      41.584  92.444  -0.076  1.00 62.94           C  
ANISOU 4935  CZ  ARG B 629     6184   8740   8991    130  -3283   1175       C  
ATOM   4936  NH1 ARG B 629      42.030  92.442   1.172  1.00 62.76           N  
ANISOU 4936  NH1 ARG B 629     6250   8668   8926     69  -3580   1186       N  
ATOM   4937  NH2 ARG B 629      41.719  91.348  -0.818  1.00 62.84           N  
ANISOU 4937  NH2 ARG B 629     6021   8826   9029    331  -3073   1220       N  
ATOM   4938  N   GLN B 630      39.541 100.413  -0.318  1.00 66.65           N  
ANISOU 4938  N   GLN B 630     7522   8500   9302   -912  -3647    881       N  
ATOM   4939  CA  GLN B 630      39.725 101.696   0.353  1.00 69.85           C  
ANISOU 4939  CA  GLN B 630     8143   8720   9675  -1125  -3918    849       C  
ATOM   4940  C   GLN B 630      38.506 102.616   0.218  1.00 66.73           C  
ANISOU 4940  C   GLN B 630     8085   8155   9113  -1104  -3798    709       C  
ATOM   4941  O   GLN B 630      38.454 103.683   0.835  1.00 67.69           O  
ANISOU 4941  O   GLN B 630     8474   8084   9158  -1243  -4002    648       O  
ATOM   4942  CB  GLN B 630      40.937 102.412  -0.247  1.00 73.50           C  
ANISOU 4942  CB  GLN B 630     8297   9228  10399  -1357  -4052   1025       C  
ATOM   4943  CG  GLN B 630      41.902 102.964   0.761  1.00 79.63           C  
ANISOU 4943  CG  GLN B 630     9106   9914  11233  -1584  -4460   1076       C  
ATOM   4944  CD  GLN B 630      42.934 101.938   1.152  1.00 82.02           C  
ANISOU 4944  CD  GLN B 630     9109  10391  11664  -1553  -4596   1197       C  
ATOM   4945  OE1 GLN B 630      42.683 100.735   1.095  1.00 82.43           O  
ANISOU 4945  OE1 GLN B 630     9084  10569  11666  -1322  -4417   1180       O  
ATOM   4946  NE2 GLN B 630      44.100 102.403   1.530  1.00 84.96           N  
ANISOU 4946  NE2 GLN B 630     9307  10766  12208  -1785  -4917   1329       N  
ATOM   4947  N   HIS B 631      37.530 102.236  -0.596  1.00 62.67           N  
ANISOU 4947  N   HIS B 631     7568   7701   8540   -929  -3479    660       N  
ATOM   4948  CA  HIS B 631      36.417 103.132  -0.841  1.00 61.15           C  
ANISOU 4948  CA  HIS B 631     7644   7368   8219   -899  -3359    553       C  
ATOM   4949  C   HIS B 631      35.615 103.388   0.451  1.00 61.51           C  
ANISOU 4949  C   HIS B 631     8108   7247   8015   -835  -3463    393       C  
ATOM   4950  O   HIS B 631      35.359 102.458   1.207  1.00 59.99           O  
ANISOU 4950  O   HIS B 631     7989   7101   7703   -710  -3456    342       O  
ATOM   4951  CB  HIS B 631      35.501 102.588  -1.950  1.00 58.82           C  
ANISOU 4951  CB  HIS B 631     7252   7186   7911   -720  -3016    539       C  
ATOM   4952  CG  HIS B 631      34.582 103.621  -2.498  1.00 57.69           C  
ANISOU 4952  CG  HIS B 631     7289   6925   7703   -712  -2900    479       C  
ATOM   4953  ND1 HIS B 631      33.428 103.993  -1.851  1.00 57.83           N  
ANISOU 4953  ND1 HIS B 631     7642   6814   7517   -606  -2865    337       N  
ATOM   4954  CD2 HIS B 631      34.672 104.409  -3.594  1.00 58.59           C  
ANISOU 4954  CD2 HIS B 631     7306   7027   7927   -792  -2817    550       C  
ATOM   4955  CE1 HIS B 631      32.824 104.943  -2.542  1.00 57.98           C  
ANISOU 4955  CE1 HIS B 631     7754   6747   7529   -607  -2768    320       C  
ATOM   4956  NE2 HIS B 631      33.558 105.214  -3.606  1.00 57.98           N  
ANISOU 4956  NE2 HIS B 631     7505   6810   7714   -725  -2743    448       N  
ATOM   4957  N   PRO B 632      35.209 104.650   0.702  1.00 64.17           N  
ANISOU 4957  N   PRO B 632     8736   7382   8262   -908  -3549    317       N  
ATOM   4958  CA  PRO B 632      34.451 105.010   1.909  1.00 64.92           C  
ANISOU 4958  CA  PRO B 632     9260   7304   8101   -830  -3631    163       C  
ATOM   4959  C   PRO B 632      33.218 104.163   2.227  1.00 62.74           C  
ANISOU 4959  C   PRO B 632     9109   7093   7636   -577  -3387     66       C  
ATOM   4960  O   PRO B 632      32.871 103.999   3.385  1.00 63.15           O  
ANISOU 4960  O   PRO B 632     9437   7067   7487   -503  -3462    -25       O  
ATOM   4961  CB  PRO B 632      34.029 106.447   1.624  1.00 66.54           C  
ANISOU 4961  CB  PRO B 632     9698   7311   8273   -896  -3647    113       C  
ATOM   4962  CG  PRO B 632      35.143 106.989   0.810  1.00 67.80           C  
ANISOU 4962  CG  PRO B 632     9593   7485   8680  -1130  -3771    258       C  
ATOM   4963  CD  PRO B 632      35.593 105.852  -0.064  1.00 65.73           C  
ANISOU 4963  CD  PRO B 632     8892   7486   8595  -1085  -3603    384       C  
ATOM   4964  N   LEU B 633      32.540 103.650   1.208  1.00 62.31           N  
ANISOU 4964  N   LEU B 633     8862   7175   7638   -453  -3100     91       N  
ATOM   4965  CA  LEU B 633      31.433 102.719   1.424  1.00 59.73           C  
ANISOU 4965  CA  LEU B 633     8593   6933   7169   -242  -2874     28       C  
ATOM   4966  C   LEU B 633      31.854 101.577   2.339  1.00 59.47           C  
ANISOU 4966  C   LEU B 633     8546   6971   7077   -209  -2965     37       C  
ATOM   4967  O   LEU B 633      31.047 101.070   3.120  1.00 57.80           O  
ANISOU 4967  O   LEU B 633     8528   6753   6681    -73  -2880    -34       O  
ATOM   4968  CB  LEU B 633      30.944 102.136   0.107  1.00 58.92           C  
ANISOU 4968  CB  LEU B 633     8222   6986   7177   -159  -2610     82       C  
ATOM   4969  CG  LEU B 633      29.658 101.294   0.176  1.00 58.58           C  
ANISOU 4969  CG  LEU B 633     8229   7022   7006     33  -2372     26       C  
ATOM   4970  CD1 LEU B 633      28.462 102.141   0.600  1.00 59.62           C  
ANISOU 4970  CD1 LEU B 633     8648   7036   6968    138  -2284    -72       C  
ATOM   4971  CD2 LEU B 633      29.390 100.626  -1.163  1.00 56.93           C  
ANISOU 4971  CD2 LEU B 633     7745   6964   6922     82  -2167     90       C  
ATOM   4972  N   PHE B 634      33.112 101.166   2.216  1.00 59.10           N  
ANISOU 4972  N   PHE B 634     8262   6999   7193   -327  -3128    139       N  
ATOM   4973  CA  PHE B 634      33.618 100.041   2.981  1.00 59.87           C  
ANISOU 4973  CA  PHE B 634     8315   7172   7260   -289  -3225    168       C  
ATOM   4974  C   PHE B 634      34.394 100.490   4.224  1.00 63.69           C  
ANISOU 4974  C   PHE B 634     9001   7533   7666   -407  -3562    150       C  
ATOM   4975  O   PHE B 634      35.060  99.674   4.847  1.00 65.05           O  
ANISOU 4975  O   PHE B 634     9112   7762   7840   -406  -3704    196       O  
ATOM   4976  CB  PHE B 634      34.487  99.143   2.086  1.00 58.10           C  
ANISOU 4976  CB  PHE B 634     7692   7124   7257   -300  -3179    299       C  
ATOM   4977  CG  PHE B 634      33.760  98.579   0.882  1.00 55.61           C  
ANISOU 4977  CG  PHE B 634     7209   6923   6995   -180  -2868    311       C  
ATOM   4978  CD1 PHE B 634      32.717  97.678   1.037  1.00 52.94           C  
ANISOU 4978  CD1 PHE B 634     6966   6623   6523    -20  -2678    253       C  
ATOM   4979  CD2 PHE B 634      34.136  98.940  -0.410  1.00 54.84           C  
ANISOU 4979  CD2 PHE B 634     6864   6892   7077   -238  -2776    390       C  
ATOM   4980  CE1 PHE B 634      32.061  97.156  -0.066  1.00 52.22           C  
ANISOU 4980  CE1 PHE B 634     6734   6626   6480     69  -2428    265       C  
ATOM   4981  CE2 PHE B 634      33.486  98.412  -1.509  1.00 52.97           C  
ANISOU 4981  CE2 PHE B 634     6504   6751   6870   -129  -2513    397       C  
ATOM   4982  CZ  PHE B 634      32.442  97.522  -1.337  1.00 50.76           C  
ANISOU 4982  CZ  PHE B 634     6328   6500   6458     20  -2352    330       C  
ATOM   4983  N   ARG B 635      34.282 101.773   4.586  1.00 67.71           N  
ANISOU 4983  N   ARG B 635     9769   7861   8095   -502  -3697     80       N  
ATOM   4984  CA  ARG B 635      34.907 102.356   5.797  1.00 72.39           C  
ANISOU 4984  CA  ARG B 635    10631   8294   8576   -625  -4040     40       C  
ATOM   4985  C   ARG B 635      34.908 101.466   7.025  1.00 72.72           C  
ANISOU 4985  C   ARG B 635    10850   8346   8433   -533  -4138      6       C  
ATOM   4986  O   ARG B 635      35.905 101.395   7.742  1.00 74.50           O  
ANISOU 4986  O   ARG B 635    11088   8543   8674   -651  -4449     48       O  
ATOM   4987  CB  ARG B 635      34.160 103.626   6.225  1.00 75.95           C  
ANISOU 4987  CB  ARG B 635    11494   8523   8840   -623  -4062    -90       C  
ATOM   4988  CG  ARG B 635      34.824 104.956   5.893  1.00 81.37           C  
ANISOU 4988  CG  ARG B 635    12212   9057   9645   -845  -4277    -67       C  
ATOM   4989  CD  ARG B 635      34.054 106.109   6.548  1.00 85.17           C  
ANISOU 4989  CD  ARG B 635    13184   9285   9888   -804  -4318   -218       C  
ATOM   4990  NE  ARG B 635      32.606 105.878   6.465  1.00 83.73           N  
ANISOU 4990  NE  ARG B 635    13141   9133   9538   -541  -3969   -308       N  
ATOM   4991  CZ  ARG B 635      31.737 106.580   5.738  1.00 86.95           C  
ANISOU 4991  CZ  ARG B 635    13600   9490   9946   -454  -3755   -346       C  
ATOM   4992  NH1 ARG B 635      32.113 107.650   5.035  1.00 89.11           N  
ANISOU 4992  NH1 ARG B 635    13850   9651  10356   -607  -3846   -313       N  
ATOM   4993  NH2 ARG B 635      30.456 106.216   5.735  1.00 86.15           N  
ANISOU 4993  NH2 ARG B 635    13577   9451   9705   -213  -3451   -408       N  
ATOM   4994  N   GLU B 636      33.760 100.859   7.310  1.00 71.09           N  
ANISOU 4994  N   GLU B 636    10799   8168   8041   -329  -3886    -66       N  
ATOM   4995  CA  GLU B 636      33.573 100.109   8.555  1.00 73.94           C  
ANISOU 4995  CA  GLU B 636    11401   8513   8177   -228  -3948   -107       C  
ATOM   4996  C   GLU B 636      33.991  98.648   8.441  1.00 71.85           C  
ANISOU 4996  C   GLU B 636    10864   8424   8009   -168  -3904     -5       C  
ATOM   4997  O   GLU B 636      33.877  97.911   9.405  1.00 73.30           O  
ANISOU 4997  O   GLU B 636    11222   8605   8022    -84  -3948    -18       O  
ATOM   4998  CB  GLU B 636      32.114 100.196   9.024  1.00 75.34           C  
ANISOU 4998  CB  GLU B 636    11898   8631   8093    -40  -3692   -220       C  
ATOM   4999  CG  GLU B 636      31.708 101.575   9.531  1.00 80.36           C  
ANISOU 4999  CG  GLU B 636    12919   9057   8555    -53  -3769   -339       C  
ATOM   5000  CD  GLU B 636      30.208 101.707   9.768  1.00 82.13           C  
ANISOU 5000  CD  GLU B 636    13387   9254   8563    160  -3456   -431       C  
ATOM   5001  OE1 GLU B 636      29.432 100.913   9.194  1.00 80.45           O  
ANISOU 5001  OE1 GLU B 636    12969   9195   8401    280  -3163   -391       O  
ATOM   5002  OE2 GLU B 636      29.797 102.611  10.530  1.00 85.45           O  
ANISOU 5002  OE2 GLU B 636    14207   9497   8761    212  -3506   -540       O  
ATOM   5003  N   ILE B 637      34.480  98.226   7.278  1.00 69.99           N  
ANISOU 5003  N   ILE B 637    10225   8332   8035   -200  -3816     96       N  
ATOM   5004  CA  ILE B 637      34.837  96.822   7.065  1.00 67.48           C  
ANISOU 5004  CA  ILE B 637     9660   8169   7810   -116  -3749    188       C  
ATOM   5005  C   ILE B 637      36.280  96.526   7.464  1.00 68.19           C  
ANISOU 5005  C   ILE B 637     9586   8296   8026   -217  -4065    291       C  
ATOM   5006  O   ILE B 637      37.212  97.170   6.984  1.00 67.68           O  
ANISOU 5006  O   ILE B 637     9309   8246   8159   -370  -4226    362       O  
ATOM   5007  CB  ILE B 637      34.674  96.402   5.589  1.00 65.83           C  
ANISOU 5007  CB  ILE B 637     9108   8098   7806    -71  -3486    249       C  
ATOM   5008  CG1 ILE B 637      33.204  96.508   5.147  1.00 64.10           C  
ANISOU 5008  CG1 ILE B 637     9010   7867   7477     39  -3175    165       C  
ATOM   5009  CG2 ILE B 637      35.223  94.990   5.364  1.00 66.65           C  
ANISOU 5009  CG2 ILE B 637     8971   8339   8014     15  -3451    346       C  
ATOM   5010  CD1 ILE B 637      32.215  95.771   6.026  1.00 63.40           C  
ANISOU 5010  CD1 ILE B 637     9169   7759   7158    178  -3054    107       C  
ATOM   5011  N   ASN B 638      36.452  95.535   8.332  1.00 67.95           N  
ANISOU 5011  N   ASN B 638     9643   8286   7885   -131  -4151    313       N  
ATOM   5012  CA  ASN B 638      37.774  94.976   8.599  1.00 68.63           C  
ANISOU 5012  CA  ASN B 638     9516   8447   8113   -179  -4413    434       C  
ATOM   5013  C   ASN B 638      37.979  93.790   7.672  1.00 67.48           C  
ANISOU 5013  C   ASN B 638     9027   8465   8145    -56  -4209    531       C  
ATOM   5014  O   ASN B 638      37.406  92.721   7.889  1.00 67.61           O  
ANISOU 5014  O   ASN B 638     9131   8506   8051     97  -4053    520       O  
ATOM   5015  CB  ASN B 638      37.904  94.533  10.050  1.00 69.72           C  
ANISOU 5015  CB  ASN B 638     9952   8509   8028   -142  -4639    413       C  
ATOM   5016  CG  ASN B 638      39.299  94.030  10.374  1.00 70.43           C  
ANISOU 5016  CG  ASN B 638     9818   8672   8267   -192  -4949    546       C  
ATOM   5017  OD1 ASN B 638      39.899  93.258   9.612  1.00 67.99           O  
ANISOU 5017  OD1 ASN B 638     9140   8510   8180   -133  -4874    661       O  
ATOM   5018  ND2 ASN B 638      39.831  94.480  11.498  1.00 73.44           N  
ANISOU 5018  ND2 ASN B 638    10424   8951   8526   -295  -5305    533       N  
ATOM   5019  N   TRP B 639      38.788  93.983   6.637  1.00 67.30           N  
ANISOU 5019  N   TRP B 639     8633   8547   8390   -122  -4203    630       N  
ATOM   5020  CA  TRP B 639      38.902  93.001   5.567  1.00 67.01           C  
ANISOU 5020  CA  TRP B 639     8292   8653   8512      8  -3965    707       C  
ATOM   5021  C   TRP B 639      39.485  91.646   6.068  1.00 68.07           C  
ANISOU 5021  C   TRP B 639     8354   8854   8654    145  -4045    789       C  
ATOM   5022  O   TRP B 639      39.070  90.564   5.642  1.00 67.44           O  
ANISOU 5022  O   TRP B 639     8237   8823   8561    308  -3825    795       O  
ATOM   5023  CB  TRP B 639      39.693  93.608   4.394  1.00 66.72           C  
ANISOU 5023  CB  TRP B 639     7890   8712   8744    -91  -3939    804       C  
ATOM   5024  CG  TRP B 639      38.947  94.752   3.732  1.00 65.57           C  
ANISOU 5024  CG  TRP B 639     7830   8500   8583   -186  -3796    725       C  
ATOM   5025  CD1 TRP B 639      39.049  96.085   4.020  1.00 66.40           C  
ANISOU 5025  CD1 TRP B 639     8059   8494   8676   -370  -3971    691       C  
ATOM   5026  CD2 TRP B 639      37.957  94.642   2.691  1.00 62.23           C  
ANISOU 5026  CD2 TRP B 639     7398   8103   8143    -95  -3462    672       C  
ATOM   5027  NE1 TRP B 639      38.187  96.812   3.212  1.00 65.24           N  
ANISOU 5027  NE1 TRP B 639     7975   8304   8509   -383  -3753    624       N  
ATOM   5028  CE2 TRP B 639      37.511  95.950   2.390  1.00 61.61           C  
ANISOU 5028  CE2 TRP B 639     7425   7936   8048   -218  -3446    613       C  
ATOM   5029  CE3 TRP B 639      37.417  93.565   1.980  1.00 60.30           C  
ANISOU 5029  CE3 TRP B 639     7077   7939   7893     74  -3194    669       C  
ATOM   5030  CZ2 TRP B 639      36.548  96.209   1.404  1.00 60.58           C  
ANISOU 5030  CZ2 TRP B 639     7307   7808   7900   -168  -3171    561       C  
ATOM   5031  CZ3 TRP B 639      36.450  93.826   0.993  1.00 58.65           C  
ANISOU 5031  CZ3 TRP B 639     6886   7731   7665    106  -2932    612       C  
ATOM   5032  CH2 TRP B 639      36.028  95.137   0.721  1.00 57.99           C  
ANISOU 5032  CH2 TRP B 639     6891   7573   7570     -9  -2924    562       C  
ATOM   5033  N   GLU B 640      40.404  91.695   7.019  1.00 73.48           N  
ANISOU 5033  N   GLU B 640     9050   9524   9344     82  -4376    849       N  
ATOM   5034  CA  GLU B 640      41.054  90.459   7.522  1.00 73.13           C  
ANISOU 5034  CA  GLU B 640     8928   9540   9315    218  -4485    942       C  
ATOM   5035  C   GLU B 640      40.153  89.578   8.430  1.00 72.30           C  
ANISOU 5035  C   GLU B 640     9186   9346   8938    353  -4419    867       C  
ATOM   5036  O   GLU B 640      40.127  88.310   8.294  1.00 73.39           O  
ANISOU 5036  O   GLU B 640     9273   9528   9081    525  -4297    916       O  
ATOM   5037  CB  GLU B 640      42.323  90.793   8.288  1.00 79.23           C  
ANISOU 5037  CB  GLU B 640     9594  10330  10180    104  -4890   1043       C  
ATOM   5038  CG  GLU B 640      43.391  91.485   7.449  1.00 81.54           C  
ANISOU 5038  CG  GLU B 640     9469  10736  10775    -30  -4976   1164       C  
ATOM   5039  CD  GLU B 640      42.918  92.826   6.888  1.00 82.20           C  
ANISOU 5039  CD  GLU B 640     9604  10753  10873   -208  -4896   1087       C  
ATOM   5040  OE1 GLU B 640      42.460  93.670   7.685  1.00 83.69           O  
ANISOU 5040  OE1 GLU B 640    10129  10788  10878   -333  -5051    979       O  
ATOM   5041  OE2 GLU B 640      42.958  93.037   5.646  1.00 82.52           O  
ANISOU 5041  OE2 GLU B 640     9379  10883  11091   -211  -4667   1130       O  
ATOM   5042  N   GLU B 641      39.339  90.274   9.255  1.00 70.56           N  
ANISOU 5042  N   GLU B 641     9337   8994   8478    279  -4461    748       N  
ATOM   5043  CA  GLU B 641      38.184  89.645   9.945  1.00 69.89           C  
ANISOU 5043  CA  GLU B 641     9606   8828   8121    391  -4303    666       C  
ATOM   5044  C   GLU B 641      37.065  89.168   8.967  1.00 67.27           C  
ANISOU 5044  C   GLU B 641     9234   8528   7796    487  -3906    621       C  
ATOM   5045  O   GLU B 641      36.436  88.118   9.150  1.00 65.40           O  
ANISOU 5045  O   GLU B 641     9116   8281   7450    608  -3749    622       O  
ATOM   5046  CB  GLU B 641      37.562  90.624  10.939  1.00 71.27           C  
ANISOU 5046  CB  GLU B 641    10170   8864   8043    305  -4403    552       C  
ATOM   5047  CG  GLU B 641      38.447  90.982  12.129  1.00 75.74           C  
ANISOU 5047  CG  GLU B 641    10896   9361   8518    219  -4808    574       C  
ATOM   5048  CD  GLU B 641      37.769  91.924  13.116  1.00 76.83           C  
ANISOU 5048  CD  GLU B 641    11480   9343   8369    158  -4887    445       C  
ATOM   5049  OE1 GLU B 641      36.646  92.415  12.853  1.00 75.98           O  
ANISOU 5049  OE1 GLU B 641    11526   9187   8153    184  -4624    343       O  
ATOM   5050  OE2 GLU B 641      38.365  92.178  14.174  1.00 81.84           O  
ANISOU 5050  OE2 GLU B 641    12320   9898   8876     95  -5219    448       O  
ATOM   5051  N   LEU B 642      36.806  89.948   7.930  1.00 66.05           N  
ANISOU 5051  N   LEU B 642     8922   8405   7766    420  -3756    586       N  
ATOM   5052  CA  LEU B 642      35.738  89.583   6.973  1.00 64.17           C  
ANISOU 5052  CA  LEU B 642     8648   8197   7534    495  -3411    543       C  
ATOM   5053  C   LEU B 642      36.049  88.263   6.260  1.00 63.91           C  
ANISOU 5053  C   LEU B 642     8407   8248   7628    624  -3288    623       C  
ATOM   5054  O   LEU B 642      35.181  87.340   6.155  1.00 62.09           O  
ANISOU 5054  O   LEU B 642     8285   8000   7305    720  -3088    603       O  
ATOM   5055  CB  LEU B 642      35.573  90.663   5.919  1.00 62.16           C  
ANISOU 5055  CB  LEU B 642     8241   7968   7408    404  -3304    509       C  
ATOM   5056  CG  LEU B 642      34.432  90.369   4.938  1.00 60.33           C  
ANISOU 5056  CG  LEU B 642     7985   7765   7173    471  -2977    463       C  
ATOM   5057  CD1 LEU B 642      33.084  90.360   5.656  1.00 60.22           C  
ANISOU 5057  CD1 LEU B 642     8285   7674   6923    506  -2850    376       C  
ATOM   5058  CD2 LEU B 642      34.457  91.383   3.806  1.00 59.11           C  
ANISOU 5058  CD2 LEU B 642     7650   7643   7163    389  -2893    453       C  
ATOM   5059  N   GLU B 643      37.302  88.203   5.789  1.00 66.55           N  
ANISOU 5059  N   GLU B 643     8445   8667   8174    623  -3414    721       N  
ATOM   5060  CA  GLU B 643      37.842  87.037   5.098  1.00 68.45           C  
ANISOU 5060  CA  GLU B 643     8469   8987   8551    767  -3323    807       C  
ATOM   5061  C   GLU B 643      37.910  85.790   6.000  1.00 69.21           C  
ANISOU 5061  C   GLU B 643     8729   9037   8531    895  -3400    846       C  
ATOM   5062  O   GLU B 643      37.769  84.672   5.510  1.00 67.99           O  
ANISOU 5062  O   GLU B 643     8542   8890   8399   1033  -3247    873       O  
ATOM   5063  CB  GLU B 643      39.241  87.362   4.541  1.00 71.19           C  
ANISOU 5063  CB  GLU B 643     8453   9447   9148    743  -3455    921       C  
ATOM   5064  CG  GLU B 643      39.667  86.466   3.383  1.00 72.12           C  
ANISOU 5064  CG  GLU B 643     8312   9662   9429    900  -3265    994       C  
ATOM   5065  CD  GLU B 643      40.495  87.200   2.337  1.00 73.09           C  
ANISOU 5065  CD  GLU B 643     8085   9902   9781    842  -3233   1070       C  
ATOM   5066  OE1 GLU B 643      41.470  87.886   2.729  1.00 75.42           O  
ANISOU 5066  OE1 GLU B 643     8213  10246  10195    732  -3470   1151       O  
ATOM   5067  OE2 GLU B 643      40.171  87.083   1.121  1.00 69.85           O  
ANISOU 5067  OE2 GLU B 643     7572   9537   9430    900  -2976   1055       O  
ATOM   5068  N   ARG B 644      38.105  85.989   7.303  1.00 70.29           N  
ANISOU 5068  N   ARG B 644     9067   9111   8529    847  -3641    846       N  
ATOM   5069  CA  ARG B 644      38.128  84.883   8.271  1.00 73.42           C  
ANISOU 5069  CA  ARG B 644     9661   9449   8783    959  -3729    887       C  
ATOM   5070  C   ARG B 644      36.746  84.594   8.878  1.00 73.32           C  
ANISOU 5070  C   ARG B 644    10008   9334   8513    965  -3569    803       C  
ATOM   5071  O   ARG B 644      36.634  83.841   9.852  1.00 73.53           O  
ANISOU 5071  O   ARG B 644    10264   9295   8378   1028  -3646    833       O  
ATOM   5072  CB  ARG B 644      39.140  85.181   9.379  1.00 78.41           C  
ANISOU 5072  CB  ARG B 644    10327  10072   9392    913  -4096    947       C  
ATOM   5073  CG  ARG B 644      40.540  85.397   8.846  1.00 81.61           C  
ANISOU 5073  CG  ARG B 644    10342  10596  10070    903  -4266   1059       C  
ATOM   5074  CD  ARG B 644      41.565  85.324   9.939  1.00 88.65           C  
ANISOU 5074  CD  ARG B 644    11247  11486  10950    892  -4640   1148       C  
ATOM   5075  NE  ARG B 644      41.445  86.412  10.910  1.00 92.60           N  
ANISOU 5075  NE  ARG B 644    11988  11902  11293    716  -4874   1079       N  
ATOM   5076  CZ  ARG B 644      42.358  87.365  11.114  1.00 96.99           C  
ANISOU 5076  CZ  ARG B 644    12399  12488  11965    560  -5166   1122       C  
ATOM   5077  NH1 ARG B 644      43.482  87.416  10.397  1.00 97.84           N  
ANISOU 5077  NH1 ARG B 644    12074  12731  12369    548  -5250   1249       N  
ATOM   5078  NH2 ARG B 644      42.144  88.284  12.055  1.00 98.73           N  
ANISOU 5078  NH2 ARG B 644    12916  12596  11999    412  -5378   1042       N  
ATOM   5079  N   LYS B 645      35.701  85.192   8.298  1.00 70.86           N  
ANISOU 5079  N   LYS B 645     9737   9016   8169    901  -3343    713       N  
ATOM   5080  CA  LYS B 645      34.304  84.974   8.715  1.00 70.95           C  
ANISOU 5080  CA  LYS B 645    10030   8958   7968    904  -3148    648       C  
ATOM   5081  C   LYS B 645      34.021  85.289  10.189  1.00 73.35           C  
ANISOU 5081  C   LYS B 645    10671   9179   8020    875  -3284    621       C  
ATOM   5082  O   LYS B 645      33.177  84.653  10.815  1.00 75.50           O  
ANISOU 5082  O   LYS B 645    11182   9398   8107    919  -3168    622       O  
ATOM   5083  CB  LYS B 645      33.858  83.546   8.377  1.00 70.62           C  
ANISOU 5083  CB  LYS B 645    10008   8899   7922   1011  -2974    693       C  
ATOM   5084  CG  LYS B 645      33.746  83.274   6.884  1.00 69.20           C  
ANISOU 5084  CG  LYS B 645     9583   8778   7929   1040  -2779    688       C  
ATOM   5085  CD  LYS B 645      33.919  81.791   6.589  1.00 71.89           C  
ANISOU 5085  CD  LYS B 645     9917   9090   8308   1167  -2720    754       C  
ATOM   5086  CE  LYS B 645      32.632  81.001   6.750  1.00 71.20           C  
ANISOU 5086  CE  LYS B 645    10052   8925   8076   1162  -2531    738       C  
ATOM   5087  NZ  LYS B 645      31.915  80.962   5.442  1.00 71.36           N  
ANISOU 5087  NZ  LYS B 645     9951   8972   8189   1138  -2309    691       N  
ATOM   5088  N   GLU B 646      34.711  86.289  10.724  1.00 74.05           N  
ANISOU 5088  N   GLU B 646    10787   9252   8095    795  -3528    601       N  
ATOM   5089  CA  GLU B 646      34.507  86.740  12.100  1.00 76.00           C  
ANISOU 5089  CA  GLU B 646    11385   9409   8083    766  -3681    561       C  
ATOM   5090  C   GLU B 646      33.542  87.926  12.195  1.00 76.44           C  
ANISOU 5090  C   GLU B 646    11618   9418   8007    701  -3554    445       C  
ATOM   5091  O   GLU B 646      33.365  88.501  13.261  1.00 82.15           O  
ANISOU 5091  O   GLU B 646    12648  10056   8507    681  -3670    393       O  
ATOM   5092  CB  GLU B 646      35.853  87.109  12.717  1.00 78.74           C  
ANISOU 5092  CB  GLU B 646    11699   9746   8473    712  -4064    606       C  
ATOM   5093  CG  GLU B 646      36.783  85.916  12.882  1.00 80.42           C  
ANISOU 5093  CG  GLU B 646    11785   9996   8772    807  -4213    730       C  
ATOM   5094  CD  GLU B 646      38.219  86.318  13.165  1.00 84.15           C  
ANISOU 5094  CD  GLU B 646    12092  10501   9378    745  -4587    799       C  
ATOM   5095  OE1 GLU B 646      38.510  87.530  13.255  1.00 87.07           O  
ANISOU 5095  OE1 GLU B 646    12460  10852   9768    603  -4747    750       O  
ATOM   5096  OE2 GLU B 646      39.064  85.414  13.298  1.00 85.12           O  
ANISOU 5096  OE2 GLU B 646    12084  10666   9592    836  -4729    910       O  
ATOM   5097  N   ILE B 647      32.927  88.300  11.082  1.00 73.40           N  
ANISOU 5097  N   ILE B 647    11054   9082   7752    681  -3321    405       N  
ATOM   5098  CA  ILE B 647      31.883  89.305  11.099  1.00 72.83           C  
ANISOU 5098  CA  ILE B 647    11138   8970   7561    654  -3162    306       C  
ATOM   5099  C   ILE B 647      30.576  88.567  10.857  1.00 70.76           C  
ANISOU 5099  C   ILE B 647    10919   8738   7228    730  -2836    310       C  
ATOM   5100  O   ILE B 647      30.432  87.904   9.844  1.00 70.05           O  
ANISOU 5100  O   ILE B 647    10595   8715   7303    747  -2690    349       O  
ATOM   5101  CB  ILE B 647      32.160  90.399  10.048  1.00 71.71           C  
ANISOU 5101  CB  ILE B 647    10772   8857   7618    565  -3167    268       C  
ATOM   5102  CG1 ILE B 647      33.306  91.296  10.554  1.00 74.12           C  
ANISOU 5102  CG1 ILE B 647    11109   9104   7947    458  -3508    262       C  
ATOM   5103  CG2 ILE B 647      30.906  91.223   9.768  1.00 70.54           C  
ANISOU 5103  CG2 ILE B 647    10731   8684   7385    574  -2931    179       C  
ATOM   5104  CD1 ILE B 647      33.955  92.169   9.503  1.00 73.26           C  
ANISOU 5104  CD1 ILE B 647    10719   9032   8082    348  -3569    271       C  
ATOM   5105  N   ASP B 648      29.651  88.647  11.810  1.00 71.77           N  
ANISOU 5105  N   ASP B 648    11349   8814   7104    775  -2730    277       N  
ATOM   5106  CA  ASP B 648      28.364  87.972  11.692  1.00 71.18           C  
ANISOU 5106  CA  ASP B 648    11311   8774   6958    830  -2425    300       C  
ATOM   5107  C   ASP B 648      27.515  88.636  10.600  1.00 67.17           C  
ANISOU 5107  C   ASP B 648    10625   8322   6571    812  -2205    251       C  
ATOM   5108  O   ASP B 648      27.309  89.849  10.609  1.00 67.22           O  
ANISOU 5108  O   ASP B 648    10697   8300   6541    799  -2209    174       O  
ATOM   5109  CB  ASP B 648      27.593  87.981  13.013  1.00 73.84           C  
ANISOU 5109  CB  ASP B 648    12008   9057   6990    890  -2347    292       C  
ATOM   5110  CG  ASP B 648      28.237  87.114  14.079  1.00 77.79           C  
ANISOU 5110  CG  ASP B 648    12705   9504   7347    920  -2527    360       C  
ATOM   5111  OD1 ASP B 648      28.692  85.988  13.771  1.00 77.91           O  
ANISOU 5111  OD1 ASP B 648    12581   9541   7478    926  -2566    444       O  
ATOM   5112  OD2 ASP B 648      28.273  87.559  15.245  1.00 82.81           O  
ANISOU 5112  OD2 ASP B 648    13659  10067   7736    949  -2631    328       O  
ATOM   5113  N   PRO B 649      27.028  87.835   9.645  1.00 63.25           N  
ANISOU 5113  N   PRO B 649     9920   7893   6217    812  -2028    298       N  
ATOM   5114  CA  PRO B 649      26.240  88.415   8.568  1.00 60.95           C  
ANISOU 5114  CA  PRO B 649     9456   7659   6042    793  -1842    260       C  
ATOM   5115  C   PRO B 649      25.012  89.149   9.103  1.00 60.89           C  
ANISOU 5115  C   PRO B 649     9622   7648   5865    837  -1660    218       C  
ATOM   5116  O   PRO B 649      24.390  88.694  10.054  1.00 60.91           O  
ANISOU 5116  O   PRO B 649     9823   7637   5681    884  -1564    251       O  
ATOM   5117  CB  PRO B 649      25.818  87.215   7.721  1.00 60.21           C  
ANISOU 5117  CB  PRO B 649     9187   7619   6069    787  -1697    325       C  
ATOM   5118  CG  PRO B 649      26.566  86.034   8.229  1.00 60.71           C  
ANISOU 5118  CG  PRO B 649     9310   7646   6111    807  -1821    394       C  
ATOM   5119  CD  PRO B 649      27.239  86.385   9.509  1.00 62.82           C  
ANISOU 5119  CD  PRO B 649     9801   7851   6217    828  -2017    385       C  
ATOM   5120  N   PRO B 650      24.667  90.288   8.497  1.00 59.58           N  
ANISOU 5120  N   PRO B 650     9385   7492   5758    833  -1603    153       N  
ATOM   5121  CA  PRO B 650      23.501  91.025   8.968  1.00 60.17           C  
ANISOU 5121  CA  PRO B 650     9616   7566   5679    906  -1418    115       C  
ATOM   5122  C   PRO B 650      22.176  90.320   8.676  1.00 58.95           C  
ANISOU 5122  C   PRO B 650     9364   7504   5531    934  -1143    182       C  
ATOM   5123  O   PRO B 650      21.157  90.695   9.222  1.00 59.49           O  
ANISOU 5123  O   PRO B 650     9552   7591   5458   1011   -962    181       O  
ATOM   5124  CB  PRO B 650      23.581  92.337   8.191  1.00 60.62           C  
ANISOU 5124  CB  PRO B 650     9587   7605   5841    892  -1447     41       C  
ATOM   5125  CG  PRO B 650      24.332  91.997   6.950  1.00 58.30           C  
ANISOU 5125  CG  PRO B 650     9003   7355   5793    806  -1532     68       C  
ATOM   5126  CD  PRO B 650      25.327  90.952   7.360  1.00 59.31           C  
ANISOU 5126  CD  PRO B 650     9132   7471   5931    774  -1695    121       C  
ATOM   5127  N   PHE B 651      22.189  89.320   7.807  1.00 56.39           N  
ANISOU 5127  N   PHE B 651     8820   7234   5370    872  -1113    243       N  
ATOM   5128  CA  PHE B 651      20.994  88.565   7.496  1.00 55.20           C  
ANISOU 5128  CA  PHE B 651     8567   7162   5243    863   -891    317       C  
ATOM   5129  C   PHE B 651      21.315  87.086   7.627  1.00 55.17           C  
ANISOU 5129  C   PHE B 651     8563   7143   5257    812   -932    399       C  
ATOM   5130  O   PHE B 651      22.297  86.610   7.045  1.00 54.64           O  
ANISOU 5130  O   PHE B 651     8399   7047   5314    776  -1085    395       O  
ATOM   5131  CB  PHE B 651      20.544  88.876   6.060  1.00 53.72           C  
ANISOU 5131  CB  PHE B 651     8117   7042   5252    827   -817    305       C  
ATOM   5132  CG  PHE B 651      19.410  88.018   5.580  1.00 52.68           C  
ANISOU 5132  CG  PHE B 651     7847   6988   5179    785   -638    387       C  
ATOM   5133  CD1 PHE B 651      18.101  88.347   5.892  1.00 53.90           C  
ANISOU 5133  CD1 PHE B 651     7998   7214   5265    829   -431    426       C  
ATOM   5134  CD2 PHE B 651      19.649  86.897   4.802  1.00 52.32           C  
ANISOU 5134  CD2 PHE B 651     7676   6942   5261    703   -681    431       C  
ATOM   5135  CE1 PHE B 651      17.047  87.574   5.444  1.00 54.23           C  
ANISOU 5135  CE1 PHE B 651     7887   7337   5380    766   -284    518       C  
ATOM   5136  CE2 PHE B 651      18.599  86.110   4.358  1.00 52.25           C  
ANISOU 5136  CE2 PHE B 651     7556   6988   5306    639   -545    509       C  
ATOM   5137  CZ  PHE B 651      17.295  86.449   4.683  1.00 53.91           C  
ANISOU 5137  CZ  PHE B 651     7738   7281   5465    657   -354    558       C  
ATOM   5138  N   ARG B 652      20.491  86.369   8.385  1.00 55.60           N  
ANISOU 5138  N   ARG B 652     8728   7212   5185    818   -788    480       N  
ATOM   5139  CA  ARG B 652      20.599  84.921   8.506  1.00 56.43           C  
ANISOU 5139  CA  ARG B 652     8851   7287   5300    762   -802    571       C  
ATOM   5140  C   ARG B 652      19.367  84.326   7.854  1.00 56.11           C  
ANISOU 5140  C   ARG B 652     8651   7317   5348    691   -606    647       C  
ATOM   5141  O   ARG B 652      18.252  84.693   8.215  1.00 55.39           O  
ANISOU 5141  O   ARG B 652     8564   7297   5184    710   -414    686       O  
ATOM   5142  CB  ARG B 652      20.698  84.472   9.975  1.00 58.74           C  
ANISOU 5142  CB  ARG B 652     9425   7526   5366    803   -812    626       C  
ATOM   5143  CG  ARG B 652      20.316  83.003  10.190  1.00 59.84           C  
ANISOU 5143  CG  ARG B 652     9602   7642   5490    741   -743    749       C  
ATOM   5144  CD  ARG B 652      20.563  82.513  11.620  1.00 62.19           C  
ANISOU 5144  CD  ARG B 652    10196   7874   5558    784   -777    811       C  
ATOM   5145  NE  ARG B 652      21.928  82.043  11.656  1.00 62.50           N  
ANISOU 5145  NE  ARG B 652    10287   7825   5633    800  -1035    791       N  
ATOM   5146  CZ  ARG B 652      22.327  80.787  11.612  1.00 61.66           C  
ANISOU 5146  CZ  ARG B 652    10209   7651   5566    771  -1108    868       C  
ATOM   5147  NH1 ARG B 652      21.475  79.776  11.652  1.00 63.33           N  
ANISOU 5147  NH1 ARG B 652    10445   7850   5765    702   -956    976       N  
ATOM   5148  NH2 ARG B 652      23.620  80.558  11.574  1.00 62.41           N  
ANISOU 5148  NH2 ARG B 652    10315   7685   5712    815  -1345    842       N  
ATOM   5149  N   PRO B 653      19.557  83.402   6.897  1.00 56.50           N  
ANISOU 5149  N   PRO B 653     8565   7347   5553    613   -657    674       N  
ATOM   5150  CA  PRO B 653      18.406  82.820   6.205  1.00 57.69           C  
ANISOU 5150  CA  PRO B 653     8567   7552   5799    518   -510    745       C  
ATOM   5151  C   PRO B 653      17.373  82.268   7.175  1.00 60.73           C  
ANISOU 5151  C   PRO B 653     9052   7964   6057    483   -338    866       C  
ATOM   5152  O   PRO B 653      17.737  81.673   8.194  1.00 61.76           O  
ANISOU 5152  O   PRO B 653     9389   8027   6049    500   -368    916       O  
ATOM   5153  CB  PRO B 653      19.036  81.699   5.375  1.00 57.37           C  
ANISOU 5153  CB  PRO B 653     8484   7433   5881    455   -633    754       C  
ATOM   5154  CG  PRO B 653      20.404  82.214   5.063  1.00 56.07           C  
ANISOU 5154  CG  PRO B 653     8309   7232   5762    534   -809    658       C  
ATOM   5155  CD  PRO B 653      20.832  82.957   6.306  1.00 56.16           C  
ANISOU 5155  CD  PRO B 653     8487   7235   5616    615   -853    634       C  
ATOM   5156  N   LYS B 654      16.104  82.483   6.861  1.00 61.74           N  
ANISOU 5156  N   LYS B 654     9026   8195   6234    436   -159    923       N  
ATOM   5157  CA  LYS B 654      14.991  82.060   7.699  1.00 67.20           C  
ANISOU 5157  CA  LYS B 654     9758   8944   6828    398     41   1059       C  
ATOM   5158  C   LYS B 654      14.490  80.698   7.195  1.00 68.58           C  
ANISOU 5158  C   LYS B 654     9854   9089   7113    224     46   1172       C  
ATOM   5159  O   LYS B 654      14.328  79.744   7.976  1.00 66.56           O  
ANISOU 5159  O   LYS B 654     9741   8781   6766    163     91   1285       O  
ATOM   5160  CB  LYS B 654      13.860  83.100   7.625  1.00 70.48           C  
ANISOU 5160  CB  LYS B 654    10019   9506   7254    455    237   1073       C  
ATOM   5161  CG  LYS B 654      13.129  83.370   8.935  1.00 74.86           C  
ANISOU 5161  CG  LYS B 654    10704  10125   7613    540    454   1158       C  
ATOM   5162  CD  LYS B 654      11.656  83.707   8.703  1.00 76.65           C  
ANISOU 5162  CD  LYS B 654    10697  10515   7911    532    692   1259       C  
ATOM   5163  CE  LYS B 654      11.029  84.465   9.870  1.00 79.53           C  
ANISOU 5163  CE  LYS B 654    11181  10960   8075    697    926   1299       C  
ATOM   5164  NZ  LYS B 654      11.480  83.999  11.211  1.00 80.74           N  
ANISOU 5164  NZ  LYS B 654    11652  11034   7990    739    949   1336       N  
ATOM   5165  N   VAL B 655      14.241  80.629   5.882  1.00 66.28           N  
ANISOU 5165  N   VAL B 655     9356   8820   7008    141     -6   1144       N  
ATOM   5166  CA  VAL B 655      13.841  79.385   5.217  1.00 68.73           C  
ANISOU 5166  CA  VAL B 655     9607   9074   7432    -34    -46   1227       C  
ATOM   5167  C   VAL B 655      15.101  78.551   4.933  1.00 68.55           C  
ANISOU 5167  C   VAL B 655     9742   8885   7419    -28   -247   1163       C  
ATOM   5168  O   VAL B 655      16.090  79.085   4.418  1.00 67.19           O  
ANISOU 5168  O   VAL B 655     9562   8687   7281     72   -372   1037       O  
ATOM   5169  CB  VAL B 655      13.079  79.659   3.886  1.00 68.87           C  
ANISOU 5169  CB  VAL B 655     9365   9173   7628   -120    -45   1214       C  
ATOM   5170  CG1 VAL B 655      12.485  78.366   3.331  1.00 69.96           C  
ANISOU 5170  CG1 VAL B 655     9466   9248   7864   -327    -86   1316       C  
ATOM   5171  CG2 VAL B 655      11.986  80.709   4.084  1.00 68.44           C  
ANISOU 5171  CG2 VAL B 655     9131   9294   7578    -72    139   1258       C  
ATOM   5172  N   LYS B 656      15.070  77.254   5.261  1.00 69.13           N  
ANISOU 5172  N   LYS B 656     9952   8846   7465   -130   -274   1260       N  
ATOM   5173  CA  LYS B 656      16.224  76.366   5.030  1.00 69.36           C  
ANISOU 5173  CA  LYS B 656    10143   8708   7500   -102   -454   1214       C  
ATOM   5174  C   LYS B 656      15.950  75.328   3.937  1.00 67.66           C  
ANISOU 5174  C   LYS B 656     9901   8394   7412   -244   -529   1233       C  
ATOM   5175  O   LYS B 656      15.162  75.566   3.026  1.00 67.40           O  
ANISOU 5175  O   LYS B 656     9685   8431   7491   -340   -500   1228       O  
ATOM   5176  CB  LYS B 656      16.623  75.632   6.315  1.00 71.17           C  
ANISOU 5176  CB  LYS B 656    10625   8841   7575    -74   -461   1298       C  
ATOM   5177  CG  LYS B 656      16.392  76.376   7.624  1.00 73.55           C  
ANISOU 5177  CG  LYS B 656    11004   9234   7707      7   -336   1338       C  
ATOM   5178  CD  LYS B 656      17.359  77.531   7.827  1.00 72.00           C  
ANISOU 5178  CD  LYS B 656    10822   9076   7457    181   -421   1202       C  
ATOM   5179  CE  LYS B 656      17.214  78.086   9.235  1.00 72.58           C  
ANISOU 5179  CE  LYS B 656    11058   9196   7323    266   -325   1239       C  
ATOM   5180  NZ  LYS B 656      18.228  79.125   9.530  1.00 71.66           N  
ANISOU 5180  NZ  LYS B 656    11001   9083   7140    414   -448   1112       N  
ATOM   5181  N   ASN B 689      36.164  61.361 -25.888  1.00117.24           N  
ANISOU 5181  N   ASN B 689    20999  11740  11805   6087    681   -942       N  
ATOM   5182  CA  ASN B 689      36.592  61.395 -24.493  1.00116.26           C  
ANISOU 5182  CA  ASN B 689    20470  11738  11963   6050    620   -798       C  
ATOM   5183  C   ASN B 689      37.691  62.433 -24.232  1.00116.25           C  
ANISOU 5183  C   ASN B 689    19828  12157  12185   6215    855   -623       C  
ATOM   5184  O   ASN B 689      38.808  62.090 -23.840  1.00116.61           O  
ANISOU 5184  O   ASN B 689    19705  12271  12330   6573   1008   -524       O  
ATOM   5185  CB  ASN B 689      37.054  60.005 -24.060  1.00118.15           C  
ANISOU 5185  CB  ASN B 689    21072  11670  12147   6353    594   -823       C  
ATOM   5186  CG  ASN B 689      38.210  59.489 -24.890  1.00121.78           C  
ANISOU 5186  CG  ASN B 689    21717  12095  12458   6932    903   -839       C  
ATOM   5187  OD1 ASN B 689      38.751  58.425 -24.610  1.00125.67           O  
ANISOU 5187  OD1 ASN B 689    22475  12365  12908   7256    928   -848       O  
ATOM   5188  ND2 ASN B 689      38.599  60.240 -25.915  1.00122.46           N  
ANISOU 5188  ND2 ASN B 689    21669  12400  12459   7079   1150   -836       N  
ATOM   5189  N   MET B 690      37.366  63.706 -24.439  1.00116.26           N  
ANISOU 5189  N   MET B 690    19467  12434  12271   5945    872   -576       N  
ATOM   5190  CA  MET B 690      38.308  64.795 -24.144  1.00117.06           C  
ANISOU 5190  CA  MET B 690    18946  12929  12601   6021   1055   -402       C  
ATOM   5191  C   MET B 690      38.178  65.194 -22.671  1.00112.94           C  
ANISOU 5191  C   MET B 690    18026  12531  12356   5743    855   -292       C  
ATOM   5192  O   MET B 690      38.347  66.362 -22.310  1.00110.20           O  
ANISOU 5192  O   MET B 690    17192  12480  12197   5564    872   -180       O  
ATOM   5193  CB  MET B 690      38.070  66.020 -25.044  1.00118.05           C  
ANISOU 5193  CB  MET B 690    18880  13285  12689   5867   1169   -394       C  
ATOM   5194  CG  MET B 690      37.545  65.728 -26.443  1.00120.96           C  
ANISOU 5194  CG  MET B 690    19747  13472  12738   5934   1232   -548       C  
ATOM   5195  SD  MET B 690      35.745  65.589 -26.453  1.00121.06           S  
ANISOU 5195  SD  MET B 690    20126  13235  12633   5427    859   -705       S  
ATOM   5196  CE  MET B 690      35.416  65.506 -28.211  1.00122.92           C  
ANISOU 5196  CE  MET B 690    20854  13342  12505   5553    972   -852       C  
ATOM   5197  N   PHE B 691      37.892  64.207 -21.825  1.00111.89           N  
ANISOU 5197  N   PHE B 691    18126  12154  12231   5714    665   -321       N  
ATOM   5198  CA  PHE B 691      37.671  64.427 -20.411  1.00107.25           C  
ANISOU 5198  CA  PHE B 691    17256  11635  11859   5455    461   -230       C  
ATOM   5199  C   PHE B 691      38.880  63.907 -19.651  1.00108.44           C  
ANISOU 5199  C   PHE B 691    17228  11829  12145   5795    530   -109       C  
ATOM   5200  O   PHE B 691      38.749  63.278 -18.600  1.00107.58           O  
ANISOU 5200  O   PHE B 691    17191  11582  12102   5737    352    -81       O  
ATOM   5201  CB  PHE B 691      36.381  63.727 -19.984  1.00105.69           C  
ANISOU 5201  CB  PHE B 691    17446  11138  11571   5137    187   -334       C  
ATOM   5202  CG  PHE B 691      35.168  64.199 -20.744  1.00104.21           C  
ANISOU 5202  CG  PHE B 691    17423  10912  11260   4804     99   -443       C  
ATOM   5203  CD1 PHE B 691      34.484  63.346 -21.600  1.00105.63           C  
ANISOU 5203  CD1 PHE B 691    18151  10783  11200   4800     32   -593       C  
ATOM   5204  CD2 PHE B 691      34.728  65.511 -20.623  1.00101.48           C  
ANISOU 5204  CD2 PHE B 691    16687  10833  11035   4503     73   -392       C  
ATOM   5205  CE1 PHE B 691      33.372  63.789 -22.301  1.00103.78           C  
ANISOU 5205  CE1 PHE B 691    18049  10522  10858   4491    -73   -682       C  
ATOM   5206  CE2 PHE B 691      33.619  65.961 -21.324  1.00100.40           C  
ANISOU 5206  CE2 PHE B 691    16683  10670  10792   4215    -14   -480       C  
ATOM   5207  CZ  PHE B 691      32.940  65.097 -22.166  1.00101.28           C  
ANISOU 5207  CZ  PHE B 691    17319  10489  10673   4206    -92   -622       C  
ATOM   5208  N   ARG B 692      40.062  64.195 -20.198  1.00110.23           N  
ANISOU 5208  N   ARG B 692    17207  12259  12415   6151    793    -25       N  
ATOM   5209  CA  ARG B 692      41.320  63.705 -19.647  1.00112.30           C  
ANISOU 5209  CA  ARG B 692    17273  12587  12807   6533    889    103       C  
ATOM   5210  C   ARG B 692      41.596  64.391 -18.326  1.00107.95           C  
ANISOU 5210  C   ARG B 692    16227  12261  12527   6327    735    254       C  
ATOM   5211  O   ARG B 692      41.549  65.620 -18.236  1.00106.54           O  
ANISOU 5211  O   ARG B 692    15648  12351  12480   6081    736    320       O  
ATOM   5212  CB  ARG B 692      42.486  63.968 -20.603  1.00115.14           C  
ANISOU 5212  CB  ARG B 692    17430  13153  13163   6942   1227    179       C  
ATOM   5213  CG  ARG B 692      42.415  63.187 -21.902  1.00118.62           C  
ANISOU 5213  CG  ARG B 692    18391  13366  13312   7241   1413     37       C  
ATOM   5214  CD  ARG B 692      43.796  62.995 -22.512  1.00122.24           C  
ANISOU 5214  CD  ARG B 692    18691  13973  13779   7781   1754    140       C  
ATOM   5215  NE  ARG B 692      43.837  61.869 -23.443  1.00125.78           N  
ANISOU 5215  NE  ARG B 692    19730  14121  13939   8158   1900      1       N  
ATOM   5216  CZ  ARG B 692      43.828  60.583 -23.090  1.00127.99           C  
ANISOU 5216  CZ  ARG B 692    20433  14072  14125   8372   1804    -68       C  
ATOM   5217  NH1 ARG B 692      43.769  60.224 -21.809  1.00126.82           N  
ANISOU 5217  NH1 ARG B 692    20183  13856  14146   8245   1560     -6       N  
ATOM   5218  NH2 ARG B 692      43.873  59.642 -24.028  1.00131.39           N  
ANISOU 5218  NH2 ARG B 692    21423  14224  14274   8719   1948   -203       N  
ATOM   5219  N   ASN B 693      41.876  63.585 -17.310  1.00106.72           N  
ANISOU 5219  N   ASN B 693    16131  11977  12440   6431    595    305       N  
ATOM   5220  CA  ASN B 693      42.118  64.082 -15.963  1.00104.48           C  
ANISOU 5220  CA  ASN B 693    15452  11862  12382   6250    415    439       C  
ATOM   5221  C   ASN B 693      41.013  65.033 -15.505  1.00 98.19           C  
ANISOU 5221  C   ASN B 693    14546  11137  11623   5731    234    403       C  
ATOM   5222  O   ASN B 693      41.288  66.088 -14.935  1.00 96.74           O  
ANISOU 5222  O   ASN B 693    13917  11219  11619   5557    187    508       O  
ATOM   5223  CB  ASN B 693      43.492  64.758 -15.870  1.00105.76           C  
ANISOU 5223  CB  ASN B 693    15058  12366  12759   6484    565    622       C  
ATOM   5224  CG  ASN B 693      44.577  63.977 -16.588  1.00108.71           C  
ANISOU 5224  CG  ASN B 693    15496  12718  13088   7024    815    663       C  
ATOM   5225  OD1 ASN B 693      45.445  64.559 -17.236  1.00108.51           O  
ANISOU 5225  OD1 ASN B 693    15132  12949  13145   7224   1048    761       O  
ATOM   5226  ND2 ASN B 693      44.523  62.657 -16.491  1.00111.64           N  
ANISOU 5226  ND2 ASN B 693    16313  12778  13327   7268    777    595       N  
ATOM   5227  N   PHE B 694      39.765  64.661 -15.786  1.00 95.04           N  
ANISOU 5227  N   PHE B 694    14560  10497  11052   5491    131    256       N  
ATOM   5228  CA  PHE B 694      38.623  65.322 -15.178  1.00 90.75           C  
ANISOU 5228  CA  PHE B 694    13964   9976  10539   5022    -62    227       C  
ATOM   5229  C   PHE B 694      38.614  64.955 -13.703  1.00 89.41           C  
ANISOU 5229  C   PHE B 694    13750   9751  10470   4928   -267    307       C  
ATOM   5230  O   PHE B 694      38.510  65.828 -12.853  1.00 85.36           O  
ANISOU 5230  O   PHE B 694    12916   9424  10091   4690   -371    381       O  
ATOM   5231  CB  PHE B 694      37.303  64.902 -15.831  1.00 89.91           C  
ANISOU 5231  CB  PHE B 694    14304   9621  10235   4800   -132     69       C  
ATOM   5232  CG  PHE B 694      36.083  65.434 -15.123  1.00 86.14           C  
ANISOU 5232  CG  PHE B 694    13782   9152   9793   4340   -330     54       C  
ATOM   5233  CD1 PHE B 694      35.699  66.757 -15.273  1.00 84.37           C  
ANISOU 5233  CD1 PHE B 694    13243   9168   9643   4089   -316     67       C  
ATOM   5234  CD2 PHE B 694      35.329  64.615 -14.297  1.00 86.53           C  
ANISOU 5234  CD2 PHE B 694    14104   8969   9803   4169   -521     37       C  
ATOM   5235  CE1 PHE B 694      34.577  67.253 -14.621  1.00 81.76           C  
ANISOU 5235  CE1 PHE B 694    12869   8851   9343   3698   -479     58       C  
ATOM   5236  CE2 PHE B 694      34.211  65.100 -13.641  1.00 83.29           C  
ANISOU 5236  CE2 PHE B 694    13635   8582   9426   3764   -675     38       C  
ATOM   5237  CZ  PHE B 694      33.833  66.421 -13.802  1.00 81.74           C  
ANISOU 5237  CZ  PHE B 694    13120   8633   9302   3540   -650     46       C  
HETATM 5238  N   SEP B 695      38.758  63.664 -13.409  1.00 91.00           N  
ANISOU 5238  N   SEP B 695    14293   9689  10594   5129   -321    294       N  
HETATM 5239  CA  SEP B 695      38.737  63.179 -12.028  1.00 90.49           C  
ANISOU 5239  CA  SEP B 695    14250   9536  10595   5060   -517    373       C  
HETATM 5240  CB  SEP B 695      38.979  61.681 -11.968  1.00 94.21           C  
ANISOU 5240  CB  SEP B 695    15150   9686  10958   5344   -541    352       C  
HETATM 5241  OG  SEP B 695      37.745  61.010 -12.189  1.00 94.68           O  
ANISOU 5241  OG  SEP B 695    15676   9444  10852   5109   -644    231       O  
HETATM 5242  C   SEP B 695      39.762  63.859 -11.160  1.00 90.04           C  
ANISOU 5242  C   SEP B 695    13711   9757  10741   5145   -541    530       C  
HETATM 5243  O   SEP B 695      40.853  64.216 -11.614  1.00 89.78           O  
ANISOU 5243  O   SEP B 695    13383   9924  10804   5417   -387    602       O  
HETATM 5244  P   SEP B 695      37.776  59.554 -12.871  1.00 98.84           P  
ANISOU 5244  P   SEP B 695    16771   9590  11193   5389   -610    135       P  
HETATM 5245  O1P SEP B 695      38.269  59.893 -14.255  1.00101.22           O  
ANISOU 5245  O1P SEP B 695    17035   9995  11429   5633   -377     65       O  
HETATM 5246  O2P SEP B 695      38.759  58.795 -12.024  1.00100.15           O  
ANISOU 5246  O2P SEP B 695    16935   9689  11428   5714   -643    249       O  
HETATM 5247  O3P SEP B 695      36.347  59.059 -12.812  1.00 98.28           O  
ANISOU 5247  O3P SEP B 695    17102   9243  10996   5010   -784     42       O  
ATOM   5248  N   PHE B 696      39.403  64.035  -9.893  1.00 88.74           N  
ANISOU 5248  N   PHE B 696    13471   9606  10639   4905   -740    591       N  
ATOM   5249  CA  PHE B 696      40.207  64.792  -8.944  1.00 88.74           C  
ANISOU 5249  CA  PHE B 696    13034   9862  10820   4903   -820    732       C  
ATOM   5250  C   PHE B 696      39.636  64.591  -7.536  1.00 89.08           C  
ANISOU 5250  C   PHE B 696    13180   9811  10854   4668  -1050    773       C  
ATOM   5251  O   PHE B 696      38.461  64.241  -7.389  1.00 86.36           O  
ANISOU 5251  O   PHE B 696    13147   9275  10388   4418  -1121    694       O  
ATOM   5252  CB  PHE B 696      40.198  66.275  -9.335  1.00 86.68           C  
ANISOU 5252  CB  PHE B 696    12381   9894  10656   4704   -749    738       C  
ATOM   5253  CG  PHE B 696      40.866  67.169  -8.338  1.00 86.61           C  
ANISOU 5253  CG  PHE B 696    11951  10132  10824   4624   -867    870       C  
ATOM   5254  CD1 PHE B 696      40.137  67.727  -7.298  1.00 84.85           C  
ANISOU 5254  CD1 PHE B 696    11703   9930  10605   4286  -1049    873       C  
ATOM   5255  CD2 PHE B 696      42.228  67.434  -8.422  1.00 89.37           C  
ANISOU 5255  CD2 PHE B 696    11935  10689  11332   4888   -803    996       C  
ATOM   5256  CE1 PHE B 696      40.747  68.547  -6.365  1.00 85.16           C  
ANISOU 5256  CE1 PHE B 696    11398  10173  10785   4208  -1179    983       C  
ATOM   5257  CE2 PHE B 696      42.848  68.253  -7.491  1.00 89.19           C  
ANISOU 5257  CE2 PHE B 696    11532  10880  11473   4791   -947   1120       C  
ATOM   5258  CZ  PHE B 696      42.107  68.809  -6.461  1.00 87.33           C  
ANISOU 5258  CZ  PHE B 696    11315  10643  11221   4449  -1144   1106       C  
ATOM   5259  N   MET B 697      40.465  64.800  -6.510  1.00 91.17           N  
ANISOU 5259  N   MET B 697    13185  10211  11243   4746  -1170    906       N  
ATOM   5260  CA  MET B 697      40.004  64.759  -5.122  1.00 93.26           C  
ANISOU 5260  CA  MET B 697    13520  10422  11491   4526  -1384    957       C  
ATOM   5261  C   MET B 697      40.785  65.699  -4.204  1.00 97.01           C  
ANISOU 5261  C   MET B 697    13580  11159  12118   4486  -1509   1080       C  
ATOM   5262  O   MET B 697      42.003  65.815  -4.327  1.00 98.00           O  
ANISOU 5262  O   MET B 697    13416  11440  12377   4749  -1482   1176       O  
ATOM   5263  CB  MET B 697      40.117  63.339  -4.587  1.00 95.83           C  
ANISOU 5263  CB  MET B 697    14205  10471  11732   4722  -1471    992       C  
ATOM   5264  CG  MET B 697      39.308  63.106  -3.323  1.00 95.84           C  
ANISOU 5264  CG  MET B 697    14410  10347  11656   4457  -1660   1021       C  
ATOM   5265  SD  MET B 697      39.027  61.359  -2.983  1.00 99.54           S  
ANISOU 5265  SD  MET B 697    15425  10414  11980   4604  -1732   1029       S  
ATOM   5266  CE  MET B 697      38.349  60.822  -4.554  1.00 99.92           C  
ANISOU 5266  CE  MET B 697    15786  10261  11918   4625  -1551    866       C  
ATOM   5267  N   ASN B 698      40.078  66.356  -3.282  1.00100.43           N  
ANISOU 5267  N   ASN B 698    13993  11638  12528   4160  -1647   1080       N  
ATOM   5268  CA  ASN B 698      40.716  67.171  -2.243  1.00106.48           C  
ANISOU 5268  CA  ASN B 698    14448  12604  13403   4092  -1812   1188       C  
ATOM   5269  C   ASN B 698      41.039  66.332  -1.014  1.00112.69           C  
ANISOU 5269  C   ASN B 698    15399  13267  14151   4196  -2005   1285       C  
ATOM   5270  O   ASN B 698      40.350  65.346  -0.742  1.00115.62           O  
ANISOU 5270  O   ASN B 698    16156  13390  14384   4179  -2027   1255       O  
ATOM   5271  CB  ASN B 698      39.826  68.349  -1.851  1.00106.94           C  
ANISOU 5271  CB  ASN B 698    14426  12769  13436   3714  -1860   1136       C  
ATOM   5272  CG  ASN B 698      40.095  69.578  -2.693  1.00109.04           C  
ANISOU 5272  CG  ASN B 698    14348  13264  13817   3644  -1749   1113       C  
ATOM   5273  OD1 ASN B 698      41.231  70.042  -2.771  1.00116.87           O  
ANISOU 5273  OD1 ASN B 698    15005  14440  14959   3784  -1766   1203       O  
ATOM   5274  ND2 ASN B 698      39.058  70.111  -3.326  1.00108.07           N  
ANISOU 5274  ND2 ASN B 698    14299  13134  13629   3422  -1641   1003       N  
ATOM   5275  N   PRO B 699      42.082  66.725  -0.255  1.00117.53           N  
ANISOU 5275  N   PRO B 699    15725  14047  14884   4291  -2161   1410       N  
ATOM   5276  CA  PRO B 699      42.534  65.908   0.891  1.00120.11           C  
ANISOU 5276  CA  PRO B 699    16193  14265  15178   4431  -2361   1518       C  
ATOM   5277  C   PRO B 699      41.408  65.593   1.895  1.00117.59           C  
ANISOU 5277  C   PRO B 699    16241  13762  14675   4179  -2472   1489       C  
ATOM   5278  O   PRO B 699      41.440  64.548   2.560  1.00117.73           O  
ANISOU 5278  O   PRO B 699    16537  13587  14606   4300  -2571   1548       O  
ATOM   5279  CB  PRO B 699      43.648  66.758   1.529  1.00121.56           C  
ANISOU 5279  CB  PRO B 699    15959  14704  15522   4462  -2535   1644       C  
ATOM   5280  CG  PRO B 699      43.477  68.137   0.973  1.00120.08           C  
ANISOU 5280  CG  PRO B 699    15476  14729  15419   4232  -2453   1586       C  
ATOM   5281  CD  PRO B 699      42.836  67.989  -0.373  1.00118.02           C  
ANISOU 5281  CD  PRO B 699    15326  14399  15115   4238  -2184   1463       C  
ATOM   5282  N   GLY B 700      40.433  66.499   1.988  1.00111.62           N  
ANISOU 5282  N   GLY B 700    15481  13067  13861   3843  -2444   1408       N  
ATOM   5283  CA  GLY B 700      39.199  66.269   2.733  1.00108.63           C  
ANISOU 5283  CA  GLY B 700    15433  12532  13309   3587  -2482   1373       C  
ATOM   5284  C   GLY B 700      38.012  66.228   1.792  1.00104.71           C  
ANISOU 5284  C   GLY B 700    15096  11941  12744   3413  -2291   1247       C  
ATOM   5285  O   GLY B 700      37.934  65.369   0.911  1.00103.11           O  
ANISOU 5285  O   GLY B 700    15064  11587  12527   3554  -2177   1202       O  
TER    5286      GLY B 700                                                      
HETATM 5287  C5  5VS A1001      27.571  75.942  26.111  1.00 37.49           C  
ANISOU 5287  C5  5VS A1001     5214   4183   4845     85   -394    292       C  
HETATM 5288  C7  5VS A1001      26.778  76.172  27.355  1.00 37.41           C  
ANISOU 5288  C7  5VS A1001     5091   4195   4925     96   -347    284       C  
HETATM 5289  C8  5VS A1001      25.871  75.211  27.838  1.00 36.96           C  
ANISOU 5289  C8  5VS A1001     4957   4182   4902     33   -361    268       C  
HETATM 5290  C10 5VS A1001      25.279  76.679  29.648  1.00 35.76           C  
ANISOU 5290  C10 5VS A1001     4679   4037   4872    114   -229    259       C  
HETATM 5291  C15 5VS A1001      26.753  80.615  27.986  1.00 40.72           C  
ANISOU 5291  C15 5VS A1001     5469   4502   5501    354   -230    347       C  
HETATM 5292  C17 5VS A1001      25.635  82.546  28.884  1.00 39.00           C  
ANISOU 5292  C17 5VS A1001     5140   4230   5445    495   -154    353       C  
HETATM 5293  C20 5VS A1001      25.703  80.385  27.135  1.00 40.80           C  
ANISOU 5293  C20 5VS A1001     5411   4558   5531    367   -332    388       C  
HETATM 5294  C22 5VS A1001      24.077  78.213  31.223  1.00 35.81           C  
ANISOU 5294  C22 5VS A1001     4523   4059   5021    207   -100    239       C  
HETATM 5295  C24 5VS A1001      23.498  80.535  31.335  1.00 40.66           C  
ANISOU 5295  C24 5VS A1001     5071   4615   5760    382    -43    252       C  
HETATM 5296  C1  5VS A1001      30.124  77.407  27.308  1.00 40.75           C  
ANISOU 5296  C1  5VS A1001     5739   4499   5244    150   -211    272       C  
HETATM 5297  C2  5VS A1001      28.913  77.924  26.581  1.00 43.63           C  
ANISOU 5297  C2  5VS A1001     6051   4887   5638    184   -286    310       C  
HETATM 5298  C3  5VS A1001      29.340  79.122  25.680  1.00 47.56           C  
ANISOU 5298  C3  5VS A1001     6612   5347   6111    237   -300    355       C  
HETATM 5299  N4  5VS A1001      28.536  76.790  25.760  1.00 36.99           N  
ANISOU 5299  N4  5VS A1001     5226   4079   4749    130   -362    306       N  
HETATM 5300  O6  5VS A1001      27.365  75.035  25.341  1.00 39.64           O  
ANISOU 5300  O6  5VS A1001     5519   4473   5069     31   -458    283       O  
HETATM 5301  C9  5VS A1001      25.129  75.471  28.966  1.00 35.03           C  
ANISOU 5301  C9  5VS A1001     4608   3966   4735     40   -302    259       C  
HETATM 5302  C11 5VS A1001      26.202  77.628  29.186  1.00 36.93           C  
ANISOU 5302  C11 5VS A1001     4911   4131   4989    174   -221    272       C  
HETATM 5303  C12 5VS A1001      26.946  77.400  28.042  1.00 38.20           C  
ANISOU 5303  C12 5VS A1001     5169   4270   5074    164   -279    289       C  
HETATM 5304  N13 5VS A1001      27.852  78.346  27.525  1.00 43.00           N  
ANISOU 5304  N13 5VS A1001     5859   4828   5650    212   -265    308       N  
HETATM 5305  C14 5VS A1001      27.970  79.726  28.014  1.00 44.62           C  
ANISOU 5305  C14 5VS A1001     6057   4990   5905    281   -207    316       C  
HETATM 5306  C16 5VS A1001      26.732  81.693  28.870  1.00 39.77           C  
ANISOU 5306  C16 5VS A1001     5330   4336   5446    410   -146    329       C  
HETATM 5307  C18 5VS A1001      24.582  82.316  28.017  1.00 40.32           C  
ANISOU 5307  C18 5VS A1001     5226   4449   5645    521   -259    405       C  
HETATM 5308  C19 5VS A1001      24.602  81.236  27.145  1.00 40.42           C  
ANISOU 5308  C19 5VS A1001     5259   4515   5581    450   -354    422       C  
HETATM 5309  N21 5VS A1001      24.565  76.952  30.825  1.00 37.03           N  
ANISOU 5309  N21 5VS A1001     4744   4223   5101    122   -151    239       N  
HETATM 5310  C23 5VS A1001      24.098  79.466  30.651  1.00 36.50           C  
ANISOU 5310  C23 5VS A1001     4618   4105   5144    304   -118    266       C  
HETATM 5311  C25 5VS A1001      22.899  80.308  32.577  1.00 40.83           C  
ANISOU 5311  C25 5VS A1001     5013   4674   5824    357     54    205       C  
HETATM 5312  N26 5VS A1001      22.894  79.079  33.111  1.00 39.02           N  
ANISOU 5312  N26 5VS A1001     4780   4495   5549    253     68    185       N  
HETATM 5313  C27 5VS A1001      23.455  78.040  32.479  1.00 38.15           C  
ANISOU 5313  C27 5VS A1001     4741   4391   5363    181     -8    204       C  
HETATM 5314  N28 5VS A1001      23.571  76.681  32.803  1.00 35.62           N  
ANISOU 5314  N28 5VS A1001     4443   4099   4991     75    -14    194       N  
HETATM 5315  C30 5VS A1001      24.240  76.059  31.805  1.00 35.94           C  
ANISOU 5315  C30 5VS A1001     4571   4117   4967     47   -100    213       C  
HETATM 5316  O31 5VS A1001      24.501  74.868  31.794  1.00 35.73           O  
ANISOU 5316  O31 5VS A1001     4590   4092   4893    -33   -122    209       O  
HETATM 5317  C5  5VS B1001      25.504  75.822 -10.887  1.00 50.01           C  
ANISOU 5317  C5  5VS B1001     7438   5847   5715   1073  -1036    149       C  
HETATM 5318  C7  5VS B1001      25.581  75.351  -9.475  1.00 49.82           C  
ANISOU 5318  C7  5VS B1001     7447   5779   5703   1049  -1089    209       C  
HETATM 5319  C8  5VS B1001      26.653  74.572  -9.022  1.00 50.84           C  
ANISOU 5319  C8  5VS B1001     7657   5829   5831   1225  -1104    234       C  
HETATM 5320  C10 5VS B1001      25.650  74.498  -6.810  1.00 48.94           C  
ANISOU 5320  C10 5VS B1001     7436   5581   5576   1000  -1189    334       C  
HETATM 5321  C15 5VS B1001      21.535  75.958  -7.685  1.00 49.09           C  
ANISOU 5321  C15 5VS B1001     7268   5776   5606    404  -1140    333       C  
HETATM 5322  C17 5VS B1001      19.894  75.141  -6.140  1.00 51.94           C  
ANISOU 5322  C17 5VS B1001     7711   6083   5939    135  -1149    470       C  
HETATM 5323  C20 5VS B1001      21.376  74.806  -8.446  1.00 50.00           C  
ANISOU 5323  C20 5VS B1001     7585   5729   5684    379  -1195    307       C  
HETATM 5324  C22 5VS B1001      24.524  73.768  -4.698  1.00 49.63           C  
ANISOU 5324  C22 5VS B1001     7685   5579   5591    790  -1250    454       C  
HETATM 5325  C24 5VS B1001      22.285  73.373  -3.953  1.00 50.24           C  
ANISOU 5325  C24 5VS B1001     7849   5619   5618    436  -1228    544       C  
HETATM 5326  C1  5VS B1001      24.490  78.689  -9.814  1.00 46.05           C  
ANISOU 5326  C1  5VS B1001     6483   5683   5330    834  -1008    203       C  
HETATM 5327  C2  5VS B1001      23.740  77.416 -10.231  1.00 47.93           C  
ANISOU 5327  C2  5VS B1001     6937   5769   5504    765  -1050    185       C  
HETATM 5328  C3  5VS B1001      22.469  77.922 -10.946  1.00 47.21           C  
ANISOU 5328  C3  5VS B1001     6802   5727   5407    607  -1058    168       C  
HETATM 5329  N4  5VS B1001      24.605  76.760 -11.208  1.00 47.57           N  
ANISOU 5329  N4  5VS B1001     7011   5641   5423    927  -1029    140       N  
HETATM 5330  O6  5VS B1001      26.206  75.361 -11.763  1.00 52.95           O  
ANISOU 5330  O6  5VS B1001     7903   6162   6053   1231   -996    112       O  
HETATM 5331  C9  5VS B1001      26.687  74.162  -7.696  1.00 51.75           C  
ANISOU 5331  C9  5VS B1001     7817   5900   5942   1198  -1164    296       C  
HETATM 5332  C11 5VS B1001      24.584  75.287  -7.274  1.00 49.32           C  
ANISOU 5332  C11 5VS B1001     7386   5717   5634    837  -1156    311       C  
HETATM 5333  C12 5VS B1001      24.523  75.723  -8.600  1.00 49.09           C  
ANISOU 5333  C12 5VS B1001     7303   5731   5617    856  -1117    249       C  
HETATM 5334  N13 5VS B1001      23.451  76.513  -9.091  1.00 48.64           N  
ANISOU 5334  N13 5VS B1001     7146   5761   5571    705  -1099    234       N  
HETATM 5335  C14 5VS B1001      22.517  77.037  -8.078  1.00 47.09           C  
ANISOU 5335  C14 5VS B1001     6859   5641   5390    554  -1097    288       C  
HETATM 5336  C16 5VS B1001      20.790  76.126  -6.528  1.00 50.38           C  
ANISOU 5336  C16 5VS B1001     7386   5986   5766    288  -1120    406       C  
HETATM 5337  C18 5VS B1001      19.725  73.998  -6.907  1.00 53.00           C  
ANISOU 5337  C18 5VS B1001     8033   6051   6053     84  -1220    452       C  
HETATM 5338  C19 5VS B1001      20.469  73.825  -8.072  1.00 52.45           C  
ANISOU 5338  C19 5VS B1001     8040   5919   5970    213  -1248    361       C  
HETATM 5339  N21 5VS B1001      25.658  74.087  -5.460  1.00 49.43           N  
ANISOU 5339  N21 5VS B1001     7569   5599   5611    975  -1238    403       N  
HETATM 5340  C23 5VS B1001      23.161  73.721  -4.973  1.00 49.19           C  
ANISOU 5340  C23 5VS B1001     7649   5516   5524    587  -1229    461       C  
HETATM 5341  C25 5VS B1001      22.790  73.084  -2.689  1.00 50.57           C  
ANISOU 5341  C25 5VS B1001     7969   5631   5614    497  -1251    607       C  
HETATM 5342  N26 5VS B1001      24.092  73.122  -2.452  1.00 50.00           N  
ANISOU 5342  N26 5VS B1001     7892   5558   5547    691  -1294    591       N  
HETATM 5343  C27 5VS B1001      24.960  73.455  -3.401  1.00 50.43           C  
ANISOU 5343  C27 5VS B1001     7851   5650   5657    835  -1294    521       C  
HETATM 5344  N28 5VS B1001      26.341  73.571  -3.414  1.00 50.25           N  
ANISOU 5344  N28 5VS B1001     7766   5654   5671   1040  -1327    510       N  
HETATM 5345  C30 5VS B1001      26.730  73.952  -4.638  1.00 49.45           C  
ANISOU 5345  C30 5VS B1001     7561   5603   5623   1119  -1283    444       C  
HETATM 5346  O31 5VS B1001      27.891  74.142  -4.938  1.00 49.36           O  
ANISOU 5346  O31 5VS B1001     7452   5638   5661   1295  -1284    436       O  
HETATM 5347  O   HOH A1101      54.916  85.508  20.814  1.00 50.22           O  
HETATM 5348  O   HOH A1102      46.014  85.988  21.150  1.00 36.48           O  
HETATM 5349  O   HOH A1103      51.045  84.567   7.705  1.00 42.17           O  
HETATM 5350  O   HOH A1104      57.340  85.951  17.723  1.00 47.28           O  
HETATM 5351  O   HOH A1105      27.722  86.049  31.177  1.00 45.98           O  
HETATM 5352  O   HOH A1106      28.578  58.107  20.390  1.00 55.13           O  
HETATM 5353  O   HOH A1107      55.105  87.430  16.168  1.00 43.98           O  
HETATM 5354  O   HOH A1108      20.505  57.838  28.203  1.00 59.07           O  
HETATM 5355  O   HOH A1109      28.002  70.502  28.407  1.00 39.59           O  
HETATM 5356  O   HOH A1110      34.298  65.415  21.647  1.00 39.26           O  
HETATM 5357  O   HOH A1111      19.638  77.158  12.377  1.00 44.08           O  
HETATM 5358  O   HOH A1112      43.813  52.476  28.971  1.00 40.04           O  
HETATM 5359  O   HOH A1113      12.274  62.380  26.988  1.00 60.56           O  
HETATM 5360  O   HOH A1114      38.945  89.886  45.639  1.00 59.55           O  
HETATM 5361  O   HOH A1115      26.886  77.961  45.569  1.00 45.32           O  
HETATM 5362  O   HOH A1116      28.677  70.635  22.580  1.00 50.13           O  
HETATM 5363  O   HOH A1117      38.555  83.396  25.815  1.00 52.85           O  
HETATM 5364  O   HOH A1118      41.440  84.351  24.491  1.00 38.70           O  
HETATM 5365  O   HOH A1119      50.461  91.995  23.656  1.00 50.80           O  
HETATM 5366  O   HOH A1120      17.205  56.743  21.487  1.00 58.97           O  
HETATM 5367  O   HOH A1121      45.101  65.748  36.227  1.00 35.67           O  
HETATM 5368  O   HOH A1122      57.009  80.873  31.075  1.00 42.46           O  
HETATM 5369  O   HOH A1123      14.497  62.538  28.685  1.00 48.83           O  
HETATM 5370  O   HOH A1124      43.427  90.231  45.906  1.00 47.08           O  
HETATM 5371  O   HOH A1125      33.105  84.779  42.234  1.00 33.59           O  
HETATM 5372  O   HOH A1126      51.734  64.803  23.614  1.00 39.45           O  
HETATM 5373  O   HOH A1127      17.959  75.442  37.662  1.00 38.32           O  
HETATM 5374  O   HOH A1128      46.829  67.313  42.978  1.00 46.82           O  
HETATM 5375  O   HOH A1129      46.144  58.322  31.582  1.00 51.69           O  
HETATM 5376  O   HOH A1130      20.551  73.794   8.065  1.00 50.75           O  
HETATM 5377  O   HOH A1131      21.940  87.284  36.328  1.00 42.13           O  
HETATM 5378  O   HOH A1132      41.594  57.621  37.718  1.00 36.56           O  
HETATM 5379  O   HOH A1133      53.142  87.255  26.420  1.00 36.02           O  
HETATM 5380  O   HOH A1134      42.855  63.638  38.492  1.00 41.84           O  
HETATM 5381  O   HOH A1135      49.297  74.983  48.237  1.00 39.85           O  
HETATM 5382  O   HOH A1136      52.032  50.820  29.565  1.00 50.25           O  
HETATM 5383  O   HOH A1137      23.392  79.465  41.026  1.00 43.19           O  
HETATM 5384  O   HOH A1138      40.880  91.592  29.671  1.00 38.16           O  
HETATM 5385  O   HOH A1139      39.649  93.528  39.232  1.00 42.32           O  
HETATM 5386  O   HOH A1140      45.584  90.747  38.395  1.00 34.11           O  
HETATM 5387  O   HOH A1141      26.549  76.414  13.677  1.00 51.96           O  
HETATM 5388  O   HOH A1142      34.941  81.041  22.236  1.00 56.00           O  
HETATM 5389  O   HOH A1143      25.063  71.854  28.240  1.00 35.29           O  
HETATM 5390  O   HOH A1144      48.172  66.333  18.078  1.00 44.10           O  
HETATM 5391  O   HOH A1145      47.258  67.704  16.186  1.00 41.27           O  
HETATM 5392  O   HOH A1146      21.410  80.462  39.528  1.00 47.24           O  
HETATM 5393  O   HOH A1147      54.766  84.538  16.387  1.00 50.30           O  
HETATM 5394  O   HOH A1148      46.622  80.686  48.812  1.00 45.45           O  
HETATM 5395  O   HOH A1149      49.797  68.105  39.885  1.00 47.68           O  
HETATM 5396  O   HOH A1150      56.521  72.233  35.480  1.00 45.98           O  
HETATM 5397  O   HOH A1151      25.748  75.951  42.827  1.00 47.57           O  
HETATM 5398  O   HOH A1152      27.222  72.501  30.023  1.00 35.07           O  
HETATM 5399  O   HOH A1153      43.829  71.060  51.975  1.00 51.75           O  
HETATM 5400  O   HOH A1154      41.602  81.922  20.364  1.00 44.95           O  
HETATM 5401  O   HOH A1155      31.597  59.546  29.478  1.00 44.42           O  
HETATM 5402  O   HOH A1156      45.626  91.716  42.653  1.00 41.30           O  
HETATM 5403  O   HOH A1157      15.605  83.474  20.202  1.00 57.45           O  
HETATM 5404  O   HOH A1158      42.764  71.767  23.099  1.00 42.94           O  
HETATM 5405  O   HOH A1159      35.513  81.748  53.500  1.00 55.95           O  
HETATM 5406  O   HOH A1160      29.676  76.005  41.804  1.00 43.12           O  
HETATM 5407  O   HOH A1161      38.579  91.366  40.415  1.00 32.95           O  
HETATM 5408  O   HOH A1162      57.116  74.126  20.264  1.00 41.89           O  
HETATM 5409  O   HOH A1163      51.511  63.967  39.427  1.00 59.98           O  
HETATM 5410  O   HOH A1164      50.458  64.476  26.060  1.00 35.59           O  
HETATM 5411  O   HOH A1165      28.068  67.256  42.832  1.00 58.02           O  
HETATM 5412  O   HOH A1166      48.090  78.139  23.813  1.00 28.70           O  
HETATM 5413  O   HOH A1167      30.541  60.469  38.314  1.00 59.35           O  
HETATM 5414  O   HOH A1168      26.308  82.168  35.121  1.00 38.36           O  
HETATM 5415  O   HOH A1169      10.793  68.569  15.795  1.00 57.65           O  
HETATM 5416  O   HOH A1170      36.113  57.866  30.401  1.00 44.27           O  
HETATM 5417  O   HOH A1171      46.724  66.765  38.293  1.00 41.20           O  
HETATM 5418  O   HOH A1172      46.904  74.302  49.881  1.00 39.53           O  
HETATM 5419  O   HOH A1173      45.171  89.148  24.243  1.00 40.73           O  
HETATM 5420  O   HOH A1174      53.767  86.972  18.668  1.00 48.93           O  
HETATM 5421  O   HOH A1175      59.852  75.822  25.356  1.00 53.20           O  
HETATM 5422  O   HOH A1176      51.080  95.255  32.895  1.00 49.45           O  
HETATM 5423  O   HOH A1177      21.585  74.564  16.297  1.00 50.89           O  
HETATM 5424  O   HOH A1178      58.577  88.366  31.370  1.00 46.03           O  
HETATM 5425  O   HOH A1179      31.211  65.272  16.289  1.00 43.85           O  
HETATM 5426  O   HOH A1180      44.262  83.596  10.544  1.00 50.49           O  
HETATM 5427  O   HOH A1181      42.590  65.995  13.745  1.00 50.28           O  
HETATM 5428  O   HOH A1182      36.940  59.748  40.634  1.00 40.03           O  
HETATM 5429  O   HOH A1183      44.830  56.192  34.727  1.00 43.19           O  
HETATM 5430  O   HOH A1184      10.871  63.497  23.232  1.00 61.57           O  
HETATM 5431  O   HOH A1185      38.989  66.939  42.249  1.00 37.19           O  
HETATM 5432  O   HOH A1186      27.317  86.567  28.742  1.00 55.98           O  
HETATM 5433  O   HOH A1187      47.326  82.774  23.989  1.00 31.51           O  
HETATM 5434  O   HOH A1188      37.514  63.454  19.320  1.00 47.98           O  
HETATM 5435  O   HOH A1189      54.058  86.074  23.387  1.00 44.41           O  
HETATM 5436  O   HOH A1190      11.688  61.629  21.015  1.00 55.58           O  
HETATM 5437  O   HOH A1191      41.559  72.415  27.386  1.00 31.17           O  
HETATM 5438  O   HOH A1192      45.182  72.317  24.527  1.00 38.16           O  
HETATM 5439  O   HOH A1193      59.474  74.476  27.760  1.00 41.53           O  
HETATM 5440  O   HOH A1194      35.530  85.021  43.471  1.00 47.65           O  
HETATM 5441  O   HOH A1195      34.041  91.460  37.411  1.00 34.92           O  
HETATM 5442  O   HOH A1196      34.403  76.858  48.283  1.00 44.52           O  
HETATM 5443  O   HOH A1197      34.710  69.869  26.225  1.00 34.75           O  
HETATM 5444  O   HOH A1198      40.166  76.002  24.560  1.00 50.81           O  
HETATM 5445  O   HOH A1199      39.381  55.192  30.536  1.00 42.97           O  
HETATM 5446  O   HOH A1200      54.823  69.709  43.026  1.00 56.60           O  
HETATM 5447  O   HOH A1201      49.803  89.917  41.189  1.00 39.56           O  
HETATM 5448  O   HOH A1202      26.531  72.760  21.693  1.00 54.81           O  
HETATM 5449  O   HOH A1203      51.966  75.335  14.070  1.00 50.21           O  
HETATM 5450  O   HOH A1204       8.137  79.561  25.198  1.00 60.90           O  
HETATM 5451  O   HOH A1205      46.435  87.186  18.718  1.00 45.09           O  
HETATM 5452  O   HOH A1206      14.441  77.868  40.055  1.00 51.39           O  
HETATM 5453  O   HOH A1207      38.186  72.488  17.731  1.00 44.24           O  
HETATM 5454  O   HOH A1208      47.146  81.849   9.188  1.00 47.35           O  
HETATM 5455  O   HOH A1209      30.342  63.237  14.444  1.00 51.52           O  
HETATM 5456  O   HOH A1210      37.875  67.087  54.894  1.00 63.95           O  
HETATM 5457  O   HOH A1211      44.033  68.148  48.751  1.00 46.41           O  
HETATM 5458  O   HOH A1212      42.167  74.759  23.361  1.00 46.29           O  
HETATM 5459  O   HOH A1213      36.710  90.657  43.956  1.00 51.75           O  
HETATM 5460  O   HOH A1214      42.142  61.266  31.788  1.00 51.20           O  
HETATM 5461  O   HOH A1215      25.494  57.314  24.276  1.00 56.26           O  
HETATM 5462  O   HOH A1216      26.577  84.950  18.104  1.00 70.31           O  
HETATM 5463  O   HOH A1217      26.842  70.512  20.327  1.00 59.81           O  
HETATM 5464  O   HOH A1218      54.670  91.630  43.415  1.00 61.46           O  
HETATM 5465  O   HOH A1219      32.447  90.587  48.500  1.00 48.84           O  
HETATM 5466  O   HOH A1220      32.588  93.680  37.988  1.00 41.47           O  
HETATM 5467  O   HOH A1221      47.326  90.217  40.571  1.00 50.32           O  
HETATM 5468  O   HOH A1222      39.550  64.155  41.946  1.00 54.26           O  
HETATM 5469  O   HOH A1223      46.309  69.342  49.950  1.00 61.02           O  
HETATM 5470  O   HOH A1224      34.161  63.444  19.848  1.00 41.22           O  
HETATM 5471  O   HOH A1225      54.271  65.243  23.081  1.00 49.63           O  
HETATM 5472  O   HOH A1226      45.312  93.618  38.893  1.00 56.80           O  
HETATM 5473  O   HOH B1101      17.563  94.927 -17.810  1.00 39.98           O  
HETATM 5474  O   HOH B1102      21.912 106.653 -23.757  1.00 48.48           O  
HETATM 5475  O   HOH B1103      17.100  80.901   2.429  1.00 59.66           O  
HETATM 5476  O   HOH B1104      13.875  97.037 -28.481  1.00 42.47           O  
HETATM 5477  O   HOH B1105      17.743  93.993   3.515  1.00 57.31           O  
HETATM 5478  O   HOH B1106      23.300  87.263   4.733  1.00 44.69           O  
HETATM 5479  O   HOH B1107      31.511  75.595 -10.483  1.00 59.00           O  
HETATM 5480  O   HOH B1108      20.182  88.422 -12.470  1.00 48.61           O  
HETATM 5481  O   HOH B1109      37.598  99.018   5.103  1.00 56.66           O  
HETATM 5482  O   HOH B1110      30.920  88.578 -19.190  1.00 60.09           O  
HETATM 5483  O   HOH B1111      28.092 100.812   3.678  1.00 61.37           O  
HETATM 5484  O   HOH B1112      19.507  90.906 -13.801  1.00 49.80           O  
HETATM 5485  O   HOH B1113      32.624 105.869 -19.085  1.00 53.94           O  
HETATM 5486  O   HOH B1114      36.994 101.342   3.006  1.00 53.70           O  
HETATM 5487  O   HOH B1115      20.246  89.469 -18.254  1.00 42.54           O  
HETATM 5488  O   HOH B1116      19.516 103.387 -15.112  1.00 37.44           O  
HETATM 5489  O   HOH B1117      15.609  95.960 -32.089  1.00 45.76           O  
HETATM 5490  O   HOH B1118      27.886  88.897 -17.997  1.00 48.32           O  
HETATM 5491  O   HOH B1119      31.785 100.167   5.563  1.00 51.94           O  
HETATM 5492  O   HOH B1120      21.128 109.576 -11.900  1.00 51.89           O  
HETATM 5493  O   HOH B1121      25.967  95.381 -18.346  1.00 38.30           O  
HETATM 5494  O   HOH B1122      35.319  90.972 -26.953  1.00 64.09           O  
HETATM 5495  O   HOH B1123      27.561 106.341 -13.646  1.00 48.17           O  
HETATM 5496  O   HOH B1124      32.836  76.272   3.350  1.00 66.81           O  
HETATM 5497  O   HOH B1125      31.141  91.426 -18.411  1.00 47.74           O  
HETATM 5498  O   HOH B1126      30.000  75.818  -8.211  1.00 49.75           O  
HETATM 5499  O   HOH B1127      31.566  88.809 -14.569  1.00 48.44           O  
HETATM 5500  O   HOH B1128      13.438  85.299  -9.311  1.00 73.85           O  
HETATM 5501  O   HOH B1129      32.110  81.190 -14.465  1.00 50.09           O  
HETATM 5502  O   HOH B1130      28.241 110.672  -4.764  1.00 63.63           O  
HETATM 5503  O   HOH B1131      21.663  95.907 -16.625  1.00 35.74           O  
HETATM 5504  O   HOH B1132      17.954  76.329 -16.202  1.00 66.71           O  
HETATM 5505  O   HOH B1133      27.129  87.626 -16.064  1.00 50.80           O  
HETATM 5506  O   HOH B1134      13.428 103.020 -26.546  1.00 40.26           O  
HETATM 5507  O   HOH B1135      17.734  92.002 -30.236  1.00 42.65           O  
HETATM 5508  O   HOH B1136      15.878  94.885 -19.838  1.00 44.44           O  
HETATM 5509  O   HOH B1137      29.849  73.081  -9.154  1.00 57.77           O  
HETATM 5510  O   HOH B1138      29.425 102.513 -28.101  1.00 58.27           O  
CONECT 2532 2538                                                                
CONECT 2538 2532 2539                                                           
CONECT 2539 2538 2540 2542                                                      
CONECT 2540 2539 2541                                                           
CONECT 2541 2540 2544                                                           
CONECT 2542 2539 2543 2548                                                      
CONECT 2543 2542                                                                
CONECT 2544 2541 2545 2546 2547                                                 
CONECT 2545 2544                                                                
CONECT 2546 2544                                                                
CONECT 2547 2544                                                                
CONECT 2548 2542                                                                
CONECT 2691 2700                                                                
CONECT 2700 2691 2701                                                           
CONECT 2701 2700 2702 2704                                                      
CONECT 2702 2701 2703                                                           
CONECT 2703 2702 2706                                                           
CONECT 2704 2701 2705 2710                                                      
CONECT 2705 2704                                                                
CONECT 2706 2703 2707 2708 2709                                                 
CONECT 2707 2706                                                                
CONECT 2708 2706                                                                
CONECT 2709 2706                                                                
CONECT 2710 2704                                                                
CONECT 5229 5238                                                                
CONECT 5238 5229 5239                                                           
CONECT 5239 5238 5240 5242                                                      
CONECT 5240 5239 5241                                                           
CONECT 5241 5240 5244                                                           
CONECT 5242 5239 5243 5248                                                      
CONECT 5243 5242                                                                
CONECT 5244 5241 5245 5246 5247                                                 
CONECT 5245 5244                                                                
CONECT 5246 5244                                                                
CONECT 5247 5244                                                                
CONECT 5248 5242                                                                
CONECT 5287 5288 5299 5300                                                      
CONECT 5288 5287 5289 5303                                                      
CONECT 5289 5288 5301                                                           
CONECT 5290 5301 5302 5309                                                      
CONECT 5291 5293 5305 5306                                                      
CONECT 5292 5306 5307                                                           
CONECT 5293 5291 5308                                                           
CONECT 5294 5309 5310 5313                                                      
CONECT 5295 5310 5311                                                           
CONECT 5296 5297                                                                
CONECT 5297 5296 5298 5299 5304                                                 
CONECT 5298 5297                                                                
CONECT 5299 5287 5297                                                           
CONECT 5300 5287                                                                
CONECT 5301 5289 5290                                                           
CONECT 5302 5290 5303                                                           
CONECT 5303 5288 5302 5304                                                      
CONECT 5304 5297 5303 5305                                                      
CONECT 5305 5291 5304                                                           
CONECT 5306 5291 5292                                                           
CONECT 5307 5292 5308                                                           
CONECT 5308 5293 5307                                                           
CONECT 5309 5290 5294 5315                                                      
CONECT 5310 5294 5295                                                           
CONECT 5311 5295 5312                                                           
CONECT 5312 5311 5313                                                           
CONECT 5313 5294 5312 5314                                                      
CONECT 5314 5313 5315                                                           
CONECT 5315 5309 5314 5316                                                      
CONECT 5316 5315                                                                
CONECT 5317 5318 5329 5330                                                      
CONECT 5318 5317 5319 5333                                                      
CONECT 5319 5318 5331                                                           
CONECT 5320 5331 5332 5339                                                      
CONECT 5321 5323 5335 5336                                                      
CONECT 5322 5336 5337                                                           
CONECT 5323 5321 5338                                                           
CONECT 5324 5339 5340 5343                                                      
CONECT 5325 5340 5341                                                           
CONECT 5326 5327                                                                
CONECT 5327 5326 5328 5329 5334                                                 
CONECT 5328 5327                                                                
CONECT 5329 5317 5327                                                           
CONECT 5330 5317                                                                
CONECT 5331 5319 5320                                                           
CONECT 5332 5320 5333                                                           
CONECT 5333 5318 5332 5334                                                      
CONECT 5334 5327 5333 5335                                                      
CONECT 5335 5321 5334                                                           
CONECT 5336 5321 5322                                                           
CONECT 5337 5322 5338                                                           
CONECT 5338 5323 5337                                                           
CONECT 5339 5320 5324 5345                                                      
CONECT 5340 5324 5325                                                           
CONECT 5341 5325 5342                                                           
CONECT 5342 5341 5343                                                           
CONECT 5343 5324 5342 5344                                                      
CONECT 5344 5343 5345                                                           
CONECT 5345 5339 5344 5346                                                      
CONECT 5346 5345                                                                
MASTER      425    0    5   32   17    0    7    6 5472    2   96   56          
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.