CNRS Nantes University UFIP UFIP
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***  Trn1-4FDD  ***

elNémo ID: 20111014251016793

Job options:

ID        	=	 20111014251016793
JOBID     	=	 Trn1-4FDD
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 Trn1-4FDD

HEADER    TRANSPORT PROTEIN                       28-MAY-12   4FDD              
TITLE     CRYSTAL STRUCTURE OF KAP BETA2-PY-NLS                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRANSPORTIN-1;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: IMPORTIN BETA-2, KARYOPHERIN BETA-2, M9 REGION INTERACTION  
COMPND   5 PROTEIN, MIP;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: RNA-BINDING PROTEIN FUS;                                   
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: 75 KDA DNA-PAIRING PROTEIN, ONCOGENE FUS, ONCOGENE TLS,     
COMPND  11 POMP75, TRANSLOCATED IN LIPOSARCOMA PROTEIN;                         
COMPND  12 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: KPNB2, MIP1, TNPO1, TRANSPORTIN-1, TRN;                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEXTEV;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: FUS, TLS;                                                      
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PGEXTEV                                   
KEYWDS    HEAT REPEATS, KARYOPHERIN, NUCLEAR IMPORT, PROTEIN TRANSPORT,         
KEYWDS   2 IMPORTIN, TRANSPORTIN, TRANSPORT PROTEIN                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.C.ZHANG,Y.M.CHOOK                                                   
REVDAT   4   15-NOV-17 4FDD    1       REMARK                                   
REVDAT   3   16-AUG-17 4FDD    1       SOURCE REMARK                            
REVDAT   2   12-DEC-12 4FDD    1       JRNL                                     
REVDAT   1   18-JUL-12 4FDD    0                                                
JRNL        AUTH   Z.C.ZHANG,Y.M.CHOOK                                          
JRNL        TITL   STRUCTURAL AND ENERGETIC BASIS OF ALS-CAUSING MUTATIONS IN   
JRNL        TITL 2 THE ATYPICAL PROLINE-TYROSINE NUCLEAR LOCALIZATION SIGNAL OF 
JRNL        TITL 3 THE FUSED IN SARCOMA PROTEIN (FUS).                          
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 109 12017 2012              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   22778397                                                     
JRNL        DOI    10.1073/PNAS.1207247109                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.E.CANSIZOGLU,Y.M.CHOOK                                     
REMARK   1  TITL   CONFORMATIONAL HETEROGENEITY OF KARYOPHERIN BETA2 IS         
REMARK   1  TITL 2 SEGMENTAL.                                                   
REMARK   1  REF    STRUCTURE                     V.  15  1431 2007              
REMARK   1  REFN                   ISSN 0969-2126                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   A.E.CANSIZOGLU,B.J.LEE,Z.C.ZHANG,B.M.FONTOURA,Y.M CHOOK      
REMARK   1  TITL   STRUCTURE-BASED DESIGN OF A PATHWAY-SPECIFIC NUCLEAR IMPORT  
REMARK   1  TITL 2 INHIBITOR.                                                   
REMARK   1  REF    NAT.STRUCT.MOL.BIOL.          V.  14   452 2007              
REMARK   1  REFN                   ISSN 1545-9993                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   B.J.LEE,A.E.CANSIZOGLU,T.H.LOUIS,Z.C.ZHANG,Y.M.CHOOK         
REMARK   1  TITL   RULES FOR NUCLEAR LOCALIZATION SEQUENCE RECOGNITION BY       
REMARK   1  TITL 2 KARYOPHERIN BETA 2.                                          
REMARK   1  REF    CELL(CAMBRIDGE,MASS.)         V. 126   543 2006              
REMARK   1  REFN                   ISSN 0092-8674                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   Y.M.CHOOK,G.BLOBEL                                           
REMARK   1  TITL   STRUCTURE OF THE NUCLEAR TRANSPORT COMPLEX                   
REMARK   1  TITL 2 KARYOPHERIN-BETA2-RAN X GPPNHP.                              
REMARK   1  REF    NATURE                        V. 399   230 1999              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 99.61                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 60430                          
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) : 0.287                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3061                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3279                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.63                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3650                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 157                          
REMARK   3   BIN FREE R VALUE                    : 0.3850                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6821                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 148                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 70.67                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.11000                                             
REMARK   3    B22 (A**2) : 0.37000                                              
REMARK   3    B33 (A**2) : 1.75000                                              
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): 0.238         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.201         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.182         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.740        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6967 ; 0.007 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9457 ; 1.223 ; 1.976       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   853 ; 4.934 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   317 ;40.998 ;24.984       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1249 ;17.894 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    36 ;19.822 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1077 ; 0.093 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5220 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  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 : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     5        A   890                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.8450  38.0960  -3.7420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0480 T22:   0.1404                                     
REMARK   3      T33:   0.0761 T12:   0.0247                                     
REMARK   3      T13:   0.0074 T23:   0.0363                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5613 L22:   0.3567                                     
REMARK   3      L33:   0.0514 L12:  -0.1140                                     
REMARK   3      L13:  -0.0727 L23:   0.1277                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0960 S12:   0.0181 S13:   0.0708                       
REMARK   3      S21:  -0.0270 S22:  -0.0814 S23:  -0.0525                       
REMARK   3      S31:  -0.0101 S32:  -0.0084 S33:  -0.0147                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   507        B   526                          
REMARK   3    ORIGIN FOR THE GROUP (A):  33.5170  42.6880   4.6610              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0835 T22:   0.1635                                     
REMARK   3      T33:   0.1367 T12:  -0.0141                                     
REMARK   3      T13:   0.0385 T23:   0.0541                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8715 L22:   1.8119                                     
REMARK   3      L33:   0.1017 L12:   0.4639                                     
REMARK   3      L13:   0.4513 L23:   0.1568                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0610 S12:  -0.0054 S13:   0.1294                       
REMARK   3      S21:   0.1183 S22:  -0.0238 S23:   0.0768                       
REMARK   3      S31:   0.0003 S32:  -0.0267 S33:  -0.0372                       
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 USED IF PRESENT IN    
REMARK   3  THE INPUT U VALUES : RESIDUAL ONLY                                  
REMARK   4                                                                      
REMARK   4 4FDD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000072759.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-NOV-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97918                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 60461                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 99.610                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : 0.07400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 12.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.34                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 78.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45300                            
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 2.3.0                                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 M SUCCINIC ACID, 0.1 M HEPES PH 7.0    
REMARK 280  AND 1% PEG MME 2000, VAPOR DIFFUSION, TEMPERATURE 293.15K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       64.36000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       78.62750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       64.36000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       78.62750            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2540 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 37430 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     TYR A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     ASP A   359                                                      
REMARK 465     VAL A   360                                                      
REMARK 465     GLU A   361                                                      
REMARK 465     GLY A   362                                                      
REMARK 465     GLY A   363                                                      
REMARK 465     SER A   364                                                      
REMARK 465     GLY A   365                                                      
REMARK 465     GLY A   366                                                      
REMARK 465     ASP A   367                                                      
REMARK 465     ASP A   368                                                      
REMARK 465     THR A   369                                                      
REMARK 465     ILE A   370                                                      
REMARK 465     ARG B   498                                                      
REMARK 465     GLY B   499                                                      
REMARK 465     GLY B   500                                                      
REMARK 465     GLY B   501                                                      
REMARK 465     ASP B   502                                                      
REMARK 465     ARG B   503                                                      
REMARK 465     GLY B   504                                                      
REMARK 465     GLY B   505                                                      
REMARK 465     PHE B   506                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 184    CG   CD   CE   NZ                                   
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    ALA A  78       -6.76   -148.27                                   
REMARK 500    SER A 119      -74.31    -56.73                                   
REMARK 500    LEU A 123     -102.42     16.31                                   
REMARK 500    GLU A 161       -9.35    126.18                                   
REMARK 500    ARG A 170       80.94      8.21                                   
REMARK 500    ARG A 246       56.49   -118.61                                   
REMARK 500    ARG A 391     -127.64     47.39                                   
REMARK 500    CYS A 512     -124.78     52.50                                   
REMARK 500    GLN A 534     -168.19    -74.89                                   
REMARK 500    ASP A 582       -7.18    -56.51                                   
REMARK 500    GLN A 598     -127.23     47.69                                   
REMARK 500    CYS A 698       75.16   -154.19                                   
REMARK 500    VAL A 750      -33.78   -138.79                                   
REMARK 500    LEU A 884       40.10    -84.47                                   
REMARK 500    ALA A 885      -31.93   -133.09                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2QMR   RELATED DB: PDB                                   
REMARK 900 KARYOPHERIN BETA2/TRANSPORTIN                                        
REMARK 900 RELATED ID: 2OT8   RELATED DB: PDB                                   
REMARK 900 KARYOPHERIN BETA2/TRANSPORTIN-HNRNPM NLS COMPLEX                     
REMARK 900 RELATED ID: 2H4M   RELATED DB: PDB                                   
REMARK 900 KARYOPHERIN BETA2/TRANSPORTIN-M9NLS                                  
REMARK 900 RELATED ID: 1QBK   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE KARYOPHERIN BETA2-RAN GPPNHP NUCLEAR TRANSPORT      
REMARK 900 COMPLEX                                                              
DBREF  4FDD A    1   361  UNP    Q92973   TNPO1_HUMAN      9    331             
DBREF  4FDD A  367   890  UNP    Q92973   TNPO1_HUMAN    375    898             
DBREF  4FDD B  498   526  UNP    P35637   FUS_HUMAN      498    526             
SEQADV 4FDD GLY A  362  UNP  Q92973              LINKER                         
SEQADV 4FDD GLY A  363  UNP  Q92973              LINKER                         
SEQADV 4FDD SER A  364  UNP  Q92973              LINKER                         
SEQADV 4FDD GLY A  365  UNP  Q92973              LINKER                         
SEQADV 4FDD GLY A  366  UNP  Q92973              LINKER                         
SEQRES   1 A  852  MET GLU TYR GLU TRP LYS PRO ASP GLU GLN GLY LEU GLN          
SEQRES   2 A  852  GLN ILE LEU GLN LEU LEU LYS GLU SER GLN SER PRO ASP          
SEQRES   3 A  852  THR THR ILE GLN ARG THR VAL GLN GLN LYS LEU GLU GLN          
SEQRES   4 A  852  LEU ASN GLN TYR PRO ASP PHE ASN ASN TYR LEU ILE PHE          
SEQRES   5 A  852  VAL LEU THR LYS LEU LYS SER GLU ASP GLU PRO THR ARG          
SEQRES   6 A  852  SER LEU SER GLY LEU ILE LEU LYS ASN ASN VAL LYS ALA          
SEQRES   7 A  852  HIS PHE GLN ASN PHE PRO ASN GLY VAL THR ASP PHE ILE          
SEQRES   8 A  852  LYS SER GLU CYS LEU ASN ASN ILE GLY ASP SER SER PRO          
SEQRES   9 A  852  LEU ILE ARG ALA THR VAL GLY ILE LEU ILE THR THR ILE          
SEQRES  10 A  852  ALA SER LYS GLY GLU LEU GLN ASN TRP PRO ASP LEU LEU          
SEQRES  11 A  852  PRO LYS LEU CYS SER LEU LEU ASP SER GLU ASP TYR ASN          
SEQRES  12 A  852  THR CYS GLU GLY ALA PHE GLY ALA LEU GLN LYS ILE CYS          
SEQRES  13 A  852  GLU ASP SER ALA GLU ILE LEU ASP SER ASP VAL LEU ASP          
SEQRES  14 A  852  ARG PRO LEU ASN ILE MET ILE PRO LYS PHE LEU GLN PHE          
SEQRES  15 A  852  PHE LYS HIS SER SER PRO LYS ILE ARG SER HIS ALA VAL          
SEQRES  16 A  852  ALA CYS VAL ASN GLN PHE ILE ILE SER ARG THR GLN ALA          
SEQRES  17 A  852  LEU MET LEU HIS ILE ASP SER PHE ILE GLU ASN LEU PHE          
SEQRES  18 A  852  ALA LEU ALA GLY ASP GLU GLU PRO GLU VAL ARG LYS ASN          
SEQRES  19 A  852  VAL CYS ARG ALA LEU VAL MET LEU LEU GLU VAL ARG MET          
SEQRES  20 A  852  ASP ARG LEU LEU PRO HIS MET HIS ASN ILE VAL GLU TYR          
SEQRES  21 A  852  MET LEU GLN ARG THR GLN ASP GLN ASP GLU ASN VAL ALA          
SEQRES  22 A  852  LEU GLU ALA CYS GLU PHE TRP LEU THR LEU ALA GLU GLN          
SEQRES  23 A  852  PRO ILE CYS LYS ASP VAL LEU VAL ARG HIS LEU PRO LYS          
SEQRES  24 A  852  LEU ILE PRO VAL LEU VAL ASN GLY MET LYS TYR SER ASP          
SEQRES  25 A  852  ILE ASP ILE ILE LEU LEU LYS GLY ASP VAL GLU GLY GLY          
SEQRES  26 A  852  SER GLY GLY ASP ASP THR ILE SER ASP TRP ASN LEU ARG          
SEQRES  27 A  852  LYS CYS SER ALA ALA ALA LEU ASP VAL LEU ALA ASN VAL          
SEQRES  28 A  852  TYR ARG ASP GLU LEU LEU PRO HIS ILE LEU PRO LEU LEU          
SEQRES  29 A  852  LYS GLU LEU LEU PHE HIS HIS GLU TRP VAL VAL LYS GLU          
SEQRES  30 A  852  SER GLY ILE LEU VAL LEU GLY ALA ILE ALA GLU GLY CYS          
SEQRES  31 A  852  MET GLN GLY MET ILE PRO TYR LEU PRO GLU LEU ILE PRO          
SEQRES  32 A  852  HIS LEU ILE GLN CYS LEU SER ASP LYS LYS ALA LEU VAL          
SEQRES  33 A  852  ARG SER ILE THR CYS TRP THR LEU SER ARG TYR ALA HIS          
SEQRES  34 A  852  TRP VAL VAL SER GLN PRO PRO ASP THR TYR LEU LYS PRO          
SEQRES  35 A  852  LEU MET THR GLU LEU LEU LYS ARG ILE LEU ASP SER ASN          
SEQRES  36 A  852  LYS ARG VAL GLN GLU ALA ALA CYS SER ALA PHE ALA THR          
SEQRES  37 A  852  LEU GLU GLU GLU ALA CYS THR GLU LEU VAL PRO TYR LEU          
SEQRES  38 A  852  ALA TYR ILE LEU ASP THR LEU VAL PHE ALA PHE SER LYS          
SEQRES  39 A  852  TYR GLN HIS LYS ASN LEU LEU ILE LEU TYR ASP ALA ILE          
SEQRES  40 A  852  GLY THR LEU ALA ASP SER VAL GLY HIS HIS LEU ASN LYS          
SEQRES  41 A  852  PRO GLU TYR ILE GLN MET LEU MET PRO PRO LEU ILE GLN          
SEQRES  42 A  852  LYS TRP ASN MET LEU LYS ASP GLU ASP LYS ASP LEU PHE          
SEQRES  43 A  852  PRO LEU LEU GLU CYS LEU SER SER VAL ALA THR ALA LEU          
SEQRES  44 A  852  GLN SER GLY PHE LEU PRO TYR CYS GLU PRO VAL TYR GLN          
SEQRES  45 A  852  ARG CYS VAL ASN LEU VAL GLN LYS THR LEU ALA GLN ALA          
SEQRES  46 A  852  MET LEU ASN ASN ALA GLN PRO ASP GLN TYR GLU ALA PRO          
SEQRES  47 A  852  ASP LYS ASP PHE MET ILE VAL ALA LEU ASP LEU LEU SER          
SEQRES  48 A  852  GLY LEU ALA GLU GLY LEU GLY GLY ASN ILE GLU GLN LEU          
SEQRES  49 A  852  VAL ALA ARG SER ASN ILE LEU THR LEU MET TYR GLN CYS          
SEQRES  50 A  852  MET GLN ASP LYS MET PRO GLU VAL ARG GLN SER SER PHE          
SEQRES  51 A  852  ALA LEU LEU GLY ASP LEU THR LYS ALA CYS PHE GLN HIS          
SEQRES  52 A  852  VAL LYS PRO CYS ILE ALA ASP PHE MET PRO ILE LEU GLY          
SEQRES  53 A  852  THR ASN LEU ASN PRO GLU PHE ILE SER VAL CYS ASN ASN          
SEQRES  54 A  852  ALA THR TRP ALA ILE GLY GLU ILE SER ILE GLN MET GLY          
SEQRES  55 A  852  ILE GLU MET GLN PRO TYR ILE PRO MET VAL LEU HIS GLN          
SEQRES  56 A  852  LEU VAL GLU ILE ILE ASN ARG PRO ASN THR PRO LYS THR          
SEQRES  57 A  852  LEU LEU GLU ASN THR ALA ILE THR ILE GLY ARG LEU GLY          
SEQRES  58 A  852  TYR VAL CYS PRO GLN GLU VAL ALA PRO MET LEU GLN GLN          
SEQRES  59 A  852  PHE ILE ARG PRO TRP CYS THR SER LEU ARG ASN ILE ARG          
SEQRES  60 A  852  ASP ASN GLU GLU LYS ASP SER ALA PHE ARG GLY ILE CYS          
SEQRES  61 A  852  THR MET ILE SER VAL ASN PRO SER GLY VAL ILE GLN ASP          
SEQRES  62 A  852  PHE ILE PHE PHE CYS ASP ALA VAL ALA SER TRP ILE ASN          
SEQRES  63 A  852  PRO LYS ASP ASP LEU ARG ASP MET PHE CYS LYS ILE LEU          
SEQRES  64 A  852  HIS GLY PHE LYS ASN GLN VAL GLY ASP GLU ASN TRP ARG          
SEQRES  65 A  852  ARG PHE SER ASP GLN PHE PRO LEU PRO LEU LYS GLU ARG          
SEQRES  66 A  852  LEU ALA ALA PHE TYR GLY VAL                                  
SEQRES   1 B   29  ARG GLY GLY GLY ASP ARG GLY GLY PHE GLY PRO GLY LYS          
SEQRES   2 B   29  MET ASP SER ARG GLY GLU HIS ARG GLN ASP ARG ARG GLU          
SEQRES   3 B   29  ARG PRO TYR                                                  
FORMUL   3  HOH   *148(H2 O)                                                    
HELIX    1   1 ASP A    8  GLN A   23  1                                  16    
HELIX    2   2 ASP A   26  ASN A   41  1                                  16    
HELIX    3   3 TYR A   43  LYS A   56  1                                  14    
HELIX    4   4 ASP A   61  VAL A   76  1                                  16    
HELIX    5   5 LYS A   77  ALA A   78  5                                   2    
HELIX    6   6 HIS A   79  PHE A   83  5                                   5    
HELIX    7   7 PRO A   84  ASN A   97  1                                  14    
HELIX    8   8 SER A  103  GLY A  121  1                                  19    
HELIX    9   9 ASP A  128  ASP A  138  1                                  11    
HELIX   10  10 ASP A  141  ALA A  160  1                                  20    
HELIX   11  11 GLU A  161  ASP A  166  1                                   6    
HELIX   12  12 PRO A  171  LEU A  180  1                                  10    
HELIX   13  13 SER A  187  GLN A  200  1                                  14    
HELIX   14  14 THR A  206  LEU A  211  1                                   6    
HELIX   15  15 HIS A  212  GLY A  225  1                                  14    
HELIX   16  16 GLU A  228  ARG A  246  1                                  19    
HELIX   17  17 ARG A  246  LEU A  251  1                                   6    
HELIX   18  18 HIS A  253  GLN A  266  1                                  14    
HELIX   19  19 ASP A  269  ALA A  284  1                                  16    
HELIX   20  20 ILE A  288  VAL A  294  1                                   7    
HELIX   21  21 HIS A  296  MET A  308  1                                  13    
HELIX   22  22 SER A  311  GLY A  320  1                                  10    
HELIX   23  23 ASN A  374  ARG A  391  1                                  18    
HELIX   24  24 LEU A  394  PHE A  407  1                                  14    
HELIX   25  25 GLU A  410  ILE A  424  1                                  15    
HELIX   26  26 CYS A  428  ILE A  433  1                                   6    
HELIX   27  27 TYR A  435  LEU A  447  1                                  13    
HELIX   28  28 LYS A  451  TYR A  465  1                                  15    
HELIX   29  29 TYR A  465  GLN A  472  1                                   8    
HELIX   30  30 TYR A  477  LEU A  490  1                                  14    
HELIX   31  31 ASN A  493  CYS A  512  1                                  20    
HELIX   32  32 THR A  513  PRO A  517  5                                   5    
HELIX   33  33 TYR A  518  TYR A  533  1                                  16    
HELIX   34  34 GLN A  534  GLY A  553  1                                  20    
HELIX   35  35 HIS A  554  ASN A  557  5                                   4    
HELIX   36  36 LYS A  558  LEU A  576  1                                  19    
HELIX   37  37 ASP A  582  GLN A  598  1                                  17    
HELIX   38  38 SER A  599  PRO A  603  5                                   5    
HELIX   39  39 TYR A  604  GLN A  629  1                                  26    
HELIX   40  40 LYS A  638  GLY A  656  1                                  19    
HELIX   41  41 ILE A  659  ARG A  665  1                                   7    
HELIX   42  42 ASN A  667  MET A  676  1                                  10    
HELIX   43  43 MET A  680  CYS A  698  1                                  19    
HELIX   44  44 PHE A  699  PRO A  704  5                                   6    
HELIX   45  45 CYS A  705  ASN A  716  1                                  12    
HELIX   46  46 PHE A  721  GLY A  740  1                                  20    
HELIX   47  47 ILE A  741  TYR A  746  5                                   6    
HELIX   48  48 ILE A  747  ASN A  759  1                                  13    
HELIX   49  49 PRO A  764  CYS A  782  1                                  19    
HELIX   50  50 CYS A  782  ALA A  787  1                                   6    
HELIX   51  51 MET A  789  ASN A  803  1                                  15    
HELIX   52  52 ASN A  807  ASN A  824  1                                  18    
HELIX   53  53 PRO A  825  GLN A  830  5                                   6    
HELIX   54  54 ASP A  831  SER A  841  1                                  11    
HELIX   55  55 LYS A  846  SER A  873  1                                  28    
HELIX   56  56 ASP A  874  PHE A  876  5                                   3    
HELIX   57  57 PRO A  877  PHE A  887  1                                  11    
HELIX   58  58 SER B  513  ARG B  522  1                                  10    
CRYST1  128.720  157.255   67.543  90.00  90.00  90.00 P 21 21 2     4          
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      0.007769  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006359  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014805        0.00000                         
ATOM      1  N   TRP A   5      57.006  -2.253 -31.742  1.00119.26           N  
ANISOU    1  N   TRP A   5    13816  15645  15853    936    -50   -870       N  
ATOM      2  CA  TRP A   5      58.148  -1.829 -30.882  1.00120.15           C  
ANISOU    2  CA  TRP A   5    13938  15708  16007    903    -37   -795       C  
ATOM      3  C   TRP A   5      58.931  -3.033 -30.389  1.00126.31           C  
ANISOU    3  C   TRP A   5    14664  16416  16914    879    -57   -815       C  
ATOM      4  O   TRP A   5      58.945  -4.074 -31.051  1.00130.05           O  
ANISOU    4  O   TRP A   5    15089  16888  17434    895    -63   -894       O  
ATOM      5  CB  TRP A   5      57.650  -0.902 -29.763  1.00115.32           C  
ANISOU    5  CB  TRP A   5    13373  15078  15363    874    -50   -708       C  
ATOM      6  CG  TRP A   5      58.550  -0.802 -28.552  1.00113.91           C  
ANISOU    6  CG  TRP A   5    13194  14834  15254    832    -58   -638       C  
ATOM      7  CD1 TRP A   5      59.832  -0.249 -28.476  1.00113.93           C  
ANISOU    7  CD1 TRP A   5    13201  14823  15265    825    -27   -599       C  
ATOM      8  CD2 TRP A   5      58.258  -1.275 -27.189  1.00108.99           C  
ANISOU    8  CD2 TRP A   5    12564  14146  14703    791   -101   -596       C  
ATOM      9  NE1 TRP A   5      60.336  -0.355 -27.200  1.00110.03           N  
ANISOU    9  NE1 TRP A   5    12702  14264  14840    784    -51   -542       N  
ATOM     10  CE2 TRP A   5      59.444  -0.959 -26.381  1.00107.36           C  
ANISOU   10  CE2 TRP A   5    12359  13894  14540    763    -95   -535       C  
ATOM     11  CE3 TRP A   5      57.178  -1.911 -26.584  1.00103.68           C  
ANISOU   11  CE3 TRP A   5    11883  13450  14062    776   -141   -603       C  
ATOM     12  CZ2 TRP A   5      59.516  -1.271 -25.034  1.00104.37           C  
ANISOU   12  CZ2 TRP A   5    11976  13454  14227    725   -130   -483       C  
ATOM     13  CZ3 TRP A   5      57.263  -2.219 -25.225  1.00100.69           C  
ANISOU   13  CZ3 TRP A   5    11501  13007  13751    736   -172   -547       C  
ATOM     14  CH2 TRP A   5      58.403  -1.906 -24.471  1.00102.07           C  
ANISOU   14  CH2 TRP A   5    11679  13143  13960    712   -167   -488       C  
ATOM     15  N   LYS A   6      59.577  -2.913 -29.230  1.00126.40           N  
ANISOU   15  N   LYS A   6    14677  16365  16982    840    -68   -745       N  
ATOM     16  CA  LYS A   6      60.573  -3.877 -28.759  1.00124.89           C  
ANISOU   16  CA  LYS A   6    14438  16107  16908    818    -82   -751       C  
ATOM     17  C   LYS A   6      60.242  -4.482 -27.367  1.00118.14           C  
ANISOU   17  C   LYS A   6    13572  15180  16136    778   -129   -707       C  
ATOM     18  O   LYS A   6      61.084  -4.458 -26.456  1.00125.75           O  
ANISOU   18  O   LYS A   6    14532  16093  17155    750   -138   -652       O  
ATOM     19  CB  LYS A   6      61.962  -3.190 -28.775  1.00131.49           C  
ANISOU   19  CB  LYS A   6    15282  16936  17741    814    -46   -712       C  
ATOM     20  CG  LYS A   6      63.168  -4.037 -28.362  1.00135.36           C  
ANISOU   20  CG  LYS A   6    15723  17359  18347    794    -55   -715       C  
ATOM     21  CD  LYS A   6      64.399  -3.171 -28.013  1.00137.31           C  
ANISOU   21  CD  LYS A   6    15986  17593  18592    781    -27   -657       C  
ATOM     22  CE  LYS A   6      64.130  -2.110 -26.920  1.00139.32           C  
ANISOU   22  CE  LYS A   6    16291  17839  18805    755    -39   -567       C  
ATOM     23  NZ  LYS A   6      63.642  -2.660 -25.608  1.00137.96           N  
ANISOU   23  NZ  LYS A   6    16114  17612  18693    721    -91   -528       N  
ATOM     24  N   PRO A   7      59.022  -5.037 -27.188  1.00106.42           N  
ANISOU   24  N   PRO A   7    12081  13692  14660    777   -160   -731       N  
ATOM     25  CA  PRO A   7      58.810  -5.694 -25.894  1.00100.82           C  
ANISOU   25  CA  PRO A   7    11358  12913  14037    740   -200   -688       C  
ATOM     26  C   PRO A   7      59.423  -7.100 -25.860  1.00 99.56           C  
ANISOU   26  C   PRO A   7    11134  12693  14003    733   -217   -730       C  
ATOM     27  O   PRO A   7      59.112  -7.930 -26.719  1.00 99.09           O  
ANISOU   27  O   PRO A   7    11034  12643  13972    755   -217   -812       O  
ATOM     28  CB  PRO A   7      57.291  -5.770 -25.787  1.00 96.03           C  
ANISOU   28  CB  PRO A   7    10766  12324  13398    742   -221   -701       C  
ATOM     29  CG  PRO A   7      56.811  -5.808 -27.199  1.00 98.83           C  
ANISOU   29  CG  PRO A   7    11112  12744  13697    784   -202   -786       C  
ATOM     30  CD  PRO A   7      57.840  -5.138 -28.065  1.00101.64           C  
ANISOU   30  CD  PRO A   7    11479  13141  13999    807   -160   -795       C  
ATOM     31  N   ASP A   8      60.301  -7.361 -24.894  1.00 93.97           N  
ANISOU   31  N   ASP A   8    10413  11923  13370    705   -232   -676       N  
ATOM     32  CA  ASP A   8      60.853  -8.710 -24.747  1.00 96.49           C  
ANISOU   32  CA  ASP A   8    10670  12178  13815    696   -251   -707       C  
ATOM     33  C   ASP A   8      60.370  -9.376 -23.464  1.00 94.36           C  
ANISOU   33  C   ASP A   8    10390  11842  13620    665   -293   -657       C  
ATOM     34  O   ASP A   8      60.003  -8.696 -22.503  1.00 88.00           O  
ANISOU   34  O   ASP A   8     9628  11034  12773    643   -305   -583       O  
ATOM     35  CB  ASP A   8      62.387  -8.726 -24.866  1.00 97.50           C  
ANISOU   35  CB  ASP A   8    10774  12283  13987    695   -235   -702       C  
ATOM     36  CG  ASP A   8      63.069  -7.978 -23.743  1.00 96.50           C  
ANISOU   36  CG  ASP A   8    10679  12130  13855    668   -242   -608       C  
ATOM     37  OD1 ASP A   8      63.509  -6.836 -23.980  1.00 95.55           O  
ANISOU   37  OD1 ASP A   8    10597  12051  13657    674   -213   -583       O  
ATOM     38  OD2 ASP A   8      63.160  -8.529 -22.626  1.00 95.82           O  
ANISOU   38  OD2 ASP A   8    10581  11983  13844    641   -277   -561       O  
ATOM     39  N   GLU A   9      60.388 -10.709 -23.467  1.00 98.14           N  
ANISOU   39  N   GLU A   9    10811  12268  14209    662   -312   -699       N  
ATOM     40  CA  GLU A   9      59.731 -11.519 -22.436  1.00103.63           C  
ANISOU   40  CA  GLU A   9    11490  12903  14981    638   -348   -665       C  
ATOM     41  C   GLU A   9      60.212 -11.253 -21.019  1.00103.25           C  
ANISOU   41  C   GLU A   9    11465  12810  14954    605   -369   -563       C  
ATOM     42  O   GLU A   9      59.397 -11.107 -20.098  1.00102.42           O  
ANISOU   42  O   GLU A   9    11387  12692  14833    586   -388   -508       O  
ATOM     43  CB  GLU A   9      59.842 -13.016 -22.759  1.00106.93           C  
ANISOU   43  CB  GLU A   9    11836  13268  15526    642   -361   -729       C  
ATOM     44  CG  GLU A   9      58.858 -13.499 -23.820  1.00115.24           C  
ANISOU   44  CG  GLU A   9    12863  14353  16571    668   -354   -826       C  
ATOM     45  CD  GLU A   9      57.425 -13.040 -23.564  1.00118.78           C  
ANISOU   45  CD  GLU A   9    13350  14832  16950    665   -362   -811       C  
ATOM     46  OE1 GLU A   9      56.818 -12.436 -24.478  1.00117.61           O  
ANISOU   46  OE1 GLU A   9    13223  14754  16708    690   -344   -860       O  
ATOM     47  OE2 GLU A   9      56.906 -13.269 -22.447  1.00119.00           O  
ANISOU   47  OE2 GLU A   9    13386  14814  17014    638   -385   -749       O  
ATOM     48  N   GLN A  10      61.532 -11.189 -20.862  1.00 99.62           N  
ANISOU   48  N   GLN A  10    10994  12328  14530    601   -366   -540       N  
ATOM     49  CA  GLN A  10      62.167 -10.903 -19.581  1.00 96.06           C  
ANISOU   49  CA  GLN A  10    10562  11839  14098    574   -387   -449       C  
ATOM     50  C   GLN A  10      61.651  -9.575 -19.014  1.00 87.95           C  
ANISOU   50  C   GLN A  10     9604  10857  12958    563   -383   -386       C  
ATOM     51  O   GLN A  10      61.261  -9.502 -17.846  1.00 78.66           O  
ANISOU   51  O   GLN A  10     8449   9655  11782    540   -408   -317       O  
ATOM     52  CB  GLN A  10      63.695 -10.888 -19.750  1.00102.95           C  
ANISOU   52  CB  GLN A  10    11411  12693  15013    577   -379   -449       C  
ATOM     53  CG  GLN A  10      64.497 -10.566 -18.495  1.00107.45           C  
ANISOU   53  CG  GLN A  10    11996  13226  15604    553   -402   -361       C  
ATOM     54  CD  GLN A  10      64.794 -11.775 -17.633  1.00114.19           C  
ANISOU   54  CD  GLN A  10    12807  14002  16579    537   -440   -332       C  
ATOM     55  OE1 GLN A  10      64.104 -12.797 -17.706  1.00114.48           O  
ANISOU   55  OE1 GLN A  10    12811  14007  16678    538   -452   -361       O  
ATOM     56  NE2 GLN A  10      65.834 -11.666 -16.804  1.00118.09           N  
ANISOU   56  NE2 GLN A  10    13298  14462  17109    523   -459   -275       N  
ATOM     57  N   GLY A  11      61.636  -8.542 -19.856  1.00 85.47           N  
ANISOU   57  N   GLY A  11     9320  10607  12545    582   -349   -411       N  
ATOM     58  CA  GLY A  11      61.145  -7.224 -19.463  1.00 86.72           C  
ANISOU   58  CA  GLY A  11     9542  10812  12596    575   -341   -359       C  
ATOM     59  C   GLY A  11      59.683  -7.264 -19.054  1.00 87.42           C  
ANISOU   59  C   GLY A  11     9653  10909  12653    567   -356   -348       C  
ATOM     60  O   GLY A  11      59.299  -6.725 -18.008  1.00 82.07           O  
ANISOU   60  O   GLY A  11     9012  10227  11942    545   -370   -280       O  
ATOM     61  N   LEU A  12      58.872  -7.923 -19.879  1.00 88.53           N  
ANISOU   61  N   LEU A  12     9769  11061  12806    585   -352   -418       N  
ATOM     62  CA  LEU A  12      57.436  -8.004 -19.646  1.00 87.56           C  
ANISOU   62  CA  LEU A  12     9661  10948  12658    581   -363   -420       C  
ATOM     63  C   LEU A  12      57.127  -8.759 -18.356  1.00 86.50           C  
ANISOU   63  C   LEU A  12     9516  10750  12600    551   -396   -365       C  
ATOM     64  O   LEU A  12      56.291  -8.323 -17.564  1.00 80.97           O  
ANISOU   64  O   LEU A  12     8851  10055  11858    534   -406   -316       O  
ATOM     65  CB  LEU A  12      56.732  -8.658 -20.835  1.00 88.32           C  
ANISOU   65  CB  LEU A  12     9726  11068  12765    608   -355   -515       C  
ATOM     66  CG  LEU A  12      55.235  -8.383 -20.992  1.00 89.67           C  
ANISOU   66  CG  LEU A  12     9919  11274  12876    614   -356   -534       C  
ATOM     67  CD1 LEU A  12      54.996  -6.960 -21.486  1.00 88.40           C  
ANISOU   67  CD1 LEU A  12     9814  11188  12586    630   -332   -525       C  
ATOM     68  CD2 LEU A  12      54.620  -9.400 -21.941  1.00 89.71           C  
ANISOU   68  CD2 LEU A  12     9875  11280  12930    637   -359   -629       C  
ATOM     69  N   GLN A  13      57.824  -9.874 -18.143  1.00 85.06           N  
ANISOU   69  N   GLN A  13     9283  10507  12528    545   -412   -371       N  
ATOM     70  CA  GLN A  13      57.617 -10.697 -16.958  1.00 88.30           C  
ANISOU   70  CA  GLN A  13     9678  10852  13020    519   -442   -316       C  
ATOM     71  C   GLN A  13      57.864  -9.907 -15.668  1.00 84.13           C  
ANISOU   71  C   GLN A  13     9197  10320  12448    494   -456   -218       C  
ATOM     72  O   GLN A  13      57.149 -10.080 -14.678  1.00 83.09           O  
ANISOU   72  O   GLN A  13     9080  10165  12325    474   -473   -166       O  
ATOM     73  CB  GLN A  13      58.514 -11.933 -17.017  1.00 95.27           C  
ANISOU   73  CB  GLN A  13    10498  11671  14027    520   -455   -338       C  
ATOM     74  CG  GLN A  13      58.089 -13.074 -16.103  1.00101.85           C  
ANISOU   74  CG  GLN A  13    11302  12435  14962    501   -482   -304       C  
ATOM     75  CD  GLN A  13      59.131 -14.182 -16.010  1.00107.02           C  
ANISOU   75  CD  GLN A  13    11899  13023  15741    501   -497   -309       C  
ATOM     76  OE1 GLN A  13      58.791 -15.344 -15.788  1.00111.35           O  
ANISOU   76  OE1 GLN A  13    12403  13514  16390    495   -511   -318       O  
ATOM     77  NE2 GLN A  13      60.406 -13.827 -16.176  1.00105.72           N  
ANISOU   77  NE2 GLN A  13    11732  12864  15574    506   -493   -304       N  
ATOM     78  N   GLN A  14      58.861  -9.025 -15.705  1.00 82.35           N  
ANISOU   78  N   GLN A  14     8993  10119  12176    496   -446   -196       N  
ATOM     79  CA  GLN A  14      59.264  -8.225 -14.543  1.00 80.99           C  
ANISOU   79  CA  GLN A  14     8861   9946  11964    475   -459   -111       C  
ATOM     80  C   GLN A  14      58.241  -7.171 -14.170  1.00 79.03           C  
ANISOU   80  C   GLN A  14     8670   9744  11613    466   -452    -80       C  
ATOM     81  O   GLN A  14      57.963  -6.950 -12.991  1.00 78.55           O  
ANISOU   81  O   GLN A  14     8636   9671  11539    444   -471    -11       O  
ATOM     82  CB  GLN A  14      60.615  -7.543 -14.796  1.00 79.16           C  
ANISOU   82  CB  GLN A  14     8633   9729  11715    481   -447   -106       C  
ATOM     83  CG  GLN A  14      61.812  -8.468 -14.669  1.00 79.87           C  
ANISOU   83  CG  GLN A  14     8674   9763  11911    480   -463   -108       C  
ATOM     84  CD  GLN A  14      62.005  -8.987 -13.257  1.00 79.81           C  
ANISOU   84  CD  GLN A  14     8662   9702  11960    457   -502    -32       C  
ATOM     85  OE1 GLN A  14      62.169  -8.212 -12.308  1.00 80.94           O  
ANISOU   85  OE1 GLN A  14     8843   9855  12055    441   -514     33       O  
ATOM     86  NE2 GLN A  14      61.996 -10.305 -13.110  1.00 77.39           N  
ANISOU   86  NE2 GLN A  14     8309   9338  11758    455   -521    -41       N  
ATOM     87  N   ILE A  15      57.702  -6.506 -15.183  1.00 78.12           N  
ANISOU   87  N   ILE A  15     8573   9684  11424    486   -424   -130       N  
ATOM     88  CA  ILE A  15      56.710  -5.467 -14.957  1.00 81.54           C  
ANISOU   88  CA  ILE A  15     9058  10164  11760    481   -415   -107       C  
ATOM     89  C   ILE A  15      55.369  -6.083 -14.505  1.00 78.07           C  
ANISOU   89  C   ILE A  15     8617   9708  11340    470   -430   -104       C  
ATOM     90  O   ILE A  15      54.775  -5.634 -13.519  1.00 74.65           O  
ANISOU   90  O   ILE A  15     8218   9276  10871    450   -440    -47       O  
ATOM     91  CB  ILE A  15      56.585  -4.516 -16.177  1.00 85.19           C  
ANISOU   91  CB  ILE A  15     9541  10692  12135    507   -381   -156       C  
ATOM     92  CG1 ILE A  15      55.464  -3.494 -15.961  1.00 88.67           C  
ANISOU   92  CG1 ILE A  15    10032  11177  12481    504   -374   -134       C  
ATOM     93  CG2 ILE A  15      56.371  -5.290 -17.470  1.00 86.83           C  
ANISOU   93  CG2 ILE A  15     9709  10908  12373    535   -369   -243       C  
ATOM     94  CD1 ILE A  15      55.349  -2.455 -17.055  1.00 89.76           C  
ANISOU   94  CD1 ILE A  15    10197  11380  12530    530   -341   -170       C  
ATOM     95  N   LEU A  16      54.924  -7.131 -15.198  1.00 73.41           N  
ANISOU   95  N   LEU A  16     7984   9098  10811    484   -430   -166       N  
ATOM     96  CA  LEU A  16      53.742  -7.876 -14.776  1.00 73.45           C  
ANISOU   96  CA  LEU A  16     7977   9076  10856    473   -444   -167       C  
ATOM     97  C   LEU A  16      53.894  -8.363 -13.352  1.00 75.51           C  
ANISOU   97  C   LEU A  16     8237   9282  11172    443   -468    -88       C  
ATOM     98  O   LEU A  16      52.957  -8.261 -12.562  1.00 76.61           O  
ANISOU   98  O   LEU A  16     8399   9417  11292    426   -475    -49       O  
ATOM     99  CB  LEU A  16      53.451  -9.058 -15.703  1.00 70.82           C  
ANISOU   99  CB  LEU A  16     7586   8720  10600    491   -443   -249       C  
ATOM    100  CG  LEU A  16      52.971  -8.709 -17.116  1.00 71.98           C  
ANISOU  100  CG  LEU A  16     7732   8926  10691    523   -421   -335       C  
ATOM    101  CD1 LEU A  16      52.845  -9.964 -17.971  1.00 69.38           C  
ANISOU  101  CD1 LEU A  16     7341   8571  10450    540   -424   -418       C  
ATOM    102  CD2 LEU A  16      51.667  -7.912 -17.087  1.00 68.52           C  
ANISOU  102  CD2 LEU A  16     7335   8533  10166    523   -415   -332       C  
ATOM    103  N   GLN A  17      55.079  -8.873 -13.021  1.00 78.19           N  
ANISOU  103  N   GLN A  17     8550   9580  11577    439   -482    -64       N  
ATOM    104  CA  GLN A  17      55.347  -9.280 -11.655  1.00 79.13           C  
ANISOU  104  CA  GLN A  17     8672   9651  11742    414   -507     17       C  
ATOM    105  C   GLN A  17      55.100  -8.107 -10.715  1.00 76.86           C  
ANISOU  105  C   GLN A  17     8444   9398  11361    397   -509     85       C  
ATOM    106  O   GLN A  17      54.402  -8.254  -9.718  1.00 75.26           O  
ANISOU  106  O   GLN A  17     8258   9179  11159    377   -521    137       O  
ATOM    107  CB  GLN A  17      56.765  -9.827 -11.489  1.00 81.51           C  
ANISOU  107  CB  GLN A  17     8940   9911  12117    415   -522     32       C  
ATOM    108  CG  GLN A  17      57.045 -10.327 -10.071  1.00 86.83           C  
ANISOU  108  CG  GLN A  17     9614  10536  12842    393   -552    118       C  
ATOM    109  CD  GLN A  17      58.494 -10.723  -9.819  1.00 90.65           C  
ANISOU  109  CD  GLN A  17    10069  10982  13390    394   -570    140       C  
ATOM    110  OE1 GLN A  17      59.176 -11.259 -10.697  1.00 94.24           O  
ANISOU  110  OE1 GLN A  17    10482  11420  13905    410   -564     84       O  
ATOM    111  NE2 GLN A  17      58.967 -10.474  -8.601  1.00 89.15           N  
ANISOU  111  NE2 GLN A  17     9903  10780  13192    377   -594    221       N  
ATOM    112  N   LEU A  18      55.653  -6.947 -11.061  1.00 74.53           N  
ANISOU  112  N   LEU A  18     8180   9151  10988    404   -495     82       N  
ATOM    113  CA  LEU A  18      55.501  -5.726 -10.269  1.00 76.07           C  
ANISOU  113  CA  LEU A  18     8428   9382  11092    389   -495    138       C  
ATOM    114  C   LEU A  18      54.042  -5.239 -10.203  1.00 76.40           C  
ANISOU  114  C   LEU A  18     8503   9456  11068    384   -484    135       C  
ATOM    115  O   LEU A  18      53.585  -4.744  -9.169  1.00 75.01           O  
ANISOU  115  O   LEU A  18     8362   9287  10851    364   -492    192       O  
ATOM    116  CB  LEU A  18      56.370  -4.622 -10.867  1.00 80.58           C  
ANISOU  116  CB  LEU A  18     9019   9996  11603    402   -477    123       C  
ATOM    117  CG  LEU A  18      57.247  -3.723  -9.992  1.00 84.30           C  
ANISOU  117  CG  LEU A  18     9518  10475  12037    388   -487    183       C  
ATOM    118  CD1 LEU A  18      57.453  -2.406 -10.721  1.00 87.22           C  
ANISOU  118  CD1 LEU A  18     9917  10899  12323    400   -458    160       C  
ATOM    119  CD2 LEU A  18      56.681  -3.469  -8.599  1.00 84.49           C  
ANISOU  119  CD2 LEU A  18     9575  10496  12032    362   -507    253       C  
ATOM    120  N   LEU A  19      53.324  -5.368 -11.316  1.00 75.88           N  
ANISOU  120  N   LEU A  19     8425   9412  10993    404   -466     65       N  
ATOM    121  CA  LEU A  19      51.903  -5.027 -11.359  1.00 75.24           C  
ANISOU  121  CA  LEU A  19     8367   9358  10862    402   -456     53       C  
ATOM    122  C   LEU A  19      51.079  -5.954 -10.476  1.00 77.35           C  
ANISOU  122  C   LEU A  19     8621   9580  11188    382   -472     83       C  
ATOM    123  O   LEU A  19      50.202  -5.494  -9.744  1.00 77.39           O  
ANISOU  123  O   LEU A  19     8658   9597  11148    365   -471    119       O  
ATOM    124  CB  LEU A  19      51.374  -5.042 -12.797  1.00 70.83           C  
ANISOU  124  CB  LEU A  19     7794   8833  10285    430   -437    -33       C  
ATOM    125  CG  LEU A  19      51.666  -3.773 -13.596  1.00 65.95           C  
ANISOU  125  CG  LEU A  19     7207   8277   9573    449   -414    -54       C  
ATOM    126  CD1 LEU A  19      51.489  -3.998 -15.085  1.00 68.31           C  
ANISOU  126  CD1 LEU A  19     7482   8604   9867    482   -398   -139       C  
ATOM    127  CD2 LEU A  19      50.776  -2.644 -13.126  1.00 68.75           C  
ANISOU  127  CD2 LEU A  19     7612   8670   9838    439   -407    -21       C  
ATOM    128  N   LYS A  20      51.367  -7.255 -10.536  1.00 79.28           N  
ANISOU  128  N   LYS A  20     8816   9770  11535    383   -483     68       N  
ATOM    129  CA  LYS A  20      50.726  -8.210  -9.640  1.00 80.31           C  
ANISOU  129  CA  LYS A  20     8930   9849  11734    364   -496    105       C  
ATOM    130  C   LYS A  20      51.000  -7.840  -8.178  1.00 79.15           C  
ANISOU  130  C   LYS A  20     8818   9693  11563    339   -511    200       C  
ATOM    131  O   LYS A  20      50.088  -7.849  -7.351  1.00 77.61           O  
ANISOU  131  O   LYS A  20     8642   9490  11354    321   -512    240       O  
ATOM    132  CB  LYS A  20      51.183  -9.642  -9.931  1.00 83.39           C  
ANISOU  132  CB  LYS A  20     9260  10179  12247    370   -506     78       C  
ATOM    133  CG  LYS A  20      50.344 -10.696  -9.222  1.00 91.79           C  
ANISOU  133  CG  LYS A  20    10300  11188  13389    354   -513    103       C  
ATOM    134  CD  LYS A  20      51.130 -11.971  -8.962  1.00 96.56           C  
ANISOU  134  CD  LYS A  20    10854  11723  14113    353   -529    119       C  
ATOM    135  CE  LYS A  20      50.483 -12.804  -7.865  1.00 99.12           C  
ANISOU  135  CE  LYS A  20    11169  11992  14501    331   -537    180       C  
ATOM    136  NZ  LYS A  20      51.457 -13.767  -7.274  1.00101.45           N  
ANISOU  136  NZ  LYS A  20    11430  12223  14891    327   -557    227       N  
ATOM    137  N   GLU A  21      52.249  -7.485  -7.880  1.00 79.67           N  
ANISOU  137  N   GLU A  21     8892   9760  11620    338   -522    233       N  
ATOM    138  CA  GLU A  21      52.671  -7.157  -6.509  1.00 81.93           C  
ANISOU  138  CA  GLU A  21     9207  10039  11885    317   -541    320       C  
ATOM    139  C   GLU A  21      52.006  -5.902  -5.957  1.00 79.18           C  
ANISOU  139  C   GLU A  21     8915   9742  11430    304   -532    350       C  
ATOM    140  O   GLU A  21      51.767  -5.796  -4.752  1.00 77.53           O  
ANISOU  140  O   GLU A  21     8729   9526  11202    284   -544    417       O  
ATOM    141  CB  GLU A  21      54.192  -7.022  -6.419  1.00 81.86           C  
ANISOU  141  CB  GLU A  21     9188  10022  11891    322   -556    338       C  
ATOM    142  CG  GLU A  21      54.934  -8.348  -6.422  1.00 87.80           C  
ANISOU  142  CG  GLU A  21     9889  10712  12759    327   -574    339       C  
ATOM    143  CD  GLU A  21      56.452  -8.198  -6.368  1.00 91.48           C  
ANISOU  143  CD  GLU A  21    10343  11170  13243    332   -590    352       C  
ATOM    144  OE1 GLU A  21      56.963  -7.125  -5.958  1.00 90.61           O  
ANISOU  144  OE1 GLU A  21    10269  11096  13062    327   -593    382       O  
ATOM    145  OE2 GLU A  21      57.141  -9.176  -6.733  1.00 90.14           O  
ANISOU  145  OE2 GLU A  21    10127  10957  13166    342   -599    332       O  
ATOM    146  N   SER A  22      51.716  -4.951  -6.840  1.00 77.80           N  
ANISOU  146  N   SER A  22     8759   9616  11184    317   -511    302       N  
ATOM    147  CA  SER A  22      51.026  -3.723  -6.440  1.00 79.55           C  
ANISOU  147  CA  SER A  22     9031   9887  11308    307   -501    323       C  
ATOM    148  C   SER A  22      49.578  -3.993  -6.028  1.00 77.83           C  
ANISOU  148  C   SER A  22     8822   9663  11085    295   -495    330       C  
ATOM    149  O   SER A  22      48.968  -3.181  -5.334  1.00 77.51           O  
ANISOU  149  O   SER A  22     8820   9651  10977    280   -490    364       O  
ATOM    150  CB  SER A  22      51.077  -2.686  -7.562  1.00 78.55           C  
ANISOU  150  CB  SER A  22     8920   9812  11114    327   -478    270       C  
ATOM    151  OG  SER A  22      50.614  -3.242  -8.775  1.00 82.60           O  
ANISOU  151  OG  SER A  22     9403  10325  11656    348   -465    198       O  
ATOM    152  N   GLN A  23      49.052  -5.147  -6.441  1.00 79.86           N  
ANISOU  152  N   GLN A  23     9040   9883  11419    300   -494    296       N  
ATOM    153  CA  GLN A  23      47.682  -5.557  -6.121  1.00 79.98           C  
ANISOU  153  CA  GLN A  23     9055   9886  11449    289   -486    297       C  
ATOM    154  C   GLN A  23      47.607  -6.478  -4.901  1.00 84.33           C  
ANISOU  154  C   GLN A  23     9596  10385  12062    267   -500    365       C  
ATOM    155  O   GLN A  23      46.538  -7.011  -4.576  1.00 87.49           O  
ANISOU  155  O   GLN A  23     9989  10763  12491    257   -492    370       O  
ATOM    156  CB  GLN A  23      47.023  -6.208  -7.340  1.00 75.33           C  
ANISOU  156  CB  GLN A  23     8428   9290  10904    309   -475    214       C  
ATOM    157  CG  GLN A  23      46.884  -5.253  -8.511  1.00 74.68           C  
ANISOU  157  CG  GLN A  23     8361   9266  10749    331   -459    151       C  
ATOM    158  CD  GLN A  23      46.248  -5.889  -9.725  1.00 77.40           C  
ANISOU  158  CD  GLN A  23     8667   9608  11133    354   -451     65       C  
ATOM    159  OE1 GLN A  23      46.943  -6.338 -10.635  1.00 77.61           O  
ANISOU  159  OE1 GLN A  23     8662   9631  11197    374   -452     16       O  
ATOM    160  NE2 GLN A  23      44.918  -5.923  -9.752  1.00 80.29           N  
ANISOU  160  NE2 GLN A  23     9036   9981  11490    351   -443     43       N  
ATOM    161  N   SER A  24      48.740  -6.646  -4.225  1.00 85.49           N  
ANISOU  161  N   SER A  24     9741  10512  12228    262   -519    417       N  
ATOM    162  CA  SER A  24      48.825  -7.453  -3.010  1.00 89.11           C  
ANISOU  162  CA  SER A  24    10194  10925  12740    244   -535    491       C  
ATOM    163  C   SER A  24      48.109  -6.785  -1.837  1.00 89.53           C  
ANISOU  163  C   SER A  24    10294  11002  12721    222   -531    553       C  
ATOM    164  O   SER A  24      48.230  -5.574  -1.648  1.00 88.62           O  
ANISOU  164  O   SER A  24    10219  10938  12515    219   -530    561       O  
ATOM    165  CB  SER A  24      50.293  -7.711  -2.639  1.00 87.71           C  
ANISOU  165  CB  SER A  24    10005  10727  12595    247   -560    529       C  
ATOM    166  OG  SER A  24      50.406  -8.419  -1.413  1.00 84.77           O  
ANISOU  166  OG  SER A  24     9630  10314  12264    233   -577    607       O  
ATOM    167  N   PRO A  25      47.367  -7.580  -1.040  1.00 93.62           N  
ANISOU  167  N   PRO A  25    10806  11484  13283    207   -529    596       N  
ATOM    168  CA  PRO A  25      46.751  -7.065   0.187  1.00 92.88           C  
ANISOU  168  CA  PRO A  25    10753  11409  13126    185   -525    661       C  
ATOM    169  C   PRO A  25      47.796  -6.729   1.252  1.00 93.73           C  
ANISOU  169  C   PRO A  25    10886  11527  13200    178   -550    734       C  
ATOM    170  O   PRO A  25      47.505  -5.972   2.180  1.00 93.27           O  
ANISOU  170  O   PRO A  25    10869  11503  13066    163   -550    779       O  
ATOM    171  CB  PRO A  25      45.874  -8.232   0.656  1.00 94.01           C  
ANISOU  171  CB  PRO A  25    10872  11499  13347    174   -515    688       C  
ATOM    172  CG  PRO A  25      46.511  -9.450   0.070  1.00 93.13           C  
ANISOU  172  CG  PRO A  25    10707  11331  13347    188   -525    666       C  
ATOM    173  CD  PRO A  25      47.043  -9.004  -1.262  1.00 93.64           C  
ANISOU  173  CD  PRO A  25    10757  11422  13398    209   -526    584       C  
ATOM    174  N   ASP A  26      48.997  -7.292   1.107  1.00 91.36           N  
ANISOU  174  N   ASP A  26    10558  11199  12957    190   -572    741       N  
ATOM    175  CA  ASP A  26      50.099  -7.047   2.034  1.00 91.59           C  
ANISOU  175  CA  ASP A  26    10603  11234  12963    187   -601    804       C  
ATOM    176  C   ASP A  26      50.586  -5.605   1.967  1.00 88.18           C  
ANISOU  176  C   ASP A  26    10208  10864  12434    188   -604    789       C  
ATOM    177  O   ASP A  26      50.855  -5.071   0.890  1.00 81.21           O  
ANISOU  177  O   ASP A  26     9319  10002  11536    201   -594    725       O  
ATOM    178  CB  ASP A  26      51.264  -8.001   1.760  1.00 95.76           C  
ANISOU  178  CB  ASP A  26    11087  11714  13582    200   -624    806       C  
ATOM    179  CG  ASP A  26      52.275  -8.039   2.897  1.00 97.60           C  
ANISOU  179  CG  ASP A  26    11332  11943  13809    197   -657    882       C  
ATOM    180  OD1 ASP A  26      52.562  -6.987   3.514  1.00 98.43           O  
ANISOU  180  OD1 ASP A  26    11476  12095  13826    191   -667    907       O  
ATOM    181  OD2 ASP A  26      52.793  -9.139   3.171  1.00102.73           O  
ANISOU  181  OD2 ASP A  26    11949  12540  14544    202   -674    915       O  
ATOM    182  N   THR A  27      50.715  -5.005   3.145  1.00 88.93           N  
ANISOU  182  N   THR A  27    10339  10986  12464    174   -617    850       N  
ATOM    183  CA  THR A  27      51.062  -3.603   3.287  1.00 89.71           C  
ANISOU  183  CA  THR A  27    10474  11142  12470    172   -620    842       C  
ATOM    184  C   THR A  27      52.547  -3.340   3.024  1.00 89.27           C  
ANISOU  184  C   THR A  27    10404  11087  12426    185   -643    833       C  
ATOM    185  O   THR A  27      52.906  -2.307   2.454  1.00 85.71           O  
ANISOU  185  O   THR A  27     9966  10673  11927    191   -635    793       O  
ATOM    186  CB  THR A  27      50.641  -3.072   4.677  1.00 95.46           C  
ANISOU  186  CB  THR A  27    11244  11900  13127    153   -626    906       C  
ATOM    187  OG1 THR A  27      50.689  -1.643   4.677  1.00 97.77           O  
ANISOU  187  OG1 THR A  27    11570  12249  13330    149   -620    885       O  
ATOM    188  CG2 THR A  27      51.527  -3.631   5.812  1.00 94.59           C  
ANISOU  188  CG2 THR A  27    11132  11772  13038    152   -661    980       C  
ATOM    189  N   THR A  28      53.398  -4.278   3.438  1.00 89.37           N  
ANISOU  189  N   THR A  28    10391  11060  12506    190   -670    871       N  
ATOM    190  CA  THR A  28      54.843  -4.160   3.228  1.00 87.66           C  
ANISOU  190  CA  THR A  28    10156  10838  12313    203   -695    863       C  
ATOM    191  C   THR A  28      55.209  -4.360   1.754  1.00 82.36           C  
ANISOU  191  C   THR A  28     9451  10151  11693    220   -678    788       C  
ATOM    192  O   THR A  28      55.984  -3.578   1.199  1.00 81.22           O  
ANISOU  192  O   THR A  28     9307  10030  11523    228   -677    753       O  
ATOM    193  CB  THR A  28      55.658  -5.122   4.122  1.00 88.99           C  
ANISOU  193  CB  THR A  28    10304  10966  12541    205   -731    927       C  
ATOM    194  OG1 THR A  28      55.107  -6.438   4.029  1.00 96.15           O  
ANISOU  194  OG1 THR A  28    11183  11821  13530    206   -725    939       O  
ATOM    195  CG2 THR A  28      55.638  -4.679   5.582  1.00 86.85           C  
ANISOU  195  CG2 THR A  28    10070  10724  12203    192   -753    998       C  
ATOM    196  N   ILE A  29      54.644  -5.389   1.119  1.00 78.82           N  
ANISOU  196  N   ILE A  29     8970   9663  11314    225   -665    762       N  
ATOM    197  CA  ILE A  29      54.831  -5.588  -0.325  1.00 79.33           C  
ANISOU  197  CA  ILE A  29     9003   9718  11420    242   -647    685       C  
ATOM    198  C   ILE A  29      54.483  -4.308  -1.091  1.00 79.92           C  
ANISOU  198  C   ILE A  29     9106   9849  11412    246   -620    633       C  
ATOM    199  O   ILE A  29      55.176  -3.939  -2.041  1.00 79.76           O  
ANISOU  199  O   ILE A  29     9072   9840  11393    261   -612    585       O  
ATOM    200  CB  ILE A  29      54.062  -6.816  -0.870  1.00 76.90           C  
ANISOU  200  CB  ILE A  29     8660   9366  11194    246   -634    658       C  
ATOM    201  CG1 ILE A  29      54.774  -8.104  -0.443  1.00 78.41           C  
ANISOU  201  CG1 ILE A  29     8811   9495  11486    249   -659    695       C  
ATOM    202  CG2 ILE A  29      53.973  -6.776  -2.392  1.00 73.99           C  
ANISOU  202  CG2 ILE A  29     8267   9005  10841    264   -610    570       C  
ATOM    203  CD1 ILE A  29      53.987  -9.375  -0.693  1.00 84.20           C  
ANISOU  203  CD1 ILE A  29     9509  10177  12308    250   -648    684       C  
ATOM    204  N   GLN A  30      53.438  -3.619  -0.639  1.00 81.57           N  
ANISOU  204  N   GLN A  30     9353  10092  11549    233   -607    648       N  
ATOM    205  CA  GLN A  30      53.030  -2.346  -1.229  1.00 86.38           C  
ANISOU  205  CA  GLN A  30     9991  10753  12075    235   -583    608       C  
ATOM    206  C   GLN A  30      54.113  -1.274  -1.117  1.00 86.56           C  
ANISOU  206  C   GLN A  30    10031  10807  12051    238   -591    613       C  
ATOM    207  O   GLN A  30      54.463  -0.654  -2.126  1.00 83.66           O  
ANISOU  207  O   GLN A  30     9660  10460  11666    252   -573    564       O  
ATOM    208  CB  GLN A  30      51.709  -1.844  -0.621  1.00 88.37           C  
ANISOU  208  CB  GLN A  30    10280  11032  12265    219   -569    628       C  
ATOM    209  CG  GLN A  30      50.455  -2.490  -1.207  1.00 89.55           C  
ANISOU  209  CG  GLN A  30    10415  11166  12442    221   -549    593       C  
ATOM    210  CD  GLN A  30      49.227  -2.328  -0.321  1.00 86.93           C  
ANISOU  210  CD  GLN A  30    10112  10845  12071    201   -540    628       C  
ATOM    211  OE1 GLN A  30      48.884  -1.221   0.096  1.00 86.33           O  
ANISOU  211  OE1 GLN A  30    10074  10812  11914    192   -533    640       O  
ATOM    212  NE2 GLN A  30      48.558  -3.437  -0.036  1.00 84.58           N  
ANISOU  212  NE2 GLN A  30     9794  10507  11835    195   -539    644       N  
ATOM    213  N   ARG A  31      54.641  -1.065   0.094  1.00 89.14           N  
ANISOU  213  N   ARG A  31    10373  11136  12359    225   -617    672       N  
ATOM    214  CA  ARG A  31      55.623   0.007   0.329  1.00 90.92           C  
ANISOU  214  CA  ARG A  31    10614  11392  12541    225   -626    677       C  
ATOM    215  C   ARG A  31      56.889  -0.171  -0.505  1.00 87.61           C  
ANISOU  215  C   ARG A  31    10161  10954  12174    243   -629    644       C  
ATOM    216  O   ARG A  31      57.458   0.805  -1.004  1.00 84.37           O  
ANISOU  216  O   ARG A  31     9757  10570  11730    249   -617    616       O  
ATOM    217  CB  ARG A  31      55.956   0.182   1.820  1.00 97.16           C  
ANISOU  217  CB  ARG A  31    11424  12189  13304    210   -657    744       C  
ATOM    218  CG  ARG A  31      56.803  -0.915   2.464  1.00106.33           C  
ANISOU  218  CG  ARG A  31    12558  13307  14536    213   -693    787       C  
ATOM    219  CD  ARG A  31      57.218  -0.550   3.888  1.00113.71           C  
ANISOU  219  CD  ARG A  31    13515  14261  15430    202   -726    849       C  
ATOM    220  NE  ARG A  31      56.148   0.147   4.607  1.00118.09           N  
ANISOU  220  NE  ARG A  31    14111  14854  15903    185   -714    870       N  
ATOM    221  CZ  ARG A  31      55.220  -0.443   5.359  1.00120.19           C  
ANISOU  221  CZ  ARG A  31    14390  15112  16164    174   -714    914       C  
ATOM    222  NH1 ARG A  31      55.215  -1.758   5.526  1.00119.95           N  
ANISOU  222  NH1 ARG A  31    14336  15035  16206    178   -726    944       N  
ATOM    223  NH2 ARG A  31      54.290   0.291   5.954  1.00118.29           N  
ANISOU  223  NH2 ARG A  31    14188  14910  15848    159   -701    927       N  
ATOM    224  N   THR A  32      57.308  -1.420  -0.678  1.00 84.13           N  
ANISOU  224  N   THR A  32     9682  10466  11819    250   -644    645       N  
ATOM    225  CA  THR A  32      58.488  -1.690  -1.479  1.00 86.64           C  
ANISOU  225  CA  THR A  32     9963  10762  12193    267   -646    611       C  
ATOM    226  C   THR A  32      58.193  -1.687  -2.985  1.00 86.02           C  
ANISOU  226  C   THR A  32     9869  10689  12124    283   -611    539       C  
ATOM    227  O   THR A  32      59.073  -1.373  -3.782  1.00 90.88           O  
ANISOU  227  O   THR A  32    10469  11310  12752    297   -601    502       O  
ATOM    228  CB  THR A  32      59.268  -2.936  -0.996  1.00 89.28           C  
ANISOU  228  CB  THR A  32    10262  11044  12618    269   -680    643       C  
ATOM    229  OG1 THR A  32      58.383  -4.049  -0.872  1.00 88.08           O  
ANISOU  229  OG1 THR A  32    10096  10858  12511    266   -680    656       O  
ATOM    230  CG2 THR A  32      59.927  -2.658   0.369  1.00 88.13           C  
ANISOU  230  CG2 THR A  32    10132  10903  12452    259   -717    708       C  
ATOM    231  N   VAL A  33      56.958  -2.013  -3.370  1.00 83.22           N  
ANISOU  231  N   VAL A  33     9520  10339  11762    283   -593    518       N  
ATOM    232  CA  VAL A  33      56.506  -1.850  -4.762  1.00 79.19           C  
ANISOU  232  CA  VAL A  33     9002   9846  11242    300   -560    449       C  
ATOM    233  C   VAL A  33      56.473  -0.374  -5.189  1.00 78.26           C  
ANISOU  233  C   VAL A  33     8918   9782  11037    304   -535    429       C  
ATOM    234  O   VAL A  33      56.758  -0.039  -6.352  1.00 73.71           O  
ANISOU  234  O   VAL A  33     8332   9222  10452    322   -511    378       O  
ATOM    235  CB  VAL A  33      55.124  -2.495  -4.982  1.00 79.18           C  
ANISOU  235  CB  VAL A  33     8998   9837  11250    299   -549    431       C  
ATOM    236  CG1 VAL A  33      54.375  -1.827  -6.123  1.00 75.90           C  
ANISOU  236  CG1 VAL A  33     8595   9462  10782    313   -516    372       C  
ATOM    237  CG2 VAL A  33      55.269  -3.988  -5.232  1.00 77.97           C  
ANISOU  237  CG2 VAL A  33     8796   9629  11199    305   -560    418       C  
ATOM    238  N   GLN A  34      56.126   0.494  -4.240  1.00 81.05           N  
ANISOU  238  N   GLN A  34     9310  10162  11326    287   -541    471       N  
ATOM    239  CA  GLN A  34      56.130   1.942  -4.451  1.00 87.11           C  
ANISOU  239  CA  GLN A  34    10108  10975  12014    288   -520    461       C  
ATOM    240  C   GLN A  34      57.507   2.452  -4.848  1.00 85.99           C  
ANISOU  240  C   GLN A  34     9953  10835  11884    297   -517    448       C  
ATOM    241  O   GLN A  34      57.630   3.165  -5.847  1.00 82.66           O  
ANISOU  241  O   GLN A  34     9535  10438  11433    312   -487    409       O  
ATOM    242  CB  GLN A  34      55.645   2.684  -3.199  1.00 96.87           C  
ANISOU  242  CB  GLN A  34    11383  12234  13191    266   -532    510       C  
ATOM    243  CG  GLN A  34      54.136   2.874  -3.123  1.00111.36           C  
ANISOU  243  CG  GLN A  34    13243  14089  14979    258   -516    507       C  
ATOM    244  CD  GLN A  34      53.615   3.946  -4.074  1.00120.72           C  
ANISOU  244  CD  GLN A  34    14448  15315  16104    270   -483    465       C  
ATOM    245  OE1 GLN A  34      52.670   3.711  -4.838  1.00118.88           O  
ANISOU  245  OE1 GLN A  34    14213  15089  15866    280   -465    430       O  
ATOM    246  NE2 GLN A  34      54.229   5.131  -4.031  1.00121.67           N  
ANISOU  246  NE2 GLN A  34    14586  15463  16181    269   -474    469       N  
ATOM    247  N   GLN A  35      58.533   2.082  -4.073  1.00 83.58           N  
ANISOU  247  N   GLN A  35     9632  10503  11622    291   -547    482       N  
ATOM    248  CA  GLN A  35      59.905   2.496  -4.380  1.00 85.12           C  
ANISOU  248  CA  GLN A  35     9810  10695  11839    299   -547    470       C  
ATOM    249  C   GLN A  35      60.431   1.869  -5.682  1.00 79.77           C  
ANISOU  249  C   GLN A  35     9095   9997  11215    320   -528    418       C  
ATOM    250  O   GLN A  35      61.207   2.498  -6.408  1.00 77.21           O  
ANISOU  250  O   GLN A  35     8765   9686  10887    332   -506    390       O  
ATOM    251  CB  GLN A  35      60.872   2.276  -3.200  1.00 88.45           C  
ANISOU  251  CB  GLN A  35    10222  11094  12292    288   -587    517       C  
ATOM    252  CG  GLN A  35      60.927   0.859  -2.654  1.00100.59           C  
ANISOU  252  CG  GLN A  35    11734  12587  13899    285   -620    545       C  
ATOM    253  CD  GLN A  35      62.307   0.467  -2.136  1.00109.75           C  
ANISOU  253  CD  GLN A  35    12865  13716  15118    287   -654    567       C  
ATOM    254  OE1 GLN A  35      62.821   1.052  -1.177  1.00113.15           O  
ANISOU  254  OE1 GLN A  35    13309  14159  15523    277   -678    603       O  
ATOM    255  NE2 GLN A  35      62.908  -0.542  -2.765  1.00107.49           N  
ANISOU  255  NE2 GLN A  35    12537  13391  14914    300   -657    544       N  
ATOM    256  N   LYS A  36      59.980   0.654  -5.989  1.00 72.83           N  
ANISOU  256  N   LYS A  36     8192   9091  10390    326   -534    404       N  
ATOM    257  CA  LYS A  36      60.373  -0.014  -7.227  1.00 71.44           C  
ANISOU  257  CA  LYS A  36     7979   8898  10266    347   -516    349       C  
ATOM    258  C   LYS A  36      59.838   0.724  -8.450  1.00 72.58           C  
ANISOU  258  C   LYS A  36     8139   9085  10354    363   -474    298       C  
ATOM    259  O   LYS A  36      60.559   0.900  -9.433  1.00 73.25           O  
ANISOU  259  O   LYS A  36     8207   9176  10450    381   -452    259       O  
ATOM    260  CB  LYS A  36      59.952  -1.483  -7.213  1.00 72.08           C  
ANISOU  260  CB  LYS A  36     8029   8937  10420    348   -533    343       C  
ATOM    261  CG  LYS A  36      60.758  -2.308  -6.220  1.00 74.19           C  
ANISOU  261  CG  LYS A  36     8272   9158  10758    338   -573    389       C  
ATOM    262  CD  LYS A  36      60.122  -3.647  -5.889  1.00 77.94           C  
ANISOU  262  CD  LYS A  36     8725   9591  11297    334   -590    403       C  
ATOM    263  CE  LYS A  36      60.612  -4.749  -6.818  1.00 80.76           C  
ANISOU  263  CE  LYS A  36     9030   9910  11744    350   -587    354       C  
ATOM    264  NZ  LYS A  36      60.293  -6.105  -6.293  1.00 78.49           N  
ANISOU  264  NZ  LYS A  36     8715   9570  11539    344   -610    378       N  
ATOM    265  N   LEU A  37      58.584   1.173  -8.368  1.00 73.89           N  
ANISOU  265  N   LEU A  37     8337   9280  10458    358   -464    301       N  
ATOM    266  CA  LEU A  37      57.975   2.013  -9.400  1.00 72.33           C  
ANISOU  266  CA  LEU A  37     8160   9126  10195    374   -427    261       C  
ATOM    267  C   LEU A  37      58.595   3.401  -9.433  1.00 70.76           C  
ANISOU  267  C   LEU A  37     7985   8958   9942    374   -408    273       C  
ATOM    268  O   LEU A  37      58.791   3.974 -10.507  1.00 66.48           O  
ANISOU  268  O   LEU A  37     7446   8442   9373    394   -375    237       O  
ATOM    269  CB  LEU A  37      56.469   2.136  -9.164  1.00 76.13           C  
ANISOU  269  CB  LEU A  37     8669   9628  10629    367   -426    266       C  
ATOM    270  CG  LEU A  37      55.635   0.899  -9.481  1.00 77.55           C  
ANISOU  270  CG  LEU A  37     8824   9785  10856    372   -433    238       C  
ATOM    271  CD1 LEU A  37      54.329   0.969  -8.713  1.00 79.78           C  
ANISOU  271  CD1 LEU A  37     9133  10075  11105    355   -441    265       C  
ATOM    272  CD2 LEU A  37      55.388   0.774 -10.981  1.00 78.03           C  
ANISOU  272  CD2 LEU A  37     8870   9867  10911    401   -406    169       C  
ATOM    273  N   GLU A  38      58.879   3.933  -8.245  1.00 73.56           N  
ANISOU  273  N   GLU A  38     8358   9311  10281    353   -428    322       N  
ATOM    274  CA  GLU A  38      59.588   5.199  -8.075  1.00 80.42           C  
ANISOU  274  CA  GLU A  38     9244  10200  11112    350   -415    336       C  
ATOM    275  C   GLU A  38      60.811   5.306  -8.977  1.00 82.88           C  
ANISOU  275  C   GLU A  38     9529  10504  11457    367   -394    306       C  
ATOM    276  O   GLU A  38      61.022   6.330  -9.621  1.00 84.24           O  
ANISOU  276  O   GLU A  38     9714  10703  11589    377   -360    292       O  
ATOM    277  CB  GLU A  38      60.035   5.365  -6.618  1.00 88.36           C  
ANISOU  277  CB  GLU A  38    10257  11192  12125    327   -451    388       C  
ATOM    278  CG  GLU A  38      59.057   6.107  -5.726  1.00 96.24           C  
ANISOU  278  CG  GLU A  38    11294  12216  13056    309   -456    420       C  
ATOM    279  CD  GLU A  38      59.026   7.599  -6.017  1.00103.96           C  
ANISOU  279  CD  GLU A  38    12299  13231  13972    311   -426    413       C  
ATOM    280  OE1 GLU A  38      60.113   8.208  -6.154  1.00102.57           O  
ANISOU  280  OE1 GLU A  38    12113  13053  13807    314   -417    409       O  
ATOM    281  OE2 GLU A  38      57.913   8.163  -6.106  1.00106.51           O  
ANISOU  281  OE2 GLU A  38    12650  13582  14237    309   -409    410       O  
ATOM    282  N   GLN A  39      61.619   4.253  -9.017  1.00 82.53           N  
ANISOU  282  N   GLN A  39     9447  10422  11489    371   -413    299       N  
ATOM    283  CA  GLN A  39      62.816   4.280  -9.831  1.00 84.07           C  
ANISOU  283  CA  GLN A  39     9614  10608  11723    386   -393    269       C  
ATOM    284  C   GLN A  39      62.486   4.133 -11.313  1.00 80.16           C  
ANISOU  284  C   GLN A  39     9111  10132  11215    411   -354    215       C  
ATOM    285  O   GLN A  39      62.971   4.905 -12.143  1.00 81.05           O  
ANISOU  285  O   GLN A  39     9226  10266  11303    426   -317    194       O  
ATOM    286  CB  GLN A  39      63.813   3.215  -9.388  1.00 86.28           C  
ANISOU  286  CB  GLN A  39     9853  10839  12091    382   -426    277       C  
ATOM    287  CG  GLN A  39      65.222   3.774  -9.292  1.00 98.29           C  
ANISOU  287  CG  GLN A  39    11358  12349  13639    381   -423    282       C  
ATOM    288  CD  GLN A  39      66.251   2.939 -10.033  1.00102.16           C  
ANISOU  288  CD  GLN A  39    11801  12808  14207    396   -418    247       C  
ATOM    289  OE1 GLN A  39      66.374   1.727  -9.813  1.00101.86           O  
ANISOU  289  OE1 GLN A  39    11734  12733  14234    395   -446    246       O  
ATOM    290  NE2 GLN A  39      67.009   3.591 -10.915  1.00 99.38           N  
ANISOU  290  NE2 GLN A  39    11441  12468  13852    409   -379    217       N  
ATOM    291  N   LEU A  40      61.646   3.154 -11.629  1.00 74.29           N  
ANISOU  291  N   LEU A  40     8357   9382  10488    418   -362    192       N  
ATOM    292  CA  LEU A  40      61.333   2.828 -13.013  1.00 76.62           C  
ANISOU  292  CA  LEU A  40     8639   9696  10778    444   -332    135       C  
ATOM    293  C   LEU A  40      60.686   3.949 -13.828  1.00 78.46           C  
ANISOU  293  C   LEU A  40     8906   9981  10923    459   -293    118       C  
ATOM    294  O   LEU A  40      60.950   4.073 -15.022  1.00 74.90           O  
ANISOU  294  O   LEU A  40     8446   9551  10460    484   -259     76       O  
ATOM    295  CB  LEU A  40      60.459   1.585 -13.073  1.00 76.01           C  
ANISOU  295  CB  LEU A  40     8544   9600  10737    445   -352    114       C  
ATOM    296  CG  LEU A  40      61.206   0.265 -12.913  1.00 79.20           C  
ANISOU  296  CG  LEU A  40     8900   9951  11240    443   -377    105       C  
ATOM    297  CD1 LEU A  40      60.221  -0.833 -12.557  1.00 78.94           C  
ANISOU  297  CD1 LEU A  40     8855   9894  11243    437   -403    104       C  
ATOM    298  CD2 LEU A  40      61.976  -0.087 -14.181  1.00 79.50           C  
ANISOU  298  CD2 LEU A  40     8904   9990  11311    468   -351     47       C  
ATOM    299  N   ASN A  41      59.843   4.758 -13.193  1.00 83.62           N  
ANISOU  299  N   ASN A  41     9598  10657  11516    447   -296    150       N  
ATOM    300  CA  ASN A  41      59.080   5.784 -13.922  1.00 89.47           C  
ANISOU  300  CA  ASN A  41    10372  11447  12176    462   -262    137       C  
ATOM    301  C   ASN A  41      59.948   6.809 -14.653  1.00 86.94           C  
ANISOU  301  C   ASN A  41    10057  11147  11828    477   -222    131       C  
ATOM    302  O   ASN A  41      59.531   7.392 -15.659  1.00 91.40           O  
ANISOU  302  O   ASN A  41    10637  11751  12338    500   -187    108       O  
ATOM    303  CB  ASN A  41      58.075   6.486 -12.998  1.00 96.19           C  
ANISOU  303  CB  ASN A  41    11261  12313  12973    443   -275    175       C  
ATOM    304  CG  ASN A  41      58.732   7.453 -12.024  1.00104.18           C  
ANISOU  304  CG  ASN A  41    12289  13321  13974    422   -280    222       C  
ATOM    305  OD1 ASN A  41      59.938   7.396 -11.775  1.00111.74           O  
ANISOU  305  OD1 ASN A  41    13226  14253  14975    416   -285    231       O  
ATOM    306  ND2 ASN A  41      57.928   8.352 -11.464  1.00107.18           N  
ANISOU  306  ND2 ASN A  41    12705  13724  14296    410   -278    247       N  
ATOM    307  N   GLN A  42      61.154   7.015 -14.134  1.00 84.82           N  
ANISOU  307  N   GLN A  42     9774  10853  11600    464   -227    154       N  
ATOM    308  CA  GLN A  42      62.099   7.968 -14.695  1.00 83.10           C  
ANISOU  308  CA  GLN A  42     9557  10647  11369    475   -188    153       C  
ATOM    309  C   GLN A  42      62.760   7.441 -15.969  1.00 82.07           C  
ANISOU  309  C   GLN A  42     9397  10518  11266    502   -159    106       C  
ATOM    310  O   GLN A  42      63.497   8.167 -16.626  1.00 84.78           O  
ANISOU  310  O   GLN A  42     9741  10874  11598    514   -119    101       O  
ATOM    311  CB  GLN A  42      63.146   8.335 -13.642  1.00 85.94           C  
ANISOU  311  CB  GLN A  42     9908  10977  11768    452   -206    189       C  
ATOM    312  CG  GLN A  42      62.641   9.319 -12.591  1.00 88.55           C  
ANISOU  312  CG  GLN A  42    10273  11318  12053    430   -219    232       C  
ATOM    313  CD  GLN A  42      63.210   9.067 -11.203  1.00 85.06           C  
ANISOU  313  CD  GLN A  42     9820  10844  11655    403   -264    266       C  
ATOM    314  OE1 GLN A  42      62.966   8.025 -10.598  1.00 84.63           O  
ANISOU  314  OE1 GLN A  42     9754  10767  11635    394   -302    274       O  
ATOM    315  NE2 GLN A  42      63.959  10.033 -10.687  1.00 88.87           N  
ANISOU  315  NE2 GLN A  42    10306  11324  12137    392   -259    287       N  
ATOM    316  N   TYR A  43      62.481   6.183 -16.311  1.00 78.11           N  
ANISOU  316  N   TYR A  43     8870  10004  10803    510   -177     72       N  
ATOM    317  CA  TYR A  43      62.999   5.558 -17.525  1.00 79.80           C  
ANISOU  317  CA  TYR A  43     9055  10222  11044    536   -152     21       C  
ATOM    318  C   TYR A  43      61.930   5.533 -18.609  1.00 86.30           C  
ANISOU  318  C   TYR A  43     9892  11090  11807    563   -130    -19       C  
ATOM    319  O   TYR A  43      61.034   4.695 -18.574  1.00 89.32           O  
ANISOU  319  O   TYR A  43    10269  11471  12199    564   -155    -40       O  
ATOM    320  CB  TYR A  43      63.487   4.133 -17.241  1.00 76.32           C  
ANISOU  320  CB  TYR A  43     8570   9734  10695    528   -186      3       C  
ATOM    321  CG  TYR A  43      64.769   4.084 -16.447  1.00 78.09           C  
ANISOU  321  CG  TYR A  43     8772   9916  10984    510   -202     31       C  
ATOM    322  CD1 TYR A  43      64.751   4.153 -15.051  1.00 76.71           C  
ANISOU  322  CD1 TYR A  43     8606   9715  10825    481   -243     82       C  
ATOM    323  CD2 TYR A  43      66.008   3.980 -17.093  1.00 77.83           C  
ANISOU  323  CD2 TYR A  43     8707   9869  10995    521   -178      6       C  
ATOM    324  CE1 TYR A  43      65.929   4.120 -14.321  1.00 78.56           C  
ANISOU  324  CE1 TYR A  43     8819   9913  11117    467   -262    106       C  
ATOM    325  CE2 TYR A  43      67.192   3.945 -16.371  1.00 77.89           C  
ANISOU  325  CE2 TYR A  43     8692   9838  11067    505   -195     30       C  
ATOM    326  CZ  TYR A  43      67.145   4.015 -14.987  1.00 80.83           C  
ANISOU  326  CZ  TYR A  43     9074  10186  11453    478   -239     79       C  
ATOM    327  OH  TYR A  43      68.313   3.984 -14.261  1.00 85.25           O  
ANISOU  327  OH  TYR A  43     9610  10709  12073    464   -259    101       O  
ATOM    328  N   PRO A  44      62.022   6.451 -19.585  1.00 89.55           N  
ANISOU  328  N   PRO A  44    10322  11543  12159    587    -83    -29       N  
ATOM    329  CA  PRO A  44      61.025   6.557 -20.644  1.00 87.36           C  
ANISOU  329  CA  PRO A  44    10062  11316  11816    616    -62    -65       C  
ATOM    330  C   PRO A  44      60.605   5.222 -21.245  1.00 85.38           C  
ANISOU  330  C   PRO A  44     9780  11063  11597    631    -79   -123       C  
ATOM    331  O   PRO A  44      59.446   5.058 -21.598  1.00 92.15           O  
ANISOU  331  O   PRO A  44    10649  11949  12413    645    -87   -146       O  
ATOM    332  CB  PRO A  44      61.737   7.409 -21.690  1.00 90.46           C  
ANISOU  332  CB  PRO A  44    10461  11740  12169    642     -7    -72       C  
ATOM    333  CG  PRO A  44      62.565   8.326 -20.867  1.00 92.24           C  
ANISOU  333  CG  PRO A  44    10696  11942  12410    618      0    -20       C  
ATOM    334  CD  PRO A  44      63.086   7.456 -19.753  1.00 92.90           C  
ANISOU  334  CD  PRO A  44    10751  11969  12576    588    -46     -8       C  
ATOM    335  N   ASP A  45      61.527   4.276 -21.351  1.00 85.54           N  
ANISOU  335  N   ASP A  45     9758  11049  11695    630    -86   -148       N  
ATOM    336  CA  ASP A  45      61.210   2.976 -21.940  1.00 87.67           C  
ANISOU  336  CA  ASP A  45     9992  11313  12006    644   -101   -208       C  
ATOM    337  C   ASP A  45      60.154   2.228 -21.119  1.00 84.60           C  
ANISOU  337  C   ASP A  45     9601  10900  11643    626   -147   -202       C  
ATOM    338  O   ASP A  45      59.399   1.406 -21.647  1.00 84.85           O  
ANISOU  338  O   ASP A  45     9615  10941  11683    640   -158   -251       O  
ATOM    339  CB  ASP A  45      62.477   2.125 -22.075  1.00 89.78           C  
ANISOU  339  CB  ASP A  45    10211  11539  12361    642   -101   -231       C  
ATOM    340  CG  ASP A  45      62.357   1.057 -23.154  1.00 95.94           C  
ANISOU  340  CG  ASP A  45    10955  12330  13168    669    -96   -307       C  
ATOM    341  OD1 ASP A  45      62.093   1.414 -24.327  1.00 97.45           O  
ANISOU  341  OD1 ASP A  45    11157  12575  13296    701    -61   -345       O  
ATOM    342  OD2 ASP A  45      62.545  -0.140 -22.834  1.00100.60           O  
ANISOU  342  OD2 ASP A  45    11505  12875  13844    658   -126   -328       O  
ATOM    343  N   PHE A  46      60.116   2.520 -19.823  1.00 79.55           N  
ANISOU  343  N   PHE A  46     8978  10231  11016    594   -173   -143       N  
ATOM    344  CA  PHE A  46      59.187   1.897 -18.896  1.00 76.33           C  
ANISOU  344  CA  PHE A  46     8571   9798  10632    573   -214   -126       C  
ATOM    345  C   PHE A  46      57.763   2.227 -19.320  1.00 74.52           C  
ANISOU  345  C   PHE A  46     8369   9613  10333    587   -209   -145       C  
ATOM    346  O   PHE A  46      56.903   1.345 -19.389  1.00 70.00           O  
ANISOU  346  O   PHE A  46     7780   9032   9784    589   -230   -176       O  
ATOM    347  CB  PHE A  46      59.491   2.400 -17.484  1.00 79.34           C  
ANISOU  347  CB  PHE A  46     8971  10151  11022    540   -236    -56       C  
ATOM    348  CG  PHE A  46      58.532   1.934 -16.433  1.00 79.45           C  
ANISOU  348  CG  PHE A  46     8993  10143  11050    517   -273    -28       C  
ATOM    349  CD1 PHE A  46      58.390   0.581 -16.142  1.00 82.22           C  
ANISOU  349  CD1 PHE A  46     9309  10452  11479    510   -302    -42       C  
ATOM    350  CD2 PHE A  46      57.798   2.860 -15.698  1.00 79.90           C  
ANISOU  350  CD2 PHE A  46     9093  10220  11047    501   -277     16       C  
ATOM    351  CE1 PHE A  46      57.513   0.161 -15.150  1.00 81.00           C  
ANISOU  351  CE1 PHE A  46     9162  10276  11339    488   -333    -12       C  
ATOM    352  CE2 PHE A  46      56.925   2.448 -14.702  1.00 79.43           C  
ANISOU  352  CE2 PHE A  46     9041  10141  10998    479   -308     44       C  
ATOM    353  CZ  PHE A  46      56.782   1.095 -14.430  1.00 78.24           C  
ANISOU  353  CZ  PHE A  46     8855   9948  10923    473   -335     31       C  
ATOM    354  N   ASN A  47      57.535   3.496 -19.644  1.00 72.99           N  
ANISOU  354  N   ASN A  47     8215   9464  10055    597   -181   -128       N  
ATOM    355  CA  ASN A  47      56.245   3.934 -20.162  1.00 76.49           C  
ANISOU  355  CA  ASN A  47     8685   9953  10425    615   -174   -146       C  
ATOM    356  C   ASN A  47      55.775   3.115 -21.370  1.00 77.43           C  
ANISOU  356  C   ASN A  47     8778  10096  10546    647   -169   -221       C  
ATOM    357  O   ASN A  47      54.586   2.822 -21.493  1.00 81.29           O  
ANISOU  357  O   ASN A  47     9270  10600  11015    654   -184   -246       O  
ATOM    358  CB  ASN A  47      56.256   5.439 -20.457  1.00 78.35           C  
ANISOU  358  CB  ASN A  47     8961  10231  10575    625   -139   -117       C  
ATOM    359  CG  ASN A  47      56.534   6.278 -19.212  1.00 79.81           C  
ANISOU  359  CG  ASN A  47     9172  10395  10757    593   -147    -49       C  
ATOM    360  OD1 ASN A  47      57.355   7.194 -19.236  1.00 84.91           O  
ANISOU  360  OD1 ASN A  47     9830  11046  11385    592   -121    -22       O  
ATOM    361  ND2 ASN A  47      55.853   5.961 -18.117  1.00 79.27           N  
ANISOU  361  ND2 ASN A  47     9108  10301  10708    566   -182    -23       N  
ATOM    362  N   ASN A  48      56.703   2.721 -22.237  1.00 74.57           N  
ANISOU  362  N   ASN A  48     8387   9737  10208    667   -149   -259       N  
ATOM    363  CA  ASN A  48      56.364   1.855 -23.366  1.00 79.34           C  
ANISOU  363  CA  ASN A  48     8962  10363  10821    698   -146   -335       C  
ATOM    364  C   ASN A  48      55.777   0.521 -22.920  1.00 78.12           C  
ANISOU  364  C   ASN A  48     8771  10166  10743    684   -185   -364       C  
ATOM    365  O   ASN A  48      54.894  -0.036 -23.581  1.00 77.56           O  
ANISOU  365  O   ASN A  48     8686  10117  10665    704   -192   -421       O  
ATOM    366  CB  ASN A  48      57.588   1.600 -24.248  1.00 84.32           C  
ANISOU  366  CB  ASN A  48     9564  10997  11475    717   -117   -369       C  
ATOM    367  CG  ASN A  48      57.719   2.596 -25.379  1.00 86.37           C  
ANISOU  367  CG  ASN A  48     9851  11320  11646    752    -72   -381       C  
ATOM    368  OD1 ASN A  48      57.277   3.737 -25.280  1.00 88.70           O  
ANISOU  368  OD1 ASN A  48    10189  11646  11867    754    -57   -341       O  
ATOM    369  ND2 ASN A  48      58.332   2.162 -26.469  1.00 93.16           N  
ANISOU  369  ND2 ASN A  48    10683  12200  12512    780    -47   -435       N  
ATOM    370  N   TYR A  49      56.291   0.013 -21.802  1.00 76.67           N  
ANISOU  370  N   TYR A  49     8573   9924  10636    651   -210   -324       N  
ATOM    371  CA  TYR A  49      55.829  -1.248 -21.243  1.00 75.08           C  
ANISOU  371  CA  TYR A  49     8337   9675  10517    634   -245   -339       C  
ATOM    372  C   TYR A  49      54.422  -1.062 -20.680  1.00 72.90           C  
ANISOU  372  C   TYR A  49     8086   9406  10206    623   -264   -322       C  
ATOM    373  O   TYR A  49      53.550  -1.912 -20.884  1.00 68.76           O  
ANISOU  373  O   TYR A  49     7538   8874   9714    629   -280   -365       O  
ATOM    374  CB  TYR A  49      56.816  -1.779 -20.184  1.00 77.49           C  
ANISOU  374  CB  TYR A  49     8621   9916  10907    604   -266   -293       C  
ATOM    375  CG  TYR A  49      57.904  -2.678 -20.756  1.00 79.64           C  
ANISOU  375  CG  TYR A  49     8844  10160  11255    615   -261   -336       C  
ATOM    376  CD1 TYR A  49      57.674  -4.046 -20.946  1.00 82.09           C  
ANISOU  376  CD1 TYR A  49     9106  10436  11649    618   -281   -385       C  
ATOM    377  CD2 TYR A  49      59.153  -2.168 -21.121  1.00 80.30           C  
ANISOU  377  CD2 TYR A  49     8926  10251  11332    622   -236   -329       C  
ATOM    378  CE1 TYR A  49      58.649  -4.880 -21.482  1.00 81.68           C  
ANISOU  378  CE1 TYR A  49     9005  10358  11670    628   -276   -427       C  
ATOM    379  CE2 TYR A  49      60.138  -2.998 -21.657  1.00 80.51           C  
ANISOU  379  CE2 TYR A  49     8906  10253  11431    632   -230   -371       C  
ATOM    380  CZ  TYR A  49      59.879  -4.353 -21.839  1.00 82.61           C  
ANISOU  380  CZ  TYR A  49     9124  10486  11778    635   -251   -421       C  
ATOM    381  OH  TYR A  49      60.839  -5.195 -22.371  1.00 84.82           O  
ANISOU  381  OH  TYR A  49     9355  10739  12133    644   -246   -465       O  
ATOM    382  N   LEU A  50      54.211   0.076 -20.017  1.00 67.72           N  
ANISOU  382  N   LEU A  50     7476   8766   9488    609   -259   -262       N  
ATOM    383  CA  LEU A  50      52.938   0.403 -19.385  1.00 68.78           C  
ANISOU  383  CA  LEU A  50     7638   8908   9586    595   -274   -238       C  
ATOM    384  C   LEU A  50      51.778   0.454 -20.381  1.00 68.96           C  
ANISOU  384  C   LEU A  50     7665   8978   9558    625   -267   -297       C  
ATOM    385  O   LEU A  50      50.775  -0.232 -20.189  1.00 68.45           O  
ANISOU  385  O   LEU A  50     7587   8901   9522    620   -287   -320       O  
ATOM    386  CB  LEU A  50      53.033   1.704 -18.575  1.00 64.11           C  
ANISOU  386  CB  LEU A  50     7094   8329   8935    576   -266   -168       C  
ATOM    387  CG  LEU A  50      53.822   1.642 -17.259  1.00 63.92           C  
ANISOU  387  CG  LEU A  50     7070   8257   8959    541   -284   -105       C  
ATOM    388  CD1 LEU A  50      54.026   3.028 -16.660  1.00 62.18           C  
ANISOU  388  CD1 LEU A  50     6894   8057   8676    528   -272    -48       C  
ATOM    389  CD2 LEU A  50      53.194   0.708 -16.231  1.00 61.29           C  
ANISOU  389  CD2 LEU A  50     6723   7880   8685    516   -318    -85       C  
ATOM    390  N   ILE A  51      51.926   1.230 -21.452  1.00 68.11           N  
ANISOU  390  N   ILE A  51     7574   8925   9378    656   -238   -321       N  
ATOM    391  CA  ILE A  51      50.897   1.274 -22.484  1.00 68.76           C  
ANISOU  391  CA  ILE A  51     7659   9058   9408    690   -232   -380       C  
ATOM    392  C   ILE A  51      50.690  -0.093 -23.130  1.00 68.80           C  
ANISOU  392  C   ILE A  51     7613   9050   9478    705   -247   -457       C  
ATOM    393  O   ILE A  51      49.557  -0.472 -23.418  1.00 75.66           O  
ANISOU  393  O   ILE A  51     8473   9933  10342    716   -262   -500       O  
ATOM    394  CB  ILE A  51      51.143   2.379 -23.543  1.00 70.48           C  
ANISOU  394  CB  ILE A  51     7906   9340   9533    724   -197   -387       C  
ATOM    395  CG1 ILE A  51      49.967   2.470 -24.521  1.00 75.32           C  
ANISOU  395  CG1 ILE A  51     8525  10009  10085    760   -197   -443       C  
ATOM    396  CG2 ILE A  51      52.421   2.134 -24.320  1.00 72.99           C  
ANISOU  396  CG2 ILE A  51     8201   9662   9870    742   -173   -412       C  
ATOM    397  CD1 ILE A  51      48.665   2.916 -23.891  1.00 74.03           C  
ANISOU  397  CD1 ILE A  51     8388   9850   9889    747   -215   -420       C  
ATOM    398  N   PHE A  52      51.772  -0.840 -23.324  1.00 68.87           N  
ANISOU  398  N   PHE A  52     7586   9029   9552    705   -244   -475       N  
ATOM    399  CA  PHE A  52      51.688  -2.170 -23.941  1.00 68.82           C  
ANISOU  399  CA  PHE A  52     7526   9006   9617    719   -257   -551       C  
ATOM    400  C   PHE A  52      50.770  -3.126 -23.167  1.00 67.81           C  
ANISOU  400  C   PHE A  52     7373   8830   9562    696   -290   -557       C  
ATOM    401  O   PHE A  52      49.982  -3.862 -23.764  1.00 70.30           O  
ANISOU  401  O   PHE A  52     7658   9153   9899    713   -301   -626       O  
ATOM    402  CB  PHE A  52      53.090  -2.789 -24.123  1.00 67.09           C  
ANISOU  402  CB  PHE A  52     7271   8755   9465    718   -249   -562       C  
ATOM    403  CG  PHE A  52      53.073  -4.145 -24.791  1.00 66.59           C  
ANISOU  403  CG  PHE A  52     7149   8674   9479    733   -260   -644       C  
ATOM    404  CD1 PHE A  52      53.205  -4.259 -26.178  1.00 67.26           C  
ANISOU  404  CD1 PHE A  52     7217   8809   9530    773   -240   -720       C  
ATOM    405  CD2 PHE A  52      52.909  -5.312 -24.039  1.00 64.13           C  
ANISOU  405  CD2 PHE A  52     6798   8295   9273    708   -289   -645       C  
ATOM    406  CE1 PHE A  52      53.183  -5.510 -26.800  1.00 67.00           C  
ANISOU  406  CE1 PHE A  52     7126   8760   9570    787   -250   -802       C  
ATOM    407  CE2 PHE A  52      52.877  -6.561 -24.654  1.00 65.03           C  
ANISOU  407  CE2 PHE A  52     6855   8389   9466    722   -298   -724       C  
ATOM    408  CZ  PHE A  52      53.017  -6.663 -26.037  1.00 65.28           C  
ANISOU  408  CZ  PHE A  52     6868   8472   9465    761   -280   -805       C  
ATOM    409  N   VAL A  53      50.899  -3.127 -21.844  1.00 66.64           N  
ANISOU  409  N   VAL A  53     7237   8633   9452    658   -305   -485       N  
ATOM    410  CA  VAL A  53      50.080  -3.961 -20.965  1.00 66.16           C  
ANISOU  410  CA  VAL A  53     7156   8522   9459    633   -333   -475       C  
ATOM    411  C   VAL A  53      48.614  -3.523 -21.029  1.00 68.76           C  
ANISOU  411  C   VAL A  53     7510   8885   9732    639   -337   -489       C  
ATOM    412  O   VAL A  53      47.701  -4.351 -20.996  1.00 65.85           O  
ANISOU  412  O   VAL A  53     7112   8495   9412    637   -354   -527       O  
ATOM    413  CB  VAL A  53      50.553  -3.863 -19.497  1.00 66.95           C  
ANISOU  413  CB  VAL A  53     7272   8572   9593    592   -345   -386       C  
ATOM    414  CG1 VAL A  53      49.752  -4.797 -18.600  1.00 67.22           C  
ANISOU  414  CG1 VAL A  53     7286   8553   9702    567   -370   -373       C  
ATOM    415  CG2 VAL A  53      52.039  -4.171 -19.383  1.00 70.74           C  
ANISOU  415  CG2 VAL A  53     7733   9021  10126    587   -343   -368       C  
ATOM    416  N   LEU A  54      48.398  -2.215 -21.108  1.00 68.20           N  
ANISOU  416  N   LEU A  54     7488   8864   9561    645   -322   -458       N  
ATOM    417  CA  LEU A  54      47.057  -1.691 -21.185  1.00 69.97           C  
ANISOU  417  CA  LEU A  54     7736   9121   9727    652   -325   -468       C  
ATOM    418  C   LEU A  54      46.363  -2.164 -22.457  1.00 73.01           C  
ANISOU  418  C   LEU A  54     8095   9545  10103    691   -327   -561       C  
ATOM    419  O   LEU A  54      45.334  -2.830 -22.393  1.00 73.43           O  
ANISOU  419  O   LEU A  54     8124   9583  10193    689   -345   -599       O  
ATOM    420  CB  LEU A  54      47.078  -0.165 -21.121  1.00 66.62           C  
ANISOU  420  CB  LEU A  54     7369   8744   9200    656   -306   -418       C  
ATOM    421  CG  LEU A  54      45.729   0.526 -21.328  1.00 63.80           C  
ANISOU  421  CG  LEU A  54     7040   8429   8773    668   -307   -430       C  
ATOM    422  CD1 LEU A  54      44.706   0.074 -20.291  1.00 64.24           C  
ANISOU  422  CD1 LEU A  54     7091   8445   8873    637   -329   -412       C  
ATOM    423  CD2 LEU A  54      45.896   2.037 -21.312  1.00 58.27           C  
ANISOU  423  CD2 LEU A  54     6392   7771   7979    672   -286   -380       C  
ATOM    424  N   THR A  55      46.956  -1.846 -23.603  1.00 75.29           N  
ANISOU  424  N   THR A  55     8383   9880  10342    726   -308   -600       N  
ATOM    425  CA  THR A  55      46.274  -1.982 -24.880  1.00 75.85           C  
ANISOU  425  CA  THR A  55     8440  10006  10375    768   -307   -683       C  
ATOM    426  C   THR A  55      46.514  -3.311 -25.577  1.00 77.90           C  
ANISOU  426  C   THR A  55     8639  10247  10711    784   -316   -766       C  
ATOM    427  O   THR A  55      45.618  -3.826 -26.243  1.00 82.70           O  
ANISOU  427  O   THR A  55     9221  10877  11325    807   -330   -840       O  
ATOM    428  CB  THR A  55      46.675  -0.859 -25.841  1.00 77.25           C  
ANISOU  428  CB  THR A  55     8653  10253  10445    803   -278   -683       C  
ATOM    429  OG1 THR A  55      48.054  -1.011 -26.190  1.00 78.83           O  
ANISOU  429  OG1 THR A  55     8841  10448  10665    808   -259   -681       O  
ATOM    430  CG2 THR A  55      46.458   0.500 -25.194  1.00 76.67           C  
ANISOU  430  CG2 THR A  55     8636  10196  10298    788   -267   -604       C  
ATOM    431  N   LYS A  56      47.715  -3.858 -25.437  1.00 78.30           N  
ANISOU  431  N   LYS A  56     8665  10260  10824    772   -310   -756       N  
ATOM    432  CA  LYS A  56      48.076  -5.069 -26.160  1.00 79.35           C  
ANISOU  432  CA  LYS A  56     8740  10378  11032    789   -316   -835       C  
ATOM    433  C   LYS A  56      47.848  -6.356 -25.371  1.00 80.98           C  
ANISOU  433  C   LYS A  56     8899  10506  11364    759   -341   -843       C  
ATOM    434  O   LYS A  56      47.346  -7.334 -25.923  1.00 84.27           O  
ANISOU  434  O   LYS A  56     9267  10915  11836    774   -354   -923       O  
ATOM    435  CB  LYS A  56      49.518  -4.982 -26.680  1.00 81.82           C  
ANISOU  435  CB  LYS A  56     9046  10699  11342    800   -291   -835       C  
ATOM    436  CG  LYS A  56      49.671  -4.203 -27.982  1.00 83.80           C  
ANISOU  436  CG  LYS A  56     9319  11032  11489    845   -265   -873       C  
ATOM    437  CD  LYS A  56      49.251  -5.056 -29.174  1.00 89.31           C  
ANISOU  437  CD  LYS A  56     9971  11762  12199    882   -271   -984       C  
ATOM    438  CE  LYS A  56      49.084  -4.245 -30.453  1.00 93.93           C  
ANISOU  438  CE  LYS A  56    10583  12439  12667    931   -249  -1022       C  
ATOM    439  NZ  LYS A  56      50.382  -3.873 -31.082  1.00 94.51           N  
ANISOU  439  NZ  LYS A  56    10664  12538  12708    947   -214  -1015       N  
ATOM    440  N   LEU A  57      48.196  -6.362 -24.090  1.00 81.62           N  
ANISOU  440  N   LEU A  57     8992  10530  11489    719   -348   -761       N  
ATOM    441  CA  LEU A  57      48.169  -7.606 -23.320  1.00 83.62           C  
ANISOU  441  CA  LEU A  57     9200  10705  11866    692   -368   -758       C  
ATOM    442  C   LEU A  57      46.783  -8.149 -22.987  1.00 84.61           C  
ANISOU  442  C   LEU A  57     9309  10810  12030    683   -387   -781       C  
ATOM    443  O   LEU A  57      46.301  -8.023 -21.854  1.00 84.36           O  
ANISOU  443  O   LEU A  57     9297  10744  12013    651   -396   -716       O  
ATOM    444  CB  LEU A  57      49.017  -7.497 -22.054  1.00 84.50           C  
ANISOU  444  CB  LEU A  57     9328  10764  12014    654   -371   -662       C  
ATOM    445  CG  LEU A  57      50.383  -8.175 -22.121  1.00 89.31           C  
ANISOU  445  CG  LEU A  57     9902  11334  12697    651   -369   -665       C  
ATOM    446  CD1 LEU A  57      51.117  -7.957 -20.808  1.00 87.94           C  
ANISOU  446  CD1 LEU A  57     9750  11115  12549    616   -376   -567       C  
ATOM    447  CD2 LEU A  57      50.250  -9.665 -22.428  1.00 88.30           C  
ANISOU  447  CD2 LEU A  57     9706  11159  12686    655   -383   -733       C  
ATOM    448  N   LYS A  58      46.167  -8.787 -23.976  1.00 88.66           N  
ANISOU  448  N   LYS A  58     9782  11343  12564    711   -393   -878       N  
ATOM    449  CA  LYS A  58      44.863  -9.428 -23.812  1.00 90.08           C  
ANISOU  449  CA  LYS A  58     9933  11499  12792    706   -411   -917       C  
ATOM    450  C   LYS A  58      44.841 -10.447 -22.674  1.00 90.27           C  
ANISOU  450  C   LYS A  58     9926  11434  12940    668   -424   -877       C  
ATOM    451  O   LYS A  58      43.824 -10.613 -22.003  1.00 87.91           O  
ANISOU  451  O   LYS A  58     9627  11108  12667    649   -433   -859       O  
ATOM    452  CB  LYS A  58      44.431 -10.087 -25.123  1.00 93.08           C  
ANISOU  452  CB  LYS A  58    10266  11911  13190    745   -416  -1037       C  
ATOM    453  CG  LYS A  58      43.360  -9.322 -25.892  1.00 96.30           C  
ANISOU  453  CG  LYS A  58    10699  12395  13497    776   -418  -1083       C  
ATOM    454  CD  LYS A  58      43.821  -7.953 -26.374  1.00 95.37           C  
ANISOU  454  CD  LYS A  58    10641  12351  13246    797   -398  -1050       C  
ATOM    455  CE  LYS A  58      42.629  -7.109 -26.801  1.00 97.27           C  
ANISOU  455  CE  LYS A  58    10913  12654  13390    820   -403  -1070       C  
ATOM    456  NZ  LYS A  58      43.042  -5.878 -27.525  1.00 95.35           N  
ANISOU  456  NZ  LYS A  58    10720  12489  13021    850   -382  -1053       N  
ATOM    457  N   SER A  59      45.978 -11.104 -22.457  1.00 93.77           N  
ANISOU  457  N   SER A  59    10340  11830  13456    657   -423   -860       N  
ATOM    458  CA  SER A  59      46.124 -12.152 -21.445  1.00 94.62           C  
ANISOU  458  CA  SER A  59    10414  11850  13688    624   -435   -821       C  
ATOM    459  C   SER A  59      45.712 -11.662 -20.067  1.00 90.66           C  
ANISOU  459  C   SER A  59     9956  11323  13168    589   -438   -719       C  
ATOM    460  O   SER A  59      45.040 -12.376 -19.322  1.00 89.81           O  
ANISOU  460  O   SER A  59     9826  11160  13138    566   -447   -701       O  
ATOM    461  CB  SER A  59      47.581 -12.643 -21.373  1.00 98.46           C  
ANISOU  461  CB  SER A  59    10876  12299  14234    620   -433   -803       C  
ATOM    462  OG  SER A  59      48.253 -12.521 -22.619  1.00103.35           O  
ANISOU  462  OG  SER A  59    11482  12967  14818    654   -421   -873       O  
ATOM    463  N   GLU A  60      46.118 -10.440 -19.741  1.00 87.98           N  
ANISOU  463  N   GLU A  60     9677  11024  12729    584   -429   -655       N  
ATOM    464  CA  GLU A  60      45.988  -9.928 -18.386  1.00 87.08           C  
ANISOU  464  CA  GLU A  60     9604  10886  12594    549   -431   -554       C  
ATOM    465  C   GLU A  60      44.563  -9.504 -18.064  1.00 87.02           C  
ANISOU  465  C   GLU A  60     9621  10896  12545    542   -432   -549       C  
ATOM    466  O   GLU A  60      43.819  -9.077 -18.951  1.00 86.28           O  
ANISOU  466  O   GLU A  60     9534  10857  12393    568   -428   -611       O  
ATOM    467  CB  GLU A  60      46.975  -8.784 -18.152  1.00 88.54           C  
ANISOU  467  CB  GLU A  60     9842  11107  12694    547   -422   -491       C  
ATOM    468  CG  GLU A  60      48.433  -9.233 -18.145  1.00 93.62           C  
ANISOU  468  CG  GLU A  60    10461  11718  13391    545   -423   -477       C  
ATOM    469  CD  GLU A  60      48.733 -10.292 -17.087  1.00 98.34           C  
ANISOU  469  CD  GLU A  60    11028  12235  14101    517   -439   -429       C  
ATOM    470  OE1 GLU A  60      48.267 -10.147 -15.932  1.00100.15           O  
ANISOU  470  OE1 GLU A  60    11283  12441  14330    489   -446   -358       O  
ATOM    471  OE2 GLU A  60      49.438 -11.275 -17.409  1.00 98.40           O  
ANISOU  471  OE2 GLU A  60    10986  12204  14199    523   -444   -462       O  
ATOM    472  N   ASP A  61      44.190  -9.642 -16.792  1.00 83.40           N  
ANISOU  472  N   ASP A  61     9176  10394  12119    508   -437   -476       N  
ATOM    473  CA  ASP A  61      42.855  -9.284 -16.343  1.00 79.40           C  
ANISOU  473  CA  ASP A  61     8691   9896  11581    497   -436   -464       C  
ATOM    474  C   ASP A  61      42.694  -7.771 -16.380  1.00 79.76           C  
ANISOU  474  C   ASP A  61     8800  10011  11496    502   -427   -435       C  
ATOM    475  O   ASP A  61      43.671  -7.033 -16.570  1.00 80.98           O  
ANISOU  475  O   ASP A  61     8982  10196  11591    510   -421   -411       O  
ATOM    476  CB  ASP A  61      42.561  -9.858 -14.949  1.00 79.62           C  
ANISOU  476  CB  ASP A  61     8716   9859  11678    459   -441   -390       C  
ATOM    477  CG  ASP A  61      43.368  -9.185 -13.844  1.00 82.20           C  
ANISOU  477  CG  ASP A  61     9089  10181  11961    435   -441   -288       C  
ATOM    478  OD1 ASP A  61      43.607  -7.968 -13.925  1.00 82.91           O  
ANISOU  478  OD1 ASP A  61     9227  10326  11948    440   -434   -266       O  
ATOM    479  OD2 ASP A  61      43.750  -9.871 -12.874  1.00 82.76           O  
ANISOU  479  OD2 ASP A  61     9147  10195  12102    411   -447   -229       O  
ATOM    480  N   GLU A  62      41.464  -7.313 -16.194  1.00 77.16           N  
ANISOU  480  N   GLU A  62     8491   9701  11126    498   -425   -438       N  
ATOM    481  CA  GLU A  62      41.145  -5.902 -16.367  1.00 76.24           C  
ANISOU  481  CA  GLU A  62     8429   9650  10891    507   -416   -423       C  
ATOM    482  C   GLU A  62      41.748  -4.951 -15.334  1.00 72.99           C  
ANISOU  482  C   GLU A  62     8069   9243  10421    482   -411   -328       C  
ATOM    483  O   GLU A  62      42.267  -3.908 -15.724  1.00 74.91           O  
ANISOU  483  O   GLU A  62     8347   9534  10580    496   -401   -317       O  
ATOM    484  CB  GLU A  62      39.639  -5.693 -16.476  1.00 78.89           C  
ANISOU  484  CB  GLU A  62     8767  10003  11204    511   -417   -457       C  
ATOM    485  CG  GLU A  62      39.074  -6.118 -17.816  1.00 81.98           C  
ANISOU  485  CG  GLU A  62     9121  10423  11605    548   -423   -562       C  
ATOM    486  CD  GLU A  62      37.577  -6.308 -17.767  1.00 83.56           C  
ANISOU  486  CD  GLU A  62     9307  10619  11822    546   -428   -600       C  
ATOM    487  OE1 GLU A  62      37.127  -7.338 -17.211  1.00 84.32           O  
ANISOU  487  OE1 GLU A  62     9365  10654  12018    525   -432   -602       O  
ATOM    488  OE2 GLU A  62      36.857  -5.425 -18.283  1.00 81.70           O  
ANISOU  488  OE2 GLU A  62     9098  10440  11505    565   -427   -625       O  
ATOM    489  N   PRO A  63      41.674  -5.284 -14.025  1.00 72.18           N  
ANISOU  489  N   PRO A  63     7972   9091  10362    447   -415   -258       N  
ATOM    490  CA  PRO A  63      42.282  -4.346 -13.079  1.00 71.02           C  
ANISOU  490  CA  PRO A  63     7873   8954  10156    426   -411   -174       C  
ATOM    491  C   PRO A  63      43.799  -4.214 -13.250  1.00 73.31           C  
ANISOU  491  C   PRO A  63     8165   9246  10443    432   -412   -154       C  
ATOM    492  O   PRO A  63      44.359  -3.183 -12.890  1.00 74.15           O  
ANISOU  492  O   PRO A  63     8312   9380  10481    426   -407   -107       O  
ATOM    493  CB  PRO A  63      41.934  -4.931 -11.701  1.00 72.81           C  
ANISOU  493  CB  PRO A  63     8098   9128  10439    390   -417   -110       C  
ATOM    494  CG  PRO A  63      41.415  -6.303 -11.949  1.00 72.90           C  
ANISOU  494  CG  PRO A  63     8054   9089  10554    392   -423   -156       C  
ATOM    495  CD  PRO A  63      40.881  -6.323 -13.341  1.00 72.55           C  
ANISOU  495  CD  PRO A  63     7988   9081  10497    425   -420   -252       C  
ATOM    496  N   THR A  64      44.442  -5.236 -13.812  1.00 72.01           N  
ANISOU  496  N   THR A  64     7954   9052  10355    444   -418   -194       N  
ATOM    497  CA  THR A  64      45.878  -5.202 -14.078  1.00 70.00           C  
ANISOU  497  CA  THR A  64     7694   8796  10107    453   -418   -185       C  
ATOM    498  C   THR A  64      46.187  -4.313 -15.276  1.00 69.21           C  
ANISOU  498  C   THR A  64     7610   8759   9927    484   -403   -231       C  
ATOM    499  O   THR A  64      47.043  -3.427 -15.181  1.00 66.52           O  
ANISOU  499  O   THR A  64     7300   8442   9533    484   -394   -194       O  
ATOM    500  CB  THR A  64      46.453  -6.615 -14.288  1.00 70.39           C  
ANISOU  500  CB  THR A  64     7685   8790  10269    455   -428   -214       C  
ATOM    501  OG1 THR A  64      46.185  -7.400 -13.124  1.00 72.37           O  
ANISOU  501  OG1 THR A  64     7924   8982  10593    426   -441   -161       O  
ATOM    502  CG2 THR A  64      47.963  -6.574 -14.517  1.00 68.63           C  
ANISOU  502  CG2 THR A  64     7455   8564  10056    462   -428   -203       C  
ATOM    503  N   ARG A  65      45.488  -4.543 -16.387  1.00 68.33           N  
ANISOU  503  N   ARG A  65     7478   8674   9809    512   -399   -310       N  
ATOM    504  CA  ARG A  65      45.638  -3.709 -17.587  1.00 68.74           C  
ANISOU  504  CA  ARG A  65     7547   8792   9779    546   -383   -355       C  
ATOM    505  C   ARG A  65      45.370  -2.231 -17.304  1.00 67.62           C  
ANISOU  505  C   ARG A  65     7464   8697   9533    543   -371   -309       C  
ATOM    506  O   ARG A  65      46.072  -1.354 -17.806  1.00 71.70           O  
ANISOU  506  O   ARG A  65     8005   9252   9986    559   -355   -302       O  
ATOM    507  CB  ARG A  65      44.711  -4.192 -18.704  1.00 70.50           C  
ANISOU  507  CB  ARG A  65     7740   9039  10007    576   -385   -447       C  
ATOM    508  CG  ARG A  65      45.191  -5.421 -19.451  1.00 73.63           C  
ANISOU  508  CG  ARG A  65     8079   9411  10488    593   -391   -514       C  
ATOM    509  CD  ARG A  65      44.052  -6.180 -20.112  1.00 78.30           C  
ANISOU  509  CD  ARG A  65     8631  10003  11115    610   -400   -597       C  
ATOM    510  NE  ARG A  65      43.235  -5.379 -21.031  1.00 84.51           N  
ANISOU  510  NE  ARG A  65     9439  10860  11809    642   -395   -644       N  
ATOM    511  CZ  ARG A  65      43.491  -5.202 -22.327  1.00 86.55           C  
ANISOU  511  CZ  ARG A  65     9691  11173  12022    682   -387   -710       C  
ATOM    512  NH1 ARG A  65      44.569  -5.747 -22.872  1.00 95.90           N  
ANISOU  512  NH1 ARG A  65    10846  12349  13243    694   -381   -738       N  
ATOM    513  NH2 ARG A  65      42.679  -4.466 -23.083  1.00 82.64           N  
ANISOU  513  NH2 ARG A  65     9217  10741  11441    710   -384   -746       N  
ATOM    514  N   SER A  66      44.366  -1.961 -16.480  1.00 63.98           N  
ANISOU  514  N   SER A  66     7023   8228   9057    522   -377   -276       N  
ATOM    515  CA  SER A  66      43.940  -0.594 -16.230  1.00 62.31           C  
ANISOU  515  CA  SER A  66     6864   8060   8751    519   -366   -240       C  
ATOM    516  C   SER A  66      44.882   0.132 -15.288  1.00 61.36           C  
ANISOU  516  C   SER A  66     6775   7931   8607    495   -362   -161       C  
ATOM    517  O   SER A  66      45.124   1.328 -15.443  1.00 61.84           O  
ANISOU  517  O   SER A  66     6873   8032   8592    502   -347   -140       O  
ATOM    518  CB  SER A  66      42.522  -0.583 -15.660  1.00 62.89           C  
ANISOU  518  CB  SER A  66     6945   8128   8821    504   -373   -236       C  
ATOM    519  OG  SER A  66      42.231   0.644 -15.010  1.00 64.95           O  
ANISOU  519  OG  SER A  66     7255   8414   9008    490   -365   -183       O  
ATOM    520  N   LEU A  67      45.387  -0.594 -14.299  1.00 59.07           N  
ANISOU  520  N   LEU A  67     6470   7588   8384    467   -375   -119       N  
ATOM    521  CA  LEU A  67      46.316  -0.041 -13.340  1.00 60.09           C  
ANISOU  521  CA  LEU A  67     6625   7707   8501    445   -376    -47       C  
ATOM    522  C   LEU A  67      47.616   0.367 -14.030  1.00 61.26           C  
ANISOU  522  C   LEU A  67     6772   7872   8631    463   -365    -55       C  
ATOM    523  O   LEU A  67      48.162   1.433 -13.759  1.00 60.16           O  
ANISOU  523  O   LEU A  67     6666   7755   8438    458   -355    -16       O  
ATOM    524  CB  LEU A  67      46.595  -1.045 -12.225  1.00 58.42           C  
ANISOU  524  CB  LEU A  67     6393   7434   8370    416   -396     -4       C  
ATOM    525  CG  LEU A  67      47.640  -0.599 -11.209  1.00 57.94           C  
ANISOU  525  CG  LEU A  67     6352   7360   8301    395   -402     67       C  
ATOM    526  CD1 LEU A  67      47.243   0.715 -10.553  1.00 55.80           C  
ANISOU  526  CD1 LEU A  67     6131   7124   7946    381   -395    110       C  
ATOM    527  CD2 LEU A  67      47.871  -1.689 -10.176  1.00 60.57           C  
ANISOU  527  CD2 LEU A  67     6663   7636   8716    371   -423    109       C  
ATOM    528  N   SER A  68      48.100  -0.486 -14.927  1.00 64.14           N  
ANISOU  528  N   SER A  68     7098   8227   9046    484   -365   -108       N  
ATOM    529  CA  SER A  68      49.209  -0.130 -15.799  1.00 62.80           C  
ANISOU  529  CA  SER A  68     6923   8079   8857    506   -348   -128       C  
ATOM    530  C   SER A  68      48.906   1.194 -16.493  1.00 61.80           C  
ANISOU  530  C   SER A  68     6835   8014   8631    527   -325   -137       C  
ATOM    531  O   SER A  68      49.726   2.113 -16.476  1.00 62.86           O  
ANISOU  531  O   SER A  68     6993   8166   8724    527   -309   -105       O  
ATOM    532  CB  SER A  68      49.450  -1.232 -16.827  1.00 66.00           C  
ANISOU  532  CB  SER A  68     7281   8474   9323    530   -349   -199       C  
ATOM    533  OG  SER A  68      50.499  -0.876 -17.708  1.00 67.96           O  
ANISOU  533  OG  SER A  68     7526   8747   9550    552   -330   -220       O  
ATOM    534  N   GLY A  69      47.706   1.301 -17.062  1.00 60.38           N  
ANISOU  534  N   GLY A  69     6661   7865   8415    543   -323   -177       N  
ATOM    535  CA  GLY A  69      47.274   2.534 -17.729  1.00 56.03           C  
ANISOU  535  CA  GLY A  69     6146   7374   7769    565   -302   -184       C  
ATOM    536  C   GLY A  69      47.292   3.744 -16.822  1.00 56.01           C  
ANISOU  536  C   GLY A  69     6187   7379   7713    543   -295   -116       C  
ATOM    537  O   GLY A  69      47.622   4.854 -17.246  1.00 56.43           O  
ANISOU  537  O   GLY A  69     6268   7469   7702    557   -273   -103       O  
ATOM    538  N   LEU A  70      46.953   3.537 -15.559  1.00 57.77           N  
ANISOU  538  N   LEU A  70     6417   7568   7966    509   -313    -72       N  
ATOM    539  CA  LEU A  70      46.806   4.661 -14.651  1.00 58.45           C  
ANISOU  539  CA  LEU A  70     6543   7664   8001    487   -309    -14       C  
ATOM    540  C   LEU A  70      48.155   5.140 -14.130  1.00 57.71           C  
ANISOU  540  C   LEU A  70     6458   7557   7911    473   -304     33       C  
ATOM    541  O   LEU A  70      48.400   6.349 -14.032  1.00 56.18           O  
ANISOU  541  O   LEU A  70     6296   7389   7661    473   -287     61       O  
ATOM    542  CB  LEU A  70      45.818   4.336 -13.519  1.00 58.94           C  
ANISOU  542  CB  LEU A  70     6611   7701   8083    457   -327     13       C  
ATOM    543  CG  LEU A  70      44.360   4.067 -13.960  1.00 62.03           C  
ANISOU  543  CG  LEU A  70     6997   8107   8464    469   -330    -32       C  
ATOM    544  CD1 LEU A  70      43.483   3.695 -12.777  1.00 61.02           C  
ANISOU  544  CD1 LEU A  70     6872   7948   8363    437   -344     -1       C  
ATOM    545  CD2 LEU A  70      43.732   5.233 -14.714  1.00 56.22           C  
ANISOU  545  CD2 LEU A  70     6290   7425   7644    493   -312    -50       C  
ATOM    546  N   ILE A  71      49.029   4.188 -13.815  1.00 57.92           N  
ANISOU  546  N   ILE A  71     6455   7543   8009    463   -318     39       N  
ATOM    547  CA  ILE A  71      50.410   4.508 -13.455  1.00 58.56           C  
ANISOU  547  CA  ILE A  71     6536   7610   8103    455   -315     74       C  
ATOM    548  C   ILE A  71      51.012   5.361 -14.576  1.00 58.09           C  
ANISOU  548  C   ILE A  71     6486   7589   7996    483   -284     52       C  
ATOM    549  O   ILE A  71      51.547   6.446 -14.328  1.00 58.35           O  
ANISOU  549  O   ILE A  71     6544   7637   7991    478   -270     85       O  
ATOM    550  CB  ILE A  71      51.244   3.235 -13.172  1.00 58.65           C  
ANISOU  550  CB  ILE A  71     6508   7572   8204    446   -335     74       C  
ATOM    551  CG1 ILE A  71      50.717   2.547 -11.907  1.00 55.93           C  
ANISOU  551  CG1 ILE A  71     6160   7189   7900    417   -363    112       C  
ATOM    552  CG2 ILE A  71      52.727   3.578 -13.012  1.00 58.21           C  
ANISOU  552  CG2 ILE A  71     6448   7505   8163    443   -331     99       C  
ATOM    553  CD1 ILE A  71      51.129   1.099 -11.751  1.00 57.00           C  
ANISOU  553  CD1 ILE A  71     6253   7274   8129    412   -383    104       C  
ATOM    554  N   LEU A  72      50.863   4.897 -15.812  1.00 58.00           N  
ANISOU  554  N   LEU A  72     6455   7596   7987    514   -273     -6       N  
ATOM    555  CA  LEU A  72      51.267   5.684 -16.961  1.00 58.82           C  
ANISOU  555  CA  LEU A  72     6569   7742   8038    545   -241    -29       C  
ATOM    556  C   LEU A  72      50.704   7.096 -16.906  1.00 60.34           C  
ANISOU  556  C   LEU A  72     6804   7972   8149    547   -223     -2       C  
ATOM    557  O   LEU A  72      51.433   8.054 -17.164  1.00 65.83           O  
ANISOU  557  O   LEU A  72     7516   8685   8811    554   -197     18       O  
ATOM    558  CB  LEU A  72      50.865   4.992 -18.268  1.00 60.27           C  
ANISOU  558  CB  LEU A  72     6729   7949   8223    579   -235    -99       C  
ATOM    559  CG  LEU A  72      51.217   5.705 -19.584  1.00 62.27           C  
ANISOU  559  CG  LEU A  72     6992   8251   8416    617   -200   -127       C  
ATOM    560  CD1 LEU A  72      52.618   6.310 -19.568  1.00 64.86           C  
ANISOU  560  CD1 LEU A  72     7324   8573   8748    614   -176    -95       C  
ATOM    561  CD2 LEU A  72      51.077   4.751 -20.759  1.00 61.93           C  
ANISOU  561  CD2 LEU A  72     6915   8223   8391    649   -199   -200       C  
ATOM    562  N   LYS A  73      49.417   7.227 -16.563  1.00 63.26           N  
ANISOU  562  N   LYS A  73     7192   8353   8492    540   -235     -1       N  
ATOM    563  CA  LYS A  73      48.770   8.538 -16.479  1.00 59.22           C  
ANISOU  563  CA  LYS A  73     6718   7875   7906    542   -219     23       C  
ATOM    564  C   LYS A  73      49.465   9.449 -15.489  1.00 58.84           C  
ANISOU  564  C   LYS A  73     6692   7814   7851    515   -214     82       C  
ATOM    565  O   LYS A  73      49.683  10.626 -15.778  1.00 59.38           O  
ANISOU  565  O   LYS A  73     6784   7909   7870    525   -189     99       O  
ATOM    566  CB  LYS A  73      47.281   8.411 -16.132  1.00 67.23           C  
ANISOU  566  CB  LYS A  73     7743   8896   8905    535   -236     13       C  
ATOM    567  CG  LYS A  73      46.570   9.742 -15.871  1.00 63.45           C  
ANISOU  567  CG  LYS A  73     7302   8446   8358    532   -224     41       C  
ATOM    568  CD  LYS A  73      45.452   9.592 -14.851  1.00 69.16           C  
ANISOU  568  CD  LYS A  73     8035   9155   9088    505   -245     56       C  
ATOM    569  CE  LYS A  73      45.950   9.213 -13.462  1.00 71.63           C  
ANISOU  569  CE  LYS A  73     8343   9425   9447    465   -263    102       C  
ATOM    570  NZ  LYS A  73      46.952  10.196 -12.978  1.00 77.69           N  
ANISOU  570  NZ  LYS A  73     9129  10193  10195    453   -250    146       N  
ATOM    571  N   ASN A  74      49.822   8.921 -14.325  1.00 60.83           N  
ANISOU  571  N   ASN A  74     6934   8026   8153    483   -239    113       N  
ATOM    572  CA  ASN A  74      50.533   9.740 -13.344  1.00 65.91           C  
ANISOU  572  CA  ASN A  74     7595   8658   8791    458   -238    164       C  
ATOM    573  C   ASN A  74      51.867  10.229 -13.910  1.00 69.65           C  
ANISOU  573  C   ASN A  74     8061   9134   9267    471   -214    167       C  
ATOM    574  O   ASN A  74      52.257  11.388 -13.715  1.00 69.62           O  
ANISOU  574  O   ASN A  74     8079   9143   9233    467   -195    194       O  
ATOM    575  CB  ASN A  74      50.751   8.981 -12.033  1.00 67.95           C  
ANISOU  575  CB  ASN A  74     7841   8875   9102    425   -271    196       C  
ATOM    576  CG  ASN A  74      49.451   8.514 -11.394  1.00 69.94           C  
ANISOU  576  CG  ASN A  74     8099   9120   9353    409   -290    199       C  
ATOM    577  OD1 ASN A  74      49.209   7.314 -11.292  1.00 72.60           O  
ANISOU  577  OD1 ASN A  74     8412   9431   9740    406   -309    184       O  
ATOM    578  ND2 ASN A  74      48.614   9.457 -10.956  1.00 68.35           N  
ANISOU  578  ND2 ASN A  74     7930   8942   9099    400   -284    217       N  
ATOM    579  N   ASN A  75      52.542   9.339 -14.638  1.00 70.00           N  
ANISOU  579  N   ASN A  75     8075   9166   9354    488   -212    135       N  
ATOM    580  CA  ASN A  75      53.815   9.654 -15.265  1.00 71.33           C  
ANISOU  580  CA  ASN A  75     8233   9336   9533    502   -188    131       C  
ATOM    581  C   ASN A  75      53.660  10.770 -16.263  1.00 72.39           C  
ANISOU  581  C   ASN A  75     8389   9513   9601    529   -148    123       C  
ATOM    582  O   ASN A  75      54.499  11.667 -16.337  1.00 74.63           O  
ANISOU  582  O   ASN A  75     8681   9801   9874    530   -123    146       O  
ATOM    583  CB  ASN A  75      54.409   8.418 -15.931  1.00 68.58           C  
ANISOU  583  CB  ASN A  75     7845   8969   9242    516   -193     92       C  
ATOM    584  CG  ASN A  75      54.925   7.421 -14.925  1.00 69.78           C  
ANISOU  584  CG  ASN A  75     7972   9072   9469    489   -228    109       C  
ATOM    585  OD1 ASN A  75      55.003   7.713 -13.730  1.00 69.84           O  
ANISOU  585  OD1 ASN A  75     7992   9061   9482    461   -247    154       O  
ATOM    586  ND2 ASN A  75      55.282   6.233 -15.398  1.00 71.01           N  
ANISOU  586  ND2 ASN A  75     8092   9206   9682    499   -237     74       N  
ATOM    587  N   VAL A  76      52.560  10.728 -17.005  1.00 71.93           N  
ANISOU  587  N   VAL A  76     8341   9488   9501    552   -143     93       N  
ATOM    588  CA  VAL A  76      52.268  11.756 -17.991  1.00 75.07           C  
ANISOU  588  CA  VAL A  76     8762   9931   9830    582   -108     87       C  
ATOM    589  C   VAL A  76      51.880  13.094 -17.353  1.00 80.30           C  
ANISOU  589  C   VAL A  76     9458  10603  10447    567    -98    131       C  
ATOM    590  O   VAL A  76      51.581  14.056 -18.057  1.00 86.25           O  
ANISOU  590  O   VAL A  76    10234  11392  11145    590    -68    134       O  
ATOM    591  CB  VAL A  76      51.191  11.281 -18.983  1.00 72.92           C  
ANISOU  591  CB  VAL A  76     8488   9693   9525    613   -110     38       C  
ATOM    592  CG1 VAL A  76      50.787  12.398 -19.936  1.00 71.30           C  
ANISOU  592  CG1 VAL A  76     8311   9538   9243    645    -76     37       C  
ATOM    593  CG2 VAL A  76      51.700  10.079 -19.762  1.00 74.05           C  
ANISOU  593  CG2 VAL A  76     8595   9830   9711    631   -113    -11       C  
ATOM    594  N   LYS A  77      51.894  13.173 -16.028  1.00 84.68           N  
ANISOU  594  N   LYS A  77    10018  11130  11028    530   -121    165       N  
ATOM    595  CA  LYS A  77      51.589  14.447 -15.390  1.00 88.75           C  
ANISOU  595  CA  LYS A  77    10563  11654  11505    516   -111    203       C  
ATOM    596  C   LYS A  77      52.588  14.854 -14.311  1.00 89.29           C  
ANISOU  596  C   LYS A  77    10628  11692  11607    485   -117    241       C  
ATOM    597  O   LYS A  77      52.288  15.663 -13.441  1.00 92.96           O  
ANISOU  597  O   LYS A  77    11112  12156  12054    464   -121    270       O  
ATOM    598  CB  LYS A  77      50.119  14.518 -14.930  1.00 92.39           C  
ANISOU  598  CB  LYS A  77    11042  12127  11934    507   -130    202       C  
ATOM    599  CG  LYS A  77      49.717  13.644 -13.752  1.00 94.84           C  
ANISOU  599  CG  LYS A  77    11344  12408  12283    474   -169    210       C  
ATOM    600  CD  LYS A  77      48.211  13.746 -13.521  1.00 94.46           C  
ANISOU  600  CD  LYS A  77    11314  12376  12202    471   -180    203       C  
ATOM    601  CE  LYS A  77      47.847  13.820 -12.040  1.00 94.16           C  
ANISOU  601  CE  LYS A  77    11285  12317  12174    432   -203    237       C  
ATOM    602  NZ  LYS A  77      48.229  12.612 -11.248  1.00 95.56           N  
ANISOU  602  NZ  LYS A  77    11440  12458  12410    410   -233    245       N  
ATOM    603  N   ALA A  78      53.788  14.294 -14.396  1.00 91.00           N  
ANISOU  603  N   ALA A  78    10819  11885  11873    484   -118    237       N  
ATOM    604  CA  ALA A  78      54.887  14.686 -13.526  1.00 93.01           C  
ANISOU  604  CA  ALA A  78    11067  12112  12163    460   -122    267       C  
ATOM    605  C   ALA A  78      56.219  14.540 -14.257  1.00 95.94           C  
ANISOU  605  C   ALA A  78    11413  12471  12568    475    -99    256       C  
ATOM    606  O   ALA A  78      57.263  14.945 -13.743  1.00 95.06           O  
ANISOU  606  O   ALA A  78    11292  12339  12489    461    -96    276       O  
ATOM    607  CB  ALA A  78      54.878  13.860 -12.245  1.00 89.93           C  
ANISOU  607  CB  ALA A  78    10665  11690  11813    429   -167    283       C  
ATOM    608  N   HIS A  79      56.173  13.968 -15.461  1.00 96.28           N  
ANISOU  608  N   HIS A  79    11444  12529  12606    505    -82    220       N  
ATOM    609  CA  HIS A  79      57.385  13.666 -16.229  1.00 99.18           C  
ANISOU  609  CA  HIS A  79    11786  12887  13010    521    -60    203       C  
ATOM    610  C   HIS A  79      57.238  13.851 -17.711  1.00 98.07           C  
ANISOU  610  C   HIS A  79    11650  12783  12828    561    -20    174       C  
ATOM    611  O   HIS A  79      58.130  13.469 -18.466  1.00 99.86           O  
ANISOU  611  O   HIS A  79    11855  13007  13081    577      1    153       O  
ATOM    612  CB  HIS A  79      57.852  12.232 -15.963  1.00 99.41           C  
ANISOU  612  CB  HIS A  79    11782  12884  13106    513    -93    183       C  
ATOM    613  CG  HIS A  79      58.473  12.034 -14.607  1.00105.53           C  
ANISOU  613  CG  HIS A  79    12546  13620  13931    478   -127    214       C  
ATOM    614  ND1 HIS A  79      58.003  11.139 -13.722  1.00110.08           N  
ANISOU  614  ND1 HIS A  79    13115  14174  14534    459   -170    221       N  
ATOM    615  CD2 HIS A  79      59.561  12.660 -13.995  1.00108.89           C  
ANISOU  615  CD2 HIS A  79    12965  14024  14384    462   -124    241       C  
ATOM    616  CE1 HIS A  79      58.751  11.185 -12.600  1.00111.70           C  
ANISOU  616  CE1 HIS A  79    13313  14351  14777    432   -195    252       C  
ATOM    617  NE2 HIS A  79      59.702  12.116 -12.770  1.00109.67           N  
ANISOU  617  NE2 HIS A  79    13054  14094  14520    435   -167    261       N  
ATOM    618  N   PHE A  80      56.129  14.439 -18.153  1.00 98.56           N  
ANISOU  618  N   PHE A  80    11740  12882  12825    577     -8    173       N  
ATOM    619  CA  PHE A  80      55.803  14.444 -19.583  1.00 96.25           C  
ANISOU  619  CA  PHE A  80    11452  12631  12488    618     23    142       C  
ATOM    620  C   PHE A  80      56.753  15.247 -20.467  1.00 98.63           C  
ANISOU  620  C   PHE A  80    11755  12946  12774    641     75    151       C  
ATOM    621  O   PHE A  80      56.963  14.900 -21.638  1.00 94.72           O  
ANISOU  621  O   PHE A  80    11250  12475  12262    674    100    119       O  
ATOM    622  CB  PHE A  80      54.354  14.861 -19.837  1.00 93.34           C  
ANISOU  622  CB  PHE A  80    11112  12299  12053    633     19    138       C  
ATOM    623  CG  PHE A  80      53.891  14.583 -21.242  1.00 91.20           C  
ANISOU  623  CG  PHE A  80    10841  12072  11738    676     37     97       C  
ATOM    624  CD1 PHE A  80      53.801  13.274 -21.713  1.00 86.72           C  
ANISOU  624  CD1 PHE A  80    10247  11505  11197    688     17     47       C  
ATOM    625  CD2 PHE A  80      53.570  15.627 -22.102  1.00 89.09           C  
ANISOU  625  CD2 PHE A  80    10601  11847  11404    707     75    108       C  
ATOM    626  CE1 PHE A  80      53.386  13.013 -23.008  1.00 87.11           C  
ANISOU  626  CE1 PHE A  80    10295  11598  11204    730     32      5       C  
ATOM    627  CE2 PHE A  80      53.159  15.373 -23.398  1.00 87.84           C  
ANISOU  627  CE2 PHE A  80    10444  11733  11199    750     90     70       C  
ATOM    628  CZ  PHE A  80      53.065  14.065 -23.852  1.00 87.68           C  
ANISOU  628  CZ  PHE A  80    10396  11716  11202    762     68     16       C  
ATOM    629  N   GLN A  81      57.307  16.322 -19.908  1.00101.67           N  
ANISOU  629  N   GLN A  81    12150  13315  13164    624     94    192       N  
ATOM    630  CA  GLN A  81      58.317  17.133 -20.593  1.00104.01           C  
ANISOU  630  CA  GLN A  81    12445  13616  13459    640    147    206       C  
ATOM    631  C   GLN A  81      59.478  16.243 -21.038  1.00101.81           C  
ANISOU  631  C   GLN A  81    12131  13318  13234    646    154    179       C  
ATOM    632  O   GLN A  81      59.978  16.377 -22.156  1.00 99.95           O  
ANISOU  632  O   GLN A  81    11891  13104  12982    676    198    167       O  
ATOM    633  CB  GLN A  81      58.853  18.255 -19.687  1.00106.96           C  
ANISOU  633  CB  GLN A  81    12825  13962  13852    613    158    250       C  
ATOM    634  CG  GLN A  81      57.842  18.897 -18.741  1.00115.31           C  
ANISOU  634  CG  GLN A  81    13907  15022  14882    592    134    275       C  
ATOM    635  CD  GLN A  81      57.765  18.209 -17.381  1.00119.57           C  
ANISOU  635  CD  GLN A  81    14437  15530  15466    554     79    277       C  
ATOM    636  OE1 GLN A  81      58.689  17.501 -16.970  1.00114.72           O  
ANISOU  636  OE1 GLN A  81    13795  14885  14910    539     61    270       O  
ATOM    637  NE2 GLN A  81      56.658  18.424 -16.672  1.00120.81           N  
ANISOU  637  NE2 GLN A  81    14615  15695  15593    539     52    288       N  
ATOM    638  N   ASN A  82      59.863  15.321 -20.152  1.00101.51           N  
ANISOU  638  N   ASN A  82    12069  13242  13259    618    112    171       N  
ATOM    639  CA  ASN A  82      61.015  14.432 -20.323  1.00101.14           C  
ANISOU  639  CA  ASN A  82    11984  13168  13278    616    110    148       C  
ATOM    640  C   ASN A  82      60.737  13.164 -21.141  1.00100.82           C  
ANISOU  640  C   ASN A  82    11924  13141  13242    638     99     98       C  
ATOM    641  O   ASN A  82      61.599  12.291 -21.259  1.00103.66           O  
ANISOU  641  O   ASN A  82    12250  13476  13661    637     93     74       O  
ATOM    642  CB  ASN A  82      61.590  14.058 -18.949  1.00105.20           C  
ANISOU  642  CB  ASN A  82    12480  13633  13859    577     68    167       C  
ATOM    643  CG  ASN A  82      62.106  15.266 -18.168  1.00109.24           C  
ANISOU  643  CG  ASN A  82    13001  14128  14377    556     80    209       C  
ATOM    644  OD1 ASN A  82      62.375  16.329 -18.735  1.00109.60           O  
ANISOU  644  OD1 ASN A  82    13059  14188  14395    570    128    223       O  
ATOM    645  ND2 ASN A  82      62.252  15.101 -16.854  1.00107.48           N  
ANISOU  645  ND2 ASN A  82    12772  13873  14192    523     37    228       N  
ATOM    646  N   PHE A  83      59.532  13.061 -21.691  1.00100.77           N  
ANISOU  646  N   PHE A  83    11938  13173  13178    659     95     78       N  
ATOM    647  CA  PHE A  83      59.201  11.998 -22.633  1.00100.91           C  
ANISOU  647  CA  PHE A  83    11937  13212  13191    686     90     24       C  
ATOM    648  C   PHE A  83      59.870  12.344 -23.959  1.00 98.55           C  
ANISOU  648  C   PHE A  83    11636  12945  12864    722    145      7       C  
ATOM    649  O   PHE A  83      59.722  13.466 -24.451  1.00100.21           O  
ANISOU  649  O   PHE A  83    11875  13186  13015    740    184     32       O  
ATOM    650  CB  PHE A  83      57.681  11.917 -22.864  1.00101.53           C  
ANISOU  650  CB  PHE A  83    12039  13327  13211    700     71      8       C  
ATOM    651  CG  PHE A  83      56.912  11.134 -21.820  1.00101.58           C  
ANISOU  651  CG  PHE A  83    12039  13305  13251    672     16      6       C  
ATOM    652  CD1 PHE A  83      57.170  11.279 -20.456  1.00 99.54           C  
ANISOU  652  CD1 PHE A  83    11781  13005  13033    632    -10     47       C  
ATOM    653  CD2 PHE A  83      55.875  10.285 -22.211  1.00 98.65           C  
ANISOU  653  CD2 PHE A  83    11662  12953  12869    686     -8    -38       C  
ATOM    654  CE1 PHE A  83      56.438  10.570 -19.512  1.00 99.46           C  
ANISOU  654  CE1 PHE A  83    11767  12972  13050    608    -56     49       C  
ATOM    655  CE2 PHE A  83      55.137   9.578 -21.272  1.00 97.81           C  
ANISOU  655  CE2 PHE A  83    11548  12819  12795    660    -53    -38       C  
ATOM    656  CZ  PHE A  83      55.419   9.721 -19.921  1.00 97.85           C  
ANISOU  656  CZ  PHE A  83    11556  12783  12838    621    -76      8       C  
ATOM    657  N   PRO A  84      60.629  11.398 -24.534  1.00 96.22           N  
ANISOU  657  N   PRO A  84    11307  12641  12612    733    150    -33       N  
ATOM    658  CA  PRO A  84      61.005  11.526 -25.945  1.00 95.73           C  
ANISOU  658  CA  PRO A  84    11242  12619  12511    773    200    -61       C  
ATOM    659  C   PRO A  84      59.797  11.295 -26.855  1.00 92.74           C  
ANISOU  659  C   PRO A  84    10879  12297  12061    808    196    -99       C  
ATOM    660  O   PRO A  84      58.793  10.740 -26.413  1.00 92.41           O  
ANISOU  660  O   PRO A  84    10839  12254  12020    799    151   -114       O  
ATOM    661  CB  PRO A  84      62.048  10.419 -26.141  1.00 95.66           C  
ANISOU  661  CB  PRO A  84    11187  12580  12577    770    196   -100       C  
ATOM    662  CG  PRO A  84      61.851   9.480 -25.002  1.00 94.19           C  
ANISOU  662  CG  PRO A  84    10980  12347  12460    736    136   -104       C  
ATOM    663  CD  PRO A  84      61.367  10.319 -23.859  1.00 94.40           C  
ANISOU  663  CD  PRO A  84    11037  12359  12472    707    117    -48       C  
ATOM    664  N   ASN A  85      59.899  11.719 -28.111  1.00 92.24           N  
ANISOU  664  N   ASN A  85    10827  12284  11937    849    243   -112       N  
ATOM    665  CA  ASN A  85      58.774  11.642 -29.051  1.00 92.95           C  
ANISOU  665  CA  ASN A  85    10934  12435  11949    887    242   -146       C  
ATOM    666  C   ASN A  85      58.396  10.221 -29.448  1.00 91.78           C  
ANISOU  666  C   ASN A  85    10753  12293  11826    899    208   -219       C  
ATOM    667  O   ASN A  85      57.224   9.928 -29.669  1.00 97.50           O  
ANISOU  667  O   ASN A  85    11486  13047  12512    914    180   -248       O  
ATOM    668  CB  ASN A  85      59.061  12.466 -30.309  1.00 94.04           C  
ANISOU  668  CB  ASN A  85    11092  12626  12013    931    303   -139       C  
ATOM    669  CG  ASN A  85      59.645  13.834 -29.997  1.00 95.15           C  
ANISOU  669  CG  ASN A  85    11258  12754  12143    920    345    -70       C  
ATOM    670  OD1 ASN A  85      59.585  14.314 -28.861  1.00 95.64           O  
ANISOU  670  OD1 ASN A  85    11328  12775  12236    883    325    -27       O  
ATOM    671  ND2 ASN A  85      60.219  14.468 -31.008  1.00 94.14           N  
ANISOU  671  ND2 ASN A  85    11139  12659  11971    952    405    -58       N  
ATOM    672  N   GLY A  86      59.393   9.348 -29.528  1.00 87.81           N  
ANISOU  672  N   GLY A  86    10211  11760  11392    891    209   -249       N  
ATOM    673  CA  GLY A  86      59.193   7.972 -29.960  1.00 88.36           C  
ANISOU  673  CA  GLY A  86    10244  11832  11497    902    182   -322       C  
ATOM    674  C   GLY A  86      58.228   7.199 -29.086  1.00 89.40           C  
ANISOU  674  C   GLY A  86    10366  11935  11668    877    122   -335       C  
ATOM    675  O   GLY A  86      57.418   6.421 -29.593  1.00 91.47           O  
ANISOU  675  O   GLY A  86    10614  12221  11920    897     99   -392       O  
ATOM    676  N   VAL A  87      58.319   7.410 -27.774  1.00 89.05           N  
ANISOU  676  N   VAL A  87    10328  11839  11669    835     97   -284       N  
ATOM    677  CA  VAL A  87      57.389   6.794 -26.814  1.00 90.54           C  
ANISOU  677  CA  VAL A  87    10512  11998  11893    809     44   -284       C  
ATOM    678  C   VAL A  87      56.023   7.493 -26.854  1.00 88.65           C  
ANISOU  678  C   VAL A  87    10310  11798  11575    820     36   -272       C  
ATOM    679  O   VAL A  87      54.990   6.838 -26.997  1.00 85.29           O  
ANISOU  679  O   VAL A  87     9877  11385  11144    829      6   -312       O  
ATOM    680  CB  VAL A  87      57.973   6.720 -25.368  1.00 91.50           C  
ANISOU  680  CB  VAL A  87    10626  12053  12088    761     19   -234       C  
ATOM    681  CG1 VAL A  87      58.960   7.840 -25.097  1.00 90.17           C  
ANISOU  681  CG1 VAL A  87    10476  11876  11910    751     53   -179       C  
ATOM    682  CG2 VAL A  87      56.872   6.716 -24.312  1.00 89.65           C  
ANISOU  682  CG2 VAL A  87    10408  11801  11853    735    -23   -208       C  
ATOM    683  N   THR A  88      56.035   8.819 -26.746  1.00 86.67           N  
ANISOU  683  N   THR A  88    10098  11565  11267    821     63   -218       N  
ATOM    684  CA  THR A  88      54.833   9.624 -26.874  1.00 87.31           C  
ANISOU  684  CA  THR A  88    10216  11687  11271    835     62   -203       C  
ATOM    685  C   THR A  88      53.994   9.155 -28.060  1.00 89.99           C  
ANISOU  685  C   THR A  88    10551  12082  11560    879     59   -267       C  
ATOM    686  O   THR A  88      52.828   8.795 -27.893  1.00 92.56           O  
ANISOU  686  O   THR A  88    10878  12416  11876    880     25   -290       O  
ATOM    687  CB  THR A  88      55.181  11.115 -27.021  1.00 88.47           C  
ANISOU  687  CB  THR A  88    10400  11854  11361    843    106   -147       C  
ATOM    688  OG1 THR A  88      55.747  11.596 -25.795  1.00 88.03           O  
ANISOU  688  OG1 THR A  88    10349  11749  11351    801    101    -91       O  
ATOM    689  CG2 THR A  88      53.948  11.930 -27.346  1.00 89.67           C  
ANISOU  689  CG2 THR A  88    10588  12053  11430    865    107   -136       C  
ATOM    690  N   ASP A  89      54.600   9.125 -29.246  1.00 88.72           N  
ANISOU  690  N   ASP A  89    10382  11957  11369    915     95   -297       N  
ATOM    691  CA  ASP A  89      53.869   8.783 -30.466  1.00 89.31           C  
ANISOU  691  CA  ASP A  89    10454  12094  11384    962     96   -358       C  
ATOM    692  C   ASP A  89      53.326   7.370 -30.427  1.00 86.09           C  
ANISOU  692  C   ASP A  89    10007  11671  11031    958     51   -427       C  
ATOM    693  O   ASP A  89      52.310   7.075 -31.053  1.00 92.99           O  
ANISOU  693  O   ASP A  89    10880  12587  11865    987     34   -476       O  
ATOM    694  CB  ASP A  89      54.737   8.989 -31.711  1.00 91.36           C  
ANISOU  694  CB  ASP A  89    10712  12397  11604   1001    146   -376       C  
ATOM    695  CG  ASP A  89      55.185  10.435 -31.881  1.00 96.08           C  
ANISOU  695  CG  ASP A  89    11348  13013  12143   1010    195   -308       C  
ATOM    696  OD1 ASP A  89      54.730  11.313 -31.107  1.00 99.19           O  
ANISOU  696  OD1 ASP A  89    11772  13393  12523    989    189   -252       O  
ATOM    697  OD2 ASP A  89      56.004  10.697 -32.786  1.00 98.44           O  
ANISOU  697  OD2 ASP A  89    11648  13341  12414   1037    243   -311       O  
ATOM    698  N   PHE A  90      53.999   6.501 -29.684  1.00 79.17           N  
ANISOU  698  N   PHE A  90     9097  10733  10250    924     32   -431       N  
ATOM    699  CA  PHE A  90      53.554   5.121 -29.553  1.00 79.16           C  
ANISOU  699  CA  PHE A  90     9055  10708  10316    916     -8   -492       C  
ATOM    700  C   PHE A  90      52.328   5.041 -28.642  1.00 80.68           C  
ANISOU  700  C   PHE A  90     9257  10879  10517    893    -50   -477       C  
ATOM    701  O   PHE A  90      51.400   4.266 -28.897  1.00 79.79           O  
ANISOU  701  O   PHE A  90     9125  10777  10416    904    -79   -533       O  
ATOM    702  CB  PHE A  90      54.690   4.231 -29.038  1.00 74.21           C  
ANISOU  702  CB  PHE A  90     8387  10019   9790    888    -14   -495       C  
ATOM    703  CG  PHE A  90      54.272   2.822 -28.749  1.00 70.48           C  
ANISOU  703  CG  PHE A  90     7871   9509   9398    875    -56   -548       C  
ATOM    704  CD1 PHE A  90      53.703   2.032 -29.742  1.00 68.30           C  
ANISOU  704  CD1 PHE A  90     7567   9268   9114    909    -65   -631       C  
ATOM    705  CD2 PHE A  90      54.450   2.279 -27.478  1.00 69.59           C  
ANISOU  705  CD2 PHE A  90     7742   9327   9371    831    -87   -515       C  
ATOM    706  CE1 PHE A  90      53.311   0.726 -29.471  1.00 69.83           C  
ANISOU  706  CE1 PHE A  90     7717   9424   9392    896   -102   -681       C  
ATOM    707  CE2 PHE A  90      54.065   0.970 -27.201  1.00 69.16           C  
ANISOU  707  CE2 PHE A  90     7646   9234   9397    820   -123   -559       C  
ATOM    708  CZ  PHE A  90      53.490   0.194 -28.199  1.00 69.51           C  
ANISOU  708  CZ  PHE A  90     7661   9309   9440    852   -130   -643       C  
ATOM    709  N   ILE A  91      52.335   5.854 -27.589  1.00 78.27           N  
ANISOU  709  N   ILE A  91     8982  10547  10211    861    -51   -404       N  
ATOM    710  CA  ILE A  91      51.196   5.955 -26.693  1.00 78.94           C  
ANISOU  710  CA  ILE A  91     9082  10616  10297    838    -84   -383       C  
ATOM    711  C   ILE A  91      50.003   6.588 -27.426  1.00 81.75           C  
ANISOU  711  C   ILE A  91     9465  11034  10564    872    -81   -402       C  
ATOM    712  O   ILE A  91      48.901   6.023 -27.428  1.00 82.01           O  
ANISOU  712  O   ILE A  91     9486  11071  10603    876   -112   -442       O  
ATOM    713  CB  ILE A  91      51.545   6.728 -25.397  1.00 77.28           C  
ANISOU  713  CB  ILE A  91     8897  10365  10101    796    -84   -302       C  
ATOM    714  CG1 ILE A  91      52.730   6.065 -24.686  1.00 71.28           C  
ANISOU  714  CG1 ILE A  91     8108   9546   9429    765    -90   -286       C  
ATOM    715  CG2 ILE A  91      50.347   6.759 -24.455  1.00 74.80           C  
ANISOU  715  CG2 ILE A  91     8597  10035   9790    771   -117   -284       C  
ATOM    716  CD1 ILE A  91      53.299   6.864 -23.533  1.00 70.50           C  
ANISOU  716  CD1 ILE A  91     8031   9414   9342    729    -87   -211       C  
ATOM    717  N   LYS A  92      50.232   7.738 -28.066  1.00 81.15           N  
ANISOU  717  N   LYS A  92     9422  11003  10409    898    -45   -374       N  
ATOM    718  CA  LYS A  92      49.178   8.430 -28.811  1.00 78.31           C  
ANISOU  718  CA  LYS A  92     9090  10704   9959    935    -40   -387       C  
ATOM    719  C   LYS A  92      48.521   7.472 -29.779  1.00 78.61           C  
ANISOU  719  C   LYS A  92     9100  10779   9990    970    -60   -472       C  
ATOM    720  O   LYS A  92      47.309   7.293 -29.755  1.00 84.72           O  
ANISOU  720  O   LYS A  92     9874  11567  10750    977    -89   -501       O  
ATOM    721  CB  LYS A  92      49.725   9.623 -29.587  1.00 75.43           C  
ANISOU  721  CB  LYS A  92     8758  10385   9517    965      8   -351       C  
ATOM    722  CG  LYS A  92      50.216  10.793 -28.754  1.00 77.38           C  
ANISOU  722  CG  LYS A  92     9036  10605   9759    936     31   -268       C  
ATOM    723  CD  LYS A  92      50.125  12.037 -29.618  1.00 81.23           C  
ANISOU  723  CD  LYS A  92     9561  11149  10155    975     71   -240       C  
ATOM    724  CE  LYS A  92      51.366  12.908 -29.607  1.00 85.87           C  
ANISOU  724  CE  LYS A  92    10162  11724  10741    969    119   -184       C  
ATOM    725  NZ  LYS A  92      51.193  14.070 -30.532  1.00 89.32           N  
ANISOU  725  NZ  LYS A  92    10634  12217  11088   1010    160   -157       N  
ATOM    726  N   SER A  93      49.336   6.843 -30.617  1.00 80.98           N  
ANISOU  726  N   SER A  93     9373  11092  10303    992    -44   -517       N  
ATOM    727  CA  SER A  93      48.855   5.871 -31.589  1.00 84.16           C  
ANISOU  727  CA  SER A  93     9743  11530  10704   1027    -61   -607       C  
ATOM    728  C   SER A  93      48.019   4.781 -30.923  1.00 83.82           C  
ANISOU  728  C   SER A  93     9666  11445  10736   1002   -109   -647       C  
ATOM    729  O   SER A  93      46.936   4.440 -31.402  1.00 86.17           O  
ANISOU  729  O   SER A  93     9954  11774  11012   1026   -133   -703       O  
ATOM    730  CB  SER A  93      50.041   5.248 -32.343  1.00 86.13           C  
ANISOU  730  CB  SER A  93     9963  11785  10979   1043    -36   -645       C  
ATOM    731  OG  SER A  93      49.706   3.991 -32.914  1.00 86.74           O  
ANISOU  731  OG  SER A  93     9994  11869  11094   1060    -62   -735       O  
ATOM    732  N   GLU A  94      48.530   4.253 -29.813  1.00 84.53           N  
ANISOU  732  N   GLU A  94     9739  11463  10917    955   -122   -617       N  
ATOM    733  CA  GLU A  94      47.949   3.085 -29.159  1.00 84.31           C  
ANISOU  733  CA  GLU A  94     9673  11386  10975    929   -162   -652       C  
ATOM    734  C   GLU A  94      46.617   3.406 -28.463  1.00 85.74           C  
ANISOU  734  C   GLU A  94     9873  11561  11141    914   -188   -633       C  
ATOM    735  O   GLU A  94      45.698   2.567 -28.431  1.00 81.50           O  
ANISOU  735  O   GLU A  94     9309  11014  10644    914   -219   -685       O  
ATOM    736  CB  GLU A  94      48.963   2.489 -28.178  1.00 84.85           C  
ANISOU  736  CB  GLU A  94     9720  11381  11139    886   -166   -617       C  
ATOM    737  CG  GLU A  94      48.898   0.976 -28.028  1.00 84.34           C  
ANISOU  737  CG  GLU A  94     9599  11270  11175    874   -194   -675       C  
ATOM    738  CD  GLU A  94      49.102   0.215 -29.326  1.00 86.36           C  
ANISOU  738  CD  GLU A  94     9817  11561  11433    914   -189   -764       C  
ATOM    739  OE1 GLU A  94      49.781   0.733 -30.241  1.00 88.52           O  
ANISOU  739  OE1 GLU A  94    10104  11883  11648    944   -156   -772       O  
ATOM    740  OE2 GLU A  94      48.579  -0.916 -29.426  1.00 87.87           O  
ANISOU  740  OE2 GLU A  94     9965  11732  11689    915   -216   -828       O  
ATOM    741  N   CYS A  95      46.522   4.625 -27.925  1.00 78.48           N  
ANISOU  741  N   CYS A  95     9001  10649  10170    901   -174   -560       N  
ATOM    742  CA  CYS A  95      45.291   5.123 -27.314  1.00 77.31           C  
ANISOU  742  CA  CYS A  95     8876  10501   9997    889   -193   -538       C  
ATOM    743  C   CYS A  95      44.152   5.238 -28.326  1.00 77.45           C  
ANISOU  743  C   CYS A  95     8896  10581   9950    933   -203   -596       C  
ATOM    744  O   CYS A  95      43.187   4.477 -28.259  1.00 79.17           O  
ANISOU  744  O   CYS A  95     9088  10790  10203    933   -234   -646       O  
ATOM    745  CB  CYS A  95      45.537   6.462 -26.626  1.00 72.86           C  
ANISOU  745  CB  CYS A  95     8360   9935   9388    870   -173   -452       C  
ATOM    746  SG  CYS A  95      46.290   6.292 -24.992  1.00 68.56           S  
ANISOU  746  SG  CYS A  95     7813   9311   8925    808   -180   -383       S  
ATOM    747  N   LEU A  96      44.287   6.160 -29.277  1.00 76.64           N  
ANISOU  747  N   LEU A  96     8822  10540   9756    973   -177   -591       N  
ATOM    748  CA  LEU A  96      43.262   6.383 -30.297  1.00 77.18           C  
ANISOU  748  CA  LEU A  96     8898  10676   9753   1021   -186   -642       C  
ATOM    749  C   LEU A  96      42.841   5.102 -31.008  1.00 78.15           C  
ANISOU  749  C   LEU A  96     8972  10810   9912   1044   -213   -740       C  
ATOM    750  O   LEU A  96      41.698   4.978 -31.433  1.00 85.65           O  
ANISOU  750  O   LEU A  96     9914  11792  10835   1069   -238   -790       O  
ATOM    751  CB  LEU A  96      43.706   7.445 -31.309  1.00 77.22           C  
ANISOU  751  CB  LEU A  96     8936  10745   9658   1064   -149   -620       C  
ATOM    752  CG  LEU A  96      44.331   8.743 -30.761  1.00 81.06           C  
ANISOU  752  CG  LEU A  96     9467  11221  10112   1046   -115   -526       C  
ATOM    753  CD1 LEU A  96      44.816   9.626 -31.902  1.00 83.40           C  
ANISOU  753  CD1 LEU A  96     9791  11580  10318   1093    -75   -512       C  
ATOM    754  CD2 LEU A  96      43.403   9.533 -29.844  1.00 78.14           C  
ANISOU  754  CD2 LEU A  96     9127  10835   9730   1021   -129   -477       C  
ATOM    755  N   ASN A  97      43.745   4.139 -31.112  1.00 79.81           N  
ANISOU  755  N   ASN A  97     9145  10991  10188   1036   -210   -771       N  
ATOM    756  CA  ASN A  97      43.409   2.860 -31.738  1.00 83.04           C  
ANISOU  756  CA  ASN A  97     9502  11405  10644   1055   -234   -868       C  
ATOM    757  C   ASN A  97      42.595   1.929 -30.836  1.00 82.98           C  
ANISOU  757  C   ASN A  97     9461  11338  10730   1019   -271   -890       C  
ATOM    758  O   ASN A  97      42.008   0.954 -31.313  1.00 85.64           O  
ANISOU  758  O   ASN A  97     9755  11679  11105   1036   -296   -974       O  
ATOM    759  CB  ASN A  97      44.669   2.153 -32.261  1.00 87.44           C  
ANISOU  759  CB  ASN A  97    10028  11955  11239   1062   -216   -898       C  
ATOM    760  CG  ASN A  97      45.081   2.630 -33.650  1.00 90.76           C  
ANISOU  760  CG  ASN A  97    10463  12456  11567   1116   -187   -928       C  
ATOM    761  OD1 ASN A  97      45.074   1.855 -34.611  1.00 94.32           O  
ANISOU  761  OD1 ASN A  97    10879  12940  12020   1150   -194  -1013       O  
ATOM    762  ND2 ASN A  97      45.436   3.909 -33.764  1.00 85.28           N  
ANISOU  762  ND2 ASN A  97     9819  11793  10791   1126   -154   -859       N  
ATOM    763  N   ASN A  98      42.555   2.225 -29.538  1.00 81.13           N  
ANISOU  763  N   ASN A  98     9245  11047  10532    972   -274   -817       N  
ATOM    764  CA  ASN A  98      41.816   1.382 -28.593  1.00 81.62           C  
ANISOU  764  CA  ASN A  98     9279  11050  10684    935   -304   -827       C  
ATOM    765  C   ASN A  98      40.703   2.114 -27.822  1.00 82.01           C  
ANISOU  765  C   ASN A  98     9360  11094  10705    917   -316   -784       C  
ATOM    766  O   ASN A  98      40.125   1.574 -26.869  1.00 79.36           O  
ANISOU  766  O   ASN A  98     9009  10706  10439    882   -335   -775       O  
ATOM    767  CB  ASN A  98      42.780   0.680 -27.638  1.00 82.32           C  
ANISOU  767  CB  ASN A  98     9347  11064  10868    891   -302   -789       C  
ATOM    768  CG  ASN A  98      43.713  -0.287 -28.353  1.00 83.83           C  
ANISOU  768  CG  ASN A  98     9495  11249  11107    907   -297   -845       C  
ATOM    769  OD1 ASN A  98      44.721   0.119 -28.953  1.00 77.94           O  
ANISOU  769  OD1 ASN A  98     8761  10532  10321    925   -271   -836       O  
ATOM    770  ND2 ASN A  98      43.391  -1.579 -28.276  1.00 76.87           N  
ANISOU  770  ND2 ASN A  98     8561  10328  10318    898   -321   -905       N  
ATOM    771  N   ILE A  99      40.398   3.329 -28.274  1.00 79.42           N  
ANISOU  771  N   ILE A  99     9075  10823  10277    943   -302   -759       N  
ATOM    772  CA  ILE A  99      39.417   4.223 -27.656  1.00 78.36           C  
ANISOU  772  CA  ILE A  99     8976  10694  10104    931   -308   -716       C  
ATOM    773  C   ILE A  99      38.033   3.606 -27.424  1.00 79.99           C  
ANISOU  773  C   ILE A  99     9157  10886  10350    926   -341   -766       C  
ATOM    774  O   ILE A  99      37.285   4.067 -26.554  1.00 79.65           O  
ANISOU  774  O   ILE A  99     9133  10822  10308    899   -348   -726       O  
ATOM    775  CB  ILE A  99      39.266   5.512 -28.493  1.00 79.09           C  
ANISOU  775  CB  ILE A  99     9111  10858  10082    972   -290   -699       C  
ATOM    776  CG1 ILE A  99      38.799   6.682 -27.621  1.00 77.13           C  
ANISOU  776  CG1 ILE A  99     8907  10601   9797    948   -283   -624       C  
ATOM    777  CG2 ILE A  99      38.357   5.281 -29.697  1.00 78.67           C  
ANISOU  777  CG2 ILE A  99     9041  10865   9983   1024   -309   -783       C  
ATOM    778  CD1 ILE A  99      39.109   8.045 -28.203  1.00 74.72           C  
ANISOU  778  CD1 ILE A  99     8648  10349   9395    977   -254   -579       C  
ATOM    779  N   GLY A 100      37.699   2.571 -28.194  1.00 78.37           N  
ANISOU  779  N   GLY A 100     8905  10692  10180    951   -361   -856       N  
ATOM    780  CA  GLY A 100      36.393   1.937 -28.094  1.00 78.28           C  
ANISOU  780  CA  GLY A 100     8863  10668  10212    950   -391   -913       C  
ATOM    781  C   GLY A 100      36.442   0.494 -27.642  1.00 82.03           C  
ANISOU  781  C   GLY A 100     9284  11078  10808    923   -407   -953       C  
ATOM    782  O   GLY A 100      35.669  -0.335 -28.126  1.00 83.08           O  
ANISOU  782  O   GLY A 100     9373  11214  10981    940   -430  -1036       O  
ATOM    783  N   ASP A 101      37.338   0.195 -26.702  1.00 82.23           N  
ANISOU  783  N   ASP A 101     9308  11044  10892    881   -395   -894       N  
ATOM    784  CA  ASP A 101      37.501  -1.167 -26.201  1.00 81.37           C  
ANISOU  784  CA  ASP A 101     9149  10867  10902    853   -407   -919       C  
ATOM    785  C   ASP A 101      36.246  -1.645 -25.491  1.00 81.98           C  
ANISOU  785  C   ASP A 101     9205  10905  11040    829   -427   -933       C  
ATOM    786  O   ASP A 101      35.670  -0.914 -24.680  1.00 86.23           O  
ANISOU  786  O   ASP A 101     9777  11434  11551    806   -424   -876       O  
ATOM    787  CB  ASP A 101      38.691  -1.256 -25.254  1.00 81.71           C  
ANISOU  787  CB  ASP A 101     9201  10856  10988    813   -391   -842       C  
ATOM    788  CG  ASP A 101      39.090  -2.685 -24.962  1.00 84.48           C  
ANISOU  788  CG  ASP A 101     9497  11143  11458    794   -401   -871       C  
ATOM    789  OD1 ASP A 101      39.667  -3.342 -25.857  1.00 85.89           O  
ANISOU  789  OD1 ASP A 101     9641  11333  11659    819   -401   -933       O  
ATOM    790  OD2 ASP A 101      38.823  -3.154 -23.838  1.00 86.07           O  
ANISOU  790  OD2 ASP A 101     9689  11282  11732    753   -408   -832       O  
ATOM    791  N   SER A 102      35.833  -2.872 -25.794  1.00 81.09           N  
ANISOU  791  N   SER A 102     9034  10764  11011    835   -445  -1011       N  
ATOM    792  CA  SER A 102      34.591  -3.435 -25.251  1.00 83.19           C  
ANISOU  792  CA  SER A 102     9272  10992  11344    816   -463  -1037       C  
ATOM    793  C   SER A 102      34.543  -3.550 -23.722  1.00 84.62           C  
ANISOU  793  C   SER A 102     9464  11101  11585    760   -456   -953       C  
ATOM    794  O   SER A 102      33.474  -3.768 -23.149  1.00 88.34           O  
ANISOU  794  O   SER A 102     9924  11544  12097    741   -464   -957       O  
ATOM    795  CB  SER A 102      34.250  -4.776 -25.910  1.00 81.94           C  
ANISOU  795  CB  SER A 102     9044  10816  11275    833   -481  -1141       C  
ATOM    796  OG  SER A 102      35.413  -5.530 -26.160  1.00 87.93           O  
ANISOU  796  OG  SER A 102     9774  11551  12084    833   -475  -1154       O  
ATOM    797  N   SER A 103      35.691  -3.407 -23.067  1.00 82.36           N  
ANISOU  797  N   SER A 103     9200  10788  11305    734   -440   -878       N  
ATOM    798  CA  SER A 103      35.721  -3.287 -21.618  1.00 77.54           C  
ANISOU  798  CA  SER A 103     8611  10123  10727    685   -432   -788       C  
ATOM    799  C   SER A 103      35.537  -1.828 -21.239  1.00 74.02           C  
ANISOU  799  C   SER A 103     8228   9716  10179    680   -421   -723       C  
ATOM    800  O   SER A 103      36.279  -0.958 -21.707  1.00 73.63           O  
ANISOU  800  O   SER A 103     8213   9711  10051    699   -409   -701       O  
ATOM    801  CB  SER A 103      37.037  -3.802 -21.041  1.00 79.48           C  
ANISOU  801  CB  SER A 103     8850  10321  11027    660   -424   -738       C  
ATOM    802  OG  SER A 103      37.242  -3.312 -19.722  1.00 76.48           O  
ANISOU  802  OG  SER A 103     8507   9910  10642    620   -415   -641       O  
ATOM    803  N   PRO A 104      34.540  -1.552 -20.394  1.00 72.51           N  
ANISOU  803  N   PRO A 104     8052   9507   9992    655   -423   -693       N  
ATOM    804  CA  PRO A 104      34.330  -0.183 -19.924  1.00 71.01           C  
ANISOU  804  CA  PRO A 104     7918   9348   9714    647   -412   -630       C  
ATOM    805  C   PRO A 104      35.508   0.359 -19.110  1.00 68.34           C  
ANISOU  805  C   PRO A 104     7616   8995   9355    620   -396   -541       C  
ATOM    806  O   PRO A 104      35.856   1.538 -19.248  1.00 68.03           O  
ANISOU  806  O   PRO A 104     7620   8997   9230    629   -384   -505       O  
ATOM    807  CB  PRO A 104      33.062  -0.296 -19.067  1.00 72.07           C  
ANISOU  807  CB  PRO A 104     8049   9452   9883    620   -417   -622       C  
ATOM    808  CG  PRO A 104      32.338  -1.481 -19.632  1.00 71.82           C  
ANISOU  808  CG  PRO A 104     7959   9400   9929    634   -433   -708       C  
ATOM    809  CD  PRO A 104      33.419  -2.442 -20.040  1.00 70.91           C  
ANISOU  809  CD  PRO A 104     7809   9262   9871    641   -435   -732       C  
ATOM    810  N   LEU A 105      36.127  -0.485 -18.284  1.00 68.83           N  
ANISOU  810  N   LEU A 105     7659   8998   9496    588   -396   -507       N  
ATOM    811  CA  LEU A 105      37.284  -0.047 -17.480  1.00 67.53           C  
ANISOU  811  CA  LEU A 105     7524   8817   9317    563   -385   -425       C  
ATOM    812  C   LEU A 105      38.512   0.307 -18.337  1.00 65.50           C  
ANISOU  812  C   LEU A 105     7275   8593   9019    590   -376   -432       C  
ATOM    813  O   LEU A 105      39.161   1.329 -18.105  1.00 61.93           O  
ANISOU  813  O   LEU A 105     6864   8163   8506    586   -363   -379       O  
ATOM    814  CB  LEU A 105      37.638  -1.061 -16.381  1.00 65.07           C  
ANISOU  814  CB  LEU A 105     7190   8434   9098    525   -390   -385       C  
ATOM    815  CG  LEU A 105      38.812  -0.717 -15.442  1.00 64.38           C  
ANISOU  815  CG  LEU A 105     7129   8326   9005    498   -384   -301       C  
ATOM    816  CD1 LEU A 105      38.573   0.564 -14.650  1.00 59.59           C  
ANISOU  816  CD1 LEU A 105     6576   7744   8323    480   -374   -238       C  
ATOM    817  CD2 LEU A 105      39.134  -1.876 -14.502  1.00 63.33           C  
ANISOU  817  CD2 LEU A 105     6968   8126   8970    468   -392   -269       C  
ATOM    818  N   ILE A 106      38.808  -0.528 -19.331  1.00 66.85           N  
ANISOU  818  N   ILE A 106     7406   8768   9227    617   -382   -501       N  
ATOM    819  CA  ILE A 106      39.866  -0.238 -20.295  1.00 65.86           C  
ANISOU  819  CA  ILE A 106     7284   8679   9061    647   -371   -518       C  
ATOM    820  C   ILE A 106      39.536   1.059 -21.030  1.00 66.83           C  
ANISOU  820  C   ILE A 106     7447   8872   9074    677   -359   -522       C  
ATOM    821  O   ILE A 106      40.380   1.955 -21.134  1.00 66.34           O  
ANISOU  821  O   ILE A 106     7418   8834   8954    682   -341   -481       O  
ATOM    822  CB  ILE A 106      40.044  -1.395 -21.306  1.00 68.96           C  
ANISOU  822  CB  ILE A 106     7623   9068   9511    674   -380   -603       C  
ATOM    823  CG1 ILE A 106      40.421  -2.702 -20.602  1.00 71.16           C  
ANISOU  823  CG1 ILE A 106     7859   9273   9906    645   -390   -598       C  
ATOM    824  CG2 ILE A 106      41.076  -1.055 -22.371  1.00 68.44           C  
ANISOU  824  CG2 ILE A 106     7562   9046   9396    707   -365   -626       C  
ATOM    825  CD1 ILE A 106      41.634  -2.608 -19.703  1.00 73.41           C  
ANISOU  825  CD1 ILE A 106     8159   9521  10211    615   -383   -519       C  
ATOM    826  N   ARG A 107      38.299   1.158 -21.519  1.00 69.67           N  
ANISOU  826  N   ARG A 107     7803   9261   9408    698   -369   -572       N  
ATOM    827  CA  ARG A 107      37.840   2.347 -22.247  1.00 70.38           C  
ANISOU  827  CA  ARG A 107     7929   9418   9396    730   -361   -578       C  
ATOM    828  C   ARG A 107      38.062   3.619 -21.432  1.00 66.69           C  
ANISOU  828  C   ARG A 107     7514   8955   8871    707   -345   -492       C  
ATOM    829  O   ARG A 107      38.615   4.597 -21.948  1.00 64.15           O  
ANISOU  829  O   ARG A 107     7223   8674   8476    728   -326   -470       O  
ATOM    830  CB  ARG A 107      36.369   2.215 -22.654  1.00 72.37           C  
ANISOU  830  CB  ARG A 107     8167   9691   9641    749   -379   -638       C  
ATOM    831  CG  ARG A 107      35.917   3.230 -23.705  1.00 76.81           C  
ANISOU  831  CG  ARG A 107     8756  10328  10101    794   -375   -663       C  
ATOM    832  CD  ARG A 107      34.424   3.140 -24.013  1.00 76.25           C  
ANISOU  832  CD  ARG A 107     8670  10276  10025    811   -397   -720       C  
ATOM    833  NE  ARG A 107      33.999   1.747 -24.157  1.00 79.55           N  
ANISOU  833  NE  ARG A 107     9031  10660  10533    810   -417   -791       N  
ATOM    834  CZ  ARG A 107      33.045   1.161 -23.437  1.00 77.92           C  
ANISOU  834  CZ  ARG A 107     8801  10410  10394    783   -431   -803       C  
ATOM    835  NH1 ARG A 107      32.372   1.844 -22.526  1.00 77.27           N  
ANISOU  835  NH1 ARG A 107     8749  10315  10296    756   -427   -751       N  
ATOM    836  NH2 ARG A 107      32.757  -0.119 -23.637  1.00 79.46           N  
ANISOU  836  NH2 ARG A 107     8941  10573  10677    783   -447   -870       N  
ATOM    837  N   ALA A 108      37.653   3.590 -20.162  1.00 63.66           N  
ANISOU  837  N   ALA A 108     7138   8527   8523    665   -350   -445       N  
ATOM    838  CA  ALA A 108      37.824   4.731 -19.265  1.00 63.16           C  
ANISOU  838  CA  ALA A 108     7120   8465   8413    640   -336   -367       C  
ATOM    839  C   ALA A 108      39.298   5.057 -19.064  1.00 63.78           C  
ANISOU  839  C   ALA A 108     7213   8535   8485    631   -320   -317       C  
ATOM    840  O   ALA A 108      39.691   6.222 -19.065  1.00 64.46           O  
ANISOU  840  O   ALA A 108     7336   8649   8507    635   -303   -276       O  
ATOM    841  CB  ALA A 108      37.160   4.467 -17.924  1.00 60.64           C  
ANISOU  841  CB  ALA A 108     6802   8099   8140    596   -345   -330       C  
ATOM    842  N   THR A 109      40.115   4.024 -18.894  1.00 64.51           N  
ANISOU  842  N   THR A 109     7274   8587   8648    619   -326   -322       N  
ATOM    843  CA  THR A 109      41.539   4.219 -18.672  1.00 61.89           C  
ANISOU  843  CA  THR A 109     6951   8244   8321    610   -313   -279       C  
ATOM    844  C   THR A 109      42.194   4.857 -19.906  1.00 60.50           C  
ANISOU  844  C   THR A 109     6785   8118   8084    650   -293   -301       C  
ATOM    845  O   THR A 109      42.882   5.869 -19.786  1.00 58.53           O  
ANISOU  845  O   THR A 109     6567   7885   7788    648   -274   -254       O  
ATOM    846  CB  THR A 109      42.209   2.898 -18.269  1.00 65.82           C  
ANISOU  846  CB  THR A 109     7408   8686   8913    591   -326   -284       C  
ATOM    847  OG1 THR A 109      41.555   2.380 -17.099  1.00 62.67           O  
ANISOU  847  OG1 THR A 109     7003   8242   8566    555   -341   -256       O  
ATOM    848  CG2 THR A 109      43.697   3.110 -17.971  1.00 66.58           C  
ANISOU  848  CG2 THR A 109     7511   8767   9018    580   -315   -238       C  
ATOM    849  N   VAL A 110      41.931   4.297 -21.085  1.00 60.17           N  
ANISOU  849  N   VAL A 110     6718   8104   8041    686   -297   -373       N  
ATOM    850  CA  VAL A 110      42.398   4.886 -22.345  1.00 62.76           C  
ANISOU  850  CA  VAL A 110     7057   8488   8303    729   -277   -398       C  
ATOM    851  C   VAL A 110      41.981   6.349 -22.448  1.00 64.28           C  
ANISOU  851  C   VAL A 110     7296   8724   8404    741   -260   -362       C  
ATOM    852  O   VAL A 110      42.775   7.209 -22.853  1.00 66.60           O  
ANISOU  852  O   VAL A 110     7613   9043   8647    755   -235   -333       O  
ATOM    853  CB  VAL A 110      41.892   4.088 -23.568  1.00 64.47           C  
ANISOU  853  CB  VAL A 110     7238   8734   8522    769   -288   -488       C  
ATOM    854  CG1 VAL A 110      42.141   4.838 -24.872  1.00 63.41           C  
ANISOU  854  CG1 VAL A 110     7123   8669   8302    817   -267   -511       C  
ATOM    855  CG2 VAL A 110      42.572   2.729 -23.617  1.00 67.07           C  
ANISOU  855  CG2 VAL A 110     7520   9022   8941    761   -297   -524       C  
ATOM    856  N   GLY A 111      40.738   6.620 -22.050  1.00 66.63           N  
ANISOU  856  N   GLY A 111     7605   9026   8686    733   -274   -362       N  
ATOM    857  CA  GLY A 111      40.162   7.957 -22.086  1.00 59.54           C  
ANISOU  857  CA  GLY A 111     6748   8164   7710    743   -262   -331       C  
ATOM    858  C   GLY A 111      40.877   8.966 -21.224  1.00 59.92           C  
ANISOU  858  C   GLY A 111     6831   8198   7740    715   -243   -252       C  
ATOM    859  O   GLY A 111      41.204  10.053 -21.705  1.00 62.94           O  
ANISOU  859  O   GLY A 111     7241   8615   8058    735   -219   -227       O  
ATOM    860  N   ILE A 112      41.114   8.622 -19.955  1.00 58.61           N  
ANISOU  860  N   ILE A 112     6661   7980   7629    670   -252   -213       N  
ATOM    861  CA  ILE A 112      41.835   9.523 -19.040  1.00 64.81           C  
ANISOU  861  CA  ILE A 112     7474   8749   8402    641   -237   -142       C  
ATOM    862  C   ILE A 112      43.231   9.824 -19.611  1.00 67.98           C  
ANISOU  862  C   ILE A 112     7877   9160   8792    656   -214   -128       C  
ATOM    863  O   ILE A 112      43.732  10.947 -19.505  1.00 66.52           O  
ANISOU  863  O   ILE A 112     7721   8988   8567    654   -191    -85       O  
ATOM    864  CB  ILE A 112      41.992   8.955 -17.600  1.00 66.88           C  
ANISOU  864  CB  ILE A 112     7728   8956   8727    592   -254   -104       C  
ATOM    865  CG1 ILE A 112      40.706   8.291 -17.083  1.00 71.84           C  
ANISOU  865  CG1 ILE A 112     8343   9566   9386    577   -276   -125       C  
ATOM    866  CG2 ILE A 112      42.460  10.039 -16.631  1.00 67.53           C  
ANISOU  866  CG2 ILE A 112     7843   9031   8786    564   -242    -37       C  
ATOM    867  CD1 ILE A 112      39.565   9.224 -16.710  1.00 74.45           C  
ANISOU  867  CD1 ILE A 112     8703   9916   9669    571   -275   -110       C  
ATOM    868  N   LEU A 113      43.840   8.813 -20.231  1.00 66.49           N  
ANISOU  868  N   LEU A 113     7656   8963   8643    670   -217   -168       N  
ATOM    869  CA  LEU A 113      45.167   8.944 -20.827  1.00 68.10           C  
ANISOU  869  CA  LEU A 113     7856   9174   8844    685   -194   -163       C  
ATOM    870  C   LEU A 113      45.159   9.991 -21.955  1.00 67.22           C  
ANISOU  870  C   LEU A 113     7769   9120   8651    726   -165   -168       C  
ATOM    871  O   LEU A 113      45.884  10.985 -21.892  1.00 66.90           O  
ANISOU  871  O   LEU A 113     7752   9086   8581    724   -138   -123       O  
ATOM    872  CB  LEU A 113      45.646   7.570 -21.318  1.00 67.81           C  
ANISOU  872  CB  LEU A 113     7776   9119   8869    694   -206   -214       C  
ATOM    873  CG  LEU A 113      47.034   7.008 -21.004  1.00 68.23           C  
ANISOU  873  CG  LEU A 113     7807   9133   8983    677   -202   -198       C  
ATOM    874  CD1 LEU A 113      47.730   7.687 -19.833  1.00 68.49           C  
ANISOU  874  CD1 LEU A 113     7861   9136   9026    640   -198   -127       C  
ATOM    875  CD2 LEU A 113      46.906   5.519 -20.731  1.00 67.45           C  
ANISOU  875  CD2 LEU A 113     7666   8993   8968    663   -230   -234       C  
ATOM    876  N   ILE A 114      44.309   9.787 -22.958  1.00 68.45           N  
ANISOU  876  N   ILE A 114     7919   9317   8771    763   -170   -221       N  
ATOM    877  CA  ILE A 114      44.139  10.769 -24.032  1.00 68.44           C  
ANISOU  877  CA  ILE A 114     7943   9374   8686    805   -145   -224       C  
ATOM    878  C   ILE A 114      43.952  12.179 -23.486  1.00 70.13           C  
ANISOU  878  C   ILE A 114     8198   9595   8855    793   -128   -161       C  
ATOM    879  O   ILE A 114      44.750  13.076 -23.774  1.00 75.07           O  
ANISOU  879  O   ILE A 114     8843  10233   9447    803    -95   -125       O  
ATOM    880  CB  ILE A 114      42.965  10.407 -24.940  1.00 67.99           C  
ANISOU  880  CB  ILE A 114     7877   9360   8595    843   -163   -288       C  
ATOM    881  CG1 ILE A 114      43.248   9.071 -25.615  1.00 68.12           C  
ANISOU  881  CG1 ILE A 114     7852   9375   8656    859   -176   -356       C  
ATOM    882  CG2 ILE A 114      42.751  11.498 -25.979  1.00 72.41           C  
ANISOU  882  CG2 ILE A 114     8468   9983   9064    888   -138   -282       C  
ATOM    883  CD1 ILE A 114      42.041   8.389 -26.211  1.00 70.00           C  
ANISOU  883  CD1 ILE A 114     8069   9639   8890    885   -204   -427       C  
ATOM    884  N   THR A 115      42.929  12.363 -22.662  1.00 68.47           N  
ANISOU  884  N   THR A 115     7997   9370   8647    770   -149   -149       N  
ATOM    885  CA  THR A 115      42.600  13.697 -22.176  1.00 68.15           C  
ANISOU  885  CA  THR A 115     7993   9338   8565    761   -135    -97       C  
ATOM    886  C   THR A 115      43.701  14.282 -21.311  1.00 67.25           C  
ANISOU  886  C   THR A 115     7890   9189   8472    727   -116    -37       C  
ATOM    887  O   THR A 115      43.920  15.486 -21.339  1.00 71.52           O  
ANISOU  887  O   THR A 115     8457   9744   8974    732    -90      3       O  
ATOM    888  CB  THR A 115      41.249  13.750 -21.417  1.00 68.73           C  
ANISOU  888  CB  THR A 115     8072   9402   8641    741   -160    -99       C  
ATOM    889  OG1 THR A 115      41.384  13.156 -20.115  1.00 66.70           O  
ANISOU  889  OG1 THR A 115     7804   9092   8447    692   -178    -79       O  
ATOM    890  CG2 THR A 115      40.159  13.042 -22.207  1.00 64.93           C  
ANISOU  890  CG2 THR A 115     7573   8948   8149    771   -183   -165       C  
ATOM    891  N   THR A 116      44.386  13.436 -20.542  1.00 70.10           N  
ANISOU  891  N   THR A 116     8229   9506   8899    695   -130    -32       N  
ATOM    892  CA  THR A 116      45.478  13.905 -19.679  1.00 71.65           C  
ANISOU  892  CA  THR A 116     8432   9670   9122    663   -117     20       C  
ATOM    893  C   THR A 116      46.680  14.311 -20.530  1.00 73.92           C  
ANISOU  893  C   THR A 116     8719   9972   9394    687    -83     27       C  
ATOM    894  O   THR A 116      47.378  15.290 -20.231  1.00 76.43           O  
ANISOU  894  O   THR A 116     9054  10284   9703    678    -59     72       O  
ATOM    895  CB  THR A 116      45.914  12.847 -18.648  1.00 68.47           C  
ANISOU  895  CB  THR A 116     8005   9217   8794    625   -144     24       C  
ATOM    896  OG1 THR A 116      44.764  12.344 -17.961  1.00 70.38           O  
ANISOU  896  OG1 THR A 116     8245   9446   9052    606   -173     14       O  
ATOM    897  CG2 THR A 116      46.871  13.449 -17.632  1.00 65.97           C  
ANISOU  897  CG2 THR A 116     7698   8871   8498    592   -136     79       C  
ATOM    898  N   ILE A 117      46.913  13.555 -21.594  1.00 73.77           N  
ANISOU  898  N   ILE A 117     8680   9972   9376    719    -80    -19       N  
ATOM    899  CA  ILE A 117      47.960  13.897 -22.528  1.00 77.44           C  
ANISOU  899  CA  ILE A 117     9145  10457   9822    746    -44    -17       C  
ATOM    900  C   ILE A 117      47.664  15.280 -23.125  1.00 79.74           C  
ANISOU  900  C   ILE A 117     9469  10788  10039    773    -11     11       C  
ATOM    901  O   ILE A 117      48.454  16.211 -22.940  1.00 81.62           O  
ANISOU  901  O   ILE A 117     9722  11019  10273    765     19     56       O  
ATOM    902  CB  ILE A 117      48.162  12.782 -23.571  1.00 77.72           C  
ANISOU  902  CB  ILE A 117     9151  10510   9870    776    -47    -78       C  
ATOM    903  CG1 ILE A 117      49.031  11.674 -22.968  1.00 76.95           C  
ANISOU  903  CG1 ILE A 117     9020  10363   9856    747    -65    -87       C  
ATOM    904  CG2 ILE A 117      48.845  13.309 -24.811  1.00 80.84           C  
ANISOU  904  CG2 ILE A 117     9553  10945  10217    816     -6    -82       C  
ATOM    905  CD1 ILE A 117      49.076  10.394 -23.778  1.00 74.98           C  
ANISOU  905  CD1 ILE A 117     8734  10119   9634    769    -77   -153       C  
ATOM    906  N   ALA A 118      46.512  15.423 -23.783  1.00 82.58           N  
ANISOU  906  N   ALA A 118     9841  11189  10346    803    -18    -15       N  
ATOM    907  CA  ALA A 118      46.075  16.714 -24.334  1.00 81.81           C  
ANISOU  907  CA  ALA A 118     9776  11131  10178    831      9     12       C  
ATOM    908  C   ALA A 118      46.234  17.846 -23.326  1.00 81.35           C  
ANISOU  908  C   ALA A 118     9739  11045  10124    798     22     74       C  
ATOM    909  O   ALA A 118      46.763  18.908 -23.648  1.00 84.66           O  
ANISOU  909  O   ALA A 118    10176  11474  10515    811     60    112       O  
ATOM    910  CB  ALA A 118      44.641  16.630 -24.807  1.00 80.36           C  
ANISOU  910  CB  ALA A 118     9599  10984   9950    857    -14    -23       C  
ATOM    911  N   SER A 119      45.786  17.596 -22.103  1.00 79.44           N  
ANISOU  911  N   SER A 119     9494  10769   9922    757     -9     82       N  
ATOM    912  CA  SER A 119      45.905  18.545 -21.010  1.00 82.94           C  
ANISOU  912  CA  SER A 119     9953  11183  10375    722     -3    133       C  
ATOM    913  C   SER A 119      47.354  18.976 -20.742  1.00 88.54           C  
ANISOU  913  C   SER A 119    10659  11867  11114    706     25    168       C  
ATOM    914  O   SER A 119      47.754  20.088 -21.100  1.00 88.56           O  
ANISOU  914  O   SER A 119    10679  11882  11090    720     62    201       O  
ATOM    915  CB  SER A 119      45.269  17.950 -19.742  1.00 80.70           C  
ANISOU  915  CB  SER A 119     9663  10868  10133    680    -42    129       C  
ATOM    916  OG  SER A 119      45.740  18.574 -18.556  1.00 78.08           O  
ANISOU  916  OG  SER A 119     9339  10503   9826    641    -39    174       O  
ATOM    917  N   LYS A 120      48.131  18.079 -20.137  1.00 95.63           N  
ANISOU  917  N   LYS A 120    11534  12730  12072    679      8    162       N  
ATOM    918  CA  LYS A 120      49.417  18.429 -19.526  1.00101.75           C  
ANISOU  918  CA  LYS A 120    12302  13472  12888    654     24    196       C  
ATOM    919  C   LYS A 120      50.454  18.965 -20.503  1.00105.02           C  
ANISOU  919  C   LYS A 120    12716  13899  13289    682     69    205       C  
ATOM    920  O   LYS A 120      51.135  19.949 -20.209  1.00107.64           O  
ANISOU  920  O   LYS A 120    13055  14217  13627    671     97    243       O  
ATOM    921  CB  LYS A 120      49.994  17.230 -18.767  1.00100.10           C  
ANISOU  921  CB  LYS A 120    12066  13224  12745    625     -8    183       C  
ATOM    922  CG  LYS A 120      50.845  17.596 -17.559  1.00 99.89           C  
ANISOU  922  CG  LYS A 120    12035  13157  12761    585    -13    221       C  
ATOM    923  CD  LYS A 120      52.322  17.698 -17.909  1.00103.32           C  
ANISOU  923  CD  LYS A 120    12453  13577  13226    590     14    229       C  
ATOM    924  CE  LYS A 120      53.205  17.590 -16.671  1.00103.44           C  
ANISOU  924  CE  LYS A 120    12454  13549  13298    551     -5    253       C  
ATOM    925  NZ  LYS A 120      53.094  18.771 -15.770  1.00101.28           N  
ANISOU  925  NZ  LYS A 120    12199  13268  13013    528      0    290       N  
ATOM    926  N   GLY A 121      50.579  18.327 -21.659  1.00103.97           N  
ANISOU  926  N   GLY A 121    12572  13792  13140    717     79    170       N  
ATOM    927  CA  GLY A 121      51.612  18.726 -22.597  1.00112.99           C  
ANISOU  927  CA  GLY A 121    13712  14947  14272    743    125    178       C  
ATOM    928  C   GLY A 121      51.082  19.110 -23.955  1.00118.79           C  
ANISOU  928  C   GLY A 121    14463  15737  14936    794    152    165       C  
ATOM    929  O   GLY A 121      51.412  20.173 -24.488  1.00116.17           O  
ANISOU  929  O   GLY A 121    14148  15420  14570    814    196    198       O  
ATOM    930  N   GLU A 122      50.237  18.242 -24.496  1.00122.92           N  
ANISOU  930  N   GLU A 122    14979  16287  15436    815    126    118       N  
ATOM    931  CA  GLU A 122      49.855  18.294 -25.901  1.00126.83           C  
ANISOU  931  CA  GLU A 122    15484  16839  15867    868    145     92       C  
ATOM    932  C   GLU A 122      49.256  19.599 -26.390  1.00122.67           C  
ANISOU  932  C   GLU A 122    14991  16347  15271    896    173    127       C  
ATOM    933  O   GLU A 122      49.171  19.795 -27.598  1.00130.00           O  
ANISOU  933  O   GLU A 122    15929  17324  16142    943    198    117       O  
ATOM    934  CB  GLU A 122      48.908  17.147 -26.258  1.00137.63           C  
ANISOU  934  CB  GLU A 122    16837  18228  17227    883    105     31       C  
ATOM    935  CG  GLU A 122      49.521  15.764 -26.142  1.00146.73           C  
ANISOU  935  CG  GLU A 122    17952  19354  18443    869     83    -12       C  
ATOM    936  CD  GLU A 122      50.542  15.427 -27.223  1.00158.10           C  
ANISOU  936  CD  GLU A 122    19378  20815  19879    899    116    -35       C  
ATOM    937  OE1 GLU A 122      50.876  16.295 -28.061  1.00166.86           O  
ANISOU  937  OE1 GLU A 122    20506  21958  20934    931    160    -12       O  
ATOM    938  OE2 GLU A 122      51.027  14.274 -27.223  1.00157.41           O  
ANISOU  938  OE2 GLU A 122    19257  20708  19843    891     99    -75       O  
ATOM    939  N   LEU A 123      48.821  20.468 -25.479  1.00111.01           N  
ANISOU  939  N   LEU A 123    13532  14849  13799    869    168    168       N  
ATOM    940  CA  LEU A 123      48.329  21.783 -25.867  1.00111.54           C  
ANISOU  940  CA  LEU A 123    13628  14942  13809    893    197    206       C  
ATOM    941  C   LEU A 123      48.021  21.803 -27.386  1.00112.17           C  
ANISOU  941  C   LEU A 123    13718  15083  13817    953    218    187       C  
ATOM    942  O   LEU A 123      47.006  21.251 -27.827  1.00106.41           O  
ANISOU  942  O   LEU A 123    12989  14388  13054    976    187    145       O  
ATOM    943  CB  LEU A 123      49.367  22.854 -25.484  1.00110.35           C  
ANISOU  943  CB  LEU A 123    13483  14760  13683    875    241    263       C  
ATOM    944  CG  LEU A 123      49.442  23.443 -24.067  1.00109.17           C  
ANISOU  944  CG  LEU A 123    13336  14563  13581    825    229    296       C  
ATOM    945  CD1 LEU A 123      49.873  22.433 -23.011  1.00104.96           C  
ANISOU  945  CD1 LEU A 123    12777  13987  13114    780    191    275       C  
ATOM    946  CD2 LEU A 123      50.379  24.643 -24.060  1.00106.61           C  
ANISOU  946  CD2 LEU A 123    13018  14220  13269    822    280    347       C  
ATOM    947  N   GLN A 124      48.924  22.402 -28.168  1.00114.09           N  
ANISOU  947  N   GLN A 124    13968  15341  14039    979    270    215       N  
ATOM    948  CA  GLN A 124      48.890  22.387 -29.642  1.00112.56           C  
ANISOU  948  CA  GLN A 124    13784  15207  13777   1037    297    200       C  
ATOM    949  C   GLN A 124      49.810  21.306 -30.227  1.00113.85           C  
ANISOU  949  C   GLN A 124    13920  15376  13960   1046    304    157       C  
ATOM    950  O   GLN A 124      49.717  20.963 -31.411  1.00114.45           O  
ANISOU  950  O   GLN A 124    13998  15505  13984   1093    315    127       O  
ATOM    951  CB  GLN A 124      49.288  23.762 -30.204  1.00113.26           C  
ANISOU  951  CB  GLN A 124    13898  15310  13826   1063    356    262       C  
ATOM    952  CG  GLN A 124      50.653  24.286 -29.757  1.00112.53           C  
ANISOU  952  CG  GLN A 124    13797  15171  13790   1034    399    305       C  
ATOM    953  CD  GLN A 124      50.675  24.759 -28.308  1.00113.37           C  
ANISOU  953  CD  GLN A 124    13900  15219  13958    979    382    333       C  
ATOM    954  OE1 GLN A 124      49.678  25.259 -27.788  1.00115.15           O  
ANISOU  954  OE1 GLN A 124    14141  15443  14170    970    359    345       O  
ATOM    955  NE2 GLN A 124      51.815  24.596 -27.651  1.00116.90           N  
ANISOU  955  NE2 GLN A 124    14326  15617  14473    943    392    341       N  
ATOM    956  N   ASN A 125      50.689  20.780 -29.372  1.00113.31           N  
ANISOU  956  N   ASN A 125    13828  15255  13971   1002    296    155       N  
ATOM    957  CA  ASN A 125      51.681  19.751 -29.716  1.00110.02           C  
ANISOU  957  CA  ASN A 125    13382  14830  13592   1002    301    117       C  
ATOM    958  C   ASN A 125      51.107  18.439 -30.275  1.00109.64           C  
ANISOU  958  C   ASN A 125    13314  14811  13532   1022    263     44       C  
ATOM    959  O   ASN A 125      51.852  17.599 -30.793  1.00106.68           O  
ANISOU  959  O   ASN A 125    12915  14441  13180   1031    271      7       O  
ATOM    960  CB  ASN A 125      52.570  19.457 -28.497  1.00107.61           C  
ANISOU  960  CB  ASN A 125    13055  14457  13377    947    289    131       C  
ATOM    961  CG  ASN A 125      53.214  20.712 -27.912  1.00110.45           C  
ANISOU  961  CG  ASN A 125    13427  14784  13755    925    325    196       C  
ATOM    962  OD1 ASN A 125      53.227  20.903 -26.696  1.00107.19           O  
ANISOU  962  OD1 ASN A 125    13011  14326  13390    881    303    217       O  
ATOM    963  ND2 ASN A 125      53.754  21.569 -28.776  1.00112.41           N  
ANISOU  963  ND2 ASN A 125    13689  15054  13967    955    383    227       N  
ATOM    964  N   TRP A 126      49.790  18.264 -30.156  1.00104.04           N  
ANISOU  964  N   TRP A 126    12613  14122  12796   1029    222     21       N  
ATOM    965  CA  TRP A 126      49.091  17.135 -30.765  1.00104.23           C  
ANISOU  965  CA  TRP A 126    12619  14179  12805   1053    186    -51       C  
ATOM    966  C   TRP A 126      48.186  17.697 -31.821  1.00110.49           C  
ANISOU  966  C   TRP A 126    13437  15040  13505   1107    194    -57       C  
ATOM    967  O   TRP A 126      46.989  17.881 -31.585  1.00109.95           O  
ANISOU  967  O   TRP A 126    13380  14984  13413   1110    163    -63       O  
ATOM    968  CB  TRP A 126      48.289  16.367 -29.718  1.00 95.49           C  
ANISOU  968  CB  TRP A 126    11495  13035  11750   1015    130    -78       C  
ATOM    969  CG  TRP A 126      47.876  14.966 -30.121  1.00 85.26           C  
ANISOU  969  CG  TRP A 126    10168  11752  10474   1027     93   -156       C  
ATOM    970  CD1 TRP A 126      47.877  14.407 -31.401  1.00 85.77           C  
ANISOU  970  CD1 TRP A 126    10221  11870  10498   1074     99   -211       C  
ATOM    971  CD2 TRP A 126      47.329  13.906 -29.244  1.00 80.97           C  
ANISOU  971  CD2 TRP A 126     9599  11169   9997    992     43   -191       C  
ATOM    972  NE1 TRP A 126      47.411  13.112 -31.373  1.00 83.97           N  
ANISOU  972  NE1 TRP A 126     9959  11634  10311   1070     57   -280       N  
ATOM    973  CE2 TRP A 126      47.057  12.752 -30.115  1.00 80.09           C  
ANISOU  973  CE2 TRP A 126     9457  11087   9886   1022     23   -269       C  
ATOM    974  CE3 TRP A 126      47.055  13.801 -27.882  1.00 77.97           C  
ANISOU  974  CE3 TRP A 126     9216  10735   9674    942     15   -166       C  
ATOM    975  CZ2 TRP A 126      46.535  11.557 -29.617  1.00 76.50           C  
ANISOU  975  CZ2 TRP A 126     8971  10603   9494   1000    -21   -319       C  
ATOM    976  CZ3 TRP A 126      46.530  12.591 -27.394  1.00 74.50           C  
ANISOU  976  CZ3 TRP A 126     8746  10268   9291    921    -28   -212       C  
ATOM    977  CH2 TRP A 126      46.276  11.499 -28.243  1.00 73.20           C  
ANISOU  977  CH2 TRP A 126     8552  10127   9132    949    -45   -286       C  
ATOM    978  N   PRO A 127      48.746  17.980 -33.009  1.00116.10           N  
ANISOU  978  N   PRO A 127    14155  15796  14160   1152    237    -56       N  
ATOM    979  CA  PRO A 127      48.055  18.774 -34.024  1.00116.43           C  
ANISOU  979  CA  PRO A 127    14227  15904  14106   1206    255    -43       C  
ATOM    980  C   PRO A 127      46.830  18.079 -34.608  1.00115.00           C  
ANISOU  980  C   PRO A 127    14040  15774  13883   1240    209   -110       C  
ATOM    981  O   PRO A 127      45.896  18.748 -35.056  1.00120.76           O  
ANISOU  981  O   PRO A 127    14794  16546  14544   1274    205    -98       O  
ATOM    982  CB  PRO A 127      49.123  18.962 -35.116  1.00119.37           C  
ANISOU  982  CB  PRO A 127    14602  16311  14441   1243    312    -33       C  
ATOM    983  CG  PRO A 127      50.417  18.516 -34.508  1.00119.10           C  
ANISOU  983  CG  PRO A 127    14542  16218  14491   1200    329    -28       C  
ATOM    984  CD  PRO A 127      50.032  17.470 -33.511  1.00117.66           C  
ANISOU  984  CD  PRO A 127    14332  15991  14382   1157    270    -71       C  
ATOM    985  N   ASP A 128      46.831  16.753 -34.583  1.00109.94           N  
ANISOU  985  N   ASP A 128    13363  15124  13285   1230    175   -180       N  
ATOM    986  CA  ASP A 128      45.820  15.977 -35.287  1.00110.62           C  
ANISOU  986  CA  ASP A 128    13436  15260  13336   1266    135   -255       C  
ATOM    987  C   ASP A 128      44.931  15.152 -34.355  1.00108.91           C  
ANISOU  987  C   ASP A 128    13195  15003  13182   1229     77   -296       C  
ATOM    988  O   ASP A 128      44.207  14.255 -34.811  1.00103.33           O  
ANISOU  988  O   ASP A 128    12465  14323  12470   1250     40   -370       O  
ATOM    989  CB  ASP A 128      46.501  15.069 -36.304  1.00117.62           C  
ANISOU  989  CB  ASP A 128    14296  16180  14212   1297    147   -315       C  
ATOM    990  CG  ASP A 128      47.589  14.222 -35.682  1.00122.62           C  
ANISOU  990  CG  ASP A 128    14897  16754  14940   1253    151   -328       C  
ATOM    991  OD1 ASP A 128      48.154  14.632 -34.637  1.00122.73           O  
ANISOU  991  OD1 ASP A 128    14916  16706  15010   1206    162   -271       O  
ATOM    992  OD2 ASP A 128      47.876  13.142 -36.240  1.00127.26           O  
ANISOU  992  OD2 ASP A 128    15452  17355  15546   1267    141   -396       O  
ATOM    993  N   LEU A 129      44.982  15.455 -33.058  1.00102.84           N  
ANISOU  993  N   LEU A 129    12431  14170  12473   1175     70   -249       N  
ATOM    994  CA  LEU A 129      44.080  14.821 -32.096  1.00 98.84           C  
ANISOU  994  CA  LEU A 129    11907  13625  12022   1139     19   -276       C  
ATOM    995  C   LEU A 129      42.627  15.157 -32.427  1.00 97.26           C  
ANISOU  995  C   LEU A 129    11721  13467  11765   1169     -9   -296       C  
ATOM    996  O   LEU A 129      41.833  14.267 -32.763  1.00 95.00           O  
ANISOU  996  O   LEU A 129    11411  13200  11484   1185    -46   -366       O  
ATOM    997  CB  LEU A 129      44.404  15.250 -30.657  1.00 94.27           C  
ANISOU  997  CB  LEU A 129    11337  12978  11505   1080     21   -215       C  
ATOM    998  CG  LEU A 129      43.408  14.843 -29.553  1.00 91.42           C  
ANISOU  998  CG  LEU A 129    10966  12577  11192   1041    -24   -226       C  
ATOM    999  CD1 LEU A 129      43.259  13.328 -29.433  1.00 85.55           C  
ANISOU  999  CD1 LEU A 129    10181  11813  10512   1028    -61   -294       C  
ATOM   1000  CD2 LEU A 129      43.788  15.466 -28.218  1.00 84.93           C  
ANISOU 1000  CD2 LEU A 129    10158  11699  10414    988    -17   -159       C  
ATOM   1001  N   LEU A 130      42.299  16.445 -32.339  1.00 91.17           N  
ANISOU 1001  N   LEU A 130    10987  12709  10946   1177     10   -236       N  
ATOM   1002  CA  LEU A 130      40.941  16.918 -32.578  1.00 89.25           C  
ANISOU 1002  CA  LEU A 130    10759  12502  10651   1203    -14   -246       C  
ATOM   1003  C   LEU A 130      40.406  16.409 -33.924  1.00 93.23           C  
ANISOU 1003  C   LEU A 130    11254  13078  11093   1265    -30   -314       C  
ATOM   1004  O   LEU A 130      39.341  15.788 -33.951  1.00 93.19           O  
ANISOU 1004  O   LEU A 130    11230  13084  11094   1272    -74   -373       O  
ATOM   1005  CB  LEU A 130      40.858  18.446 -32.473  1.00 81.82           C  
ANISOU 1005  CB  LEU A 130     9859  11568   9662   1210     17   -167       C  
ATOM   1006  CG  LEU A 130      41.413  19.125 -31.212  1.00 83.46           C  
ANISOU 1006  CG  LEU A 130    10078  11711   9923   1154     36    -99       C  
ATOM   1007  CD1 LEU A 130      41.602  20.619 -31.428  1.00 81.95           C  
ANISOU 1007  CD1 LEU A 130     9923  11533   9682   1171     79    -25       C  
ATOM   1008  CD2 LEU A 130      40.548  18.880 -29.984  1.00 82.29           C  
ANISOU 1008  CD2 LEU A 130     9921  11517   9829   1108     -3   -106       C  
ATOM   1009  N   PRO A 131      41.154  16.635 -35.036  1.00 98.41           N  
ANISOU 1009  N   PRO A 131    11919  13782  11689   1309      6   -310       N  
ATOM   1010  CA  PRO A 131      40.680  16.158 -36.348  1.00 96.76           C  
ANISOU 1010  CA  PRO A 131    11701  13649  11414   1371     -8   -377       C  
ATOM   1011  C   PRO A 131      40.379  14.660 -36.399  1.00 92.99           C  
ANISOU 1011  C   PRO A 131    11178  13165  10989   1365    -52   -472       C  
ATOM   1012  O   PRO A 131      39.330  14.268 -36.913  1.00 92.08           O  
ANISOU 1012  O   PRO A 131    11051  13091  10845   1397    -90   -534       O  
ATOM   1013  CB  PRO A 131      41.831  16.515 -37.292  1.00 97.37           C  
ANISOU 1013  CB  PRO A 131    11793  13764  11440   1405     45   -351       C  
ATOM   1014  CG  PRO A 131      42.475  17.698 -36.651  1.00 99.25           C  
ANISOU 1014  CG  PRO A 131    12061  13963  11687   1377     89   -255       C  
ATOM   1015  CD  PRO A 131      42.388  17.441 -35.171  1.00 98.53           C  
ANISOU 1015  CD  PRO A 131    11956  13790  11689   1308     64   -241       C  
ATOM   1016  N   LYS A 132      41.274  13.834 -35.862  1.00 93.69           N  
ANISOU 1016  N   LYS A 132    11239  13202  11157   1324    -47   -484       N  
ATOM   1017  CA  LYS A 132      41.039  12.388 -35.848  1.00 97.70           C  
ANISOU 1017  CA  LYS A 132    11699  13695  11726   1315    -85   -571       C  
ATOM   1018  C   LYS A 132      39.851  12.048 -34.953  1.00 94.78           C  
ANISOU 1018  C   LYS A 132    11316  13289  11407   1284   -133   -592       C  
ATOM   1019  O   LYS A 132      38.987  11.243 -35.324  1.00 93.52           O  
ANISOU 1019  O   LYS A 132    11128  13149  11256   1303   -172   -670       O  
ATOM   1020  CB  LYS A 132      42.290  11.615 -35.405  1.00102.70           C  
ANISOU 1020  CB  LYS A 132    12306  14275  12440   1277    -69   -572       C  
ATOM   1021  CG  LYS A 132      42.125  10.091 -35.400  1.00104.54           C  
ANISOU 1021  CG  LYS A 132    12488  14488  12745   1267   -106   -661       C  
ATOM   1022  CD  LYS A 132      42.607   9.414 -36.679  1.00107.22           C  
ANISOU 1022  CD  LYS A 132    12804  14882  13054   1314    -96   -731       C  
ATOM   1023  CE  LYS A 132      44.074   9.012 -36.581  1.00106.15           C  
ANISOU 1023  CE  LYS A 132    12652  14711  12967   1292    -63   -717       C  
ATOM   1024  NZ  LYS A 132      44.480   8.077 -37.666  1.00106.53           N  
ANISOU 1024  NZ  LYS A 132    12666  14801  13010   1329    -61   -800       N  
ATOM   1025  N   LEU A 133      39.817  12.682 -33.783  1.00 92.76           N  
ANISOU 1025  N   LEU A 133    11079  12978  11186   1237   -127   -523       N  
ATOM   1026  CA  LEU A 133      38.749  12.487 -32.806  1.00 90.87           C  
ANISOU 1026  CA  LEU A 133    10832  12699  10995   1202   -165   -530       C  
ATOM   1027  C   LEU A 133      37.370  12.776 -33.414  1.00 91.18           C  
ANISOU 1027  C   LEU A 133    10877  12792  10975   1244   -194   -568       C  
ATOM   1028  O   LEU A 133      36.452  11.957 -33.296  1.00 90.06           O  
ANISOU 1028  O   LEU A 133    10705  12643  10870   1241   -234   -632       O  
ATOM   1029  CB  LEU A 133      39.013  13.354 -31.568  1.00 87.32           C  
ANISOU 1029  CB  LEU A 133    10410  12196  10573   1152   -147   -444       C  
ATOM   1030  CG  LEU A 133      38.942  12.732 -30.167  1.00 83.56           C  
ANISOU 1030  CG  LEU A 133     9914  11644  10192   1089   -168   -435       C  
ATOM   1031  CD1 LEU A 133      39.466  11.304 -30.121  1.00 79.65           C  
ANISOU 1031  CD1 LEU A 133     9375  11119   9770   1073   -182   -489       C  
ATOM   1032  CD2 LEU A 133      39.701  13.604 -29.182  1.00 82.60           C  
ANISOU 1032  CD2 LEU A 133     9819  11479  10087   1048   -139   -349       C  
ATOM   1033  N   CYS A 134      37.245  13.921 -34.088  1.00 92.41           N  
ANISOU 1033  N   CYS A 134    11071  13001  11041   1285   -172   -529       N  
ATOM   1034  CA  CYS A 134      36.011  14.288 -34.797  1.00 96.01           C  
ANISOU 1034  CA  CYS A 134    11534  13514  11429   1333   -199   -561       C  
ATOM   1035  C   CYS A 134      35.563  13.222 -35.790  1.00 98.11           C  
ANISOU 1035  C   CYS A 134    11765  13828  11683   1376   -231   -662       C  
ATOM   1036  O   CYS A 134      34.415  12.787 -35.762  1.00 97.72           O  
ANISOU 1036  O   CYS A 134    11695  13785  11649   1382   -274   -719       O  
ATOM   1037  CB  CYS A 134      36.177  15.623 -35.518  1.00 95.98           C  
ANISOU 1037  CB  CYS A 134    11576  13564  11330   1376   -165   -500       C  
ATOM   1038  SG  CYS A 134      36.189  17.042 -34.406  1.00103.31           S  
ANISOU 1038  SG  CYS A 134    12544  14444  12266   1335   -138   -393       S  
ATOM   1039  N   SER A 135      36.481  12.802 -36.660  1.00105.31           N  
ANISOU 1039  N   SER A 135    12669  14774  12572   1404   -210   -688       N  
ATOM   1040  CA  SER A 135      36.208  11.773 -37.668  1.00104.03           C  
ANISOU 1040  CA  SER A 135    12470  14661  12396   1446   -238   -789       C  
ATOM   1041  C   SER A 135      35.854  10.443 -37.017  1.00101.33           C  
ANISOU 1041  C   SER A 135    12077  14264  12160   1407   -275   -857       C  
ATOM   1042  O   SER A 135      35.090   9.651 -37.572  1.00101.53           O  
ANISOU 1042  O   SER A 135    12069  14319  12190   1435   -313   -947       O  
ATOM   1043  CB  SER A 135      37.406  11.614 -38.606  1.00102.79           C  
ANISOU 1043  CB  SER A 135    12313  14542  12198   1477   -201   -795       C  
ATOM   1044  OG  SER A 135      38.619  11.776 -37.894  1.00 98.37           O  
ANISOU 1044  OG  SER A 135    11763  13926  11688   1431   -161   -730       O  
ATOM   1045  N   LEU A 136      36.405  10.217 -35.828  1.00102.44           N  
ANISOU 1045  N   LEU A 136    12212  14324  12385   1344   -264   -814       N  
ATOM   1046  CA  LEU A 136      36.083   9.039 -35.036  1.00104.99           C  
ANISOU 1046  CA  LEU A 136    12490  14585  12815   1300   -296   -862       C  
ATOM   1047  C   LEU A 136      34.635   9.015 -34.541  1.00107.42           C  
ANISOU 1047  C   LEU A 136    12790  14880  13144   1291   -335   -886       C  
ATOM   1048  O   LEU A 136      34.131   7.960 -34.150  1.00110.02           O  
ANISOU 1048  O   LEU A 136    13077  15171  13554   1269   -365   -944       O  
ATOM   1049  CB  LEU A 136      37.051   8.904 -33.867  1.00103.99           C  
ANISOU 1049  CB  LEU A 136    12366  14380  12767   1238   -273   -799       C  
ATOM   1050  CG  LEU A 136      38.343   8.158 -34.194  1.00106.16           C  
ANISOU 1050  CG  LEU A 136    12617  14643  13075   1235   -252   -818       C  
ATOM   1051  CD1 LEU A 136      39.440   8.569 -33.227  1.00104.39           C  
ANISOU 1051  CD1 LEU A 136    12412  14361  12889   1186   -219   -732       C  
ATOM   1052  CD2 LEU A 136      38.123   6.648 -34.172  1.00104.44           C  
ANISOU 1052  CD2 LEU A 136    12342  14397  12944   1224   -284   -905       C  
ATOM   1053  N   LEU A 137      33.973  10.172 -34.560  1.00106.35           N  
ANISOU 1053  N   LEU A 137    12693  14774  12943   1308   -333   -841       N  
ATOM   1054  CA  LEU A 137      32.527  10.247 -34.302  1.00105.99           C  
ANISOU 1054  CA  LEU A 137    12640  14729  12903   1310   -371   -870       C  
ATOM   1055  C   LEU A 137      31.720   9.551 -35.393  1.00108.05           C  
ANISOU 1055  C   LEU A 137    12867  15047  13140   1363   -408   -975       C  
ATOM   1056  O   LEU A 137      30.712   8.895 -35.109  1.00106.19           O  
ANISOU 1056  O   LEU A 137    12597  14791  12958   1353   -445  -1034       O  
ATOM   1057  CB  LEU A 137      32.072  11.702 -34.190  1.00104.33           C  
ANISOU 1057  CB  LEU A 137    12478  14541  12621   1321   -358   -799       C  
ATOM   1058  CG  LEU A 137      32.059  12.433 -32.840  1.00103.93           C  
ANISOU 1058  CG  LEU A 137    12454  14429  12608   1264   -342   -715       C  
ATOM   1059  CD1 LEU A 137      32.762  11.665 -31.727  1.00102.53           C  
ANISOU 1059  CD1 LEU A 137    12256  14173  12527   1201   -334   -698       C  
ATOM   1060  CD2 LEU A 137      32.632  13.836 -32.992  1.00 96.09           C  
ANISOU 1060  CD2 LEU A 137    11511  13459  11541   1278   -303   -628       C  
ATOM   1061  N   ASP A 138      32.182   9.698 -36.637  1.00110.89           N  
ANISOU 1061  N   ASP A 138    13235  15480  13419   1420   -397   -998       N  
ATOM   1062  CA  ASP A 138      31.499   9.150 -37.816  1.00111.10           C  
ANISOU 1062  CA  ASP A 138    13234  15576  13405   1479   -432  -1098       C  
ATOM   1063  C   ASP A 138      31.597   7.630 -37.885  1.00108.62           C  
ANISOU 1063  C   ASP A 138    12859  15235  13178   1467   -455  -1192       C  
ATOM   1064  O   ASP A 138      30.866   6.992 -38.645  1.00103.11           O  
ANISOU 1064  O   ASP A 138    12126  14579  12472   1506   -491  -1288       O  
ATOM   1065  CB  ASP A 138      32.066   9.759 -39.109  1.00110.61           C  
ANISOU 1065  CB  ASP A 138    13200  15600  13227   1544   -409  -1090       C  
ATOM   1066  CG  ASP A 138      32.193  11.280 -39.049  1.00111.05           C  
ANISOU 1066  CG  ASP A 138    13316  15676  13203   1554   -377   -986       C  
ATOM   1067  OD1 ASP A 138      31.323  11.947 -38.442  1.00109.52           O  
ANISOU 1067  OD1 ASP A 138    13138  15462  13011   1540   -391   -951       O  
ATOM   1068  OD2 ASP A 138      33.169  11.809 -39.624  1.00107.64           O  
ANISOU 1068  OD2 ASP A 138    12911  15277  12708   1577   -336   -941       O  
ATOM   1069  N   SER A 139      32.500   7.063 -37.084  1.00107.67           N  
ANISOU 1069  N   SER A 139    12725  15044  13140   1414   -434  -1165       N  
ATOM   1070  CA  SER A 139      32.773   5.625 -37.075  1.00107.92           C  
ANISOU 1070  CA  SER A 139    12700  15042  13265   1398   -449  -1243       C  
ATOM   1071  C   SER A 139      31.531   4.759 -36.844  1.00104.86           C  
ANISOU 1071  C   SER A 139    12264  14630  12949   1390   -496  -1326       C  
ATOM   1072  O   SER A 139      30.462   5.258 -36.487  1.00 98.60           O  
ANISOU 1072  O   SER A 139    11482  13836  12146   1388   -516  -1315       O  
ATOM   1073  CB  SER A 139      33.858   5.289 -36.043  1.00107.68           C  
ANISOU 1073  CB  SER A 139    12667  14929  13316   1336   -420  -1184       C  
ATOM   1074  OG  SER A 139      33.345   5.328 -34.721  1.00106.09           O  
ANISOU 1074  OG  SER A 139    12467  14656  13186   1280   -428  -1139       O  
ATOM   1075  N   GLU A 140      31.697   3.457 -37.053  1.00107.72           N  
ANISOU 1075  N   GLU A 140    12570  14971  13388   1387   -511  -1409       N  
ATOM   1076  CA  GLU A 140      30.604   2.504 -36.957  1.00112.33           C  
ANISOU 1076  CA  GLU A 140    13100  15532  14049   1383   -554  -1499       C  
ATOM   1077  C   GLU A 140      30.354   2.047 -35.527  1.00110.06           C  
ANISOU 1077  C   GLU A 140    12795  15145  13877   1313   -555  -1463       C  
ATOM   1078  O   GLU A 140      29.258   2.246 -35.006  1.00109.53           O  
ANISOU 1078  O   GLU A 140    12727  15059  13831   1300   -575  -1463       O  
ATOM   1079  CB  GLU A 140      30.845   1.304 -37.894  1.00121.26           C  
ANISOU 1079  CB  GLU A 140    14173  16688  15212   1414   -571  -1612       C  
ATOM   1080  CG  GLU A 140      30.022   0.046 -37.597  1.00128.47           C  
ANISOU 1080  CG  GLU A 140    15018  17551  16244   1395   -606  -1704       C  
ATOM   1081  CD  GLU A 140      28.556   0.326 -37.278  1.00131.21           C  
ANISOU 1081  CD  GLU A 140    15361  17895  16598   1396   -639  -1722       C  
ATOM   1082  OE1 GLU A 140      28.085  -0.134 -36.214  1.00129.71           O  
ANISOU 1082  OE1 GLU A 140    15149  17625  16509   1344   -644  -1709       O  
ATOM   1083  OE2 GLU A 140      27.877   1.014 -38.074  1.00133.50           O  
ANISOU 1083  OE2 GLU A 140    15670  18262  16792   1448   -658  -1747       O  
ATOM   1084  N   ASP A 141      31.363   1.439 -34.905  1.00110.88           N  
ANISOU 1084  N   ASP A 141    12886  15186  14055   1271   -532  -1432       N  
ATOM   1085  CA  ASP A 141      31.208   0.801 -33.592  1.00114.46           C  
ANISOU 1085  CA  ASP A 141    13317  15544  14627   1207   -534  -1405       C  
ATOM   1086  C   ASP A 141      30.745   1.788 -32.517  1.00107.73           C  
ANISOU 1086  C   ASP A 141    12511  14663  13759   1171   -524  -1311       C  
ATOM   1087  O   ASP A 141      31.321   2.871 -32.373  1.00102.25           O  
ANISOU 1087  O   ASP A 141    11870  13987  12991   1169   -498  -1227       O  
ATOM   1088  CB  ASP A 141      32.512   0.105 -33.171  1.00117.74           C  
ANISOU 1088  CB  ASP A 141    13717  15906  15111   1173   -510  -1378       C  
ATOM   1089  CG  ASP A 141      32.439  -0.487 -31.768  1.00120.45           C  
ANISOU 1089  CG  ASP A 141    14044  16153  15570   1107   -509  -1336       C  
ATOM   1090  OD1 ASP A 141      31.592  -1.376 -31.540  1.00121.27           O  
ANISOU 1090  OD1 ASP A 141    14099  16219  15757   1096   -534  -1396       O  
ATOM   1091  OD2 ASP A 141      33.233  -0.062 -30.896  1.00120.30           O  
ANISOU 1091  OD2 ASP A 141    14058  16095  15557   1069   -483  -1242       O  
ATOM   1092  N   TYR A 142      29.703   1.403 -31.776  1.00105.63           N  
ANISOU 1092  N   TYR A 142    12221  14350  13563   1142   -545  -1327       N  
ATOM   1093  CA  TYR A 142      29.088   2.282 -30.776  1.00103.97           C  
ANISOU 1093  CA  TYR A 142    12049  14114  13341   1109   -538  -1251       C  
ATOM   1094  C   TYR A 142      30.128   2.817 -29.791  1.00101.38           C  
ANISOU 1094  C   TYR A 142    11762  13744  13014   1064   -503  -1141       C  
ATOM   1095  O   TYR A 142      30.292   4.037 -29.646  1.00 93.62           O  
ANISOU 1095  O   TYR A 142    10831  12787  11952   1066   -485  -1069       O  
ATOM   1096  CB  TYR A 142      27.947   1.574 -30.026  1.00104.94           C  
ANISOU 1096  CB  TYR A 142    12132  14179  13559   1078   -560  -1286       C  
ATOM   1097  CG  TYR A 142      27.456   2.342 -28.807  1.00110.07           C  
ANISOU 1097  CG  TYR A 142    12818  14791  14213   1034   -549  -1203       C  
ATOM   1098  CD1 TYR A 142      26.495   3.349 -28.929  1.00109.57           C  
ANISOU 1098  CD1 TYR A 142    12782  14766  14081   1053   -558  -1194       C  
ATOM   1099  CD2 TYR A 142      27.965   2.073 -27.532  1.00109.78           C  
ANISOU 1099  CD2 TYR A 142    12787  14681  14245    975   -528  -1132       C  
ATOM   1100  CE1 TYR A 142      26.053   4.058 -27.820  1.00107.58           C  
ANISOU 1100  CE1 TYR A 142    12562  14480  13833   1013   -546  -1121       C  
ATOM   1101  CE2 TYR A 142      27.530   2.780 -26.420  1.00105.93           C  
ANISOU 1101  CE2 TYR A 142    12332  14162  13756    936   -517  -1059       C  
ATOM   1102  CZ  TYR A 142      26.576   3.770 -26.568  1.00106.75           C  
ANISOU 1102  CZ  TYR A 142    12462  14305  13794    954   -525  -1054       C  
ATOM   1103  OH  TYR A 142      26.143   4.471 -25.462  1.00106.99           O  
ANISOU 1103  OH  TYR A 142    12523  14305  13825    915   -512   -985       O  
ATOM   1104  N   ASN A 143      30.830   1.889 -29.137  1.00 98.25           N  
ANISOU 1104  N   ASN A 143    11339  13283  12709   1025   -495  -1130       N  
ATOM   1105  CA  ASN A 143      31.851   2.216 -28.142  1.00 91.32           C  
ANISOU 1105  CA  ASN A 143    10492  12359  11846    980   -466  -1033       C  
ATOM   1106  C   ASN A 143      32.880   3.211 -28.651  1.00 88.52           C  
ANISOU 1106  C   ASN A 143    10183  12053  11398   1002   -440   -982       C  
ATOM   1107  O   ASN A 143      33.338   4.084 -27.904  1.00 86.73           O  
ANISOU 1107  O   ASN A 143     9999  11811  11144    975   -418   -893       O  
ATOM   1108  CB  ASN A 143      32.541   0.945 -27.661  1.00 90.43           C  
ANISOU 1108  CB  ASN A 143    10336  12181  11841    947   -465  -1045       C  
ATOM   1109  CG  ASN A 143      31.654   0.112 -26.762  1.00 89.43           C  
ANISOU 1109  CG  ASN A 143    10174  11989  11816    910   -481  -1061       C  
ATOM   1110  OD1 ASN A 143      30.792   0.642 -26.065  1.00 91.67           O  
ANISOU 1110  OD1 ASN A 143    10478  12261  12092    890   -483  -1028       O  
ATOM   1111  ND2 ASN A 143      31.865  -1.198 -26.767  1.00 88.28           N  
ANISOU 1111  ND2 ASN A 143     9975  11799  11769    900   -490  -1111       N  
ATOM   1112  N   THR A 144      33.205   3.089 -29.934  1.00 85.17           N  
ANISOU 1112  N   THR A 144     9749  11688  10925   1052   -441  -1039       N  
ATOM   1113  CA  THR A 144      34.192   3.941 -30.581  1.00 87.85           C  
ANISOU 1113  CA  THR A 144    10125  12076  11176   1080   -413   -999       C  
ATOM   1114  C   THR A 144      33.754   5.409 -30.597  1.00 86.58           C  
ANISOU 1114  C   THR A 144    10020  11957  10920   1094   -403   -941       C  
ATOM   1115  O   THR A 144      34.520   6.301 -30.200  1.00 81.37           O  
ANISOU 1115  O   THR A 144     9400  11291  10224   1079   -373   -858       O  
ATOM   1116  CB  THR A 144      34.498   3.435 -32.010  1.00 92.35           C  
ANISOU 1116  CB  THR A 144    10670  12706  11713   1134   -418  -1083       C  
ATOM   1117  OG1 THR A 144      34.688   2.013 -31.980  1.00 90.95           O  
ANISOU 1117  OG1 THR A 144    10435  12486  11635   1121   -433  -1149       O  
ATOM   1118  CG2 THR A 144      35.750   4.107 -32.580  1.00 88.87           C  
ANISOU 1118  CG2 THR A 144    10263  12303  11201   1155   -382  -1038       C  
ATOM   1119  N   CYS A 145      32.519   5.654 -31.039  1.00 92.93           N  
ANISOU 1119  N   CYS A 145    10821  12799  11687   1124   -428   -984       N  
ATOM   1120  CA  CYS A 145      31.979   7.017 -31.079  1.00 89.74           C  
ANISOU 1120  CA  CYS A 145    10466  12434  11198   1141   -421   -934       C  
ATOM   1121  C   CYS A 145      31.751   7.556 -29.664  1.00 83.77           C  
ANISOU 1121  C   CYS A 145     9734  11620  10477   1085   -412   -855       C  
ATOM   1122  O   CYS A 145      32.104   8.697 -29.366  1.00 79.53           O  
ANISOU 1122  O   CYS A 145     9241  11089   9886   1078   -387   -778       O  
ATOM   1123  CB  CYS A 145      30.724   7.098 -31.962  1.00 97.93           C  
ANISOU 1123  CB  CYS A 145    11492  13530  12189   1191   -453  -1005       C  
ATOM   1124  SG  CYS A 145      29.136   6.642 -31.222  1.00105.42           S  
ANISOU 1124  SG  CYS A 145    12408  14437  13208   1166   -490  -1048       S  
ATOM   1125  N   GLU A 146      31.210   6.707 -28.792  1.00 81.87           N  
ANISOU 1125  N   GLU A 146     9460  11318  10327   1044   -429   -875       N  
ATOM   1126  CA  GLU A 146      31.060   7.027 -27.374  1.00 86.08           C  
ANISOU 1126  CA  GLU A 146    10012  11793  10903    988   -420   -805       C  
ATOM   1127  C   GLU A 146      32.386   7.456 -26.733  1.00 84.62           C  
ANISOU 1127  C   GLU A 146     9856  11580  10716    956   -388   -721       C  
ATOM   1128  O   GLU A 146      32.459   8.507 -26.080  1.00 80.22           O  
ANISOU 1128  O   GLU A 146     9338  11017  10125    936   -370   -649       O  
ATOM   1129  CB  GLU A 146      30.487   5.826 -26.626  1.00 91.72           C  
ANISOU 1129  CB  GLU A 146    10680  12445  11723    951   -440   -843       C  
ATOM   1130  CG  GLU A 146      30.077   6.140 -25.200  1.00 97.23           C  
ANISOU 1130  CG  GLU A 146    11395  13088  12459    897   -433   -779       C  
ATOM   1131  CD  GLU A 146      30.380   5.006 -24.242  1.00104.46           C  
ANISOU 1131  CD  GLU A 146    12278  13930  13479    849   -434   -772       C  
ATOM   1132  OE1 GLU A 146      29.584   4.042 -24.194  1.00104.44           O  
ANISOU 1132  OE1 GLU A 146    12233  13902  13546    844   -454   -832       O  
ATOM   1133  OE2 GLU A 146      31.412   5.088 -23.533  1.00107.12           O  
ANISOU 1133  OE2 GLU A 146    12633  14236  13832    817   -414   -707       O  
ATOM   1134  N   GLY A 147      33.425   6.640 -26.933  1.00 82.55           N  
ANISOU 1134  N   GLY A 147     9571  11300  10494    952   -381   -736       N  
ATOM   1135  CA  GLY A 147      34.755   6.908 -26.388  1.00 75.99           C  
ANISOU 1135  CA  GLY A 147     8761  10442   9671    925   -352   -666       C  
ATOM   1136  C   GLY A 147      35.322   8.217 -26.892  1.00 75.62           C  
ANISOU 1136  C   GLY A 147     8760  10443   9531    950   -325   -616       C  
ATOM   1137  O   GLY A 147      35.895   9.004 -26.121  1.00 76.20           O  
ANISOU 1137  O   GLY A 147     8864  10494   9594    921   -303   -539       O  
ATOM   1138  N   ALA A 148      35.149   8.458 -28.189  1.00 73.54           N  
ANISOU 1138  N   ALA A 148     8498  10245   9199   1006   -326   -659       N  
ATOM   1139  CA  ALA A 148      35.639   9.687 -28.808  1.00 75.36           C  
ANISOU 1139  CA  ALA A 148     8770  10525   9338   1036   -297   -614       C  
ATOM   1140  C   ALA A 148      34.924  10.932 -28.266  1.00 73.53           C  
ANISOU 1140  C   ALA A 148     8578  10298   9063   1027   -292   -557       C  
ATOM   1141  O   ALA A 148      35.569  11.928 -27.921  1.00 74.85           O  
ANISOU 1141  O   ALA A 148     8779  10460   9199   1015   -263   -484       O  
ATOM   1142  CB  ALA A 148      35.521   9.598 -30.324  1.00 79.45           C  
ANISOU 1142  CB  ALA A 148     9281  11115   9790   1101   -301   -676       C  
ATOM   1143  N   PHE A 149      33.598  10.859 -28.167  1.00 72.37           N  
ANISOU 1143  N   PHE A 149     8422  10157   8920   1032   -321   -592       N  
ATOM   1144  CA  PHE A 149      32.801  11.956 -27.596  1.00 75.97           C  
ANISOU 1144  CA  PHE A 149     8909  10612   9344   1021   -320   -545       C  
ATOM   1145  C   PHE A 149      33.211  12.304 -26.164  1.00 74.51           C  
ANISOU 1145  C   PHE A 149     8741  10366   9203    960   -303   -472       C  
ATOM   1146  O   PHE A 149      33.375  13.494 -25.815  1.00 68.89           O  
ANISOU 1146  O   PHE A 149     8065   9658   8451    953   -282   -408       O  
ATOM   1147  CB  PHE A 149      31.308  11.617 -27.635  1.00 79.47           C  
ANISOU 1147  CB  PHE A 149     9332  11063   9801   1031   -355   -603       C  
ATOM   1148  CG  PHE A 149      30.508  12.466 -28.586  1.00 83.37           C  
ANISOU 1148  CG  PHE A 149     9844  11621  10211   1084   -363   -620       C  
ATOM   1149  CD1 PHE A 149      30.812  13.813 -28.774  1.00 83.31           C  
ANISOU 1149  CD1 PHE A 149     9881  11643  10131   1100   -337   -554       C  
ATOM   1150  CD2 PHE A 149      29.418  11.930 -29.265  1.00 86.62           C  
ANISOU 1150  CD2 PHE A 149    10228  12065  10620   1118   -399   -700       C  
ATOM   1151  CE1 PHE A 149      30.063  14.605 -29.637  1.00 84.45           C  
ANISOU 1151  CE1 PHE A 149    10042  11846  10199   1151   -345   -564       C  
ATOM   1152  CE2 PHE A 149      28.665  12.719 -30.129  1.00 88.83           C  
ANISOU 1152  CE2 PHE A 149    10524  12406  10820   1170   -410   -714       C  
ATOM   1153  CZ  PHE A 149      28.986  14.058 -30.312  1.00 87.44           C  
ANISOU 1153  CZ  PHE A 149    10394  12258  10570   1187   -383   -643       C  
ATOM   1154  N   GLY A 150      33.371  11.254 -25.349  1.00 72.51           N  
ANISOU 1154  N   GLY A 150     8458  10058   9033    919   -315   -484       N  
ATOM   1155  CA  GLY A 150      33.795  11.381 -23.959  1.00 69.94           C  
ANISOU 1155  CA  GLY A 150     8144   9675   8754    862   -304   -421       C  
ATOM   1156  C   GLY A 150      35.063  12.189 -23.875  1.00 70.64           C  
ANISOU 1156  C   GLY A 150     8262   9765   8812    856   -271   -357       C  
ATOM   1157  O   GLY A 150      35.189  13.093 -23.037  1.00 70.94           O  
ANISOU 1157  O   GLY A 150     8328   9785   8839    828   -256   -294       O  
ATOM   1158  N   ALA A 151      35.988  11.884 -24.780  1.00 72.25           N  
ANISOU 1158  N   ALA A 151     8457   9992   9001    885   -259   -375       N  
ATOM   1159  CA  ALA A 151      37.268  12.583 -24.842  1.00 73.06           C  
ANISOU 1159  CA  ALA A 151     8583  10097   9078    884   -225   -320       C  
ATOM   1160  C   ALA A 151      37.075  14.057 -25.182  1.00 71.63           C  
ANISOU 1160  C   ALA A 151     8442   9955   8820    907   -203   -277       C  
ATOM   1161  O   ALA A 151      37.571  14.950 -24.469  1.00 66.96           O  
ANISOU 1161  O   ALA A 151     7876   9343   8224    881   -182   -212       O  
ATOM   1162  CB  ALA A 151      38.189  11.908 -25.852  1.00 76.14           C  
ANISOU 1162  CB  ALA A 151     8953  10508   9468    914   -217   -357       C  
ATOM   1163  N   LEU A 152      36.336  14.301 -26.262  1.00 70.71           N  
ANISOU 1163  N   LEU A 152     8329   9892   8644    957   -210   -314       N  
ATOM   1164  CA  LEU A 152      36.037  15.664 -26.704  1.00 70.98           C  
ANISOU 1164  CA  LEU A 152     8399   9966   8603    986   -191   -276       C  
ATOM   1165  C   LEU A 152      35.411  16.510 -25.593  1.00 67.00           C  
ANISOU 1165  C   LEU A 152     7916   9432   8108    949   -192   -228       C  
ATOM   1166  O   LEU A 152      35.872  17.640 -25.314  1.00 61.31           O  
ANISOU 1166  O   LEU A 152     7225   8709   7362    942   -163   -166       O  
ATOM   1167  CB  LEU A 152      35.132  15.619 -27.929  1.00 76.35           C  
ANISOU 1167  CB  LEU A 152     9076  10708   9225   1043   -209   -332       C  
ATOM   1168  CG  LEU A 152      35.766  14.978 -29.169  1.00 77.78           C  
ANISOU 1168  CG  LEU A 152     9241  10931   9381   1087   -204   -378       C  
ATOM   1169  CD1 LEU A 152      34.720  14.225 -29.972  1.00 78.30           C  
ANISOU 1169  CD1 LEU A 152     9281  11036   9433   1125   -241   -462       C  
ATOM   1170  CD2 LEU A 152      36.468  16.019 -30.025  1.00 75.57           C  
ANISOU 1170  CD2 LEU A 152     8993  10696   9024   1126   -165   -333       C  
ATOM   1171  N   GLN A 153      34.390  15.939 -24.944  1.00 67.63           N  
ANISOU 1171  N   GLN A 153     7979   9490   8229    926   -223   -259       N  
ATOM   1172  CA  GLN A 153      33.681  16.609 -23.846  1.00 65.04           C  
ANISOU 1172  CA  GLN A 153     7665   9132   7913    890   -226   -223       C  
ATOM   1173  C   GLN A 153      34.656  17.101 -22.805  1.00 64.22           C  
ANISOU 1173  C   GLN A 153     7579   8988   7836    845   -202   -156       C  
ATOM   1174  O   GLN A 153      34.646  18.281 -22.439  1.00 63.49           O  
ANISOU 1174  O   GLN A 153     7513   8895   7715    837   -183   -107       O  
ATOM   1175  CB  GLN A 153      32.628  15.695 -23.201  1.00 64.25           C  
ANISOU 1175  CB  GLN A 153     7539   9004   7868    865   -259   -266       C  
ATOM   1176  CG  GLN A 153      31.625  16.463 -22.343  1.00 65.00           C  
ANISOU 1176  CG  GLN A 153     7649   9085   7961    840   -263   -241       C  
ATOM   1177  CD  GLN A 153      30.684  15.569 -21.551  1.00 64.38           C  
ANISOU 1177  CD  GLN A 153     7545   8971   7944    808   -289   -276       C  
ATOM   1178  OE1 GLN A 153      30.015  14.690 -22.100  1.00 65.51           O  
ANISOU 1178  OE1 GLN A 153     7660   9125   8107    828   -313   -340       O  
ATOM   1179  NE2 GLN A 153      30.614  15.807 -20.251  1.00 58.70           N  
ANISOU 1179  NE2 GLN A 153     6835   8211   7258    758   -282   -234       N  
ATOM   1180  N   LYS A 154      35.515  16.189 -22.351  1.00 65.82           N  
ANISOU 1180  N   LYS A 154     7762   9156   8092    817   -203   -158       N  
ATOM   1181  CA  LYS A 154      36.540  16.514 -21.361  1.00 64.95           C  
ANISOU 1181  CA  LYS A 154     7662   9006   8010    776   -184   -101       C  
ATOM   1182  C   LYS A 154      37.516  17.581 -21.864  1.00 65.85           C  
ANISOU 1182  C   LYS A 154     7799   9139   8080    795   -148    -56       C  
ATOM   1183  O   LYS A 154      37.915  18.484 -21.112  1.00 65.00           O  
ANISOU 1183  O   LYS A 154     7712   9012   7973    769   -130     -3       O  
ATOM   1184  CB  LYS A 154      37.291  15.245 -20.932  1.00 63.39           C  
ANISOU 1184  CB  LYS A 154     7436   8770   7879    749   -195   -115       C  
ATOM   1185  CG  LYS A 154      38.298  15.457 -19.811  1.00 61.22           C  
ANISOU 1185  CG  LYS A 154     7168   8453   7639    705   -183    -60       C  
ATOM   1186  CD  LYS A 154      37.618  15.815 -18.508  1.00 63.50           C  
ANISOU 1186  CD  LYS A 154     7469   8715   7945    663   -192    -30       C  
ATOM   1187  CE  LYS A 154      38.560  15.648 -17.328  1.00 62.99           C  
ANISOU 1187  CE  LYS A 154     7403   8606   7925    618   -190     12       C  
ATOM   1188  NZ  LYS A 154      39.138  16.955 -16.929  1.00 60.90           N  
ANISOU 1188  NZ  LYS A 154     7165   8343   7632    608   -165     65       N  
ATOM   1189  N   ILE A 155      37.896  17.489 -23.135  1.00 70.34           N  
ANISOU 1189  N   ILE A 155     8366   9748   8612    841   -137    -79       N  
ATOM   1190  CA  ILE A 155      38.818  18.476 -23.700  1.00 75.45           C  
ANISOU 1190  CA  ILE A 155     9035  10414   9218    862    -98    -37       C  
ATOM   1191  C   ILE A 155      38.185  19.862 -23.606  1.00 77.33           C  
ANISOU 1191  C   ILE A 155     9303  10668   9411    870    -84      3       C  
ATOM   1192  O   ILE A 155      38.784  20.799 -23.078  1.00 75.68           O  
ANISOU 1192  O   ILE A 155     9111  10440   9204    850    -58     57       O  
ATOM   1193  CB  ILE A 155      39.249  18.121 -25.140  1.00 78.97           C  
ANISOU 1193  CB  ILE A 155     9474  10906   9625    914    -87    -71       C  
ATOM   1194  CG1 ILE A 155      40.159  16.886 -25.118  1.00 79.87           C  
ANISOU 1194  CG1 ILE A 155     9559  10997   9793    900    -93   -100       C  
ATOM   1195  CG2 ILE A 155      39.979  19.297 -25.783  1.00 79.06           C  
ANISOU 1195  CG2 ILE A 155     9511  10942   9585    941    -43    -22       C  
ATOM   1196  CD1 ILE A 155      40.006  15.978 -26.320  1.00 81.71           C  
ANISOU 1196  CD1 ILE A 155     9769  11268  10008    944   -105   -166       C  
ATOM   1197  N   CYS A 156      36.942  19.970 -24.057  1.00 79.97           N  
ANISOU 1197  N   CYS A 156     9641  11034   9712    897   -104    -27       N  
ATOM   1198  CA  CYS A 156      36.222  21.233 -23.947  1.00 79.40           C  
ANISOU 1198  CA  CYS A 156     9593  10973   9601    905    -94      7       C  
ATOM   1199  C   CYS A 156      36.061  21.740 -22.517  1.00 80.21           C  
ANISOU 1199  C   CYS A 156     9704  11031   9743    851    -95     44       C  
ATOM   1200  O   CYS A 156      36.046  22.941 -22.282  1.00 81.64           O  
ANISOU 1200  O   CYS A 156     9906  11210   9904    848    -73     89       O  
ATOM   1201  CB  CYS A 156      34.878  21.113 -24.624  1.00 77.58           C  
ANISOU 1201  CB  CYS A 156     9361  10782   9335    941   -121    -38       C  
ATOM   1202  SG  CYS A 156      35.087  20.863 -26.389  1.00 81.10           S  
ANISOU 1202  SG  CYS A 156     9805  11293   9716   1013   -116    -73       S  
ATOM   1203  N   GLU A 157      35.961  20.836 -21.555  1.00 80.35           N  
ANISOU 1203  N   GLU A 157     9702  11010   9815    809   -118     27       N  
ATOM   1204  CA  GLU A 157      35.775  21.274 -20.181  1.00 84.27           C  
ANISOU 1204  CA  GLU A 157    10206  11468  10344    759   -119     59       C  
ATOM   1205  C   GLU A 157      36.974  22.050 -19.620  1.00 88.54           C  
ANISOU 1205  C   GLU A 157    10760  11986  10896    735    -89    115       C  
ATOM   1206  O   GLU A 157      36.814  23.179 -19.155  1.00 90.34           O  
ANISOU 1206  O   GLU A 157    11005  12207  11111    723    -73    152       O  
ATOM   1207  CB  GLU A 157      35.365  20.103 -19.289  1.00 81.84           C  
ANISOU 1207  CB  GLU A 157     9876  11128  10091    721   -149     31       C  
ATOM   1208  CG  GLU A 157      33.860  19.884 -19.277  1.00 81.23           C  
ANISOU 1208  CG  GLU A 157     9793  11061  10010    727   -175     -7       C  
ATOM   1209  CD  GLU A 157      33.462  18.425 -19.171  1.00 80.46           C  
ANISOU 1209  CD  GLU A 157     9666  10949   9959    718   -204    -58       C  
ATOM   1210  OE1 GLU A 157      34.318  17.572 -18.835  1.00 83.75           O  
ANISOU 1210  OE1 GLU A 157    10067  11338  10417    697   -205    -56       O  
ATOM   1211  OE2 GLU A 157      32.280  18.135 -19.431  1.00 74.08           O  
ANISOU 1211  OE2 GLU A 157     8847  10154   9148    732   -224    -99       O  
ATOM   1212  N   ASP A 158      38.169  21.469 -19.682  1.00 94.41           N  
ANISOU 1212  N   ASP A 158    11492  12715  11664    728    -80    119       N  
ATOM   1213  CA  ASP A 158      39.360  22.164 -19.177  1.00 94.44           C  
ANISOU 1213  CA  ASP A 158    11504  12695  11684    706    -53    168       C  
ATOM   1214  C   ASP A 158      40.067  22.992 -20.246  1.00 92.18           C  
ANISOU 1214  C   ASP A 158    11231  12436  11359    745    -15    191       C  
ATOM   1215  O   ASP A 158      40.830  23.897 -19.913  1.00 93.64           O  
ANISOU 1215  O   ASP A 158    11425  12604  11550    732     13    234       O  
ATOM   1216  CB  ASP A 158      40.341  21.214 -18.464  1.00 97.20           C  
ANISOU 1216  CB  ASP A 158    11834  13009  12089    672    -63    168       C  
ATOM   1217  CG  ASP A 158      40.024  19.743 -18.702  1.00 98.37           C  
ANISOU 1217  CG  ASP A 158    11959  13156  12261    676    -93    118       C  
ATOM   1218  OD1 ASP A 158      39.018  19.253 -18.147  1.00100.68           O  
ANISOU 1218  OD1 ASP A 158    12245  13439  12569    659   -119     97       O  
ATOM   1219  OD2 ASP A 158      40.782  19.073 -19.429  1.00 94.87           O  
ANISOU 1219  OD2 ASP A 158    11500  12718  11826    695    -88     99       O  
ATOM   1220  N   SER A 159      39.795  22.699 -21.517  1.00 88.40           N  
ANISOU 1220  N   SER A 159    10751  11997  10840    793    -14    162       N  
ATOM   1221  CA  SER A 159      40.428  23.416 -22.629  1.00 92.10           C  
ANISOU 1221  CA  SER A 159    11233  12496  11267    835     24    184       C  
ATOM   1222  C   SER A 159      39.630  24.617 -23.124  1.00 96.74           C  
ANISOU 1222  C   SER A 159    11843  13112  11801    866     39    207       C  
ATOM   1223  O   SER A 159      40.146  25.420 -23.909  1.00 90.84           O  
ANISOU 1223  O   SER A 159    11111  12385  11020    897     76    238       O  
ATOM   1224  CB  SER A 159      40.691  22.473 -23.809  1.00 93.76           C  
ANISOU 1224  CB  SER A 159    11429  12739  11456    874     21    141       C  
ATOM   1225  OG  SER A 159      41.635  21.468 -23.484  1.00 88.02           O  
ANISOU 1225  OG  SER A 159    10680  11984  10780    850     15    126       O  
ATOM   1226  N   ALA A 160      38.382  24.732 -22.667  1.00101.97           N  
ANISOU 1226  N   ALA A 160    12509  13775  12459    857     12    192       N  
ATOM   1227  CA  ALA A 160      37.451  25.749 -23.167  1.00104.40           C  
ANISOU 1227  CA  ALA A 160    12837  14113  12719    889     19    206       C  
ATOM   1228  C   ALA A 160      38.140  27.084 -23.350  1.00103.82           C  
ANISOU 1228  C   ALA A 160    12781  14035  12629    898     64    266       C  
ATOM   1229  O   ALA A 160      38.698  27.647 -22.404  1.00106.75           O  
ANISOU 1229  O   ALA A 160    13153  14367  13038    859     80    300       O  
ATOM   1230  CB  ALA A 160      36.233  25.891 -22.258  1.00103.82           C  
ANISOU 1230  CB  ALA A 160    12762  14023  12660    862    -10    195       C  
ATOM   1231  N   GLU A 161      38.092  27.566 -24.586  1.00100.36           N  
ANISOU 1231  N   GLU A 161    12357  13639  12136    953     85    277       N  
ATOM   1232  CA  GLU A 161      38.769  28.781 -25.015  1.00103.33           C  
ANISOU 1232  CA  GLU A 161    12750  14017  12493    972    134    334       C  
ATOM   1233  C   GLU A 161      39.635  28.451 -26.231  1.00106.46           C  
ANISOU 1233  C   GLU A 161    13147  14447  12856   1014    161    334       C  
ATOM   1234  O   GLU A 161      40.148  29.351 -26.897  1.00115.65           O  
ANISOU 1234  O   GLU A 161    14326  15623  13992   1043    204    379       O  
ATOM   1235  CB  GLU A 161      39.533  29.470 -23.854  1.00 98.34           C  
ANISOU 1235  CB  GLU A 161    12116  13331  11917    921    157    375       C  
ATOM   1236  CG  GLU A 161      41.020  29.701 -24.056  1.00100.12           C  
ANISOU 1236  CG  GLU A 161    12338  13540  12162    918    200    408       C  
ATOM   1237  CD  GLU A 161      41.815  28.412 -23.967  1.00102.63           C  
ANISOU 1237  CD  GLU A 161    12637  13850  12509    901    185    374       C  
ATOM   1238  OE1 GLU A 161      41.867  27.828 -22.863  1.00103.68           O  
ANISOU 1238  OE1 GLU A 161    12756  13949  12691    854    157    356       O  
ATOM   1239  OE2 GLU A 161      42.383  27.981 -24.998  1.00102.51           O  
ANISOU 1239  OE2 GLU A 161    12620  13862  12468    936    201    364       O  
ATOM   1240  N   ILE A 162      39.763  27.158 -26.530  1.00102.73           N  
ANISOU 1240  N   ILE A 162    12658  13988  12387   1018    135    283       N  
ATOM   1241  CA  ILE A 162      40.473  26.699 -27.720  1.00102.66           C  
ANISOU 1241  CA  ILE A 162    12648  14017  12344   1059    156    270       C  
ATOM   1242  C   ILE A 162      40.160  27.605 -28.919  1.00112.65           C  
ANISOU 1242  C   ILE A 162    13936  15332  13534   1120    183    299       C  
ATOM   1243  O   ILE A 162      41.002  27.785 -29.799  1.00120.57           O  
ANISOU 1243  O   ILE A 162    14946  16358  14509   1152    222    320       O  
ATOM   1244  CB  ILE A 162      40.120  25.238 -28.087  1.00 98.69           C  
ANISOU 1244  CB  ILE A 162    12123  13536  11838   1070    115    198       C  
ATOM   1245  CG1 ILE A 162      39.983  24.349 -26.852  1.00 94.26           C  
ANISOU 1245  CG1 ILE A 162    11541  12928  11347   1013     77    168       C  
ATOM   1246  CG2 ILE A 162      41.164  24.656 -29.020  1.00100.38           C  
ANISOU 1246  CG2 ILE A 162    12329  13773  12038   1097    138    184       C  
ATOM   1247  CD1 ILE A 162      38.557  24.034 -26.461  1.00 95.44           C  
ANISOU 1247  CD1 ILE A 162    11685  13081  11495   1007     32    132       C  
ATOM   1248  N   LEU A 163      38.950  28.171 -28.942  1.00121.06           N  
ANISOU 1248  N   LEU A 163    15014  16414  14570   1137    164    302       N  
ATOM   1249  CA  LEU A 163      38.544  29.149 -29.961  1.00130.69           C  
ANISOU 1249  CA  LEU A 163    16257  17678  15721   1193    188    336       C  
ATOM   1250  C   LEU A 163      39.104  30.531 -29.660  1.00138.92           C  
ANISOU 1250  C   LEU A 163    17315  18689  16779   1183    237    412       C  
ATOM   1251  O   LEU A 163      39.846  31.096 -30.466  1.00142.58           O  
ANISOU 1251  O   LEU A 163    17791  19170  17212   1215    285    454       O  
ATOM   1252  CB  LEU A 163      37.012  29.234 -30.075  1.00130.61           C  
ANISOU 1252  CB  LEU A 163    16251  17695  15678   1215    145    309       C  
ATOM   1253  CG  LEU A 163      36.250  30.122 -31.085  1.00128.65           C  
ANISOU 1253  CG  LEU A 163    16026  17498  15356   1278    153    334       C  
ATOM   1254  CD1 LEU A 163      36.171  31.588 -30.670  1.00126.85           C  
ANISOU 1254  CD1 LEU A 163    15816  17242  15140   1269    185    405       C  
ATOM   1255  CD2 LEU A 163      36.783  29.993 -32.505  1.00129.60           C  
ANISOU 1255  CD2 LEU A 163    16157  17677  15408   1339    178    338       C  
ATOM   1256  N   ASP A 164      38.732  31.063 -28.496  1.00144.20           N  
ANISOU 1256  N   ASP A 164    17981  19311  17495   1137    228    428       N  
ATOM   1257  CA  ASP A 164      39.060  32.434 -28.101  1.00153.89           C  
ANISOU 1257  CA  ASP A 164    19220  20506  18744   1125    269    493       C  
ATOM   1258  C   ASP A 164      40.564  32.711 -28.074  1.00160.22           C  
ANISOU 1258  C   ASP A 164    20019  21279  19579   1110    320    532       C  
ATOM   1259  O   ASP A 164      40.986  33.856 -28.242  1.00167.97           O  
ANISOU 1259  O   ASP A 164    21011  22248  20564   1120    367    590       O  
ATOM   1260  CB  ASP A 164      38.441  32.766 -26.737  1.00155.48           C  
ANISOU 1260  CB  ASP A 164    19416  20663  18999   1072    245    491       C  
ATOM   1261  CG  ASP A 164      36.957  32.419 -26.658  1.00153.95           C  
ANISOU 1261  CG  ASP A 164    19221  20490  18782   1081    194    448       C  
ATOM   1262  OD1 ASP A 164      36.227  32.609 -27.656  1.00150.07           O  
ANISOU 1262  OD1 ASP A 164    18742  20047  18231   1135    188    445       O  
ATOM   1263  OD2 ASP A 164      36.523  31.959 -25.581  1.00149.55           O  
ANISOU 1263  OD2 ASP A 164    18651  19903  18267   1035    161    418       O  
ATOM   1264  N   SER A 165      41.361  31.662 -27.868  1.00161.03           N  
ANISOU 1264  N   SER A 165    20103  21370  19709   1086    311    499       N  
ATOM   1265  CA  SER A 165      42.822  31.774 -27.860  1.00156.11           C  
ANISOU 1265  CA  SER A 165    19473  20721  19122   1072    356    526       C  
ATOM   1266  C   SER A 165      43.409  31.789 -29.276  1.00152.70           C  
ANISOU 1266  C   SER A 165    19051  20332  18635   1127    396    542       C  
ATOM   1267  O   SER A 165      44.186  32.685 -29.620  1.00150.59           O  
ANISOU 1267  O   SER A 165    18791  20054  18371   1139    451    596       O  
ATOM   1268  CB  SER A 165      43.452  30.650 -27.025  1.00156.64           C  
ANISOU 1268  CB  SER A 165    19516  20755  19245   1024    329    486       C  
ATOM   1269  OG  SER A 165      43.207  29.374 -27.596  1.00155.62           O  
ANISOU 1269  OG  SER A 165    19378  20661  19089   1043    296    430       O  
ATOM   1270  N   ASP A 166      43.024  30.801 -30.086  1.00147.87           N  
ANISOU 1270  N   ASP A 166    18437  19770  17975   1162    369    494       N  
ATOM   1271  CA  ASP A 166      43.542  30.627 -31.450  1.00145.07           C  
ANISOU 1271  CA  ASP A 166    18091  19465  17562   1216    402    498       C  
ATOM   1272  C   ASP A 166      45.051  30.323 -31.477  1.00143.11           C  
ANISOU 1272  C   ASP A 166    17828  19192  17354   1198    441    507       C  
ATOM   1273  O   ASP A 166      45.797  30.888 -32.282  1.00138.98           O  
ANISOU 1273  O   ASP A 166    17316  18685  16807   1229    497    548       O  
ATOM   1274  CB  ASP A 166      43.197  31.840 -32.332  1.00143.01           C  
ANISOU 1274  CB  ASP A 166    17857  19238  17241   1268    440    555       C  
ATOM   1275  CG  ASP A 166      43.546  31.625 -33.794  1.00142.51           C  
ANISOU 1275  CG  ASP A 166    17806  19238  17104   1330    469    557       C  
ATOM   1276  OD1 ASP A 166      43.148  30.586 -34.364  1.00143.49           O  
ANISOU 1276  OD1 ASP A 166    17924  19408  17189   1355    433    496       O  
ATOM   1277  OD2 ASP A 166      44.222  32.502 -34.373  1.00134.91           O  
ANISOU 1277  OD2 ASP A 166    16857  18278  16124   1355    530    617       O  
ATOM   1278  N   VAL A 167      45.492  29.436 -30.585  1.00142.30           N  
ANISOU 1278  N   VAL A 167    17701  19050  17314   1149    413    469       N  
ATOM   1279  CA  VAL A 167      46.880  28.957 -30.592  1.00135.33           C  
ANISOU 1279  CA  VAL A 167    16801  18145  16474   1131    442    467       C  
ATOM   1280  C   VAL A 167      47.021  27.854 -31.648  1.00131.37           C  
ANISOU 1280  C   VAL A 167    16292  17694  15930   1169    434    416       C  
ATOM   1281  O   VAL A 167      48.084  27.703 -32.247  1.00135.96           O  
ANISOU 1281  O   VAL A 167    16867  18281  16512   1182    474    423       O  
ATOM   1282  CB  VAL A 167      47.368  28.493 -29.195  1.00135.35           C  
ANISOU 1282  CB  VAL A 167    16780  18085  16563   1065    416    451       C  
ATOM   1283  CG1 VAL A 167      48.864  28.207 -29.212  1.00131.50           C  
ANISOU 1283  CG1 VAL A 167    16273  17570  16122   1049    451    457       C  
ATOM   1284  CG2 VAL A 167      47.065  29.548 -28.137  1.00131.25           C  
ANISOU 1284  CG2 VAL A 167    16267  17523  16080   1029    417    492       C  
ATOM   1285  N   LEU A 168      45.950  27.087 -31.865  1.00124.36           N  
ANISOU 1285  N   LEU A 168    15402  16841  15007   1186    382    363       N  
ATOM   1286  CA  LEU A 168      45.799  26.292 -33.086  1.00119.37           C  
ANISOU 1286  CA  LEU A 168    14768  16272  14314   1236    376    317       C  
ATOM   1287  C   LEU A 168      45.012  27.143 -34.074  1.00120.20           C  
ANISOU 1287  C   LEU A 168    14903  16435  14333   1296    391    345       C  
ATOM   1288  O   LEU A 168      44.309  28.067 -33.665  1.00123.30           O  
ANISOU 1288  O   LEU A 168    15312  16815  14720   1291    388    383       O  
ATOM   1289  CB  LEU A 168      45.077  24.962 -32.814  1.00114.50           C  
ANISOU 1289  CB  LEU A 168    14130  15661  13713   1224    311    239       C  
ATOM   1290  CG  LEU A 168      44.818  23.986 -33.981  1.00112.28           C  
ANISOU 1290  CG  LEU A 168    13840  15443  13378   1273    294    176       C  
ATOM   1291  CD1 LEU A 168      46.110  23.573 -34.678  1.00113.07           C  
ANISOU 1291  CD1 LEU A 168    13929  15554  13479   1287    336    170       C  
ATOM   1292  CD2 LEU A 168      44.046  22.752 -33.525  1.00104.50           C  
ANISOU 1292  CD2 LEU A 168    12829  14451  12424   1253    230    102       C  
ATOM   1293  N   ASP A 169      45.138  26.849 -35.366  1.00126.71           N  
ANISOU 1293  N   ASP A 169    15734  17322  15089   1352    408    327       N  
ATOM   1294  CA  ASP A 169      44.391  27.584 -36.388  1.00135.38           C  
ANISOU 1294  CA  ASP A 169    16861  18483  16096   1414    420    353       C  
ATOM   1295  C   ASP A 169      42.884  27.339 -36.251  1.00137.01           C  
ANISOU 1295  C   ASP A 169    17069  18713  16277   1425    356    311       C  
ATOM   1296  O   ASP A 169      42.377  26.271 -36.633  1.00136.42           O  
ANISOU 1296  O   ASP A 169    16978  18674  16181   1442    313    238       O  
ATOM   1297  CB  ASP A 169      44.910  27.285 -37.811  1.00142.84           C  
ANISOU 1297  CB  ASP A 169    17812  19494  16968   1473    453    341       C  
ATOM   1298  CG  ASP A 169      44.854  25.798 -38.180  1.00146.76           C  
ANISOU 1298  CG  ASP A 169    18282  20021  17461   1481    412    250       C  
ATOM   1299  OD1 ASP A 169      44.928  25.489 -39.396  1.00142.05           O  
ANISOU 1299  OD1 ASP A 169    17690  19492  16790   1537    425    226       O  
ATOM   1300  OD2 ASP A 169      44.742  24.940 -37.272  1.00148.71           O  
ANISOU 1300  OD2 ASP A 169    18502  20225  17776   1432    369    203       O  
ATOM   1301  N   ARG A 170      42.199  28.339 -35.680  1.00138.55           N  
ANISOU 1301  N   ARG A 170    17279  18884  16478   1414    353    356       N  
ATOM   1302  CA  ARG A 170      40.760  28.297 -35.359  1.00137.39           C  
ANISOU 1302  CA  ARG A 170    17134  18748  16319   1416    297    326       C  
ATOM   1303  C   ARG A 170      40.100  26.914 -35.549  1.00136.86           C  
ANISOU 1303  C   ARG A 170    17044  18711  16246   1423    237    234       C  
ATOM   1304  O   ARG A 170      39.461  26.661 -36.582  1.00137.30           O  
ANISOU 1304  O   ARG A 170    17105  18833  16228   1480    218    200       O  
ATOM   1305  CB  ARG A 170      40.007  29.386 -36.144  1.00136.06           C  
ANISOU 1305  CB  ARG A 170    16995  18626  16075   1472    310    371       C  
ATOM   1306  CG  ARG A 170      39.125  30.280 -35.284  1.00134.44           C  
ANISOU 1306  CG  ARG A 170    16799  18385  15897   1448    294    404       C  
ATOM   1307  CD  ARG A 170      39.890  31.485 -34.753  1.00141.10           C  
ANISOU 1307  CD  ARG A 170    17654  19177  16782   1422    350    485       C  
ATOM   1308  NE  ARG A 170      39.254  32.070 -33.569  1.00148.22           N  
ANISOU 1308  NE  ARG A 170    18553  20026  17738   1376    330    501       N  
ATOM   1309  CZ  ARG A 170      39.677  33.165 -32.937  1.00148.80           C  
ANISOU 1309  CZ  ARG A 170    18632  20049  17855   1348    368    563       C  
ATOM   1310  NH1 ARG A 170      40.746  33.828 -33.365  1.00147.39           N  
ANISOU 1310  NH1 ARG A 170    18463  19863  17676   1360    431    621       N  
ATOM   1311  NH2 ARG A 170      39.024  33.605 -31.867  1.00148.21           N  
ANISOU 1311  NH2 ARG A 170    18554  19933  17827   1308    346    567       N  
ATOM   1312  N   PRO A 171      40.266  26.015 -34.550  1.00128.40           N  
ANISOU 1312  N   PRO A 171    15946  17590  15251   1366    207    193       N  
ATOM   1313  CA  PRO A 171      39.807  24.619 -34.644  1.00122.46           C  
ANISOU 1313  CA  PRO A 171    15166  16853  14510   1365    156    106       C  
ATOM   1314  C   PRO A 171      38.322  24.417 -34.355  1.00115.02           C  
ANISOU 1314  C   PRO A 171    14219  15921  13563   1367    100     65       C  
ATOM   1315  O   PRO A 171      37.740  23.413 -34.781  1.00112.12           O  
ANISOU 1315  O   PRO A 171    13832  15586  13185   1387     59     -8       O  
ATOM   1316  CB  PRO A 171      40.636  23.909 -33.574  1.00120.51           C  
ANISOU 1316  CB  PRO A 171    14894  16540  14354   1301    154     96       C  
ATOM   1317  CG  PRO A 171      40.925  24.961 -32.562  1.00121.28           C  
ANISOU 1317  CG  PRO A 171    15006  16582  14493   1258    179    165       C  
ATOM   1318  CD  PRO A 171      40.970  26.280 -33.280  1.00123.73           C  
ANISOU 1318  CD  PRO A 171    15347  16922  14742   1300    223    229       C  
ATOM   1319  N   LEU A 172      37.726  25.365 -33.637  1.00105.05           N  
ANISOU 1319  N   LEU A 172    12972  14630  12314   1347     99    110       N  
ATOM   1320  CA  LEU A 172      36.334  25.260 -33.216  1.00107.14           C  
ANISOU 1320  CA  LEU A 172    13230  14894  12584   1342     48     76       C  
ATOM   1321  C   LEU A 172      35.337  25.503 -34.345  1.00105.32           C  
ANISOU 1321  C   LEU A 172    13011  14735  12270   1410     29     55       C  
ATOM   1322  O   LEU A 172      34.173  25.105 -34.254  1.00 92.00           O  
ANISOU 1322  O   LEU A 172    11312  13061  10584   1416    -20      4       O  
ATOM   1323  CB  LEU A 172      36.061  26.183 -32.027  1.00104.90           C  
ANISOU 1323  CB  LEU A 172    12957  14555  12346   1295     55    127       C  
ATOM   1324  CG  LEU A 172      36.458  25.557 -30.688  1.00106.92           C  
ANISOU 1324  CG  LEU A 172    13191  14743  12689   1224     43    116       C  
ATOM   1325  CD1 LEU A 172      37.967  25.399 -30.566  1.00107.23           C  
ANISOU 1325  CD1 LEU A 172    13227  14755  12760   1201     82    142       C  
ATOM   1326  CD2 LEU A 172      35.892  26.343 -29.523  1.00102.31           C  
ANISOU 1326  CD2 LEU A 172    12615  14114  12144   1181     38    150       C  
ATOM   1327  N   ASN A 173      35.819  26.134 -35.415  1.00108.82           N  
ANISOU 1327  N   ASN A 173    13477  15226  12644   1463     67     93       N  
ATOM   1328  CA  ASN A 173      35.021  26.407 -36.611  1.00111.04           C  
ANISOU 1328  CA  ASN A 173    13772  15583  12834   1535     52     80       C  
ATOM   1329  C   ASN A 173      34.670  25.114 -37.356  1.00111.75           C  
ANISOU 1329  C   ASN A 173    13838  15724  12899   1567     11    -13       C  
ATOM   1330  O   ASN A 173      33.946  25.121 -38.359  1.00111.03           O  
ANISOU 1330  O   ASN A 173    13752  15701  12734   1628    -12    -42       O  
ATOM   1331  CB  ASN A 173      35.765  27.386 -37.534  1.00111.61           C  
ANISOU 1331  CB  ASN A 173    13875  15691  12840   1582    111    151       C  
ATOM   1332  CG  ASN A 173      36.156  28.690 -36.837  1.00111.13           C  
ANISOU 1332  CG  ASN A 173    13835  15577  12811   1552    156    242       C  
ATOM   1333  OD1 ASN A 173      36.816  29.541 -37.431  1.00113.14           O  
ANISOU 1333  OD1 ASN A 173    14112  15847  13028   1581    208    308       O  
ATOM   1334  ND2 ASN A 173      35.750  28.852 -35.581  1.00112.93           N  
ANISOU 1334  ND2 ASN A 173    14054  15744  13111   1495    136    246       N  
ATOM   1335  N   ILE A 174      35.190  24.004 -36.847  1.00110.62           N  
ANISOU 1335  N   ILE A 174    13666  15546  12820   1524     -1    -61       N  
ATOM   1336  CA  ILE A 174      34.953  22.706 -37.440  1.00111.59           C  
ANISOU 1336  CA  ILE A 174    13759  15705  12935   1546    -38   -153       C  
ATOM   1337  C   ILE A 174      34.151  21.859 -36.462  1.00109.82           C  
ANISOU 1337  C   ILE A 174    13504  15435  12787   1499    -90   -211       C  
ATOM   1338  O   ILE A 174      33.160  21.246 -36.844  1.00110.55           O  
ANISOU 1338  O   ILE A 174    13577  15560  12865   1524   -137   -281       O  
ATOM   1339  CB  ILE A 174      36.275  22.000 -37.836  1.00111.82           C  
ANISOU 1339  CB  ILE A 174    13776  15736  12973   1543     -7   -167       C  
ATOM   1340  CG1 ILE A 174      37.159  22.911 -38.699  1.00109.87           C  
ANISOU 1340  CG1 ILE A 174    13561  15527  12658   1584     53   -100       C  
ATOM   1341  CG2 ILE A 174      35.990  20.718 -38.603  1.00109.77           C  
ANISOU 1341  CG2 ILE A 174    13486  15523  12698   1574    -45   -266       C  
ATOM   1342  CD1 ILE A 174      38.013  23.890 -37.921  1.00106.81           C  
ANISOU 1342  CD1 ILE A 174    13193  15079  12310   1542    104     -9       C  
ATOM   1343  N   MET A 175      34.563  21.856 -35.197  1.00107.58           N  
ANISOU 1343  N   MET A 175    13214  15075  12585   1431    -80   -180       N  
ATOM   1344  CA  MET A 175      33.956  20.983 -34.180  1.00110.10           C  
ANISOU 1344  CA  MET A 175    13503  15345  12984   1380   -121   -229       C  
ATOM   1345  C   MET A 175      32.468  21.272 -33.853  1.00108.20           C  
ANISOU 1345  C   MET A 175    13263  15107  12742   1383   -162   -248       C  
ATOM   1346  O   MET A 175      31.629  20.356 -33.905  1.00101.47           O  
ANISOU 1346  O   MET A 175    12381  14262  11911   1387   -207   -323       O  
ATOM   1347  CB  MET A 175      34.801  20.982 -32.893  1.00107.11           C  
ANISOU 1347  CB  MET A 175    13122  14889  12686   1310    -99   -185       C  
ATOM   1348  CG  MET A 175      36.238  20.494 -33.040  1.00107.12           C  
ANISOU 1348  CG  MET A 175    13116  14877  12708   1298    -67   -177       C  
ATOM   1349  SD  MET A 175      37.394  21.289 -31.889  1.00111.00           S  
ANISOU 1349  SD  MET A 175    13623  15299  13253   1239    -21    -90       S  
ATOM   1350  CE  MET A 175      36.896  20.638 -30.291  1.00108.66           C  
ANISOU 1350  CE  MET A 175    13304  14930  13051   1166    -59   -107       C  
ATOM   1351  N   ILE A 176      32.154  22.533 -33.516  1.00106.27           N  
ANISOU 1351  N   ILE A 176    13046  14852  12478   1381   -145   -182       N  
ATOM   1352  CA  ILE A 176      30.792  22.949 -33.084  1.00 98.68           C  
ANISOU 1352  CA  ILE A 176    12085  13885  11522   1378   -178   -191       C  
ATOM   1353  C   ILE A 176      29.723  22.595 -34.111  1.00 94.23           C  
ANISOU 1353  C   ILE A 176    11511  13387  10904   1438   -220   -257       C  
ATOM   1354  O   ILE A 176      28.757  21.912 -33.770  1.00 93.94           O  
ANISOU 1354  O   ILE A 176    11448  13339  10905   1425   -263   -319       O  
ATOM   1355  CB  ILE A 176      30.706  24.453 -32.691  1.00 96.47           C  
ANISOU 1355  CB  ILE A 176    11839  13590  11226   1372   -148   -107       C  
ATOM   1356  CG1 ILE A 176      31.319  24.683 -31.307  1.00 97.64           C  
ANISOU 1356  CG1 ILE A 176    11989  13663  11449   1299   -125    -61       C  
ATOM   1357  CG2 ILE A 176      29.262  24.942 -32.678  1.00 99.25           C  
ANISOU 1357  CG2 ILE A 176    12194  13958  11561   1391   -182   -121       C  
ATOM   1358  CD1 ILE A 176      31.834  26.089 -31.078  1.00 95.38           C  
ANISOU 1358  CD1 ILE A 176    11732  13359  11148   1294    -79     26       C  
ATOM   1359  N   PRO A 177      29.904  23.029 -35.377  1.00 96.25           N  
ANISOU 1359  N   PRO A 177    11787  13712  11074   1504   -207   -246       N  
ATOM   1360  CA  PRO A 177      28.931  22.625 -36.388  1.00 96.41           C  
ANISOU 1360  CA  PRO A 177    11793  13798  11039   1565   -250   -316       C  
ATOM   1361  C   PRO A 177      28.846  21.108 -36.565  1.00 95.58           C  
ANISOU 1361  C   PRO A 177    11647  13700  10970   1560   -286   -413       C  
ATOM   1362  O   PRO A 177      28.003  20.632 -37.325  1.00 95.64           O  
ANISOU 1362  O   PRO A 177    11637  13759  10945   1606   -327   -484       O  
ATOM   1363  CB  PRO A 177      29.458  23.295 -37.665  1.00 97.29           C  
ANISOU 1363  CB  PRO A 177    11935  13980  11051   1632   -220   -278       C  
ATOM   1364  CG  PRO A 177      30.227  24.477 -37.174  1.00 95.64           C  
ANISOU 1364  CG  PRO A 177    11758  13734  10846   1608   -165   -175       C  
ATOM   1365  CD  PRO A 177      30.895  23.976 -35.929  1.00 95.11           C  
ANISOU 1365  CD  PRO A 177    11675  13588  10875   1530   -153   -170       C  
ATOM   1366  N   LYS A 178      29.699  20.362 -35.864  1.00 98.26           N  
ANISOU 1366  N   LYS A 178    11970  13986  11381   1507   -271   -418       N  
ATOM   1367  CA  LYS A 178      29.720  18.904 -35.996  1.00100.03           C  
ANISOU 1367  CA  LYS A 178    12151  14208  11648   1500   -300   -507       C  
ATOM   1368  C   LYS A 178      28.953  18.186 -34.888  1.00 95.65           C  
ANISOU 1368  C   LYS A 178    11565  13592  11186   1445   -334   -547       C  
ATOM   1369  O   LYS A 178      28.424  17.092 -35.102  1.00 96.12           O  
ANISOU 1369  O   LYS A 178    11587  13658  11277   1451   -372   -633       O  
ATOM   1370  CB  LYS A 178      31.156  18.370 -36.115  1.00 98.60           C  
ANISOU 1370  CB  LYS A 178    11966  14014  11484   1484   -265   -497       C  
ATOM   1371  CG  LYS A 178      31.884  18.814 -37.376  1.00 99.41           C  
ANISOU 1371  CG  LYS A 178    12091  14184  11494   1544   -233   -476       C  
ATOM   1372  CD  LYS A 178      31.208  18.327 -38.656  1.00103.44           C  
ANISOU 1372  CD  LYS A 178    12588  14777  11938   1614   -268   -556       C  
ATOM   1373  CE  LYS A 178      31.809  18.959 -39.909  1.00100.63           C  
ANISOU 1373  CE  LYS A 178    12261  14496  11477   1679   -235   -524       C  
ATOM   1374  NZ  LYS A 178      33.293  18.810 -40.016  1.00 94.06           N  
ANISOU 1374  NZ  LYS A 178    11436  13651  10654   1664   -184   -491       N  
ATOM   1375  N   PHE A 179      28.866  18.805 -33.718  1.00 91.83           N  
ANISOU 1375  N   PHE A 179    11096  13049  10747   1393   -320   -488       N  
ATOM   1376  CA  PHE A 179      28.162  18.172 -32.600  1.00 94.81           C  
ANISOU 1376  CA  PHE A 179    11446  13367  11211   1339   -348   -518       C  
ATOM   1377  C   PHE A 179      26.648  18.050 -32.803  1.00 96.73           C  
ANISOU 1377  C   PHE A 179    11671  13632  11450   1363   -394   -578       C  
ATOM   1378  O   PHE A 179      26.067  16.983 -32.564  1.00 94.12           O  
ANISOU 1378  O   PHE A 179    11302  13282  11179   1347   -427   -649       O  
ATOM   1379  CB  PHE A 179      28.468  18.889 -31.283  1.00 91.70           C  
ANISOU 1379  CB  PHE A 179    11073  12909  10860   1278   -320   -440       C  
ATOM   1380  CG  PHE A 179      29.928  18.910 -30.923  1.00 90.31           C  
ANISOU 1380  CG  PHE A 179    10908  12701  10703   1247   -279   -387       C  
ATOM   1381  CD1 PHE A 179      30.734  17.789 -31.134  1.00 90.34           C  
ANISOU 1381  CD1 PHE A 179    10887  12698  10739   1241   -278   -426       C  
ATOM   1382  CD2 PHE A 179      30.498  20.044 -30.353  1.00 88.82           C  
ANISOU 1382  CD2 PHE A 179    10752  12488  10506   1224   -241   -302       C  
ATOM   1383  CE1 PHE A 179      32.080  17.811 -30.801  1.00 88.70           C  
ANISOU 1383  CE1 PHE A 179    10689  12462  10552   1213   -242   -379       C  
ATOM   1384  CE2 PHE A 179      31.844  20.069 -30.013  1.00 89.17           C  
ANISOU 1384  CE2 PHE A 179    10805  12504  10573   1196   -205   -257       C  
ATOM   1385  CZ  PHE A 179      32.636  18.953 -30.241  1.00 87.81           C  
ANISOU 1385  CZ  PHE A 179    10608  12326  10429   1191   -206   -295       C  
ATOM   1386  N   LEU A 180      26.019  19.129 -33.267  1.00 99.05           N  
ANISOU 1386  N   LEU A 180    11990  13966  11678   1403   -396   -550       N  
ATOM   1387  CA  LEU A 180      24.553  19.173 -33.361  1.00 98.45           C  
ANISOU 1387  CA  LEU A 180    11899  13907  11601   1423   -440   -599       C  
ATOM   1388  C   LEU A 180      23.915  18.136 -34.281  1.00 99.63           C  
ANISOU 1388  C   LEU A 180    12011  14102  11742   1467   -485   -703       C  
ATOM   1389  O   LEU A 180      22.708  17.911 -34.209  1.00102.64           O  
ANISOU 1389  O   LEU A 180    12368  14484  12145   1474   -524   -757       O  
ATOM   1390  CB  LEU A 180      24.004  20.587 -33.641  1.00 96.41           C  
ANISOU 1390  CB  LEU A 180    11676  13679  11277   1457   -434   -544       C  
ATOM   1391  CG  LEU A 180      24.765  21.760 -34.277  1.00 98.18           C  
ANISOU 1391  CG  LEU A 180    11944  13939  11420   1494   -394   -464       C  
ATOM   1392  CD1 LEU A 180      25.701  22.460 -33.299  1.00 96.32           C  
ANISOU 1392  CD1 LEU A 180    11733  13646  11217   1439   -345   -376       C  
ATOM   1393  CD2 LEU A 180      25.506  21.335 -35.533  1.00105.67           C  
ANISOU 1393  CD2 LEU A 180    12894  14951  12305   1547   -387   -489       C  
ATOM   1394  N   GLN A 181      24.718  17.488 -35.120  1.00100.73           N  
ANISOU 1394  N   GLN A 181    12141  14277  11853   1496   -479   -734       N  
ATOM   1395  CA  GLN A 181      24.213  16.400 -35.959  1.00105.36           C  
ANISOU 1395  CA  GLN A 181    12687  14905  12440   1534   -521   -840       C  
ATOM   1396  C   GLN A 181      23.872  15.229 -35.064  1.00104.97           C  
ANISOU 1396  C   GLN A 181    12593  14790  12501   1479   -541   -896       C  
ATOM   1397  O   GLN A 181      23.014  14.403 -35.394  1.00104.68           O  
ANISOU 1397  O   GLN A 181    12515  14767  12493   1497   -583   -987       O  
ATOM   1398  CB  GLN A 181      25.251  15.970 -37.002  1.00110.24           C  
ANISOU 1398  CB  GLN A 181    13305  15573  13007   1573   -505   -859       C  
ATOM   1399  CG  GLN A 181      25.507  16.985 -38.107  1.00114.28           C  
ANISOU 1399  CG  GLN A 181    13858  16163  13401   1640   -488   -817       C  
ATOM   1400  CD  GLN A 181      25.903  18.355 -37.577  1.00116.79           C  
ANISOU 1400  CD  GLN A 181    14224  16457  13695   1621   -445   -703       C  
ATOM   1401  OE1 GLN A 181      26.495  18.477 -36.503  1.00110.31           O  
ANISOU 1401  OE1 GLN A 181    13411  15567  12936   1558   -416   -649       O  
ATOM   1402  NE2 GLN A 181      25.563  19.397 -38.326  1.00120.78           N  
ANISOU 1402  NE2 GLN A 181    14760  17020  14110   1677   -443   -666       N  
ATOM   1403  N   PHE A 182      24.544  15.186 -33.915  1.00105.96           N  
ANISOU 1403  N   PHE A 182    12725  14843  12690   1413   -510   -840       N  
ATOM   1404  CA  PHE A 182      24.427  14.071 -32.989  1.00103.91           C  
ANISOU 1404  CA  PHE A 182    12426  14516  12537   1356   -521   -878       C  
ATOM   1405  C   PHE A 182      23.399  14.309 -31.896  1.00100.93           C  
ANISOU 1405  C   PHE A 182    12044  14088  12216   1314   -533   -866       C  
ATOM   1406  O   PHE A 182      23.088  13.403 -31.126  1.00100.99           O  
ANISOU 1406  O   PHE A 182    12018  14041  12313   1270   -544   -900       O  
ATOM   1407  CB  PHE A 182      25.800  13.694 -32.425  1.00105.96           C  
ANISOU 1407  CB  PHE A 182    12692  14731  12837   1312   -484   -832       C  
ATOM   1408  CG  PHE A 182      26.762  13.227 -33.477  1.00103.17           C  
ANISOU 1408  CG  PHE A 182    12333  14422  12445   1351   -475   -860       C  
ATOM   1409  CD1 PHE A 182      26.676  11.935 -33.989  1.00102.39           C  
ANISOU 1409  CD1 PHE A 182    12187  14332  12385   1365   -501   -953       C  
ATOM   1410  CD2 PHE A 182      27.729  14.090 -33.986  1.00103.93           C  
ANISOU 1410  CD2 PHE A 182    12469  14553  12466   1375   -438   -796       C  
ATOM   1411  CE1 PHE A 182      27.548  11.508 -34.975  1.00102.44           C  
ANISOU 1411  CE1 PHE A 182    12187  14382  12353   1401   -492   -983       C  
ATOM   1412  CE2 PHE A 182      28.609  13.668 -34.970  1.00101.63           C  
ANISOU 1412  CE2 PHE A 182    12173  14304  12136   1411   -426   -822       C  
ATOM   1413  CZ  PHE A 182      28.517  12.376 -35.463  1.00105.91           C  
ANISOU 1413  CZ  PHE A 182    12669  14858  12716   1424   -454   -916       C  
ATOM   1414  N   PHE A 183      22.858  15.527 -31.851  1.00100.76           N  
ANISOU 1414  N   PHE A 183    12055  14085  12144   1328   -529   -818       N  
ATOM   1415  CA  PHE A 183      21.651  15.816 -31.070  1.00 95.14           C  
ANISOU 1415  CA  PHE A 183    11336  13341  11472   1302   -547   -822       C  
ATOM   1416  C   PHE A 183      20.561  14.822 -31.467  1.00 93.92           C  
ANISOU 1416  C   PHE A 183    11131  13196  11356   1323   -594   -928       C  
ATOM   1417  O   PHE A 183      19.894  14.232 -30.609  1.00 90.32           O  
ANISOU 1417  O   PHE A 183    10647  12688  10985   1279   -606   -956       O  
ATOM   1418  CB  PHE A 183      21.175  17.254 -31.315  1.00 94.06           C  
ANISOU 1418  CB  PHE A 183    11237  13238  11262   1333   -543   -771       C  
ATOM   1419  CG  PHE A 183      21.954  18.307 -30.559  1.00 94.13           C  
ANISOU 1419  CG  PHE A 183    11290  13217  11260   1298   -497   -667       C  
ATOM   1420  CD1 PHE A 183      21.297  19.389 -29.984  1.00 94.45           C  
ANISOU 1420  CD1 PHE A 183    11351  13242  11293   1285   -492   -620       C  
ATOM   1421  CD2 PHE A 183      23.337  18.225 -30.417  1.00 95.21           C  
ANISOU 1421  CD2 PHE A 183    11443  13338  11396   1277   -461   -619       C  
ATOM   1422  CE1 PHE A 183      21.998  20.371 -29.294  1.00 93.45           C  
ANISOU 1422  CE1 PHE A 183    11261  13087  11159   1253   -451   -530       C  
ATOM   1423  CE2 PHE A 183      24.045  19.199 -29.724  1.00 94.37           C  
ANISOU 1423  CE2 PHE A 183    11373  13204  11282   1246   -421   -529       C  
ATOM   1424  CZ  PHE A 183      23.375  20.273 -29.161  1.00 95.35           C  
ANISOU 1424  CZ  PHE A 183    11516  13313  11399   1234   -416   -485       C  
ATOM   1425  N   LYS A 184      20.425  14.623 -32.779  1.00 98.28           N  
ANISOU 1425  N   LYS A 184    11673  13819  11850   1389   -619   -987       N  
ATOM   1426  CA  LYS A 184      19.461  13.694 -33.367  1.00 99.58           C  
ANISOU 1426  CA  LYS A 184    11787  14006  12042   1419   -667  -1097       C  
ATOM   1427  C   LYS A 184      19.671  12.233 -32.946  1.00101.27           C  
ANISOU 1427  C   LYS A 184    11953  14169  12355   1380   -673  -1156       C  
ATOM   1428  O   LYS A 184      18.737  11.428 -33.025  1.00104.67           O  
ANISOU 1428  O   LYS A 184    12337  14591  12842   1384   -708  -1242       O  
ATOM   1429  CB  LYS A 184      19.482  13.817 -34.888  1.00 98.55           C  
ANISOU 1429  CB  LYS A 184    11661  13968  11817   1500   -689  -1141       C  
ATOM   1430  N   HIS A 185      20.883  11.913 -32.486  1.00101.66           N  
ANISOU 1430  N   HIS A 185    12013  14183  12431   1342   -638  -1110       N  
ATOM   1431  CA  HIS A 185      21.325  10.530 -32.238  1.00 97.23           C  
ANISOU 1431  CA  HIS A 185    11409  13579  11956   1312   -639  -1160       C  
ATOM   1432  C   HIS A 185      20.426   9.701 -31.362  1.00 96.02           C  
ANISOU 1432  C   HIS A 185    11212  13361  11911   1268   -657  -1204       C  
ATOM   1433  O   HIS A 185      19.841  10.193 -30.393  1.00 94.42           O  
ANISOU 1433  O   HIS A 185    11022  13117  11737   1230   -649  -1161       O  
ATOM   1434  CB  HIS A 185      22.744  10.512 -31.675  1.00100.59           C  
ANISOU 1434  CB  HIS A 185    11859  13968  12395   1272   -597  -1086       C  
ATOM   1435  CG  HIS A 185      23.409   9.153 -31.732  1.00103.01           C  
ANISOU 1435  CG  HIS A 185    12124  14246  12771   1257   -597  -1136       C  
ATOM   1436  ND1 HIS A 185      24.495   8.912 -32.488  1.00101.08           N  
ANISOU 1436  ND1 HIS A 185    11883  14034  12489   1282   -584  -1141       N  
ATOM   1437  CD2 HIS A 185      23.097   7.948 -31.096  1.00102.33           C  
ANISOU 1437  CD2 HIS A 185    11989  14099  12795   1217   -610  -1185       C  
ATOM   1438  CE1 HIS A 185      24.858   7.621 -32.349  1.00103.98           C  
ANISOU 1438  CE1 HIS A 185    12206  14363  12940   1260   -589  -1192       C  
ATOM   1439  NE2 HIS A 185      23.997   7.033 -31.498  1.00104.07           N  
ANISOU 1439  NE2 HIS A 185    12185  14315  13041   1221   -605  -1218       N  
ATOM   1440  N   SER A 186      20.352   8.417 -31.704  1.00 95.68           N  
ANISOU 1440  N   SER A 186    11117  13308  11931   1273   -678  -1291       N  
ATOM   1441  CA  SER A 186      19.475   7.440 -31.064  1.00 97.48           C  
ANISOU 1441  CA  SER A 186    11292  13477  12269   1238   -696  -1349       C  
ATOM   1442  C   SER A 186      19.756   7.158 -29.581  1.00 97.09           C  
ANISOU 1442  C   SER A 186    11246  13339  12306   1162   -666  -1285       C  
ATOM   1443  O   SER A 186      18.836   6.817 -28.835  1.00 97.03           O  
ANISOU 1443  O   SER A 186    11212  13283  12373   1129   -673  -1304       O  
ATOM   1444  CB  SER A 186      19.514   6.127 -31.856  1.00 98.52           C  
ANISOU 1444  CB  SER A 186    11366  13620  12448   1264   -722  -1455       C  
ATOM   1445  OG  SER A 186      18.596   5.180 -31.334  1.00 98.07           O  
ANISOU 1445  OG  SER A 186    11254  13507  12500   1236   -740  -1519       O  
ATOM   1446  N   SER A 187      21.015   7.283 -29.162  1.00 99.80           N  
ANISOU 1446  N   SER A 187    11619  13662  12640   1134   -632  -1211       N  
ATOM   1447  CA  SER A 187      21.408   6.955 -27.783  1.00 95.10           C  
ANISOU 1447  CA  SER A 187    11025  12986  12121   1064   -604  -1150       C  
ATOM   1448  C   SER A 187      21.533   8.179 -26.872  1.00 87.41           C  
ANISOU 1448  C   SER A 187    10106  11998  11108   1033   -577  -1048       C  
ATOM   1449  O   SER A 187      22.111   9.200 -27.264  1.00 81.28           O  
ANISOU 1449  O   SER A 187     9373  11265  10243   1056   -562   -997       O  
ATOM   1450  CB  SER A 187      22.706   6.140 -27.753  1.00 98.63           C  
ANISOU 1450  CB  SER A 187    11462  13408  12604   1048   -587  -1139       C  
ATOM   1451  OG  SER A 187      23.814   6.939 -28.132  1.00101.28           O  
ANISOU 1451  OG  SER A 187    11844  13782  12856   1065   -564  -1079       O  
ATOM   1452  N   PRO A 188      20.990   8.073 -25.647  1.00 85.90           N  
ANISOU 1452  N   PRO A 188     9910  11746  10982    980   -567  -1019       N  
ATOM   1453  CA  PRO A 188      21.014   9.162 -24.661  1.00 88.39           C  
ANISOU 1453  CA  PRO A 188    10270  12043  11269    944   -542   -929       C  
ATOM   1454  C   PRO A 188      22.427   9.693 -24.337  1.00 89.40           C  
ANISOU 1454  C   PRO A 188    10442  12169  11359    927   -510   -844       C  
ATOM   1455  O   PRO A 188      22.634  10.920 -24.302  1.00 87.35           O  
ANISOU 1455  O   PRO A 188    10226  11935  11029    934   -494   -785       O  
ATOM   1456  CB  PRO A 188      20.364   8.528 -23.425  1.00 90.48           C  
ANISOU 1456  CB  PRO A 188    10511  12237  11630    888   -537   -926       C  
ATOM   1457  CG  PRO A 188      19.498   7.438 -23.965  1.00 87.99           C  
ANISOU 1457  CG  PRO A 188    10138  11916  11378    907   -567  -1026       C  
ATOM   1458  CD  PRO A 188      20.222   6.907 -25.168  1.00 86.46           C  
ANISOU 1458  CD  PRO A 188     9927  11763  11159    952   -581  -1077       C  
ATOM   1459  N   LYS A 189      23.384   8.787 -24.126  1.00 84.88           N  
ANISOU 1459  N   LYS A 189     9853  11564  10835    906   -500   -839       N  
ATOM   1460  CA  LYS A 189      24.761   9.176 -23.814  1.00 81.05           C  
ANISOU 1460  CA  LYS A 189     9402  11072  10322    888   -471   -765       C  
ATOM   1461  C   LYS A 189      25.324  10.144 -24.833  1.00 77.82           C  
ANISOU 1461  C   LYS A 189     9027  10728   9814    936   -464   -747       C  
ATOM   1462  O   LYS A 189      25.901  11.174 -24.471  1.00 74.16           O  
ANISOU 1462  O   LYS A 189     8606  10270   9304    925   -439   -673       O  
ATOM   1463  CB  LYS A 189      25.671   7.953 -23.724  1.00 85.05           C  
ANISOU 1463  CB  LYS A 189     9878  11543  10894    871   -468   -780       C  
ATOM   1464  CG  LYS A 189      25.627   7.265 -22.375  1.00 88.81           C  
ANISOU 1464  CG  LYS A 189    10340  11946  11459    811   -459   -749       C  
ATOM   1465  CD  LYS A 189      26.736   6.243 -22.221  1.00 86.48           C  
ANISOU 1465  CD  LYS A 189    10024  11615  11221    793   -452   -745       C  
ATOM   1466  CE  LYS A 189      26.604   5.548 -20.878  1.00 86.60           C  
ANISOU 1466  CE  LYS A 189    10023  11557  11323    736   -445   -713       C  
ATOM   1467  NZ  LYS A 189      27.600   4.459 -20.700  1.00 89.17           N  
ANISOU 1467  NZ  LYS A 189    10323  11843  11714    719   -441   -710       N  
ATOM   1468  N   ILE A 190      25.140   9.811 -26.108  1.00 76.48           N  
ANISOU 1468  N   ILE A 190     8837  10609   9614    990   -485   -817       N  
ATOM   1469  CA  ILE A 190      25.726  10.583 -27.193  1.00 77.32           C  
ANISOU 1469  CA  ILE A 190     8972  10781   9627   1041   -477   -806       C  
ATOM   1470  C   ILE A 190      25.082  11.962 -27.277  1.00 77.89           C  
ANISOU 1470  C   ILE A 190     9081  10886   9626   1060   -474   -767       C  
ATOM   1471  O   ILE A 190      25.776  12.978 -27.437  1.00 78.75           O  
ANISOU 1471  O   ILE A 190     9231  11019   9671   1071   -449   -704       O  
ATOM   1472  CB  ILE A 190      25.657   9.829 -28.542  1.00 78.43           C  
ANISOU 1472  CB  ILE A 190     9079  10971   9749   1096   -501   -895       C  
ATOM   1473  CG1 ILE A 190      26.800   8.818 -28.660  1.00 79.99           C  
ANISOU 1473  CG1 ILE A 190     9255  11148   9992   1085   -491   -910       C  
ATOM   1474  CG2 ILE A 190      25.810  10.794 -29.703  1.00 79.65           C  
ANISOU 1474  CG2 ILE A 190     9266  11204   9795   1156   -498   -887       C  
ATOM   1475  CD1 ILE A 190      26.657   7.567 -27.815  1.00 82.98           C  
ANISOU 1475  CD1 ILE A 190     9590  11456  10484   1038   -500   -938       C  
ATOM   1476  N   ARG A 191      23.759  11.999 -27.138  1.00 79.91           N  
ANISOU 1476  N   ARG A 191     9322  11141   9899   1063   -499   -805       N  
ATOM   1477  CA  ARG A 191      23.038  13.268 -27.119  1.00 78.34           C  
ANISOU 1477  CA  ARG A 191     9155  10968   9643   1078   -498   -771       C  
ATOM   1478  C   ARG A 191      23.673  14.181 -26.063  1.00 74.40           C  
ANISOU 1478  C   ARG A 191     8696  10434   9138   1033   -462   -674       C  
ATOM   1479  O   ARG A 191      24.076  15.319 -26.366  1.00 68.68           O  
ANISOU 1479  O   ARG A 191     8010   9741   8345   1053   -443   -620       O  
ATOM   1480  CB  ARG A 191      21.533  13.050 -26.855  1.00 80.80           C  
ANISOU 1480  CB  ARG A 191     9439  11267   9996   1074   -528   -825       C  
ATOM   1481  CG  ARG A 191      20.795  12.219 -27.910  1.00 81.21           C  
ANISOU 1481  CG  ARG A 191     9448  11356  10054   1122   -567   -928       C  
ATOM   1482  CD  ARG A 191      19.282  12.139 -27.668  1.00 78.89           C  
ANISOU 1482  CD  ARG A 191     9126  11050   9798   1120   -596   -979       C  
ATOM   1483  NE  ARG A 191      18.800  10.757 -27.780  1.00 79.42           N  
ANISOU 1483  NE  ARG A 191     9136  11094   9946   1116   -621  -1068       N  
ATOM   1484  CZ  ARG A 191      18.169  10.078 -26.816  1.00 79.61           C  
ANISOU 1484  CZ  ARG A 191     9130  11055  10064   1068   -621  -1085       C  
ATOM   1485  NH1 ARG A 191      17.893  10.647 -25.650  1.00 77.51           N  
ANISOU 1485  NH1 ARG A 191     8885  10746   9819   1020   -600  -1022       N  
ATOM   1486  NH2 ARG A 191      17.790   8.818 -27.023  1.00 75.81           N  
ANISOU 1486  NH2 ARG A 191     8593  10553   9658   1069   -643  -1167       N  
ATOM   1487  N   SER A 192      23.813  13.648 -24.846  1.00 73.00           N  
ANISOU 1487  N   SER A 192     8508  10193   9036    973   -452   -652       N  
ATOM   1488  CA  SER A 192      24.387  14.391 -23.718  1.00 73.34           C  
ANISOU 1488  CA  SER A 192     8584  10199   9081    925   -421   -566       C  
ATOM   1489  C   SER A 192      25.748  14.970 -24.057  1.00 75.01           C  
ANISOU 1489  C   SER A 192     8827  10430   9243    936   -393   -511       C  
ATOM   1490  O   SER A 192      25.971  16.182 -23.897  1.00 73.29           O  
ANISOU 1490  O   SER A 192     8646  10224   8979    937   -372   -451       O  
ATOM   1491  CB  SER A 192      24.506  13.510 -22.473  1.00 75.74           C  
ANISOU 1491  CB  SER A 192     8869  10437   9472    865   -416   -556       C  
ATOM   1492  OG  SER A 192      23.308  12.800 -22.217  1.00 80.24           O  
ANISOU 1492  OG  SER A 192     9404  10985  10097    855   -438   -612       O  
ATOM   1493  N   HIS A 193      26.651  14.108 -24.533  1.00 71.07           N  
ANISOU 1493  N   HIS A 193     8312   9933   8760    945   -392   -533       N  
ATOM   1494  CA  HIS A 193      27.997  14.539 -24.897  1.00 68.78           C  
ANISOU 1494  CA  HIS A 193     8045   9658   8429    956   -364   -486       C  
ATOM   1495  C   HIS A 193      27.924  15.710 -25.835  1.00 68.24           C  
ANISOU 1495  C   HIS A 193     8008   9648   8272   1006   -355   -467       C  
ATOM   1496  O   HIS A 193      28.549  16.761 -25.599  1.00 65.93           O  
ANISOU 1496  O   HIS A 193     7750   9356   7944    999   -326   -398       O  
ATOM   1497  CB  HIS A 193      28.782  13.399 -25.542  1.00 71.62           C  
ANISOU 1497  CB  HIS A 193     8378  10023   8813    970   -369   -530       C  
ATOM   1498  CG  HIS A 193      29.202  12.307 -24.579  1.00 73.29           C  
ANISOU 1498  CG  HIS A 193     8563  10171   9113    919   -370   -531       C  
ATOM   1499  ND1 HIS A 193      29.859  12.561 -23.425  1.00 73.19           N  
ANISOU 1499  ND1 HIS A 193     8568  10113   9129    869   -350   -464       N  
ATOM   1500  CD2 HIS A 193      29.072  10.921 -24.659  1.00 71.08           C  
ANISOU 1500  CD2 HIS A 193     8239   9869   8901    913   -391   -593       C  
ATOM   1501  CE1 HIS A 193      30.111  11.401 -22.788  1.00 71.30           C  
ANISOU 1501  CE1 HIS A 193     8299   9825   8968    835   -357   -478       C  
ATOM   1502  NE2 HIS A 193      29.633  10.397 -23.546  1.00 70.49           N  
ANISOU 1502  NE2 HIS A 193     8157   9734   8891    861   -381   -557       N  
ATOM   1503  N   ALA A 194      27.129  15.542 -26.893  1.00 68.02           N  
ANISOU 1503  N   ALA A 194     7966   9669   8209   1057   -381   -529       N  
ATOM   1504  CA  ALA A 194      26.954  16.566 -27.917  1.00 68.90           C  
ANISOU 1504  CA  ALA A 194     8104   9843   8232   1113   -377   -516       C  
ATOM   1505  C   ALA A 194      26.573  17.918 -27.313  1.00 68.81           C  
ANISOU 1505  C   ALA A 194     8127   9823   8196   1099   -361   -450       C  
ATOM   1506  O   ALA A 194      27.235  18.933 -27.573  1.00 70.16           O  
ANISOU 1506  O   ALA A 194     8331  10012   8315   1114   -331   -390       O  
ATOM   1507  CB  ALA A 194      25.925  16.115 -28.936  1.00 69.09           C  
ANISOU 1507  CB  ALA A 194     8104   9916   8232   1165   -415   -598       C  
ATOM   1508  N   VAL A 195      25.536  17.921 -26.477  1.00 69.08           N  
ANISOU 1508  N   VAL A 195     8151   9826   8272   1069   -377   -461       N  
ATOM   1509  CA  VAL A 195      25.055  19.158 -25.854  1.00 67.03           C  
ANISOU 1509  CA  VAL A 195     7919   9555   7995   1053   -365   -407       C  
ATOM   1510  C   VAL A 195      26.078  19.703 -24.867  1.00 65.42           C  
ANISOU 1510  C   VAL A 195     7738   9309   7808   1005   -328   -330       C  
ATOM   1511  O   VAL A 195      26.417  20.899 -24.892  1.00 63.52           O  
ANISOU 1511  O   VAL A 195     7530   9079   7527   1013   -302   -272       O  
ATOM   1512  CB  VAL A 195      23.699  18.955 -25.141  1.00 70.37           C  
ANISOU 1512  CB  VAL A 195     8322   9951   8464   1029   -390   -442       C  
ATOM   1513  CG1 VAL A 195      23.139  20.285 -24.644  1.00 66.48           C  
ANISOU 1513  CG1 VAL A 195     7855   9454   7949   1021   -378   -392       C  
ATOM   1514  CG2 VAL A 195      22.707  18.271 -26.072  1.00 69.76           C  
ANISOU 1514  CG2 VAL A 195     8214   9911   8382   1074   -429   -527       C  
ATOM   1515  N   ALA A 196      26.583  18.818 -24.011  1.00 68.03           N  
ANISOU 1515  N   ALA A 196     8053   9593   8203    957   -325   -332       N  
ATOM   1516  CA  ALA A 196      27.568  19.207 -22.998  1.00 67.57           C  
ANISOU 1516  CA  ALA A 196     8013   9493   8166    910   -295   -265       C  
ATOM   1517  C   ALA A 196      28.779  19.866 -23.650  1.00 65.06           C  
ANISOU 1517  C   ALA A 196     7719   9200   7799    934   -265   -220       C  
ATOM   1518  O   ALA A 196      29.396  20.764 -23.074  1.00 63.18           O  
ANISOU 1518  O   ALA A 196     7505   8944   7556    912   -237   -158       O  
ATOM   1519  CB  ALA A 196      27.985  18.008 -22.161  1.00 68.46           C  
ANISOU 1519  CB  ALA A 196     8102   9559   8351    863   -300   -278       C  
ATOM   1520  N   CYS A 197      29.097  19.430 -24.865  1.00 67.84           N  
ANISOU 1520  N   CYS A 197     8064   9594   8118    982   -270   -255       N  
ATOM   1521  CA  CYS A 197      30.181  20.040 -25.620  1.00 72.13           C  
ANISOU 1521  CA  CYS A 197     8629  10165   8611   1011   -239   -216       C  
ATOM   1522  C   CYS A 197      29.861  21.465 -26.045  1.00 74.89           C  
ANISOU 1522  C   CYS A 197     9010  10546   8899   1043   -223   -173       C  
ATOM   1523  O   CYS A 197      30.526  22.413 -25.598  1.00 76.69           O  
ANISOU 1523  O   CYS A 197     9262  10756   9122   1024   -190   -108       O  
ATOM   1524  CB  CYS A 197      30.550  19.175 -26.814  1.00 77.98           C  
ANISOU 1524  CB  CYS A 197     9353  10947   9331   1055   -249   -268       C  
ATOM   1525  SG  CYS A 197      31.720  17.891 -26.336  1.00 82.06           S  
ANISOU 1525  SG  CYS A 197     9843  11420   9915   1016   -244   -281       S  
ATOM   1526  N   VAL A 198      28.830  21.615 -26.881  1.00 73.25           N  
ANISOU 1526  N   VAL A 198     8800  10383   8648   1090   -246   -210       N  
ATOM   1527  CA  VAL A 198      28.380  22.930 -27.338  1.00 69.54           C  
ANISOU 1527  CA  VAL A 198     8357   9944   8120   1125   -234   -171       C  
ATOM   1528  C   VAL A 198      28.304  23.915 -26.163  1.00 67.81           C  
ANISOU 1528  C   VAL A 198     8155   9680   7929   1079   -215   -113       C  
ATOM   1529  O   VAL A 198      28.837  25.040 -26.228  1.00 64.99           O  
ANISOU 1529  O   VAL A 198     7824   9324   7544   1086   -181    -51       O  
ATOM   1530  CB  VAL A 198      27.018  22.823 -28.044  1.00 71.35           C  
ANISOU 1530  CB  VAL A 198     8575  10215   8319   1169   -273   -227       C  
ATOM   1531  CG1 VAL A 198      26.557  24.186 -28.523  1.00 73.34           C  
ANISOU 1531  CG1 VAL A 198     8855  10498   8512   1207   -262   -184       C  
ATOM   1532  CG2 VAL A 198      27.096  21.858 -29.219  1.00 71.66           C  
ANISOU 1532  CG2 VAL A 198     8595  10302   8329   1217   -294   -291       C  
ATOM   1533  N   ASN A 199      27.679  23.458 -25.077  1.00 68.14           N  
ANISOU 1533  N   ASN A 199     8181   9680   8029   1031   -233   -133       N  
ATOM   1534  CA  ASN A 199      27.471  24.273 -23.876  1.00 65.68           C  
ANISOU 1534  CA  ASN A 199     7881   9327   7747    984   -219    -89       C  
ATOM   1535  C   ASN A 199      28.708  25.005 -23.387  1.00 67.21           C  
ANISOU 1535  C   ASN A 199     8096   9496   7945    958   -179    -21       C  
ATOM   1536  O   ASN A 199      28.602  26.091 -22.808  1.00 61.48           O  
ANISOU 1536  O   ASN A 199     7387   8753   7221    941   -160     24       O  
ATOM   1537  CB  ASN A 199      26.869  23.434 -22.748  1.00 67.47           C  
ANISOU 1537  CB  ASN A 199     8085   9511   8039    932   -241   -121       C  
ATOM   1538  CG  ASN A 199      25.387  23.137 -22.960  1.00 73.32           C  
ANISOU 1538  CG  ASN A 199     8809  10267   8784    950   -276   -178       C  
ATOM   1539  OD1 ASN A 199      24.827  22.215 -22.355  1.00 70.63           O  
ANISOU 1539  OD1 ASN A 199     8443   9899   8493    920   -297   -218       O  
ATOM   1540  ND2 ASN A 199      24.749  23.913 -23.832  1.00 71.74           N  
ANISOU 1540  ND2 ASN A 199     8619  10107   8531   1000   -283   -180       N  
ATOM   1541  N   GLN A 200      29.881  24.424 -23.650  1.00 71.26           N  
ANISOU 1541  N   GLN A 200     8605  10007   8463    957   -165    -16       N  
ATOM   1542  CA  GLN A 200      31.154  24.993 -23.187  1.00 73.97           C  
ANISOU 1542  CA  GLN A 200     8964  10325   8818    932   -128     42       C  
ATOM   1543  C   GLN A 200      31.494  26.337 -23.801  1.00 73.94           C  
ANISOU 1543  C   GLN A 200     8985  10342   8767    964    -94     95       C  
ATOM   1544  O   GLN A 200      32.345  27.061 -23.288  1.00 68.90           O  
ANISOU 1544  O   GLN A 200     8358   9677   8143    940    -62    146       O  
ATOM   1545  CB  GLN A 200      32.306  24.022 -23.448  1.00 78.08           C  
ANISOU 1545  CB  GLN A 200     9471  10840   9355    928   -122     30       C  
ATOM   1546  CG  GLN A 200      32.200  22.713 -22.684  1.00 78.03           C  
ANISOU 1546  CG  GLN A 200     9438  10802   9407    889   -150    -10       C  
ATOM   1547  CD  GLN A 200      32.089  22.913 -21.185  1.00 77.82           C  
ANISOU 1547  CD  GLN A 200     9413  10727   9428    829   -149     17       C  
ATOM   1548  OE1 GLN A 200      32.830  23.701 -20.582  1.00 75.08           O  
ANISOU 1548  OE1 GLN A 200     9081  10358   9088    804   -123     68       O  
ATOM   1549  NE2 GLN A 200      31.152  22.199 -20.576  1.00 80.35           N  
ANISOU 1549  NE2 GLN A 200     9717  11030   9783    806   -178    -20       N  
ATOM   1550  N   PHE A 201      30.817  26.677 -24.891  1.00 80.35           N  
ANISOU 1550  N   PHE A 201     9804  11201   9524   1020   -101     82       N  
ATOM   1551  CA  PHE A 201      31.214  27.833 -25.668  1.00 82.59           C  
ANISOU 1551  CA  PHE A 201    10112  11510   9758   1059    -67    133       C  
ATOM   1552  C   PHE A 201      30.131  28.896 -25.809  1.00 81.37           C  
ANISOU 1552  C   PHE A 201     9970  11370   9576   1083    -72    150       C  
ATOM   1553  O   PHE A 201      30.189  29.747 -26.699  1.00 81.71           O  
ANISOU 1553  O   PHE A 201    10032  11445   9569   1130    -51    184       O  
ATOM   1554  CB  PHE A 201      31.761  27.355 -27.009  1.00 86.67           C  
ANISOU 1554  CB  PHE A 201    10629  12075  10225   1112    -61    117       C  
ATOM   1555  CG  PHE A 201      32.887  26.368 -26.865  1.00 88.52           C  
ANISOU 1555  CG  PHE A 201    10850  12292  10492   1089    -54    103       C  
ATOM   1556  CD1 PHE A 201      34.092  26.746 -26.259  1.00 88.42           C  
ANISOU 1556  CD1 PHE A 201    10842  12241  10512   1054    -18    152       C  
ATOM   1557  CD2 PHE A 201      32.739  25.055 -27.297  1.00 91.39           C  
ANISOU 1557  CD2 PHE A 201    11190  12674  10858   1101    -84     38       C  
ATOM   1558  CE1 PHE A 201      35.131  25.837 -26.102  1.00 90.48           C  
ANISOU 1558  CE1 PHE A 201    11089  12484  10806   1032    -13    138       C  
ATOM   1559  CE2 PHE A 201      33.778  24.143 -27.151  1.00 93.81           C  
ANISOU 1559  CE2 PHE A 201    11482  12962  11200   1079    -78     25       C  
ATOM   1560  CZ  PHE A 201      34.974  24.535 -26.551  1.00 90.46           C  
ANISOU 1560  CZ  PHE A 201    11064  12500  10805   1044    -43     76       C  
ATOM   1561  N   ILE A 202      29.168  28.862 -24.893  1.00 78.08           N  
ANISOU 1561  N   ILE A 202     9545  10928   9196   1049    -96    129       N  
ATOM   1562  CA  ILE A 202      28.052  29.796 -24.922  1.00 71.65           C  
ANISOU 1562  CA  ILE A 202     8738  10121   8364   1067   -104    138       C  
ATOM   1563  C   ILE A 202      28.439  31.125 -24.293  1.00 73.39           C  
ANISOU 1563  C   ILE A 202     8974  10310   8600   1044    -67    204       C  
ATOM   1564  O   ILE A 202      28.433  32.136 -24.979  1.00 76.13           O  
ANISOU 1564  O   ILE A 202     9338  10677   8910   1083    -46    244       O  
ATOM   1565  CB  ILE A 202      26.797  29.211 -24.257  1.00 71.21           C  
ANISOU 1565  CB  ILE A 202     8663  10053   8342   1042   -145     85       C  
ATOM   1566  CG1 ILE A 202      26.347  27.947 -24.994  1.00 67.97           C  
ANISOU 1566  CG1 ILE A 202     8232   9675   7917   1071   -182     16       C  
ATOM   1567  CG2 ILE A 202      25.675  30.238 -24.231  1.00 71.49           C  
ANISOU 1567  CG2 ILE A 202     8705  10094   8365   1058   -152     95       C  
ATOM   1568  CD1 ILE A 202      25.277  27.156 -24.271  1.00 71.94           C  
ANISOU 1568  CD1 ILE A 202     8711  10158   8466   1040   -219    -40       C  
ATOM   1569  N   ILE A 203      28.803  31.127 -23.010  1.00 73.61           N  
ANISOU 1569  N   ILE A 203     8996  10288   8682    982    -59    215       N  
ATOM   1570  CA  ILE A 203      29.062  32.384 -22.284  1.00 75.61           C  
ANISOU 1570  CA  ILE A 203     9261  10509   8959    955    -27    268       C  
ATOM   1571  C   ILE A 203      30.249  33.141 -22.868  1.00 75.53           C  
ANISOU 1571  C   ILE A 203     9266  10502   8931    977     18    324       C  
ATOM   1572  O   ILE A 203      30.349  34.366 -22.745  1.00 75.06           O  
ANISOU 1572  O   ILE A 203     9216  10427   8875    978     47    371       O  
ATOM   1573  CB  ILE A 203      29.237  32.167 -20.756  1.00 79.25           C  
ANISOU 1573  CB  ILE A 203     9711  10920   9479    885    -29    264       C  
ATOM   1574  CG1 ILE A 203      27.937  31.660 -20.137  1.00 81.97           C  
ANISOU 1574  CG1 ILE A 203    10042  11259   9843    864    -66    217       C  
ATOM   1575  CG2 ILE A 203      29.617  33.462 -20.039  1.00 78.47           C  
ANISOU 1575  CG2 ILE A 203     9621  10789   9405    859      5    314       C  
ATOM   1576  CD1 ILE A 203      27.849  30.156 -20.074  1.00 85.27           C  
ANISOU 1576  CD1 ILE A 203    10443  11680  10274    853    -96    166       C  
ATOM   1577  N   SER A 204      31.133  32.397 -23.522  1.00 79.53           N  
ANISOU 1577  N   SER A 204     9772  11027   9421    994     24    318       N  
ATOM   1578  CA  SER A 204      32.277  32.970 -24.218  1.00 81.86           C  
ANISOU 1578  CA  SER A 204    10080  11329   9695   1019     68    367       C  
ATOM   1579  C   SER A 204      31.857  33.742 -25.483  1.00 88.18           C  
ANISOU 1579  C   SER A 204    10898  12174  10435   1085     81    392       C  
ATOM   1580  O   SER A 204      32.660  34.487 -26.057  1.00 91.34           O  
ANISOU 1580  O   SER A 204    11310  12578  10817   1109    123    444       O  
ATOM   1581  CB  SER A 204      33.269  31.860 -24.571  1.00 76.42           C  
ANISOU 1581  CB  SER A 204     9382  10648   9005   1019     69    346       C  
ATOM   1582  OG  SER A 204      32.741  31.000 -25.566  1.00 72.89           O  
ANISOU 1582  OG  SER A 204     8932  10250   8515   1063     40    300       O  
ATOM   1583  N   ARG A 205      30.596  33.567 -25.893  1.00 90.11           N  
ANISOU 1583  N   ARG A 205    11140  12449  10649   1115     44    357       N  
ATOM   1584  CA  ARG A 205      30.056  34.156 -27.126  1.00 93.45           C  
ANISOU 1584  CA  ARG A 205    11578  12920  11007   1184     47    374       C  
ATOM   1585  C   ARG A 205      30.882  33.696 -28.319  1.00 94.10           C  
ANISOU 1585  C   ARG A 205    11668  13046  11039   1229     63    378       C  
ATOM   1586  O   ARG A 205      31.339  34.508 -29.125  1.00 95.28           O  
ANISOU 1586  O   ARG A 205    11836  13216  11150   1270    100    430       O  
ATOM   1587  CB  ARG A 205      30.005  35.692 -27.051  1.00 94.20           C  
ANISOU 1587  CB  ARG A 205    11689  12998  11106   1192     82    440       C  
ATOM   1588  CG  ARG A 205      28.912  36.240 -26.152  1.00 95.68           C  
ANISOU 1588  CG  ARG A 205    11869  13156  11329   1164     62    432       C  
ATOM   1589  CD  ARG A 205      28.967  37.755 -26.077  1.00 98.97           C  
ANISOU 1589  CD  ARG A 205    12297  13551  11756   1171    100    497       C  
ATOM   1590  NE  ARG A 205      28.070  38.266 -25.042  1.00103.54           N  
ANISOU 1590  NE  ARG A 205    12867  14095  12380   1133     85    486       N  
ATOM   1591  CZ  ARG A 205      26.787  38.569 -25.231  1.00106.21           C  
ANISOU 1591  CZ  ARG A 205    13203  14449  12702   1158     56    469       C  
ATOM   1592  NH1 ARG A 205      26.225  38.420 -26.425  1.00108.60           N  
ANISOU 1592  NH1 ARG A 205    13515  14805  12945   1222     37    460       N  
ATOM   1593  NH2 ARG A 205      26.060  39.025 -24.219  1.00104.85           N  
ANISOU 1593  NH2 ARG A 205    13020  14241  12576   1119     46    459       N  
ATOM   1594  N   THR A 206      31.059  32.383 -28.423  1.00 93.48           N  
ANISOU 1594  N   THR A 206    11574  12981  10961   1223     37    322       N  
ATOM   1595  CA  THR A 206      31.988  31.804 -29.383  1.00 92.10           C  
ANISOU 1595  CA  THR A 206    11403  12840  10750   1255     54    318       C  
ATOM   1596  C   THR A 206      31.522  31.954 -30.835  1.00 91.71           C  
ANISOU 1596  C   THR A 206    11367  12860  10618   1333     49    315       C  
ATOM   1597  O   THR A 206      30.482  31.424 -31.231  1.00 90.67           O  
ANISOU 1597  O   THR A 206    11227  12764  10459   1360      4    262       O  
ATOM   1598  CB  THR A 206      32.343  30.348 -29.008  1.00 90.62           C  
ANISOU 1598  CB  THR A 206    11193  12642  10598   1222     28    258       C  
ATOM   1599  OG1 THR A 206      33.315  30.366 -27.956  1.00 84.87           O  
ANISOU 1599  OG1 THR A 206    10458  11857   9931   1163     52    284       O  
ATOM   1600  CG2 THR A 206      32.914  29.584 -30.190  1.00 92.34           C  
ANISOU 1600  CG2 THR A 206    11409  12909  10768   1267     32    233       C  
ATOM   1601  N   GLN A 207      32.327  32.695 -31.596  1.00 90.84           N  
ANISOU 1601  N   GLN A 207    11277  12769  10471   1367     96    374       N  
ATOM   1602  CA  GLN A 207      32.144  32.958 -33.024  1.00 85.76           C  
ANISOU 1602  CA  GLN A 207    10650  12193   9741   1444    103    387       C  
ATOM   1603  C   GLN A 207      31.472  31.809 -33.762  1.00 81.02           C  
ANISOU 1603  C   GLN A 207    10037  11649   9096   1480     53    308       C  
ATOM   1604  O   GLN A 207      30.401  31.977 -34.327  1.00 79.35           O  
ANISOU 1604  O   GLN A 207     9830  11480   8840   1525     21    289       O  
ATOM   1605  CB  GLN A 207      33.514  33.273 -33.651  1.00 91.47           C  
ANISOU 1605  CB  GLN A 207    11388  12924  10444   1462    163    439       C  
ATOM   1606  CG  GLN A 207      33.492  33.846 -35.061  1.00 91.90           C  
ANISOU 1606  CG  GLN A 207    11466  13043  10409   1540    186    477       C  
ATOM   1607  CD  GLN A 207      32.949  35.262 -35.126  1.00 96.74           C  
ANISOU 1607  CD  GLN A 207    12099  13650  11009   1563    206    544       C  
ATOM   1608  OE1 GLN A 207      32.352  35.765 -34.168  1.00 93.63           O  
ANISOU 1608  OE1 GLN A 207    11699  13210  10667   1524    192    551       O  
ATOM   1609  NE2 GLN A 207      33.149  35.916 -36.268  1.00 98.55           N  
ANISOU 1609  NE2 GLN A 207    12352  13926  11168   1626    240    596       N  
ATOM   1610  N   ALA A 208      32.100  30.637 -33.738  1.00 80.68           N  
ANISOU 1610  N   ALA A 208     9977  11606   9073   1461     45    260       N  
ATOM   1611  CA  ALA A 208      31.560  29.451 -34.403  1.00 79.03           C  
ANISOU 1611  CA  ALA A 208     9751  11447   8832   1492     -1    178       C  
ATOM   1612  C   ALA A 208      30.129  29.121 -33.977  1.00 79.78           C  
ANISOU 1612  C   ALA A 208     9829  11539   8945   1484    -59    122       C  
ATOM   1613  O   ALA A 208      29.354  28.603 -34.774  1.00 80.83           O  
ANISOU 1613  O   ALA A 208     9953  11726   9032   1531    -98     66       O  
ATOM   1614  CB  ALA A 208      32.468  28.256 -34.173  1.00 77.45           C  
ANISOU 1614  CB  ALA A 208     9529  11228   8670   1459     -1    136       C  
ATOM   1615  N   LEU A 209      29.790  29.412 -32.722  1.00 78.92           N  
ANISOU 1615  N   LEU A 209     9714  11370   8904   1426    -65    134       N  
ATOM   1616  CA  LEU A 209      28.468  29.082 -32.197  1.00 78.12           C  
ANISOU 1616  CA  LEU A 209     9595  11259   8830   1412   -115     82       C  
ATOM   1617  C   LEU A 209      27.457  30.177 -32.499  1.00 76.62           C  
ANISOU 1617  C   LEU A 209     9419  11089   8602   1449   -124    110       C  
ATOM   1618  O   LEU A 209      26.343  29.885 -32.924  1.00 75.70           O  
ANISOU 1618  O   LEU A 209     9292  11008   8462   1482   -168     59       O  
ATOM   1619  CB  LEU A 209      28.531  28.819 -30.687  1.00 78.28           C  
ANISOU 1619  CB  LEU A 209     9600  11206   8938   1333   -118     78       C  
ATOM   1620  CG  LEU A 209      27.244  28.441 -29.931  1.00 76.03           C  
ANISOU 1620  CG  LEU A 209     9294  10900   8695   1305   -163     27       C  
ATOM   1621  CD1 LEU A 209      26.627  27.137 -30.433  1.00 72.44           C  
ANISOU 1621  CD1 LEU A 209     8812  10476   8234   1326   -210    -60       C  
ATOM   1622  CD2 LEU A 209      27.537  28.352 -28.440  1.00 78.94           C  
ANISOU 1622  CD2 LEU A 209     9655  11198   9142   1228   -153     42       C  
ATOM   1623  N   MET A 210      27.868  31.427 -32.274  1.00 78.34           N  
ANISOU 1623  N   MET A 210     9661  11284   8821   1444    -81    190       N  
ATOM   1624  CA  MET A 210      27.018  32.618 -32.434  1.00 78.05           C  
ANISOU 1624  CA  MET A 210     9639  11256   8761   1473    -81    229       C  
ATOM   1625  C   MET A 210      26.440  32.777 -33.825  1.00 80.31           C  
ANISOU 1625  C   MET A 210     9937  11618   8960   1556    -99    221       C  
ATOM   1626  O   MET A 210      25.321  33.282 -33.987  1.00 84.59           O  
ANISOU 1626  O   MET A 210    10479  12175   9484   1583   -127    216       O  
ATOM   1627  CB  MET A 210      27.796  33.885 -32.068  1.00 79.60           C  
ANISOU 1627  CB  MET A 210     9856  11414   8975   1456    -24    318       C  
ATOM   1628  CG  MET A 210      28.325  33.899 -30.643  1.00 83.27           C  
ANISOU 1628  CG  MET A 210    10311  11806   9524   1375     -7    330       C  
ATOM   1629  SD  MET A 210      27.051  33.951 -29.361  1.00 89.06           S  
ANISOU 1629  SD  MET A 210    11025  12494  10319   1325    -46    294       S  
ATOM   1630  CE  MET A 210      26.389  32.277 -29.376  1.00 77.79           C  
ANISOU 1630  CE  MET A 210     9571  11088   8899   1319   -104    194       C  
ATOM   1631  N   LEU A 211      27.218  32.361 -34.821  1.00 79.88           N  
ANISOU 1631  N   LEU A 211     9890  11609   8850   1596    -83    221       N  
ATOM   1632  CA  LEU A 211      26.785  32.395 -36.205  1.00 78.65           C  
ANISOU 1632  CA  LEU A 211     9746  11535   8604   1678   -100    210       C  
ATOM   1633  C   LEU A 211      26.178  31.039 -36.586  1.00 79.51           C  
ANISOU 1633  C   LEU A 211     9827  11682   8700   1693   -157    108       C  
ATOM   1634  O   LEU A 211      25.996  30.740 -37.764  1.00 79.33           O  
ANISOU 1634  O   LEU A 211     9809  11732   8602   1759   -175     80       O  
ATOM   1635  CB  LEU A 211      27.956  32.774 -37.123  1.00 78.36           C  
ANISOU 1635  CB  LEU A 211     9733  11530   8509   1716    -46    268       C  
ATOM   1636  CG  LEU A 211      28.641  34.137 -36.945  1.00 77.87           C  
ANISOU 1636  CG  LEU A 211     9698  11435   8456   1710     16    372       C  
ATOM   1637  CD1 LEU A 211      30.102  34.032 -37.348  1.00 78.41           C  
ANISOU 1637  CD1 LEU A 211     9776  11505   8510   1711     72    408       C  
ATOM   1638  CD2 LEU A 211      27.958  35.245 -37.735  1.00 77.02           C  
ANISOU 1638  CD2 LEU A 211     9613  11367   8284   1775     19    424       C  
ATOM   1639  N   HIS A 212      25.872  30.222 -35.581  1.00 76.58           N  
ANISOU 1639  N   HIS A 212     9428  11264   8404   1634   -185     52       N  
ATOM   1640  CA  HIS A 212      25.202  28.939 -35.792  1.00 80.45           C  
ANISOU 1640  CA  HIS A 212     9888  11780   8901   1641   -239    -47       C  
ATOM   1641  C   HIS A 212      24.041  28.779 -34.843  1.00 80.98           C  
ANISOU 1641  C   HIS A 212     9932  11806   9031   1602   -279    -88       C  
ATOM   1642  O   HIS A 212      23.417  27.706 -34.736  1.00 76.21           O  
ANISOU 1642  O   HIS A 212     9297  11204   8455   1593   -323   -171       O  
ATOM   1643  CB  HIS A 212      26.205  27.802 -35.655  1.00 85.33           C  
ANISOU 1643  CB  HIS A 212    10489  12383   9549   1609   -229    -82       C  
ATOM   1644  CG  HIS A 212      26.980  27.525 -36.923  1.00 90.00           C  
ANISOU 1644  CG  HIS A 212    11091  13039  10067   1666   -212    -85       C  
ATOM   1645  ND1 HIS A 212      27.622  28.491 -37.609  1.00 90.85           N  
ANISOU 1645  ND1 HIS A 212    11231  13175  10112   1705   -167    -10       N  
ATOM   1646  CD2 HIS A 212      27.198  26.339 -37.621  1.00 92.25           C  
ANISOU 1646  CD2 HIS A 212    11355  13365  10331   1689   -233   -158       C  
ATOM   1647  CE1 HIS A 212      28.212  27.956 -38.694  1.00 92.69           C  
ANISOU 1647  CE1 HIS A 212    11467  13468  10285   1751   -159    -33       C  
ATOM   1648  NE2 HIS A 212      27.952  26.638 -38.700  1.00 95.25           N  
ANISOU 1648  NE2 HIS A 212    11757  13800  10633   1742   -201   -126       N  
ATOM   1649  N   ILE A 213      23.720  29.891 -34.190  1.00 78.26           N  
ANISOU 1649  N   ILE A 213     9603  11425   8708   1581   -262    -29       N  
ATOM   1650  CA  ILE A 213      22.782  29.941 -33.069  1.00 86.32           C  
ANISOU 1650  CA  ILE A 213    10605  12394   9797   1532   -286    -51       C  
ATOM   1651  C   ILE A 213      21.378  29.355 -33.326  1.00 87.62           C  
ANISOU 1651  C   ILE A 213    10744  12586   9962   1557   -347   -133       C  
ATOM   1652  O   ILE A 213      20.810  28.700 -32.442  1.00 85.67           O  
ANISOU 1652  O   ILE A 213    10471  12298   9782   1509   -371   -182       O  
ATOM   1653  CB  ILE A 213      22.726  31.386 -32.483  1.00 88.10           C  
ANISOU 1653  CB  ILE A 213    10854  12583  10038   1515   -253     30       C  
ATOM   1654  CG1 ILE A 213      22.118  31.395 -31.076  1.00 88.18           C  
ANISOU 1654  CG1 ILE A 213    10846  12527  10130   1447   -263     16       C  
ATOM   1655  CG2 ILE A 213      22.054  32.370 -33.441  1.00 85.27           C  
ANISOU 1655  CG2 ILE A 213    10514  12274   9613   1586   -261     60       C  
ATOM   1656  CD1 ILE A 213      22.998  30.755 -30.025  1.00 90.01           C  
ANISOU 1656  CD1 ILE A 213    11069  12704  10426   1376   -242     15       C  
ATOM   1657  N   ASP A 214      20.845  29.574 -34.530  1.00 89.81           N  
ANISOU 1657  N   ASP A 214    11028  12933  10165   1633   -371   -147       N  
ATOM   1658  CA  ASP A 214      19.519  29.083 -34.920  1.00 90.26           C  
ANISOU 1658  CA  ASP A 214    11058  13022  10213   1666   -432   -227       C  
ATOM   1659  C   ASP A 214      19.444  27.567 -34.943  1.00 85.96           C  
ANISOU 1659  C   ASP A 214    10478  12482   9700   1652   -465   -321       C  
ATOM   1660  O   ASP A 214      18.465  26.975 -34.490  1.00 82.59           O  
ANISOU 1660  O   ASP A 214    10020  12036   9324   1632   -504   -387       O  
ATOM   1661  CB  ASP A 214      19.138  29.621 -36.303  1.00101.27           C  
ANISOU 1661  CB  ASP A 214    12470  14498  11511   1756   -449   -219       C  
ATOM   1662  CG  ASP A 214      18.375  30.935 -36.238  1.00108.40           C  
ANISOU 1662  CG  ASP A 214    13390  15397  12401   1777   -449   -165       C  
ATOM   1663  OD1 ASP A 214      18.506  31.672 -35.236  1.00108.61           O  
ANISOU 1663  OD1 ASP A 214    13425  15361  12481   1725   -418   -110       O  
ATOM   1664  OD2 ASP A 214      17.644  31.238 -37.207  1.00116.81           O  
ANISOU 1664  OD2 ASP A 214    14458  16523  13401   1847   -482   -179       O  
ATOM   1665  N   SER A 215      20.489  26.953 -35.487  1.00 88.60           N  
ANISOU 1665  N   SER A 215    10816  12841  10007   1663   -446   -326       N  
ATOM   1666  CA  SER A 215      20.583  25.501 -35.612  1.00 89.81           C  
ANISOU 1666  CA  SER A 215    10936  13001  10189   1653   -473   -412       C  
ATOM   1667  C   SER A 215      20.606  24.873 -34.229  1.00 83.49           C  
ANISOU 1667  C   SER A 215    10112  12120   9491   1570   -469   -428       C  
ATOM   1668  O   SER A 215      19.949  23.859 -33.963  1.00 80.43           O  
ANISOU 1668  O   SER A 215     9687  11717   9154   1552   -506   -507       O  
ATOM   1669  CB  SER A 215      21.862  25.135 -36.361  1.00 90.27           C  
ANISOU 1669  CB  SER A 215    11005  13092  10200   1675   -443   -399       C  
ATOM   1670  OG  SER A 215      22.196  26.144 -37.297  1.00 97.48           O  
ANISOU 1670  OG  SER A 215    11956  14059  11025   1734   -419   -336       O  
ATOM   1671  N   PHE A 216      21.373  25.505 -33.352  1.00 79.42           N  
ANISOU 1671  N   PHE A 216     9619  11552   9006   1520   -423   -352       N  
ATOM   1672  CA  PHE A 216      21.471  25.097 -31.965  1.00 78.58           C  
ANISOU 1672  CA  PHE A 216     9497  11369   8989   1440   -414   -351       C  
ATOM   1673  C   PHE A 216      20.092  25.112 -31.305  1.00 80.30           C  
ANISOU 1673  C   PHE A 216     9695  11562   9255   1420   -448   -389       C  
ATOM   1674  O   PHE A 216      19.574  24.056 -30.901  1.00 80.92           O  
ANISOU 1674  O   PHE A 216     9738  11618   9390   1394   -476   -458       O  
ATOM   1675  CB  PHE A 216      22.450  26.030 -31.243  1.00 75.32           C  
ANISOU 1675  CB  PHE A 216     9115  10914   8588   1401   -361   -258       C  
ATOM   1676  CG  PHE A 216      22.711  25.663 -29.809  1.00 70.72           C  
ANISOU 1676  CG  PHE A 216     8522  10259   8090   1321   -348   -250       C  
ATOM   1677  CD1 PHE A 216      22.508  24.363 -29.349  1.00 68.58           C  
ANISOU 1677  CD1 PHE A 216     8217   9963   7877   1288   -373   -315       C  
ATOM   1678  CD2 PHE A 216      23.191  26.617 -28.928  1.00 67.63           C  
ANISOU 1678  CD2 PHE A 216     8153   9824   7721   1280   -310   -176       C  
ATOM   1679  CE1 PHE A 216      22.759  24.031 -28.037  1.00 66.44           C  
ANISOU 1679  CE1 PHE A 216     7938   9627   7679   1217   -360   -303       C  
ATOM   1680  CE2 PHE A 216      23.447  26.294 -27.611  1.00 67.94           C  
ANISOU 1680  CE2 PHE A 216     8183   9801   7831   1209   -299   -168       C  
ATOM   1681  CZ  PHE A 216      23.226  24.998 -27.166  1.00 68.15           C  
ANISOU 1681  CZ  PHE A 216     8178   9805   7909   1178   -324   -230       C  
ATOM   1682  N   ILE A 217      19.499  26.305 -31.236  1.00 78.76           N  
ANISOU 1682  N   ILE A 217     9518  11369   9037   1435   -444   -346       N  
ATOM   1683  CA  ILE A 217      18.201  26.526 -30.585  1.00 79.39           C  
ANISOU 1683  CA  ILE A 217     9582  11423   9161   1416   -471   -372       C  
ATOM   1684  C   ILE A 217      17.080  25.606 -31.081  1.00 79.01           C  
ANISOU 1684  C   ILE A 217     9496  11402   9122   1445   -526   -470       C  
ATOM   1685  O   ILE A 217      16.313  25.063 -30.271  1.00 72.47           O  
ANISOU 1685  O   ILE A 217     8638  10533   8363   1403   -545   -515       O  
ATOM   1686  CB  ILE A 217      17.791  28.003 -30.692  1.00 77.57           C  
ANISOU 1686  CB  ILE A 217     9377  11201   8894   1441   -459   -310       C  
ATOM   1687  CG1 ILE A 217      18.650  28.829 -29.738  1.00 76.50           C  
ANISOU 1687  CG1 ILE A 217     9267  11013   8786   1388   -407   -227       C  
ATOM   1688  CG2 ILE A 217      16.323  28.182 -30.350  1.00 79.01           C  
ANISOU 1688  CG2 ILE A 217     9539  11373   9109   1439   -495   -351       C  
ATOM   1689  CD1 ILE A 217      18.842  30.266 -30.159  1.00 77.95           C  
ANISOU 1689  CD1 ILE A 217     9484  11214   8920   1423   -379   -149       C  
ATOM   1690  N   GLU A 218      17.008  25.423 -32.401  1.00 82.00           N  
ANISOU 1690  N   GLU A 218     9874  11852   9432   1515   -550   -503       N  
ATOM   1691  CA  GLU A 218      16.030  24.524 -33.009  1.00 87.00           C  
ANISOU 1691  CA  GLU A 218    10469  12518  10068   1550   -605   -602       C  
ATOM   1692  C   GLU A 218      16.225  23.094 -32.512  1.00 86.76           C  
ANISOU 1692  C   GLU A 218    10402  12452  10110   1505   -613   -666       C  
ATOM   1693  O   GLU A 218      15.259  22.408 -32.155  1.00 87.07           O  
ANISOU 1693  O   GLU A 218    10404  12471  10208   1488   -646   -736       O  
ATOM   1694  CB  GLU A 218      16.133  24.571 -34.534  1.00 92.70           C  
ANISOU 1694  CB  GLU A 218    11199  13327  10695   1635   -625   -621       C  
ATOM   1695  CG  GLU A 218      15.162  23.637 -35.248  1.00101.07           C  
ANISOU 1695  CG  GLU A 218    12218  14428  11754   1676   -684   -730       C  
ATOM   1696  CD  GLU A 218      15.700  23.104 -36.571  1.00111.06           C  
ANISOU 1696  CD  GLU A 218    13483  15769  12945   1740   -697   -767       C  
ATOM   1697  OE1 GLU A 218      16.805  23.518 -36.997  1.00116.59           O  
ANISOU 1697  OE1 GLU A 218    14218  16493  13588   1756   -659   -704       O  
ATOM   1698  OE2 GLU A 218      15.016  22.258 -37.190  1.00111.55           O  
ANISOU 1698  OE2 GLU A 218    13509  15868  13007   1774   -746   -863       O  
ATOM   1699  N   ASN A 219      17.484  22.658 -32.492  1.00 86.86           N  
ANISOU 1699  N   ASN A 219    10426  12457  10122   1486   -582   -641       N  
ATOM   1700  CA  ASN A 219      17.841  21.316 -32.044  1.00 83.31           C  
ANISOU 1700  CA  ASN A 219     9944  11972   9740   1444   -585   -693       C  
ATOM   1701  C   ASN A 219      17.639  21.099 -30.548  1.00 79.52           C  
ANISOU 1701  C   ASN A 219     9451  11410   9351   1365   -571   -679       C  
ATOM   1702  O   ASN A 219      17.264  20.000 -30.117  1.00 74.20           O  
ANISOU 1702  O   ASN A 219     8740  10705   8748   1335   -590   -741       O  
ATOM   1703  CB  ASN A 219      19.271  20.999 -32.451  1.00 85.54           C  
ANISOU 1703  CB  ASN A 219    10241  12267   9992   1448   -555   -665       C  
ATOM   1704  CG  ASN A 219      19.382  20.647 -33.912  1.00 86.19           C  
ANISOU 1704  CG  ASN A 219    10318  12429  10003   1522   -577   -714       C  
ATOM   1705  OD1 ASN A 219      19.428  19.471 -34.264  1.00 85.67           O  
ANISOU 1705  OD1 ASN A 219    10218  12373   9961   1528   -599   -790       O  
ATOM   1706  ND2 ASN A 219      19.387  21.660 -34.776  1.00 86.20           N  
ANISOU 1706  ND2 ASN A 219    10351  12486   9914   1579   -572   -673       N  
ATOM   1707  N   LEU A 220      17.882  22.148 -29.763  1.00 72.86           N  
ANISOU 1707  N   LEU A 220     8640  10534   8509   1332   -538   -598       N  
ATOM   1708  CA  LEU A 220      17.537  22.116 -28.343  1.00 75.89           C  
ANISOU 1708  CA  LEU A 220     9015  10848   8971   1261   -526   -583       C  
ATOM   1709  C   LEU A 220      16.058  21.842 -28.112  1.00 76.90           C  
ANISOU 1709  C   LEU A 220     9110  10966   9141   1260   -563   -647       C  
ATOM   1710  O   LEU A 220      15.722  20.936 -27.345  1.00 77.48           O  
ANISOU 1710  O   LEU A 220     9154  10994   9291   1214   -570   -686       O  
ATOM   1711  CB  LEU A 220      17.939  23.407 -27.635  1.00 73.85           C  
ANISOU 1711  CB  LEU A 220     8794  10564   8700   1234   -487   -491       C  
ATOM   1712  CG  LEU A 220      19.409  23.560 -27.252  1.00 70.89           C  
ANISOU 1712  CG  LEU A 220     8445  10168   8322   1203   -443   -425       C  
ATOM   1713  CD1 LEU A 220      19.671  24.990 -26.821  1.00 66.56           C  
ANISOU 1713  CD1 LEU A 220     7932   9606   7751   1192   -409   -342       C  
ATOM   1714  CD2 LEU A 220      19.808  22.579 -26.159  1.00 69.21           C  
ANISOU 1714  CD2 LEU A 220     8213   9897   8185   1137   -434   -436       C  
ATOM   1715  N   PHE A 221      15.183  22.605 -28.781  1.00 76.45           N  
ANISOU 1715  N   PHE A 221     9057  10949   9039   1310   -587   -657       N  
ATOM   1716  CA  PHE A 221      13.735  22.394 -28.646  1.00 76.95           C  
ANISOU 1716  CA  PHE A 221     9088  11007   9143   1314   -624   -723       C  
ATOM   1717  C   PHE A 221      13.347  20.978 -29.014  1.00 77.67           C  
ANISOU 1717  C   PHE A 221     9133  11103   9274   1322   -659   -819       C  
ATOM   1718  O   PHE A 221      12.559  20.343 -28.312  1.00 78.99           O  
ANISOU 1718  O   PHE A 221     9266  11228   9519   1285   -672   -866       O  
ATOM   1719  CB  PHE A 221      12.922  23.372 -29.490  1.00 76.13           C  
ANISOU 1719  CB  PHE A 221     8995  10955   8978   1377   -649   -723       C  
ATOM   1720  CG  PHE A 221      13.072  24.796 -29.074  1.00 77.41           C  
ANISOU 1720  CG  PHE A 221     9195  11104   9112   1368   -618   -636       C  
ATOM   1721  CD1 PHE A 221      13.285  25.130 -27.740  1.00 78.33           C  
ANISOU 1721  CD1 PHE A 221     9322  11157   9283   1298   -582   -587       C  
ATOM   1722  CD2 PHE A 221      12.993  25.812 -30.015  1.00 76.12           C  
ANISOU 1722  CD2 PHE A 221     9058  10994   8871   1431   -624   -602       C  
ATOM   1723  CE1 PHE A 221      13.430  26.455 -27.359  1.00 80.50           C  
ANISOU 1723  CE1 PHE A 221     9629  11420   9538   1289   -553   -511       C  
ATOM   1724  CE2 PHE A 221      13.126  27.139 -29.641  1.00 77.10           C  
ANISOU 1724  CE2 PHE A 221     9214  11103   8977   1423   -593   -521       C  
ATOM   1725  CZ  PHE A 221      13.350  27.463 -28.313  1.00 79.03           C  
ANISOU 1725  CZ  PHE A 221     9466  11282   9279   1352   -558   -478       C  
ATOM   1726  N   ALA A 222      13.910  20.485 -30.113  1.00 77.80           N  
ANISOU 1726  N   ALA A 222     9147  11172   9242   1370   -672   -848       N  
ATOM   1727  CA  ALA A 222      13.652  19.120 -30.550  1.00 78.77           C  
ANISOU 1727  CA  ALA A 222     9223  11302   9402   1382   -705   -943       C  
ATOM   1728  C   ALA A 222      13.899  18.136 -29.404  1.00 76.53           C  
ANISOU 1728  C   ALA A 222     8916  10946   9217   1308   -686   -952       C  
ATOM   1729  O   ALA A 222      13.338  17.039 -29.383  1.00 74.97           O  
ANISOU 1729  O   ALA A 222     8672  10731   9083   1300   -712  -1032       O  
ATOM   1730  CB  ALA A 222      14.508  18.788 -31.761  1.00 79.48           C  
ANISOU 1730  CB  ALA A 222     9320  11454   9424   1435   -710   -959       C  
ATOM   1731  N   LEU A 223      14.709  18.558 -28.434  1.00 81.88           N  
ANISOU 1731  N   LEU A 223     9623  11578   9908   1255   -642   -870       N  
ATOM   1732  CA  LEU A 223      15.054  17.715 -27.286  1.00 85.31           C  
ANISOU 1732  CA  LEU A 223    10042  11944  10428   1185   -621   -865       C  
ATOM   1733  C   LEU A 223      14.150  17.871 -26.067  1.00 85.91           C  
ANISOU 1733  C   LEU A 223    10108  11964  10572   1132   -615   -858       C  
ATOM   1734  O   LEU A 223      14.084  16.971 -25.223  1.00 84.06           O  
ANISOU 1734  O   LEU A 223     9848  11676  10416   1082   -608   -876       O  
ATOM   1735  CB  LEU A 223      16.523  17.903 -26.886  1.00 83.73           C  
ANISOU 1735  CB  LEU A 223     9876  11727  10212   1156   -579   -787       C  
ATOM   1736  CG  LEU A 223      17.516  16.891 -27.468  1.00 86.12           C  
ANISOU 1736  CG  LEU A 223    10165  12042  10515   1168   -579   -814       C  
ATOM   1737  CD1 LEU A 223      17.046  15.453 -27.260  1.00 83.79           C  
ANISOU 1737  CD1 LEU A 223     9818  11714  10305   1147   -601   -893       C  
ATOM   1738  CD2 LEU A 223      17.766  17.154 -28.945  1.00 91.65           C  
ANISOU 1738  CD2 LEU A 223    10875  12818  11128   1242   -595   -835       C  
ATOM   1739  N   ALA A 224      13.449  19.002 -25.988  1.00 87.57           N  
ANISOU 1739  N   ALA A 224    10336  12185  10751   1144   -617   -832       N  
ATOM   1740  CA  ALA A 224      12.545  19.295 -24.866  1.00 87.94           C  
ANISOU 1740  CA  ALA A 224    10375  12183  10854   1097   -609   -824       C  
ATOM   1741  C   ALA A 224      11.723  18.088 -24.406  1.00 87.16           C  
ANISOU 1741  C   ALA A 224    10226  12044  10846   1068   -626   -897       C  
ATOM   1742  O   ALA A 224      11.562  17.870 -23.205  1.00 92.46           O  
ANISOU 1742  O   ALA A 224    10891  12658  11580   1008   -603   -877       O  
ATOM   1743  CB  ALA A 224      11.634  20.472 -25.197  1.00 87.44           C  
ANISOU 1743  CB  ALA A 224    10324  12149  10750   1132   -624   -817       C  
ATOM   1744  N   GLY A 225      11.238  17.295 -25.360  1.00 87.06           N  
ANISOU 1744  N   GLY A 225    10177  12063  10841   1112   -665   -982       N  
ATOM   1745  CA  GLY A 225      10.418  16.115 -25.064  1.00 89.74           C  
ANISOU 1745  CA  GLY A 225    10462  12365  11271   1091   -683  -1061       C  
ATOM   1746  C   GLY A 225      11.145  14.910 -24.477  1.00 94.35           C  
ANISOU 1746  C   GLY A 225    11027  12901  11921   1045   -664  -1063       C  
ATOM   1747  O   GLY A 225      10.509  13.909 -24.133  1.00 94.73           O  
ANISOU 1747  O   GLY A 225    11029  12910  12053   1022   -673  -1121       O  
ATOM   1748  N   ASP A 226      12.468  14.998 -24.349  1.00 91.38           N  
ANISOU 1748  N   ASP A 226    10684  12525  11512   1031   -636   -999       N  
ATOM   1749  CA  ASP A 226      13.264  13.861 -23.909  1.00 89.95           C  
ANISOU 1749  CA  ASP A 226    10485  12303  11387    994   -620   -999       C  
ATOM   1750  C   ASP A 226      13.178  13.659 -22.403  1.00 92.26           C  
ANISOU 1750  C   ASP A 226    10778  12525  11750    921   -589   -956       C  
ATOM   1751  O   ASP A 226      13.257  14.617 -21.630  1.00 92.76           O  
ANISOU 1751  O   ASP A 226    10877  12576  11790    893   -564   -887       O  
ATOM   1752  CB  ASP A 226      14.717  14.027 -24.334  1.00 89.59           C  
ANISOU 1752  CB  ASP A 226    10473  12283  11282   1008   -603   -949       C  
ATOM   1753  CG  ASP A 226      15.477  12.714 -24.358  1.00 92.91           C  
ANISOU 1753  CG  ASP A 226    10866  12679  11755    992   -600   -976       C  
ATOM   1754  OD1 ASP A 226      15.031  11.714 -23.749  1.00 94.12           O  
ANISOU 1754  OD1 ASP A 226    10982  12783  11998    957   -602  -1012       O  
ATOM   1755  OD2 ASP A 226      16.543  12.687 -24.997  1.00 96.52           O  
ANISOU 1755  OD2 ASP A 226    11340  13167  12166   1016   -595   -959       O  
ATOM   1756  N   GLU A 227      13.031  12.401 -22.001  1.00 93.19           N  
ANISOU 1756  N   GLU A 227    10855  12597  11954    892   -589   -996       N  
ATOM   1757  CA  GLU A 227      12.841  12.051 -20.598  1.00 94.77           C  
ANISOU 1757  CA  GLU A 227    11050  12731  12228    825   -561   -962       C  
ATOM   1758  C   GLU A 227      14.104  11.513 -19.924  1.00 92.68           C  
ANISOU 1758  C   GLU A 227    10800  12431  11983    786   -532   -904       C  
ATOM   1759  O   GLU A 227      14.106  11.242 -18.724  1.00 90.23           O  
ANISOU 1759  O   GLU A 227    10491  12069  11725    731   -506   -865       O  
ATOM   1760  CB  GLU A 227      11.670  11.071 -20.448  1.00101.95           C  
ANISOU 1760  CB  GLU A 227    11902  13604  13229    815   -576  -1040       C  
ATOM   1761  CG  GLU A 227      10.307  11.756 -20.485  1.00106.43           C  
ANISOU 1761  CG  GLU A 227    12461  14183  13795    828   -592  -1073       C  
ATOM   1762  CD  GLU A 227       9.148  10.805 -20.246  1.00109.73           C  
ANISOU 1762  CD  GLU A 227    12821  14560  14313    813   -603  -1148       C  
ATOM   1763  OE1 GLU A 227       8.847   9.988 -21.141  1.00111.05           O  
ANISOU 1763  OE1 GLU A 227    12944  14741  14510    849   -634  -1231       O  
ATOM   1764  OE2 GLU A 227       8.524  10.889 -19.166  1.00111.37           O  
ANISOU 1764  OE2 GLU A 227    13025  14721  14569    767   -579  -1125       O  
ATOM   1765  N   GLU A 228      15.176  11.376 -20.694  1.00 90.45           N  
ANISOU 1765  N   GLU A 228    10529  12180  11658    814   -537   -898       N  
ATOM   1766  CA  GLU A 228      16.457  10.941 -20.148  1.00 90.07           C  
ANISOU 1766  CA  GLU A 228    10495  12104  11623    782   -512   -843       C  
ATOM   1767  C   GLU A 228      17.139  12.062 -19.355  1.00 85.21           C  
ANISOU 1767  C   GLU A 228     9933  11486  10956    753   -481   -747       C  
ATOM   1768  O   GLU A 228      17.507  13.092 -19.921  1.00 88.99           O  
ANISOU 1768  O   GLU A 228    10446  12010  11357    784   -481   -720       O  
ATOM   1769  CB  GLU A 228      17.363  10.430 -21.264  1.00 95.89           C  
ANISOU 1769  CB  GLU A 228    11225  12875  12334    822   -526   -873       C  
ATOM   1770  CG  GLU A 228      16.890   9.126 -21.896  1.00103.14           C  
ANISOU 1770  CG  GLU A 228    12085  13785  13318    842   -553   -966       C  
ATOM   1771  CD  GLU A 228      17.224   7.902 -21.057  1.00105.28           C  
ANISOU 1771  CD  GLU A 228    12326  13989  13685    794   -538   -962       C  
ATOM   1772  OE1 GLU A 228      18.010   8.017 -20.091  1.00104.81           O  
ANISOU 1772  OE1 GLU A 228    12294  13896  13632    750   -509   -885       O  
ATOM   1773  OE2 GLU A 228      16.701   6.813 -21.369  1.00109.66           O  
ANISOU 1773  OE2 GLU A 228    12830  14525  14313    800   -556  -1037       O  
ATOM   1774  N   PRO A 229      17.318  11.854 -18.040  1.00 77.38           N  
ANISOU 1774  N   PRO A 229     8948  10442  10010    695   -456   -697       N  
ATOM   1775  CA  PRO A 229      17.805  12.867 -17.095  1.00 75.26           C  
ANISOU 1775  CA  PRO A 229     8725  10166   9704    662   -427   -613       C  
ATOM   1776  C   PRO A 229      19.046  13.622 -17.567  1.00 74.31           C  
ANISOU 1776  C   PRO A 229     8643  10081   9511    683   -418   -564       C  
ATOM   1777  O   PRO A 229      19.074  14.861 -17.528  1.00 70.30           O  
ANISOU 1777  O   PRO A 229     8169   9597   8945    690   -408   -525       O  
ATOM   1778  CB  PRO A 229      18.138  12.045 -15.850  1.00 73.54           C  
ANISOU 1778  CB  PRO A 229     8499   9890   9553    605   -407   -579       C  
ATOM   1779  CG  PRO A 229      17.217  10.882 -15.926  1.00 76.61           C  
ANISOU 1779  CG  PRO A 229     8838  10250  10022    602   -421   -646       C  
ATOM   1780  CD  PRO A 229      17.122  10.551 -17.385  1.00 76.55           C  
ANISOU 1780  CD  PRO A 229     8805  10282   9998    659   -452   -719       C  
ATOM   1781  N   GLU A 230      20.057  12.878 -18.011  1.00 74.80           N  
ANISOU 1781  N   GLU A 230     8696  10143   9580    693   -421   -569       N  
ATOM   1782  CA  GLU A 230      21.312  13.466 -18.467  1.00 75.16           C  
ANISOU 1782  CA  GLU A 230     8773  10217   9565    711   -409   -525       C  
ATOM   1783  C   GLU A 230      21.093  14.456 -19.618  1.00 72.69           C  
ANISOU 1783  C   GLU A 230     8479   9966   9175    767   -419   -539       C  
ATOM   1784  O   GLU A 230      21.739  15.512 -19.681  1.00 68.48           O  
ANISOU 1784  O   GLU A 230     7982   9453   8583    774   -402   -484       O  
ATOM   1785  CB  GLU A 230      22.301  12.359 -18.859  1.00 77.17           C  
ANISOU 1785  CB  GLU A 230     9008  10463   9850    716   -413   -541       C  
ATOM   1786  CG  GLU A 230      23.772  12.762 -18.790  1.00 82.26           C  
ANISOU 1786  CG  GLU A 230     9684  11113  10459    710   -392   -479       C  
ATOM   1787  CD  GLU A 230      24.195  13.277 -17.417  1.00 86.86           C  
ANISOU 1787  CD  GLU A 230    10294  11661  11049    658   -367   -404       C  
ATOM   1788  OE1 GLU A 230      23.702  12.758 -16.390  1.00 85.64           O  
ANISOU 1788  OE1 GLU A 230    10126  11463  10951    616   -365   -398       O  
ATOM   1789  OE2 GLU A 230      25.028  14.209 -17.363  1.00 91.30           O  
ANISOU 1789  OE2 GLU A 230    10890  12239  11562    659   -350   -351       O  
ATOM   1790  N   VAL A 231      20.164  14.115 -20.510  1.00 70.76           N  
ANISOU 1790  N   VAL A 231     8206   9746   8931    806   -448   -611       N  
ATOM   1791  CA  VAL A 231      19.793  15.001 -21.609  1.00 72.86           C  
ANISOU 1791  CA  VAL A 231     8487  10072   9125    863   -462   -628       C  
ATOM   1792  C   VAL A 231      19.030  16.228 -21.106  1.00 69.75           C  
ANISOU 1792  C   VAL A 231     8117   9680   8704    854   -454   -594       C  
ATOM   1793  O   VAL A 231      19.327  17.363 -21.499  1.00 65.03           O  
ANISOU 1793  O   VAL A 231     7553   9116   8040    879   -444   -554       O  
ATOM   1794  CB  VAL A 231      18.938  14.289 -22.676  1.00 75.75           C  
ANISOU 1794  CB  VAL A 231     8814  10468   9500    909   -498   -721       C  
ATOM   1795  CG1 VAL A 231      19.095  14.999 -24.010  1.00 74.40           C  
ANISOU 1795  CG1 VAL A 231     8661  10366   9241    975   -511   -731       C  
ATOM   1796  CG2 VAL A 231      19.332  12.824 -22.808  1.00 75.38           C  
ANISOU 1796  CG2 VAL A 231     8728  10397   9515    901   -507   -769       C  
ATOM   1797  N   ARG A 232      18.049  15.992 -20.238  1.00 72.32           N  
ANISOU 1797  N   ARG A 232     8425   9969   9086    818   -456   -610       N  
ATOM   1798  CA  ARG A 232      17.293  17.075 -19.613  1.00 71.19           C  
ANISOU 1798  CA  ARG A 232     8301   9820   8929    803   -447   -580       C  
ATOM   1799  C   ARG A 232      18.233  18.046 -18.922  1.00 68.62           C  
ANISOU 1799  C   ARG A 232     8018   9486   8568    775   -414   -495       C  
ATOM   1800  O   ARG A 232      18.161  19.260 -19.148  1.00 68.55           O  
ANISOU 1800  O   ARG A 232     8037   9504   8507    795   -407   -464       O  
ATOM   1801  CB  ARG A 232      16.275  16.523 -18.619  1.00 73.65           C  
ANISOU 1801  CB  ARG A 232     8586  10085   9314    759   -447   -605       C  
ATOM   1802  CG  ARG A 232      14.924  16.256 -19.236  1.00 75.29           C  
ANISOU 1802  CG  ARG A 232     8759  10307   9542    790   -478   -683       C  
ATOM   1803  CD  ARG A 232      13.909  15.856 -18.192  1.00 77.08           C  
ANISOU 1803  CD  ARG A 232     8960  10484   9841    745   -472   -701       C  
ATOM   1804  NE  ARG A 232      12.613  15.610 -18.818  1.00 85.28           N  
ANISOU 1804  NE  ARG A 232     9962  11536  10904    776   -503   -780       N  
ATOM   1805  CZ  ARG A 232      11.594  14.986 -18.232  1.00 84.81           C  
ANISOU 1805  CZ  ARG A 232     9867  11438  10919    748   -504   -820       C  
ATOM   1806  NH1 ARG A 232      11.696  14.527 -16.987  1.00 85.19           N  
ANISOU 1806  NH1 ARG A 232     9913  11432  11022    689   -475   -787       N  
ATOM   1807  NH2 ARG A 232      10.468  14.813 -18.900  1.00 84.72           N  
ANISOU 1807  NH2 ARG A 232     9822  11442  10927    782   -535   -896       N  
ATOM   1808  N   LYS A 233      19.130  17.498 -18.104  1.00 69.07           N  
ANISOU 1808  N   LYS A 233     8078   9507   8658    732   -395   -459       N  
ATOM   1809  CA  LYS A 233      20.123  18.288 -17.386  1.00 67.92           C  
ANISOU 1809  CA  LYS A 233     7968   9351   8487    704   -365   -383       C  
ATOM   1810  C   LYS A 233      20.888  19.225 -18.336  1.00 64.67           C  
ANISOU 1810  C   LYS A 233     7585   8983   8003    747   -358   -354       C  
ATOM   1811  O   LYS A 233      20.996  20.424 -18.084  1.00 63.57           O  
ANISOU 1811  O   LYS A 233     7474   8850   7828    744   -341   -308       O  
ATOM   1812  CB  LYS A 233      21.071  17.365 -16.611  1.00 72.74           C  
ANISOU 1812  CB  LYS A 233     8574   9923   9141    662   -353   -359       C  
ATOM   1813  CG  LYS A 233      22.211  18.096 -15.915  1.00 80.66           C  
ANISOU 1813  CG  LYS A 233     9610  10916  10120    635   -325   -285       C  
ATOM   1814  CD  LYS A 233      23.510  17.296 -15.891  1.00 82.26           C  
ANISOU 1814  CD  LYS A 233     9810  11104  10339    625   -320   -267       C  
ATOM   1815  CE  LYS A 233      24.698  18.144 -16.342  1.00 80.24           C  
ANISOU 1815  CE  LYS A 233     9584  10874  10031    643   -303   -222       C  
ATOM   1816  NZ  LYS A 233      24.803  19.463 -15.659  1.00 74.10           N  
ANISOU 1816  NZ  LYS A 233     8837  10094   9224    624   -282   -167       N  
ATOM   1817  N   ASN A 234      21.388  18.682 -19.441  1.00 66.07           N  
ANISOU 1817  N   ASN A 234     7753   9190   8161    788   -371   -384       N  
ATOM   1818  CA  ASN A 234      22.162  19.469 -20.398  1.00 64.74           C  
ANISOU 1818  CA  ASN A 234     7610   9064   7924    831   -362   -356       C  
ATOM   1819  C   ASN A 234      21.337  20.492 -21.178  1.00 65.41           C  
ANISOU 1819  C   ASN A 234     7706   9190   7955    877   -371   -365       C  
ATOM   1820  O   ASN A 234      21.773  21.629 -21.378  1.00 67.15           O  
ANISOU 1820  O   ASN A 234     7957   9428   8127    892   -352   -314       O  
ATOM   1821  CB  ASN A 234      22.945  18.552 -21.341  1.00 68.18           C  
ANISOU 1821  CB  ASN A 234     8031   9520   8354    861   -370   -387       C  
ATOM   1822  CG  ASN A 234      24.197  17.977 -20.693  1.00 69.33           C  
ANISOU 1822  CG  ASN A 234     8179   9632   8533    822   -351   -352       C  
ATOM   1823  OD1 ASN A 234      24.449  16.770 -20.766  1.00 69.83           O  
ANISOU 1823  OD1 ASN A 234     8215   9679   8638    816   -362   -388       O  
ATOM   1824  ND2 ASN A 234      24.989  18.840 -20.055  1.00 67.48           N  
ANISOU 1824  ND2 ASN A 234     7974   9383   8281    797   -323   -284       N  
ATOM   1825  N   VAL A 235      20.141  20.099 -21.610  1.00 67.92           N  
ANISOU 1825  N   VAL A 235     7998   9522   8285    900   -402   -428       N  
ATOM   1826  CA  VAL A 235      19.220  21.055 -22.255  1.00 68.61           C  
ANISOU 1826  CA  VAL A 235     8095   9647   8328    943   -415   -438       C  
ATOM   1827  C   VAL A 235      18.955  22.216 -21.311  1.00 66.14           C  
ANISOU 1827  C   VAL A 235     7804   9310   8015    910   -393   -383       C  
ATOM   1828  O   VAL A 235      19.037  23.378 -21.709  1.00 65.97           O  
ANISOU 1828  O   VAL A 235     7809   9314   7944    937   -382   -345       O  
ATOM   1829  CB  VAL A 235      17.871  20.420 -22.650  1.00 69.21           C  
ANISOU 1829  CB  VAL A 235     8134   9733   8430    964   -453   -518       C  
ATOM   1830  CG1 VAL A 235      16.917  21.480 -23.199  1.00 69.91           C  
ANISOU 1830  CG1 VAL A 235     8232   9856   8474   1006   -468   -523       C  
ATOM   1831  CG2 VAL A 235      18.078  19.321 -23.673  1.00 69.05           C  
ANISOU 1831  CG2 VAL A 235     8087   9740   8407   1002   -478   -580       C  
ATOM   1832  N   CYS A 236      18.653  21.888 -20.057  1.00 65.92           N  
ANISOU 1832  N   CYS A 236     7767   9234   8046    852   -385   -379       N  
ATOM   1833  CA  CYS A 236      18.387  22.903 -19.045  1.00 64.53           C  
ANISOU 1833  CA  CYS A 236     7609   9032   7876    816   -363   -333       C  
ATOM   1834  C   CYS A 236      19.505  23.925 -18.951  1.00 62.32           C  
ANISOU 1834  C   CYS A 236     7366   8758   7557    813   -332   -262       C  
ATOM   1835  O   CYS A 236      19.234  25.125 -18.974  1.00 62.66           O  
ANISOU 1835  O   CYS A 236     7426   8810   7571    825   -322   -232       O  
ATOM   1836  CB  CYS A 236      18.123  22.270 -17.682  1.00 67.56           C  
ANISOU 1836  CB  CYS A 236     7980   9366   8325    753   -354   -335       C  
ATOM   1837  SG  CYS A 236      16.465  21.569 -17.529  1.00 73.69           S  
ANISOU 1837  SG  CYS A 236     8717  10128   9154    749   -381   -409       S  
ATOM   1838  N   ARG A 237      20.757  23.473 -18.867  1.00 60.11           N  
ANISOU 1838  N   ARG A 237     7092   8469   7277    800   -317   -235       N  
ATOM   1839  CA  ARG A 237      21.853  24.438 -18.706  1.00 61.38           C  
ANISOU 1839  CA  ARG A 237     7284   8629   7408    794   -286   -168       C  
ATOM   1840  C   ARG A 237      22.208  25.177 -19.981  1.00 60.86           C  
ANISOU 1840  C   ARG A 237     7235   8609   7281    853   -282   -153       C  
ATOM   1841  O   ARG A 237      22.746  26.285 -19.924  1.00 61.59           O  
ANISOU 1841  O   ARG A 237     7352   8703   7348    854   -256    -99       O  
ATOM   1842  CB  ARG A 237      23.093  23.860 -18.009  1.00 66.04           C  
ANISOU 1842  CB  ARG A 237     7877   9190   8024    753   -268   -139       C  
ATOM   1843  CG  ARG A 237      23.550  22.471 -18.422  1.00 72.46           C  
ANISOU 1843  CG  ARG A 237     8669  10004   8858    759   -284   -175       C  
ATOM   1844  CD  ARG A 237      24.427  21.858 -17.332  1.00 77.79           C  
ANISOU 1844  CD  ARG A 237     9342  10637   9576    706   -271   -148       C  
ATOM   1845  NE  ARG A 237      24.898  22.860 -16.364  1.00 88.01           N  
ANISOU 1845  NE  ARG A 237    10660  11911  10867    671   -244    -89       N  
ATOM   1846  CZ  ARG A 237      26.001  23.606 -16.488  1.00 88.90           C  
ANISOU 1846  CZ  ARG A 237    10795  12031  10954    675   -221    -42       C  
ATOM   1847  NH1 ARG A 237      26.798  23.476 -17.545  1.00 86.59           N  
ANISOU 1847  NH1 ARG A 237    10504  11762  10632    713   -218    -41       N  
ATOM   1848  NH2 ARG A 237      26.304  24.494 -15.547  1.00 85.71           N  
ANISOU 1848  NH2 ARG A 237    10407  11606  10553    641   -200      3       N  
ATOM   1849  N   ALA A 238      21.882  24.580 -21.124  1.00 60.80           N  
ANISOU 1849  N   ALA A 238     7214   8639   7250    901   -307   -200       N  
ATOM   1850  CA  ALA A 238      21.951  25.290 -22.391  1.00 62.61           C  
ANISOU 1850  CA  ALA A 238     7459   8917   7414    964   -307   -190       C  
ATOM   1851  C   ALA A 238      21.060  26.539 -22.314  1.00 64.08           C  
ANISOU 1851  C   ALA A 238     7657   9109   7582    976   -305   -170       C  
ATOM   1852  O   ALA A 238      21.529  27.679 -22.467  1.00 61.65           O  
ANISOU 1852  O   ALA A 238     7375   8808   7243    989   -279   -113       O  
ATOM   1853  CB  ALA A 238      21.515  24.375 -23.527  1.00 61.51           C  
ANISOU 1853  CB  ALA A 238     7298   8818   7256   1013   -341   -256       C  
ATOM   1854  N   LEU A 239      19.780  26.321 -22.023  1.00 65.29           N  
ANISOU 1854  N   LEU A 239     7790   9255   7763    970   -331   -215       N  
ATOM   1855  CA  LEU A 239      18.821  27.417 -21.960  1.00 64.64           C  
ANISOU 1855  CA  LEU A 239     7715   9176   7670    983   -334   -204       C  
ATOM   1856  C   LEU A 239      19.259  28.494 -20.979  1.00 65.13           C  
ANISOU 1856  C   LEU A 239     7798   9205   7745    942   -298   -140       C  
ATOM   1857  O   LEU A 239      19.193  29.684 -21.299  1.00 66.36           O  
ANISOU 1857  O   LEU A 239     7971   9372   7869    966   -284   -101       O  
ATOM   1858  CB  LEU A 239      17.422  26.893 -21.634  1.00 67.69           C  
ANISOU 1858  CB  LEU A 239     8071   9552   8096    973   -365   -266       C  
ATOM   1859  CG  LEU A 239      16.809  26.002 -22.720  1.00 67.67           C  
ANISOU 1859  CG  LEU A 239     8044   9588   8079   1022   -405   -337       C  
ATOM   1860  CD1 LEU A 239      15.531  25.331 -22.229  1.00 68.81           C  
ANISOU 1860  CD1 LEU A 239     8154   9710   8279   1001   -432   -401       C  
ATOM   1861  CD2 LEU A 239      16.554  26.804 -23.988  1.00 67.79           C  
ANISOU 1861  CD2 LEU A 239     8073   9657   8026   1093   -418   -331       C  
ATOM   1862  N   VAL A 240      19.740  28.080 -19.805  1.00 64.74           N  
ANISOU 1862  N   VAL A 240     7745   9113   7740    881   -282   -128       N  
ATOM   1863  CA  VAL A 240      20.219  29.038 -18.802  1.00 64.68           C  
ANISOU 1863  CA  VAL A 240     7756   9074   7747    839   -249    -72       C  
ATOM   1864  C   VAL A 240      21.310  29.927 -19.376  1.00 63.71           C  
ANISOU 1864  C   VAL A 240     7657   8965   7583    865   -221    -15       C  
ATOM   1865  O   VAL A 240      21.251  31.149 -19.256  1.00 64.72           O  
ANISOU 1865  O   VAL A 240     7800   9088   7702    868   -201     24       O  
ATOM   1866  CB  VAL A 240      20.726  28.347 -17.519  1.00 64.42           C  
ANISOU 1866  CB  VAL A 240     7717   9000   7761    774   -238    -67       C  
ATOM   1867  CG1 VAL A 240      21.419  29.350 -16.597  1.00 62.39           C  
ANISOU 1867  CG1 VAL A 240     7478   8716   7511    737   -204    -10       C  
ATOM   1868  CG2 VAL A 240      19.568  27.683 -16.796  1.00 62.84           C  
ANISOU 1868  CG2 VAL A 240     7494   8779   7605    745   -258   -114       C  
ATOM   1869  N   MET A 241      22.297  29.307 -20.009  1.00 67.70           N  
ANISOU 1869  N   MET A 241     8167   9487   8070    882   -217    -11       N  
ATOM   1870  CA  MET A 241      23.434  30.038 -20.557  1.00 68.25           C  
ANISOU 1870  CA  MET A 241     8258   9568   8105    904   -187     43       C  
ATOM   1871  C   MET A 241      22.987  30.954 -21.698  1.00 64.21           C  
ANISOU 1871  C   MET A 241     7759   9096   7542    967   -187     58       C  
ATOM   1872  O   MET A 241      23.339  32.136 -21.730  1.00 61.91           O  
ANISOU 1872  O   MET A 241     7486   8800   7238    974   -158    111       O  
ATOM   1873  CB  MET A 241      24.533  29.061 -20.991  1.00 72.68           C  
ANISOU 1873  CB  MET A 241     8817  10139   8660    909   -184     37       C  
ATOM   1874  CG  MET A 241      25.262  28.434 -19.810  1.00 80.67           C  
ANISOU 1874  CG  MET A 241     9822  11108   9721    848   -175     44       C  
ATOM   1875  SD  MET A 241      26.339  27.030 -20.178  1.00 81.17           S  
ANISOU 1875  SD  MET A 241     9875  11175   9793    848   -181     24       S  
ATOM   1876  CE  MET A 241      27.141  26.845 -18.583  1.00 90.49           C  
ANISOU 1876  CE  MET A 241    11054  12302  11028    774   -164     54       C  
ATOM   1877  N   LEU A 242      22.183  30.403 -22.605  1.00 62.43           N  
ANISOU 1877  N   LEU A 242     7522   8908   7291   1011   -220      9       N  
ATOM   1878  CA  LEU A 242      21.602  31.162 -23.710  1.00 66.98           C  
ANISOU 1878  CA  LEU A 242     8109   9527   7815   1075   -228     17       C  
ATOM   1879  C   LEU A 242      20.870  32.407 -23.244  1.00 68.59           C  
ANISOU 1879  C   LEU A 242     8319   9713   8030   1068   -220     45       C  
ATOM   1880  O   LEU A 242      20.986  33.471 -23.851  1.00 71.30           O  
ANISOU 1880  O   LEU A 242     8680  10073   8339   1105   -202     91       O  
ATOM   1881  CB  LEU A 242      20.650  30.273 -24.503  1.00 67.04           C  
ANISOU 1881  CB  LEU A 242     8096   9572   7805   1114   -274    -53       C  
ATOM   1882  CG  LEU A 242      21.120  29.762 -25.862  1.00 68.66           C  
ANISOU 1882  CG  LEU A 242     8304   9830   7952   1173   -283    -69       C  
ATOM   1883  CD1 LEU A 242      22.543  30.182 -26.197  1.00 72.10           C  
ANISOU 1883  CD1 LEU A 242     8763  10270   8359   1180   -241     -8       C  
ATOM   1884  CD2 LEU A 242      20.958  28.256 -25.926  1.00 67.93           C  
ANISOU 1884  CD2 LEU A 242     8184   9742   7883   1165   -314   -141       C  
ATOM   1885  N   LEU A 243      20.136  32.269 -22.147  1.00 67.40           N  
ANISOU 1885  N   LEU A 243     8152   9526   7929   1020   -230     20       N  
ATOM   1886  CA  LEU A 243      19.395  33.374 -21.573  1.00 69.47           C  
ANISOU 1886  CA  LEU A 243     8416   9767   8211   1007   -222     40       C  
ATOM   1887  C   LEU A 243      20.311  34.536 -21.223  1.00 68.15           C  
ANISOU 1887  C   LEU A 243     8270   9577   8046    992   -178    110       C  
ATOM   1888  O   LEU A 243      19.918  35.701 -21.310  1.00 69.25           O  
ANISOU 1888  O   LEU A 243     8417   9714   8181   1008   -166    141       O  
ATOM   1889  CB  LEU A 243      18.622  32.892 -20.339  1.00 71.95           C  
ANISOU 1889  CB  LEU A 243     8711  10044   8582    950   -235      1       C  
ATOM   1890  CG  LEU A 243      17.748  33.872 -19.553  1.00 74.05           C  
ANISOU 1890  CG  LEU A 243     8974  10284   8879    926   -228      8       C  
ATOM   1891  CD1 LEU A 243      16.570  34.349 -20.394  1.00 76.07           C  
ANISOU 1891  CD1 LEU A 243     9222  10568   9112    979   -255    -13       C  
ATOM   1892  CD2 LEU A 243      17.267  33.219 -18.264  1.00 73.26           C  
ANISOU 1892  CD2 LEU A 243     8855  10147   8832    864   -233    -27       C  
ATOM   1893  N   GLU A 244      21.541  34.221 -20.847  1.00 71.49           N  
ANISOU 1893  N   GLU A 244     8701   9984   8479    962   -154    135       N  
ATOM   1894  CA  GLU A 244      22.473  35.259 -20.431  1.00 74.64           C  
ANISOU 1894  CA  GLU A 244     9114  10357   8888    942   -112    196       C  
ATOM   1895  C   GLU A 244      23.114  36.007 -21.598  1.00 71.71           C  
ANISOU 1895  C   GLU A 244     8762  10014   8471    998    -88    245       C  
ATOM   1896  O   GLU A 244      23.489  37.167 -21.453  1.00 70.81           O  
ANISOU 1896  O   GLU A 244     8658   9881   8365    996    -55    296       O  
ATOM   1897  CB  GLU A 244      23.550  34.671 -19.521  1.00 80.19           C  
ANISOU 1897  CB  GLU A 244     9815  11030   9623    888    -96    203       C  
ATOM   1898  CG  GLU A 244      24.184  35.677 -18.566  1.00 87.18           C  
ANISOU 1898  CG  GLU A 244    10707  11876  10541    847    -60    248       C  
ATOM   1899  CD  GLU A 244      25.372  35.098 -17.813  1.00 94.36           C  
ANISOU 1899  CD  GLU A 244    11616  12762  11476    802    -46    258       C  
ATOM   1900  OE1 GLU A 244      25.299  33.924 -17.394  1.00 95.28           O  
ANISOU 1900  OE1 GLU A 244    11722  12876  11606    777    -69    220       O  
ATOM   1901  OE2 GLU A 244      26.384  35.813 -17.640  1.00101.38           O  
ANISOU 1901  OE2 GLU A 244    12513  13634  12374    792    -13    302       O  
ATOM   1902  N   VAL A 245      23.239  35.354 -22.751  1.00 72.73           N  
ANISOU 1902  N   VAL A 245     8894  10186   8554   1047   -103    229       N  
ATOM   1903  CA  VAL A 245      24.051  35.909 -23.847  1.00 78.04           C  
ANISOU 1903  CA  VAL A 245     9586  10887   9179   1097    -76    278       C  
ATOM   1904  C   VAL A 245      23.301  36.100 -25.173  1.00 81.52           C  
ANISOU 1904  C   VAL A 245    10034  11381   9560   1171    -96    271       C  
ATOM   1905  O   VAL A 245      23.636  36.991 -25.961  1.00 86.10           O  
ANISOU 1905  O   VAL A 245    10631  11979  10103   1214    -71    323       O  
ATOM   1906  CB  VAL A 245      25.372  35.107 -24.086  1.00 78.38           C  
ANISOU 1906  CB  VAL A 245     9633  10935   9214   1090    -60    283       C  
ATOM   1907  CG1 VAL A 245      26.267  35.123 -22.850  1.00 75.51           C  
ANISOU 1907  CG1 VAL A 245     9265  10520   8905   1023    -35    302       C  
ATOM   1908  CG2 VAL A 245      25.091  33.678 -24.536  1.00 75.82           C  
ANISOU 1908  CG2 VAL A 245     9294  10640   8872   1104    -98    218       C  
ATOM   1909  N   ARG A 246      22.312  35.247 -25.425  1.00 80.56           N  
ANISOU 1909  N   ARG A 246     9896  11285   9428   1186   -142    207       N  
ATOM   1910  CA  ARG A 246      21.469  35.380 -26.608  1.00 83.14           C  
ANISOU 1910  CA  ARG A 246    10226  11664   9700   1256   -170    191       C  
ATOM   1911  C   ARG A 246      19.990  35.606 -26.254  1.00 83.76           C  
ANISOU 1911  C   ARG A 246    10289  11736   9801   1254   -205    154       C  
ATOM   1912  O   ARG A 246      19.102  34.851 -26.672  1.00 78.49           O  
ANISOU 1912  O   ARG A 246     9604  11097   9120   1278   -249     93       O  
ATOM   1913  CB  ARG A 246      21.667  34.197 -27.560  1.00 85.31           C  
ANISOU 1913  CB  ARG A 246    10495  11988   9932   1292   -195    145       C  
ATOM   1914  CG  ARG A 246      22.784  34.410 -28.574  1.00 91.39           C  
ANISOU 1914  CG  ARG A 246    11287  12791  10646   1335   -163    191       C  
ATOM   1915  CD  ARG A 246      22.479  35.548 -29.552  1.00102.09           C  
ANISOU 1915  CD  ARG A 246    12662  14182  11945   1400   -153    240       C  
ATOM   1916  NE  ARG A 246      23.668  35.961 -30.302  1.00111.25           N  
ANISOU 1916  NE  ARG A 246    13845  15361  13063   1430   -109    300       N  
ATOM   1917  CZ  ARG A 246      24.561  36.856 -29.875  1.00115.66           C  
ANISOU 1917  CZ  ARG A 246    14417  15881  13646   1405    -57    370       C  
ATOM   1918  NH1 ARG A 246      24.403  37.456 -28.699  1.00117.60           N  
ANISOU 1918  NH1 ARG A 246    14657  16069  13957   1350    -45    386       N  
ATOM   1919  NH2 ARG A 246      25.620  37.151 -30.626  1.00110.39           N  
ANISOU 1919  NH2 ARG A 246    13768  15232  12941   1435    -16    420       N  
ATOM   1920  N   MET A 247      19.743  36.655 -25.474  1.00 85.59           N  
ANISOU 1920  N   MET A 247    10523  11929  10070   1226   -184    190       N  
ATOM   1921  CA  MET A 247      18.388  37.030 -25.095  1.00 89.67           C  
ANISOU 1921  CA  MET A 247    11025  12435  10611   1223   -211    162       C  
ATOM   1922  C   MET A 247      17.505  37.208 -26.337  1.00 89.50           C  
ANISOU 1922  C   MET A 247    11004  12466  10535   1299   -244    147       C  
ATOM   1923  O   MET A 247      16.425  36.608 -26.439  1.00 83.31           O  
ANISOU 1923  O   MET A 247    10200  11698   9755   1310   -288     83       O  
ATOM   1924  CB  MET A 247      18.404  38.307 -24.248  1.00 92.62           C  
ANISOU 1924  CB  MET A 247    11403  12761  11025   1190   -178    212       C  
ATOM   1925  CG  MET A 247      17.020  38.796 -23.850  1.00 95.94           C  
ANISOU 1925  CG  MET A 247    11808  13169  11475   1187   -202    185       C  
ATOM   1926  SD  MET A 247      16.112  37.533 -22.942  1.00102.73           S  
ANISOU 1926  SD  MET A 247    12639  14012  12380   1138   -240     98       S  
ATOM   1927  CE  MET A 247      16.629  37.916 -21.278  1.00 95.22           C  
ANISOU 1927  CE  MET A 247    11686  12997  11495   1052   -202    121       C  
ATOM   1928  N   ASP A 248      17.986  38.025 -27.276  1.00 89.16           N  
ANISOU 1928  N   ASP A 248    10983  12451  10441   1351   -222    206       N  
ATOM   1929  CA  ASP A 248      17.312  38.268 -28.558  1.00 90.95           C  
ANISOU 1929  CA  ASP A 248    11216  12735  10605   1431   -250    203       C  
ATOM   1930  C   ASP A 248      16.707  36.998 -29.158  1.00 87.68           C  
ANISOU 1930  C   ASP A 248    10785  12367  10164   1459   -302    122       C  
ATOM   1931  O   ASP A 248      15.542  36.974 -29.542  1.00 86.45           O  
ANISOU 1931  O   ASP A 248    10615  12236   9996   1493   -345     81       O  
ATOM   1932  CB  ASP A 248      18.262  38.953 -29.565  1.00 91.03           C  
ANISOU 1932  CB  ASP A 248    11256  12776  10556   1482   -214    277       C  
ATOM   1933  CG  ASP A 248      19.608  38.229 -29.719  1.00 95.78           C  
ANISOU 1933  CG  ASP A 248    11867  13384  11142   1468   -187    286       C  
ATOM   1934  OD1 ASP A 248      20.321  38.028 -28.707  1.00 95.19           O  
ANISOU 1934  OD1 ASP A 248    11788  13260  11120   1402   -161    291       O  
ATOM   1935  OD2 ASP A 248      19.966  37.881 -30.865  1.00 95.36           O  
ANISOU 1935  OD2 ASP A 248    11825  13386  11021   1523   -191    287       O  
ATOM   1936  N   ARG A 249      17.498  35.935 -29.186  1.00 90.07           N  
ANISOU 1936  N   ARG A 249    11085  12677  10462   1441   -299     96       N  
ATOM   1937  CA  ARG A 249      17.131  34.712 -29.881  1.00 90.26           C  
ANISOU 1937  CA  ARG A 249    11093  12746  10458   1471   -343     22       C  
ATOM   1938  C   ARG A 249      15.971  33.918 -29.280  1.00 88.30           C  
ANISOU 1938  C   ARG A 249    10810  12481  10260   1443   -388    -60       C  
ATOM   1939  O   ARG A 249      15.297  33.183 -30.003  1.00 86.56           O  
ANISOU 1939  O   ARG A 249    10572  12302  10013   1483   -432   -124       O  
ATOM   1940  CB  ARG A 249      18.367  33.826 -30.046  1.00 95.63           C  
ANISOU 1940  CB  ARG A 249    11777  13433  11125   1457   -324     19       C  
ATOM   1941  CG  ARG A 249      18.982  33.839 -31.441  1.00102.58           C  
ANISOU 1941  CG  ARG A 249    12677  14377  11923   1527   -317     40       C  
ATOM   1942  CD  ARG A 249      19.168  35.235 -32.023  1.00107.13           C  
ANISOU 1942  CD  ARG A 249    13282  14969  12453   1571   -287    123       C  
ATOM   1943  NE  ARG A 249      19.217  35.205 -33.486  1.00115.09           N  
ANISOU 1943  NE  ARG A 249    14303  16052  13372   1653   -298    126       N  
ATOM   1944  CZ  ARG A 249      18.150  35.277 -34.280  1.00117.86           C  
ANISOU 1944  CZ  ARG A 249    14649  16454  13678   1714   -343     94       C  
ATOM   1945  NH1 ARG A 249      16.930  35.388 -33.764  1.00115.17           N  
ANISOU 1945  NH1 ARG A 249    14288  16093  13378   1701   -380     55       N  
ATOM   1946  NH2 ARG A 249      18.302  35.238 -35.598  1.00118.08           N  
ANISOU 1946  NH2 ARG A 249    14691  16553  13619   1788   -351     99       N  
ATOM   1947  N   LEU A 250      15.720  34.047 -27.979  1.00 86.73           N  
ANISOU 1947  N   LEU A 250    10600  12222  10132   1376   -376    -61       N  
ATOM   1948  CA  LEU A 250      14.666  33.210 -27.375  1.00 85.21           C  
ANISOU 1948  CA  LEU A 250    10375  12011   9990   1346   -414   -139       C  
ATOM   1949  C   LEU A 250      13.348  33.854 -26.914  1.00 80.28           C  
ANISOU 1949  C   LEU A 250     9736  11367   9401   1340   -433   -155       C  
ATOM   1950  O   LEU A 250      12.416  33.129 -26.563  1.00 80.20           O  
ANISOU 1950  O   LEU A 250     9695  11346   9430   1323   -465   -224       O  
ATOM   1951  CB  LEU A 250      15.220  32.254 -26.312  1.00 83.35           C  
ANISOU 1951  CB  LEU A 250    10127  11730   9812   1274   -399   -159       C  
ATOM   1952  CG  LEU A 250      16.533  32.532 -25.599  1.00 86.27           C  
ANISOU 1952  CG  LEU A 250    10517  12064  10198   1227   -350    -98       C  
ATOM   1953  CD1 LEU A 250      16.441  33.777 -24.732  1.00 88.28           C  
ANISOU 1953  CD1 LEU A 250    10783  12277  10481   1194   -320    -44       C  
ATOM   1954  CD2 LEU A 250      16.881  31.312 -24.765  1.00 85.19           C  
ANISOU 1954  CD2 LEU A 250    10362  11895  10110   1169   -351   -135       C  
ATOM   1955  N   LEU A 251      13.258  35.185 -26.945  1.00 77.13           N  
ANISOU 1955  N   LEU A 251     9354  10962   8990   1356   -413    -95       N  
ATOM   1956  CA  LEU A 251      11.989  35.886 -26.656  1.00 79.33           C  
ANISOU 1956  CA  LEU A 251     9618  11226   9297   1360   -432   -110       C  
ATOM   1957  C   LEU A 251      10.765  35.227 -27.302  1.00 78.28           C  
ANISOU 1957  C   LEU A 251     9458  11129   9156   1402   -490   -189       C  
ATOM   1958  O   LEU A 251       9.854  34.824 -26.591  1.00 78.90           O  
ANISOU 1958  O   LEU A 251     9509  11180   9291   1368   -510   -243       O  
ATOM   1959  CB  LEU A 251      12.044  37.367 -27.050  1.00 78.58           C  
ANISOU 1959  CB  LEU A 251     9546  11135   9174   1397   -411    -36       C  
ATOM   1960  CG  LEU A 251      12.865  38.349 -26.218  1.00 82.12           C  
ANISOU 1960  CG  LEU A 251    10013  11535   9652   1352   -356     37       C  
ATOM   1961  CD1 LEU A 251      12.837  39.725 -26.871  1.00 83.84           C  
ANISOU 1961  CD1 LEU A 251    10250  11766   9839   1402   -340    105       C  
ATOM   1962  CD2 LEU A 251      12.348  38.421 -24.790  1.00 81.60           C  
ANISOU 1962  CD2 LEU A 251     9928  11411   9664   1280   -348     14       C  
ATOM   1963  N   PRO A 252      10.752  35.091 -28.645  1.00 83.28           N  
ANISOU 1963  N   PRO A 252    10098  11826   9719   1477   -517   -197       N  
ATOM   1964  CA  PRO A 252       9.596  34.495 -29.329  1.00 84.29           C  
ANISOU 1964  CA  PRO A 252    10198  11993   9835   1522   -576   -276       C  
ATOM   1965  C   PRO A 252       9.123  33.144 -28.783  1.00 82.08           C  
ANISOU 1965  C   PRO A 252     9882  11693   9611   1481   -601   -364       C  
ATOM   1966  O   PRO A 252       8.022  32.713 -29.110  1.00 82.15           O  
ANISOU 1966  O   PRO A 252     9861  11720   9631   1507   -648   -434       O  
ATOM   1967  CB  PRO A 252      10.090  34.323 -30.781  1.00 86.77           C  
ANISOU 1967  CB  PRO A 252    10529  12380  10059   1599   -591   -269       C  
ATOM   1968  CG  PRO A 252      11.570  34.546 -30.742  1.00 85.19           C  
ANISOU 1968  CG  PRO A 252    10362  12173   9834   1582   -538   -197       C  
ATOM   1969  CD  PRO A 252      11.778  35.512 -29.621  1.00 84.37           C  
ANISOU 1969  CD  PRO A 252    10269  12005   9782   1526   -495   -136       C  
ATOM   1970  N   HIS A 253       9.938  32.480 -27.968  1.00 82.55           N  
ANISOU 1970  N   HIS A 253     9943  11715   9708   1419   -571   -360       N  
ATOM   1971  CA  HIS A 253       9.558  31.171 -27.423  1.00 80.53           C  
ANISOU 1971  CA  HIS A 253     9652  11436   9509   1379   -591   -436       C  
ATOM   1972  C   HIS A 253       9.511  31.194 -25.921  1.00 76.57           C  
ANISOU 1972  C   HIS A 253     9144  10865   9083   1296   -561   -425       C  
ATOM   1973  O   HIS A 253       9.326  30.161 -25.265  1.00 72.97           O  
ANISOU 1973  O   HIS A 253     8663  10380   8681   1252   -566   -474       O  
ATOM   1974  CB  HIS A 253      10.508  30.094 -27.926  1.00 80.44           C  
ANISOU 1974  CB  HIS A 253     9641  11448   9472   1386   -590   -456       C  
ATOM   1975  CG  HIS A 253      10.732  30.141 -29.414  1.00 86.66           C  
ANISOU 1975  CG  HIS A 253    10442  12310  10177   1467   -613   -458       C  
ATOM   1976  ND1 HIS A 253      10.078  29.334 -30.270  1.00 90.27           N  
ANISOU 1976  ND1 HIS A 253    10871  12811  10615   1514   -662   -537       N  
ATOM   1977  CD2 HIS A 253      11.560  30.954 -30.190  1.00 86.11           C  
ANISOU 1977  CD2 HIS A 253    10409  12276  10033   1511   -590   -388       C  
ATOM   1978  CE1 HIS A 253      10.473  29.606 -31.529  1.00 90.62           C  
ANISOU 1978  CE1 HIS A 253    10936  12921  10574   1585   -672   -520       C  
ATOM   1979  NE2 HIS A 253      11.377  30.601 -31.477  1.00 89.46           N  
ANISOU 1979  NE2 HIS A 253    10828  12768  10393   1583   -626   -426       N  
ATOM   1980  N   MET A 254       9.647  32.391 -25.365  1.00 76.09           N  
ANISOU 1980  N   MET A 254     9104  10778   9027   1277   -529   -360       N  
ATOM   1981  CA  MET A 254       9.769  32.551 -23.928  1.00 78.68           C  
ANISOU 1981  CA  MET A 254     9432  11045   9418   1200   -494   -340       C  
ATOM   1982  C   MET A 254       8.657  31.891 -23.116  1.00 79.53           C  
ANISOU 1982  C   MET A 254     9504  11120   9594   1160   -513   -407       C  
ATOM   1983  O   MET A 254       8.950  31.221 -22.126  1.00 82.48           O  
ANISOU 1983  O   MET A 254     9870  11454  10014   1098   -494   -415       O  
ATOM   1984  CB  MET A 254       9.914  34.020 -23.554  1.00 78.05           C  
ANISOU 1984  CB  MET A 254     9375  10946   9334   1193   -462   -269       C  
ATOM   1985  CG  MET A 254      10.612  34.214 -22.218  1.00 84.16           C  
ANISOU 1985  CG  MET A 254    10159  11667  10151   1118   -417   -230       C  
ATOM   1986  SD  MET A 254      12.210  33.377 -22.079  1.00 86.85           S  
ANISOU 1986  SD  MET A 254    10516  12004  10477   1090   -390   -204       S  
ATOM   1987  CE  MET A 254      13.258  34.539 -22.952  1.00 84.76           C  
ANISOU 1987  CE  MET A 254    10289  11767  10150   1137   -362   -121       C  
ATOM   1988  N   HIS A 255       7.400  32.044 -23.534  1.00 76.80           N  
ANISOU 1988  N   HIS A 255     9135  10789   9256   1194   -550   -454       N  
ATOM   1989  CA  HIS A 255       6.304  31.392 -22.813  1.00 79.14           C  
ANISOU 1989  CA  HIS A 255     9394  11054   9622   1158   -567   -522       C  
ATOM   1990  C   HIS A 255       6.527  29.910 -22.709  1.00 74.56           C  
ANISOU 1990  C   HIS A 255     8793  10468   9069   1135   -576   -573       C  
ATOM   1991  O   HIS A 255       6.449  29.339 -21.621  1.00 75.78           O  
ANISOU 1991  O   HIS A 255     8934  10577   9283   1073   -557   -587       O  
ATOM   1992  CB  HIS A 255       4.925  31.698 -23.420  1.00 80.96           C  
ANISOU 1992  CB  HIS A 255     9598  11305   9856   1205   -610   -573       C  
ATOM   1993  CG  HIS A 255       3.788  30.898 -22.789  1.00 82.86           C  
ANISOU 1993  CG  HIS A 255     9795  11514  10171   1172   -629   -650       C  
ATOM   1994  ND1 HIS A 255       3.333  29.734 -23.311  1.00 81.65           N  
ANISOU 1994  ND1 HIS A 255     9610  11379  10034   1192   -666   -727       N  
ATOM   1995  CD2 HIS A 255       3.037  31.125 -21.630  1.00 81.81           C  
ANISOU 1995  CD2 HIS A 255     9647  11332  10107   1117   -611   -662       C  
ATOM   1996  CE1 HIS A 255       2.343  29.248 -22.534  1.00 81.80           C  
ANISOU 1996  CE1 HIS A 255     9593  11359  10129   1152   -670   -782       C  
ATOM   1997  NE2 HIS A 255       2.162  30.099 -21.507  1.00 81.70           N  
ANISOU 1997  NE2 HIS A 255     9592  11306  10146   1106   -636   -741       N  
ATOM   1998  N   ASN A 256       6.810  29.273 -23.836  1.00 73.73           N  
ANISOU 1998  N   ASN A 256     8685  10409   8921   1187   -605   -602       N  
ATOM   1999  CA  ASN A 256       7.077  27.840 -23.851  1.00 74.12           C  
ANISOU 1999  CA  ASN A 256     8711  10455   8997   1171   -615   -654       C  
ATOM   2000  C   ASN A 256       8.323  27.461 -23.045  1.00 72.06           C  
ANISOU 2000  C   ASN A 256     8470  10160   8748   1115   -572   -606       C  
ATOM   2001  O   ASN A 256       8.383  26.380 -22.443  1.00 71.34           O  
ANISOU 2001  O   ASN A 256     8358  10038   8709   1072   -568   -638       O  
ATOM   2002  CB  ASN A 256       7.207  27.342 -25.285  1.00 74.37           C  
ANISOU 2002  CB  ASN A 256     8737  10548   8973   1242   -653   -692       C  
ATOM   2003  CG  ASN A 256       5.953  27.582 -26.099  1.00 78.42           C  
ANISOU 2003  CG  ASN A 256     9226  11096   9473   1300   -701   -749       C  
ATOM   2004  OD1 ASN A 256       5.234  26.642 -26.428  1.00 77.10           O  
ANISOU 2004  OD1 ASN A 256     9020  10938   9337   1314   -738   -831       O  
ATOM   2005  ND2 ASN A 256       5.683  28.847 -26.426  1.00 77.89           N  
ANISOU 2005  ND2 ASN A 256     9180  11048   9365   1335   -702   -704       N  
ATOM   2006  N   ILE A 257       9.310  28.350 -23.024  1.00 66.57           N  
ANISOU 2006  N   ILE A 257     7814   9470   8010   1115   -540   -528       N  
ATOM   2007  CA  ILE A 257      10.541  28.061 -22.285  1.00 69.02           C  
ANISOU 2007  CA  ILE A 257     8143   9751   8330   1065   -502   -481       C  
ATOM   2008  C   ILE A 257      10.259  28.080 -20.775  1.00 68.13           C  
ANISOU 2008  C   ILE A 257     8024   9580   8283    990   -476   -471       C  
ATOM   2009  O   ILE A 257      10.547  27.100 -20.062  1.00 63.18           O  
ANISOU 2009  O   ILE A 257     7385   8923   7699    944   -466   -486       O  
ATOM   2010  CB  ILE A 257      11.701  29.000 -22.681  1.00 65.43           C  
ANISOU 2010  CB  ILE A 257     7729   9317   7816   1085   -473   -403       C  
ATOM   2011  CG1 ILE A 257      12.105  28.749 -24.140  1.00 64.04           C  
ANISOU 2011  CG1 ILE A 257     7559   9200   7574   1154   -495   -414       C  
ATOM   2012  CG2 ILE A 257      12.896  28.765 -21.780  1.00 64.00           C  
ANISOU 2012  CG2 ILE A 257     7563   9099   7653   1028   -434   -357       C  
ATOM   2013  CD1 ILE A 257      12.920  29.861 -24.771  1.00 62.65           C  
ANISOU 2013  CD1 ILE A 257     7419   9050   7333   1191   -472   -342       C  
ATOM   2014  N   VAL A 258       9.666  29.180 -20.308  1.00 63.12           N  
ANISOU 2014  N   VAL A 258     7396   8932   7656    981   -465   -447       N  
ATOM   2015  CA  VAL A 258       9.226  29.291 -18.925  1.00 62.50           C  
ANISOU 2015  CA  VAL A 258     7310   8804   7636    916   -442   -444       C  
ATOM   2016  C   VAL A 258       8.358  28.093 -18.505  1.00 65.60           C  
ANISOU 2016  C   VAL A 258     7663   9172   8088    890   -460   -514       C  
ATOM   2017  O   VAL A 258       8.557  27.533 -17.423  1.00 65.30           O  
ANISOU 2017  O   VAL A 258     7621   9096   8093    831   -437   -510       O  
ATOM   2018  CB  VAL A 258       8.500  30.625 -18.668  1.00 60.23           C  
ANISOU 2018  CB  VAL A 258     7028   8509   7349    919   -435   -424       C  
ATOM   2019  CG1 VAL A 258       8.083  30.736 -17.206  1.00 58.72           C  
ANISOU 2019  CG1 VAL A 258     6828   8268   7215    851   -408   -422       C  
ATOM   2020  CG2 VAL A 258       9.402  31.790 -19.038  1.00 56.39           C  
ANISOU 2020  CG2 VAL A 258     6577   8038   6811    942   -413   -352       C  
ATOM   2021  N   GLU A 259       7.425  27.675 -19.363  1.00 66.54           N  
ANISOU 2021  N   GLU A 259     7755   9317   8211    934   -500   -579       N  
ATOM   2022  CA  GLU A 259       6.588  26.508 -19.054  1.00 70.10           C  
ANISOU 2022  CA  GLU A 259     8165   9744   8725    913   -517   -650       C  
ATOM   2023  C   GLU A 259       7.466  25.285 -18.832  1.00 69.78           C  
ANISOU 2023  C   GLU A 259     8120   9690   8702    886   -508   -653       C  
ATOM   2024  O   GLU A 259       7.266  24.527 -17.878  1.00 72.70           O  
ANISOU 2024  O   GLU A 259     8473  10018   9132    833   -492   -668       O  
ATOM   2025  CB  GLU A 259       5.574  26.230 -20.173  1.00 74.41           C  
ANISOU 2025  CB  GLU A 259     8680  10326   9268    973   -567   -723       C  
ATOM   2026  CG  GLU A 259       4.536  25.161 -19.843  1.00 75.91           C  
ANISOU 2026  CG  GLU A 259     8822  10488   9533    952   -584   -801       C  
ATOM   2027  CD  GLU A 259       3.256  25.725 -19.221  1.00 85.59           C  
ANISOU 2027  CD  GLU A 259    10028  11687  10804    934   -584   -824       C  
ATOM   2028  OE1 GLU A 259       3.159  26.951 -18.981  1.00 87.13           O  
ANISOU 2028  OE1 GLU A 259    10246  11883  10975    934   -570   -780       O  
ATOM   2029  OE2 GLU A 259       2.324  24.932 -18.970  1.00 83.92           O  
ANISOU 2029  OE2 GLU A 259     9776  11453  10658    918   -597   -890       O  
ATOM   2030  N   TYR A 260       8.440  25.109 -19.719  1.00 68.31           N  
ANISOU 2030  N   TYR A 260     7951   9539   8464    922   -515   -636       N  
ATOM   2031  CA  TYR A 260       9.354  23.976 -19.652  1.00 69.56           C  
ANISOU 2031  CA  TYR A 260     8106   9687   8636    903   -508   -639       C  
ATOM   2032  C   TYR A 260      10.197  24.024 -18.374  1.00 66.08           C  
ANISOU 2032  C   TYR A 260     7687   9205   8216    838   -465   -578       C  
ATOM   2033  O   TYR A 260      10.235  23.062 -17.609  1.00 68.78           O  
ANISOU 2033  O   TYR A 260     8011   9510   8611    793   -455   -592       O  
ATOM   2034  CB  TYR A 260      10.231  23.916 -20.914  1.00 69.62           C  
ANISOU 2034  CB  TYR A 260     8129   9746   8579    960   -522   -632       C  
ATOM   2035  CG  TYR A 260      11.242  22.792 -20.900  1.00 71.17           C  
ANISOU 2035  CG  TYR A 260     8321   9933   8788    942   -515   -634       C  
ATOM   2036  CD1 TYR A 260      10.837  21.465 -21.051  1.00 72.80           C  
ANISOU 2036  CD1 TYR A 260     8488  10129   9045    940   -537   -704       C  
ATOM   2037  CD2 TYR A 260      12.603  23.052 -20.723  1.00 68.84           C  
ANISOU 2037  CD2 TYR A 260     8059   9636   8460    928   -485   -568       C  
ATOM   2038  CE1 TYR A 260      11.757  20.427 -21.029  1.00 73.11           C  
ANISOU 2038  CE1 TYR A 260     8521  10156   9102    925   -530   -707       C  
ATOM   2039  CE2 TYR A 260      13.528  22.019 -20.697  1.00 69.74           C  
ANISOU 2039  CE2 TYR A 260     8167   9740   8590    912   -479   -571       C  
ATOM   2040  CZ  TYR A 260      13.100  20.712 -20.853  1.00 71.53           C  
ANISOU 2040  CZ  TYR A 260     8355   9956   8867    911   -501   -639       C  
ATOM   2041  OH  TYR A 260      14.009  19.679 -20.830  1.00 73.10           O  
ANISOU 2041  OH  TYR A 260     8546  10143   9087    896   -495   -642       O  
ATOM   2042  N   MET A 261      10.840  25.157 -18.130  1.00 63.84           N  
ANISOU 2042  N   MET A 261     7439   8926   7893    832   -439   -511       N  
ATOM   2043  CA  MET A 261      11.697  25.295 -16.964  1.00 65.17           C  
ANISOU 2043  CA  MET A 261     7628   9059   8073    774   -401   -453       C  
ATOM   2044  C   MET A 261      10.939  25.105 -15.652  1.00 66.18           C  
ANISOU 2044  C   MET A 261     7741   9142   8261    716   -385   -464       C  
ATOM   2045  O   MET A 261      11.422  24.429 -14.738  1.00 65.62           O  
ANISOU 2045  O   MET A 261     7670   9040   8223    667   -366   -448       O  
ATOM   2046  CB  MET A 261      12.435  26.626 -17.009  1.00 65.20           C  
ANISOU 2046  CB  MET A 261     7669   9076   8027    783   -378   -386       C  
ATOM   2047  CG  MET A 261      13.394  26.742 -18.191  1.00 66.19           C  
ANISOU 2047  CG  MET A 261     7813   9242   8095    834   -385   -365       C  
ATOM   2048  SD  MET A 261      14.525  25.337 -18.351  1.00 72.24           S  
ANISOU 2048  SD  MET A 261     8574  10006   8869    824   -385   -373       S  
ATOM   2049  CE  MET A 261      15.944  25.905 -17.425  1.00 69.30           C  
ANISOU 2049  CE  MET A 261     8235   9609   8488    779   -342   -291       C  
ATOM   2050  N   LEU A 262       9.739  25.670 -15.585  1.00 66.54           N  
ANISOU 2050  N   LEU A 262     7773   9186   8323    723   -394   -491       N  
ATOM   2051  CA  LEU A 262       8.875  25.525 -14.416  1.00 64.41           C  
ANISOU 2051  CA  LEU A 262     7487   8877   8110    671   -379   -507       C  
ATOM   2052  C   LEU A 262       8.494  24.066 -14.162  1.00 61.87           C  
ANISOU 2052  C   LEU A 262     7131   8530   7846    650   -387   -557       C  
ATOM   2053  O   LEU A 262       8.418  23.635 -13.011  1.00 56.99           O  
ANISOU 2053  O   LEU A 262     6509   7875   7271    595   -363   -546       O  
ATOM   2054  CB  LEU A 262       7.628  26.410 -14.547  1.00 63.69           C  
ANISOU 2054  CB  LEU A 262     7383   8790   8025    690   -390   -534       C  
ATOM   2055  CG  LEU A 262       6.680  26.534 -13.346  1.00 67.10           C  
ANISOU 2055  CG  LEU A 262     7800   9185   8511    639   -370   -547       C  
ATOM   2056  CD1 LEU A 262       7.361  27.120 -12.104  1.00 65.33           C  
ANISOU 2056  CD1 LEU A 262     7603   8937   8282    584   -329   -486       C  
ATOM   2057  CD2 LEU A 262       5.444  27.337 -13.728  1.00 66.11           C  
ANISOU 2057  CD2 LEU A 262     7658   9068   8392    668   -389   -582       C  
ATOM   2058  N   GLN A 263       8.270  23.301 -15.226  1.00 61.01           N  
ANISOU 2058  N   GLN A 263     6999   8443   7740    693   -421   -609       N  
ATOM   2059  CA  GLN A 263       8.050  21.858 -15.067  1.00 68.03           C  
ANISOU 2059  CA  GLN A 263     7853   9306   8688    675   -428   -656       C  
ATOM   2060  C   GLN A 263       9.283  21.151 -14.482  1.00 66.35           C  
ANISOU 2060  C   GLN A 263     7655   9073   8481    638   -405   -612       C  
ATOM   2061  O   GLN A 263       9.171  20.428 -13.486  1.00 63.50           O  
ANISOU 2061  O   GLN A 263     7282   8672   8173    589   -385   -609       O  
ATOM   2062  CB  GLN A 263       7.624  21.190 -16.386  1.00 75.67           C  
ANISOU 2062  CB  GLN A 263     8790  10304   9656    732   -471   -726       C  
ATOM   2063  CG  GLN A 263       6.214  21.521 -16.855  1.00 84.62           C  
ANISOU 2063  CG  GLN A 263     9896  11449  10807    762   -499   -787       C  
ATOM   2064  CD  GLN A 263       5.167  21.321 -15.767  1.00 92.62           C  
ANISOU 2064  CD  GLN A 263    10884  12416  11892    713   -482   -809       C  
ATOM   2065  OE1 GLN A 263       5.050  20.235 -15.186  1.00 95.09           O  
ANISOU 2065  OE1 GLN A 263    11172  12691  12267    677   -470   -830       O  
ATOM   2066  NE2 GLN A 263       4.402  22.376 -15.482  1.00 89.89           N  
ANISOU 2066  NE2 GLN A 263    10544  12070  11540    712   -477   -802       N  
ATOM   2067  N   ARG A 264      10.447  21.381 -15.092  1.00 61.78           N  
ANISOU 2067  N   ARG A 264     7103   8522   7848    664   -406   -576       N  
ATOM   2068  CA  ARG A 264      11.688  20.728 -14.674  1.00 60.77           C  
ANISOU 2068  CA  ARG A 264     6989   8379   7723    636   -388   -537       C  
ATOM   2069  C   ARG A 264      12.117  21.111 -13.263  1.00 59.75           C  
ANISOU 2069  C   ARG A 264     6883   8218   7603    576   -351   -476       C  
ATOM   2070  O   ARG A 264      12.675  20.285 -12.541  1.00 59.64           O  
ANISOU 2070  O   ARG A 264     6866   8174   7619    539   -336   -457       O  
ATOM   2071  CB  ARG A 264      12.825  21.031 -15.650  1.00 61.54           C  
ANISOU 2071  CB  ARG A 264     7110   8515   7758    677   -395   -510       C  
ATOM   2072  CG  ARG A 264      12.496  20.849 -17.131  1.00 65.94           C  
ANISOU 2072  CG  ARG A 264     7651   9116   8289    743   -431   -565       C  
ATOM   2073  CD  ARG A 264      12.663  19.408 -17.598  1.00 67.81           C  
ANISOU 2073  CD  ARG A 264     7856   9348   8562    752   -450   -616       C  
ATOM   2074  NE  ARG A 264      11.758  18.507 -16.894  1.00 70.38           N  
ANISOU 2074  NE  ARG A 264     8145   9631   8966    717   -451   -659       N  
ATOM   2075  CZ  ARG A 264      10.468  18.361 -17.177  1.00 71.40           C  
ANISOU 2075  CZ  ARG A 264     8241   9761   9126    733   -474   -722       C  
ATOM   2076  NH1 ARG A 264       9.905  19.043 -18.167  1.00 71.05           N  
ANISOU 2076  NH1 ARG A 264     8197   9760   9038    787   -501   -751       N  
ATOM   2077  NH2 ARG A 264       9.738  17.527 -16.455  1.00 74.58           N  
ANISOU 2077  NH2 ARG A 264     8612  10121   9606    696   -468   -755       N  
ATOM   2078  N   THR A 265      11.863  22.357 -12.871  1.00 57.73           N  
ANISOU 2078  N   THR A 265     6648   7967   7319    569   -337   -446       N  
ATOM   2079  CA  THR A 265      12.177  22.800 -11.519  1.00 58.08           C  
ANISOU 2079  CA  THR A 265     6713   7985   7370    514   -303   -394       C  
ATOM   2080  C   THR A 265      11.446  21.922 -10.499  1.00 62.31           C  
ANISOU 2080  C   THR A 265     7224   8481   7969    468   -291   -416       C  
ATOM   2081  O   THR A 265      11.897  21.760  -9.369  1.00 63.39           O  
ANISOU 2081  O   THR A 265     7372   8593   8118    420   -266   -376       O  
ATOM   2082  CB  THR A 265      11.822  24.289 -11.316  1.00 58.03           C  
ANISOU 2082  CB  THR A 265     6726   7990   7333    517   -292   -371       C  
ATOM   2083  OG1 THR A 265      12.492  25.076 -12.305  1.00 56.05           O  
ANISOU 2083  OG1 THR A 265     6496   7774   7026    562   -300   -348       O  
ATOM   2084  CG2 THR A 265      12.247  24.784  -9.940  1.00 56.57           C  
ANISOU 2084  CG2 THR A 265     6562   7782   7150    462   -257   -321       C  
ATOM   2085  N   GLN A 266      10.324  21.342 -10.915  1.00 66.42           N  
ANISOU 2085  N   GLN A 266     7710   8997   8532    483   -310   -478       N  
ATOM   2086  CA  GLN A 266       9.517  20.490 -10.043  1.00 68.01           C  
ANISOU 2086  CA  GLN A 266     7883   9157   8799    442   -298   -503       C  
ATOM   2087  C   GLN A 266       9.828  19.016 -10.257  1.00 71.98           C  
ANISOU 2087  C   GLN A 266     8361   9642   9345    441   -307   -526       C  
ATOM   2088  O   GLN A 266       9.157  18.142  -9.696  1.00 71.84           O  
ANISOU 2088  O   GLN A 266     8315   9590   9392    413   -298   -552       O  
ATOM   2089  CB  GLN A 266       8.032  20.741 -10.285  1.00 64.74           C  
ANISOU 2089  CB  GLN A 266     7440   8742   8415    457   -310   -561       C  
ATOM   2090  CG  GLN A 266       7.598  22.162  -9.995  1.00 64.52           C  
ANISOU 2090  CG  GLN A 266     7433   8728   8356    455   -300   -542       C  
ATOM   2091  CD  GLN A 266       6.162  22.396 -10.382  1.00 67.25           C  
ANISOU 2091  CD  GLN A 266     7747   9073   8730    476   -317   -603       C  
ATOM   2092  OE1 GLN A 266       5.245  21.840  -9.779  1.00 70.74           O  
ANISOU 2092  OE1 GLN A 266     8162   9485   9232    447   -307   -636       O  
ATOM   2093  NE2 GLN A 266       5.954  23.214 -11.402  1.00 69.21           N  
ANISOU 2093  NE2 GLN A 266     8001   9358   8939    527   -343   -617       N  
ATOM   2094  N   ASP A 267      10.843  18.743 -11.071  1.00 73.07           N  
ANISOU 2094  N   ASP A 267     8508   9801   9453    471   -323   -518       N  
ATOM   2095  CA  ASP A 267      11.239  17.382 -11.352  1.00 80.54           C  
ANISOU 2095  CA  ASP A 267     9430  10731  10439    472   -332   -540       C  
ATOM   2096  C   ASP A 267      11.619  16.684 -10.057  1.00 85.77           C  
ANISOU 2096  C   ASP A 267    10096  11351  11143    415   -303   -499       C  
ATOM   2097  O   ASP A 267      12.221  17.285  -9.166  1.00 87.88           O  
ANISOU 2097  O   ASP A 267    10395  11615  11381    384   -278   -438       O  
ATOM   2098  CB  ASP A 267      12.411  17.363 -12.321  1.00 82.99           C  
ANISOU 2098  CB  ASP A 267     9756  11073  10702    510   -348   -527       C  
ATOM   2099  CG  ASP A 267      12.422  16.132 -13.182  1.00 90.50           C  
ANISOU 2099  CG  ASP A 267    10673  12024  11691    537   -373   -583       C  
ATOM   2100  OD1 ASP A 267      12.768  15.041 -12.664  1.00 91.42           O  
ANISOU 2100  OD1 ASP A 267    10773  12105  11859    507   -363   -579       O  
ATOM   2101  OD2 ASP A 267      12.083  16.265 -14.380  1.00 93.24           O  
ANISOU 2101  OD2 ASP A 267    11007  12407  12014    589   -402   -632       O  
ATOM   2102  N   GLN A 268      11.239  15.418  -9.954  1.00 95.00           N  
ANISOU 2102  N   GLN A 268    11228  12487  12381    403   -305   -534       N  
ATOM   2103  CA  GLN A 268      11.564  14.584  -8.798  1.00101.70           C  
ANISOU 2103  CA  GLN A 268    12074  13293  13275    353   -277   -496       C  
ATOM   2104  C   GLN A 268      13.062  14.258  -8.727  1.00101.10           C  
ANISOU 2104  C   GLN A 268    12021  13219  13175    348   -275   -445       C  
ATOM   2105  O   GLN A 268      13.594  14.022  -7.639  1.00 99.89           O  
ANISOU 2105  O   GLN A 268    11882  13041  13030    306   -251   -390       O  
ATOM   2106  CB  GLN A 268      10.713  13.303  -8.787  1.00106.73           C  
ANISOU 2106  CB  GLN A 268    12662  13891  14001    344   -279   -549       C  
ATOM   2107  CG  GLN A 268      10.532  12.636 -10.153  1.00111.91           C  
ANISOU 2107  CG  GLN A 268    13282  14560  14679    393   -315   -621       C  
ATOM   2108  CD  GLN A 268       9.564  13.380 -11.068  1.00112.61           C  
ANISOU 2108  CD  GLN A 268    13359  14683  14744    435   -341   -680       C  
ATOM   2109  OE1 GLN A 268       8.400  13.606 -10.717  1.00113.80           O  
ANISOU 2109  OE1 GLN A 268    13493  14820  14926    423   -335   -708       O  
ATOM   2110  NE2 GLN A 268      10.043  13.766 -12.250  1.00108.97           N  
ANISOU 2110  NE2 GLN A 268    12908  14267  14228    485   -370   -698       N  
ATOM   2111  N   ASP A 269      13.739  14.256  -9.876  1.00 99.31           N  
ANISOU 2111  N   ASP A 269    11795  13021  12915    391   -300   -462       N  
ATOM   2112  CA  ASP A 269      15.197  14.125  -9.890  1.00100.78           C  
ANISOU 2112  CA  ASP A 269    12005  13214  13073    391   -297   -414       C  
ATOM   2113  C   ASP A 269      15.905  15.440  -9.535  1.00101.60           C  
ANISOU 2113  C   ASP A 269    12154  13343  13104    385   -284   -355       C  
ATOM   2114  O   ASP A 269      15.902  16.402 -10.312  1.00106.41           O  
ANISOU 2114  O   ASP A 269    12779  13990  13662    420   -295   -362       O  
ATOM   2115  CB  ASP A 269      15.706  13.586 -11.229  1.00102.11           C  
ANISOU 2115  CB  ASP A 269    12156  13404  13235    438   -325   -455       C  
ATOM   2116  CG  ASP A 269      17.229  13.490 -11.280  1.00103.25           C  
ANISOU 2116  CG  ASP A 269    12324  13555  13350    438   -321   -407       C  
ATOM   2117  OD1 ASP A 269      17.882  13.532 -10.211  1.00101.04           O  
ANISOU 2117  OD1 ASP A 269    12066  13255  13072    398   -300   -346       O  
ATOM   2118  OD2 ASP A 269      17.775  13.374 -12.395  1.00102.06           O  
ANISOU 2118  OD2 ASP A 269    12170  13433  13177    479   -340   -431       O  
ATOM   2119  N   GLU A 270      16.536  15.435  -8.364  1.00100.27           N  
ANISOU 2119  N   GLU A 270    12006  13154  12936    341   -261   -295       N  
ATOM   2120  CA  GLU A 270      17.226  16.594  -7.775  1.00 96.09           C  
ANISOU 2120  CA  GLU A 270    11518  12642  12351    326   -245   -238       C  
ATOM   2121  C   GLU A 270      18.151  17.395  -8.694  1.00 87.66           C  
ANISOU 2121  C   GLU A 270    10472  11611  11223    363   -255   -224       C  
ATOM   2122  O   GLU A 270      18.227  18.617  -8.575  1.00 83.23           O  
ANISOU 2122  O   GLU A 270     9937  11070  10617    365   -246   -200       O  
ATOM   2123  CB  GLU A 270      18.000  16.148  -6.525  1.00100.58           C  
ANISOU 2123  CB  GLU A 270    12099  13184  12933    280   -226   -181       C  
ATOM   2124  CG  GLU A 270      18.980  15.002  -6.757  1.00108.11           C  
ANISOU 2124  CG  GLU A 270    13041  14121  13915    283   -235   -172       C  
ATOM   2125  CD  GLU A 270      19.104  14.069  -5.566  1.00113.59           C  
ANISOU 2125  CD  GLU A 270    13729  14775  14654    239   -219   -139       C  
ATOM   2126  OE1 GLU A 270      18.536  14.379  -4.494  1.00118.76           O  
ANISOU 2126  OE1 GLU A 270    14393  15420  15311    205   -199   -116       O  
ATOM   2127  OE2 GLU A 270      19.770  13.018  -5.704  1.00113.59           O  
ANISOU 2127  OE2 GLU A 270    13715  14756  14690    240   -226   -134       O  
ATOM   2128  N   ASN A 271      18.849  16.702  -9.592  1.00 84.16           N  
ANISOU 2128  N   ASN A 271    10018  11175  10784    392   -272   -240       N  
ATOM   2129  CA  ASN A 271      19.829  17.327 -10.478  1.00 85.19           C  
ANISOU 2129  CA  ASN A 271    10168  11338  10862    427   -278   -225       C  
ATOM   2130  C   ASN A 271      19.184  18.115 -11.594  1.00 79.78           C  
ANISOU 2130  C   ASN A 271     9483  10690  10139    474   -292   -261       C  
ATOM   2131  O   ASN A 271      19.654  19.195 -11.941  1.00 81.21           O  
ANISOU 2131  O   ASN A 271     9690  10898  10268    492   -286   -234       O  
ATOM   2132  CB  ASN A 271      20.763  16.281 -11.090  1.00 92.62           C  
ANISOU 2132  CB  ASN A 271    11095  12276  11821    443   -290   -234       C  
ATOM   2133  CG  ASN A 271      21.457  15.430 -10.046  1.00 99.80           C  
ANISOU 2133  CG  ASN A 271    12002  13147  12770    400   -279   -197       C  
ATOM   2134  OD1 ASN A 271      21.566  15.815  -8.877  1.00 99.03           O  
ANISOU 2134  OD1 ASN A 271    11923  13034  12669    361   -261   -152       O  
ATOM   2135  ND2 ASN A 271      21.936  14.262 -10.466  1.00102.04           N  
ANISOU 2135  ND2 ASN A 271    12263  13416  13091    409   -290   -217       N  
ATOM   2136  N   VAL A 272      18.124  17.556 -12.171  1.00 76.95           N  
ANISOU 2136  N   VAL A 272     9095  10334   9810    495   -311   -322       N  
ATOM   2137  CA  VAL A 272      17.353  18.252 -13.198  1.00 71.17           C  
ANISOU 2137  CA  VAL A 272     8359   9636   9044    541   -328   -361       C  
ATOM   2138  C   VAL A 272      16.841  19.546 -12.566  1.00 64.99           C  
ANISOU 2138  C   VAL A 272     7600   8858   8236    525   -312   -331       C  
ATOM   2139  O   VAL A 272      17.086  20.651 -13.073  1.00 57.87           O  
ANISOU 2139  O   VAL A 272     6720   7985   7281    552   -310   -311       O  
ATOM   2140  CB  VAL A 272      16.156  17.411 -13.711  1.00 72.36           C  
ANISOU 2140  CB  VAL A 272     8469   9783   9241    559   -351   -435       C  
ATOM   2141  CG1 VAL A 272      15.579  18.013 -14.988  1.00 74.69           C  
ANISOU 2141  CG1 VAL A 272     8761  10123   9494    617   -376   -477       C  
ATOM   2142  CG2 VAL A 272      16.565  15.974 -13.967  1.00 73.36           C  
ANISOU 2142  CG2 VAL A 272     8568   9891   9415    559   -362   -465       C  
ATOM   2143  N   ALA A 273      16.167  19.394 -11.428  1.00 61.47           N  
ANISOU 2143  N   ALA A 273     7147   8380   7829    480   -297   -327       N  
ATOM   2144  CA  ALA A 273      15.561  20.526 -10.736  1.00 59.78           C  
ANISOU 2144  CA  ALA A 273     6949   8166   7600    461   -281   -307       C  
ATOM   2145  C   ALA A 273      16.580  21.642 -10.474  1.00 58.92           C  
ANISOU 2145  C   ALA A 273     6877   8070   7440    455   -263   -247       C  
ATOM   2146  O   ALA A 273      16.283  22.815 -10.716  1.00 58.12           O  
ANISOU 2146  O   ALA A 273     6789   7988   7305    472   -260   -239       O  
ATOM   2147  CB  ALA A 273      14.887  20.073  -9.448  1.00 57.60           C  
ANISOU 2147  CB  ALA A 273     6661   7851   7372    409   -264   -306       C  
ATOM   2148  N   LEU A 274      17.779  21.274 -10.014  1.00 56.10           N  
ANISOU 2148  N   LEU A 274     6532   7702   7080    434   -253   -206       N  
ATOM   2149  CA  LEU A 274      18.825  22.262  -9.746  1.00 55.49           C  
ANISOU 2149  CA  LEU A 274     6487   7635   6962    427   -236   -151       C  
ATOM   2150  C   LEU A 274      19.245  23.016 -11.001  1.00 55.11           C  
ANISOU 2150  C   LEU A 274     6450   7622   6867    478   -244   -150       C  
ATOM   2151  O   LEU A 274      19.344  24.234 -10.971  1.00 56.73           O  
ANISOU 2151  O   LEU A 274     6675   7838   7040    484   -231   -123       O  
ATOM   2152  CB  LEU A 274      20.045  21.635  -9.068  1.00 55.07           C  
ANISOU 2152  CB  LEU A 274     6442   7564   6919    397   -226   -112       C  
ATOM   2153  CG  LEU A 274      21.231  22.578  -8.829  1.00 54.08           C  
ANISOU 2153  CG  LEU A 274     6345   7448   6756    391   -211    -60       C  
ATOM   2154  CD1 LEU A 274      20.857  23.717  -7.894  1.00 51.01           C  
ANISOU 2154  CD1 LEU A 274     5972   7056   6354    363   -191    -37       C  
ATOM   2155  CD2 LEU A 274      22.428  21.808  -8.296  1.00 51.18           C  
ANISOU 2155  CD2 LEU A 274     5981   7063   6402    367   -207    -28       C  
ATOM   2156  N   GLU A 275      19.483  22.310 -12.102  1.00 59.06           N  
ANISOU 2156  N   GLU A 275     6938   8138   7363    517   -263   -178       N  
ATOM   2157  CA  GLU A 275      19.826  22.994 -13.353  1.00 59.58           C  
ANISOU 2157  CA  GLU A 275     7016   8242   7381    569   -269   -177       C  
ATOM   2158  C   GLU A 275      18.654  23.836 -13.836  1.00 59.10           C  
ANISOU 2158  C   GLU A 275     6953   8200   7302    598   -278   -202       C  
ATOM   2159  O   GLU A 275      18.837  24.955 -14.307  1.00 60.91           O  
ANISOU 2159  O   GLU A 275     7201   8451   7490    624   -270   -177       O  
ATOM   2160  CB  GLU A 275      20.263  22.013 -14.440  1.00 65.62           C  
ANISOU 2160  CB  GLU A 275     7765   9023   8143    606   -288   -208       C  
ATOM   2161  CG  GLU A 275      21.349  21.022 -14.025  1.00 72.67           C  
ANISOU 2161  CG  GLU A 275     8655   9894   9063    580   -283   -191       C  
ATOM   2162  CD  GLU A 275      22.651  21.658 -13.525  1.00 74.93           C  
ANISOU 2162  CD  GLU A 275     8968  10174   9327    560   -259   -129       C  
ATOM   2163  OE1 GLU A 275      22.951  22.831 -13.846  1.00 69.62           O  
ANISOU 2163  OE1 GLU A 275     8318   9521   8613    578   -246   -100       O  
ATOM   2164  OE2 GLU A 275      23.390  20.959 -12.796  1.00 78.01           O  
ANISOU 2164  OE2 GLU A 275     9356  10538   9745    526   -253   -108       O  
ATOM   2165  N   ALA A 276      17.444  23.307 -13.701  1.00 59.39           N  
ANISOU 2165  N   ALA A 276     6964   8227   7373    593   -293   -250       N  
ATOM   2166  CA  ALA A 276      16.251  24.066 -14.058  1.00 58.65           C  
ANISOU 2166  CA  ALA A 276     6865   8148   7270    617   -304   -277       C  
ATOM   2167  C   ALA A 276      16.149  25.326 -13.204  1.00 59.54           C  
ANISOU 2167  C   ALA A 276     6998   8250   7373    590   -279   -235       C  
ATOM   2168  O   ALA A 276      15.967  26.418 -13.729  1.00 60.91           O  
ANISOU 2168  O   ALA A 276     7184   8445   7512    620   -278   -223       O  
ATOM   2169  CB  ALA A 276      15.013  23.206 -13.907  1.00 60.05           C  
ANISOU 2169  CB  ALA A 276     7009   8311   7498    609   -322   -336       C  
ATOM   2170  N   CYS A 277      16.327  25.182 -11.893  1.00 59.39           N  
ANISOU 2170  N   CYS A 277     6983   8199   7382    534   -259   -211       N  
ATOM   2171  CA  CYS A 277      16.187  26.316 -10.977  1.00 59.71           C  
ANISOU 2171  CA  CYS A 277     7040   8230   7417    504   -235   -179       C  
ATOM   2172  C   CYS A 277      17.120  27.500 -11.262  1.00 59.14           C  
ANISOU 2172  C   CYS A 277     6995   8173   7302    520   -220   -130       C  
ATOM   2173  O   CYS A 277      16.772  28.642 -10.950  1.00 57.83           O  
ANISOU 2173  O   CYS A 277     6838   8006   7129    515   -207   -115       O  
ATOM   2174  CB  CYS A 277      16.316  25.867  -9.525  1.00 59.04           C  
ANISOU 2174  CB  CYS A 277     6955   8112   7365    443   -216   -162       C  
ATOM   2175  SG  CYS A 277      15.828  27.145  -8.348  1.00 59.76           S  
ANISOU 2175  SG  CYS A 277     7058   8191   7455    405   -190   -140       S  
ATOM   2176  N   GLU A 278      18.281  27.239 -11.868  1.00 58.02           N  
ANISOU 2176  N   GLU A 278     6864   8043   7137    539   -220   -108       N  
ATOM   2177  CA  GLU A 278      19.227  28.314 -12.246  1.00 57.65           C  
ANISOU 2177  CA  GLU A 278     6840   8010   7054    558   -203    -62       C  
ATOM   2178  C   GLU A 278      18.616  29.311 -13.221  1.00 57.57           C  
ANISOU 2178  C   GLU A 278     6834   8025   7014    606   -209    -66       C  
ATOM   2179  O   GLU A 278      19.028  30.473 -13.276  1.00 56.08           O  
ANISOU 2179  O   GLU A 278     6662   7840   6806    614   -190    -28       O  
ATOM   2180  CB  GLU A 278      20.482  27.739 -12.898  1.00 61.70           C  
ANISOU 2180  CB  GLU A 278     7360   8534   7549    577   -204    -45       C  
ATOM   2181  CG  GLU A 278      21.256  26.746 -12.046  1.00 64.12           C  
ANISOU 2181  CG  GLU A 278     7663   8816   7882    534   -200    -35       C  
ATOM   2182  CD  GLU A 278      22.262  27.408 -11.138  1.00 64.63           C  
ANISOU 2182  CD  GLU A 278     7746   8865   7945    499   -175     15       C  
ATOM   2183  OE1 GLU A 278      22.413  28.647 -11.205  1.00 64.15           O  
ANISOU 2183  OE1 GLU A 278     7699   8810   7864    508   -159     42       O  
ATOM   2184  OE2 GLU A 278      22.903  26.672 -10.362  1.00 70.42           O  
ANISOU 2184  OE2 GLU A 278     8478   9579   8699    464   -173     27       O  
ATOM   2185  N   PHE A 279      17.641  28.848 -14.001  1.00 59.58           N  
ANISOU 2185  N   PHE A 279     7071   8297   7269    641   -236   -114       N  
ATOM   2186  CA  PHE A 279      16.957  29.703 -14.965  1.00 60.43           C  
ANISOU 2186  CA  PHE A 279     7181   8432   7349    691   -246   -122       C  
ATOM   2187  C   PHE A 279      16.379  30.938 -14.295  1.00 58.98           C  
ANISOU 2187  C   PHE A 279     7003   8233   7174    673   -230   -103       C  
ATOM   2188  O   PHE A 279      16.503  32.045 -14.826  1.00 58.76           O  
ANISOU 2188  O   PHE A 279     6988   8218   7118    703   -221    -73       O  
ATOM   2189  CB  PHE A 279      15.843  28.934 -15.663  1.00 62.04           C  
ANISOU 2189  CB  PHE A 279     7360   8652   7561    722   -281   -184       C  
ATOM   2190  CG  PHE A 279      15.273  29.635 -16.863  1.00 64.19           C  
ANISOU 2190  CG  PHE A 279     7634   8960   7795    785   -299   -194       C  
ATOM   2191  CD1 PHE A 279      14.186  30.494 -16.736  1.00 62.81           C  
ANISOU 2191  CD1 PHE A 279     7453   8783   7628    791   -303   -204       C  
ATOM   2192  CD2 PHE A 279      15.808  29.418 -18.135  1.00 65.17           C  
ANISOU 2192  CD2 PHE A 279     7764   9122   7874    838   -312   -194       C  
ATOM   2193  CE1 PHE A 279      13.653  31.130 -17.847  1.00 61.34           C  
ANISOU 2193  CE1 PHE A 279     7268   8631   7407    851   -322   -211       C  
ATOM   2194  CE2 PHE A 279      15.280  30.057 -19.246  1.00 62.20           C  
ANISOU 2194  CE2 PHE A 279     7391   8783   7458    899   -329   -201       C  
ATOM   2195  CZ  PHE A 279      14.202  30.913 -19.099  1.00 61.21           C  
ANISOU 2195  CZ  PHE A 279     7260   8654   7341    906   -335   -208       C  
ATOM   2196  N   TRP A 280      15.767  30.743 -13.126  1.00 55.08           N  
ANISOU 2196  N   TRP A 280     6497   7711   6720    623   -224   -119       N  
ATOM   2197  CA  TRP A 280      15.067  31.829 -12.427  1.00 56.01           C  
ANISOU 2197  CA  TRP A 280     6615   7813   6852    603   -209   -112       C  
ATOM   2198  C   TRP A 280      16.041  32.819 -11.903  1.00 58.57           C  
ANISOU 2198  C   TRP A 280     6961   8127   7166    583   -179    -58       C  
ATOM   2199  O   TRP A 280      15.806  34.038 -11.964  1.00 56.95           O  
ANISOU 2199  O   TRP A 280     6761   7921   6955    594   -167    -39       O  
ATOM   2200  CB  TRP A 280      14.173  31.279 -11.311  1.00 52.95           C  
ANISOU 2200  CB  TRP A 280     6210   7400   6509    555   -209   -146       C  
ATOM   2201  CG  TRP A 280      13.384  30.104 -11.816  1.00 51.93           C  
ANISOU 2201  CG  TRP A 280     6056   7276   6397    572   -237   -200       C  
ATOM   2202  CD1 TRP A 280      13.469  28.778 -11.404  1.00 51.51           C  
ANISOU 2202  CD1 TRP A 280     5991   7209   6372    545   -243   -221       C  
ATOM   2203  CD2 TRP A 280      12.424  30.101 -12.925  1.00 53.27           C  
ANISOU 2203  CD2 TRP A 280     6210   7469   6560    624   -267   -242       C  
ATOM   2204  NE1 TRP A 280      12.634  27.981 -12.141  1.00 54.00           N  
ANISOU 2204  NE1 TRP A 280     6281   7534   6702    574   -271   -275       N  
ATOM   2205  CE2 TRP A 280      11.972  28.714 -13.070  1.00 53.79           C  
ANISOU 2205  CE2 TRP A 280     6252   7532   6654    623   -289   -292       C  
ATOM   2206  CE3 TRP A 280      11.898  31.079 -13.770  1.00 53.97           C  
ANISOU 2206  CE3 TRP A 280     6301   7580   6624    671   -279   -243       C  
ATOM   2207  CZ2 TRP A 280      11.030  28.342 -14.024  1.00 56.92           C  
ANISOU 2207  CZ2 TRP A 280     6625   7948   7055    666   -322   -347       C  
ATOM   2208  CZ3 TRP A 280      10.955  30.694 -14.730  1.00 54.83           C  
ANISOU 2208  CZ3 TRP A 280     6389   7711   6732    717   -313   -294       C  
ATOM   2209  CH2 TRP A 280      10.532  29.355 -14.853  1.00 57.09           C  
ANISOU 2209  CH2 TRP A 280     6651   7995   7046    714   -335   -347       C  
ATOM   2210  N   LEU A 281      17.164  32.290 -11.413  1.00 62.14           N  
ANISOU 2210  N   LEU A 281     7422   8570   7618    554   -167    -34       N  
ATOM   2211  CA  LEU A 281      18.249  33.098 -10.888  1.00 60.02           C  
ANISOU 2211  CA  LEU A 281     7171   8291   7343    533   -139     15       C  
ATOM   2212  C   LEU A 281      18.773  34.052 -11.954  1.00 61.13           C  
ANISOU 2212  C   LEU A 281     7325   8449   7452    581   -131     47       C  
ATOM   2213  O   LEU A 281      18.913  35.247 -11.696  1.00 62.41           O  
ANISOU 2213  O   LEU A 281     7495   8602   7617    576   -109     75       O  
ATOM   2214  CB  LEU A 281      19.378  32.203 -10.377  1.00 60.75           C  
ANISOU 2214  CB  LEU A 281     7269   8373   7438    503   -134     31       C  
ATOM   2215  CG  LEU A 281      20.014  32.509  -9.014  1.00 61.67           C  
ANISOU 2215  CG  LEU A 281     7393   8468   7572    449   -112     56       C  
ATOM   2216  CD1 LEU A 281      21.373  31.828  -8.936  1.00 58.17           C  
ANISOU 2216  CD1 LEU A 281     6957   8022   7122    439   -109     81       C  
ATOM   2217  CD2 LEU A 281      20.145  33.999  -8.723  1.00 59.72           C  
ANISOU 2217  CD2 LEU A 281     7154   8215   7323    444    -88     83       C  
ATOM   2218  N   THR A 282      19.050  33.541 -13.154  1.00 61.89           N  
ANISOU 2218  N   THR A 282     7424   8571   7520    627   -146     43       N  
ATOM   2219  CA  THR A 282      19.617  34.404 -14.190  1.00 63.37           C  
ANISOU 2219  CA  THR A 282     7626   8778   7675    674   -135     79       C  
ATOM   2220  C   THR A 282      18.551  35.249 -14.912  1.00 64.08           C  
ANISOU 2220  C   THR A 282     7713   8883   7752    717   -144     71       C  
ATOM   2221  O   THR A 282      18.826  36.385 -15.309  1.00 65.88           O  
ANISOU 2221  O   THR A 282     7952   9113   7966    741   -125    110       O  
ATOM   2222  CB  THR A 282      20.542  33.657 -15.175  1.00 66.38           C  
ANISOU 2222  CB  THR A 282     8013   9182   8025    708   -141     87       C  
ATOM   2223  OG1 THR A 282      19.764  33.002 -16.173  1.00 71.02           O  
ANISOU 2223  OG1 THR A 282     8591   9799   8593    752   -172     46       O  
ATOM   2224  CG2 THR A 282      21.421  32.625 -14.444  1.00 71.69           C  
ANISOU 2224  CG2 THR A 282     8684   9837   8716    665   -138     85       C  
ATOM   2225  N   LEU A 283      17.339  34.708 -15.059  1.00 63.03           N  
ANISOU 2225  N   LEU A 283     7563   8759   7627    727   -173     22       N  
ATOM   2226  CA  LEU A 283      16.200  35.498 -15.568  1.00 61.36           C  
ANISOU 2226  CA  LEU A 283     7344   8557   7411    762   -186      9       C  
ATOM   2227  C   LEU A 283      15.949  36.753 -14.753  1.00 61.59           C  
ANISOU 2227  C   LEU A 283     7375   8560   7466    735   -161     33       C  
ATOM   2228  O   LEU A 283      15.650  37.799 -15.311  1.00 67.12           O  
ANISOU 2228  O   LEU A 283     8080   9268   8156    770   -156     54       O  
ATOM   2229  CB  LEU A 283      14.908  34.676 -15.639  1.00 59.32           C  
ANISOU 2229  CB  LEU A 283     7063   8306   7170    767   -220    -55       C  
ATOM   2230  CG  LEU A 283      13.689  35.400 -16.235  1.00 58.71           C  
ANISOU 2230  CG  LEU A 283     6977   8243   7089    808   -238    -74       C  
ATOM   2231  CD1 LEU A 283      13.971  35.895 -17.651  1.00 58.74           C  
ANISOU 2231  CD1 LEU A 283     6994   8284   7041    877   -247    -48       C  
ATOM   2232  CD2 LEU A 283      12.462  34.504 -16.218  1.00 54.02           C  
ANISOU 2232  CD2 LEU A 283     6356   7651   6519    808   -271   -141       C  
ATOM   2233  N   ALA A 284      16.084  36.650 -13.439  1.00 62.72           N  
ANISOU 2233  N   ALA A 284     7515   8674   7643    674   -145     30       N  
ATOM   2234  CA  ALA A 284      15.866  37.787 -12.550  1.00 66.19           C  
ANISOU 2234  CA  ALA A 284     7953   9087   8110    643   -121     46       C  
ATOM   2235  C   ALA A 284      16.880  38.937 -12.737  1.00 70.46           C  
ANISOU 2235  C   ALA A 284     8509   9621   8641    653    -91    102       C  
ATOM   2236  O   ALA A 284      16.658  40.046 -12.248  1.00 71.41           O  
ANISOU 2236  O   ALA A 284     8627   9723   8785    640    -71    116       O  
ATOM   2237  CB  ALA A 284      15.825  37.315 -11.103  1.00 63.42           C  
ANISOU 2237  CB  ALA A 284     7595   8711   7791    577   -111     28       C  
ATOM   2238  N   GLU A 285      17.974  38.677 -13.455  1.00 75.88           N  
ANISOU 2238  N   GLU A 285     9209  10322   9298    678    -85    133       N  
ATOM   2239  CA  GLU A 285      18.977  39.715 -13.752  1.00 82.16           C  
ANISOU 2239  CA  GLU A 285    10018  11111  10087    691    -54    187       C  
ATOM   2240  C   GLU A 285      18.638  40.538 -14.985  1.00 79.30           C  
ANISOU 2240  C   GLU A 285     9662  10768   9700    754    -55    211       C  
ATOM   2241  O   GLU A 285      19.118  41.660 -15.136  1.00 81.40           O  
ANISOU 2241  O   GLU A 285     9934  11022   9972    765    -26    255       O  
ATOM   2242  CB  GLU A 285      20.376  39.113 -13.922  1.00 87.47           C  
ANISOU 2242  CB  GLU A 285    10703  11789  10743    687    -43    212       C  
ATOM   2243  CG  GLU A 285      21.345  39.467 -12.804  1.00 95.51           C  
ANISOU 2243  CG  GLU A 285    11722  12777  11789    635    -15    234       C  
ATOM   2244  CD  GLU A 285      21.138  38.633 -11.552  1.00100.56           C  
ANISOU 2244  CD  GLU A 285    12354  13404  12452    579    -26    200       C  
ATOM   2245  OE1 GLU A 285      21.303  39.179 -10.438  1.00 99.81           O  
ANISOU 2245  OE1 GLU A 285    12255  13285  12384    535     -9    204       O  
ATOM   2246  OE2 GLU A 285      20.817  37.431 -11.680  1.00104.07           O  
ANISOU 2246  OE2 GLU A 285    12794  13861  12886    579    -51    169       O  
ATOM   2247  N   GLN A 286      17.823  39.961 -15.862  1.00 75.58           N  
ANISOU 2247  N   GLN A 286     9187  10327   9202    796    -87    182       N  
ATOM   2248  CA  GLN A 286      17.412  40.607 -17.104  1.00 76.91           C  
ANISOU 2248  CA  GLN A 286     9362  10522   9340    862    -94    201       C  
ATOM   2249  C   GLN A 286      16.286  41.619 -16.870  1.00 75.78           C  
ANISOU 2249  C   GLN A 286     9207  10363   9223    866    -96    195       C  
ATOM   2250  O   GLN A 286      15.362  41.351 -16.096  1.00 71.41           O  
ANISOU 2250  O   GLN A 286     8636   9796   8701    834   -112    151       O  
ATOM   2251  CB  GLN A 286      16.960  39.551 -18.109  1.00 77.24           C  
ANISOU 2251  CB  GLN A 286     9402  10604   9342    906   -132    165       C  
ATOM   2252  CG  GLN A 286      17.868  38.330 -18.178  1.00 81.67           C  
ANISOU 2252  CG  GLN A 286     9967  11176   9888    893   -136    154       C  
ATOM   2253  CD  GLN A 286      19.292  38.664 -18.591  1.00 84.89           C  
ANISOU 2253  CD  GLN A 286    10395  11587  10274    905   -104    209       C  
ATOM   2254  OE1 GLN A 286      20.228  38.491 -17.812  1.00 87.78           O  
ANISOU 2254  OE1 GLN A 286    10763  11928  10661    860    -82    224       O  
ATOM   2255  NE2 GLN A 286      19.461  39.151 -19.815  1.00 90.07           N  
ANISOU 2255  NE2 GLN A 286    11063  12272  10886    966   -100    241       N  
ATOM   2256  N   PRO A 287      16.356  42.783 -17.543  1.00 76.84           N  
ANISOU 2256  N   PRO A 287     9349  10499   9348    907    -80    241       N  
ATOM   2257  CA  PRO A 287      15.333  43.830 -17.393  1.00 78.45           C  
ANISOU 2257  CA  PRO A 287     9540  10686   9580    916    -81    241       C  
ATOM   2258  C   PRO A 287      13.931  43.414 -17.876  1.00 78.27           C  
ANISOU 2258  C   PRO A 287     9504  10688   9548    948   -124    191       C  
ATOM   2259  O   PRO A 287      12.935  44.021 -17.475  1.00 77.02           O  
ANISOU 2259  O   PRO A 287     9330  10512   9423    940   -130    173       O  
ATOM   2260  CB  PRO A 287      15.880  44.988 -18.239  1.00 75.89           C  
ANISOU 2260  CB  PRO A 287     9230  10364   9240    962    -54    308       C  
ATOM   2261  CG  PRO A 287      16.828  44.350 -19.195  1.00 80.22           C  
ANISOU 2261  CG  PRO A 287     9798  10947   9737    997    -53    331       C  
ATOM   2262  CD  PRO A 287      17.440  43.202 -18.451  1.00 78.05           C  
ANISOU 2262  CD  PRO A 287     9521  10666   9467    946    -55    300       C  
ATOM   2263  N   ILE A 288      13.861  42.380 -18.708  1.00 77.52           N  
ANISOU 2263  N   ILE A 288     9413  10632   9410    982   -155    166       N  
ATOM   2264  CA  ILE A 288      12.583  41.905 -19.233  1.00 81.86           C  
ANISOU 2264  CA  ILE A 288     9947  11206   9950   1015   -199    114       C  
ATOM   2265  C   ILE A 288      11.890  40.872 -18.317  1.00 79.96           C  
ANISOU 2265  C   ILE A 288     9685  10952   9745    966   -220     47       C  
ATOM   2266  O   ILE A 288      10.885  40.254 -18.698  1.00 78.98           O  
ANISOU 2266  O   ILE A 288     9544  10846   9618    988   -257     -5       O  
ATOM   2267  CB  ILE A 288      12.730  41.396 -20.693  1.00 86.10           C  
ANISOU 2267  CB  ILE A 288    10495  11796  10423   1085   -225    117       C  
ATOM   2268  CG1 ILE A 288      11.365  41.410 -21.403  1.00 92.07           C  
ANISOU 2268  CG1 ILE A 288    11236  12579  11168   1135   -269     77       C  
ATOM   2269  CG2 ILE A 288      13.417  40.033 -20.742  1.00 81.88           C  
ANISOU 2269  CG2 ILE A 288     9963  11277   9868   1070   -233     90       C  
ATOM   2270  CD1 ILE A 288      11.423  41.641 -22.900  1.00100.34           C  
ANISOU 2270  CD1 ILE A 288    12297  13677  12150   1217   -286    104       C  
ATOM   2271  N   CYS A 289      12.407  40.719 -17.100  1.00 77.85           N  
ANISOU 2271  N   CYS A 289     9417  10650   9512    900   -194     48       N  
ATOM   2272  CA  CYS A 289      11.934  39.694 -16.171  1.00 71.81           C  
ANISOU 2272  CA  CYS A 289     8635   9871   8779    849   -205     -6       C  
ATOM   2273  C   CYS A 289      10.434  39.773 -15.826  1.00 72.91           C  
ANISOU 2273  C   CYS A 289     8749  10000   8953    843   -227    -57       C  
ATOM   2274  O   CYS A 289       9.694  38.791 -16.006  1.00 70.28           O  
ANISOU 2274  O   CYS A 289     8399   9679   8624    849   -258   -111       O  
ATOM   2275  CB  CYS A 289      12.771  39.721 -14.901  1.00 70.32           C  
ANISOU 2275  CB  CYS A 289     8453   9649   8617    782   -171     13       C  
ATOM   2276  SG  CYS A 289      12.419  38.343 -13.789  1.00 70.02           S  
ANISOU 2276  SG  CYS A 289     8399   9596   8611    722   -181    -42       S  
ATOM   2277  N   LYS A 290       9.988  40.928 -15.333  1.00 72.27           N  
ANISOU 2277  N   LYS A 290     8662   9895   8902    831   -209    -43       N  
ATOM   2278  CA  LYS A 290       8.572  41.111 -14.986  1.00 72.07           C  
ANISOU 2278  CA  LYS A 290     8612   9857   8914    825   -227    -90       C  
ATOM   2279  C   LYS A 290       7.625  40.689 -16.121  1.00 74.33           C  
ANISOU 2279  C   LYS A 290     8885  10176   9180    885   -272   -127       C  
ATOM   2280  O   LYS A 290       6.717  39.884 -15.900  1.00 75.40           O  
ANISOU 2280  O   LYS A 290     8999  10311   9340    873   -295   -187       O  
ATOM   2281  CB  LYS A 290       8.287  42.551 -14.551  1.00 70.31           C  
ANISOU 2281  CB  LYS A 290     8384   9607   8722    816   -203    -64       C  
ATOM   2282  CG  LYS A 290       8.766  42.899 -13.150  1.00 69.52           C  
ANISOU 2282  CG  LYS A 290     8285   9471   8658    747   -164    -54       C  
ATOM   2283  CD  LYS A 290       8.502  44.367 -12.840  1.00 67.59           C  
ANISOU 2283  CD  LYS A 290     8035   9202   8446    745   -142    -30       C  
ATOM   2284  CE  LYS A 290       8.841  44.706 -11.399  1.00 67.41           C  
ANISOU 2284  CE  LYS A 290     8007   9145   8460    676   -107    -32       C  
ATOM   2285  NZ  LYS A 290       8.871  46.175 -11.162  1.00 67.69           N  
ANISOU 2285  NZ  LYS A 290     8038   9155   8527    675    -80     -3       N  
ATOM   2286  N   ASP A 291       7.856  41.211 -17.329  1.00 74.39           N  
ANISOU 2286  N   ASP A 291     8907  10214   9146    949   -283    -93       N  
ATOM   2287  CA  ASP A 291       7.008  40.933 -18.500  1.00 75.59           C  
ANISOU 2287  CA  ASP A 291     9048  10403   9271   1014   -328   -125       C  
ATOM   2288  C   ASP A 291       6.904  39.455 -18.830  1.00 74.33           C  
ANISOU 2288  C   ASP A 291     8878  10267   9096   1019   -358   -178       C  
ATOM   2289  O   ASP A 291       5.842  38.954 -19.187  1.00 78.68           O  
ANISOU 2289  O   ASP A 291     9405  10832   9656   1042   -396   -236       O  
ATOM   2290  CB  ASP A 291       7.537  41.664 -19.736  1.00 82.25           C  
ANISOU 2290  CB  ASP A 291     9913  11278  10059   1082   -329    -69       C  
ATOM   2291  CG  ASP A 291       7.428  43.170 -19.616  1.00 90.47           C  
ANISOU 2291  CG  ASP A 291    10959  12297  11119   1091   -305    -19       C  
ATOM   2292  OD1 ASP A 291       8.406  43.861 -19.977  1.00 95.41           O  
ANISOU 2292  OD1 ASP A 291    11608  12925  11720   1108   -276     47       O  
ATOM   2293  OD2 ASP A 291       6.372  43.664 -19.156  1.00 88.38           O  
ANISOU 2293  OD2 ASP A 291    10672  12010  10898   1080   -313    -46       O  
ATOM   2294  N   VAL A 292       8.024  38.764 -18.700  1.00 73.34           N  
ANISOU 2294  N   VAL A 292     8770  10145   8951    997   -342   -160       N  
ATOM   2295  CA  VAL A 292       8.139  37.376 -19.097  1.00 70.12           C  
ANISOU 2295  CA  VAL A 292     8355   9761   8528   1004   -367   -203       C  
ATOM   2296  C   VAL A 292       7.463  36.428 -18.108  1.00 69.66           C  
ANISOU 2296  C   VAL A 292     8270   9674   8524    950   -373   -263       C  
ATOM   2297  O   VAL A 292       7.032  35.335 -18.488  1.00 71.50           O  
ANISOU 2297  O   VAL A 292     8485   9923   8760    963   -404   -317       O  
ATOM   2298  CB  VAL A 292       9.631  37.028 -19.295  1.00 72.66           C  
ANISOU 2298  CB  VAL A 292     8703  10093   8814   1000   -344   -160       C  
ATOM   2299  CG1 VAL A 292       9.908  35.542 -19.088  1.00 70.34           C  
ANISOU 2299  CG1 VAL A 292     8398   9800   8528    974   -355   -202       C  
ATOM   2300  CG2 VAL A 292      10.096  37.512 -20.668  1.00 75.04           C  
ANISOU 2300  CG2 VAL A 292     9023  10436   9051   1072   -352   -122       C  
ATOM   2301  N   LEU A 293       7.357  36.855 -16.853  1.00 68.88           N  
ANISOU 2301  N   LEU A 293     8169   9534   8469    891   -343   -253       N  
ATOM   2302  CA  LEU A 293       6.849  35.989 -15.781  1.00 71.14           C  
ANISOU 2302  CA  LEU A 293     8434   9791   8805    833   -339   -299       C  
ATOM   2303  C   LEU A 293       5.342  36.045 -15.519  1.00 74.05           C  
ANISOU 2303  C   LEU A 293     8770  10146   9218    829   -358   -355       C  
ATOM   2304  O   LEU A 293       4.788  35.139 -14.880  1.00 72.83           O  
ANISOU 2304  O   LEU A 293     8594   9974   9105    793   -361   -402       O  
ATOM   2305  CB  LEU A 293       7.611  36.266 -14.484  1.00 69.61           C  
ANISOU 2305  CB  LEU A 293     8254   9563   8632    767   -296   -262       C  
ATOM   2306  CG  LEU A 293       8.707  35.264 -14.105  1.00 67.59           C  
ANISOU 2306  CG  LEU A 293     8010   9304   8367    734   -283   -249       C  
ATOM   2307  CD1 LEU A 293       9.391  34.705 -15.333  1.00 67.92           C  
ANISOU 2307  CD1 LEU A 293     8063   9382   8363    785   -303   -242       C  
ATOM   2308  CD2 LEU A 293       9.719  35.907 -13.174  1.00 61.68           C  
ANISOU 2308  CD2 LEU A 293     7283   8534   7619    690   -242   -195       C  
ATOM   2309  N   VAL A 294       4.697  37.096 -16.030  1.00 74.85           N  
ANISOU 2309  N   VAL A 294     8868  10255   9315    868   -370   -349       N  
ATOM   2310  CA  VAL A 294       3.292  37.425 -15.748  1.00 73.59           C  
ANISOU 2310  CA  VAL A 294     8680  10081   9202    866   -384   -395       C  
ATOM   2311  C   VAL A 294       2.320  36.239 -15.756  1.00 71.45           C  
ANISOU 2311  C   VAL A 294     8375   9809   8965    861   -413   -472       C  
ATOM   2312  O   VAL A 294       1.396  36.194 -14.961  1.00 73.38           O  
ANISOU 2312  O   VAL A 294     8595  10025   9263    826   -407   -510       O  
ATOM   2313  CB  VAL A 294       2.783  38.541 -16.696  1.00 77.73           C  
ANISOU 2313  CB  VAL A 294     9204  10625   9705    929   -405   -380       C  
ATOM   2314  CG1 VAL A 294       2.584  38.013 -18.116  1.00 78.79           C  
ANISOU 2314  CG1 VAL A 294     9335  10807   9796   1000   -451   -404       C  
ATOM   2315  CG2 VAL A 294       1.508  39.173 -16.153  1.00 79.67           C  
ANISOU 2315  CG2 VAL A 294     9423  10845  10005    915   -407   -414       C  
ATOM   2316  N   ARG A 295       2.533  35.277 -16.639  1.00 69.51           N  
ANISOU 2316  N   ARG A 295     8127   9594   8692    897   -443   -496       N  
ATOM   2317  CA  ARG A 295       1.620  34.154 -16.732  1.00 68.96           C  
ANISOU 2317  CA  ARG A 295     8021   9522   8658    897   -472   -572       C  
ATOM   2318  C   ARG A 295       1.960  33.013 -15.753  1.00 67.13           C  
ANISOU 2318  C   ARG A 295     7782   9261   8462    833   -449   -587       C  
ATOM   2319  O   ARG A 295       1.170  32.077 -15.595  1.00 66.26           O  
ANISOU 2319  O   ARG A 295     7640   9139   8397    821   -464   -648       O  
ATOM   2320  CB  ARG A 295       1.576  33.647 -18.174  1.00 70.12           C  
ANISOU 2320  CB  ARG A 295     8162   9717   8763    968   -519   -600       C  
ATOM   2321  CG  ARG A 295       0.216  33.135 -18.582  1.00 81.91           C  
ANISOU 2321  CG  ARG A 295     9613  11216  10293    993   -561   -681       C  
ATOM   2322  CD  ARG A 295       0.234  32.459 -19.942  1.00 87.61           C  
ANISOU 2322  CD  ARG A 295    10327  11988  10974   1060   -608   -718       C  
ATOM   2323  NE  ARG A 295       0.045  33.409 -21.034  1.00 90.89           N  
ANISOU 2323  NE  ARG A 295    10754  12445  11336   1131   -636   -698       N  
ATOM   2324  CZ  ARG A 295      -0.347  33.080 -22.263  1.00 97.19           C  
ANISOU 2324  CZ  ARG A 295    11538  13290  12100   1200   -685   -740       C  
ATOM   2325  NH1 ARG A 295      -0.606  31.814 -22.580  1.00 95.80           N  
ANISOU 2325  NH1 ARG A 295    11333  13124  11942   1205   -713   -809       N  
ATOM   2326  NH2 ARG A 295      -0.486  34.027 -23.182  1.00100.92           N  
ANISOU 2326  NH2 ARG A 295    12024  13800  12521   1264   -707   -712       N  
ATOM   2327  N   HIS A 296       3.121  33.105 -15.093  1.00 62.98           N  
ANISOU 2327  N   HIS A 296     7287   8724   7920    795   -412   -530       N  
ATOM   2328  CA  HIS A 296       3.708  31.971 -14.359  1.00 57.62           C  
ANISOU 2328  CA  HIS A 296     6608   8025   7261    745   -393   -533       C  
ATOM   2329  C   HIS A 296       4.147  32.282 -12.946  1.00 55.19           C  
ANISOU 2329  C   HIS A 296     6314   7682   6972    677   -347   -495       C  
ATOM   2330  O   HIS A 296       4.260  31.387 -12.101  1.00 55.32           O  
ANISOU 2330  O   HIS A 296     6324   7676   7021    629   -331   -505       O  
ATOM   2331  CB  HIS A 296       4.896  31.411 -15.130  1.00 56.45           C  
ANISOU 2331  CB  HIS A 296     6480   7904   7064    772   -401   -508       C  
ATOM   2332  CG  HIS A 296       4.523  30.635 -16.370  1.00 55.09           C  
ANISOU 2332  CG  HIS A 296     6288   7766   6879    829   -446   -559       C  
ATOM   2333  ND1 HIS A 296       4.527  31.189 -17.601  1.00 54.97           N  
ANISOU 2333  ND1 HIS A 296     6280   7791   6813    896   -473   -554       N  
ATOM   2334  CD2 HIS A 296       4.168  29.297 -16.542  1.00 54.57           C  
ANISOU 2334  CD2 HIS A 296     6193   7697   6844    827   -467   -619       C  
ATOM   2335  CE1 HIS A 296       4.165  30.258 -18.514  1.00 54.29           C  
ANISOU 2335  CE1 HIS A 296     6171   7732   6723    936   -512   -611       C  
ATOM   2336  NE2 HIS A 296       3.947  29.103 -17.866  1.00 54.00           N  
ANISOU 2336  NE2 HIS A 296     6111   7667   6740    893   -508   -652       N  
ATOM   2337  N   LEU A 297       4.408  33.551 -12.675  1.00 50.38           N  
ANISOU 2337  N   LEU A 297     5725   7070   6347    673   -327   -450       N  
ATOM   2338  CA  LEU A 297       4.805  33.984 -11.342  1.00 52.22           C  
ANISOU 2338  CA  LEU A 297     5971   7274   6597    612   -284   -417       C  
ATOM   2339  C   LEU A 297       4.027  33.358 -10.171  1.00 52.75           C  
ANISOU 2339  C   LEU A 297     6016   7310   6718    555   -268   -454       C  
ATOM   2340  O   LEU A 297       4.644  32.906  -9.208  1.00 53.19           O  
ANISOU 2340  O   LEU A 297     6081   7348   6779    506   -241   -433       O  
ATOM   2341  CB  LEU A 297       4.749  35.507 -11.264  1.00 52.72           C  
ANISOU 2341  CB  LEU A 297     6045   7335   6651    620   -270   -384       C  
ATOM   2342  CG  LEU A 297       5.156  36.159  -9.956  1.00 53.40           C  
ANISOU 2342  CG  LEU A 297     6144   7395   6752    562   -228   -352       C  
ATOM   2343  CD1 LEU A 297       6.643  35.959  -9.703  1.00 54.32           C  
ANISOU 2343  CD1 LEU A 297     6289   7515   6836    544   -208   -301       C  
ATOM   2344  CD2 LEU A 297       4.793  37.636 -10.013  1.00 53.65           C  
ANISOU 2344  CD2 LEU A 297     6176   7422   6788    578   -219   -336       C  
ATOM   2345  N   PRO A 298       2.677  33.311 -10.254  1.00 54.42           N  
ANISOU 2345  N   PRO A 298     6196   7513   6970    564   -284   -509       N  
ATOM   2346  CA  PRO A 298       1.915  32.717  -9.151  1.00 52.39           C  
ANISOU 2346  CA  PRO A 298     5916   7224   6766    510   -264   -543       C  
ATOM   2347  C   PRO A 298       2.307  31.282  -8.805  1.00 49.32           C  
ANISOU 2347  C   PRO A 298     5524   6826   6392    482   -259   -552       C  
ATOM   2348  O   PRO A 298       2.264  30.908  -7.643  1.00 47.21           O  
ANISOU 2348  O   PRO A 298     5254   6532   6150    427   -228   -548       O  
ATOM   2349  CB  PRO A 298       0.468  32.775  -9.664  1.00 54.12           C  
ANISOU 2349  CB  PRO A 298     6099   7441   7023    539   -291   -606       C  
ATOM   2350  CG  PRO A 298       0.459  33.972 -10.558  1.00 53.04           C  
ANISOU 2350  CG  PRO A 298     5973   7328   6853    591   -311   -587       C  
ATOM   2351  CD  PRO A 298       1.765  33.840 -11.294  1.00 54.34           C  
ANISOU 2351  CD  PRO A 298     6168   7520   6959    621   -319   -541       C  
ATOM   2352  N   LYS A 299       2.688  30.487  -9.794  1.00 51.47           N  
ANISOU 2352  N   LYS A 299     5793   7117   6646    520   -289   -563       N  
ATOM   2353  CA  LYS A 299       3.147  29.133  -9.522  1.00 53.99           C  
ANISOU 2353  CA  LYS A 299     6107   7425   6980    496   -284   -569       C  
ATOM   2354  C   LYS A 299       4.627  29.103  -9.103  1.00 54.61           C  
ANISOU 2354  C   LYS A 299     6222   7507   7021    473   -262   -505       C  
ATOM   2355  O   LYS A 299       5.023  28.290  -8.252  1.00 52.90           O  
ANISOU 2355  O   LYS A 299     6008   7270   6823    429   -241   -492       O  
ATOM   2356  CB  LYS A 299       2.937  28.239 -10.741  1.00 55.22           C  
ANISOU 2356  CB  LYS A 299     6242   7600   7139    545   -325   -614       C  
ATOM   2357  CG  LYS A 299       3.367  26.793 -10.534  1.00 57.35           C  
ANISOU 2357  CG  LYS A 299     6501   7855   7434    523   -323   -625       C  
ATOM   2358  CD  LYS A 299       2.479  26.064  -9.533  1.00 63.15           C  
ANISOU 2358  CD  LYS A 299     7207   8550   8237    474   -302   -658       C  
ATOM   2359  CE  LYS A 299       2.785  24.570  -9.516  1.00 65.48           C  
ANISOU 2359  CE  LYS A 299     7486   8829   8565    461   -305   -675       C  
ATOM   2360  NZ  LYS A 299       1.646  23.819  -8.932  1.00 71.22           N  
ANISOU 2360  NZ  LYS A 299     8174   9521   9367    431   -294   -725       N  
ATOM   2361  N   LEU A 300       5.427  29.991  -9.693  1.00 52.96           N  
ANISOU 2361  N   LEU A 300     6039   7322   6761    504   -266   -464       N  
ATOM   2362  CA  LEU A 300       6.878  29.993  -9.461  1.00 54.16           C  
ANISOU 2362  CA  LEU A 300     6223   7480   6876    489   -249   -407       C  
ATOM   2363  C   LEU A 300       7.253  30.199  -7.982  1.00 52.85           C  
ANISOU 2363  C   LEU A 300     6071   7289   6721    426   -210   -373       C  
ATOM   2364  O   LEU A 300       8.058  29.449  -7.412  1.00 52.00           O  
ANISOU 2364  O   LEU A 300     5974   7172   6613    395   -197   -350       O  
ATOM   2365  CB  LEU A 300       7.575  31.035 -10.350  1.00 54.87           C  
ANISOU 2365  CB  LEU A 300     6337   7597   6914    534   -256   -369       C  
ATOM   2366  CG  LEU A 300       9.099  31.149 -10.181  1.00 52.81           C  
ANISOU 2366  CG  LEU A 300     6107   7341   6617    523   -238   -311       C  
ATOM   2367  CD1 LEU A 300       9.773  29.854 -10.593  1.00 51.80           C  
ANISOU 2367  CD1 LEU A 300     5977   7219   6484    529   -251   -317       C  
ATOM   2368  CD2 LEU A 300       9.665  32.315 -10.965  1.00 51.62           C  
ANISOU 2368  CD2 LEU A 300     5977   7212   6423    563   -238   -273       C  
ATOM   2369  N   ILE A 301       6.639  31.192  -7.357  1.00 50.16           N  
ANISOU 2369  N   ILE A 301     5729   6939   6392    407   -192   -373       N  
ATOM   2370  CA  ILE A 301       6.957  31.506  -5.972  1.00 48.66           C  
ANISOU 2370  CA  ILE A 301     5551   6730   6206    349   -156   -345       C  
ATOM   2371  C   ILE A 301       6.780  30.307  -5.022  1.00 52.40           C  
ANISOU 2371  C   ILE A 301     6014   7182   6712    303   -141   -357       C  
ATOM   2372  O   ILE A 301       7.707  29.963  -4.288  1.00 51.39           O  
ANISOU 2372  O   ILE A 301     5905   7050   6570    270   -123   -320       O  
ATOM   2373  CB  ILE A 301       6.195  32.759  -5.486  1.00 46.92           C  
ANISOU 2373  CB  ILE A 301     5326   6503   5999    338   -140   -352       C  
ATOM   2374  CG1 ILE A 301       6.423  33.948  -6.437  1.00 47.31           C  
ANISOU 2374  CG1 ILE A 301     5385   6570   6019    386   -153   -334       C  
ATOM   2375  CG2 ILE A 301       6.602  33.117  -4.072  1.00 46.34           C  
ANISOU 2375  CG2 ILE A 301     5266   6416   5925    281   -103   -325       C  
ATOM   2376  CD1 ILE A 301       7.861  34.124  -6.916  1.00 44.12           C  
ANISOU 2376  CD1 ILE A 301     5010   6182   5571    404   -153   -283       C  
ATOM   2377  N   PRO A 302       5.607  29.638  -5.051  1.00 53.22           N  
ANISOU 2377  N   PRO A 302     6088   7273   6860    301   -149   -407       N  
ATOM   2378  CA  PRO A 302       5.423  28.476  -4.177  1.00 50.83           C  
ANISOU 2378  CA  PRO A 302     5775   6948   6593    258   -131   -416       C  
ATOM   2379  C   PRO A 302       6.374  27.351  -4.509  1.00 46.62           C  
ANISOU 2379  C   PRO A 302     5248   6416   6050    264   -143   -398       C  
ATOM   2380  O   PRO A 302       6.777  26.605  -3.619  1.00 47.46           O  
ANISOU 2380  O   PRO A 302     5359   6506   6167    224   -122   -376       O  
ATOM   2381  CB  PRO A 302       3.974  28.032  -4.475  1.00 54.02           C  
ANISOU 2381  CB  PRO A 302     6140   7337   7049    268   -143   -479       C  
ATOM   2382  CG  PRO A 302       3.299  29.277  -4.929  1.00 53.46           C  
ANISOU 2382  CG  PRO A 302     6064   7277   6970    296   -153   -497       C  
ATOM   2383  CD  PRO A 302       4.353  29.993  -5.735  1.00 54.35           C  
ANISOU 2383  CD  PRO A 302     6204   7418   7028    333   -169   -458       C  
ATOM   2384  N   VAL A 303       6.710  27.220  -5.784  1.00 45.12           N  
ANISOU 2384  N   VAL A 303     5057   6246   5841    315   -175   -407       N  
ATOM   2385  CA  VAL A 303       7.648  26.209  -6.224  1.00 44.14           C  
ANISOU 2385  CA  VAL A 303     4937   6125   5708    326   -188   -394       C  
ATOM   2386  C   VAL A 303       9.050  26.484  -5.666  1.00 47.40           C  
ANISOU 2386  C   VAL A 303     5384   6543   6082    304   -170   -331       C  
ATOM   2387  O   VAL A 303       9.696  25.570  -5.132  1.00 46.34           O  
ANISOU 2387  O   VAL A 303     5255   6397   5957    277   -161   -310       O  
ATOM   2388  CB  VAL A 303       7.679  26.116  -7.764  1.00 46.73           C  
ANISOU 2388  CB  VAL A 303     5257   6479   6019    388   -226   -421       C  
ATOM   2389  CG1 VAL A 303       8.934  25.383  -8.227  1.00 44.31           C  
ANISOU 2389  CG1 VAL A 303     4964   6183   5690    401   -235   -395       C  
ATOM   2390  CG2 VAL A 303       6.428  25.386  -8.249  1.00 47.08           C  
ANISOU 2390  CG2 VAL A 303     5262   6515   6112    406   -247   -489       C  
ATOM   2391  N   LEU A 304       9.502  27.738  -5.773  1.00 45.57           N  
ANISOU 2391  N   LEU A 304     5175   6329   5812    315   -164   -301       N  
ATOM   2392  CA  LEU A 304      10.768  28.157  -5.164  1.00 46.34           C  
ANISOU 2392  CA  LEU A 304     5302   6430   5876    292   -146   -246       C  
ATOM   2393  C   LEU A 304      10.740  27.928  -3.671  1.00 46.52           C  
ANISOU 2393  C   LEU A 304     5329   6433   5915    234   -116   -229       C  
ATOM   2394  O   LEU A 304      11.640  27.308  -3.112  1.00 46.58           O  
ANISOU 2394  O   LEU A 304     5349   6435   5916    209   -108   -197       O  
ATOM   2395  CB  LEU A 304      11.051  29.635  -5.427  1.00 44.97           C  
ANISOU 2395  CB  LEU A 304     5145   6272   5669    311   -141   -223       C  
ATOM   2396  CG  LEU A 304      11.325  30.029  -6.876  1.00 45.86           C  
ANISOU 2396  CG  LEU A 304     5262   6409   5755    370   -165   -224       C  
ATOM   2397  CD1 LEU A 304      11.858  31.452  -6.929  1.00 45.78           C  
ANISOU 2397  CD1 LEU A 304     5272   6408   5715    380   -151   -187       C  
ATOM   2398  CD2 LEU A 304      12.301  29.059  -7.523  1.00 43.52           C  
ANISOU 2398  CD2 LEU A 304     4972   6122   5444    389   -179   -212       C  
ATOM   2399  N   VAL A 305       9.687  28.413  -3.031  1.00 45.81           N  
ANISOU 2399  N   VAL A 305     5227   6332   5845    212   -101   -251       N  
ATOM   2400  CA  VAL A 305       9.533  28.267  -1.593  1.00 45.63           C  
ANISOU 2400  CA  VAL A 305     5207   6294   5834    157    -70   -239       C  
ATOM   2401  C   VAL A 305       9.616  26.794  -1.153  1.00 48.20           C  
ANISOU 2401  C   VAL A 305     5524   6602   6186    133    -67   -236       C  
ATOM   2402  O   VAL A 305      10.173  26.474  -0.106  1.00 46.83           O  
ANISOU 2402  O   VAL A 305     5364   6423   6004     95    -47   -203       O  
ATOM   2403  CB  VAL A 305       8.210  28.905  -1.126  1.00 43.50           C  
ANISOU 2403  CB  VAL A 305     4922   6017   5590    142    -55   -273       C  
ATOM   2404  CG1 VAL A 305       7.866  28.452   0.283  1.00 45.33           C  
ANISOU 2404  CG1 VAL A 305     5151   6232   5840     87    -23   -268       C  
ATOM   2405  CG2 VAL A 305       8.314  30.419  -1.187  1.00 40.71           C  
ANISOU 2405  CG2 VAL A 305     4580   5677   5212    152    -50   -264       C  
ATOM   2406  N   ASN A 306       9.080  25.891  -1.964  1.00 49.20           N  
ANISOU 2406  N   ASN A 306     5627   6721   6345    158    -87   -272       N  
ATOM   2407  CA  ASN A 306       9.012  24.493  -1.556  1.00 49.54           C  
ANISOU 2407  CA  ASN A 306     5656   6741   6425    136    -81   -275       C  
ATOM   2408  C   ASN A 306      10.393  23.834  -1.664  1.00 50.16           C  
ANISOU 2408  C   ASN A 306     5752   6824   6483    139    -90   -234       C  
ATOM   2409  O   ASN A 306      10.787  23.067  -0.788  1.00 50.90           O  
ANISOU 2409  O   ASN A 306     5851   6902   6587    105    -74   -206       O  
ATOM   2410  CB  ASN A 306       7.928  23.749  -2.359  1.00 50.72           C  
ANISOU 2410  CB  ASN A 306     5769   6877   6623    161   -100   -333       C  
ATOM   2411  CG  ASN A 306       7.987  22.245  -2.174  1.00 55.13           C  
ANISOU 2411  CG  ASN A 306     6311   7411   7226    146    -98   -337       C  
ATOM   2412  OD1 ASN A 306       7.650  21.711  -1.110  1.00 58.25           O  
ANISOU 2412  OD1 ASN A 306     6700   7783   7650    104    -69   -326       O  
ATOM   2413  ND2 ASN A 306       8.439  21.549  -3.210  1.00 54.21           N  
ANISOU 2413  ND2 ASN A 306     6184   7299   7114    181   -126   -351       N  
ATOM   2414  N   GLY A 307      11.132  24.165  -2.724  1.00 49.68           N  
ANISOU 2414  N   GLY A 307     5701   6783   6391    179   -114   -229       N  
ATOM   2415  CA  GLY A 307      12.518  23.721  -2.890  1.00 51.02           C  
ANISOU 2415  CA  GLY A 307     5888   6959   6539    184   -121   -190       C  
ATOM   2416  C   GLY A 307      13.534  24.273  -1.881  1.00 53.11           C  
ANISOU 2416  C   GLY A 307     6182   7229   6768    152   -102   -136       C  
ATOM   2417  O   GLY A 307      14.682  23.850  -1.875  1.00 55.64           O  
ANISOU 2417  O   GLY A 307     6515   7551   7074    151   -107   -103       O  
ATOM   2418  N   MET A 308      13.113  25.195  -1.017  1.00 50.38           N  
ANISOU 2418  N   MET A 308     5845   6886   6411    125    -80   -130       N  
ATOM   2419  CA  MET A 308      14.001  25.817  -0.042  1.00 46.49           C  
ANISOU 2419  CA  MET A 308     5378   6402   5886     96    -63    -85       C  
ATOM   2420  C   MET A 308      14.053  25.050   1.265  1.00 48.18           C  
ANISOU 2420  C   MET A 308     5594   6601   6109     50    -43    -63       C  
ATOM   2421  O   MET A 308      14.813  25.409   2.170  1.00 48.78           O  
ANISOU 2421  O   MET A 308     5691   6686   6158     24    -30    -26       O  
ATOM   2422  CB  MET A 308      13.587  27.268   0.210  1.00 44.86           C  
ANISOU 2422  CB  MET A 308     5178   6207   5660     92    -50    -92       C  
ATOM   2423  CG  MET A 308      13.901  28.180  -0.962  1.00 43.53           C  
ANISOU 2423  CG  MET A 308     5015   6055   5472    137    -66    -96       C  
ATOM   2424  SD  MET A 308      13.148  29.815  -0.892  1.00 45.64           S  
ANISOU 2424  SD  MET A 308     5281   6329   5731    141    -54   -112       S  
ATOM   2425  CE  MET A 308      13.798  30.504   0.628  1.00 42.75           C  
ANISOU 2425  CE  MET A 308     4933   5965   5344     91    -26    -79       C  
ATOM   2426  N   LYS A 309      13.248  23.999   1.373  1.00 48.05           N  
ANISOU 2426  N   LYS A 309     5557   6564   6135     40    -39    -83       N  
ATOM   2427  CA  LYS A 309      13.363  23.088   2.500  1.00 51.18           C  
ANISOU 2427  CA  LYS A 309     5957   6945   6545      1    -21    -56       C  
ATOM   2428  C   LYS A 309      14.645  22.290   2.347  1.00 51.70           C  
ANISOU 2428  C   LYS A 309     6032   7008   6603      7    -36    -19       C  
ATOM   2429  O   LYS A 309      15.049  21.970   1.228  1.00 50.91           O  
ANISOU 2429  O   LYS A 309     5924   6909   6510     42    -60    -32       O  
ATOM   2430  CB  LYS A 309      12.197  22.103   2.524  1.00 53.96           C  
ANISOU 2430  CB  LYS A 309     6280   7270   6952     -7    -13    -88       C  
ATOM   2431  CG  LYS A 309      10.867  22.693   2.964  1.00 58.02           C  
ANISOU 2431  CG  LYS A 309     6783   7782   7482    -23      9   -121       C  
ATOM   2432  CD  LYS A 309       9.789  21.624   3.095  1.00 58.89           C  
ANISOU 2432  CD  LYS A 309     6863   7862   7652    -35     21   -149       C  
ATOM   2433  CE  LYS A 309       9.197  21.269   1.747  1.00 64.06           C  
ANISOU 2433  CE  LYS A 309     7489   8508   8345      6     -7   -201       C  
ATOM   2434  NZ  LYS A 309       8.152  20.214   1.869  1.00 73.19           N  
ANISOU 2434  NZ  LYS A 309     8611   9630   9567     -6      5   -233       N  
ATOM   2435  N   TYR A 310      15.284  21.954   3.462  1.00 50.55           N  
ANISOU 2435  N   TYR A 310     5901   6861   6443    -26    -22     24       N  
ATOM   2436  CA  TYR A 310      16.394  21.011   3.411  1.00 50.95           C  
ANISOU 2436  CA  TYR A 310     5958   6905   6498    -23    -35     58       C  
ATOM   2437  C   TYR A 310      15.921  19.717   2.760  1.00 51.15           C  
ANISOU 2437  C   TYR A 310     5955   6902   6578     -9    -45     35       C  
ATOM   2438  O   TYR A 310      14.796  19.284   2.986  1.00 53.95           O  
ANISOU 2438  O   TYR A 310     6291   7238   6970    -21    -30     10       O  
ATOM   2439  CB  TYR A 310      16.874  20.691   4.813  1.00 47.98           C  
ANISOU 2439  CB  TYR A 310     5597   6527   6104    -62    -18    106       C  
ATOM   2440  CG  TYR A 310      17.727  21.753   5.465  1.00 46.88           C  
ANISOU 2440  CG  TYR A 310     5485   6416   5912    -74    -15    134       C  
ATOM   2441  CD1 TYR A 310      18.965  22.127   4.922  1.00 46.85           C  
ANISOU 2441  CD1 TYR A 310     5493   6424   5883    -53    -36    151       C  
ATOM   2442  CD2 TYR A 310      17.318  22.355   6.650  1.00 44.97           C  
ANISOU 2442  CD2 TYR A 310     5256   6187   5645   -107      9    143       C  
ATOM   2443  CE1 TYR A 310      19.758  23.091   5.536  1.00 44.62           C  
ANISOU 2443  CE1 TYR A 310     5231   6165   5558    -65    -34    173       C  
ATOM   2444  CE2 TYR A 310      18.091  23.312   7.268  1.00 46.88           C  
ANISOU 2444  CE2 TYR A 310     5518   6454   5841   -118     10    164       C  
ATOM   2445  CZ  TYR A 310      19.321  23.668   6.709  1.00 46.69           C  
ANISOU 2445  CZ  TYR A 310     5503   6440   5797    -97    -12    178       C  
ATOM   2446  OH  TYR A 310      20.085  24.610   7.338  1.00 45.49           O  
ANISOU 2446  OH  TYR A 310     5368   6311   5605   -109    -10    195       O  
ATOM   2447  N   SER A 311      16.772  19.091   1.961  1.00 54.52           N  
ANISOU 2447  N   SER A 311     6378   7324   7014     16    -67     40       N  
ATOM   2448  CA  SER A 311      16.449  17.783   1.392  1.00 54.40           C  
ANISOU 2448  CA  SER A 311     6334   7281   7054     28    -77     18       C  
ATOM   2449  C   SER A 311      16.482  16.767   2.513  1.00 55.80           C  
ANISOU 2449  C   SER A 311     6510   7433   7260     -8    -58     55       C  
ATOM   2450  O   SER A 311      17.068  17.020   3.582  1.00 54.64           O  
ANISOU 2450  O   SER A 311     6386   7295   7079    -36    -45    102       O  
ATOM   2451  CB  SER A 311      17.445  17.394   0.287  1.00 59.10           C  
ANISOU 2451  CB  SER A 311     6926   7881   7650     63   -105     15       C  
ATOM   2452  OG  SER A 311      18.752  17.131   0.804  1.00 59.48           O  
ANISOU 2452  OG  SER A 311     6992   7929   7678     51   -107     66       O  
ATOM   2453  N   ASP A 312      15.859  15.621   2.269  1.00 56.84           N  
ANISOU 2453  N   ASP A 312     6611   7533   7453     -7    -56     33       N  
ATOM   2454  CA  ASP A 312      15.819  14.551   3.252  1.00 63.32           C  
ANISOU 2454  CA  ASP A 312     7426   8323   8309    -39    -36     68       C  
ATOM   2455  C   ASP A 312      17.201  14.035   3.693  1.00 63.92           C  
ANISOU 2455  C   ASP A 312     7519   8398   8370    -46    -44    126       C  
ATOM   2456  O   ASP A 312      17.417  13.784   4.891  1.00 63.09           O  
ANISOU 2456  O   ASP A 312     7428   8287   8254    -78    -25    176       O  
ATOM   2457  CB  ASP A 312      14.931  13.414   2.748  1.00 71.33           C  
ANISOU 2457  CB  ASP A 312     8399   9300   9402    -32    -34     29       C  
ATOM   2458  CG  ASP A 312      13.465  13.814   2.677  1.00 76.30           C  
ANISOU 2458  CG  ASP A 312     9011   9926  10053    -36    -19    -21       C  
ATOM   2459  OD1 ASP A 312      12.961  14.431   3.647  1.00 78.58           O  
ANISOU 2459  OD1 ASP A 312     9315  10223  10317    -64      8     -4       O  
ATOM   2460  OD2 ASP A 312      12.820  13.518   1.649  1.00 83.22           O  
ANISOU 2460  OD2 ASP A 312     9857  10792  10971     -9    -35    -78       O  
ATOM   2461  N   ILE A 313      18.129  13.907   2.741  1.00 60.40           N  
ANISOU 2461  N   ILE A 313     7071   7958   7920    -16    -72    119       N  
ATOM   2462  CA  ILE A 313      19.500  13.464   3.051  1.00 59.07           C  
ANISOU 2462  CA  ILE A 313     6917   7788   7739    -19    -84    170       C  
ATOM   2463  C   ILE A 313      20.273  14.496   3.887  1.00 58.27           C  
ANISOU 2463  C   ILE A 313     6852   7718   7569    -35    -80    212       C  
ATOM   2464  O   ILE A 313      20.938  14.146   4.870  1.00 57.87           O  
ANISOU 2464  O   ILE A 313     6816   7665   7507    -58    -75    264       O  
ATOM   2465  CB  ILE A 313      20.307  13.052   1.784  1.00 58.41           C  
ANISOU 2465  CB  ILE A 313     6820   7703   7672     18   -113    148       C  
ATOM   2466  CG1 ILE A 313      21.707  12.586   2.171  1.00 56.54           C  
ANISOU 2466  CG1 ILE A 313     6595   7461   7426     13   -124    200       C  
ATOM   2467  CG2 ILE A 313      20.434  14.193   0.782  1.00 55.50           C  
ANISOU 2467  CG2 ILE A 313     6460   7367   7259     49   -128    114       C  
ATOM   2468  CD1 ILE A 313      21.721  11.348   3.037  1.00 59.89           C  
ANISOU 2468  CD1 ILE A 313     7008   7849   7897    -12   -112    238       C  
ATOM   2469  N   ASP A 314      20.163  15.763   3.503  1.00 56.75           N  
ANISOU 2469  N   ASP A 314     6673   7557   7334    -23    -83    189       N  
ATOM   2470  CA  ASP A 314      20.824  16.828   4.233  1.00 56.20           C  
ANISOU 2470  CA  ASP A 314     6633   7516   7204    -37    -79    220       C  
ATOM   2471  C   ASP A 314      20.362  16.922   5.669  1.00 58.32           C  
ANISOU 2471  C   ASP A 314     6915   7788   7457    -76    -54    250       C  
ATOM   2472  O   ASP A 314      21.184  17.130   6.560  1.00 60.07           O  
ANISOU 2472  O   ASP A 314     7157   8023   7642    -94    -53    293       O  
ATOM   2473  CB  ASP A 314      20.670  18.158   3.513  1.00 55.25           C  
ANISOU 2473  CB  ASP A 314     6520   7422   7049    -16    -85    188       C  
ATOM   2474  CG  ASP A 314      21.599  18.266   2.327  1.00 59.26           C  
ANISOU 2474  CG  ASP A 314     7026   7938   7552     20   -109    178       C  
ATOM   2475  OD1 ASP A 314      22.506  17.417   2.202  1.00 63.14           O  
ANISOU 2475  OD1 ASP A 314     7514   8416   8060     25   -122    200       O  
ATOM   2476  OD2 ASP A 314      21.431  19.184   1.509  1.00 64.94           O  
ANISOU 2476  OD2 ASP A 314     7747   8675   8251     45   -114    150       O  
ATOM   2477  N   ILE A 315      19.058  16.754   5.892  1.00 59.11           N  
ANISOU 2477  N   ILE A 315     7001   7875   7583    -89    -32    226       N  
ATOM   2478  CA  ILE A 315      18.507  16.681   7.239  1.00 59.94           C  
ANISOU 2478  CA  ILE A 315     7116   7980   7678   -126     -3    253       C  
ATOM   2479  C   ILE A 315      19.251  15.622   8.049  1.00 61.24           C  
ANISOU 2479  C   ILE A 315     7286   8130   7852   -143     -2    310       C  
ATOM   2480  O   ILE A 315      19.663  15.873   9.181  1.00 61.31           O  
ANISOU 2480  O   ILE A 315     7319   8158   7819   -166      8    351       O  
ATOM   2481  CB  ILE A 315      16.997  16.356   7.206  1.00 62.33           C  
ANISOU 2481  CB  ILE A 315     7396   8262   8027   -135     20    216       C  
ATOM   2482  CG1 ILE A 315      16.182  17.611   6.856  1.00 61.20           C  
ANISOU 2482  CG1 ILE A 315     7253   8139   7863   -128     25    170       C  
ATOM   2483  CG2 ILE A 315      16.530  15.783   8.541  1.00 62.16           C  
ANISOU 2483  CG2 ILE A 315     7378   8229   8011   -172     53    253       C  
ATOM   2484  CD1 ILE A 315      14.857  17.310   6.176  1.00 63.96           C  
ANISOU 2484  CD1 ILE A 315     7571   8466   8265   -118     32    116       C  
ATOM   2485  N   ILE A 316      19.426  14.443   7.455  1.00 65.45           N  
ANISOU 2485  N   ILE A 316     7798   8631   8439   -129    -13    310       N  
ATOM   2486  CA  ILE A 316      20.086  13.330   8.133  1.00 69.86           C  
ANISOU 2486  CA  ILE A 316     8358   9169   9017   -142    -12    364       C  
ATOM   2487  C   ILE A 316      21.568  13.622   8.345  1.00 68.82           C  
ANISOU 2487  C   ILE A 316     8249   9059   8841   -137    -36    403       C  
ATOM   2488  O   ILE A 316      22.091  13.426   9.440  1.00 69.76           O  
ANISOU 2488  O   ILE A 316     8386   9186   8934   -157    -31    455       O  
ATOM   2489  CB  ILE A 316      19.891  11.990   7.388  1.00 70.59           C  
ANISOU 2489  CB  ILE A 316     8417   9217   9187   -128    -18    350       C  
ATOM   2490  CG1 ILE A 316      18.398  11.667   7.259  1.00 69.45           C  
ANISOU 2490  CG1 ILE A 316     8247   9048   9093   -135      6    311       C  
ATOM   2491  CG2 ILE A 316      20.594  10.872   8.143  1.00 72.75           C  
ANISOU 2491  CG2 ILE A 316     8691   9467   9482   -142    -17    411       C  
ATOM   2492  CD1 ILE A 316      18.052  10.668   6.173  1.00 71.62           C  
ANISOU 2492  CD1 ILE A 316     8482   9285   9444   -113     -5    269       C  
ATOM   2493  N   LEU A 317      22.229  14.114   7.303  1.00 70.17           N  
ANISOU 2493  N   LEU A 317     8418   9241   9001   -108    -62    376       N  
ATOM   2494  CA  LEU A 317      23.640  14.473   7.399  1.00 72.74           C  
ANISOU 2494  CA  LEU A 317     8762   9587   9290   -101    -84    406       C  
ATOM   2495  C   LEU A 317      23.889  15.525   8.472  1.00 74.82           C  
ANISOU 2495  C   LEU A 317     9054   9886   9488   -123    -75    430       C  
ATOM   2496  O   LEU A 317      24.793  15.363   9.294  1.00 78.32           O  
ANISOU 2496  O   LEU A 317     9512  10338   9906   -134    -83    475       O  
ATOM   2497  CB  LEU A 317      24.183  14.961   6.053  1.00 70.96           C  
ANISOU 2497  CB  LEU A 317     8530   9369   9064    -67   -106    370       C  
ATOM   2498  CG  LEU A 317      24.242  13.958   4.900  1.00 71.16           C  
ANISOU 2498  CG  LEU A 317     8527   9364   9145    -41   -121    345       C  
ATOM   2499  CD1 LEU A 317      24.655  14.657   3.622  1.00 71.07           C  
ANISOU 2499  CD1 LEU A 317     8514   9370   9120     -7   -138    307       C  
ATOM   2500  CD2 LEU A 317      25.190  12.811   5.200  1.00 71.23           C  
ANISOU 2500  CD2 LEU A 317     8531   9350   9184    -44   -133    386       C  
ATOM   2501  N   LEU A 318      23.081  16.588   8.470  1.00 72.68           N  
ANISOU 2501  N   LEU A 318     8788   9634   9191   -127    -61    396       N  
ATOM   2502  CA  LEU A 318      23.299  17.730   9.370  1.00 75.93           C  
ANISOU 2502  CA  LEU A 318     9223  10082   9543   -145    -53    407       C  
ATOM   2503  C   LEU A 318      23.014  17.409  10.842  1.00 81.19           C  
ANISOU 2503  C   LEU A 318     9904  10757  10188   -179    -33    447       C  
ATOM   2504  O   LEU A 318      23.443  18.144  11.729  1.00 78.11           O  
ANISOU 2504  O   LEU A 318     9534  10398   9746   -194    -31    464       O  
ATOM   2505  CB  LEU A 318      22.496  18.963   8.928  1.00 69.90           C  
ANISOU 2505  CB  LEU A 318     8459   9335   8764   -140    -43    359       C  
ATOM   2506  CG  LEU A 318      22.888  19.642   7.613  1.00 67.83           C  
ANISOU 2506  CG  LEU A 318     8191   9077   8504   -107    -61    326       C  
ATOM   2507  CD1 LEU A 318      21.730  20.453   7.058  1.00 63.44           C  
ANISOU 2507  CD1 LEU A 318     7627   8525   7952    -99    -49    278       C  
ATOM   2508  CD2 LEU A 318      24.120  20.512   7.769  1.00 64.64           C  
ANISOU 2508  CD2 LEU A 318     7804   8697   8059   -103    -75    343       C  
ATOM   2509  N   LYS A 319      22.289  16.317  11.088  1.00 87.73           N  
ANISOU 2509  N   LYS A 319    10719  11557  11056   -189    -16    460       N  
ATOM   2510  CA  LYS A 319      22.088  15.802  12.443  1.00 93.91           C  
ANISOU 2510  CA  LYS A 319    11514  12343  11823   -218      5    506       C  
ATOM   2511  C   LYS A 319      23.390  15.207  13.002  1.00100.77           C  
ANISOU 2511  C   LYS A 319    12396  13216  12675   -218    -16    563       C  
ATOM   2512  O   LYS A 319      23.685  15.354  14.191  1.00101.49           O  
ANISOU 2512  O   LYS A 319    12508  13333  12719   -238    -10    602       O  
ATOM   2513  CB  LYS A 319      20.963  14.761  12.468  1.00 92.82           C  
ANISOU 2513  CB  LYS A 319    11356  12168  11742   -228     32    506       C  
ATOM   2514  CG  LYS A 319      20.559  14.345  13.872  1.00 96.97           C  
ANISOU 2514  CG  LYS A 319    11896  12700  12249   -259     62    552       C  
ATOM   2515  CD  LYS A 319      19.217  13.633  13.906  1.00 99.95           C  
ANISOU 2515  CD  LYS A 319    12252  13044  12681   -271     97    540       C  
ATOM   2516  CE  LYS A 319      18.841  13.292  15.342  1.00 98.43           C  
ANISOU 2516  CE  LYS A 319    12075  12860  12463   -302    131    590       C  
ATOM   2517  NZ  LYS A 319      17.472  12.724  15.434  1.00 94.66           N  
ANISOU 2517  NZ  LYS A 319    11577  12350  12038   -316    171    576       N  
ATOM   2518  N   GLY A 320      24.159  14.551  12.130  1.00110.20           N  
ANISOU 2518  N   GLY A 320    13576  14386  13908   -195    -42    566       N  
ATOM   2519  CA  GLY A 320      25.414  13.889  12.502  1.00108.77           C  
ANISOU 2519  CA  GLY A 320    13402  14203  13723   -191    -65    616       C  
ATOM   2520  C   GLY A 320      26.652  14.550  11.922  1.00108.41           C  
ANISOU 2520  C   GLY A 320    13361  14174  13655   -171    -98    606       C  
ATOM   2521  O   GLY A 320      27.115  15.578  12.422  1.00102.50           O  
ANISOU 2521  O   GLY A 320    12632  13462  12852   -177   -103    606       O  
ATOM   2522  N   SER A 371      29.554  22.734   2.839  1.00104.99           N  
ANISOU 2522  N   SER A 371    12909  13824  13157     41   -151    328       N  
ATOM   2523  CA  SER A 371      28.283  22.503   2.160  1.00 99.93           C  
ANISOU 2523  CA  SER A 371    12260  13178  12532     54   -145    296       C  
ATOM   2524  C   SER A 371      28.225  23.296   0.849  1.00 94.54           C  
ANISOU 2524  C   SER A 371    11574  12503  11844     90   -142    270       C  
ATOM   2525  O   SER A 371      28.540  24.490   0.815  1.00 94.85           O  
ANISOU 2525  O   SER A 371    11622  12555  11861     93   -133    272       O  
ATOM   2526  CB  SER A 371      27.110  22.863   3.079  1.00 98.23           C  
ANISOU 2526  CB  SER A 371    12049  12968  12305     27   -129    287       C  
ATOM   2527  OG  SER A 371      25.913  22.234   2.647  1.00 96.10           O  
ANISOU 2527  OG  SER A 371    11767  12687  12061     34   -125    261       O  
ATOM   2528  N   ASP A 372      27.823  22.626  -0.227  1.00 85.85           N  
ANISOU 2528  N   ASP A 372    10461  11395  10763    118   -149    247       N  
ATOM   2529  CA  ASP A 372      27.851  23.241  -1.552  1.00 81.87           C  
ANISOU 2529  CA  ASP A 372     9954  10902  10251    156   -149    226       C  
ATOM   2530  C   ASP A 372      26.475  23.468  -2.220  1.00 73.69           C  
ANISOU 2530  C   ASP A 372     8911   9872   9217    175   -145    189       C  
ATOM   2531  O   ASP A 372      25.426  23.243  -1.611  1.00 70.69           O  
ANISOU 2531  O   ASP A 372     8527   9486   8847    155   -141    176       O  
ATOM   2532  CB  ASP A 372      28.815  22.479  -2.476  1.00 92.80           C  
ANISOU 2532  CB  ASP A 372    11330  12280  11648    183   -162    229       C  
ATOM   2533  CG  ASP A 372      28.520  20.984  -2.549  1.00100.99           C  
ANISOU 2533  CG  ASP A 372    12352  13300  12721    181   -175    219       C  
ATOM   2534  OD1 ASP A 372      27.355  20.567  -2.336  1.00 97.68           O  
ANISOU 2534  OD1 ASP A 372    11924  12874  12317    172   -174    198       O  
ATOM   2535  OD2 ASP A 372      29.473  20.224  -2.832  1.00100.41           O  
ANISOU 2535  OD2 ASP A 372    12271  13217  12664    189   -186    230       O  
ATOM   2536  N   TRP A 373      26.512  23.909  -3.476  1.00 60.43           N  
ANISOU 2536  N   TRP A 373     7229   8204   7526    214   -148    172       N  
ATOM   2537  CA  TRP A 373      25.348  24.367  -4.212  1.00 57.61           C  
ANISOU 2537  CA  TRP A 373     6867   7857   7165    238   -146    138       C  
ATOM   2538  C   TRP A 373      24.315  23.289  -4.396  1.00 56.07           C  
ANISOU 2538  C   TRP A 373     6653   7652   6998    240   -157    105       C  
ATOM   2539  O   TRP A 373      24.634  22.188  -4.844  1.00 57.76           O  
ANISOU 2539  O   TRP A 373     6855   7858   7233    251   -170     97       O  
ATOM   2540  CB  TRP A 373      25.801  24.909  -5.562  1.00 56.07           C  
ANISOU 2540  CB  TRP A 373     6675   7680   6951    284   -148    134       C  
ATOM   2541  CG  TRP A 373      24.846  25.885  -6.206  1.00 54.77           C  
ANISOU 2541  CG  TRP A 373     6511   7530   6768    309   -143    113       C  
ATOM   2542  CD1 TRP A 373      24.186  25.750  -7.428  1.00 53.84           C  
ANISOU 2542  CD1 TRP A 373     6384   7427   6646    351   -155     81       C  
ATOM   2543  CD2 TRP A 373      24.419  27.195  -5.685  1.00 54.15           C  
ANISOU 2543  CD2 TRP A 373     6443   7456   6677    296   -127    120       C  
ATOM   2544  NE1 TRP A 373      23.406  26.853  -7.686  1.00 54.86           N  
ANISOU 2544  NE1 TRP A 373     6517   7567   6759    366   -147     72       N  
ATOM   2545  CE2 TRP A 373      23.494  27.752  -6.681  1.00 53.58           C  
ANISOU 2545  CE2 TRP A 373     6366   7397   6594    334   -130     95       C  
ATOM   2546  CE3 TRP A 373      24.695  27.932  -4.534  1.00 54.87           C  
ANISOU 2546  CE3 TRP A 373     6543   7540   6765    260   -111    143       C  
ATOM   2547  CZ2 TRP A 373      22.894  28.991  -6.514  1.00 54.34           C  
ANISOU 2547  CZ2 TRP A 373     6468   7499   6681    333   -117     95       C  
ATOM   2548  CZ3 TRP A 373      24.071  29.178  -4.374  1.00 56.01           C  
ANISOU 2548  CZ3 TRP A 373     6692   7690   6901    259    -98    139       C  
ATOM   2549  CH2 TRP A 373      23.196  29.692  -5.341  1.00 53.83           C  
ANISOU 2549  CH2 TRP A 373     6411   7425   6619    295   -100    117       C  
ATOM   2550  N   ASN A 374      23.069  23.591  -4.034  1.00 49.19           N  
ANISOU 2550  N   ASN A 374     5778   6781   6133    229   -151     83       N  
ATOM   2551  CA  ASN A 374      21.958  22.635  -4.170  1.00 47.09           C  
ANISOU 2551  CA  ASN A 374     5491   6503   5900    230   -159     47       C  
ATOM   2552  C   ASN A 374      20.638  23.338  -4.506  1.00 46.82           C  
ANISOU 2552  C   ASN A 374     5450   6477   5862    243   -157     12       C  
ATOM   2553  O   ASN A 374      20.603  24.559  -4.643  1.00 46.80           O  
ANISOU 2553  O   ASN A 374     5460   6489   5832    253   -149     19       O  
ATOM   2554  CB  ASN A 374      21.827  21.758  -2.912  1.00 44.53           C  
ANISOU 2554  CB  ASN A 374     5163   6155   5602    186   -152     63       C  
ATOM   2555  CG  ASN A 374      21.695  22.574  -1.637  1.00 44.88           C  
ANISOU 2555  CG  ASN A 374     5223   6201   5627    148   -133     88       C  
ATOM   2556  OD1 ASN A 374      21.332  23.746  -1.671  1.00 50.76           O  
ANISOU 2556  OD1 ASN A 374     5977   6961   6351    152   -124     81       O  
ATOM   2557  ND2 ASN A 374      21.973  21.957  -0.510  1.00 42.08           N  
ANISOU 2557  ND2 ASN A 374     4873   5834   5283    112   -126    115       N  
ATOM   2558  N   LEU A 375      19.564  22.566  -4.671  1.00 48.71           N  
ANISOU 2558  N   LEU A 375     5668   6706   6135    245   -164    -25       N  
ATOM   2559  CA  LEU A 375      18.248  23.126  -4.978  1.00 46.83           C  
ANISOU 2559  CA  LEU A 375     5420   6474   5900    258   -165    -63       C  
ATOM   2560  C   LEU A 375      17.839  24.197  -3.955  1.00 44.78           C  
ANISOU 2560  C   LEU A 375     5174   6215   5627    227   -143    -47       C  
ATOM   2561  O   LEU A 375      17.438  25.295  -4.337  1.00 42.98           O  
ANISOU 2561  O   LEU A 375     4950   6001   5380    245   -141    -57       O  
ATOM   2562  CB  LEU A 375      17.198  22.017  -5.044  1.00 48.86           C  
ANISOU 2562  CB  LEU A 375     5648   6712   6204    255   -172   -105       C  
ATOM   2563  CG  LEU A 375      15.763  22.400  -5.400  1.00 50.20           C  
ANISOU 2563  CG  LEU A 375     5801   6886   6388    270   -176   -152       C  
ATOM   2564  CD1 LEU A 375      15.710  23.097  -6.750  1.00 49.94           C  
ANISOU 2564  CD1 LEU A 375     5770   6882   6326    322   -195   -173       C  
ATOM   2565  CD2 LEU A 375      14.898  21.148  -5.397  1.00 49.59           C  
ANISOU 2565  CD2 LEU A 375     5693   6785   6366    263   -183   -191       C  
ATOM   2566  N   ARG A 376      17.987  23.886  -2.669  1.00 42.10           N  
ANISOU 2566  N   ARG A 376     4839   5860   5296    182   -127    -23       N  
ATOM   2567  CA  ARG A 376      17.653  24.834  -1.615  1.00 42.51           C  
ANISOU 2567  CA  ARG A 376     4903   5914   5334    150   -106    -10       C  
ATOM   2568  C   ARG A 376      18.344  26.178  -1.824  1.00 46.17           C  
ANISOU 2568  C   ARG A 376     5386   6397   5761    162   -101     10       C  
ATOM   2569  O   ARG A 376      17.675  27.217  -1.813  1.00 48.06           O  
ANISOU 2569  O   ARG A 376     5625   6642   5992    165    -93     -4       O  
ATOM   2570  CB  ARG A 376      17.985  24.264  -0.229  1.00 41.62           C  
ANISOU 2570  CB  ARG A 376     4798   5789   5227    103    -91     21       C  
ATOM   2571  CG  ARG A 376      18.084  25.304   0.883  1.00 38.66           C  
ANISOU 2571  CG  ARG A 376     4440   5424   4826     71    -70     42       C  
ATOM   2572  CD  ARG A 376      18.323  24.607   2.195  1.00 38.81           C  
ANISOU 2572  CD  ARG A 376     4465   5434   4846     29    -57     70       C  
ATOM   2573  NE  ARG A 376      18.689  25.499   3.288  1.00 38.47           N  
ANISOU 2573  NE  ARG A 376     4439   5404   4772      0    -41     93       N  
ATOM   2574  CZ  ARG A 376      17.887  25.763   4.322  1.00 42.38           C  
ANISOU 2574  CZ  ARG A 376     4935   5901   5266    -32    -20     86       C  
ATOM   2575  NH1 ARG A 376      16.668  25.218   4.385  1.00 41.91           N  
ANISOU 2575  NH1 ARG A 376     4860   5828   5237    -39    -10     60       N  
ATOM   2576  NH2 ARG A 376      18.291  26.567   5.301  1.00 40.32           N  
ANISOU 2576  NH2 ARG A 376     4689   5656   4974    -57     -7    104       N  
ATOM   2577  N   LYS A 377      19.662  26.171  -2.027  1.00 44.19           N  
ANISOU 2577  N   LYS A 377     5147   6151   5491    170   -106     42       N  
ATOM   2578  CA  LYS A 377      20.396  27.447  -2.148  1.00 45.12           C  
ANISOU 2578  CA  LYS A 377     5280   6282   5580    179    -99     63       C  
ATOM   2579  C   LYS A 377      19.992  28.202  -3.400  1.00 44.54           C  
ANISOU 2579  C   LYS A 377     5204   6222   5498    224   -105     44       C  
ATOM   2580  O   LYS A 377      19.849  29.426  -3.372  1.00 45.74           O  
ANISOU 2580  O   LYS A 377     5362   6380   5636    228    -93     48       O  
ATOM   2581  CB  LYS A 377      21.920  27.246  -2.129  1.00 43.28           C  
ANISOU 2581  CB  LYS A 377     5059   6051   5334    179   -102     99       C  
ATOM   2582  CG  LYS A 377      22.427  26.669  -0.831  1.00 45.60           C  
ANISOU 2582  CG  LYS A 377     5359   6336   5632    136    -97    124       C  
ATOM   2583  CD  LYS A 377      23.926  26.863  -0.704  1.00 49.32           C  
ANISOU 2583  CD  LYS A 377     5842   6810   6088    134    -99    159       C  
ATOM   2584  CE  LYS A 377      24.441  26.351   0.636  1.00 47.25           C  
ANISOU 2584  CE  LYS A 377     5586   6543   5825     94    -97    185       C  
ATOM   2585  NZ  LYS A 377      24.411  24.869   0.668  1.00 50.74           N  
ANISOU 2585  NZ  LYS A 377     6019   6970   6290     90   -108    188       N  
ATOM   2586  N   CYS A 378      19.817  27.472  -4.498  1.00 43.48           N  
ANISOU 2586  N   CYS A 378     5059   6092   5370    259   -123     23       N  
ATOM   2587  CA  CYS A 378      19.453  28.097  -5.759  1.00 44.56           C  
ANISOU 2587  CA  CYS A 378     5194   6245   5492    307   -132      6       C  
ATOM   2588  C   CYS A 378      18.066  28.745  -5.614  1.00 44.68           C  
ANISOU 2588  C   CYS A 378     5199   6259   5517    306   -128    -24       C  
ATOM   2589  O   CYS A 378      17.892  29.934  -5.888  1.00 45.03           O  
ANISOU 2589  O   CYS A 378     5249   6312   5547    322   -121    -19       O  
ATOM   2590  CB  CYS A 378      19.480  27.061  -6.870  1.00 45.75           C  
ANISOU 2590  CB  CYS A 378     5332   6402   5648    343   -154    -17       C  
ATOM   2591  SG  CYS A 378      19.431  27.758  -8.528  1.00 54.10           S  
ANISOU 2591  SG  CYS A 378     6392   7489   6675    408   -166    -28       S  
ATOM   2592  N   SER A 379      17.102  27.980  -5.113  1.00 44.24           N  
ANISOU 2592  N   SER A 379     5128   6191   5491    285   -131    -53       N  
ATOM   2593  CA  SER A 379      15.758  28.512  -4.875  1.00 46.10           C  
ANISOU 2593  CA  SER A 379     5352   6423   5742    279   -127    -84       C  
ATOM   2594  C   SER A 379      15.786  29.750  -3.972  1.00 44.92           C  
ANISOU 2594  C   SER A 379     5214   6272   5582    252   -103    -64       C  
ATOM   2595  O   SER A 379      15.179  30.762  -4.307  1.00 44.34           O  
ANISOU 2595  O   SER A 379     5138   6205   5505    269   -101    -75       O  
ATOM   2596  CB  SER A 379      14.839  27.440  -4.293  1.00 45.22           C  
ANISOU 2596  CB  SER A 379     5221   6294   5668    253   -127   -114       C  
ATOM   2597  OG  SER A 379      14.864  26.272  -5.087  1.00 44.06           O  
ANISOU 2597  OG  SER A 379     5059   6145   5536    277   -148   -134       O  
ATOM   2598  N   ALA A 380      16.521  29.685  -2.860  1.00 44.00           N  
ANISOU 2598  N   ALA A 380     5109   6148   5460    211    -87    -34       N  
ATOM   2599  CA  ALA A 380      16.612  30.835  -1.958  1.00 44.25           C  
ANISOU 2599  CA  ALA A 380     5151   6180   5482    184    -66    -19       C  
ATOM   2600  C   ALA A 380      17.276  32.044  -2.625  1.00 45.25           C  
ANISOU 2600  C   ALA A 380     5287   6317   5588    212    -63      0       C  
ATOM   2601  O   ALA A 380      16.816  33.194  -2.479  1.00 44.86           O  
ANISOU 2601  O   ALA A 380     5236   6267   5540    212    -51     -5       O  
ATOM   2602  CB  ALA A 380      17.323  30.469  -0.669  1.00 42.49           C  
ANISOU 2602  CB  ALA A 380     4938   5952   5253    138    -53      7       C  
ATOM   2603  N   ALA A 381      18.346  31.799  -3.371  1.00 45.87           N  
ANISOU 2603  N   ALA A 381     5375   6403   5652    237    -72     24       N  
ATOM   2604  CA  ALA A 381      18.978  32.901  -4.103  1.00 46.00           C  
ANISOU 2604  CA  ALA A 381     5400   6427   5651    267    -67     45       C  
ATOM   2605  C   ALA A 381      18.033  33.484  -5.157  1.00 44.88           C  
ANISOU 2605  C   ALA A 381     5250   6293   5508    310    -75     24       C  
ATOM   2606  O   ALA A 381      17.999  34.701  -5.352  1.00 44.55           O  
ANISOU 2606  O   ALA A 381     5211   6252   5464    323    -63     34       O  
ATOM   2607  CB  ALA A 381      20.295  32.465  -4.734  1.00 43.39           C  
ANISOU 2607  CB  ALA A 381     5079   6102   5304    287    -73     73       C  
ATOM   2608  N   ALA A 382      17.265  32.625  -5.827  1.00 44.99           N  
ANISOU 2608  N   ALA A 382     5253   6313   5530    333    -95     -7       N  
ATOM   2609  CA  ALA A 382      16.346  33.091  -6.872  1.00 45.60           C  
ANISOU 2609  CA  ALA A 382     5321   6401   5604    377   -108    -30       C  
ATOM   2610  C   ALA A 382      15.264  33.985  -6.270  1.00 47.14           C  
ANISOU 2610  C   ALA A 382     5506   6586   5817    360    -97    -49       C  
ATOM   2611  O   ALA A 382      14.926  35.040  -6.825  1.00 46.18           O  
ANISOU 2611  O   ALA A 382     5385   6470   5692    389    -95    -46       O  
ATOM   2612  CB  ALA A 382      15.727  31.914  -7.606  1.00 47.27           C  
ANISOU 2612  CB  ALA A 382     5519   6620   5823    401   -134    -66       C  
ATOM   2613  N   LEU A 383      14.752  33.561  -5.115  1.00 44.82           N  
ANISOU 2613  N   LEU A 383     5205   6278   5546    314    -88    -66       N  
ATOM   2614  CA  LEU A 383      13.747  34.310  -4.388  1.00 47.03           C  
ANISOU 2614  CA  LEU A 383     5475   6548   5846    291    -74    -86       C  
ATOM   2615  C   LEU A 383      14.273  35.660  -3.942  1.00 47.84           C  
ANISOU 2615  C   LEU A 383     5588   6648   5943    280    -52    -60       C  
ATOM   2616  O   LEU A 383      13.565  36.655  -4.037  1.00 53.73           O  
ANISOU 2616  O   LEU A 383     6325   7390   6700    289    -46    -71       O  
ATOM   2617  CB  LEU A 383      13.227  33.513  -3.184  1.00 46.97           C  
ANISOU 2617  CB  LEU A 383     5459   6527   5859    242    -64   -105       C  
ATOM   2618  CG  LEU A 383      11.952  34.034  -2.489  1.00 48.67           C  
ANISOU 2618  CG  LEU A 383     5660   6733   6101    219    -51   -138       C  
ATOM   2619  CD1 LEU A 383      10.752  34.050  -3.432  1.00 49.42           C  
ANISOU 2619  CD1 LEU A 383     5735   6829   6215    256    -70   -177       C  
ATOM   2620  CD2 LEU A 383      11.651  33.176  -1.273  1.00 47.68           C  
ANISOU 2620  CD2 LEU A 383     5530   6597   5991    169    -37   -147       C  
ATOM   2621  N   ASP A 384      15.515  35.683  -3.463  1.00 50.26           N  
ANISOU 2621  N   ASP A 384     5909   6954   6234    260    -41    -26       N  
ATOM   2622  CA  ASP A 384      16.203  36.910  -3.042  1.00 47.16           C  
ANISOU 2622  CA  ASP A 384     5524   6557   5839    248    -20     -1       C  
ATOM   2623  C   ASP A 384      16.233  37.924  -4.178  1.00 45.66           C  
ANISOU 2623  C   ASP A 384     5334   6370   5645    296    -21     13       C  
ATOM   2624  O   ASP A 384      15.872  39.089  -3.981  1.00 45.87           O  
ANISOU 2624  O   ASP A 384     5355   6388   5686    294     -6     11       O  
ATOM   2625  CB  ASP A 384      17.630  36.573  -2.560  1.00 47.62           C  
ANISOU 2625  CB  ASP A 384     5596   6616   5881    227    -14     32       C  
ATOM   2626  CG  ASP A 384      18.308  37.735  -1.833  1.00 48.38           C  
ANISOU 2626  CG  ASP A 384     5696   6706   5981    205      8     50       C  
ATOM   2627  OD1 ASP A 384      18.421  38.834  -2.422  1.00 46.80           O  
ANISOU 2627  OD1 ASP A 384     5494   6502   5787    230     17     61       O  
ATOM   2628  OD2 ASP A 384      18.746  37.545  -0.670  1.00 47.13           O  
ANISOU 2628  OD2 ASP A 384     5541   6547   5821    162     17     53       O  
ATOM   2629  N   VAL A 385      16.637  37.488  -5.370  1.00 47.41           N  
ANISOU 2629  N   VAL A 385     5563   6605   5848    339    -37     26       N  
ATOM   2630  CA  VAL A 385      16.708  38.411  -6.510  1.00 50.10           C  
ANISOU 2630  CA  VAL A 385     5905   6951   6179    388    -36     44       C  
ATOM   2631  C   VAL A 385      15.306  38.821  -6.954  1.00 51.13           C  
ANISOU 2631  C   VAL A 385     6021   7082   6322    413    -47     14       C  
ATOM   2632  O   VAL A 385      15.048  40.003  -7.223  1.00 50.77           O  
ANISOU 2632  O   VAL A 385     5973   7031   6286    431    -37     25       O  
ATOM   2633  CB  VAL A 385      17.469  37.843  -7.733  1.00 52.71           C  
ANISOU 2633  CB  VAL A 385     6247   7299   6481    432    -50     65       C  
ATOM   2634  CG1 VAL A 385      17.757  38.958  -8.733  1.00 53.23           C  
ANISOU 2634  CG1 VAL A 385     6319   7371   6536    478    -41     96       C  
ATOM   2635  CG2 VAL A 385      18.789  37.231  -7.320  1.00 59.32           C  
ANISOU 2635  CG2 VAL A 385     7096   8135   7310    409    -44     89       C  
ATOM   2636  N   LEU A 386      14.402  37.849  -7.042  1.00 49.66           N  
ANISOU 2636  N   LEU A 386     5824   6902   6141    414    -68    -23       N  
ATOM   2637  CA  LEU A 386      13.031  38.172  -7.411  1.00 50.60           C  
ANISOU 2637  CA  LEU A 386     5928   7022   6277    435    -81    -57       C  
ATOM   2638  C   LEU A 386      12.434  39.201  -6.460  1.00 48.63           C  
ANISOU 2638  C   LEU A 386     5668   6754   6057    403    -60    -67       C  
ATOM   2639  O   LEU A 386      11.791  40.132  -6.917  1.00 51.28           O  
ANISOU 2639  O   LEU A 386     5995   7086   6402    430    -61    -70       O  
ATOM   2640  CB  LEU A 386      12.160  36.925  -7.558  1.00 49.35           C  
ANISOU 2640  CB  LEU A 386     5755   6869   6127    437   -106   -101       C  
ATOM   2641  CG  LEU A 386      12.522  36.119  -8.824  1.00 50.53           C  
ANISOU 2641  CG  LEU A 386     5909   7041   6249    485   -132   -101       C  
ATOM   2642  CD1 LEU A 386      12.067  34.672  -8.702  1.00 50.79           C  
ANISOU 2642  CD1 LEU A 386     5928   7073   6295    472   -150   -139       C  
ATOM   2643  CD2 LEU A 386      11.991  36.760 -10.110  1.00 47.55           C  
ANISOU 2643  CD2 LEU A 386     5529   6683   5857    547   -150   -104       C  
ATOM   2644  N   ALA A 387      12.697  39.064  -5.161  1.00 44.95           N  
ANISOU 2644  N   ALA A 387     5203   6275   5601    348    -40    -69       N  
ATOM   2645  CA  ALA A 387      12.303  40.086  -4.184  1.00 46.34           C  
ANISOU 2645  CA  ALA A 387     5370   6435   5802    315    -17    -77       C  
ATOM   2646  C   ALA A 387      12.845  41.472  -4.518  1.00 48.04           C  
ANISOU 2646  C   ALA A 387     5589   6643   6020    334     -1    -46       C  
ATOM   2647  O   ALA A 387      12.148  42.462  -4.347  1.00 48.97           O  
ANISOU 2647  O   ALA A 387     5694   6749   6164    334      9    -59       O  
ATOM   2648  CB  ALA A 387      12.728  39.688  -2.778  1.00 45.08           C  
ANISOU 2648  CB  ALA A 387     5215   6270   5644    256      1    -79       C  
ATOM   2649  N   ASN A 388      14.090  41.540  -4.975  1.00 47.38           N  
ANISOU 2649  N   ASN A 388     5522   6566   5916    349      3     -6       N  
ATOM   2650  CA  ASN A 388      14.682  42.812  -5.381  1.00 50.76           C  
ANISOU 2650  CA  ASN A 388     5953   6985   6350    371     20     28       C  
ATOM   2651  C   ASN A 388      14.115  43.352  -6.675  1.00 48.83           C  
ANISOU 2651  C   ASN A 388     5705   6746   6103    429      8     37       C  
ATOM   2652  O   ASN A 388      14.111  44.553  -6.877  1.00 49.87           O  
ANISOU 2652  O   ASN A 388     5831   6864   6252    444     23     55       O  
ATOM   2653  CB  ASN A 388      16.208  42.722  -5.480  1.00 48.90           C  
ANISOU 2653  CB  ASN A 388     5733   6751   6096    369     30     69       C  
ATOM   2654  CG  ASN A 388      16.868  42.841  -4.133  1.00 52.55           C  
ANISOU 2654  CG  ASN A 388     6195   7202   6568    314     49     67       C  
ATOM   2655  OD1 ASN A 388      17.410  41.873  -3.625  1.00 57.16           O  
ANISOU 2655  OD1 ASN A 388     6787   7794   7137    289     43     67       O  
ATOM   2656  ND2 ASN A 388      16.786  44.018  -3.526  1.00 52.63           N  
ANISOU 2656  ND2 ASN A 388     6194   7195   6607    296     71     65       N  
ATOM   2657  N   VAL A 389      13.660  42.467  -7.550  1.00 49.06           N  
ANISOU 2657  N   VAL A 389     5737   6795   6111    463    -20     24       N  
ATOM   2658  CA  VAL A 389      12.985  42.881  -8.772  1.00 53.94           C  
ANISOU 2658  CA  VAL A 389     6350   7423   6721    522    -37     26       C  
ATOM   2659  C   VAL A 389      11.558  43.395  -8.469  1.00 58.36           C  
ANISOU 2659  C   VAL A 389     6889   7971   7314    518    -43    -12       C  
ATOM   2660  O   VAL A 389      11.193  44.521  -8.827  1.00 60.85           O  
ANISOU 2660  O   VAL A 389     7198   8278   7646    542    -36      1       O  
ATOM   2661  CB  VAL A 389      12.913  41.726  -9.787  1.00 53.95           C  
ANISOU 2661  CB  VAL A 389     6359   7453   6689    560    -68     16       C  
ATOM   2662  CG1 VAL A 389      12.023  42.102 -10.975  1.00 56.51           C  
ANISOU 2662  CG1 VAL A 389     6675   7792   7003    620    -91      9       C  
ATOM   2663  CG2 VAL A 389      14.309  41.336 -10.253  1.00 51.78           C  
ANISOU 2663  CG2 VAL A 389     6103   7190   6381    571    -62     55       C  
ATOM   2664  N   TYR A 390      10.766  42.574  -7.790  1.00 56.29           N  
ANISOU 2664  N   TYR A 390     6614   7707   7065    486    -53    -58       N  
ATOM   2665  CA  TYR A 390       9.361  42.871  -7.602  1.00 57.07           C  
ANISOU 2665  CA  TYR A 390     6691   7797   7196    485    -61    -99       C  
ATOM   2666  C   TYR A 390       9.105  43.792  -6.439  1.00 59.32           C  
ANISOU 2666  C   TYR A 390     6964   8057   7517    440    -32   -108       C  
ATOM   2667  O   TYR A 390       8.048  44.415  -6.366  1.00 58.36           O  
ANISOU 2667  O   TYR A 390     6823   7924   7426    445    -34   -134       O  
ATOM   2668  CB  TYR A 390       8.574  41.578  -7.423  1.00 56.34           C  
ANISOU 2668  CB  TYR A 390     6587   7712   7106    472    -82   -146       C  
ATOM   2669  CG  TYR A 390       8.372  40.871  -8.727  1.00 57.12           C  
ANISOU 2669  CG  TYR A 390     6688   7836   7180    527   -117   -153       C  
ATOM   2670  CD1 TYR A 390       9.300  39.934  -9.186  1.00 56.61           C  
ANISOU 2670  CD1 TYR A 390     6639   7788   7081    537   -126   -136       C  
ATOM   2671  CD2 TYR A 390       7.267  41.161  -9.528  1.00 54.19           C  
ANISOU 2671  CD2 TYR A 390     6300   7472   6818    570   -142   -179       C  
ATOM   2672  CE1 TYR A 390       9.125  39.294 -10.401  1.00 56.26           C  
ANISOU 2672  CE1 TYR A 390     6595   7770   7012    589   -158   -147       C  
ATOM   2673  CE2 TYR A 390       7.080  40.526 -10.741  1.00 56.15           C  
ANISOU 2673  CE2 TYR A 390     6548   7746   7039    623   -176   -189       C  
ATOM   2674  CZ  TYR A 390       8.004  39.595 -11.175  1.00 58.36           C  
ANISOU 2674  CZ  TYR A 390     6844   8045   7285    632   -183   -174       C  
ATOM   2675  OH  TYR A 390       7.808  38.966 -12.386  1.00 60.27           O  
ANISOU 2675  OH  TYR A 390     7084   8316   7499    686   -218   -190       O  
ATOM   2676  N   ARG A 391      10.073  43.876  -5.531  1.00 61.22           N  
ANISOU 2676  N   ARG A 391     7215   8290   7755    398     -8    -90       N  
ATOM   2677  CA  ARG A 391       9.933  44.673  -4.312  1.00 63.11           C  
ANISOU 2677  CA  ARG A 391     7444   8510   8027    350     21   -103       C  
ATOM   2678  C   ARG A 391       8.581  44.395  -3.620  1.00 63.67           C  
ANISOU 2678  C   ARG A 391     7494   8574   8125    323     18   -156       C  
ATOM   2679  O   ARG A 391       8.254  43.230  -3.391  1.00 60.70           O  
ANISOU 2679  O   ARG A 391     7118   8207   7739    308      7   -179       O  
ATOM   2680  CB  ARG A 391      10.204  46.162  -4.591  1.00 65.24           C  
ANISOU 2680  CB  ARG A 391     7709   8763   8318    370     38    -76       C  
ATOM   2681  CG  ARG A 391      11.469  46.395  -5.424  1.00 68.87           C  
ANISOU 2681  CG  ARG A 391     8187   9228   8752    402     42    -22       C  
ATOM   2682  CD  ARG A 391      12.280  47.570  -4.892  1.00 76.02           C  
ANISOU 2682  CD  ARG A 391     9090  10112   9681    383     74      3       C  
ATOM   2683  NE  ARG A 391      13.072  47.201  -3.716  1.00 81.52           N  
ANISOU 2683  NE  ARG A 391     9792  10809  10373    329     89     -3       N  
ATOM   2684  CZ  ARG A 391      13.321  48.001  -2.673  1.00 87.77           C  
ANISOU 2684  CZ  ARG A 391    10572  11583  11193    289    114    -13       C  
ATOM   2685  NH1 ARG A 391      12.834  49.238  -2.628  1.00 93.56           N  
ANISOU 2685  NH1 ARG A 391    11287  12295  11968    294    130    -19       N  
ATOM   2686  NH2 ARG A 391      14.051  47.557  -1.656  1.00 84.68           N  
ANISOU 2686  NH2 ARG A 391    10187  11198  10790    244    123    -18       N  
ATOM   2687  N   ASP A 392       7.795  45.426  -3.308  1.00 63.68           N  
ANISOU 2687  N   ASP A 392     7475   8557   8163    318     31   -176       N  
ATOM   2688  CA  ASP A 392       6.567  45.221  -2.531  1.00 62.95           C  
ANISOU 2688  CA  ASP A 392     7361   8456   8099    287     34   -228       C  
ATOM   2689  C   ASP A 392       5.469  44.449  -3.284  1.00 62.65           C  
ANISOU 2689  C   ASP A 392     7312   8427   8067    317      4   -259       C  
ATOM   2690  O   ASP A 392       4.561  43.893  -2.660  1.00 64.26           O  
ANISOU 2690  O   ASP A 392     7501   8626   8290    289      6   -302       O  
ATOM   2691  CB  ASP A 392       6.042  46.546  -1.941  1.00 65.98           C  
ANISOU 2691  CB  ASP A 392     7725   8819   8526    270     57   -245       C  
ATOM   2692  CG  ASP A 392       7.001  47.166  -0.889  1.00 69.67           C  
ANISOU 2692  CG  ASP A 392     8198   9280   8994    227     89   -230       C  
ATOM   2693  OD1 ASP A 392       7.888  46.466  -0.326  1.00 65.86           O  
ANISOU 2693  OD1 ASP A 392     7733   8809   8481    198     95   -216       O  
ATOM   2694  OD2 ASP A 392       6.857  48.381  -0.622  1.00 73.59           O  
ANISOU 2694  OD2 ASP A 392     8680   9758   9525    222    107   -234       O  
ATOM   2695  N   GLU A 393       5.577  44.368  -4.610  1.00 58.13           N  
ANISOU 2695  N   GLU A 393     6746   7867   7475    375    -23   -239       N  
ATOM   2696  CA  GLU A 393       4.625  43.603  -5.417  1.00 58.89           C  
ANISOU 2696  CA  GLU A 393     6830   7973   7572    409    -56   -271       C  
ATOM   2697  C   GLU A 393       4.682  42.106  -5.124  1.00 59.13           C  
ANISOU 2697  C   GLU A 393     6865   8014   7588    386    -65   -291       C  
ATOM   2698  O   GLU A 393       3.750  41.364  -5.441  1.00 58.25           O  
ANISOU 2698  O   GLU A 393     6737   7905   7490    398    -86   -330       O  
ATOM   2699  CB  GLU A 393       4.864  43.821  -6.915  1.00 61.76           C  
ANISOU 2699  CB  GLU A 393     7203   8355   7909    478    -84   -242       C  
ATOM   2700  CG  GLU A 393       4.689  45.254  -7.403  1.00 70.50           C  
ANISOU 2700  CG  GLU A 393     8303   9450   9032    511    -80   -220       C  
ATOM   2701  CD  GLU A 393       5.037  45.416  -8.885  1.00 79.03           C  
ANISOU 2701  CD  GLU A 393     9398  10553  10078    581   -104   -184       C  
ATOM   2702  OE1 GLU A 393       4.689  44.514  -9.692  1.00 81.22           O  
ANISOU 2702  OE1 GLU A 393     9675  10854  10333    615   -137   -202       O  
ATOM   2703  OE2 GLU A 393       5.655  46.447  -9.249  1.00 78.33           O  
ANISOU 2703  OE2 GLU A 393     9318  10458   9985    603    -90   -137       O  
ATOM   2704  N   LEU A 394       5.780  41.655  -4.524  1.00 57.03           N  
ANISOU 2704  N   LEU A 394     6619   7752   7299    354    -48   -263       N  
ATOM   2705  CA  LEU A 394       5.954  40.240  -4.246  1.00 54.02           C  
ANISOU 2705  CA  LEU A 394     6243   7378   6905    332    -55   -275       C  
ATOM   2706  C   LEU A 394       5.195  39.805  -3.006  1.00 51.81           C  
ANISOU 2706  C   LEU A 394     5948   7084   6654    278    -35   -311       C  
ATOM   2707  O   LEU A 394       4.846  38.626  -2.849  1.00 49.21           O  
ANISOU 2707  O   LEU A 394     5612   6755   6330    265    -42   -334       O  
ATOM   2708  CB  LEU A 394       7.437  39.912  -4.073  1.00 56.32           C  
ANISOU 2708  CB  LEU A 394     6560   7677   7160    320    -45   -230       C  
ATOM   2709  CG  LEU A 394       7.755  38.420  -4.112  1.00 56.46           C  
ANISOU 2709  CG  LEU A 394     6584   7705   7164    312    -58   -234       C  
ATOM   2710  CD1 LEU A 394       7.573  37.863  -5.516  1.00 56.43           C  
ANISOU 2710  CD1 LEU A 394     6577   7716   7146    368    -93   -242       C  
ATOM   2711  CD2 LEU A 394       9.164  38.169  -3.604  1.00 58.27           C  
ANISOU 2711  CD2 LEU A 394     6837   7938   7365    287    -44   -192       C  
ATOM   2712  N   LEU A 395       4.941  40.757  -2.123  1.00 49.97           N  
ANISOU 2712  N   LEU A 395     5708   6838   6440    247     -9   -318       N  
ATOM   2713  CA  LEU A 395       4.397  40.435  -0.804  1.00 54.02           C  
ANISOU 2713  CA  LEU A 395     6212   7341   6974    191     17   -346       C  
ATOM   2714  C   LEU A 395       3.067  39.658  -0.766  1.00 54.98           C  
ANISOU 2714  C   LEU A 395     6308   7453   7128    186     10   -396       C  
ATOM   2715  O   LEU A 395       2.908  38.775   0.088  1.00 54.05           O  
ANISOU 2715  O   LEU A 395     6189   7332   7015    146     25   -408       O  
ATOM   2716  CB  LEU A 395       4.306  41.693   0.050  1.00 54.95           C  
ANISOU 2716  CB  LEU A 395     6323   7448   7108    163     46   -350       C  
ATOM   2717  CG  LEU A 395       5.656  42.151   0.576  1.00 57.17           C  
ANISOU 2717  CG  LEU A 395     6626   7735   7361    143     64   -309       C  
ATOM   2718  CD1 LEU A 395       5.447  43.459   1.294  1.00 60.45           C  
ANISOU 2718  CD1 LEU A 395     7029   8138   7800    121     89   -321       C  
ATOM   2719  CD2 LEU A 395       6.262  41.123   1.520  1.00 60.78           C  
ANISOU 2719  CD2 LEU A 395     7098   8201   7793    100     76   -299       C  
ATOM   2720  N   PRO A 396       2.113  39.981  -1.676  1.00 54.97           N  
ANISOU 2720  N   PRO A 396     6286   7449   7152    227    -14   -424       N  
ATOM   2721  CA  PRO A 396       0.865  39.213  -1.731  1.00 54.41           C  
ANISOU 2721  CA  PRO A 396     6189   7369   7117    227    -24   -475       C  
ATOM   2722  C   PRO A 396       1.076  37.751  -2.159  1.00 54.17           C  
ANISOU 2722  C   PRO A 396     6161   7346   7075    235    -43   -477       C  
ATOM   2723  O   PRO A 396       0.322  36.871  -1.741  1.00 53.05           O  
ANISOU 2723  O   PRO A 396     6001   7193   6962    213    -38   -512       O  
ATOM   2724  CB  PRO A 396       0.031  39.979  -2.769  1.00 53.60           C  
ANISOU 2724  CB  PRO A 396     6065   7264   7035    278    -51   -497       C  
ATOM   2725  CG  PRO A 396       0.589  41.358  -2.759  1.00 50.72           C  
ANISOU 2725  CG  PRO A 396     5713   6899   6660    286    -39   -463       C  
ATOM   2726  CD  PRO A 396       2.057  41.140  -2.589  1.00 53.49           C  
ANISOU 2726  CD  PRO A 396     6096   7262   6966    274    -29   -412       C  
ATOM   2727  N   HIS A 397       2.097  37.490  -2.973  1.00 53.82           N  
ANISOU 2727  N   HIS A 397     6138   7319   6992    267    -64   -442       N  
ATOM   2728  CA  HIS A 397       2.491  36.107  -3.260  1.00 51.03           C  
ANISOU 2728  CA  HIS A 397     5789   6973   6627    270    -78   -440       C  
ATOM   2729  C   HIS A 397       3.100  35.394  -2.089  1.00 50.27           C  
ANISOU 2729  C   HIS A 397     5707   6870   6524    216    -49   -421       C  
ATOM   2730  O   HIS A 397       2.853  34.202  -1.897  1.00 54.47           O  
ANISOU 2730  O   HIS A 397     6230   7395   7072    201    -50   -437       O  
ATOM   2731  CB  HIS A 397       3.427  36.045  -4.435  1.00 48.69           C  
ANISOU 2731  CB  HIS A 397     5511   6697   6291    319   -105   -409       C  
ATOM   2732  CG  HIS A 397       2.828  36.578  -5.699  1.00 49.02           C  
ANISOU 2732  CG  HIS A 397     5541   6751   6334    379   -138   -427       C  
ATOM   2733  ND1 HIS A 397       2.266  35.775  -6.629  1.00 48.91           N  
ANISOU 2733  ND1 HIS A 397     5510   6746   6328    417   -172   -462       N  
ATOM   2734  CD2 HIS A 397       2.697  37.885  -6.168  1.00 48.11           C  
ANISOU 2734  CD2 HIS A 397     5427   6639   6214    410   -142   -413       C  
ATOM   2735  CE1 HIS A 397       1.822  36.528  -7.658  1.00 49.13           C  
ANISOU 2735  CE1 HIS A 397     5531   6788   6350    470   -198   -469       C  
ATOM   2736  NE2 HIS A 397       2.078  37.821  -7.369  1.00 51.34           N  
ANISOU 2736  NE2 HIS A 397     5822   7062   6622    466   -178   -437       N  
ATOM   2737  N   ILE A 398       3.852  36.110  -1.261  1.00 48.98           N  
ANISOU 2737  N   ILE A 398     5562   6708   6339    186    -23   -387       N  
ATOM   2738  CA  ILE A 398       4.712  35.446  -0.287  1.00 49.13           C  
ANISOU 2738  CA  ILE A 398     5600   6728   6338    142     -2   -358       C  
ATOM   2739  C   ILE A 398       4.132  35.373   1.117  1.00 48.64           C  
ANISOU 2739  C   ILE A 398     5530   6654   6295     87     33   -374       C  
ATOM   2740  O   ILE A 398       4.411  34.418   1.864  1.00 48.89           O  
ANISOU 2740  O   ILE A 398     5569   6684   6322     53     47   -363       O  
ATOM   2741  CB  ILE A 398       6.151  36.060  -0.278  1.00 51.09           C  
ANISOU 2741  CB  ILE A 398     5877   6990   6545    145      2   -307       C  
ATOM   2742  CG1 ILE A 398       7.169  35.082   0.288  1.00 49.38           C  
ANISOU 2742  CG1 ILE A 398     5679   6777   6304    118      8   -275       C  
ATOM   2743  CG2 ILE A 398       6.226  37.353   0.515  1.00 50.09           C  
ANISOU 2743  CG2 ILE A 398     5754   6860   6418    121     28   -301       C  
ATOM   2744  CD1 ILE A 398       7.661  34.094  -0.747  1.00 49.97           C  
ANISOU 2744  CD1 ILE A 398     5758   6859   6369    153    -20   -266       C  
ATOM   2745  N   LEU A 399       3.342  36.378   1.491  1.00 48.00           N  
ANISOU 2745  N   LEU A 399     5435   6566   6236     77     48   -399       N  
ATOM   2746  CA  LEU A 399       2.767  36.412   2.845  1.00 50.40           C  
ANISOU 2746  CA  LEU A 399     5732   6862   6556     24     85   -417       C  
ATOM   2747  C   LEU A 399       1.822  35.240   3.187  1.00 50.86           C  
ANISOU 2747  C   LEU A 399     5771   6906   6647      4     94   -448       C  
ATOM   2748  O   LEU A 399       1.847  34.750   4.325  1.00 53.13           O  
ANISOU 2748  O   LEU A 399     6065   7193   6932    -42    124   -441       O  
ATOM   2749  CB  LEU A 399       2.064  37.744   3.107  1.00 52.30           C  
ANISOU 2749  CB  LEU A 399     5957   7096   6818     20     99   -443       C  
ATOM   2750  CG  LEU A 399       2.907  39.008   3.238  1.00 51.59           C  
ANISOU 2750  CG  LEU A 399     5882   7015   6705     22    106   -416       C  
ATOM   2751  CD1 LEU A 399       2.024  40.236   3.095  1.00 54.49           C  
ANISOU 2751  CD1 LEU A 399     6227   7370   7106     33    110   -447       C  
ATOM   2752  CD2 LEU A 399       3.639  39.035   4.571  1.00 52.40           C  
ANISOU 2752  CD2 LEU A 399     6002   7127   6780    -28    137   -396       C  
ATOM   2753  N   PRO A 400       0.981  34.785   2.218  1.00 49.47           N  
ANISOU 2753  N   PRO A 400     5572   6721   6505     38     68   -482       N  
ATOM   2754  CA  PRO A 400       0.138  33.610   2.520  1.00 49.56           C  
ANISOU 2754  CA  PRO A 400     5562   6714   6554     19     77   -512       C  
ATOM   2755  C   PRO A 400       0.973  32.349   2.777  1.00 50.20           C  
ANISOU 2755  C   PRO A 400     5659   6797   6617      3     80   -479       C  
ATOM   2756  O   PRO A 400       0.642  31.551   3.664  1.00 52.94           O  
ANISOU 2756  O   PRO A 400     6000   7132   6982    -35    107   -481       O  
ATOM   2757  CB  PRO A 400      -0.723  33.445   1.266  1.00 47.58           C  
ANISOU 2757  CB  PRO A 400     5283   6457   6339     66     41   -555       C  
ATOM   2758  CG  PRO A 400      -0.055  34.260   0.205  1.00 49.32           C  
ANISOU 2758  CG  PRO A 400     5517   6695   6525    115     10   -534       C  
ATOM   2759  CD  PRO A 400       0.638  35.380   0.914  1.00 47.24           C  
ANISOU 2759  CD  PRO A 400     5278   6441   6232     93     33   -500       C  
ATOM   2760  N   LEU A 401       2.056  32.195   2.025  1.00 47.52           N  
ANISOU 2760  N   LEU A 401     5340   6472   6244     33     53   -446       N  
ATOM   2761  CA  LEU A 401       3.026  31.122   2.274  1.00 49.12           C  
ANISOU 2761  CA  LEU A 401     5561   6677   6425     19     54   -409       C  
ATOM   2762  C   LEU A 401       3.717  31.268   3.622  1.00 48.32           C  
ANISOU 2762  C   LEU A 401     5483   6583   6293    -29     87   -370       C  
ATOM   2763  O   LEU A 401       3.867  30.295   4.356  1.00 47.81           O  
ANISOU 2763  O   LEU A 401     5423   6512   6232    -59    105   -354       O  
ATOM   2764  CB  LEU A 401       4.067  31.073   1.174  1.00 47.34           C  
ANISOU 2764  CB  LEU A 401     5351   6467   6168     62     20   -383       C  
ATOM   2765  CG  LEU A 401       3.536  30.578  -0.165  1.00 47.12           C  
ANISOU 2765  CG  LEU A 401     5302   6437   6165    110    -16   -418       C  
ATOM   2766  CD1 LEU A 401       4.477  30.959  -1.301  1.00 44.95           C  
ANISOU 2766  CD1 LEU A 401     5043   6183   5851    158    -47   -394       C  
ATOM   2767  CD2 LEU A 401       3.320  29.073  -0.117  1.00 47.44           C  
ANISOU 2767  CD2 LEU A 401     5326   6461   6237    100    -18   -431       C  
ATOM   2768  N   LEU A 402       4.115  32.483   3.961  1.00 49.16           N  
ANISOU 2768  N   LEU A 402     5604   6703   6372    -34     96   -357       N  
ATOM   2769  CA  LEU A 402       4.785  32.701   5.241  1.00 52.47           C  
ANISOU 2769  CA  LEU A 402     6045   7134   6759    -78    126   -326       C  
ATOM   2770  C   LEU A 402       3.898  32.322   6.413  1.00 54.67           C  
ANISOU 2770  C   LEU A 402     6312   7403   7058   -123    162   -344       C  
ATOM   2771  O   LEU A 402       4.371  31.694   7.375  1.00 56.69           O  
ANISOU 2771  O   LEU A 402     6582   7663   7293   -157    183   -314       O  
ATOM   2772  CB  LEU A 402       5.280  34.150   5.389  1.00 51.99           C  
ANISOU 2772  CB  LEU A 402     5995   7087   6673    -76    129   -317       C  
ATOM   2773  CG  LEU A 402       6.523  34.558   4.591  1.00 54.04           C  
ANISOU 2773  CG  LEU A 402     6274   7358   6901    -43    104   -283       C  
ATOM   2774  CD1 LEU A 402       6.772  36.056   4.751  1.00 55.17           C  
ANISOU 2774  CD1 LEU A 402     6420   7509   7034    -42    113   -282       C  
ATOM   2775  CD2 LEU A 402       7.742  33.757   5.022  1.00 49.02           C  
ANISOU 2775  CD2 LEU A 402     5662   6733   6233    -59    103   -239       C  
ATOM   2776  N   LYS A 403       2.619  32.696   6.336  1.00 54.58           N  
ANISOU 2776  N   LYS A 403     6273   7377   7086   -122    171   -390       N  
ATOM   2777  CA  LYS A 403       1.701  32.367   7.415  1.00 56.04           C  
ANISOU 2777  CA  LYS A 403     6445   7552   7294   -165    210   -410       C  
ATOM   2778  C   LYS A 403       1.613  30.875   7.634  1.00 53.96           C  
ANISOU 2778  C   LYS A 403     6180   7276   7049   -179    218   -398       C  
ATOM   2779  O   LYS A 403       1.621  30.433   8.783  1.00 54.15           O  
ANISOU 2779  O   LYS A 403     6211   7301   7061   -219    252   -380       O  
ATOM   2780  CB  LYS A 403       0.318  33.040   7.267  1.00 61.53           C  
ANISOU 2780  CB  LYS A 403     7109   8233   8036   -161    219   -466       C  
ATOM   2781  CG  LYS A 403       0.242  34.400   7.985  1.00 72.79           C  
ANISOU 2781  CG  LYS A 403     8539   9671   9446   -181    241   -475       C  
ATOM   2782  CD  LYS A 403       1.436  35.337   7.661  1.00 75.09           C  
ANISOU 2782  CD  LYS A 403     8853   9982   9694   -162    221   -444       C  
ATOM   2783  CE  LYS A 403       1.727  36.401   8.726  1.00 72.90           C  
ANISOU 2783  CE  LYS A 403     8586   9721   9391   -194    249   -442       C  
ATOM   2784  NZ  LYS A 403       3.191  36.683   8.720  1.00 62.26           N  
ANISOU 2784  NZ  LYS A 403     7267   8392   7996   -188    236   -397       N  
ATOM   2785  N   GLU A 404       1.588  30.084   6.562  1.00 53.26           N  
ANISOU 2785  N   GLU A 404     6079   7174   6985   -145    187   -406       N  
ATOM   2786  CA  GLU A 404       1.547  28.628   6.762  1.00 55.86           C  
ANISOU 2786  CA  GLU A 404     6401   7485   7336   -158    195   -394       C  
ATOM   2787  C   GLU A 404       2.896  28.028   7.217  1.00 55.63           C  
ANISOU 2787  C   GLU A 404     6404   7470   7264   -171    195   -334       C  
ATOM   2788  O   GLU A 404       2.930  26.934   7.785  1.00 56.29           O  
ANISOU 2788  O   GLU A 404     6488   7540   7359   -194    213   -314       O  
ATOM   2789  CB  GLU A 404       0.897  27.857   5.578  1.00 58.45           C  
ANISOU 2789  CB  GLU A 404     6699   7791   7717   -123    166   -432       C  
ATOM   2790  CG  GLU A 404       1.683  27.749   4.263  1.00 63.78           C  
ANISOU 2790  CG  GLU A 404     7381   8477   8376    -74    119   -425       C  
ATOM   2791  CD  GLU A 404       1.085  26.725   3.275  1.00 68.36           C  
ANISOU 2791  CD  GLU A 404     7930   9037   9008    -45     94   -462       C  
ATOM   2792  OE1 GLU A 404       0.660  27.116   2.159  1.00 66.34           O  
ANISOU 2792  OE1 GLU A 404     7657   8785   8764     -2     61   -499       O  
ATOM   2793  OE2 GLU A 404       1.049  25.509   3.596  1.00 73.75           O  
ANISOU 2793  OE2 GLU A 404     8603   9699   9720    -63    106   -455       O  
ATOM   2794  N   LEU A 405       3.995  28.755   6.998  1.00 53.47           N  
ANISOU 2794  N   LEU A 405     6156   7219   6941   -157    176   -306       N  
ATOM   2795  CA  LEU A 405       5.323  28.232   7.311  1.00 48.15           C  
ANISOU 2795  CA  LEU A 405     5509   6557   6227   -164    170   -252       C  
ATOM   2796  C   LEU A 405       5.852  28.673   8.677  1.00 47.40           C  
ANISOU 2796  C   LEU A 405     5439   6483   6089   -204    199   -220       C  
ATOM   2797  O   LEU A 405       6.351  27.861   9.431  1.00 49.28           O  
ANISOU 2797  O   LEU A 405     5691   6723   6311   -227    213   -183       O  
ATOM   2798  CB  LEU A 405       6.313  28.585   6.205  1.00 46.83           C  
ANISOU 2798  CB  LEU A 405     5354   6402   6037   -122    131   -239       C  
ATOM   2799  CG  LEU A 405       5.998  28.069   4.795  1.00 49.11           C  
ANISOU 2799  CG  LEU A 405     5623   6678   6359    -78     98   -266       C  
ATOM   2800  CD1 LEU A 405       6.870  28.792   3.798  1.00 46.51           C  
ANISOU 2800  CD1 LEU A 405     5307   6366   5999    -38     67   -254       C  
ATOM   2801  CD2 LEU A 405       6.155  26.569   4.640  1.00 47.72           C  
ANISOU 2801  CD2 LEU A 405     5439   6484   6208    -78     92   -256       C  
ATOM   2802  N   LEU A 406       5.718  29.944   9.014  1.00 48.18           N  
ANISOU 2802  N   LEU A 406     5541   6597   6168   -211    209   -235       N  
ATOM   2803  CA  LEU A 406       6.422  30.488  10.179  1.00 48.43           C  
ANISOU 2803  CA  LEU A 406     5596   6654   6151   -242    229   -208       C  
ATOM   2804  C   LEU A 406       6.021  29.930  11.542  1.00 52.25           C  
ANISOU 2804  C   LEU A 406     6084   7142   6627   -287    269   -196       C  
ATOM   2805  O   LEU A 406       6.758  30.074  12.527  1.00 57.36           O  
ANISOU 2805  O   LEU A 406     6754   7814   7228   -311    281   -165       O  
ATOM   2806  CB  LEU A 406       6.333  32.015  10.198  1.00 47.03           C  
ANISOU 2806  CB  LEU A 406     5416   6489   5962   -239    231   -232       C  
ATOM   2807  CG  LEU A 406       7.144  32.799   9.160  1.00 48.53           C  
ANISOU 2807  CG  LEU A 406     5613   6685   6140   -200    198   -226       C  
ATOM   2808  CD1 LEU A 406       6.803  34.276   9.240  1.00 47.62           C  
ANISOU 2808  CD1 LEU A 406     5490   6576   6028   -200    207   -254       C  
ATOM   2809  CD2 LEU A 406       8.643  32.601   9.342  1.00 49.29           C  
ANISOU 2809  CD2 LEU A 406     5736   6799   6195   -201    185   -178       C  
ATOM   2810  N   PHE A 407       4.870  29.281  11.611  1.00 53.89           N  
ANISOU 2810  N   PHE A 407     6269   7326   6878   -297    289   -220       N  
ATOM   2811  CA  PHE A 407       4.323  28.881  12.902  1.00 57.01           C  
ANISOU 2811  CA  PHE A 407     6667   7725   7269   -340    333   -213       C  
ATOM   2812  C   PHE A 407       4.045  27.393  12.928  1.00 57.81           C  
ANISOU 2812  C   PHE A 407     6760   7801   7404   -346    343   -194       C  
ATOM   2813  O   PHE A 407       3.590  26.865  13.944  1.00 59.99           O  
ANISOU 2813  O   PHE A 407     7037   8076   7681   -379    382   -181       O  
ATOM   2814  CB  PHE A 407       3.051  29.691  13.219  1.00 55.06           C  
ANISOU 2814  CB  PHE A 407     6398   7474   7048   -355    361   -265       C  
ATOM   2815  CG  PHE A 407       3.275  31.171  13.227  1.00 52.51           C  
ANISOU 2815  CG  PHE A 407     6079   7172   6699   -350    355   -285       C  
ATOM   2816  CD1 PHE A 407       3.693  31.817  14.389  1.00 54.59           C  
ANISOU 2816  CD1 PHE A 407     6361   7467   6915   -380    378   -274       C  
ATOM   2817  CD2 PHE A 407       3.099  31.918  12.071  1.00 50.33           C  
ANISOU 2817  CD2 PHE A 407     5788   6886   6449   -313    324   -316       C  
ATOM   2818  CE1 PHE A 407       3.920  33.189  14.400  1.00 52.74           C  
ANISOU 2818  CE1 PHE A 407     6127   7248   6663   -375    372   -295       C  
ATOM   2819  CE2 PHE A 407       3.323  33.288  12.072  1.00 50.64           C  
ANISOU 2819  CE2 PHE A 407     5830   6940   6470   -308    320   -332       C  
ATOM   2820  CZ  PHE A 407       3.735  33.924  13.238  1.00 52.01           C  
ANISOU 2820  CZ  PHE A 407     6019   7141   6601   -340    344   -323       C  
ATOM   2821  N   HIS A 408       4.344  26.739  11.805  1.00 56.17           N  
ANISOU 2821  N   HIS A 408     6543   7574   7223   -313    308   -192       N  
ATOM   2822  CA  HIS A 408       4.112  25.307  11.584  1.00 56.92           C  
ANISOU 2822  CA  HIS A 408     6626   7640   7363   -312    311   -180       C  
ATOM   2823  C   HIS A 408       4.727  24.431  12.646  1.00 57.79           C  
ANISOU 2823  C   HIS A 408     6757   7756   7446   -341    333   -123       C  
ATOM   2824  O   HIS A 408       5.733  24.787  13.268  1.00 56.28           O  
ANISOU 2824  O   HIS A 408     6595   7594   7196   -351    330    -85       O  
ATOM   2825  CB  HIS A 408       4.666  24.939  10.228  1.00 54.69           C  
ANISOU 2825  CB  HIS A 408     6337   7346   7097   -269    264   -184       C  
ATOM   2826  CG  HIS A 408       4.047  23.715   9.610  1.00 55.82           C  
ANISOU 2826  CG  HIS A 408     6450   7453   7305   -258    260   -202       C  
ATOM   2827  ND1 HIS A 408       4.151  22.489  10.159  1.00 55.78           N  
ANISOU 2827  ND1 HIS A 408     6444   7429   7319   -278    280   -169       N  
ATOM   2828  CD2 HIS A 408       3.354  23.552   8.400  1.00 54.18           C  
ANISOU 2828  CD2 HIS A 408     6213   7225   7149   -225    235   -252       C  
ATOM   2829  CE1 HIS A 408       3.543  21.587   9.355  1.00 56.24           C  
ANISOU 2829  CE1 HIS A 408     6471   7453   7444   -260    269   -199       C  
ATOM   2830  NE2 HIS A 408       3.067  22.241   8.274  1.00 54.52           N  
ANISOU 2830  NE2 HIS A 408     6234   7236   7243   -227    241   -252       N  
ATOM   2831  N   HIS A 409       4.113  23.277  12.874  1.00 59.86           N  
ANISOU 2831  N   HIS A 409     7002   7988   7754   -355    357   -117       N  
ATOM   2832  CA  HIS A 409       4.548  22.371  13.938  1.00 63.05           C  
ANISOU 2832  CA  HIS A 409     7423   8393   8139   -383    384    -59       C  
ATOM   2833  C   HIS A 409       5.684  21.467  13.500  1.00 59.81           C  
ANISOU 2833  C   HIS A 409     7024   7975   7725   -365    353    -15       C  
ATOM   2834  O   HIS A 409       6.383  20.904  14.337  1.00 56.39           O  
ANISOU 2834  O   HIS A 409     6613   7552   7261   -382    365     41       O  
ATOM   2835  CB  HIS A 409       3.363  21.570  14.496  1.00 65.53           C  
ANISOU 2835  CB  HIS A 409     7715   8677   8507   -409    431    -67       C  
ATOM   2836  CG  HIS A 409       2.714  20.659  13.480  1.00 71.35           C  
ANISOU 2836  CG  HIS A 409     8414   9368   9327   -389    419    -99       C  
ATOM   2837  ND1 HIS A 409       2.810  19.312  13.546  1.00 75.43           N  
ANISOU 2837  ND1 HIS A 409     8922   9854   9885   -393    428    -68       N  
ATOM   2838  CD2 HIS A 409       1.962  20.948  12.333  1.00 72.70           C  
ANISOU 2838  CD2 HIS A 409     8554   9521   9549   -361    395   -163       C  
ATOM   2839  CE1 HIS A 409       2.148  18.763  12.501  1.00 75.63           C  
ANISOU 2839  CE1 HIS A 409     8910   9842   9985   -371    412   -114       C  
ATOM   2840  NE2 HIS A 409       1.632  19.766  11.758  1.00 76.49           N  
ANISOU 2840  NE2 HIS A 409     9006   9961  10097   -350    391   -172       N  
ATOM   2841  N   GLU A 410       5.884  21.331  12.191  1.00 57.66           N  
ANISOU 2841  N   GLU A 410     6737   7688   7484   -328    313    -41       N  
ATOM   2842  CA  GLU A 410       7.047  20.613  11.663  1.00 57.56           C  
ANISOU 2842  CA  GLU A 410     6735   7672   7466   -307    280     -5       C  
ATOM   2843  C   GLU A 410       8.262  21.528  11.454  1.00 53.85           C  
ANISOU 2843  C   GLU A 410     6293   7237   6932   -291    248     12       C  
ATOM   2844  O   GLU A 410       8.239  22.462  10.631  1.00 50.86           O  
ANISOU 2844  O   GLU A 410     5910   6868   6546   -266    224    -24       O  
ATOM   2845  CB  GLU A 410       6.684  19.875  10.381  1.00 60.23           C  
ANISOU 2845  CB  GLU A 410     7040   7975   7869   -276    254    -41       C  
ATOM   2846  CG  GLU A 410       5.771  18.689  10.641  1.00 67.48           C  
ANISOU 2846  CG  GLU A 410     7930   8853   8856   -293    284    -46       C  
ATOM   2847  CD  GLU A 410       5.299  18.021   9.368  1.00 73.33           C  
ANISOU 2847  CD  GLU A 410     8634   9561   9667   -262    259    -93       C  
ATOM   2848  OE1 GLU A 410       5.673  18.477   8.270  1.00 75.20           O  
ANISOU 2848  OE1 GLU A 410     8870   9810   9893   -226    218   -120       O  
ATOM   2849  OE2 GLU A 410       4.541  17.033   9.464  1.00 86.27           O  
ANISOU 2849  OE2 GLU A 410    10244  11162  11372   -273    281   -104       O  
ATOM   2850  N   TRP A 411       9.327  21.235  12.201  1.00 53.71           N  
ANISOU 2850  N   TRP A 411     6302   7236   6871   -304    248     68       N  
ATOM   2851  CA  TRP A 411      10.520  22.092  12.241  1.00 50.25           C  
ANISOU 2851  CA  TRP A 411     5890   6832   6371   -295    223     88       C  
ATOM   2852  C   TRP A 411      11.137  22.328  10.888  1.00 48.45           C  
ANISOU 2852  C   TRP A 411     5657   6601   6151   -255    181     70       C  
ATOM   2853  O   TRP A 411      11.502  23.451  10.563  1.00 48.93           O  
ANISOU 2853  O   TRP A 411     5727   6684   6182   -242    166     55       O  
ATOM   2854  CB  TRP A 411      11.525  21.594  13.273  1.00 52.72           C  
ANISOU 2854  CB  TRP A 411     6229   7161   6641   -315    228    150       C  
ATOM   2855  CG  TRP A 411      12.308  20.371  12.867  1.00 55.50           C  
ANISOU 2855  CG  TRP A 411     6580   7492   7018   -301    207    187       C  
ATOM   2856  CD1 TRP A 411      12.045  19.044  13.192  1.00 55.80           C  
ANISOU 2856  CD1 TRP A 411     6607   7499   7094   -312    224    215       C  
ATOM   2857  CD2 TRP A 411      13.530  20.331  12.054  1.00 54.30           C  
ANISOU 2857  CD2 TRP A 411     6434   7342   6855   -272    166    200       C  
ATOM   2858  NE1 TRP A 411      12.981  18.210  12.636  1.00 54.18           N  
ANISOU 2858  NE1 TRP A 411     6402   7279   6906   -293    196    242       N  
ATOM   2859  CE2 TRP A 411      13.897  18.915  11.938  1.00 55.14           C  
ANISOU 2859  CE2 TRP A 411     6533   7419   6997   -268    160    233       C  
ATOM   2860  CE3 TRP A 411      14.323  21.293  11.419  1.00 53.68           C  
ANISOU 2860  CE3 TRP A 411     6365   7285   6745   -250    137    187       C  
ATOM   2861  CZ2 TRP A 411      15.018  18.501  11.218  1.00 55.26           C  
ANISOU 2861  CZ2 TRP A 411     6550   7429   7016   -244    125    251       C  
ATOM   2862  CZ3 TRP A 411      15.443  20.864  10.691  1.00 51.81           C  
ANISOU 2862  CZ3 TRP A 411     6132   7043   6511   -225    104    206       C  
ATOM   2863  CH2 TRP A 411      15.782  19.503  10.596  1.00 52.33           C  
ANISOU 2863  CH2 TRP A 411     6190   7082   6610   -222     98    236       C  
ATOM   2864  N   VAL A 412      11.210  21.296  10.059  1.00 47.43           N  
ANISOU 2864  N   VAL A 412     5511   6443   6067   -235    163     69       N  
ATOM   2865  CA  VAL A 412      11.716  21.456   8.698  1.00 47.32           C  
ANISOU 2865  CA  VAL A 412     5491   6428   6062   -194    125     48       C  
ATOM   2866  C   VAL A 412      10.935  22.525   7.929  1.00 48.01           C  
ANISOU 2866  C   VAL A 412     5565   6522   6155   -174    118     -6       C  
ATOM   2867  O   VAL A 412      11.524  23.378   7.257  1.00 48.23           O  
ANISOU 2867  O   VAL A 412     5602   6568   6156   -150     95    -13       O  
ATOM   2868  CB  VAL A 412      11.712  20.115   7.920  1.00 48.49           C  
ANISOU 2868  CB  VAL A 412     5617   6543   6264   -176    110     45       C  
ATOM   2869  CG1 VAL A 412      12.061  20.324   6.444  1.00 44.87           C  
ANISOU 2869  CG1 VAL A 412     5148   6086   5814   -132     72     14       C  
ATOM   2870  CG2 VAL A 412      12.678  19.134   8.574  1.00 48.31           C  
ANISOU 2870  CG2 VAL A 412     5608   6514   6235   -191    111    103       C  
ATOM   2871  N   VAL A 413       9.609  22.479   8.036  1.00 48.91           N  
ANISOU 2871  N   VAL A 413     5658   6620   6307   -185    140    -43       N  
ATOM   2872  CA  VAL A 413       8.741  23.444   7.353  1.00 43.46           C  
ANISOU 2872  CA  VAL A 413     4952   5933   5628   -166    134    -96       C  
ATOM   2873  C   VAL A 413       8.955  24.841   7.936  1.00 42.52           C  
ANISOU 2873  C   VAL A 413     4852   5843   5459   -178    144    -92       C  
ATOM   2874  O   VAL A 413       9.126  25.803   7.192  1.00 42.25           O  
ANISOU 2874  O   VAL A 413     4821   5823   5411   -152    124   -110       O  
ATOM   2875  CB  VAL A 413       7.255  22.998   7.437  1.00 46.96           C  
ANISOU 2875  CB  VAL A 413     5363   6350   6128   -177    156   -137       C  
ATOM   2876  CG1 VAL A 413       6.326  24.007   6.775  1.00 44.41           C  
ANISOU 2876  CG1 VAL A 413     5024   6031   5819   -157    149   -191       C  
ATOM   2877  CG2 VAL A 413       7.072  21.628   6.783  1.00 45.64           C  
ANISOU 2877  CG2 VAL A 413     5172   6151   6016   -163    144   -146       C  
ATOM   2878  N   LYS A 414       8.991  24.943   9.266  1.00 41.01           N  
ANISOU 2878  N   LYS A 414     4676   5664   5242   -217    174    -66       N  
ATOM   2879  CA  LYS A 414       9.220  26.213   9.935  1.00 41.60           C  
ANISOU 2879  CA  LYS A 414     4768   5767   5271   -232    185    -65       C  
ATOM   2880  C   LYS A 414      10.561  26.848   9.506  1.00 42.86           C  
ANISOU 2880  C   LYS A 414     4948   5948   5391   -211    156    -42       C  
ATOM   2881  O   LYS A 414      10.619  28.033   9.147  1.00 40.96           O  
ANISOU 2881  O   LYS A 414     4707   5718   5136   -197    149    -62       O  
ATOM   2882  CB  LYS A 414       9.148  26.027  11.461  1.00 44.63           C  
ANISOU 2882  CB  LYS A 414     5165   6163   5628   -276    222    -38       C  
ATOM   2883  CG  LYS A 414       9.474  27.278  12.256  1.00 48.31           C  
ANISOU 2883  CG  LYS A 414     5649   6663   6046   -293    233    -39       C  
ATOM   2884  CD  LYS A 414       8.593  27.430  13.487  1.00 53.19           C  
ANISOU 2884  CD  LYS A 414     6265   7289   6656   -332    276    -48       C  
ATOM   2885  CE  LYS A 414       9.254  26.918  14.749  1.00 58.59           C  
ANISOU 2885  CE  LYS A 414     6972   7994   7294   -361    293      1       C  
ATOM   2886  NZ  LYS A 414       8.256  26.387  15.737  1.00 60.53           N  
ANISOU 2886  NZ  LYS A 414     7213   8235   7550   -394    337      2       N  
ATOM   2887  N   GLU A 415      11.621  26.039   9.516  1.00 41.46           N  
ANISOU 2887  N   GLU A 415     4783   5770   5199   -207    141     -1       N  
ATOM   2888  CA  GLU A 415      12.946  26.483   9.164  1.00 41.31           C  
ANISOU 2888  CA  GLU A 415     4781   5767   5146   -190    116     23       C  
ATOM   2889  C   GLU A 415      12.915  27.091   7.767  1.00 43.10           C  
ANISOU 2889  C   GLU A 415     4998   5989   5388   -149     92     -6       C  
ATOM   2890  O   GLU A 415      13.475  28.173   7.544  1.00 43.28           O  
ANISOU 2890  O   GLU A 415     5030   6028   5387   -137     83     -6       O  
ATOM   2891  CB  GLU A 415      13.927  25.290   9.236  1.00 44.35           C  
ANISOU 2891  CB  GLU A 415     5177   6146   5530   -189    102     68       C  
ATOM   2892  CG  GLU A 415      15.418  25.633   9.213  1.00 42.91           C  
ANISOU 2892  CG  GLU A 415     5014   5982   5309   -180     81    100       C  
ATOM   2893  CD  GLU A 415      15.935  26.084   7.840  1.00 46.23           C  
ANISOU 2893  CD  GLU A 415     5430   6400   5736   -139     53     86       C  
ATOM   2894  OE1 GLU A 415      15.375  25.692   6.791  1.00 44.93           O  
ANISOU 2894  OE1 GLU A 415     5248   6217   5605   -113     42     61       O  
ATOM   2895  OE2 GLU A 415      16.923  26.847   7.806  1.00 49.01           O  
ANISOU 2895  OE2 GLU A 415     5795   6768   6058   -132     43    101       O  
ATOM   2896  N   SER A 416      12.265  26.423   6.817  1.00 41.85           N  
ANISOU 2896  N   SER A 416     4819   5810   5270   -125     80    -30       N  
ATOM   2897  CA  SER A 416      12.224  26.987   5.468  1.00 43.10           C  
ANISOU 2897  CA  SER A 416     4969   5969   5437    -83     55    -57       C  
ATOM   2898  C   SER A 416      11.515  28.349   5.500  1.00 44.93           C  
ANISOU 2898  C   SER A 416     5197   6211   5665    -82     66    -87       C  
ATOM   2899  O   SER A 416      11.930  29.304   4.808  1.00 44.38           O  
ANISOU 2899  O   SER A 416     5132   6152   5580    -56     52    -89       O  
ATOM   2900  CB  SER A 416      11.530  26.035   4.491  1.00 43.96           C  
ANISOU 2900  CB  SER A 416     5055   6058   5592    -58     40    -86       C  
ATOM   2901  OG  SER A 416      10.164  25.868   4.838  1.00 43.99           O  
ANISOU 2901  OG  SER A 416     5037   6046   5630    -74     60   -120       O  
ATOM   2902  N   GLY A 417      10.468  28.451   6.324  1.00 43.20           N  
ANISOU 2902  N   GLY A 417     4968   5986   5460   -111     93   -108       N  
ATOM   2903  CA  GLY A 417       9.699  29.701   6.417  1.00 42.84           C  
ANISOU 2903  CA  GLY A 417     4914   5945   5416   -113    105   -140       C  
ATOM   2904  C   GLY A 417      10.580  30.849   6.876  1.00 45.47           C  
ANISOU 2904  C   GLY A 417     5267   6300   5710   -121    109   -121       C  
ATOM   2905  O   GLY A 417      10.540  31.950   6.313  1.00 46.02           O  
ANISOU 2905  O   GLY A 417     5333   6374   5779   -100    102   -136       O  
ATOM   2906  N   ILE A 418      11.403  30.578   7.884  1.00 43.12           N  
ANISOU 2906  N   ILE A 418     4988   6016   5382   -150    119    -86       N  
ATOM   2907  CA  ILE A 418      12.310  31.571   8.423  1.00 42.15           C  
ANISOU 2907  CA  ILE A 418     4880   5913   5222   -160    122    -69       C  
ATOM   2908  C   ILE A 418      13.324  31.980   7.347  1.00 43.12           C  
ANISOU 2908  C   ILE A 418     5009   6037   5337   -123     95    -54       C  
ATOM   2909  O   ILE A 418      13.642  33.168   7.184  1.00 41.55           O  
ANISOU 2909  O   ILE A 418     4812   5846   5130   -114     95    -60       O  
ATOM   2910  CB  ILE A 418      13.007  31.041   9.684  1.00 42.28           C  
ANISOU 2910  CB  ILE A 418     4915   5945   5205   -195    134    -35       C  
ATOM   2911  CG1 ILE A 418      11.946  30.704  10.735  1.00 39.16           C  
ANISOU 2911  CG1 ILE A 418     4514   5550   4816   -231    166    -49       C  
ATOM   2912  CG2 ILE A 418      14.035  32.054  10.187  1.00 42.16           C  
ANISOU 2912  CG2 ILE A 418     4913   5952   5154   -203    133    -22       C  
ATOM   2913  CD1 ILE A 418      12.464  30.178  12.058  1.00 41.35           C  
ANISOU 2913  CD1 ILE A 418     4809   5846   5057   -265    181    -15       C  
ATOM   2914  N   LEU A 419      13.791  30.991   6.595  1.00 40.83           N  
ANISOU 2914  N   LEU A 419     4721   5738   5053   -101     74    -37       N  
ATOM   2915  CA  LEU A 419      14.681  31.240   5.485  1.00 39.98           C  
ANISOU 2915  CA  LEU A 419     4618   5631   4940    -64     50    -23       C  
ATOM   2916  C   LEU A 419      14.054  32.212   4.501  1.00 40.66           C  
ANISOU 2916  C   LEU A 419     4692   5714   5042    -32     45    -52       C  
ATOM   2917  O   LEU A 419      14.635  33.250   4.198  1.00 41.85           O  
ANISOU 2917  O   LEU A 419     4848   5872   5181    -18     43    -45       O  
ATOM   2918  CB  LEU A 419      15.098  29.925   4.794  1.00 39.00           C  
ANISOU 2918  CB  LEU A 419     4494   5498   4826    -45     30     -8       C  
ATOM   2919  CG  LEU A 419      15.921  30.070   3.511  1.00 41.59           C  
ANISOU 2919  CG  LEU A 419     4825   5828   5150     -2      6      2       C  
ATOM   2920  CD1 LEU A 419      17.203  30.873   3.759  1.00 38.70           C  
ANISOU 2920  CD1 LEU A 419     4475   5474   4754     -5      6     31       C  
ATOM   2921  CD2 LEU A 419      16.243  28.701   2.924  1.00 40.13           C  
ANISOU 2921  CD2 LEU A 419     4636   5633   4978     13    -12     11       C  
ATOM   2922  N   VAL A 420      12.863  31.876   4.011  1.00 43.99           N  
ANISOU 2922  N   VAL A 420     5096   6125   5493    -20     43    -85       N  
ATOM   2923  CA  VAL A 420      12.109  32.757   3.111  1.00 41.35           C  
ANISOU 2923  CA  VAL A 420     4749   5788   5175     12     36   -115       C  
ATOM   2924  C   VAL A 420      12.038  34.189   3.631  1.00 39.83           C  
ANISOU 2924  C   VAL A 420     4558   5601   4977     -1     54   -120       C  
ATOM   2925  O   VAL A 420      12.296  35.155   2.900  1.00 39.46           O  
ANISOU 2925  O   VAL A 420     4510   5556   4927     28     47   -118       O  
ATOM   2926  CB  VAL A 420      10.668  32.241   2.929  1.00 41.99           C  
ANISOU 2926  CB  VAL A 420     4807   5855   5292     14     37   -155       C  
ATOM   2927  CG1 VAL A 420       9.844  33.267   2.157  1.00 42.53           C  
ANISOU 2927  CG1 VAL A 420     4861   5922   5376     43     31   -186       C  
ATOM   2928  CG2 VAL A 420      10.672  30.912   2.189  1.00 40.32           C  
ANISOU 2928  CG2 VAL A 420     4589   5637   5095     34     17   -158       C  
ATOM   2929  N   LEU A 421      11.687  34.306   4.905  1.00 38.39           N  
ANISOU 2929  N   LEU A 421     4375   5421   4792    -44     79   -128       N  
ATOM   2930  CA  LEU A 421      11.530  35.586   5.540  1.00 38.53           C  
ANISOU 2930  CA  LEU A 421     4390   5444   4807    -61     98   -140       C  
ATOM   2931  C   LEU A 421      12.842  36.356   5.441  1.00 40.96           C  
ANISOU 2931  C   LEU A 421     4711   5760   5091    -53     93   -111       C  
ATOM   2932  O   LEU A 421      12.849  37.575   5.237  1.00 41.18           O  
ANISOU 2932  O   LEU A 421     4733   5786   5127    -43     99   -120       O  
ATOM   2933  CB  LEU A 421      11.124  35.388   7.010  1.00 38.27           C  
ANISOU 2933  CB  LEU A 421     4357   5417   4767   -111    125   -149       C  
ATOM   2934  CG  LEU A 421      10.975  36.672   7.818  1.00 41.59           C  
ANISOU 2934  CG  LEU A 421     4774   5846   5184   -134    147   -167       C  
ATOM   2935  CD1 LEU A 421       9.967  37.603   7.150  1.00 43.06           C  
ANISOU 2935  CD1 LEU A 421     4939   6018   5405   -112    149   -203       C  
ATOM   2936  CD2 LEU A 421      10.553  36.383   9.255  1.00 42.52           C  
ANISOU 2936  CD2 LEU A 421     4893   5975   5289   -181    175   -177       C  
ATOM   2937  N   GLY A 422      13.951  35.635   5.618  1.00 40.62           N  
ANISOU 2937  N   GLY A 422     4684   5725   5025    -58     84    -78       N  
ATOM   2938  CA  GLY A 422      15.265  36.222   5.506  1.00 40.95           C  
ANISOU 2938  CA  GLY A 422     4737   5773   5048    -50     79    -50       C  
ATOM   2939  C   GLY A 422      15.581  36.532   4.069  1.00 41.02           C  
ANISOU 2939  C   GLY A 422     4745   5775   5066     -3     61    -41       C  
ATOM   2940  O   GLY A 422      15.986  37.651   3.755  1.00 42.66           O  
ANISOU 2940  O   GLY A 422     4951   5981   5277     11     66    -36       O  
ATOM   2941  N   ALA A 423      15.366  35.561   3.190  1.00 39.32           N  
ANISOU 2941  N   ALA A 423     4529   5556   4856     23     43    -39       N  
ATOM   2942  CA  ALA A 423      15.673  35.752   1.772  1.00 43.02           C  
ANISOU 2942  CA  ALA A 423     4998   6022   5326     72     26    -30       C  
ATOM   2943  C   ALA A 423      15.035  37.012   1.188  1.00 45.40           C  
ANISOU 2943  C   ALA A 423     5288   6319   5642     96     31    -46       C  
ATOM   2944  O   ALA A 423      15.687  37.757   0.468  1.00 47.98           O  
ANISOU 2944  O   ALA A 423     5619   6645   5965    124     29    -27       O  
ATOM   2945  CB  ALA A 423      15.287  34.519   0.961  1.00 40.92           C  
ANISOU 2945  CB  ALA A 423     4728   5754   5066     95      5    -38       C  
ATOM   2946  N   ILE A 424      13.768  37.268   1.513  1.00 47.67           N  
ANISOU 2946  N   ILE A 424     5561   6601   5951     85     39    -81       N  
ATOM   2947  CA  ILE A 424      13.051  38.378   0.872  1.00 47.08           C  
ANISOU 2947  CA  ILE A 424     5474   6519   5895    112     41    -98       C  
ATOM   2948  C   ILE A 424      13.342  39.723   1.523  1.00 47.75           C  
ANISOU 2948  C   ILE A 424     5556   6600   5986     93     63    -95       C  
ATOM   2949  O   ILE A 424      12.896  40.756   1.010  1.00 49.68           O  
ANISOU 2949  O   ILE A 424     5790   6836   6249    116     66   -103       O  
ATOM   2950  CB  ILE A 424      11.512  38.166   0.869  1.00 47.78           C  
ANISOU 2950  CB  ILE A 424     5543   6601   6009    111     39   -140       C  
ATOM   2951  CG1 ILE A 424      10.980  38.160   2.313  1.00 46.82           C  
ANISOU 2951  CG1 ILE A 424     5416   6477   5896     58     64   -161       C  
ATOM   2952  CG2 ILE A 424      11.148  36.899   0.105  1.00 43.51           C  
ANISOU 2952  CG2 ILE A 424     5000   6062   5470    134     16   -149       C  
ATOM   2953  CD1 ILE A 424       9.473  38.238   2.455  1.00 50.08           C  
ANISOU 2953  CD1 ILE A 424     5808   6881   6341     53     70   -205       C  
ATOM   2954  N   ALA A 425      14.064  39.713   2.648  1.00 45.28           N  
ANISOU 2954  N   ALA A 425     5252   6293   5660     54     77    -85       N  
ATOM   2955  CA  ALA A 425      14.258  40.928   3.453  1.00 47.73           C  
ANISOU 2955  CA  ALA A 425     5555   6600   5979     30     99    -92       C  
ATOM   2956  C   ALA A 425      14.725  42.153   2.650  1.00 49.22           C  
ANISOU 2956  C   ALA A 425     5740   6778   6183     62    102    -76       C  
ATOM   2957  O   ALA A 425      14.177  43.240   2.805  1.00 56.02           O  
ANISOU 2957  O   ALA A 425     6586   7628   7070     60    116    -95       O  
ATOM   2958  CB  ALA A 425      15.184  40.666   4.638  1.00 43.80           C  
ANISOU 2958  CB  ALA A 425     5069   6115   5459    -11    108    -80       C  
ATOM   2959  N   GLU A 426      15.716  41.987   1.789  1.00 50.48           N  
ANISOU 2959  N   GLU A 426     5912   6939   6329     92     90    -42       N  
ATOM   2960  CA  GLU A 426      16.278  43.143   1.085  1.00 53.57           C  
ANISOU 2960  CA  GLU A 426     6300   7319   6736    120     98    -21       C  
ATOM   2961  C   GLU A 426      15.264  43.754   0.125  1.00 51.86           C  
ANISOU 2961  C   GLU A 426     6072   7093   6541    158     94    -31       C  
ATOM   2962  O   GLU A 426      15.005  44.945   0.181  1.00 53.86           O  
ANISOU 2962  O   GLU A 426     6312   7332   6821    161    110    -37       O  
ATOM   2963  CB  GLU A 426      17.574  42.772   0.355  1.00 54.90           C  
ANISOU 2963  CB  GLU A 426     6483   7491   6884    144     89     20       C  
ATOM   2964  CG  GLU A 426      18.392  43.961  -0.142  1.00 57.94           C  
ANISOU 2964  CG  GLU A 426     6866   7864   7286    165    104     46       C  
ATOM   2965  CD  GLU A 426      19.498  43.571  -1.128  1.00 60.76           C  
ANISOU 2965  CD  GLU A 426     7236   8224   7625    198     96     86       C  
ATOM   2966  OE1 GLU A 426      19.570  42.408  -1.582  1.00 58.30           O  
ANISOU 2966  OE1 GLU A 426     6937   7927   7289    210     77     91       O  
ATOM   2967  OE2 GLU A 426      20.310  44.440  -1.469  1.00 65.01           O  
ANISOU 2967  OE2 GLU A 426     7773   8751   8177    212    111    111       O  
ATOM   2968  N   GLY A 427      14.686  42.929  -0.742  1.00 50.14           N  
ANISOU 2968  N   GLY A 427     5857   6883   6311    188     73    -34       N  
ATOM   2969  CA  GLY A 427      13.676  43.395  -1.696  1.00 52.06           C  
ANISOU 2969  CA  GLY A 427     6089   7121   6570    229     64    -45       C  
ATOM   2970  C   GLY A 427      12.399  43.991  -1.108  1.00 52.71           C  
ANISOU 2970  C   GLY A 427     6151   7192   6684    210     73    -85       C  
ATOM   2971  O   GLY A 427      11.936  45.035  -1.553  1.00 53.40           O  
ANISOU 2971  O   GLY A 427     6226   7267   6796    233     78    -86       O  
ATOM   2972  N   CYS A 428      11.858  43.352  -0.079  1.00 49.96           N  
ANISOU 2972  N   CYS A 428     5799   6847   6338    168     78   -116       N  
ATOM   2973  CA  CYS A 428      10.504  43.628   0.384  1.00 49.71           C  
ANISOU 2973  CA  CYS A 428     5746   6807   6334    153     84   -159       C  
ATOM   2974  C   CYS A 428      10.496  44.412   1.668  1.00 50.57           C  
ANISOU 2974  C   CYS A 428     5845   6908   6459    107    112   -177       C  
ATOM   2975  O   CYS A 428       9.483  44.466   2.377  1.00 53.35           O  
ANISOU 2975  O   CYS A 428     6182   7257   6831     81    123   -215       O  
ATOM   2976  CB  CYS A 428       9.776  42.303   0.594  1.00 46.50           C  
ANISOU 2976  CB  CYS A 428     5339   6409   5922    140     72   -184       C  
ATOM   2977  SG  CYS A 428       9.735  41.349  -0.935  1.00 48.07           S  
ANISOU 2977  SG  CYS A 428     5544   6617   6104    195     37   -172       S  
ATOM   2978  N   MET A 429      11.633  45.021   1.966  1.00 51.79           N  
ANISOU 2978  N   MET A 429     6008   7062   6607     98    124   -151       N  
ATOM   2979  CA  MET A 429      11.842  45.607   3.266  1.00 50.27           C  
ANISOU 2979  CA  MET A 429     5808   6869   6422     51    149   -169       C  
ATOM   2980  C   MET A 429      10.718  46.576   3.617  1.00 51.54           C  
ANISOU 2980  C   MET A 429     5944   7015   6623     42    164   -208       C  
ATOM   2981  O   MET A 429      10.154  46.507   4.722  1.00 48.85           O  
ANISOU 2981  O   MET A 429     5594   6679   6286      1    180   -243       O  
ATOM   2982  CB  MET A 429      13.188  46.321   3.317  1.00 49.34           C  
ANISOU 2982  CB  MET A 429     5697   6748   6303     52    158   -140       C  
ATOM   2983  CG  MET A 429      13.464  46.929   4.672  1.00 50.28           C  
ANISOU 2983  CG  MET A 429     5805   6869   6429      5    180   -163       C  
ATOM   2984  SD  MET A 429      13.718  45.601   5.863  1.00 54.94           S  
ANISOU 2984  SD  MET A 429     6413   7487   6974    -40    178   -169       S  
ATOM   2985  CE  MET A 429      13.286  46.461   7.359  1.00 56.18           C  
ANISOU 2985  CE  MET A 429     6552   7649   7146    -89    205   -215       C  
ATOM   2986  N   GLN A 430      10.398  47.475   2.684  1.00 52.11           N  
ANISOU 2986  N   GLN A 430     6004   7069   6725     81    161   -202       N  
ATOM   2987  CA  GLN A 430       9.390  48.511   2.952  1.00 58.50           C  
ANISOU 2987  CA  GLN A 430     6788   7861   7580     75    176   -237       C  
ATOM   2988  C   GLN A 430       8.057  47.862   3.288  1.00 57.07           C  
ANISOU 2988  C   GLN A 430     6596   7684   7405     61    172   -278       C  
ATOM   2989  O   GLN A 430       7.440  48.173   4.309  1.00 56.34           O  
ANISOU 2989  O   GLN A 430     6488   7589   7331     23    192   -317       O  
ATOM   2990  CB  GLN A 430       9.241  49.485   1.774  1.00 62.05           C  
ANISOU 2990  CB  GLN A 430     7227   8291   8059    125    170   -216       C  
ATOM   2991  CG  GLN A 430      10.457  50.380   1.564  1.00 71.38           C  
ANISOU 2991  CG  GLN A 430     8412   9461   9249    136    183   -179       C  
ATOM   2992  CD  GLN A 430      11.020  50.923   2.875  1.00 76.68           C  
ANISOU 2992  CD  GLN A 430     9074  10129   9931     86    208   -199       C  
ATOM   2993  OE1 GLN A 430      10.344  51.665   3.595  1.00 76.57           O  
ANISOU 2993  OE1 GLN A 430     9037  10104   9951     62    226   -238       O  
ATOM   2994  NE2 GLN A 430      12.265  50.548   3.192  1.00 72.69           N  
ANISOU 2994  NE2 GLN A 430     8585   9636   9396     71    210   -176       N  
ATOM   2995  N   GLY A 431       7.654  46.914   2.450  1.00 53.89           N  
ANISOU 2995  N   GLY A 431     6200   7287   6986     89    147   -272       N  
ATOM   2996  CA  GLY A 431       6.416  46.204   2.659  1.00 52.99           C  
ANISOU 2996  CA  GLY A 431     6075   7175   6883     79    143   -310       C  
ATOM   2997  C   GLY A 431       6.335  45.373   3.923  1.00 53.48           C  
ANISOU 2997  C   GLY A 431     6142   7250   6928     26    159   -330       C  
ATOM   2998  O   GLY A 431       5.240  45.066   4.362  1.00 57.51           O  
ANISOU 2998  O   GLY A 431     6637   7757   7457      8    166   -368       O  
ATOM   2999  N   MET A 432       7.470  45.001   4.517  1.00 51.90           N  
ANISOU 2999  N   MET A 432     5962   7064   6692      2    166   -305       N  
ATOM   3000  CA  MET A 432       7.449  44.122   5.696  1.00 50.06           C  
ANISOU 3000  CA  MET A 432     5737   6846   6437    -44    180   -316       C  
ATOM   3001  C   MET A 432       7.385  44.864   7.020  1.00 50.06           C  
ANISOU 3001  C   MET A 432     5727   6850   6442    -90    210   -342       C  
ATOM   3002  O   MET A 432       6.996  44.289   8.051  1.00 50.38           O  
ANISOU 3002  O   MET A 432     5769   6902   6470   -129    227   -362       O  
ATOM   3003  CB  MET A 432       8.669  43.202   5.706  1.00 50.80           C  
ANISOU 3003  CB  MET A 432     5858   6957   6489    -47    168   -276       C  
ATOM   3004  CG  MET A 432       8.700  42.139   4.626  1.00 50.27           C  
ANISOU 3004  CG  MET A 432     5800   6890   6411    -12    141   -256       C  
ATOM   3005  SD  MET A 432       7.472  40.828   4.811  1.00 54.74           S  
ANISOU 3005  SD  MET A 432     6357   7454   6987    -25    138   -286       S  
ATOM   3006  CE  MET A 432       7.583  40.420   6.557  1.00 48.59           C  
ANISOU 3006  CE  MET A 432     5585   6689   6188    -88    169   -293       C  
ATOM   3007  N   ILE A 433       7.785  46.133   6.993  1.00 52.61           N  
ANISOU 3007  N   ILE A 433     6040   7164   6784    -84    219   -343       N  
ATOM   3008  CA  ILE A 433       7.790  46.988   8.182  1.00 54.53           C  
ANISOU 3008  CA  ILE A 433     6271   7411   7036   -123    247   -372       C  
ATOM   3009  C   ILE A 433       6.527  46.801   9.038  1.00 55.48           C  
ANISOU 3009  C   ILE A 433     6376   7534   7170   -156    267   -419       C  
ATOM   3010  O   ILE A 433       6.627  46.525  10.243  1.00 56.02           O  
ANISOU 3010  O   ILE A 433     6450   7623   7214   -198    287   -433       O  
ATOM   3011  CB  ILE A 433       7.933  48.482   7.816  1.00 57.86           C  
ANISOU 3011  CB  ILE A 433     6673   7811   7499   -106    253   -377       C  
ATOM   3012  CG1 ILE A 433       9.100  48.713   6.841  1.00 61.73           C  
ANISOU 3012  CG1 ILE A 433     7177   8295   7982    -69    237   -329       C  
ATOM   3013  CG2 ILE A 433       8.050  49.331   9.076  1.00 58.64           C  
ANISOU 3013  CG2 ILE A 433     6758   7916   7608   -147    281   -411       C  
ATOM   3014  CD1 ILE A 433      10.433  49.055   7.477  1.00 60.96           C  
ANISOU 3014  CD1 ILE A 433     7088   8207   7867    -89    245   -313       C  
ATOM   3015  N   PRO A 434       5.332  46.916   8.418  1.00 55.21           N  
ANISOU 3015  N   PRO A 434     6323   7481   7174   -136    263   -443       N  
ATOM   3016  CA  PRO A 434       4.094  46.743   9.197  1.00 52.21           C  
ANISOU 3016  CA  PRO A 434     5925   7100   6811   -167    284   -490       C  
ATOM   3017  C   PRO A 434       4.074  45.446  10.012  1.00 53.03           C  
ANISOU 3017  C   PRO A 434     6046   7226   6878   -200    294   -486       C  
ATOM   3018  O   PRO A 434       3.526  45.419  11.117  1.00 49.74           O  
ANISOU 3018  O   PRO A 434     5622   6820   6459   -240    322   -517       O  
ATOM   3019  CB  PRO A 434       3.008  46.689   8.124  1.00 52.96           C  
ANISOU 3019  CB  PRO A 434     6003   7174   6947   -129    266   -504       C  
ATOM   3020  CG  PRO A 434       3.588  47.367   6.923  1.00 54.03           C  
ANISOU 3020  CG  PRO A 434     6140   7296   7092    -81    242   -473       C  
ATOM   3021  CD  PRO A 434       5.064  47.131   6.980  1.00 53.50           C  
ANISOU 3021  CD  PRO A 434     6100   7245   6982    -83    237   -428       C  
ATOM   3022  N   TYR A 435       4.688  44.386   9.488  1.00 53.03           N  
ANISOU 3022  N   TYR A 435     6069   7234   6848   -183    272   -447       N  
ATOM   3023  CA  TYR A 435       4.646  43.073  10.143  1.00 51.12           C  
ANISOU 3023  CA  TYR A 435     5842   7007   6575   -210    279   -438       C  
ATOM   3024  C   TYR A 435       5.758  42.821  11.165  1.00 50.72           C  
ANISOU 3024  C   TYR A 435     5814   6983   6474   -242    290   -413       C  
ATOM   3025  O   TYR A 435       5.718  41.835  11.917  1.00 50.48           O  
ANISOU 3025  O   TYR A 435     5796   6967   6417   -269    301   -405       O  
ATOM   3026  CB  TYR A 435       4.646  41.976   9.083  1.00 53.13           C  
ANISOU 3026  CB  TYR A 435     6104   7253   6828   -177    250   -414       C  
ATOM   3027  CG  TYR A 435       3.555  42.140   8.051  1.00 52.91           C  
ANISOU 3027  CG  TYR A 435     6055   7204   6846   -143    235   -440       C  
ATOM   3028  CD1 TYR A 435       2.228  41.790   8.349  1.00 55.27           C  
ANISOU 3028  CD1 TYR A 435     6331   7491   7176   -158    250   -481       C  
ATOM   3029  CD2 TYR A 435       3.837  42.632   6.782  1.00 53.30           C  
ANISOU 3029  CD2 TYR A 435     6103   7243   6907    -95    207   -425       C  
ATOM   3030  CE1 TYR A 435       1.213  41.936   7.409  1.00 54.18           C  
ANISOU 3030  CE1 TYR A 435     6170   7334   7082   -125    233   -509       C  
ATOM   3031  CE2 TYR A 435       2.833  42.773   5.827  1.00 54.22           C  
ANISOU 3031  CE2 TYR A 435     6198   7342   7060    -60    190   -449       C  
ATOM   3032  CZ  TYR A 435       1.517  42.427   6.151  1.00 56.58           C  
ANISOU 3032  CZ  TYR A 435     6475   7631   7393    -75    201   -492       C  
ATOM   3033  OH  TYR A 435       0.500  42.572   5.224  1.00 54.09           O  
ANISOU 3033  OH  TYR A 435     6136   7299   7117    -40    182   -520       O  
ATOM   3034  N   LEU A 436       6.740  43.712  11.213  1.00 49.43           N  
ANISOU 3034  N   LEU A 436     5654   6825   6300   -238    286   -401       N  
ATOM   3035  CA  LEU A 436       7.910  43.469  12.043  1.00 49.94           C  
ANISOU 3035  CA  LEU A 436     5741   6916   6319   -261    289   -376       C  
ATOM   3036  C   LEU A 436       7.641  43.521  13.534  1.00 52.41           C  
ANISOU 3036  C   LEU A 436     6052   7253   6608   -309    320   -402       C  
ATOM   3037  O   LEU A 436       8.250  42.751  14.289  1.00 54.38           O  
ANISOU 3037  O   LEU A 436     6322   7527   6813   -330    322   -379       O  
ATOM   3038  CB  LEU A 436       9.083  44.374  11.657  1.00 50.55           C  
ANISOU 3038  CB  LEU A 436     5821   6991   6395   -243    276   -357       C  
ATOM   3039  CG  LEU A 436       9.628  44.091  10.249  1.00 50.71           C  
ANISOU 3039  CG  LEU A 436     5851   6996   6423   -197    246   -319       C  
ATOM   3040  CD1 LEU A 436      10.682  45.115   9.845  1.00 50.59           C  
ANISOU 3040  CD1 LEU A 436     5834   6974   6416   -179    240   -303       C  
ATOM   3041  CD2 LEU A 436      10.161  42.671  10.104  1.00 52.09           C  
ANISOU 3041  CD2 LEU A 436     6049   7181   6562   -194    229   -283       C  
ATOM   3042  N   PRO A 437       6.716  44.397  13.975  1.00 52.55           N  
ANISOU 3042  N   PRO A 437     6045   7264   6656   -325    343   -450       N  
ATOM   3043  CA  PRO A 437       6.405  44.387  15.406  1.00 51.47           C  
ANISOU 3043  CA  PRO A 437     5909   7155   6494   -370    375   -477       C  
ATOM   3044  C   PRO A 437       5.907  43.033  15.907  1.00 53.30           C  
ANISOU 3044  C   PRO A 437     6154   7398   6699   -389    387   -464       C  
ATOM   3045  O   PRO A 437       6.019  42.747  17.109  1.00 53.08           O  
ANISOU 3045  O   PRO A 437     6136   7400   6630   -424    409   -466       O  
ATOM   3046  CB  PRO A 437       5.312  45.453  15.528  1.00 51.22           C  
ANISOU 3046  CB  PRO A 437     5845   7108   6510   -377    397   -532       C  
ATOM   3047  CG  PRO A 437       5.631  46.421  14.436  1.00 51.23           C  
ANISOU 3047  CG  PRO A 437     5834   7082   6552   -339    376   -528       C  
ATOM   3048  CD  PRO A 437       6.120  45.568  13.295  1.00 52.22           C  
ANISOU 3048  CD  PRO A 437     5978   7196   6669   -303    343   -479       C  
ATOM   3049  N   GLU A 438       5.380  42.200  15.005  1.00 51.14           N  
ANISOU 3049  N   GLU A 438     5881   7102   6449   -366    373   -449       N  
ATOM   3050  CA  GLU A 438       4.994  40.831  15.381  1.00 53.91           C  
ANISOU 3050  CA  GLU A 438     6244   7459   6782   -382    383   -432       C  
ATOM   3051  C   GLU A 438       6.108  39.809  15.094  1.00 51.21           C  
ANISOU 3051  C   GLU A 438     5929   7125   6405   -370    358   -376       C  
ATOM   3052  O   GLU A 438       6.423  38.977  15.953  1.00 49.40           O  
ANISOU 3052  O   GLU A 438     5717   6916   6135   -394    369   -352       O  
ATOM   3053  CB  GLU A 438       3.684  40.387  14.696  1.00 58.48           C  
ANISOU 3053  CB  GLU A 438     6802   8008   7411   -369    385   -455       C  
ATOM   3054  CG  GLU A 438       3.266  38.949  15.032  1.00 66.44           C  
ANISOU 3054  CG  GLU A 438     7819   9016   8411   -385    398   -437       C  
ATOM   3055  CD  GLU A 438       2.331  38.276  14.007  1.00 74.80           C  
ANISOU 3055  CD  GLU A 438     8859  10042   9520   -360    385   -449       C  
ATOM   3056  OE1 GLU A 438       2.306  38.669  12.813  1.00 80.61           O  
ANISOU 3056  OE1 GLU A 438     9585  10759  10285   -321    355   -455       O  
ATOM   3057  OE2 GLU A 438       1.627  37.312  14.396  1.00 71.58           O  
ANISOU 3057  OE2 GLU A 438     8448   9628   9124   -378    406   -452       O  
ATOM   3058  N   LEU A 439       6.674  39.861  13.885  1.00 48.11           N  
ANISOU 3058  N   LEU A 439     5538   6715   6025   -331    324   -356       N  
ATOM   3059  CA  LEU A 439       7.644  38.851  13.440  1.00 49.04           C  
ANISOU 3059  CA  LEU A 439     5679   6836   6119   -315    298   -307       C  
ATOM   3060  C   LEU A 439       8.948  38.831  14.236  1.00 48.26           C  
ANISOU 3060  C   LEU A 439     5602   6766   5969   -332    295   -276       C  
ATOM   3061  O   LEU A 439       9.433  37.751  14.591  1.00 48.71           O  
ANISOU 3061  O   LEU A 439     5678   6834   5996   -341    291   -241       O  
ATOM   3062  CB  LEU A 439       7.968  39.013  11.962  1.00 48.77           C  
ANISOU 3062  CB  LEU A 439     5640   6780   6109   -268    265   -295       C  
ATOM   3063  CG  LEU A 439       6.803  38.807  11.008  1.00 49.84           C  
ANISOU 3063  CG  LEU A 439     5757   6890   6291   -244    259   -319       C  
ATOM   3064  CD1 LEU A 439       7.237  39.243   9.631  1.00 49.63           C  
ANISOU 3064  CD1 LEU A 439     5728   6850   6279   -197    227   -308       C  
ATOM   3065  CD2 LEU A 439       6.354  37.356  10.998  1.00 49.22           C  
ANISOU 3065  CD2 LEU A 439     5681   6805   6216   -249    259   -309       C  
ATOM   3066  N   ILE A 440       9.508  40.012  14.497  1.00 47.79           N  
ANISOU 3066  N   ILE A 440     5538   6716   5903   -335    296   -290       N  
ATOM   3067  CA  ILE A 440      10.783  40.130  15.230  1.00 48.02           C  
ANISOU 3067  CA  ILE A 440     5585   6774   5888   -348    291   -267       C  
ATOM   3068  C   ILE A 440      10.705  39.476  16.604  1.00 48.96           C  
ANISOU 3068  C   ILE A 440     5718   6924   5962   -387    312   -262       C  
ATOM   3069  O   ILE A 440      11.525  38.602  16.894  1.00 50.14           O  
ANISOU 3069  O   ILE A 440     5888   7088   6075   -390    300   -222       O  
ATOM   3070  CB  ILE A 440      11.299  41.592  15.326  1.00 46.64           C  
ANISOU 3070  CB  ILE A 440     5397   6601   5721   -347    291   -291       C  
ATOM   3071  CG1 ILE A 440      11.580  42.167  13.934  1.00 45.87           C  
ANISOU 3071  CG1 ILE A 440     5291   6475   5663   -306    270   -283       C  
ATOM   3072  CG2 ILE A 440      12.543  41.681  16.202  1.00 49.20           C  
ANISOU 3072  CG2 ILE A 440     5737   6958   6001   -364    286   -275       C  
ATOM   3073  CD1 ILE A 440      12.582  41.376  13.097  1.00 45.89           C  
ANISOU 3073  CD1 ILE A 440     5312   6472   5653   -278    240   -235       C  
ATOM   3074  N   PRO A 441       9.725  39.876  17.452  1.00 50.62           N  
ANISOU 3074  N   PRO A 441     5916   7145   6175   -415    345   -301       N  
ATOM   3075  CA  PRO A 441       9.585  39.168  18.731  1.00 50.47           C  
ANISOU 3075  CA  PRO A 441     5910   7156   6109   -449    368   -292       C  
ATOM   3076  C   PRO A 441       9.416  37.663  18.549  1.00 50.77           C  
ANISOU 3076  C   PRO A 441     5963   7185   6142   -447    365   -250       C  
ATOM   3077  O   PRO A 441       9.871  36.889  19.384  1.00 52.79           O  
ANISOU 3077  O   PRO A 441     6240   7466   6354   -464    370   -218       O  
ATOM   3078  CB  PRO A 441       8.310  39.777  19.320  1.00 48.08           C  
ANISOU 3078  CB  PRO A 441     5588   6856   5826   -473    405   -343       C  
ATOM   3079  CG  PRO A 441       8.353  41.175  18.839  1.00 47.41           C  
ANISOU 3079  CG  PRO A 441     5481   6757   5775   -459    398   -381       C  
ATOM   3080  CD  PRO A 441       8.896  41.101  17.435  1.00 50.04           C  
ANISOU 3080  CD  PRO A 441     5815   7060   6138   -418    362   -354       C  
ATOM   3081  N   HIS A 442       8.780  37.248  17.463  1.00 47.63           N  
ANISOU 3081  N   HIS A 442     5555   6752   5792   -423    356   -252       N  
ATOM   3082  CA  HIS A 442       8.585  35.832  17.228  1.00 49.10           C  
ANISOU 3082  CA  HIS A 442     5750   6924   5983   -420    353   -218       C  
ATOM   3083  C   HIS A 442       9.894  35.147  16.902  1.00 49.76           C  
ANISOU 3083  C   HIS A 442     5854   7012   6041   -403    322   -167       C  
ATOM   3084  O   HIS A 442      10.211  34.093  17.466  1.00 49.19           O  
ANISOU 3084  O   HIS A 442     5798   6950   5941   -416    325   -130       O  
ATOM   3085  CB  HIS A 442       7.572  35.613  16.112  1.00 49.18           C  
ANISOU 3085  CB  HIS A 442     5738   6895   6052   -397    349   -240       C  
ATOM   3086  CG  HIS A 442       7.444  34.170  15.696  1.00 51.96           C  
ANISOU 3086  CG  HIS A 442     6095   7229   6418   -388    341   -209       C  
ATOM   3087  ND1 HIS A 442       7.833  33.727  14.480  1.00 52.00           N  
ANISOU 3087  ND1 HIS A 442     6099   7212   6446   -353    308   -193       N  
ATOM   3088  CD2 HIS A 442       6.972  33.051  16.394  1.00 53.09           C  
ANISOU 3088  CD2 HIS A 442     6243   7372   6558   -412    366   -191       C  
ATOM   3089  CE1 HIS A 442       7.603  32.400  14.390  1.00 52.33           C  
ANISOU 3089  CE1 HIS A 442     6142   7239   6501   -354    310   -171       C  
ATOM   3090  NE2 HIS A 442       7.076  31.986  15.564  1.00 53.39           N  
ANISOU 3090  NE2 HIS A 442     6280   7384   6621   -390    346   -168       N  
ATOM   3091  N   LEU A 443      10.651  35.734  15.971  1.00 46.51           N  
ANISOU 3091  N   LEU A 443     5440   6590   5639   -373    292   -165       N  
ATOM   3092  CA  LEU A 443      12.011  35.299  15.671  1.00 44.63           C  
ANISOU 3092  CA  LEU A 443     5221   6359   5379   -357    262   -122       C  
ATOM   3093  C   LEU A 443      12.892  35.261  16.934  1.00 45.37           C  
ANISOU 3093  C   LEU A 443     5333   6490   5416   -384    266   -100       C  
ATOM   3094  O   LEU A 443      13.577  34.275  17.210  1.00 45.42           O  
ANISOU 3094  O   LEU A 443     5357   6505   5396   -386    255    -58       O  
ATOM   3095  CB  LEU A 443      12.624  36.204  14.612  1.00 42.22           C  
ANISOU 3095  CB  LEU A 443     4909   6041   5094   -325    237   -129       C  
ATOM   3096  CG  LEU A 443      12.101  36.059  13.182  1.00 42.82           C  
ANISOU 3096  CG  LEU A 443     4972   6084   5215   -290    222   -136       C  
ATOM   3097  CD1 LEU A 443      12.779  37.025  12.228  1.00 40.60           C  
ANISOU 3097  CD1 LEU A 443     4686   5793   4947   -259    201   -138       C  
ATOM   3098  CD2 LEU A 443      12.270  34.639  12.677  1.00 42.56           C  
ANISOU 3098  CD2 LEU A 443     4947   6038   5185   -277    206   -103       C  
ATOM   3099  N   ILE A 444      12.871  36.322  17.722  1.00 46.78           N  
ANISOU 3099  N   ILE A 444     5506   6691   5575   -403    281   -131       N  
ATOM   3100  CA  ILE A 444      13.627  36.283  18.968  1.00 48.83           C  
ANISOU 3100  CA  ILE A 444     5783   6992   5779   -427    284   -116       C  
ATOM   3101  C   ILE A 444      13.311  34.997  19.756  1.00 51.48           C  
ANISOU 3101  C   ILE A 444     6135   7341   6086   -447    301    -83       C  
ATOM   3102  O   ILE A 444      14.224  34.348  20.250  1.00 52.22           O  
ANISOU 3102  O   ILE A 444     6248   7454   6139   -450    287    -42       O  
ATOM   3103  CB  ILE A 444      13.443  37.574  19.787  1.00 48.82           C  
ANISOU 3103  CB  ILE A 444     5770   7016   5764   -447    303   -163       C  
ATOM   3104  CG1 ILE A 444      14.129  38.736  19.056  1.00 49.40           C  
ANISOU 3104  CG1 ILE A 444     5830   7076   5864   -426    283   -183       C  
ATOM   3105  CG2 ILE A 444      14.013  37.421  21.186  1.00 48.62           C  
ANISOU 3105  CG2 ILE A 444     5762   7039   5675   -474    310   -153       C  
ATOM   3106  CD1 ILE A 444      13.920  40.102  19.683  1.00 48.29           C  
ANISOU 3106  CD1 ILE A 444     5671   6951   5725   -442    300   -235       C  
ATOM   3107  N   GLN A 445      12.037  34.596  19.820  1.00 53.67           N  
ANISOU 3107  N   GLN A 445     6403   7602   6386   -458    329    -97       N  
ATOM   3108  CA  GLN A 445      11.641  33.364  20.536  1.00 52.98           C  
ANISOU 3108  CA  GLN A 445     6329   7522   6280   -477    350    -64       C  
ATOM   3109  C   GLN A 445      12.261  32.146  19.903  1.00 50.08           C  
ANISOU 3109  C   GLN A 445     5973   7134   5922   -457    325    -13       C  
ATOM   3110  O   GLN A 445      12.717  31.243  20.598  1.00 50.41           O  
ANISOU 3110  O   GLN A 445     6033   7192   5929   -468    327     31       O  
ATOM   3111  CB  GLN A 445      10.113  33.185  20.578  1.00 55.47           C  
ANISOU 3111  CB  GLN A 445     6628   7819   6632   -491    387    -93       C  
ATOM   3112  CG  GLN A 445       9.411  34.076  21.590  1.00 65.84           C  
ANISOU 3112  CG  GLN A 445     7933   9158   7924   -520    423   -135       C  
ATOM   3113  CD  GLN A 445      10.042  33.976  22.974  1.00 71.51           C  
ANISOU 3113  CD  GLN A 445     8674   9928   8570   -544    434   -113       C  
ATOM   3114  OE1 GLN A 445       9.982  32.924  23.618  1.00 72.98           O  
ANISOU 3114  OE1 GLN A 445     8876  10124   8729   -557    450    -72       O  
ATOM   3115  NE2 GLN A 445      10.669  35.073  23.432  1.00 70.48           N  
ANISOU 3115  NE2 GLN A 445     8543   9829   8407   -549    425   -139       N  
ATOM   3116  N   CYS A 446      12.265  32.137  18.574  1.00 48.17           N  
ANISOU 3116  N   CYS A 446     5718   6856   5727   -428    302    -20       N  
ATOM   3117  CA  CYS A 446      12.821  31.045  17.803  1.00 50.05           C  
ANISOU 3117  CA  CYS A 446     5962   7072   5983   -406    276     20       C  
ATOM   3118  C   CYS A 446      14.310  30.817  18.076  1.00 52.16           C  
ANISOU 3118  C   CYS A 446     6250   7360   6210   -400    249     61       C  
ATOM   3119  O   CYS A 446      14.804  29.689  17.944  1.00 51.92           O  
ANISOU 3119  O   CYS A 446     6229   7320   6180   -393    235    104       O  
ATOM   3120  CB  CYS A 446      12.574  31.285  16.314  1.00 50.14           C  
ANISOU 3120  CB  CYS A 446     5956   7048   6046   -372    256     -3       C  
ATOM   3121  SG  CYS A 446      10.827  31.111  15.843  1.00 51.29           S  
ANISOU 3121  SG  CYS A 446     6075   7162   6249   -373    281    -45       S  
ATOM   3122  N   LEU A 447      15.021  31.872  18.482  1.00 50.56           N  
ANISOU 3122  N   LEU A 447     6051   7185   5975   -404    240     47       N  
ATOM   3123  CA  LEU A 447      16.421  31.712  18.857  1.00 51.79           C  
ANISOU 3123  CA  LEU A 447     6223   7363   6091   -401    214     82       C  
ATOM   3124  C   LEU A 447      16.615  30.627  19.917  1.00 54.12           C  
ANISOU 3124  C   LEU A 447     6538   7678   6346   -420    222    127       C  
ATOM   3125  O   LEU A 447      17.692  30.045  19.995  1.00 55.81           O  
ANISOU 3125  O   LEU A 447     6765   7900   6541   -412    197    168       O  
ATOM   3126  CB  LEU A 447      17.052  33.030  19.323  1.00 47.76           C  
ANISOU 3126  CB  LEU A 447     5711   6882   5554   -406    208     54       C  
ATOM   3127  CG  LEU A 447      17.282  34.106  18.262  1.00 45.94           C  
ANISOU 3127  CG  LEU A 447     5464   6630   5360   -383    194     23       C  
ATOM   3128  CD1 LEU A 447      17.760  35.368  18.949  1.00 44.64           C  
ANISOU 3128  CD1 LEU A 447     5294   6494   5172   -395    195     -8       C  
ATOM   3129  CD2 LEU A 447      18.255  33.652  17.188  1.00 45.33           C  
ANISOU 3129  CD2 LEU A 447     5391   6531   5303   -352    161     53       C  
ATOM   3130  N   SER A 448      15.595  30.349  20.730  1.00 52.33           N  
ANISOU 3130  N   SER A 448     6312   7462   6108   -445    258    123       N  
ATOM   3131  CA  SER A 448      15.741  29.270  21.708  1.00 54.90           C  
ANISOU 3131  CA  SER A 448     6657   7806   6397   -461    269    172       C  
ATOM   3132  C   SER A 448      14.910  28.044  21.368  1.00 53.18           C  
ANISOU 3132  C   SER A 448     6435   7552   6220   -461    288    195       C  
ATOM   3133  O   SER A 448      14.673  27.197  22.217  1.00 55.50           O  
ANISOU 3133  O   SER A 448     6741   7856   6493   -479    310    232       O  
ATOM   3134  CB  SER A 448      15.548  29.739  23.160  1.00 54.47           C  
ANISOU 3134  CB  SER A 448     6614   7801   6282   -490    295    164       C  
ATOM   3135  OG  SER A 448      14.415  30.557  23.289  1.00 56.94           O  
ANISOU 3135  OG  SER A 448     6911   8114   6609   -505    328    111       O  
ATOM   3136  N   ASP A 449      14.520  27.928  20.103  1.00 51.43           N  
ANISOU 3136  N   ASP A 449     6194   7287   6059   -440    277    176       N  
ATOM   3137  CA  ASP A 449      13.958  26.688  19.606  1.00 53.02           C  
ANISOU 3137  CA  ASP A 449     6388   7451   6307   -435    285    198       C  
ATOM   3138  C   ASP A 449      14.895  25.531  19.923  1.00 56.34           C  
ANISOU 3138  C   ASP A 449     6826   7872   6710   -432    269    261       C  
ATOM   3139  O   ASP A 449      16.113  25.696  19.947  1.00 59.02           O  
ANISOU 3139  O   ASP A 449     7177   8229   7019   -421    238    281       O  
ATOM   3140  CB  ASP A 449      13.737  26.771  18.106  1.00 56.07           C  
ANISOU 3140  CB  ASP A 449     6753   7797   6752   -405    264    168       C  
ATOM   3141  CG  ASP A 449      12.770  25.719  17.605  1.00 57.94           C  
ANISOU 3141  CG  ASP A 449     6975   7995   7046   -403    279    168       C  
ATOM   3142  OD1 ASP A 449      13.193  24.548  17.453  1.00 57.31           O  
ANISOU 3142  OD1 ASP A 449     6897   7897   6981   -396    269    209       O  
ATOM   3143  OD2 ASP A 449      11.587  26.068  17.367  1.00 59.47           O  
ANISOU 3143  OD2 ASP A 449     7149   8174   7273   -407    301    126       O  
ATOM   3144  N   LYS A 450      14.339  24.355  20.176  1.00 57.48           N  
ANISOU 3144  N   LYS A 450     6968   7995   6876   -441    291    292       N  
ATOM   3145  CA  LYS A 450      15.183  23.237  20.555  1.00 57.91           C  
ANISOU 3145  CA  LYS A 450     7038   8049   6917   -439    279    355       C  
ATOM   3146  C   LYS A 450      15.900  22.559  19.381  1.00 54.68           C  
ANISOU 3146  C   LYS A 450     6620   7604   6551   -410    241    369       C  
ATOM   3147  O   LYS A 450      16.803  21.766  19.609  1.00 53.81           O  
ANISOU 3147  O   LYS A 450     6521   7494   6429   -404    223    419       O  
ATOM   3148  CB  LYS A 450      14.455  22.235  21.469  1.00 66.71           C  
ANISOU 3148  CB  LYS A 450     8157   9158   8031   -462    319    393       C  
ATOM   3149  CG  LYS A 450      13.079  21.790  21.018  1.00 73.42           C  
ANISOU 3149  CG  LYS A 450     8982   9966   8946   -468    352    367       C  
ATOM   3150  CD  LYS A 450      12.428  20.909  22.080  1.00 79.61           C  
ANISOU 3150  CD  LYS A 450     9773  10750   9725   -494    398    408       C  
ATOM   3151  CE  LYS A 450      11.032  20.448  21.662  1.00 84.96           C  
ANISOU 3151  CE  LYS A 450    10423  11383  10475   -501    433    379       C  
ATOM   3152  NZ  LYS A 450      10.996  19.812  20.313  1.00 82.58           N  
ANISOU 3152  NZ  LYS A 450    10097  11031  10249   -476    408    364       N  
ATOM   3153  N   LYS A 451      15.524  22.895  18.144  1.00 50.41           N  
ANISOU 3153  N   LYS A 451     6059   7036   6059   -389    229    325       N  
ATOM   3154  CA  LYS A 451      16.216  22.397  16.953  1.00 49.64           C  
ANISOU 3154  CA  LYS A 451     5952   6910   5999   -359    193    330       C  
ATOM   3155  C   LYS A 451      17.312  23.375  16.491  1.00 50.24           C  
ANISOU 3155  C   LYS A 451     6035   7006   6047   -340    159    318       C  
ATOM   3156  O   LYS A 451      17.021  24.541  16.152  1.00 49.74           O  
ANISOU 3156  O   LYS A 451     5967   6953   5980   -336    159    274       O  
ATOM   3157  CB  LYS A 451      15.231  22.134  15.808  1.00 52.31           C  
ANISOU 3157  CB  LYS A 451     6263   7208   6404   -343    197    290       C  
ATOM   3158  CG  LYS A 451      14.074  21.189  16.137  1.00 56.57           C  
ANISOU 3158  CG  LYS A 451     6790   7721   6985   -361    233    295       C  
ATOM   3159  CD  LYS A 451      14.525  19.793  16.555  1.00 58.64           C  
ANISOU 3159  CD  LYS A 451     7056   7964   7259   -366    235    353       C  
ATOM   3160  CE  LYS A 451      15.094  19.014  15.382  1.00 65.57           C  
ANISOU 3160  CE  LYS A 451     7920   8810   8185   -336    201    356       C  
ATOM   3161  NZ  LYS A 451      15.869  17.813  15.818  1.00 74.66           N  
ANISOU 3161  NZ  LYS A 451     9079   9949   9340   -339    195    418       N  
ATOM   3162  N   ALA A 452      18.561  22.896  16.480  1.00 46.78           N  
ANISOU 3162  N   ALA A 452     5609   6572   5595   -329    130    357       N  
ATOM   3163  CA  ALA A 452      19.740  23.723  16.134  1.00 45.18           C  
ANISOU 3163  CA  ALA A 452     5412   6387   5367   -313     99    352       C  
ATOM   3164  C   ALA A 452      19.569  24.434  14.803  1.00 42.73           C  
ANISOU 3164  C   ALA A 452     5086   6060   5090   -288     86    307       C  
ATOM   3165  O   ALA A 452      19.864  25.628  14.688  1.00 41.64           O  
ANISOU 3165  O   ALA A 452     4949   5940   4933   -283     81    282       O  
ATOM   3166  CB  ALA A 452      21.013  22.870  16.109  1.00 44.03           C  
ANISOU 3166  CB  ALA A 452     5274   6237   5217   -302     69    400       C  
ATOM   3167  N   LEU A 453      19.064  23.704  13.810  1.00 42.74           N  
ANISOU 3167  N   LEU A 453     5072   6027   5143   -270     84    298       N  
ATOM   3168  CA  LEU A 453      18.884  24.257  12.473  1.00 44.51           C  
ANISOU 3168  CA  LEU A 453     5280   6234   5395   -241     70    259       C  
ATOM   3169  C   LEU A 453      17.866  25.389  12.417  1.00 46.57           C  
ANISOU 3169  C   LEU A 453     5534   6504   5657   -246     90    212       C  
ATOM   3170  O   LEU A 453      17.936  26.245  11.543  1.00 51.21           O  
ANISOU 3170  O   LEU A 453     6115   7091   6252   -224     78    184       O  
ATOM   3171  CB  LEU A 453      18.544  23.163  11.476  1.00 44.65           C  
ANISOU 3171  CB  LEU A 453     5281   6217   5466   -221     62    255       C  
ATOM   3172  CG  LEU A 453      19.701  22.177  11.249  1.00 45.41           C  
ANISOU 3172  CG  LEU A 453     5381   6302   5569   -209     37    295       C  
ATOM   3173  CD1 LEU A 453      19.220  20.999  10.417  1.00 43.04           C  
ANISOU 3173  CD1 LEU A 453     5061   5966   5325   -194     33    289       C  
ATOM   3174  CD2 LEU A 453      20.915  22.847  10.592  1.00 43.40           C  
ANISOU 3174  CD2 LEU A 453     5133   6060   5297   -186      9    296       C  
ATOM   3175  N   VAL A 454      16.934  25.407  13.364  1.00 46.87           N  
ANISOU 3175  N   VAL A 454     5572   6549   5687   -275    120    205       N  
ATOM   3176  CA  VAL A 454      16.008  26.528  13.485  1.00 46.60           C  
ANISOU 3176  CA  VAL A 454     5530   6524   5650   -283    140    161       C  
ATOM   3177  C   VAL A 454      16.740  27.702  14.133  1.00 46.43           C  
ANISOU 3177  C   VAL A 454     5522   6536   5582   -293    137    159       C  
ATOM   3178  O   VAL A 454      16.641  28.840  13.667  1.00 46.39           O  
ANISOU 3178  O   VAL A 454     5510   6535   5581   -282    135    126       O  
ATOM   3179  CB  VAL A 454      14.744  26.141  14.289  1.00 45.59           C  
ANISOU 3179  CB  VAL A 454     5396   6392   5532   -311    177    152       C  
ATOM   3180  CG1 VAL A 454      13.840  27.344  14.509  1.00 43.08           C  
ANISOU 3180  CG1 VAL A 454     5070   6086   5211   -322    198    106       C  
ATOM   3181  CG2 VAL A 454      13.995  25.026  13.573  1.00 46.13           C  
ANISOU 3181  CG2 VAL A 454     5446   6423   5656   -300    179    148       C  
ATOM   3182  N   ARG A 455      17.484  27.414  15.197  1.00 46.30           N  
ANISOU 3182  N   ARG A 455     5523   6544   5524   -312    137    195       N  
ATOM   3183  CA  ARG A 455      18.270  28.432  15.879  1.00 46.95           C  
ANISOU 3183  CA  ARG A 455     5616   6661   5563   -321    132    192       C  
ATOM   3184  C   ARG A 455      19.204  29.154  14.908  1.00 46.59           C  
ANISOU 3184  C   ARG A 455     5566   6609   5527   -294    104    183       C  
ATOM   3185  O   ARG A 455      19.209  30.392  14.834  1.00 47.60           O  
ANISOU 3185  O   ARG A 455     5689   6747   5650   -292    107    151       O  
ATOM   3186  CB  ARG A 455      19.062  27.809  17.021  1.00 48.22           C  
ANISOU 3186  CB  ARG A 455     5796   6846   5678   -339    127    236       C  
ATOM   3187  CG  ARG A 455      18.321  27.766  18.342  1.00 49.69           C  
ANISOU 3187  CG  ARG A 455     5990   7059   5831   -372    160    238       C  
ATOM   3188  CD  ARG A 455      19.208  27.159  19.410  1.00 50.61           C  
ANISOU 3188  CD  ARG A 455     6127   7203   5898   -384    151    286       C  
ATOM   3189  NE  ARG A 455      18.794  25.785  19.525  1.00 57.80           N  
ANISOU 3189  NE  ARG A 455     7040   8093   6827   -388    163    325       N  
ATOM   3190  CZ  ARG A 455      19.594  24.750  19.670  1.00 56.50           C  
ANISOU 3190  CZ  ARG A 455     6886   7923   6657   -382    145    377       C  
ATOM   3191  NH1 ARG A 455      20.903  24.906  19.726  1.00 55.21           N  
ANISOU 3191  NH1 ARG A 455     6731   7776   6468   -371    111    396       N  
ATOM   3192  NH2 ARG A 455      19.053  23.548  19.734  1.00 58.40           N  
ANISOU 3192  NH2 ARG A 455     7125   8139   6924   -387    161    408       N  
ATOM   3193  N   SER A 456      19.969  28.385  14.138  1.00 45.59           N  
ANISOU 3193  N   SER A 456     5440   6464   5416   -271     79    209       N  
ATOM   3194  CA  SER A 456      20.946  28.992  13.237  1.00 44.48           C  
ANISOU 3194  CA  SER A 456     5298   6319   5284   -245     55    206       C  
ATOM   3195  C   SER A 456      20.312  29.858  12.152  1.00 43.48           C  
ANISOU 3195  C   SER A 456     5156   6177   5188   -223     59    167       C  
ATOM   3196  O   SER A 456      20.787  30.972  11.912  1.00 43.82           O  
ANISOU 3196  O   SER A 456     5196   6227   5226   -215     55    151       O  
ATOM   3197  CB  SER A 456      21.911  27.967  12.635  1.00 43.11           C  
ANISOU 3197  CB  SER A 456     5128   6131   5123   -225     29    241       C  
ATOM   3198  OG  SER A 456      21.205  26.959  11.944  1.00 48.40           O  
ANISOU 3198  OG  SER A 456     5788   6772   5828   -214     31    242       O  
ATOM   3199  N   ILE A 457      19.239  29.388  11.512  1.00 41.87           N  
ANISOU 3199  N   ILE A 457     4942   5952   5017   -214     67    150       N  
ATOM   3200  CA  ILE A 457      18.644  30.212  10.461  1.00 41.55           C  
ANISOU 3200  CA  ILE A 457     4887   5899   5002   -190     68    115       C  
ATOM   3201  C   ILE A 457      18.003  31.488  11.043  1.00 42.58           C  
ANISOU 3201  C   ILE A 457     5012   6042   5124   -208     89     82       C  
ATOM   3202  O   ILE A 457      17.999  32.534  10.394  1.00 42.95           O  
ANISOU 3202  O   ILE A 457     5051   6085   5182   -190     87     61       O  
ATOM   3203  CB  ILE A 457      17.666  29.433   9.563  1.00 45.81           C  
ANISOU 3203  CB  ILE A 457     5413   6413   5579   -173     67    100       C  
ATOM   3204  CG1 ILE A 457      17.298  30.264   8.325  1.00 45.31           C  
ANISOU 3204  CG1 ILE A 457     5337   6340   5538   -140     59     70       C  
ATOM   3205  CG2 ILE A 457      16.404  29.024  10.318  1.00 46.15           C  
ANISOU 3205  CG2 ILE A 457     5450   6453   5633   -199     92     85       C  
ATOM   3206  CD1 ILE A 457      18.364  30.284   7.261  1.00 42.45           C  
ANISOU 3206  CD1 ILE A 457     4978   5973   5176   -106     35     86       C  
ATOM   3207  N   THR A 458      17.520  31.412  12.284  1.00 41.46           N  
ANISOU 3207  N   THR A 458     4875   5916   4961   -242    110     79       N  
ATOM   3208  CA  THR A 458      16.892  32.564  12.934  1.00 43.45           C  
ANISOU 3208  CA  THR A 458     5121   6184   5206   -261    132     45       C  
ATOM   3209  C   THR A 458      17.917  33.675  13.105  1.00 45.13           C  
ANISOU 3209  C   THR A 458     5336   6412   5399   -259    124     42       C  
ATOM   3210  O   THR A 458      17.631  34.839  12.791  1.00 45.97           O  
ANISOU 3210  O   THR A 458     5431   6515   5521   -252    131     11       O  
ATOM   3211  CB  THR A 458      16.270  32.167  14.288  1.00 43.74           C  
ANISOU 3211  CB  THR A 458     5164   6239   5218   -298    158     46       C  
ATOM   3212  OG1 THR A 458      15.289  31.161  14.047  1.00 49.40           O  
ANISOU 3212  OG1 THR A 458     5873   6934   5961   -299    169     47       O  
ATOM   3213  CG2 THR A 458      15.592  33.312  14.940  1.00 41.24           C  
ANISOU 3213  CG2 THR A 458     4838   5936   4894   -318    182      6       C  
ATOM   3214  N   CYS A 459      19.114  33.301  13.568  1.00 43.70           N  
ANISOU 3214  N   CYS A 459     5168   6246   5189   -264    108     74       N  
ATOM   3215  CA  CYS A 459      20.243  34.232  13.676  1.00 40.84           C  
ANISOU 3215  CA  CYS A 459     4807   5896   4814   -260     96     74       C  
ATOM   3216  C   CYS A 459      20.371  35.018  12.395  1.00 39.18           C  
ANISOU 3216  C   CYS A 459     4584   5663   4638   -228     89     60       C  
ATOM   3217  O   CYS A 459      20.389  36.236  12.412  1.00 39.75           O  
ANISOU 3217  O   CYS A 459     4646   5737   4719   -228     97     34       O  
ATOM   3218  CB  CYS A 459      21.545  33.476  13.910  1.00 42.09           C  
ANISOU 3218  CB  CYS A 459     4978   6064   4950   -258     72    114       C  
ATOM   3219  SG  CYS A 459      21.696  32.742  15.547  1.00 45.25           S  
ANISOU 3219  SG  CYS A 459     5395   6498   5300   -293     77    136       S  
ATOM   3220  N   TRP A 460      20.421  34.315  11.273  1.00 37.95           N  
ANISOU 3220  N   TRP A 460     4429   5486   4504   -200     75     77       N  
ATOM   3221  CA  TRP A 460      20.643  34.973  10.021  1.00 38.50           C  
ANISOU 3221  CA  TRP A 460     4490   5537   4600   -166     67     71       C  
ATOM   3222  C   TRP A 460      19.495  35.875   9.645  1.00 41.38           C  
ANISOU 3222  C   TRP A 460     4840   5892   4989   -160     84     35       C  
ATOM   3223  O   TRP A 460      19.694  37.048   9.325  1.00 43.53           O  
ANISOU 3223  O   TRP A 460     5104   6160   5274   -150     89     21       O  
ATOM   3224  CB  TRP A 460      20.901  33.951   8.950  1.00 39.01           C  
ANISOU 3224  CB  TRP A 460     4558   5586   4677   -138     49     94       C  
ATOM   3225  CG  TRP A 460      21.112  34.604   7.623  1.00 41.03           C  
ANISOU 3225  CG  TRP A 460     4807   5827   4955   -100     42     90       C  
ATOM   3226  CD1 TRP A 460      22.250  35.257   7.167  1.00 40.00           C  
ANISOU 3226  CD1 TRP A 460     4677   5695   4826    -84     36    104       C  
ATOM   3227  CD2 TRP A 460      20.150  34.701   6.527  1.00 41.89           C  
ANISOU 3227  CD2 TRP A 460     4907   5922   5089    -72     43     71       C  
ATOM   3228  NE1 TRP A 460      22.066  35.727   5.892  1.00 40.57           N  
ANISOU 3228  NE1 TRP A 460     4743   5753   4919    -48     34     99       N  
ATOM   3229  CE2 TRP A 460      20.829  35.429   5.449  1.00 40.82           C  
ANISOU 3229  CE2 TRP A 460     4769   5778   4963    -38     37     80       C  
ATOM   3230  CE3 TRP A 460      18.841  34.275   6.337  1.00 42.31           C  
ANISOU 3230  CE3 TRP A 460     4952   5967   5157    -71     48     49       C  
ATOM   3231  CZ2 TRP A 460      20.202  35.712   4.247  1.00 40.48           C  
ANISOU 3231  CZ2 TRP A 460     4718   5724   4937     -3     34     68       C  
ATOM   3232  CZ3 TRP A 460      18.223  34.558   5.116  1.00 40.70           C  
ANISOU 3232  CZ3 TRP A 460     4738   5752   4974    -35     43     33       C  
ATOM   3233  CH2 TRP A 460      18.890  35.248   4.095  1.00 40.86           C  
ANISOU 3233  CH2 TRP A 460     4758   5768   4997     -1     35     44       C  
ATOM   3234  N   THR A 461      18.271  35.349   9.714  1.00 42.10           N  
ANISOU 3234  N   THR A 461     4927   5978   5089   -167     94     19       N  
ATOM   3235  CA  THR A 461      17.094  36.113   9.318  1.00 39.94           C  
ANISOU 3235  CA  THR A 461     4638   5694   4842   -160    108    -17       C  
ATOM   3236  C   THR A 461      16.956  37.384  10.164  1.00 38.32           C  
ANISOU 3236  C   THR A 461     4426   5501   4635   -182    127    -43       C  
ATOM   3237  O   THR A 461      16.699  38.459   9.626  1.00 36.21           O  
ANISOU 3237  O   THR A 461     4145   5222   4390   -167    132    -63       O  
ATOM   3238  CB  THR A 461      15.836  35.225   9.362  1.00 42.61           C  
ANISOU 3238  CB  THR A 461     4971   6024   5194   -167    116    -31       C  
ATOM   3239  OG1 THR A 461      15.963  34.205   8.360  1.00 46.37           O  
ANISOU 3239  OG1 THR A 461     5449   6487   5682   -139     96    -14       O  
ATOM   3240  CG2 THR A 461      14.562  36.048   9.074  1.00 42.41           C  
ANISOU 3240  CG2 THR A 461     4927   5988   5198   -162    130    -72       C  
ATOM   3241  N   LEU A 462      17.129  37.260  11.478  1.00 37.53           N  
ANISOU 3241  N   LEU A 462     4333   5423   4506   -218    138    -44       N  
ATOM   3242  CA  LEU A 462      17.115  38.432  12.329  1.00 40.78           C  
ANISOU 3242  CA  LEU A 462     4735   5848   4911   -240    155    -72       C  
ATOM   3243  C   LEU A 462      18.120  39.452  11.831  1.00 43.59           C  
ANISOU 3243  C   LEU A 462     5085   6198   5279   -222    146    -69       C  
ATOM   3244  O   LEU A 462      17.783  40.635  11.686  1.00 45.72           O  
ANISOU 3244  O   LEU A 462     5339   6458   5574   -219    158    -97       O  
ATOM   3245  CB  LEU A 462      17.395  38.085  13.793  1.00 41.46           C  
ANISOU 3245  CB  LEU A 462     4832   5966   4955   -277    164    -69       C  
ATOM   3246  CG  LEU A 462      16.137  37.644  14.548  1.00 44.26           C  
ANISOU 3246  CG  LEU A 462     5186   6329   5304   -303    188    -87       C  
ATOM   3247  CD1 LEU A 462      16.492  36.946  15.846  1.00 44.95           C  
ANISOU 3247  CD1 LEU A 462     5289   6447   5342   -334    193    -69       C  
ATOM   3248  CD2 LEU A 462      15.182  38.806  14.802  1.00 42.34           C  
ANISOU 3248  CD2 LEU A 462     4923   6083   5081   -315    211   -136       C  
ATOM   3249  N   SER A 463      19.335  38.994  11.525  1.00 42.92           N  
ANISOU 3249  N   SER A 463     5012   6115   5182   -209    126    -35       N  
ATOM   3250  CA  SER A 463      20.389  39.905  11.053  1.00 43.94           C  
ANISOU 3250  CA  SER A 463     5134   6235   5325   -192    119    -29       C  
ATOM   3251  C   SER A 463      19.988  40.628   9.778  1.00 43.84           C  
ANISOU 3251  C   SER A 463     5110   6196   5352   -158    122    -35       C  
ATOM   3252  O   SER A 463      20.472  41.732   9.506  1.00 44.02           O  
ANISOU 3252  O   SER A 463     5121   6208   5396   -148    128    -42       O  
ATOM   3253  CB  SER A 463      21.738  39.175  10.858  1.00 41.96           C  
ANISOU 3253  CB  SER A 463     4897   5988   5058   -182     97      9       C  
ATOM   3254  OG  SER A 463      21.832  38.572   9.583  1.00 39.81           O  
ANISOU 3254  OG  SER A 463     4630   5697   4800   -148     84     33       O  
ATOM   3255  N   ARG A 464      19.111  40.014   8.988  1.00 42.06           N  
ANISOU 3255  N   ARG A 464     4886   5959   5136   -139    118    -33       N  
ATOM   3256  CA  ARG A 464      18.681  40.662   7.742  1.00 43.44           C  
ANISOU 3256  CA  ARG A 464     5050   6111   5343   -103    119    -37       C  
ATOM   3257  C   ARG A 464      17.763  41.861   7.999  1.00 44.52           C  
ANISOU 3257  C   ARG A 464     5169   6241   5506   -111    139    -74       C  
ATOM   3258  O   ARG A 464      17.533  42.681   7.094  1.00 42.56           O  
ANISOU 3258  O   ARG A 464     4910   5975   5287    -82    142    -77       O  
ATOM   3259  CB  ARG A 464      18.001  39.667   6.827  1.00 41.70           C  
ANISOU 3259  CB  ARG A 464     4835   5884   5126    -78    106    -30       C  
ATOM   3260  CG  ARG A 464      18.950  38.640   6.272  1.00 41.44           C  
ANISOU 3260  CG  ARG A 464     4816   5852   5076    -61     86      6       C  
ATOM   3261  CD  ARG A 464      19.569  39.136   4.985  1.00 41.05           C  
ANISOU 3261  CD  ARG A 464     4767   5791   5041    -20     78     24       C  
ATOM   3262  NE  ARG A 464      18.621  39.011   3.893  1.00 41.15           N  
ANISOU 3262  NE  ARG A 464     4774   5794   5068     13     72     15       N  
ATOM   3263  CZ  ARG A 464      18.840  39.389   2.630  1.00 43.63           C  
ANISOU 3263  CZ  ARG A 464     5087   6099   5391     56     65     28       C  
ATOM   3264  NH1 ARG A 464      20.004  39.935   2.268  1.00 36.70           N  
ANISOU 3264  NH1 ARG A 464     4214   5219   4513     69     68     54       N  
ATOM   3265  NH2 ARG A 464      17.870  39.226   1.715  1.00 42.85           N  
ANISOU 3265  NH2 ARG A 464     4983   5997   5303     86     57     15       N  
ATOM   3266  N   TYR A 465      17.282  41.975   9.237  1.00 44.03           N  
ANISOU 3266  N   TYR A 465     5102   6194   5433   -149    154   -101       N  
ATOM   3267  CA  TYR A 465      16.359  43.050   9.625  1.00 48.58           C  
ANISOU 3267  CA  TYR A 465     5659   6764   6035   -161    175   -142       C  
ATOM   3268  C   TYR A 465      17.006  43.962  10.664  1.00 52.11           C  
ANISOU 3268  C   TYR A 465     6098   7224   6479   -189    188   -160       C  
ATOM   3269  O   TYR A 465      16.326  44.691  11.385  1.00 52.52           O  
ANISOU 3269  O   TYR A 465     6134   7279   6542   -212    207   -198       O  
ATOM   3270  CB  TYR A 465      15.004  42.481  10.111  1.00 45.73           C  
ANISOU 3270  CB  TYR A 465     5295   6409   5672   -181    186   -168       C  
ATOM   3271  CG  TYR A 465      14.181  41.845   8.984  1.00 46.74           C  
ANISOU 3271  CG  TYR A 465     5422   6519   5817   -150    175   -162       C  
ATOM   3272  CD1 TYR A 465      13.448  42.641   8.075  1.00 46.51           C  
ANISOU 3272  CD1 TYR A 465     5376   6469   5825   -121    176   -178       C  
ATOM   3273  CD2 TYR A 465      14.158  40.451   8.803  1.00 46.14           C  
ANISOU 3273  CD2 TYR A 465     5361   6448   5723   -147    161   -141       C  
ATOM   3274  CE1 TYR A 465      12.724  42.070   7.032  1.00 43.69           C  
ANISOU 3274  CE1 TYR A 465     5018   6101   5482    -90    161   -176       C  
ATOM   3275  CE2 TYR A 465      13.428  39.877   7.765  1.00 44.51           C  
ANISOU 3275  CE2 TYR A 465     5151   6227   5534   -117    149   -142       C  
ATOM   3276  CZ  TYR A 465      12.711  40.686   6.892  1.00 45.18           C  
ANISOU 3276  CZ  TYR A 465     5219   6295   5651    -89    148   -161       C  
ATOM   3277  OH  TYR A 465      12.006  40.104   5.867  1.00 44.23           O  
ANISOU 3277  OH  TYR A 465     5095   6165   5547    -58    132   -165       O  
ATOM   3278  N   ALA A 466      18.339  43.935  10.711  1.00 52.77           N  
ANISOU 3278  N   ALA A 466     6189   7313   6548   -187    177   -135       N  
ATOM   3279  CA  ALA A 466      19.087  44.693  11.714  1.00 52.17           C  
ANISOU 3279  CA  ALA A 466     6105   7252   6467   -212    184   -154       C  
ATOM   3280  C   ALA A 466      18.859  46.210  11.632  1.00 50.55           C  
ANISOU 3280  C   ALA A 466     5872   7027   6307   -210    202   -186       C  
ATOM   3281  O   ALA A 466      18.755  46.870  12.672  1.00 46.68           O  
ANISOU 3281  O   ALA A 466     5368   6551   5817   -239    216   -223       O  
ATOM   3282  CB  ALA A 466      20.577  44.365  11.642  1.00 49.57           C  
ANISOU 3282  CB  ALA A 466     5785   6928   6120   -206    166   -121       C  
ATOM   3283  N   HIS A 467      18.793  46.757  10.418  1.00 47.16           N  
ANISOU 3283  N   HIS A 467     5434   6567   5915   -175    203   -172       N  
ATOM   3284  CA  HIS A 467      18.557  48.194  10.253  1.00 52.60           C  
ANISOU 3284  CA  HIS A 467     6097   7233   6655   -169    221   -197       C  
ATOM   3285  C   HIS A 467      17.284  48.636  10.957  1.00 56.17           C  
ANISOU 3285  C   HIS A 467     6534   7690   7120   -192    239   -244       C  
ATOM   3286  O   HIS A 467      17.301  49.563  11.779  1.00 58.68           O  
ANISOU 3286  O   HIS A 467     6830   8009   7455   -216    256   -282       O  
ATOM   3287  CB  HIS A 467      18.528  48.581   8.775  1.00 53.63           C  
ANISOU 3287  CB  HIS A 467     6224   7332   6819   -124    219   -168       C  
ATOM   3288  CG  HIS A 467      18.489  50.073   8.539  1.00 59.69           C  
ANISOU 3288  CG  HIS A 467     6964   8071   7643   -115    239   -184       C  
ATOM   3289  ND1 HIS A 467      17.352  50.793   8.627  1.00 61.00           N  
ANISOU 3289  ND1 HIS A 467     7111   8225   7842   -118    253   -217       N  
ATOM   3290  CD2 HIS A 467      19.507  50.982   8.224  1.00 62.02           C  
ANISOU 3290  CD2 HIS A 467     7246   8346   7973   -102    247   -170       C  
ATOM   3291  CE1 HIS A 467      17.622  52.092   8.375  1.00 62.72           C  
ANISOU 3291  CE1 HIS A 467     7305   8415   8113   -107    270   -223       C  
ATOM   3292  NE2 HIS A 467      18.942  52.204   8.131  1.00 62.83           N  
ANISOU 3292  NE2 HIS A 467     7322   8423   8128    -98    267   -194       N  
ATOM   3293  N   TRP A 468      16.176  47.953  10.667  1.00 53.30           N  
ANISOU 3293  N   TRP A 468     6177   7326   6747   -187    237   -245       N  
ATOM   3294  CA  TRP A 468      14.913  48.279  11.287  1.00 53.05           C  
ANISOU 3294  CA  TRP A 468     6130   7296   6729   -208    255   -290       C  
ATOM   3295  C   TRP A 468      15.009  48.198  12.783  1.00 54.72           C  
ANISOU 3295  C   TRP A 468     6342   7540   6909   -253    267   -320       C  
ATOM   3296  O   TRP A 468      14.530  49.085  13.497  1.00 55.67           O  
ANISOU 3296  O   TRP A 468     6440   7662   7049   -275    287   -365       O  
ATOM   3297  CB  TRP A 468      13.801  47.367  10.780  1.00 53.37           C  
ANISOU 3297  CB  TRP A 468     6180   7335   6764   -197    249   -285       C  
ATOM   3298  CG  TRP A 468      12.452  47.787  11.316  1.00 53.66           C  
ANISOU 3298  CG  TRP A 468     6198   7369   6823   -216    270   -333       C  
ATOM   3299  CD1 TRP A 468      11.617  48.782  10.815  1.00 52.17           C  
ANISOU 3299  CD1 TRP A 468     5984   7154   6685   -201    280   -357       C  
ATOM   3300  CD2 TRP A 468      11.759  47.272  12.512  1.00 51.91           C  
ANISOU 3300  CD2 TRP A 468     5977   7171   6574   -256    286   -363       C  
ATOM   3301  NE1 TRP A 468      10.492  48.901  11.584  1.00 55.21           N  
ANISOU 3301  NE1 TRP A 468     6354   7544   7079   -228    299   -402       N  
ATOM   3302  CE2 TRP A 468      10.508  48.026  12.613  1.00 53.49           C  
ANISOU 3302  CE2 TRP A 468     6151   7356   6815   -262    305   -407       C  
ATOM   3303  CE3 TRP A 468      12.032  46.292  13.455  1.00 52.73           C  
ANISOU 3303  CE3 TRP A 468     6100   7306   6627   -285    287   -355       C  
ATOM   3304  CZ2 TRP A 468       9.581  47.790  13.621  1.00 53.17           C  
ANISOU 3304  CZ2 TRP A 468     6105   7333   6765   -297    327   -445       C  
ATOM   3305  CZ3 TRP A 468      11.096  46.068  14.474  1.00 56.89           C  
ANISOU 3305  CZ3 TRP A 468     6623   7851   7141   -319    309   -389       C  
ATOM   3306  CH2 TRP A 468       9.898  46.801  14.552  1.00 54.02           C  
ANISOU 3306  CH2 TRP A 468     6233   7473   6818   -325    330   -434       C  
ATOM   3307  N   VAL A 469      15.633  47.135  13.273  1.00 52.39           N  
ANISOU 3307  N   VAL A 469     6070   7271   6563   -266    255   -297       N  
ATOM   3308  CA  VAL A 469      15.732  46.918  14.706  1.00 53.09           C  
ANISOU 3308  CA  VAL A 469     6163   7397   6612   -306    264   -320       C  
ATOM   3309  C   VAL A 469      16.435  48.076  15.393  1.00 57.70           C  
ANISOU 3309  C   VAL A 469     6727   7988   7209   -322    272   -352       C  
ATOM   3310  O   VAL A 469      15.953  48.606  16.409  1.00 56.58           O  
ANISOU 3310  O   VAL A 469     6571   7864   7063   -351    291   -398       O  
ATOM   3311  CB  VAL A 469      16.449  45.602  15.030  1.00 51.88           C  
ANISOU 3311  CB  VAL A 469     6039   7269   6405   -312    245   -281       C  
ATOM   3312  CG1 VAL A 469      16.713  45.498  16.523  1.00 51.59           C  
ANISOU 3312  CG1 VAL A 469     6007   7274   6323   -350    253   -302       C  
ATOM   3313  CG2 VAL A 469      15.601  44.427  14.565  1.00 50.46           C  
ANISOU 3313  CG2 VAL A 469     5874   7083   6215   -304    242   -260       C  
ATOM   3314  N   VAL A 470      17.558  48.485  14.812  1.00 57.90           N  
ANISOU 3314  N   VAL A 470     6749   7997   7252   -302    259   -329       N  
ATOM   3315  CA  VAL A 470      18.379  49.516  15.411  1.00 60.11           C  
ANISOU 3315  CA  VAL A 470     7009   8281   7548   -315    264   -358       C  
ATOM   3316  C   VAL A 470      17.606  50.825  15.418  1.00 61.81           C  
ANISOU 3316  C   VAL A 470     7191   8474   7820   -318    288   -404       C  
ATOM   3317  O   VAL A 470      17.721  51.595  16.367  1.00 60.54           O  
ANISOU 3317  O   VAL A 470     7010   8327   7665   -343    300   -450       O  
ATOM   3318  CB  VAL A 470      19.759  49.645  14.709  1.00 59.73           C  
ANISOU 3318  CB  VAL A 470     6963   8217   7515   -291    247   -322       C  
ATOM   3319  CG1 VAL A 470      20.507  50.895  15.159  1.00 57.66           C  
ANISOU 3319  CG1 VAL A 470     6671   7948   7289   -300    256   -356       C  
ATOM   3320  CG2 VAL A 470      20.605  48.416  15.001  1.00 56.81           C  
ANISOU 3320  CG2 VAL A 470     6621   7875   7089   -295    224   -286       C  
ATOM   3321  N   SER A 471      16.794  51.043  14.384  1.00 60.89           N  
ANISOU 3321  N   SER A 471     7069   8324   7742   -292    293   -393       N  
ATOM   3322  CA  SER A 471      16.046  52.289  14.245  1.00 61.77           C  
ANISOU 3322  CA  SER A 471     7149   8408   7914   -290    314   -431       C  
ATOM   3323  C   SER A 471      14.875  52.438  15.228  1.00 62.17           C  
ANISOU 3323  C   SER A 471     7187   8477   7959   -322    334   -484       C  
ATOM   3324  O   SER A 471      14.342  53.524  15.381  1.00 64.93           O  
ANISOU 3324  O   SER A 471     7506   8808   8357   -328    353   -525       O  
ATOM   3325  CB  SER A 471      15.554  52.448  12.816  1.00 60.58           C  
ANISOU 3325  CB  SER A 471     6997   8218   7803   -249    311   -400       C  
ATOM   3326  OG  SER A 471      14.454  51.588  12.597  1.00 68.98           O  
ANISOU 3326  OG  SER A 471     8074   9288   8846   -246    308   -396       O  
ATOM   3327  N   GLN A 472      14.476  51.358  15.892  1.00 62.79           N  
ANISOU 3327  N   GLN A 472     7288   8589   7982   -343    332   -483       N  
ATOM   3328  CA  GLN A 472      13.392  51.419  16.883  1.00 63.36           C  
ANISOU 3328  CA  GLN A 472     7349   8680   8043   -375    355   -531       C  
ATOM   3329  C   GLN A 472      13.960  51.707  18.261  1.00 66.24           C  
ANISOU 3329  C   GLN A 472     7709   9085   8374   -410    363   -568       C  
ATOM   3330  O   GLN A 472      15.161  51.601  18.440  1.00 67.37           O  
ANISOU 3330  O   GLN A 472     7860   9242   8494   -409    346   -550       O  
ATOM   3331  CB  GLN A 472      12.609  50.105  16.914  1.00 59.52           C  
ANISOU 3331  CB  GLN A 472     6889   8210   7517   -379    353   -511       C  
ATOM   3332  CG  GLN A 472      11.964  49.743  15.589  1.00 60.58           C  
ANISOU 3332  CG  GLN A 472     7027   8310   7682   -345    343   -481       C  
ATOM   3333  CD  GLN A 472      11.073  50.849  15.049  1.00 60.96           C  
ANISOU 3333  CD  GLN A 472     7044   8323   7795   -331    356   -513       C  
ATOM   3334  OE1 GLN A 472      10.178  51.332  15.739  1.00 62.55           O  
ANISOU 3334  OE1 GLN A 472     7225   8527   8013   -354    379   -561       O  
ATOM   3335  NE2 GLN A 472      11.315  51.253  13.808  1.00 60.11           N  
ANISOU 3335  NE2 GLN A 472     6931   8181   7726   -292    343   -484       N  
ATOM   3336  N   PRO A 473      13.106  52.085  19.242  1.00 70.53           N  
ANISOU 3336  N   PRO A 473     8236   9647   8914   -440    388   -623       N  
ATOM   3337  CA  PRO A 473      13.643  52.276  20.593  1.00 68.82           C  
ANISOU 3337  CA  PRO A 473     8016   9476   8655   -473    393   -659       C  
ATOM   3338  C   PRO A 473      14.399  51.028  21.053  1.00 69.47           C  
ANISOU 3338  C   PRO A 473     8136   9598   8661   -479    374   -617       C  
ATOM   3339  O   PRO A 473      13.875  49.918  20.945  1.00 66.48           O  
ANISOU 3339  O   PRO A 473     7783   9228   8250   -479    373   -584       O  
ATOM   3340  CB  PRO A 473      12.392  52.501  21.448  1.00 72.09           C  
ANISOU 3340  CB  PRO A 473     8417   9908   9067   -502    424   -713       C  
ATOM   3341  CG  PRO A 473      11.383  53.056  20.510  1.00 71.85           C  
ANISOU 3341  CG  PRO A 473     8365   9828   9107   -483    436   -722       C  
ATOM   3342  CD  PRO A 473      11.704  52.534  19.134  1.00 69.99           C  
ANISOU 3342  CD  PRO A 473     8147   9559   8888   -444    411   -659       C  
ATOM   3343  N   PRO A 474      15.637  51.213  21.546  1.00 71.66           N  
ANISOU 3343  N   PRO A 474     8414   9899   8916   -484    358   -618       N  
ATOM   3344  CA  PRO A 474      16.568  50.143  21.920  1.00 69.94           C  
ANISOU 3344  CA  PRO A 474     8228   9716   8632   -485    334   -576       C  
ATOM   3345  C   PRO A 474      15.998  49.059  22.832  1.00 68.56           C  
ANISOU 3345  C   PRO A 474     8080   9585   8387   -508    343   -567       C  
ATOM   3346  O   PRO A 474      16.357  47.895  22.675  1.00 65.31           O  
ANISOU 3346  O   PRO A 474     7698   9182   7935   -501    326   -514       O  
ATOM   3347  CB  PRO A 474      17.702  50.893  22.641  1.00 71.30           C  
ANISOU 3347  CB  PRO A 474     8383   9911   8798   -496    324   -608       C  
ATOM   3348  CG  PRO A 474      17.203  52.286  22.851  1.00 72.97           C  
ANISOU 3348  CG  PRO A 474     8555  10107   9066   -506    347   -674       C  
ATOM   3349  CD  PRO A 474      16.256  52.536  21.722  1.00 72.25           C  
ANISOU 3349  CD  PRO A 474     8454   9963   9035   -486    360   -662       C  
ATOM   3350  N   ASP A 475      15.127  49.433  23.767  1.00 68.51           N  
ANISOU 3350  N   ASP A 475     8061   9603   8367   -536    371   -617       N  
ATOM   3351  CA  ASP A 475      14.609  48.490  24.761  1.00 71.52           C  
ANISOU 3351  CA  ASP A 475     8466  10029   8679   -560    384   -611       C  
ATOM   3352  C   ASP A 475      13.589  47.513  24.216  1.00 69.20           C  
ANISOU 3352  C   ASP A 475     8189   9715   8389   -554    396   -575       C  
ATOM   3353  O   ASP A 475      13.340  46.463  24.814  1.00 69.06           O  
ANISOU 3353  O   ASP A 475     8197   9727   8317   -567    402   -549       O  
ATOM   3354  CB  ASP A 475      13.992  49.232  25.947  1.00 76.96           C  
ANISOU 3354  CB  ASP A 475     9135  10754   9353   -591    414   -679       C  
ATOM   3355  CG  ASP A 475      14.985  49.461  27.065  1.00 81.61           C  
ANISOU 3355  CG  ASP A 475     9725  11397   9887   -606    402   -703       C  
ATOM   3356  OD1 ASP A 475      15.988  50.168  26.835  1.00 81.56           O  
ANISOU 3356  OD1 ASP A 475     9702  11381   9907   -595    380   -715       O  
ATOM   3357  OD2 ASP A 475      14.763  48.925  28.174  1.00 84.61           O  
ANISOU 3357  OD2 ASP A 475    10122  11830  10196   -628    414   -708       O  
ATOM   3358  N   THR A 476      12.992  47.850  23.084  1.00 67.80           N  
ANISOU 3358  N   THR A 476     7997   9486   8277   -533    398   -574       N  
ATOM   3359  CA  THR A 476      11.923  47.015  22.568  1.00 68.95           C  
ANISOU 3359  CA  THR A 476     8153   9611   8434   -528    409   -552       C  
ATOM   3360  C   THR A 476      12.424  45.844  21.694  1.00 65.12           C  
ANISOU 3360  C   THR A 476     7695   9110   7938   -503    382   -484       C  
ATOM   3361  O   THR A 476      11.975  44.706  21.853  1.00 64.37           O  
ANISOU 3361  O   THR A 476     7620   9023   7814   -509    388   -455       O  
ATOM   3362  CB  THR A 476      10.724  47.842  21.991  1.00 70.44           C  
ANISOU 3362  CB  THR A 476     8311   9761   8691   -523    430   -593       C  
ATOM   3363  OG1 THR A 476      10.346  47.350  20.702  1.00 75.05           O  
ANISOU 3363  OG1 THR A 476     8900  10303   9313   -493    416   -557       O  
ATOM   3364  CG2 THR A 476      11.049  49.334  21.890  1.00 68.42           C  
ANISOU 3364  CG2 THR A 476     8023   9489   8484   -519    431   -637       C  
ATOM   3365  N   TYR A 477      13.373  46.107  20.807  1.00 62.16           N  
ANISOU 3365  N   TYR A 477     7319   8711   7587   -476    354   -459       N  
ATOM   3366  CA  TYR A 477      13.896  45.024  19.983  1.00 59.93           C  
ANISOU 3366  CA  TYR A 477     7060   8415   7295   -452    329   -399       C  
ATOM   3367  C   TYR A 477      15.395  44.752  20.173  1.00 58.14           C  
ANISOU 3367  C   TYR A 477     6849   8208   7033   -447    301   -367       C  
ATOM   3368  O   TYR A 477      15.782  43.627  20.522  1.00 56.45           O  
ANISOU 3368  O   TYR A 477     6661   8015   6772   -451    290   -328       O  
ATOM   3369  CB  TYR A 477      13.527  45.242  18.516  1.00 61.17           C  
ANISOU 3369  CB  TYR A 477     7208   8524   7512   -418    320   -388       C  
ATOM   3370  CG  TYR A 477      12.046  45.503  18.304  1.00 62.90           C  
ANISOU 3370  CG  TYR A 477     7409   8722   7769   -421    344   -421       C  
ATOM   3371  CD1 TYR A 477      11.108  44.491  18.465  1.00 61.67           C  
ANISOU 3371  CD1 TYR A 477     7263   8569   7599   -431    356   -413       C  
ATOM   3372  CD2 TYR A 477      11.589  46.771  17.944  1.00 65.14           C  
ANISOU 3372  CD2 TYR A 477     7664   8982   8106   -414    354   -461       C  
ATOM   3373  CE1 TYR A 477       9.758  44.734  18.266  1.00 63.91           C  
ANISOU 3373  CE1 TYR A 477     7528   8833   7921   -433    377   -446       C  
ATOM   3374  CE2 TYR A 477      10.243  47.024  17.750  1.00 63.04           C  
ANISOU 3374  CE2 TYR A 477     7379   8696   7877   -415    374   -492       C  
ATOM   3375  CZ  TYR A 477       9.331  46.005  17.908  1.00 63.48           C  
ANISOU 3375  CZ  TYR A 477     7445   8756   7919   -425    384   -486       C  
ATOM   3376  OH  TYR A 477       7.992  46.265  17.725  1.00 62.62           O  
ANISOU 3376  OH  TYR A 477     7315   8627   7850   -427    403   -521       O  
ATOM   3377  N   LEU A 478      16.218  45.783  19.960  1.00 55.86           N  
ANISOU 3377  N   LEU A 478     6543   7910   6770   -437    291   -384       N  
ATOM   3378  CA  LEU A 478      17.677  45.693  20.069  1.00 52.62           C  
ANISOU 3378  CA  LEU A 478     6142   7513   6338   -431    265   -360       C  
ATOM   3379  C   LEU A 478      18.173  44.975  21.313  1.00 53.37           C  
ANISOU 3379  C   LEU A 478     6257   7660   6362   -454    259   -351       C  
ATOM   3380  O   LEU A 478      18.883  43.972  21.209  1.00 54.21           O  
ANISOU 3380  O   LEU A 478     6386   7774   6437   -445    237   -303       O  
ATOM   3381  CB  LEU A 478      18.305  47.084  19.996  1.00 57.03           C  
ANISOU 3381  CB  LEU A 478     6672   8060   6937   -427    265   -396       C  
ATOM   3382  CG  LEU A 478      19.829  47.163  19.903  1.00 57.40           C  
ANISOU 3382  CG  LEU A 478     6721   8111   6979   -415    238   -376       C  
ATOM   3383  CD1 LEU A 478      20.360  46.284  18.777  1.00 54.83           C  
ANISOU 3383  CD1 LEU A 478     6415   7760   6659   -386    217   -315       C  
ATOM   3384  CD2 LEU A 478      20.232  48.612  19.683  1.00 55.79           C  
ANISOU 3384  CD2 LEU A 478     6482   7883   6831   -410    245   -415       C  
ATOM   3385  N   LYS A 479      17.783  45.475  22.480  1.00 53.65           N  
ANISOU 3385  N   LYS A 479     6283   7731   6372   -482    278   -397       N  
ATOM   3386  CA  LYS A 479      18.228  44.912  23.741  1.00 55.90           C  
ANISOU 3386  CA  LYS A 479     6586   8070   6585   -504    273   -393       C  
ATOM   3387  C   LYS A 479      17.935  43.420  23.857  1.00 55.72           C  
ANISOU 3387  C   LYS A 479     6595   8058   6518   -505    272   -339       C  
ATOM   3388  O   LYS A 479      18.868  42.640  24.069  1.00 55.80           O  
ANISOU 3388  O   LYS A 479     6625   8087   6489   -500    247   -297       O  
ATOM   3389  CB  LYS A 479      17.676  45.701  24.948  1.00 62.46           C  
ANISOU 3389  CB  LYS A 479     7400   8939   7393   -534    299   -455       C  
ATOM   3390  CG  LYS A 479      18.245  45.229  26.277  1.00 69.48           C  
ANISOU 3390  CG  LYS A 479     8307   9891   8202   -553    291   -453       C  
ATOM   3391  CD  LYS A 479      18.278  46.323  27.337  1.00 75.82           C  
ANISOU 3391  CD  LYS A 479     9087  10732   8989   -574    303   -523       C  
ATOM   3392  CE  LYS A 479      17.160  46.149  28.359  1.00 82.14           C  
ANISOU 3392  CE  LYS A 479     9893  11570   9746   -602    338   -549       C  
ATOM   3393  NZ  LYS A 479      17.290  44.884  29.142  1.00 82.66           N  
ANISOU 3393  NZ  LYS A 479     9995  11681   9730   -610    335   -501       N  
ATOM   3394  N   PRO A 480      16.653  43.002  23.717  1.00 54.90           N  
ANISOU 3394  N   PRO A 480     6494   7941   6425   -512    298   -338       N  
ATOM   3395  CA  PRO A 480      16.408  41.554  23.832  1.00 54.42           C  
ANISOU 3395  CA  PRO A 480     6461   7887   6329   -514    298   -286       C  
ATOM   3396  C   PRO A 480      17.087  40.734  22.724  1.00 52.21           C  
ANISOU 3396  C   PRO A 480     6194   7574   6069   -485    269   -231       C  
ATOM   3397  O   PRO A 480      17.524  39.605  22.970  1.00 52.37           O  
ANISOU 3397  O   PRO A 480     6238   7608   6052   -484    256   -183       O  
ATOM   3398  CB  PRO A 480      14.875  41.431  23.741  1.00 52.45           C  
ANISOU 3398  CB  PRO A 480     6204   7620   6104   -525    334   -305       C  
ATOM   3399  CG  PRO A 480      14.407  42.726  23.176  1.00 53.70           C  
ANISOU 3399  CG  PRO A 480     6332   7750   6321   -519    343   -357       C  
ATOM   3400  CD  PRO A 480      15.397  43.767  23.606  1.00 54.11           C  
ANISOU 3400  CD  PRO A 480     6371   7823   6366   -521    330   -387       C  
ATOM   3401  N   LEU A 481      17.178  41.294  21.523  1.00 49.20           N  
ANISOU 3401  N   LEU A 481     5797   7150   5745   -460    258   -237       N  
ATOM   3402  CA  LEU A 481      17.851  40.602  20.428  1.00 51.98           C  
ANISOU 3402  CA  LEU A 481     6160   7474   6117   -431    231   -189       C  
ATOM   3403  C   LEU A 481      19.343  40.385  20.735  1.00 54.99           C  
ANISOU 3403  C   LEU A 481     6552   7875   6466   -427    201   -162       C  
ATOM   3404  O   LEU A 481      19.836  39.262  20.688  1.00 57.20           O  
ANISOU 3404  O   LEU A 481     6852   8159   6721   -420    184   -115       O  
ATOM   3405  CB  LEU A 481      17.676  41.374  19.122  1.00 50.11           C  
ANISOU 3405  CB  LEU A 481     5904   7193   5944   -405    228   -203       C  
ATOM   3406  CG  LEU A 481      18.516  40.912  17.936  1.00 49.73           C  
ANISOU 3406  CG  LEU A 481     5863   7116   5916   -372    200   -161       C  
ATOM   3407  CD1 LEU A 481      18.184  39.497  17.507  1.00 48.30           C  
ANISOU 3407  CD1 LEU A 481     5701   6926   5727   -363    194   -120       C  
ATOM   3408  CD2 LEU A 481      18.314  41.872  16.783  1.00 50.81           C  
ANISOU 3408  CD2 LEU A 481     5980   7216   6109   -347    202   -178       C  
ATOM   3409  N   MET A 482      20.039  41.465  21.062  1.00 56.81           N  
ANISOU 3409  N   MET A 482     6768   8119   6700   -430    195   -195       N  
ATOM   3410  CA  MET A 482      21.436  41.403  21.457  1.00 61.24           C  
ANISOU 3410  CA  MET A 482     7334   8701   7233   -427    167   -179       C  
ATOM   3411  C   MET A 482      21.629  40.376  22.565  1.00 58.95           C  
ANISOU 3411  C   MET A 482     7069   8456   6875   -444    161   -152       C  
ATOM   3412  O   MET A 482      22.531  39.533  22.493  1.00 58.43           O  
ANISOU 3412  O   MET A 482     7018   8393   6788   -434    135   -107       O  
ATOM   3413  CB  MET A 482      21.898  42.791  21.899  1.00 68.32           C  
ANISOU 3413  CB  MET A 482     8206   9610   8144   -435    169   -232       C  
ATOM   3414  CG  MET A 482      23.166  42.839  22.730  1.00 78.98           C  
ANISOU 3414  CG  MET A 482     9557  10996   9455   -441    144   -233       C  
ATOM   3415  SD  MET A 482      23.280  44.394  23.639  1.00 96.16           S  
ANISOU 3415  SD  MET A 482    11701  13198  11638   -461    155   -311       S  
ATOM   3416  CE  MET A 482      23.013  45.585  22.315  1.00 90.02           C  
ANISOU 3416  CE  MET A 482    10893  12357  10953   -441    169   -334       C  
ATOM   3417  N   THR A 483      20.754  40.418  23.564  1.00 57.73           N  
ANISOU 3417  N   THR A 483     6916   8332   6686   -470    187   -176       N  
ATOM   3418  CA  THR A 483      20.810  39.477  24.676  1.00 55.51           C  
ANISOU 3418  CA  THR A 483     6660   8096   6337   -486    187   -148       C  
ATOM   3419  C   THR A 483      20.724  38.023  24.226  1.00 57.53           C  
ANISOU 3419  C   THR A 483     6938   8333   6588   -476    180    -84       C  
ATOM   3420  O   THR A 483      21.493  37.180  24.703  1.00 58.17           O  
ANISOU 3420  O   THR A 483     7038   8436   6627   -474    159    -42       O  
ATOM   3421  CB  THR A 483      19.697  39.768  25.696  1.00 55.18           C  
ANISOU 3421  CB  THR A 483     6615   8086   6264   -515    223   -185       C  
ATOM   3422  OG1 THR A 483      19.919  41.062  26.262  1.00 59.31           O  
ANISOU 3422  OG1 THR A 483     7116   8632   6785   -526    226   -246       O  
ATOM   3423  CG2 THR A 483      19.674  38.734  26.818  1.00 50.96           C  
ANISOU 3423  CG2 THR A 483     6108   7597   5657   -530    228   -149       C  
ATOM   3424  N   GLU A 484      19.795  37.718  23.320  1.00 55.92           N  
ANISOU 3424  N   GLU A 484     6730   8088   6429   -468    196    -78       N  
ATOM   3425  CA  GLU A 484      19.601  36.322  22.937  1.00 57.65           C  
ANISOU 3425  CA  GLU A 484     6968   8288   6649   -460    193    -24       C  
ATOM   3426  C   GLU A 484      20.647  35.856  21.936  1.00 55.32           C  
ANISOU 3426  C   GLU A 484     6676   7965   6379   -431    158     13       C  
ATOM   3427  O   GLU A 484      20.990  34.676  21.906  1.00 56.54           O  
ANISOU 3427  O   GLU A 484     6847   8116   6520   -425    145     62       O  
ATOM   3428  CB  GLU A 484      18.187  36.050  22.413  1.00 57.79           C  
ANISOU 3428  CB  GLU A 484     6978   8274   6704   -462    222    -33       C  
ATOM   3429  CG  GLU A 484      17.079  36.295  23.424  1.00 62.09           C  
ANISOU 3429  CG  GLU A 484     7521   8845   7225   -491    261    -64       C  
ATOM   3430  CD  GLU A 484      17.139  35.381  24.636  1.00 62.95           C  
ANISOU 3430  CD  GLU A 484     7653   8994   7270   -511    271    -29       C  
ATOM   3431  OE1 GLU A 484      17.116  34.142  24.469  1.00 62.89           O  
ANISOU 3431  OE1 GLU A 484     7660   8972   7261   -505    268     22       O  
ATOM   3432  OE2 GLU A 484      17.190  35.915  25.765  1.00 64.98           O  
ANISOU 3432  OE2 GLU A 484     7912   9297   7479   -531    283    -53       O  
ATOM   3433  N   LEU A 485      21.136  36.775  21.110  1.00 52.98           N  
ANISOU 3433  N   LEU A 485     6363   7646   6121   -414    145    -11       N  
ATOM   3434  CA  LEU A 485      22.276  36.472  20.243  1.00 53.02           C  
ANISOU 3434  CA  LEU A 485     6369   7629   6146   -388    113     20       C  
ATOM   3435  C   LEU A 485      23.524  36.111  21.042  1.00 53.05           C  
ANISOU 3435  C   LEU A 485     6385   7666   6106   -392     87     45       C  
ATOM   3436  O   LEU A 485      24.191  35.117  20.725  1.00 49.04           O  
ANISOU 3436  O   LEU A 485     5889   7148   5595   -378     65     91       O  
ATOM   3437  CB  LEU A 485      22.571  37.621  19.288  1.00 51.58           C  
ANISOU 3437  CB  LEU A 485     6165   7419   6012   -369    109     -9       C  
ATOM   3438  CG  LEU A 485      22.338  37.417  17.788  1.00 51.00           C  
ANISOU 3438  CG  LEU A 485     6088   7300   5990   -340    106      5       C  
ATOM   3439  CD1 LEU A 485      21.287  36.374  17.454  1.00 47.05           C  
ANISOU 3439  CD1 LEU A 485     5596   6785   5496   -339    117     23       C  
ATOM   3440  CD2 LEU A 485      22.009  38.759  17.149  1.00 51.04           C  
ANISOU 3440  CD2 LEU A 485     6071   7285   6038   -331    118    -35       C  
ATOM   3441  N   LEU A 486      23.818  36.897  22.083  1.00 51.54           N  
ANISOU 3441  N   LEU A 486     6189   7514   5881   -409     88     13       N  
ATOM   3442  CA  LEU A 486      24.985  36.627  22.925  1.00 53.59           C  
ANISOU 3442  CA  LEU A 486     6458   7810   6094   -412     60     31       C  
ATOM   3443  C   LEU A 486      24.909  35.240  23.528  1.00 53.31           C  
ANISOU 3443  C   LEU A 486     6448   7793   6014   -418     56     84       C  
ATOM   3444  O   LEU A 486      25.886  34.484  23.480  1.00 50.96           O  
ANISOU 3444  O   LEU A 486     6160   7496   5706   -406     27    125       O  
ATOM   3445  CB  LEU A 486      25.174  37.681  24.021  1.00 52.55           C  
ANISOU 3445  CB  LEU A 486     6314   7722   5929   -431     63    -18       C  
ATOM   3446  CG  LEU A 486      25.547  39.084  23.539  1.00 52.47           C  
ANISOU 3446  CG  LEU A 486     6275   7694   5965   -425     62    -69       C  
ATOM   3447  CD1 LEU A 486      25.879  39.969  24.737  1.00 55.05           C  
ANISOU 3447  CD1 LEU A 486     6591   8069   6257   -443     60   -117       C  
ATOM   3448  CD2 LEU A 486      26.723  39.041  22.587  1.00 51.76           C  
ANISOU 3448  CD2 LEU A 486     6180   7573   5914   -399     34    -46       C  
ATOM   3449  N   LYS A 487      23.744  34.901  24.070  1.00 54.39           N  
ANISOU 3449  N   LYS A 487     6594   7942   6131   -437     88     83       N  
ATOM   3450  CA  LYS A 487      23.502  33.560  24.599  1.00 56.00           C  
ANISOU 3450  CA  LYS A 487     6820   8157   6299   -443     92    136       C  
ATOM   3451  C   LYS A 487      23.802  32.511  23.540  1.00 54.19           C  
ANISOU 3451  C   LYS A 487     6597   7884   6110   -421     75    184       C  
ATOM   3452  O   LYS A 487      24.387  31.468  23.829  1.00 54.46           O  
ANISOU 3452  O   LYS A 487     6646   7923   6122   -417     57    234       O  
ATOM   3453  CB  LYS A 487      22.040  33.399  25.000  1.00 60.11           C  
ANISOU 3453  CB  LYS A 487     7345   8681   6814   -463    135    125       C  
ATOM   3454  CG  LYS A 487      21.648  33.994  26.330  1.00 65.38           C  
ANISOU 3454  CG  LYS A 487     8015   9402   7425   -488    156     94       C  
ATOM   3455  CD  LYS A 487      20.351  33.337  26.771  1.00 70.37           C  
ANISOU 3455  CD  LYS A 487     8657  10036   8046   -507    197    107       C  
ATOM   3456  CE  LYS A 487      19.502  34.285  27.602  1.00 75.74           C  
ANISOU 3456  CE  LYS A 487     9328  10749   8701   -531    231     52       C  
ATOM   3457  NZ  LYS A 487      18.190  33.664  27.957  1.00 84.60           N  
ANISOU 3457  NZ  LYS A 487    10457  11867   9820   -548    275     63       N  
ATOM   3458  N   ARG A 488      23.366  32.802  22.319  1.00 49.73           N  
ANISOU 3458  N   ARG A 488     6016   7273   5604   -407     82    166       N  
ATOM   3459  CA  ARG A 488      23.422  31.880  21.198  1.00 50.74           C  
ANISOU 3459  CA  ARG A 488     6146   7358   5776   -386     71    200       C  
ATOM   3460  C   ARG A 488      24.862  31.726  20.656  1.00 51.43           C  
ANISOU 3460  C   ARG A 488     6232   7435   5873   -364     33    223       C  
ATOM   3461  O   ARG A 488      25.250  30.664  20.149  1.00 49.48           O  
ANISOU 3461  O   ARG A 488     5992   7166   5642   -350     17    264       O  
ATOM   3462  CB  ARG A 488      22.467  32.404  20.128  1.00 52.49           C  
ANISOU 3462  CB  ARG A 488     6351   7543   6051   -377     90    166       C  
ATOM   3463  CG  ARG A 488      21.667  31.386  19.320  1.00 55.49           C  
ANISOU 3463  CG  ARG A 488     6731   7886   6467   -367     99    186       C  
ATOM   3464  CD  ARG A 488      21.155  30.201  20.128  1.00 52.90           C  
ANISOU 3464  CD  ARG A 488     6417   7567   6115   -384    115    223       C  
ATOM   3465  NE  ARG A 488      20.483  30.584  21.359  1.00 53.54           N  
ANISOU 3465  NE  ARG A 488     6504   7685   6155   -412    143    205       N  
ATOM   3466  CZ  ARG A 488      20.605  29.929  22.508  1.00 51.27           C  
ANISOU 3466  CZ  ARG A 488     6234   7428   5817   -429    149    239       C  
ATOM   3467  NH1 ARG A 488      21.400  28.872  22.603  1.00 51.04           N  
ANISOU 3467  NH1 ARG A 488     6218   7397   5777   -421    127    293       N  
ATOM   3468  NH2 ARG A 488      19.942  30.345  23.565  1.00 54.43           N  
ANISOU 3468  NH2 ARG A 488     6638   7863   6179   -454    178    219       N  
ATOM   3469  N   ILE A 489      25.655  32.787  20.784  1.00 51.07           N  
ANISOU 3469  N   ILE A 489     6177   7406   5823   -362     19    193       N  
ATOM   3470  CA  ILE A 489      27.089  32.713  20.516  1.00 51.35           C  
ANISOU 3470  CA  ILE A 489     6210   7438   5862   -345    -16    212       C  
ATOM   3471  C   ILE A 489      27.722  31.553  21.324  1.00 54.65           C  
ANISOU 3471  C   ILE A 489     6647   7879   6239   -348    -37    262       C  
ATOM   3472  O   ILE A 489      28.563  30.816  20.808  1.00 56.17           O  
ANISOU 3472  O   ILE A 489     6842   8053   6448   -331    -62    297       O  
ATOM   3473  CB  ILE A 489      27.768  34.085  20.746  1.00 49.65           C  
ANISOU 3473  CB  ILE A 489     5978   7239   5647   -346    -24    168       C  
ATOM   3474  CG1 ILE A 489      27.577  34.974  19.516  1.00 47.53           C  
ANISOU 3474  CG1 ILE A 489     5691   6932   5435   -330    -14    138       C  
ATOM   3475  CG2 ILE A 489      29.254  33.947  21.060  1.00 50.37           C  
ANISOU 3475  CG2 ILE A 489     6070   7347   5723   -338    -61    185       C  
ATOM   3476  CD1 ILE A 489      28.050  36.397  19.734  1.00 47.80           C  
ANISOU 3476  CD1 ILE A 489     5705   6976   5479   -334    -14     92       C  
ATOM   3477  N   LEU A 490      27.262  31.355  22.559  1.00 55.00           N  
ANISOU 3477  N   LEU A 490     6704   7963   6230   -370    -25    267       N  
ATOM   3478  CA  LEU A 490      27.762  30.266  23.395  1.00 54.42           C  
ANISOU 3478  CA  LEU A 490     6649   7913   6113   -373    -42    319       C  
ATOM   3479  C   LEU A 490      26.932  28.977  23.296  1.00 54.72           C  
ANISOU 3479  C   LEU A 490     6702   7931   6160   -376    -23    364       C  
ATOM   3480  O   LEU A 490      26.972  28.152  24.208  1.00 55.11           O  
ANISOU 3480  O   LEU A 490     6768   8004   6167   -384    -23    405       O  
ATOM   3481  CB  LEU A 490      27.892  30.710  24.861  1.00 53.29           C  
ANISOU 3481  CB  LEU A 490     6515   7831   5901   -392    -42    305       C  
ATOM   3482  CG  LEU A 490      28.702  31.961  25.222  1.00 55.40           C  
ANISOU 3482  CG  LEU A 490     6768   8128   6155   -392    -61    257       C  
ATOM   3483  CD1 LEU A 490      28.649  32.198  26.726  1.00 57.98           C  
ANISOU 3483  CD1 LEU A 490     7105   8518   6407   -411    -59    246       C  
ATOM   3484  CD2 LEU A 490      30.151  31.885  24.769  1.00 54.19           C  
ANISOU 3484  CD2 LEU A 490     6607   7962   6022   -372   -103    271       C  
ATOM   3485  N   ASP A 491      26.193  28.799  22.196  1.00 56.68           N  
ANISOU 3485  N   ASP A 491     6939   8133   6462   -367     -6    356       N  
ATOM   3486  CA  ASP A 491      25.418  27.569  21.972  1.00 57.43           C  
ANISOU 3486  CA  ASP A 491     7041   8201   6577   -368     11    393       C  
ATOM   3487  C   ASP A 491      26.370  26.402  22.015  1.00 60.48           C  
ANISOU 3487  C   ASP A 491     7438   8580   6963   -356    -17    450       C  
ATOM   3488  O   ASP A 491      27.536  26.545  21.665  1.00 61.59           O  
ANISOU 3488  O   ASP A 491     7574   8719   7110   -340    -50    454       O  
ATOM   3489  CB  ASP A 491      24.752  27.565  20.594  1.00 55.42           C  
ANISOU 3489  CB  ASP A 491     6772   7898   6388   -354     22    372       C  
ATOM   3490  CG  ASP A 491      23.509  26.657  20.537  1.00 57.23           C  
ANISOU 3490  CG  ASP A 491     7003   8105   6639   -363     52    387       C  
ATOM   3491  OD1 ASP A 491      23.624  25.467  20.158  1.00 52.72           O  
ANISOU 3491  OD1 ASP A 491     6433   7506   6093   -353     45    426       O  
ATOM   3492  OD2 ASP A 491      22.407  27.144  20.883  1.00 57.41           O  
ANISOU 3492  OD2 ASP A 491     7022   8135   6655   -380     84    356       O  
ATOM   3493  N   SER A 492      25.882  25.239  22.419  1.00 63.38           N  
ANISOU 3493  N   SER A 492     7815   8940   7325   -363     -3    495       N  
ATOM   3494  CA  SER A 492      26.726  24.055  22.398  1.00 63.69           C  
ANISOU 3494  CA  SER A 492     7862   8966   7372   -350    -29    551       C  
ATOM   3495  C   SER A 492      26.878  23.531  20.972  1.00 61.88           C  
ANISOU 3495  C   SER A 492     7617   8682   7211   -328    -40    552       C  
ATOM   3496  O   SER A 492      27.794  22.752  20.690  1.00 65.06           O  
ANISOU 3496  O   SER A 492     8020   9069   7631   -313    -68    588       O  
ATOM   3497  CB  SER A 492      26.179  22.977  23.322  1.00 64.71           C  
ANISOU 3497  CB  SER A 492     8006   9103   7477   -365     -8    603       C  
ATOM   3498  OG  SER A 492      24.810  22.763  23.057  1.00 71.81           O  
ANISOU 3498  OG  SER A 492     8900   9979   8407   -376     32    589       O  
ATOM   3499  N   ASN A 493      25.995  23.965  20.075  1.00 57.03           N  
ANISOU 3499  N   ASN A 493     6989   8042   6637   -326    -20    512       N  
ATOM   3500  CA  ASN A 493      26.061  23.544  18.675  1.00 55.69           C  
ANISOU 3500  CA  ASN A 493     6804   7826   6529   -303    -30    506       C  
ATOM   3501  C   ASN A 493      26.960  24.463  17.852  1.00 55.90           C  
ANISOU 3501  C   ASN A 493     6822   7851   6568   -284    -54    476       C  
ATOM   3502  O   ASN A 493      26.831  25.689  17.900  1.00 58.79           O  
ANISOU 3502  O   ASN A 493     7184   8235   6919   -288    -47    435       O  
ATOM   3503  CB  ASN A 493      24.662  23.460  18.067  1.00 51.34           C  
ANISOU 3503  CB  ASN A 493     6242   7248   6016   -306      1    478       C  
ATOM   3504  CG  ASN A 493      24.668  22.925  16.642  1.00 51.10           C  
ANISOU 3504  CG  ASN A 493     6196   7173   6046   -281    -10    471       C  
ATOM   3505  OD1 ASN A 493      24.998  23.636  15.693  1.00 52.57           O  
ANISOU 3505  OD1 ASN A 493     6373   7351   6250   -262    -23    440       O  
ATOM   3506  ND2 ASN A 493      24.266  21.673  16.485  1.00 50.16           N  
ANISOU 3506  ND2 ASN A 493     6073   7026   5961   -279     -3    498       N  
ATOM   3507  N   LYS A 494      27.851  23.861  17.077  1.00 58.27           N  
ANISOU 3507  N   LYS A 494     7116   8126   6899   -262    -80    496       N  
ATOM   3508  CA  LYS A 494      28.864  24.622  16.342  1.00 61.31           C  
ANISOU 3508  CA  LYS A 494     7492   8509   7296   -243   -102    475       C  
ATOM   3509  C   LYS A 494      28.321  25.465  15.182  1.00 58.38           C  
ANISOU 3509  C   LYS A 494     7107   8118   6956   -230    -90    430       C  
ATOM   3510  O   LYS A 494      28.782  26.596  14.979  1.00 54.40           O  
ANISOU 3510  O   LYS A 494     6598   7625   6447   -224    -94    403       O  
ATOM   3511  CB  LYS A 494      30.036  23.724  15.902  1.00 65.42           C  
ANISOU 3511  CB  LYS A 494     8009   9009   7838   -225   -133    510       C  
ATOM   3512  CG  LYS A 494      31.169  23.651  16.927  1.00 71.28           C  
ANISOU 3512  CG  LYS A 494     8760   9780   8542   -231   -159    539       C  
ATOM   3513  CD  LYS A 494      31.981  22.361  16.831  1.00 77.94           C  
ANISOU 3513  CD  LYS A 494     9604  10604   9406   -219   -183    587       C  
ATOM   3514  CE  LYS A 494      31.360  21.247  17.671  1.00 84.29           C  
ANISOU 3514  CE  LYS A 494    10419  11409  10197   -234   -172    630       C  
ATOM   3515  NZ  LYS A 494      31.792  19.887  17.238  1.00 86.83           N  
ANISOU 3515  NZ  LYS A 494    10736  11696  10561   -220   -187    670       N  
ATOM   3516  N   ARG A 495      27.355  24.928  14.431  1.00 58.14           N  
ANISOU 3516  N   ARG A 495     7071   8061   6961   -222    -74    422       N  
ATOM   3517  CA  ARG A 495      26.675  25.710  13.370  1.00 57.75           C  
ANISOU 3517  CA  ARG A 495     7010   7996   6938   -208    -62    380       C  
ATOM   3518  C   ARG A 495      25.938  26.912  13.940  1.00 53.79           C  
ANISOU 3518  C   ARG A 495     6508   7516   6411   -226    -40    345       C  
ATOM   3519  O   ARG A 495      25.949  27.992  13.364  1.00 50.99           O  
ANISOU 3519  O   ARG A 495     6146   7161   6065   -215    -37    314       O  
ATOM   3520  CB  ARG A 495      25.716  24.852  12.560  1.00 61.79           C  
ANISOU 3520  CB  ARG A 495     7512   8477   7489   -198    -52    375       C  
ATOM   3521  CG  ARG A 495      26.441  23.902  11.635  1.00 71.24           C  
ANISOU 3521  CG  ARG A 495     8702   9648   8719   -174    -74    394       C  
ATOM   3522  CD  ARG A 495      25.502  23.087  10.764  1.00 79.97           C  
ANISOU 3522  CD  ARG A 495     9794  10724   9867   -161    -66    382       C  
ATOM   3523  NE  ARG A 495      26.277  22.285   9.813  1.00 88.06           N  
ANISOU 3523  NE  ARG A 495    10810  11726  10923   -136    -87    394       N  
ATOM   3524  CZ  ARG A 495      26.633  21.011   9.992  1.00 89.62           C  
ANISOU 3524  CZ  ARG A 495    11005  11906  11140   -137    -97    427       C  
ATOM   3525  NH1 ARG A 495      26.269  20.348  11.089  1.00 87.51           N  
ANISOU 3525  NH1 ARG A 495    10745  11641  10863   -162    -87    456       N  
ATOM   3526  NH2 ARG A 495      27.347  20.393   9.054  1.00 90.28           N  
ANISOU 3526  NH2 ARG A 495    11079  11970  11254   -113   -117    431       N  
ATOM   3527  N   VAL A 496      25.326  26.727  15.097  1.00 51.88           N  
ANISOU 3527  N   VAL A 496     6276   7295   6141   -252    -23    353       N  
ATOM   3528  CA  VAL A 496      24.653  27.828  15.748  1.00 51.16           C  
ANISOU 3528  CA  VAL A 496     6185   7228   6026   -271     -2    319       C  
ATOM   3529  C   VAL A 496      25.675  28.892  16.148  1.00 49.86           C  
ANISOU 3529  C   VAL A 496     6021   7089   5835   -272    -16    306       C  
ATOM   3530  O   VAL A 496      25.464  30.093  15.902  1.00 48.70           O  
ANISOU 3530  O   VAL A 496     5864   6945   5694   -271     -7    268       O  
ATOM   3531  CB  VAL A 496      23.827  27.358  16.968  1.00 52.15           C  
ANISOU 3531  CB  VAL A 496     6321   7374   6122   -300     22    331       C  
ATOM   3532  CG1 VAL A 496      23.120  28.538  17.596  1.00 50.94           C  
ANISOU 3532  CG1 VAL A 496     6165   7245   5946   -319     45    290       C  
ATOM   3533  CG2 VAL A 496      22.800  26.308  16.556  1.00 51.67           C  
ANISOU 3533  CG2 VAL A 496     6255   7282   6095   -299     38    341       C  
ATOM   3534  N   GLN A 497      26.777  28.447  16.753  1.00 48.56           N  
ANISOU 3534  N   GLN A 497     5865   6941   5646   -274    -39    338       N  
ATOM   3535  CA  GLN A 497      27.828  29.360  17.212  1.00 48.03           C  
ANISOU 3535  CA  GLN A 497     5796   6898   5556   -276    -56    326       C  
ATOM   3536  C   GLN A 497      28.203  30.316  16.106  1.00 46.62           C  
ANISOU 3536  C   GLN A 497     5602   6699   5413   -256    -59    297       C  
ATOM   3537  O   GLN A 497      28.126  31.530  16.276  1.00 44.98           O  
ANISOU 3537  O   GLN A 497     5386   6503   5202   -262    -49    261       O  
ATOM   3538  CB  GLN A 497      29.053  28.584  17.676  1.00 49.95           C  
ANISOU 3538  CB  GLN A 497     6046   7151   5780   -272    -86    367       C  
ATOM   3539  CG  GLN A 497      28.933  28.006  19.077  1.00 50.64           C  
ANISOU 3539  CG  GLN A 497     6150   7273   5817   -294    -86    394       C  
ATOM   3540  CD  GLN A 497      30.082  27.068  19.412  1.00 53.49           C  
ANISOU 3540  CD  GLN A 497     6519   7638   6166   -286   -118    441       C  
ATOM   3541  OE1 GLN A 497      30.984  26.845  18.594  1.00 51.76           O  
ANISOU 3541  OE1 GLN A 497     6291   7396   5979   -266   -140    451       O  
ATOM   3542  NE2 GLN A 497      30.061  26.520  20.626  1.00 52.12           N  
ANISOU 3542  NE2 GLN A 497     6361   7497   5946   -301   -120    471       N  
ATOM   3543  N   GLU A 498      28.544  29.778  14.942  1.00 47.97           N  
ANISOU 3543  N   GLU A 498     5768   6838   5620   -231    -70    312       N  
ATOM   3544  CA  GLU A 498      28.938  30.658  13.855  1.00 53.67           C  
ANISOU 3544  CA  GLU A 498     6477   7541   6374   -209    -71    290       C  
ATOM   3545  C   GLU A 498      27.825  31.536  13.280  1.00 51.17           C  
ANISOU 3545  C   GLU A 498     6152   7215   6077   -206    -46    253       C  
ATOM   3546  O   GLU A 498      28.045  32.715  12.987  1.00 52.16           O  
ANISOU 3546  O   GLU A 498     6267   7339   6214   -200    -40    227       O  
ATOM   3547  CB  GLU A 498      29.727  29.936  12.770  1.00 60.62           C  
ANISOU 3547  CB  GLU A 498     7354   8394   7284   -182    -89    314       C  
ATOM   3548  CG  GLU A 498      29.044  28.791  12.074  1.00 69.27           C  
ANISOU 3548  CG  GLU A 498     8452   9467   8400   -171    -87    329       C  
ATOM   3549  CD  GLU A 498      29.680  28.546  10.721  1.00 75.45           C  
ANISOU 3549  CD  GLU A 498     9227  10224   9217   -139    -99    335       C  
ATOM   3550  OE1 GLU A 498      30.016  29.544  10.047  1.00 74.73           O  
ANISOU 3550  OE1 GLU A 498     9128  10129   9139   -124    -95    316       O  
ATOM   3551  OE2 GLU A 498      29.847  27.368  10.336  1.00 83.35           O  
ANISOU 3551  OE2 GLU A 498    10228  11209  10233   -129   -111    358       O  
ATOM   3552  N   ALA A 499      26.633  30.960  13.145  1.00 49.63           N  
ANISOU 3552  N   ALA A 499     5960   7010   5887   -209    -31    251       N  
ATOM   3553  CA  ALA A 499      25.460  31.706  12.727  1.00 43.96           C  
ANISOU 3553  CA  ALA A 499     5233   6285   5186   -208     -8    216       C  
ATOM   3554  C   ALA A 499      25.225  32.870  13.685  1.00 42.68           C  
ANISOU 3554  C   ALA A 499     5067   6146   5002   -231      7    186       C  
ATOM   3555  O   ALA A 499      25.044  33.994  13.253  1.00 41.49           O  
ANISOU 3555  O   ALA A 499     4905   5989   4870   -223     17    157       O  
ATOM   3556  CB  ALA A 499      24.257  30.788  12.692  1.00 42.31           C  
ANISOU 3556  CB  ALA A 499     5026   6065   4985   -213      5    219       C  
ATOM   3557  N   ALA A 500      25.279  32.601  14.988  1.00 40.97           N  
ANISOU 3557  N   ALA A 500     4860   5958   4747   -257      9    194       N  
ATOM   3558  CA  ALA A 500      25.044  33.639  15.985  1.00 41.35           C  
ANISOU 3558  CA  ALA A 500     4904   6034   4771   -280     23    161       C  
ATOM   3559  C   ALA A 500      26.125  34.711  15.922  1.00 44.41           C  
ANISOU 3559  C   ALA A 500     5282   6428   5166   -274     11    145       C  
ATOM   3560  O   ALA A 500      25.851  35.927  15.872  1.00 45.03           O  
ANISOU 3560  O   ALA A 500     5346   6505   5258   -276     25    107       O  
ATOM   3561  CB  ALA A 500      24.996  33.013  17.365  1.00 44.20           C  
ANISOU 3561  CB  ALA A 500     5280   6430   5085   -307     24    178       C  
ATOM   3562  N   CYS A 501      27.365  34.239  15.898  1.00 45.82           N  
ANISOU 3562  N   CYS A 501     5464   6608   5337   -265    -15    173       N  
ATOM   3563  CA  CYS A 501      28.525  35.100  15.787  1.00 45.67           C  
ANISOU 3563  CA  CYS A 501     5433   6589   5329   -256    -29    162       C  
ATOM   3564  C   CYS A 501      28.511  35.931  14.497  1.00 43.83           C  
ANISOU 3564  C   CYS A 501     5186   6324   5145   -233    -19    146       C  
ATOM   3565  O   CYS A 501      28.694  37.154  14.538  1.00 44.16           O  
ANISOU 3565  O   CYS A 501     5211   6364   5202   -234    -10    115       O  
ATOM   3566  CB  CYS A 501      29.772  34.233  15.861  1.00 51.86           C  
ANISOU 3566  CB  CYS A 501     6224   7376   6103   -248    -59    199       C  
ATOM   3567  SG  CYS A 501      31.057  34.958  16.868  1.00 60.55           S  
ANISOU 3567  SG  CYS A 501     7316   8506   7182   -259    -79    184       S  
ATOM   3568  N   SER A 502      28.285  35.292  13.354  1.00 41.79           N  
ANISOU 3568  N   SER A 502     4931   6038   4910   -209    -20    167       N  
ATOM   3569  CA  SER A 502      28.100  36.061  12.108  1.00 46.78           C  
ANISOU 3569  CA  SER A 502     5551   6642   5582   -184     -9    154       C  
ATOM   3570  C   SER A 502      27.006  37.136  12.239  1.00 49.68           C  
ANISOU 3570  C   SER A 502     5908   7010   5960   -193     17    115       C  
ATOM   3571  O   SER A 502      27.212  38.296  11.849  1.00 51.24           O  
ANISOU 3571  O   SER A 502     6091   7195   6184   -184     27     96       O  
ATOM   3572  CB  SER A 502      27.740  35.141  10.943  1.00 45.99           C  
ANISOU 3572  CB  SER A 502     5456   6518   5498   -159    -13    176       C  
ATOM   3573  OG  SER A 502      28.757  34.192  10.734  1.00 48.85           O  
ANISOU 3573  OG  SER A 502     5826   6877   5858   -149    -35    208       O  
ATOM   3574  N   ALA A 503      25.856  36.740  12.805  1.00 47.01           N  
ANISOU 3574  N   ALA A 503     5576   6683   5604   -211     28    105       N  
ATOM   3575  CA  ALA A 503      24.673  37.604  12.901  1.00 46.11           C  
ANISOU 3575  CA  ALA A 503     5452   6566   5502   -220     53     69       C  
ATOM   3576  C   ALA A 503      24.922  38.755  13.839  1.00 43.37           C  
ANISOU 3576  C   ALA A 503     5093   6238   5148   -241     62     36       C  
ATOM   3577  O   ALA A 503      24.518  39.878  13.565  1.00 44.46           O  
ANISOU 3577  O   ALA A 503     5215   6364   5314   -238     78      6       O  
ATOM   3578  CB  ALA A 503      23.441  36.802  13.351  1.00 46.15           C  
ANISOU 3578  CB  ALA A 503     5466   6580   5491   -236     64     67       C  
ATOM   3579  N   PHE A 504      25.608  38.478  14.942  1.00 45.99           N  
ANISOU 3579  N   PHE A 504     5431   6599   5444   -262     50     41       N  
ATOM   3580  CA  PHE A 504      25.967  39.531  15.888  1.00 49.69           C  
ANISOU 3580  CA  PHE A 504     5887   7090   5904   -281     55      6       C  
ATOM   3581  C   PHE A 504      26.891  40.585  15.275  1.00 50.12           C  
ANISOU 3581  C   PHE A 504     5921   7123   5997   -265     52     -5       C  
ATOM   3582  O   PHE A 504      26.756  41.794  15.543  1.00 50.66           O  
ANISOU 3582  O   PHE A 504     5970   7191   6086   -273     67    -44       O  
ATOM   3583  CB  PHE A 504      26.620  38.941  17.131  1.00 52.87           C  
ANISOU 3583  CB  PHE A 504     6301   7531   6256   -302     38     17       C  
ATOM   3584  CG  PHE A 504      26.728  39.916  18.256  1.00 57.30           C  
ANISOU 3584  CG  PHE A 504     6850   8123   6800   -325     44    -26       C  
ATOM   3585  CD1 PHE A 504      25.585  40.336  18.941  1.00 62.43           C  
ANISOU 3585  CD1 PHE A 504     7496   8789   7435   -347     69    -61       C  
ATOM   3586  CD2 PHE A 504      27.955  40.439  18.623  1.00 58.78           C  
ANISOU 3586  CD2 PHE A 504     7025   8321   6986   -325     26    -37       C  
ATOM   3587  CE1 PHE A 504      25.674  41.253  19.979  1.00 64.77           C  
ANISOU 3587  CE1 PHE A 504     7778   9116   7715   -368     76   -106       C  
ATOM   3588  CE2 PHE A 504      28.054  41.349  19.665  1.00 59.14           C  
ANISOU 3588  CE2 PHE A 504     7056   8397   7018   -346     30    -83       C  
ATOM   3589  CZ  PHE A 504      26.918  41.763  20.339  1.00 61.62           C  
ANISOU 3589  CZ  PHE A 504     7367   8730   7315   -367     55   -118       C  
ATOM   3590  N   ALA A 505      27.823  40.122  14.447  1.00 47.68           N  
ANISOU 3590  N   ALA A 505     5617   6796   5703   -242     35     28       N  
ATOM   3591  CA  ALA A 505      28.745  41.017  13.779  1.00 48.69           C  
ANISOU 3591  CA  ALA A 505     5727   6901   5871   -224     34     24       C  
ATOM   3592  C   ALA A 505      27.956  41.970  12.913  1.00 48.31           C  
ANISOU 3592  C   ALA A 505     5665   6825   5864   -209     59      6       C  
ATOM   3593  O   ALA A 505      28.217  43.185  12.931  1.00 49.12           O  
ANISOU 3593  O   ALA A 505     5747   6917   6000   -210     72    -20       O  
ATOM   3594  CB  ALA A 505      29.742  40.237  12.935  1.00 47.04           C  
ANISOU 3594  CB  ALA A 505     5526   6676   5669   -200     15     65       C  
ATOM   3595  N   THR A 506      26.991  41.416  12.170  1.00 46.37           N  
ANISOU 3595  N   THR A 506     5431   6567   5620   -195     65     20       N  
ATOM   3596  CA  THR A 506      26.167  42.203  11.245  1.00 46.98           C  
ANISOU 3596  CA  THR A 506     5498   6619   5735   -176     85      8       C  
ATOM   3597  C   THR A 506      25.411  43.245  12.045  1.00 47.23           C  
ANISOU 3597  C   THR A 506     5513   6658   5776   -199    105    -37       C  
ATOM   3598  O   THR A 506      25.282  44.394  11.634  1.00 48.65           O  
ANISOU 3598  O   THR A 506     5673   6816   5995   -190    121    -55       O  
ATOM   3599  CB  THR A 506      25.134  41.339  10.490  1.00 44.41           C  
ANISOU 3599  CB  THR A 506     5185   6284   5404   -160     85     24       C  
ATOM   3600  OG1 THR A 506      25.807  40.425   9.616  1.00 43.67           O  
ANISOU 3600  OG1 THR A 506     5104   6181   5307   -136     67     62       O  
ATOM   3601  CG2 THR A 506      24.208  42.220   9.660  1.00 41.33           C  
ANISOU 3601  CG2 THR A 506     4782   5871   5049   -142    103      7       C  
ATOM   3602  N   LEU A 507      24.924  42.821  13.198  1.00 47.23           N  
ANISOU 3602  N   LEU A 507     5519   6687   5738   -229    105    -53       N  
ATOM   3603  CA  LEU A 507      24.183  43.693  14.072  1.00 50.43           C  
ANISOU 3603  CA  LEU A 507     5911   7106   6146   -254    124    -99       C  
ATOM   3604  C   LEU A 507      25.102  44.785  14.598  1.00 51.96           C  
ANISOU 3604  C   LEU A 507     6083   7303   6357   -264    125   -126       C  
ATOM   3605  O   LEU A 507      24.735  45.965  14.588  1.00 54.51           O  
ANISOU 3605  O   LEU A 507     6383   7612   6717   -266    144   -161       O  
ATOM   3606  CB  LEU A 507      23.561  42.891  15.222  1.00 49.28           C  
ANISOU 3606  CB  LEU A 507     5779   6994   5950   -283    125   -106       C  
ATOM   3607  CG  LEU A 507      22.740  43.700  16.224  1.00 53.06           C  
ANISOU 3607  CG  LEU A 507     6244   7492   6425   -311    147   -156       C  
ATOM   3608  CD1 LEU A 507      21.520  44.280  15.521  1.00 55.48           C  
ANISOU 3608  CD1 LEU A 507     6537   7771   6771   -301    168   -176       C  
ATOM   3609  CD2 LEU A 507      22.328  42.866  17.437  1.00 55.06           C  
ANISOU 3609  CD2 LEU A 507     6514   7785   6622   -340    148   -158       C  
ATOM   3610  N   GLU A 508      26.289  44.386  15.058  1.00 51.68           N  
ANISOU 3610  N   GLU A 508     6053   7284   6299   -268    104   -112       N  
ATOM   3611  CA  GLU A 508      27.313  45.345  15.480  1.00 51.69           C  
ANISOU 3611  CA  GLU A 508     6031   7287   6321   -275    102   -137       C  
ATOM   3612  C   GLU A 508      27.551  46.450  14.454  1.00 49.81           C  
ANISOU 3612  C   GLU A 508     5770   7006   6149   -252    117   -141       C  
ATOM   3613  O   GLU A 508      27.512  47.632  14.801  1.00 47.49           O  
ANISOU 3613  O   GLU A 508     5450   6705   5889   -262    133   -182       O  
ATOM   3614  CB  GLU A 508      28.617  44.632  15.780  1.00 52.49           C  
ANISOU 3614  CB  GLU A 508     6142   7405   6397   -274     73   -112       C  
ATOM   3615  CG  GLU A 508      28.700  44.064  17.187  1.00 52.86           C  
ANISOU 3615  CG  GLU A 508     6200   7500   6384   -301     59   -124       C  
ATOM   3616  CD  GLU A 508      29.962  43.251  17.415  1.00 51.70           C  
ANISOU 3616  CD  GLU A 508     6064   7368   6213   -297     27    -93       C  
ATOM   3617  OE1 GLU A 508      30.587  42.801  16.423  1.00 49.02           O  
ANISOU 3617  OE1 GLU A 508     5730   7001   5895   -273     18    -56       O  
ATOM   3618  OE2 GLU A 508      30.325  43.063  18.595  1.00 51.30           O  
ANISOU 3618  OE2 GLU A 508     6015   7356   6118   -316     12   -108       O  
ATOM   3619  N   GLU A 509      27.773  46.062  13.198  1.00 50.71           N  
ANISOU 3619  N   GLU A 509     5895   7093   6281   -221    115   -100       N  
ATOM   3620  CA  GLU A 509      27.951  47.013  12.100  1.00 53.32           C  
ANISOU 3620  CA  GLU A 509     6208   7382   6670   -195    132    -93       C  
ATOM   3621  C   GLU A 509      26.826  48.024  12.050  1.00 56.20           C  
ANISOU 3621  C   GLU A 509     6554   7732   7066   -198    157   -126       C  
ATOM   3622  O   GLU A 509      27.081  49.205  11.908  1.00 59.40           O  
ANISOU 3622  O   GLU A 509     6934   8115   7522   -195    174   -145       O  
ATOM   3623  CB  GLU A 509      28.027  46.292  10.750  1.00 59.84           C  
ANISOU 3623  CB  GLU A 509     7051   8188   7498   -161    127    -44       C  
ATOM   3624  CG  GLU A 509      29.425  46.171  10.163  1.00 67.22           C  
ANISOU 3624  CG  GLU A 509     7984   9108   8448   -142    117    -14       C  
ATOM   3625  CD  GLU A 509      29.524  45.131   9.051  1.00 74.24           C  
ANISOU 3625  CD  GLU A 509     8896   9989   9322   -113    107     32       C  
ATOM   3626  OE1 GLU A 509      28.530  44.930   8.322  1.00 78.35           O  
ANISOU 3626  OE1 GLU A 509     9426  10502   9841    -96    113     42       O  
ATOM   3627  OE2 GLU A 509      30.607  44.510   8.893  1.00 82.71           O  
ANISOU 3627  OE2 GLU A 509     9975  11063  10388   -106     91     57       O  
ATOM   3628  N   GLU A 510      25.584  47.561  12.182  1.00 57.10           N  
ANISOU 3628  N   GLU A 510     6681   7857   7156   -205    161   -132       N  
ATOM   3629  CA  GLU A 510      24.423  48.443  12.120  1.00 56.31           C  
ANISOU 3629  CA  GLU A 510     6564   7743   7087   -207    184   -163       C  
ATOM   3630  C   GLU A 510      24.271  49.312  13.356  1.00 57.75           C  
ANISOU 3630  C   GLU A 510     6725   7942   7277   -240    196   -218       C  
ATOM   3631  O   GLU A 510      23.945  50.485  13.233  1.00 59.81           O  
ANISOU 3631  O   GLU A 510     6958   8179   7586   -239    216   -246       O  
ATOM   3632  CB  GLU A 510      23.142  47.635  11.914  1.00 61.13           C  
ANISOU 3632  CB  GLU A 510     7194   8362   7672   -205    184   -157       C  
ATOM   3633  CG  GLU A 510      22.945  47.126  10.494  1.00 64.69           C  
ANISOU 3633  CG  GLU A 510     7658   8790   8132   -167    178   -115       C  
ATOM   3634  CD  GLU A 510      22.474  48.196   9.515  1.00 67.94           C  
ANISOU 3634  CD  GLU A 510     8052   9167   8596   -140    195   -117       C  
ATOM   3635  OE1 GLU A 510      22.053  49.300   9.939  1.00 67.66           O  
ANISOU 3635  OE1 GLU A 510     7992   9121   8594   -152    214   -153       O  
ATOM   3636  OE2 GLU A 510      22.517  47.915   8.300  1.00 68.47           O  
ANISOU 3636  OE2 GLU A 510     8129   9217   8671   -104    190    -81       O  
ATOM   3637  N   ALA A 511      24.500  48.740  14.537  1.00 56.40           N  
ANISOU 3637  N   ALA A 511     6563   7811   7056   -268    184   -234       N  
ATOM   3638  CA  ALA A 511      24.281  49.452  15.805  1.00 60.99           C  
ANISOU 3638  CA  ALA A 511     7125   8417   7633   -301    194   -290       C  
ATOM   3639  C   ALA A 511      25.288  50.570  16.132  1.00 67.07           C  
ANISOU 3639  C   ALA A 511     7863   9178   8443   -306    196   -321       C  
ATOM   3640  O   ALA A 511      24.894  51.629  16.619  1.00 71.09           O  
ANISOU 3640  O   ALA A 511     8344   9683   8984   -321    215   -371       O  
ATOM   3641  CB  ALA A 511      24.207  48.463  16.956  1.00 61.46           C  
ANISOU 3641  CB  ALA A 511     7205   8525   7621   -327    180   -294       C  
ATOM   3642  N   CYS A 512      26.576  50.321  15.871  1.00 71.38           N  
ANISOU 3642  N   CYS A 512     8411   9719   8989   -295    178   -295       N  
ATOM   3643  CA  CYS A 512      27.685  51.252  16.185  1.00 68.39           C  
ANISOU 3643  CA  CYS A 512     8002   9332   8650   -299    178   -323       C  
ATOM   3644  C   CYS A 512      27.705  51.726  17.629  1.00 68.03           C  
ANISOU 3644  C   CYS A 512     7938   9324   8585   -332    176   -384       C  
ATOM   3645  O   CYS A 512      27.716  50.908  18.549  1.00 69.62           O  
ANISOU 3645  O   CYS A 512     8160   9573   8721   -350    158   -388       O  
ATOM   3646  CB  CYS A 512      27.703  52.435  15.232  1.00 68.55           C  
ANISOU 3646  CB  CYS A 512     7994   9299   8751   -279    202   -325       C  
ATOM   3647  SG  CYS A 512      27.722  51.882  13.524  1.00 75.52           S  
ANISOU 3647  SG  CYS A 512     8900  10144   9648   -236    203   -252       S  
ATOM   3648  N   THR A 513      27.697  53.041  17.822  1.00 68.40           N  
ANISOU 3648  N   THR A 513     7947   9352   8691   -339    195   -433       N  
ATOM   3649  CA  THR A 513      27.757  53.615  19.165  1.00 74.76           C  
ANISOU 3649  CA  THR A 513     8729  10192   9484   -369    194   -500       C  
ATOM   3650  C   THR A 513      26.646  53.063  20.077  1.00 78.09           C  
ANISOU 3650  C   THR A 513     9171  10660   9840   -393    197   -520       C  
ATOM   3651  O   THR A 513      26.807  52.994  21.297  1.00 79.90           O  
ANISOU 3651  O   THR A 513     9398  10938  10024   -417    186   -559       O  
ATOM   3652  CB  THR A 513      27.719  55.158  19.122  1.00 76.89           C  
ANISOU 3652  CB  THR A 513     8951  10426   9836   -373    219   -552       C  
ATOM   3653  OG1 THR A 513      26.533  55.584  18.450  1.00 85.49           O  
ANISOU 3653  OG1 THR A 513    10038  11483  10962   -364    246   -547       O  
ATOM   3654  CG2 THR A 513      28.921  55.712  18.368  1.00 75.42           C  
ANISOU 3654  CG2 THR A 513     8743  10197   9716   -352    219   -535       C  
ATOM   3655  N   GLU A 514      25.538  52.632  19.475  1.00 79.92           N  
ANISOU 3655  N   GLU A 514     9423  10878  10065   -385    210   -492       N  
ATOM   3656  CA  GLU A 514      24.402  52.080  20.219  1.00 80.56           C  
ANISOU 3656  CA  GLU A 514     9522  10996  10092   -405    217   -507       C  
ATOM   3657  C   GLU A 514      24.789  50.873  21.071  1.00 81.13           C  
ANISOU 3657  C   GLU A 514     9626  11122  10079   -418    193   -487       C  
ATOM   3658  O   GLU A 514      24.013  50.427  21.919  1.00 80.73           O  
ANISOU 3658  O   GLU A 514     9588  11108   9976   -439    200   -502       O  
ATOM   3659  CB  GLU A 514      23.263  51.699  19.269  1.00 82.07           C  
ANISOU 3659  CB  GLU A 514     9729  11158  10294   -390    232   -473       C  
ATOM   3660  CG  GLU A 514      22.775  52.828  18.368  1.00 83.03           C  
ANISOU 3660  CG  GLU A 514     9823  11227  10497   -373    255   -486       C  
ATOM   3661  CD  GLU A 514      21.993  53.889  19.114  1.00 87.82           C  
ANISOU 3661  CD  GLU A 514    10397  11837  11132   -396    279   -554       C  
ATOM   3662  OE1 GLU A 514      21.432  53.581  20.190  1.00 87.91           O  
ANISOU 3662  OE1 GLU A 514    10415  11892  11094   -423    283   -586       O  
ATOM   3663  OE2 GLU A 514      21.936  55.034  18.615  1.00 90.19           O  
ANISOU 3663  OE2 GLU A 514    10666  12097  11506   -386    296   -574       O  
ATOM   3664  N   LEU A 515      25.995  50.356  20.843  1.00 78.09           N  
ANISOU 3664  N   LEU A 515     9251  10737   9682   -405    167   -451       N  
ATOM   3665  CA  LEU A 515      26.504  49.210  21.585  1.00 74.85           C  
ANISOU 3665  CA  LEU A 515     8870  10374   9197   -413    140   -426       C  
ATOM   3666  C   LEU A 515      27.261  49.630  22.832  1.00 71.73           C  
ANISOU 3666  C   LEU A 515     8457  10023   8773   -433    126   -474       C  
ATOM   3667  O   LEU A 515      27.419  48.836  23.758  1.00 70.16           O  
ANISOU 3667  O   LEU A 515     8280   9875   8504   -445    108   -467       O  
ATOM   3668  CB  LEU A 515      27.429  48.378  20.699  1.00 75.58           C  
ANISOU 3668  CB  LEU A 515     8981  10446   9292   -388    117   -364       C  
ATOM   3669  CG  LEU A 515      26.803  47.691  19.488  1.00 80.43           C  
ANISOU 3669  CG  LEU A 515     9616  11024   9918   -367    125   -312       C  
ATOM   3670  CD1 LEU A 515      27.882  47.355  18.466  1.00 81.52           C  
ANISOU 3670  CD1 LEU A 515     9758  11132  10082   -339    107   -266       C  
ATOM   3671  CD2 LEU A 515      26.010  46.454  19.898  1.00 75.09           C  
ANISOU 3671  CD2 LEU A 515     8973  10378   9181   -376    122   -285       C  
ATOM   3672  N   VAL A 516      27.731  50.876  22.843  1.00 71.67           N  
ANISOU 3672  N   VAL A 516     8410   9996   8824   -434    132   -523       N  
ATOM   3673  CA  VAL A 516      28.603  51.378  23.908  1.00 72.96           C  
ANISOU 3673  CA  VAL A 516     8551  10196   8973   -449    115   -574       C  
ATOM   3674  C   VAL A 516      28.073  51.113  25.324  1.00 76.70           C  
ANISOU 3674  C   VAL A 516     9034  10737   9369   -475    113   -611       C  
ATOM   3675  O   VAL A 516      28.831  50.632  26.175  1.00 79.90           O  
ANISOU 3675  O   VAL A 516     9450  11191   9718   -481     84   -613       O  
ATOM   3676  CB  VAL A 516      28.957  52.870  23.710  1.00 72.91           C  
ANISOU 3676  CB  VAL A 516     8495  10154   9053   -448    129   -630       C  
ATOM   3677  CG1 VAL A 516      29.794  53.391  24.870  1.00 73.68           C  
ANISOU 3677  CG1 VAL A 516     8566  10293   9136   -464    110   -692       C  
ATOM   3678  CG2 VAL A 516      29.698  53.069  22.396  1.00 68.76           C  
ANISOU 3678  CG2 VAL A 516     7961   9568   8597   -421    129   -588       C  
ATOM   3679  N   PRO A 517      26.775  51.402  25.584  1.00 80.71           N  
ANISOU 3679  N   PRO A 517     9542  11251   9873   -490    143   -638       N  
ATOM   3680  CA  PRO A 517      26.226  51.089  26.917  1.00 77.82           C  
ANISOU 3680  CA  PRO A 517     9188  10951   9429   -515    146   -669       C  
ATOM   3681  C   PRO A 517      26.313  49.613  27.313  1.00 76.10           C  
ANISOU 3681  C   PRO A 517     9016  10774   9125   -515    127   -610       C  
ATOM   3682  O   PRO A 517      26.389  49.293  28.505  1.00 75.39           O  
ANISOU 3682  O   PRO A 517     8937  10746   8961   -530    117   -628       O  
ATOM   3683  CB  PRO A 517      24.759  51.532  26.818  1.00 78.15           C  
ANISOU 3683  CB  PRO A 517     9223  10977   9494   -527    186   -694       C  
ATOM   3684  CG  PRO A 517      24.500  51.788  25.366  1.00 80.76           C  
ANISOU 3684  CG  PRO A 517     9548  11237   9902   -505    198   -661       C  
ATOM   3685  CD  PRO A 517      25.818  52.188  24.783  1.00 79.34           C  
ANISOU 3685  CD  PRO A 517     9349  11026   9769   -486    177   -651       C  
ATOM   3686  N   TYR A 518      26.332  48.725  26.328  1.00 73.60           N  
ANISOU 3686  N   TYR A 518     8725  10423   8816   -496    121   -540       N  
ATOM   3687  CA  TYR A 518      26.349  47.289  26.607  1.00 78.01           C  
ANISOU 3687  CA  TYR A 518     9325  11011   9303   -494    105   -480       C  
ATOM   3688  C   TYR A 518      27.728  46.649  26.410  1.00 72.85           C  
ANISOU 3688  C   TYR A 518     8682  10359   8637   -477     66   -438       C  
ATOM   3689  O   TYR A 518      27.873  45.417  26.457  1.00 68.18           O  
ANISOU 3689  O   TYR A 518     8125   9783   7999   -471     50   -381       O  
ATOM   3690  CB  TYR A 518      25.285  46.585  25.753  1.00 90.23           C  
ANISOU 3690  CB  TYR A 518    10895  12524  10863   -487    127   -434       C  
ATOM   3691  CG  TYR A 518      23.902  47.206  25.862  1.00100.46           C  
ANISOU 3691  CG  TYR A 518    12178  13812  12178   -503    165   -475       C  
ATOM   3692  CD1 TYR A 518      23.094  46.974  26.985  1.00106.34           C  
ANISOU 3692  CD1 TYR A 518    12934  14607  12864   -527    183   -497       C  
ATOM   3693  CD2 TYR A 518      23.405  48.028  24.850  1.00102.62           C  
ANISOU 3693  CD2 TYR A 518    12430  14032  12530   -492    184   -490       C  
ATOM   3694  CE1 TYR A 518      21.833  47.540  27.092  1.00115.55           C  
ANISOU 3694  CE1 TYR A 518    14087  15766  14051   -542    219   -537       C  
ATOM   3695  CE2 TYR A 518      22.144  48.598  24.944  1.00113.79           C  
ANISOU 3695  CE2 TYR A 518    13831  15438  13966   -505    218   -528       C  
ATOM   3696  CZ  TYR A 518      21.361  48.354  26.066  1.00120.70           C  
ANISOU 3696  CZ  TYR A 518    14715  16360  14784   -531    236   -553       C  
ATOM   3697  OH  TYR A 518      20.106  48.920  26.162  1.00122.41           O  
ANISOU 3697  OH  TYR A 518    14916  16568  15026   -545    270   -593       O  
ATOM   3698  N   LEU A 519      28.737  47.500  26.223  1.00 70.23           N  
ANISOU 3698  N   LEU A 519     8320  10012   8353   -469     51   -469       N  
ATOM   3699  CA  LEU A 519      30.099  47.064  25.891  1.00 68.14           C  
ANISOU 3699  CA  LEU A 519     8058   9739   8094   -451     15   -435       C  
ATOM   3700  C   LEU A 519      30.682  46.019  26.852  1.00 64.84           C  
ANISOU 3700  C   LEU A 519     7667   9378   7592   -454    -18   -408       C  
ATOM   3701  O   LEU A 519      31.242  45.017  26.410  1.00 61.48           O  
ANISOU 3701  O   LEU A 519     7263   8942   7154   -439    -39   -348       O  
ATOM   3702  CB  LEU A 519      31.026  48.280  25.749  1.00 68.20           C  
ANISOU 3702  CB  LEU A 519     8023   9725   8166   -447      8   -485       C  
ATOM   3703  CG  LEU A 519      32.453  48.140  25.211  1.00 66.41           C  
ANISOU 3703  CG  LEU A 519     7786   9475   7970   -427    -21   -461       C  
ATOM   3704  CD1 LEU A 519      32.509  47.344  23.914  1.00 65.61           C  
ANISOU 3704  CD1 LEU A 519     7707   9326   7894   -404    -20   -389       C  
ATOM   3705  CD2 LEU A 519      33.046  49.525  25.012  1.00 66.43           C  
ANISOU 3705  CD2 LEU A 519     7741   9448   8052   -426    -14   -518       C  
ATOM   3706  N   ALA A 520      30.515  46.236  28.153  1.00 68.03           N  
ANISOU 3706  N   ALA A 520     8067   9842   7938   -473    -21   -451       N  
ATOM   3707  CA  ALA A 520      31.064  45.326  29.160  1.00 70.40           C  
ANISOU 3707  CA  ALA A 520     8392  10203   8154   -475    -52   -428       C  
ATOM   3708  C   ALA A 520      30.402  43.959  29.075  1.00 71.37           C  
ANISOU 3708  C   ALA A 520     8558  10330   8227   -474    -45   -356       C  
ATOM   3709  O   ALA A 520      31.075  42.925  29.096  1.00 75.08           O  
ANISOU 3709  O   ALA A 520     9051  10811   8666   -462    -74   -301       O  
ATOM   3710  CB  ALA A 520      30.908  45.915  30.555  1.00 70.28           C  
ANISOU 3710  CB  ALA A 520     8365  10254   8083   -495    -53   -493       C  
ATOM   3711  N   TYR A 521      29.078  43.970  28.963  1.00 76.27           N  
ANISOU 3711  N   TYR A 521     9188  10943   8850   -486     -7   -358       N  
ATOM   3712  CA  TYR A 521      28.278  42.751  28.874  1.00 77.31           C  
ANISOU 3712  CA  TYR A 521     9356  11074   8944   -487      7   -297       C  
ATOM   3713  C   TYR A 521      28.610  42.002  27.573  1.00 72.87           C  
ANISOU 3713  C   TYR A 521     8805  10454   8428   -465     -3   -235       C  
ATOM   3714  O   TYR A 521      28.824  40.780  27.585  1.00 71.52           O  
ANISOU 3714  O   TYR A 521     8662  10290   8224   -457    -19   -175       O  
ATOM   3715  CB  TYR A 521      26.787  43.113  29.017  1.00 88.11           C  
ANISOU 3715  CB  TYR A 521    10722  12440  10314   -506     52   -325       C  
ATOM   3716  CG  TYR A 521      25.780  41.992  28.815  1.00 99.45           C  
ANISOU 3716  CG  TYR A 521    12190  13867  11730   -509     74   -271       C  
ATOM   3717  CD1 TYR A 521      25.843  40.811  29.564  1.00105.30           C  
ANISOU 3717  CD1 TYR A 521    12964  14648  12399   -512     65   -221       C  
ATOM   3718  CD2 TYR A 521      24.735  42.133  27.891  1.00104.52           C  
ANISOU 3718  CD2 TYR A 521    12827  14460  12427   -507    105   -271       C  
ATOM   3719  CE1 TYR A 521      24.911  39.793  29.379  1.00109.24           C  
ANISOU 3719  CE1 TYR A 521    13487  15134  12886   -515     89   -173       C  
ATOM   3720  CE2 TYR A 521      23.800  41.125  27.701  1.00109.01           C  
ANISOU 3720  CE2 TYR A 521    13419  15017  12982   -510    126   -227       C  
ATOM   3721  CZ  TYR A 521      23.890  39.959  28.446  1.00111.85           C  
ANISOU 3721  CZ  TYR A 521    13809  15413  13275   -515    119   -179       C  
ATOM   3722  OH  TYR A 521      22.960  38.961  28.254  1.00114.66           O  
ANISOU 3722  OH  TYR A 521    14186  15754  13626   -518    141   -136       O  
ATOM   3723  N   ILE A 522      28.710  42.743  26.468  1.00 64.17           N  
ANISOU 3723  N   ILE A 522     7680   9297   7404   -453      4   -251       N  
ATOM   3724  CA  ILE A 522      29.174  42.155  25.205  1.00 61.11           C  
ANISOU 3724  CA  ILE A 522     7300   8859   7061   -429     -7   -199       C  
ATOM   3725  C   ILE A 522      30.533  41.459  25.354  1.00 61.05           C  
ANISOU 3725  C   ILE A 522     7301   8865   7032   -416    -49   -164       C  
ATOM   3726  O   ILE A 522      30.685  40.290  24.971  1.00 59.82           O  
ANISOU 3726  O   ILE A 522     7168   8698   6863   -404    -61   -104       O  
ATOM   3727  CB  ILE A 522      29.178  43.177  24.034  1.00 59.29           C  
ANISOU 3727  CB  ILE A 522     7042   8573   6915   -416      7   -223       C  
ATOM   3728  CG1 ILE A 522      27.737  43.613  23.723  1.00 58.44           C  
ANISOU 3728  CG1 ILE A 522     6930   8446   6830   -424     46   -244       C  
ATOM   3729  CG2 ILE A 522      29.811  42.577  22.774  1.00 53.24           C  
ANISOU 3729  CG2 ILE A 522     6282   7759   6187   -389     -7   -171       C  
ATOM   3730  CD1 ILE A 522      27.604  44.941  23.010  1.00 57.39           C  
ANISOU 3730  CD1 ILE A 522     6764   8271   6769   -418     65   -285       C  
ATOM   3731  N   LEU A 523      31.513  42.158  25.926  1.00 61.34           N  
ANISOU 3731  N   LEU A 523     7315   8924   7066   -417    -71   -203       N  
ATOM   3732  CA  LEU A 523      32.873  41.603  25.985  1.00 64.30           C  
ANISOU 3732  CA  LEU A 523     7693   9307   7432   -403   -112   -174       C  
ATOM   3733  C   LEU A 523      32.958  40.335  26.815  1.00 65.15           C  
ANISOU 3733  C   LEU A 523     7833   9459   7462   -405   -133   -127       C  
ATOM   3734  O   LEU A 523      33.651  39.381  26.437  1.00 64.18           O  
ANISOU 3734  O   LEU A 523     7724   9323   7339   -390   -158    -74       O  
ATOM   3735  CB  LEU A 523      33.887  42.630  26.492  1.00 65.53           C  
ANISOU 3735  CB  LEU A 523     7815   9480   7602   -404   -133   -231       C  
ATOM   3736  CG  LEU A 523      34.201  43.732  25.485  1.00 65.76           C  
ANISOU 3736  CG  LEU A 523     7810   9454   7722   -395   -119   -262       C  
ATOM   3737  CD1 LEU A 523      34.810  44.919  26.209  1.00 64.50           C  
ANISOU 3737  CD1 LEU A 523     7613   9316   7577   -404   -128   -335       C  
ATOM   3738  CD2 LEU A 523      35.099  43.214  24.368  1.00 63.30           C  
ANISOU 3738  CD2 LEU A 523     7500   9096   7454   -371   -135   -214       C  
ATOM   3739  N   ASP A 524      32.248  40.335  27.941  1.00 67.22           N  
ANISOU 3739  N   ASP A 524     8107   9773   7662   -424   -122   -146       N  
ATOM   3740  CA  ASP A 524      32.121  39.147  28.770  1.00 69.59           C  
ANISOU 3740  CA  ASP A 524     8440  10116   7886   -428   -133    -97       C  
ATOM   3741  C   ASP A 524      31.883  37.869  27.964  1.00 69.74           C  
ANISOU 3741  C   ASP A 524     8485  10097   7918   -416   -130    -23       C  
ATOM   3742  O   ASP A 524      32.528  36.845  28.213  1.00 71.73           O  
ANISOU 3742  O   ASP A 524     8755  10362   8138   -406   -158     29       O  
ATOM   3743  CB  ASP A 524      31.002  39.346  29.783  1.00 73.80           C  
ANISOU 3743  CB  ASP A 524     8983  10696   8363   -451   -103   -124       C  
ATOM   3744  CG  ASP A 524      31.517  39.788  31.131  1.00 78.07           C  
ANISOU 3744  CG  ASP A 524     9517  11307   8839   -459   -124   -165       C  
ATOM   3745  OD1 ASP A 524      32.583  40.443  31.189  1.00 80.46           O  
ANISOU 3745  OD1 ASP A 524     9795  11615   9162   -451   -155   -201       O  
ATOM   3746  OD2 ASP A 524      30.857  39.470  32.140  1.00 82.26           O  
ANISOU 3746  OD2 ASP A 524    10068  11890   9299   -474   -110   -162       O  
ATOM   3747  N   THR A 525      30.977  37.943  26.986  1.00 65.12           N  
ANISOU 3747  N   THR A 525     7898   9464   7381   -415    -98    -19       N  
ATOM   3748  CA  THR A 525      30.608  36.779  26.192  1.00 61.13           C  
ANISOU 3748  CA  THR A 525     7413   8921   6892   -405    -92     43       C  
ATOM   3749  C   THR A 525      31.663  36.486  25.144  1.00 60.27           C  
ANISOU 3749  C   THR A 525     7297   8770   6833   -381   -118     70       C  
ATOM   3750  O   THR A 525      32.119  35.342  25.017  1.00 57.66           O  
ANISOU 3750  O   THR A 525     6983   8433   6491   -370   -138    125       O  
ATOM   3751  CB  THR A 525      29.243  36.984  25.509  1.00 62.03           C  
ANISOU 3751  CB  THR A 525     7526   9001   7042   -411    -50     32       C  
ATOM   3752  OG1 THR A 525      28.245  37.162  26.516  1.00 66.65           O  
ANISOU 3752  OG1 THR A 525     8119   9626   7580   -434    -23      9       O  
ATOM   3753  CG2 THR A 525      28.876  35.787  24.627  1.00 57.82           C  
ANISOU 3753  CG2 THR A 525     7010   8428   6531   -398    -45     90       C  
ATOM   3754  N   LEU A 526      32.045  37.515  24.386  1.00 58.28           N  
ANISOU 3754  N   LEU A 526     7019   8487   6639   -372   -116     33       N  
ATOM   3755  CA  LEU A 526      33.075  37.344  23.363  1.00 59.39           C  
ANISOU 3755  CA  LEU A 526     7150   8587   6829   -349   -137     55       C  
ATOM   3756  C   LEU A 526      34.369  36.743  23.932  1.00 60.48           C  
ANISOU 3756  C   LEU A 526     7292   8750   6939   -342   -180     80       C  
ATOM   3757  O   LEU A 526      34.929  35.817  23.351  1.00 62.02           O  
ANISOU 3757  O   LEU A 526     7496   8921   7148   -326   -198    127       O  
ATOM   3758  CB  LEU A 526      33.345  38.654  22.619  1.00 58.55           C  
ANISOU 3758  CB  LEU A 526     7012   8448   6785   -343   -126      9       C  
ATOM   3759  CG  LEU A 526      32.157  39.324  21.915  1.00 60.24           C  
ANISOU 3759  CG  LEU A 526     7219   8632   7036   -346    -87    -13       C  
ATOM   3760  CD1 LEU A 526      32.616  40.504  21.070  1.00 56.05           C  
ANISOU 3760  CD1 LEU A 526     6660   8064   6573   -334    -79    -46       C  
ATOM   3761  CD2 LEU A 526      31.361  38.333  21.068  1.00 56.55           C  
ANISOU 3761  CD2 LEU A 526     6773   8135   6577   -336    -74     32       C  
ATOM   3762  N   VAL A 527      34.820  37.238  25.081  1.00 63.47           N  
ANISOU 3762  N   VAL A 527     7663   9177   7276   -353   -197     46       N  
ATOM   3763  CA  VAL A 527      36.016  36.673  25.707  1.00 66.99           C  
ANISOU 3763  CA  VAL A 527     8112   9652   7690   -345   -241     68       C  
ATOM   3764  C   VAL A 527      35.790  35.213  26.073  1.00 65.47           C  
ANISOU 3764  C   VAL A 527     7952   9474   7449   -343   -250    134       C  
ATOM   3765  O   VAL A 527      36.577  34.338  25.694  1.00 65.99           O  
ANISOU 3765  O   VAL A 527     8024   9522   7528   -327   -277    179       O  
ATOM   3766  CB  VAL A 527      36.485  37.486  26.934  1.00 70.34           C  
ANISOU 3766  CB  VAL A 527     8521  10132   8074   -356   -260     15       C  
ATOM   3767  CG1 VAL A 527      37.504  36.697  27.744  1.00 69.94           C  
ANISOU 3767  CG1 VAL A 527     8480  10121   7974   -347   -306     45       C  
ATOM   3768  CG2 VAL A 527      37.080  38.817  26.485  1.00 69.24           C  
ANISOU 3768  CG2 VAL A 527     8343   9969   7997   -353   -259    -45       C  
ATOM   3769  N   PHE A 528      34.695  34.938  26.774  1.00 64.65           N  
ANISOU 3769  N   PHE A 528     7868   9400   7296   -359   -227    140       N  
ATOM   3770  CA  PHE A 528      34.430  33.573  27.184  1.00 60.90           C  
ANISOU 3770  CA  PHE A 528     7423   8939   6778   -359   -231    205       C  
ATOM   3771  C   PHE A 528      34.454  32.640  25.987  1.00 59.04           C  
ANISOU 3771  C   PHE A 528     7194   8646   6594   -343   -229    255       C  
ATOM   3772  O   PHE A 528      34.895  31.501  26.094  1.00 63.91           O  
ANISOU 3772  O   PHE A 528     7825   9261   7196   -333   -250    310       O  
ATOM   3773  CB  PHE A 528      33.109  33.450  27.940  1.00 64.84           C  
ANISOU 3773  CB  PHE A 528     7940   9468   7227   -379   -195    204       C  
ATOM   3774  CG  PHE A 528      32.875  32.072  28.500  1.00 65.67           C  
ANISOU 3774  CG  PHE A 528     8075   9590   7285   -379   -198    273       C  
ATOM   3775  CD1 PHE A 528      33.329  31.741  29.775  1.00 63.87           C  
ANISOU 3775  CD1 PHE A 528     7862   9423   6982   -381   -221    290       C  
ATOM   3776  CD2 PHE A 528      32.239  31.089  27.738  1.00 63.66           C  
ANISOU 3776  CD2 PHE A 528     7833   9291   7063   -375   -178    320       C  
ATOM   3777  CE1 PHE A 528      33.137  30.464  30.283  1.00 64.93           C  
ANISOU 3777  CE1 PHE A 528     8024   9571   7075   -380   -222    359       C  
ATOM   3778  CE2 PHE A 528      32.045  29.808  28.242  1.00 66.88           C  
ANISOU 3778  CE2 PHE A 528     8266   9709   7435   -375   -179    385       C  
ATOM   3779  CZ  PHE A 528      32.491  29.494  29.522  1.00 65.21           C  
ANISOU 3779  CZ  PHE A 528     8070   9556   7149   -377   -199    407       C  
ATOM   3780  N   ALA A 529      33.990  33.128  24.841  1.00 57.11           N  
ANISOU 3780  N   ALA A 529     6936   8353   6410   -339   -205    234       N  
ATOM   3781  CA  ALA A 529      34.003  32.337  23.614  1.00 54.79           C  
ANISOU 3781  CA  ALA A 529     6646   8006   6167   -322   -203    273       C  
ATOM   3782  C   ALA A 529      35.409  31.874  23.188  1.00 57.80           C  
ANISOU 3782  C   ALA A 529     7019   8370   6572   -302   -241    299       C  
ATOM   3783  O   ALA A 529      35.562  30.795  22.602  1.00 57.34           O  
ANISOU 3783  O   ALA A 529     6971   8283   6534   -289   -249    346       O  
ATOM   3784  CB  ALA A 529      33.337  33.115  22.493  1.00 53.36           C  
ANISOU 3784  CB  ALA A 529     6450   7784   6042   -319   -173    240       C  
ATOM   3785  N   PHE A 530      36.430  32.690  23.461  1.00 62.69           N  
ANISOU 3785  N   PHE A 530     7620   9004   7195   -298   -265    266       N  
ATOM   3786  CA  PHE A 530      37.826  32.286  23.198  1.00 68.95           C  
ANISOU 3786  CA  PHE A 530     8404   9785   8010   -280   -303    287       C  
ATOM   3787  C   PHE A 530      38.145  30.899  23.756  1.00 72.19           C  
ANISOU 3787  C   PHE A 530     8835  10211   8384   -275   -329    347       C  
ATOM   3788  O   PHE A 530      38.631  30.023  23.038  1.00 72.12           O  
ANISOU 3788  O   PHE A 530     8827  10167   8407   -260   -342    386       O  
ATOM   3789  CB  PHE A 530      38.807  33.288  23.801  1.00 70.14           C  
ANISOU 3789  CB  PHE A 530     8531   9963   8155   -282   -327    240       C  
ATOM   3790  CG  PHE A 530      38.992  34.528  22.981  1.00 70.57           C  
ANISOU 3790  CG  PHE A 530     8558   9986   8269   -278   -310    191       C  
ATOM   3791  CD1 PHE A 530      39.381  34.446  21.642  1.00 70.85           C  
ANISOU 3791  CD1 PHE A 530     8584   9968   8369   -261   -304    205       C  
ATOM   3792  CD2 PHE A 530      38.811  35.783  23.554  1.00 70.74           C  
ANISOU 3792  CD2 PHE A 530     8562  10032   8284   -292   -300    131       C  
ATOM   3793  CE1 PHE A 530      39.561  35.595  20.887  1.00 71.98           C  
ANISOU 3793  CE1 PHE A 530     8702  10082   8567   -256   -286    165       C  
ATOM   3794  CE2 PHE A 530      38.989  36.937  22.808  1.00 71.85           C  
ANISOU 3794  CE2 PHE A 530     8674  10139   8485   -289   -283     88       C  
ATOM   3795  CZ  PHE A 530      39.360  36.843  21.472  1.00 74.10           C  
ANISOU 3795  CZ  PHE A 530     8952  10370   8832   -271   -275    108       C  
ATOM   3796  N   SER A 531      37.848  30.710  25.039  1.00 76.22           N  
ANISOU 3796  N   SER A 531     9361  10774   8826   -288   -335    354       N  
ATOM   3797  CA  SER A 531      38.084  29.438  25.715  1.00 80.68           C  
ANISOU 3797  CA  SER A 531     9947  11358   9349   -284   -357    414       C  
ATOM   3798  C   SER A 531      37.123  28.342  25.273  1.00 82.17           C  
ANISOU 3798  C   SER A 531    10156  11517   9549   -285   -331    464       C  
ATOM   3799  O   SER A 531      37.452  27.156  25.334  1.00 87.21           O  
ANISOU 3799  O   SER A 531    10805  12146  10184   -276   -348    521       O  
ATOM   3800  CB  SER A 531      38.015  29.619  27.229  1.00 82.42           C  
ANISOU 3800  CB  SER A 531    10180  11648   9489   -296   -369    407       C  
ATOM   3801  OG  SER A 531      36.988  30.524  27.589  1.00 86.51           O  
ANISOU 3801  OG  SER A 531    10698  12188   9985   -316   -333    361       O  
ATOM   3802  N   LYS A 532      35.941  28.733  24.815  1.00 80.98           N  
ANISOU 3802  N   LYS A 532    10006  11349   9414   -297   -289    441       N  
ATOM   3803  CA  LYS A 532      34.964  27.754  24.379  1.00 78.93           C  
ANISOU 3803  CA  LYS A 532     9760  11059   9169   -299   -262    481       C  
ATOM   3804  C   LYS A 532      35.225  27.246  22.968  1.00 75.42           C  
ANISOU 3804  C   LYS A 532     9306  10555   8795   -280   -265    496       C  
ATOM   3805  O   LYS A 532      35.178  26.045  22.741  1.00 77.11           O  
ANISOU 3805  O   LYS A 532     9529  10747   9023   -273   -268    545       O  
ATOM   3806  CB  LYS A 532      33.541  28.310  24.508  1.00 84.41           C  
ANISOU 3806  CB  LYS A 532    10459  11760   9852   -318   -218    450       C  
ATOM   3807  CG  LYS A 532      32.459  27.240  24.584  1.00 84.44           C  
ANISOU 3807  CG  LYS A 532    10480  11751   9851   -325   -190    492       C  
ATOM   3808  CD  LYS A 532      31.098  27.831  24.943  1.00 85.32           C  
ANISOU 3808  CD  LYS A 532    10595  11878   9943   -346   -147    459       C  
ATOM   3809  CE  LYS A 532      30.113  26.758  25.393  1.00 81.35           C  
ANISOU 3809  CE  LYS A 532    10111  11374   9422   -357   -120    504       C  
ATOM   3810  NZ  LYS A 532      29.824  25.764  24.319  1.00 84.27           N  
ANISOU 3810  NZ  LYS A 532    10479  11687   9853   -345   -114    536       N  
ATOM   3811  N   TYR A 533      35.513  28.153  22.035  1.00 74.86           N  
ANISOU 3811  N   TYR A 533     9215  10460   8769   -272   -262    454       N  
ATOM   3812  CA  TYR A 533      35.543  27.829  20.596  1.00 76.70           C  
ANISOU 3812  CA  TYR A 533     9438  10638   9065   -254   -255    461       C  
ATOM   3813  C   TYR A 533      36.716  26.963  20.154  1.00 82.63           C  
ANISOU 3813  C   TYR A 533    10185  11367   9844   -235   -288    497       C  
ATOM   3814  O   TYR A 533      37.842  27.150  20.614  1.00 86.92           O  
ANISOU 3814  O   TYR A 533    10722  11929  10377   -230   -319    497       O  
ATOM   3815  CB  TYR A 533      35.551  29.115  19.749  1.00 71.34           C  
ANISOU 3815  CB  TYR A 533     8740   9942   8423   -249   -241    409       C  
ATOM   3816  CG  TYR A 533      34.203  29.768  19.539  1.00 69.29           C  
ANISOU 3816  CG  TYR A 533     8482   9679   8166   -260   -202    377       C  
ATOM   3817  CD1 TYR A 533      33.074  29.329  20.235  1.00 68.05           C  
ANISOU 3817  CD1 TYR A 533     8341   9540   7975   -278   -181    388       C  
ATOM   3818  CD2 TYR A 533      34.060  30.854  18.672  1.00 66.62           C  
ANISOU 3818  CD2 TYR A 533     8128   9320   7866   -254   -186    336       C  
ATOM   3819  CE1 TYR A 533      31.841  29.930  20.057  1.00 63.92           C  
ANISOU 3819  CE1 TYR A 533     7817   9013   7458   -288   -147    356       C  
ATOM   3820  CE2 TYR A 533      32.828  31.466  18.487  1.00 64.35           C  
ANISOU 3820  CE2 TYR A 533     7838   9028   7582   -263   -152    307       C  
ATOM   3821  CZ  TYR A 533      31.718  30.991  19.186  1.00 64.61           C  
ANISOU 3821  CZ  TYR A 533     7886   9079   7582   -281   -134    316       C  
ATOM   3822  OH  TYR A 533      30.484  31.572  19.046  1.00 57.74           O  
ANISOU 3822  OH  TYR A 533     7014   8205   6719   -290   -101    285       O  
ATOM   3823  N   GLN A 534      36.441  26.028  19.246  1.00 88.41           N  
ANISOU 3823  N   GLN A 534    10918  12058  10614   -223   -281    524       N  
ATOM   3824  CA  GLN A 534      37.481  25.362  18.468  1.00 88.89           C  
ANISOU 3824  CA  GLN A 534    10968  12088  10717   -202   -306    547       C  
ATOM   3825  C   GLN A 534      37.956  26.347  17.426  1.00 88.42           C  
ANISOU 3825  C   GLN A 534    10891  12008  10699   -189   -301    507       C  
ATOM   3826  O   GLN A 534      37.588  27.521  17.479  1.00 84.72           O  
ANISOU 3826  O   GLN A 534    10417  11551  10222   -197   -284    466       O  
ATOM   3827  CB  GLN A 534      36.945  24.109  17.775  1.00 96.40           C  
ANISOU 3827  CB  GLN A 534    11924  13003  11701   -194   -296    581       C  
ATOM   3828  CG  GLN A 534      37.385  22.798  18.408  1.00100.84           C  
ANISOU 3828  CG  GLN A 534    12495  13566  12254   -192   -319    636       C  
ATOM   3829  CD  GLN A 534      36.694  21.594  17.789  1.00107.27           C  
ANISOU 3829  CD  GLN A 534    13310  14342  13104   -187   -305    665       C  
ATOM   3830  OE1 GLN A 534      36.318  21.609  16.610  1.00108.82           O  
ANISOU 3830  OE1 GLN A 534    13497  14506  13344   -176   -289    644       O  
ATOM   3831  NE2 GLN A 534      36.522  20.541  18.585  1.00104.83           N  
ANISOU 3831  NE2 GLN A 534    13014  14039  12779   -194   -310    714       N  
ATOM   3832  N   HIS A 535      38.730  25.869  16.456  1.00 88.49           N  
ANISOU 3832  N   HIS A 535    10888  11982  10752   -169   -314    520       N  
ATOM   3833  CA  HIS A 535      39.439  26.780  15.570  1.00 87.59           C  
ANISOU 3833  CA  HIS A 535    10755  11850  10673   -155   -312    488       C  
ATOM   3834  C   HIS A 535      38.602  27.460  14.527  1.00 82.47           C  
ANISOU 3834  C   HIS A 535    10103  11182  10049   -149   -279    459       C  
ATOM   3835  O   HIS A 535      38.678  28.680  14.395  1.00 84.49           O  
ANISOU 3835  O   HIS A 535    10350  11443  10311   -150   -267    424       O  
ATOM   3836  CB  HIS A 535      40.686  26.152  14.950  1.00 89.08           C  
ANISOU 3836  CB  HIS A 535    10932  12014  10900   -135   -337    508       C  
ATOM   3837  CG  HIS A 535      41.622  27.173  14.343  1.00 89.54           C  
ANISOU 3837  CG  HIS A 535    10970  12062  10989   -124   -338    478       C  
ATOM   3838  ND1 HIS A 535      42.462  27.925  15.091  1.00 88.28           N  
ANISOU 3838  ND1 HIS A 535    10800  11924  10818   -131   -356    459       N  
ATOM   3839  CD2 HIS A 535      41.794  27.585  13.024  1.00 85.61           C  
ANISOU 3839  CD2 HIS A 535    10460  11533  10535   -106   -319    462       C  
ATOM   3840  CE1 HIS A 535      43.147  28.760  14.290  1.00 87.57           C  
ANISOU 3840  CE1 HIS A 535    10691  11814  10768   -119   -348    434       C  
ATOM   3841  NE2 HIS A 535      42.741  28.550  13.024  1.00 87.30           N  
ANISOU 3841  NE2 HIS A 535    10657  11748  10765   -104   -324    438       N  
ATOM   3842  N   LYS A 536      37.807  26.693  13.783  1.00 77.31           N  
ANISOU 3842  N   LYS A 536     9456  10506   9414   -141   -264    473       N  
ATOM   3843  CA  LYS A 536      36.960  27.262  12.717  1.00 76.37           C  
ANISOU 3843  CA  LYS A 536     9333  10368   9316   -132   -235    446       C  
ATOM   3844  C   LYS A 536      36.123  28.462  13.192  1.00 75.44           C  
ANISOU 3844  C   LYS A 536     9218  10271   9176   -148   -212    412       C  
ATOM   3845  O   LYS A 536      35.997  29.472  12.480  1.00 76.80           O  
ANISOU 3845  O   LYS A 536     9380  10433   9368   -139   -195    383       O  
ATOM   3846  CB  LYS A 536      36.068  26.189  12.077  1.00 77.01           C  
ANISOU 3846  CB  LYS A 536     9419  10427   9413   -124   -225    462       C  
ATOM   3847  CG  LYS A 536      35.568  25.141  13.063  1.00 93.45           C  
ANISOU 3847  CG  LYS A 536    11515  12520  11471   -141   -231    493       C  
ATOM   3848  CD  LYS A 536      34.735  24.048  12.396  1.00102.48           C  
ANISOU 3848  CD  LYS A 536    12659  13637  12640   -133   -221    506       C  
ATOM   3849  CE  LYS A 536      34.693  22.771  13.236  1.00102.15           C  
ANISOU 3849  CE  LYS A 536    12626  13597  12590   -145   -232    548       C  
ATOM   3850  NZ  LYS A 536      34.451  23.038  14.691  1.00104.43           N  
ANISOU 3850  NZ  LYS A 536    12929  13921  12828   -169   -231    559       N  
ATOM   3851  N   ASN A 537      35.575  28.358  14.401  1.00 71.10           N  
ANISOU 3851  N   ASN A 537     8679   9750   8586   -171   -212    415       N  
ATOM   3852  CA  ASN A 537      34.704  29.400  14.928  1.00 64.56           C  
ANISOU 3852  CA  ASN A 537     7852   8943   7736   -188   -189    381       C  
ATOM   3853  C   ASN A 537      35.429  30.560  15.581  1.00 62.59           C  
ANISOU 3853  C   ASN A 537     7592   8716   7472   -196   -197    353       C  
ATOM   3854  O   ASN A 537      34.869  31.656  15.681  1.00 60.07           O  
ANISOU 3854  O   ASN A 537     7266   8405   7151   -205   -176    317       O  
ATOM   3855  CB  ASN A 537      33.668  28.817  15.872  1.00 61.34           C  
ANISOU 3855  CB  ASN A 537     7459   8555   7290   -209   -179    394       C  
ATOM   3856  CG  ASN A 537      32.542  28.125  15.133  1.00 63.62           C  
ANISOU 3856  CG  ASN A 537     7753   8819   7601   -203   -159    401       C  
ATOM   3857  OD1 ASN A 537      32.453  28.189  13.898  1.00 63.18           O  
ANISOU 3857  OD1 ASN A 537     7688   8734   7583   -183   -153    392       O  
ATOM   3858  ND2 ASN A 537      31.677  27.436  15.884  1.00 57.73           N  
ANISOU 3858  ND2 ASN A 537     7019   8085   6831   -220   -148    418       N  
ATOM   3859  N   LEU A 538      36.665  30.325  16.025  1.00 62.86           N  
ANISOU 3859  N   LEU A 538     7622   8761   7502   -194   -227    367       N  
ATOM   3860  CA  LEU A 538      37.524  31.424  16.499  1.00 62.44           C  
ANISOU 3860  CA  LEU A 538     7553   8724   7447   -198   -237    336       C  
ATOM   3861  C   LEU A 538      37.756  32.451  15.382  1.00 59.24           C  
ANISOU 3861  C   LEU A 538     7129   8289   7090   -183   -219    308       C  
ATOM   3862  O   LEU A 538      37.879  33.646  15.667  1.00 58.74           O  
ANISOU 3862  O   LEU A 538     7052   8235   7032   -191   -210    271       O  
ATOM   3863  CB  LEU A 538      38.854  30.924  17.107  1.00 65.71           C  
ANISOU 3863  CB  LEU A 538     7964   9152   7852   -195   -275    356       C  
ATOM   3864  CG  LEU A 538      38.836  30.305  18.533  1.00 72.22           C  
ANISOU 3864  CG  LEU A 538     8803  10018   8618   -211   -297    376       C  
ATOM   3865  CD1 LEU A 538      40.026  29.383  18.784  1.00 72.90           C  
ANISOU 3865  CD1 LEU A 538     8889  10106   8704   -200   -336    412       C  
ATOM   3866  CD2 LEU A 538      38.718  31.298  19.686  1.00 67.41           C  
ANISOU 3866  CD2 LEU A 538     8191   9454   7969   -230   -297    338       C  
ATOM   3867  N   LEU A 539      37.756  31.997  14.123  1.00 53.18           N  
ANISOU 3867  N   LEU A 539     6361   7486   6358   -162   -211    326       N  
ATOM   3868  CA  LEU A 539      37.995  32.886  12.989  1.00 53.74           C  
ANISOU 3868  CA  LEU A 539     6417   7530   6473   -145   -192    307       C  
ATOM   3869  C   LEU A 539      36.868  33.892  12.825  1.00 56.56           C  
ANISOU 3869  C   LEU A 539     6773   7887   6831   -151   -161    276       C  
ATOM   3870  O   LEU A 539      37.106  35.082  12.558  1.00 58.00           O  
ANISOU 3870  O   LEU A 539     6939   8060   7039   -148   -147    249       O  
ATOM   3871  CB  LEU A 539      38.187  32.088  11.694  1.00 53.86           C  
ANISOU 3871  CB  LEU A 539     6434   7513   6518   -119   -191    333       C  
ATOM   3872  CG  LEU A 539      39.615  31.708  11.256  1.00 58.78           C  
ANISOU 3872  CG  LEU A 539     7046   8120   7169   -103   -212    350       C  
ATOM   3873  CD1 LEU A 539      40.568  31.494  12.429  1.00 55.98           C  
ANISOU 3873  CD1 LEU A 539     6687   7787   6795   -117   -243    355       C  
ATOM   3874  CD2 LEU A 539      39.618  30.496  10.327  1.00 55.64           C  
ANISOU 3874  CD2 LEU A 539     6655   7700   6786    -84   -216    379       C  
ATOM   3875  N   ILE A 540      35.642  33.399  12.987  1.00 52.34           N  
ANISOU 3875  N   ILE A 540     6253   7359   6274   -159   -150    281       N  
ATOM   3876  CA  ILE A 540      34.445  34.236  12.916  1.00 49.90           C  
ANISOU 3876  CA  ILE A 540     5943   7052   5965   -166   -122    252       C  
ATOM   3877  C   ILE A 540      34.406  35.147  14.130  1.00 47.83           C  
ANISOU 3877  C   ILE A 540     5674   6819   5680   -191   -120    220       C  
ATOM   3878  O   ILE A 540      34.017  36.312  14.017  1.00 47.27           O  
ANISOU 3878  O   ILE A 540     5591   6744   5626   -193    -99    187       O  
ATOM   3879  CB  ILE A 540      33.164  33.372  12.858  1.00 51.13           C  
ANISOU 3879  CB  ILE A 540     6116   7208   6105   -170   -112    264       C  
ATOM   3880  CG1 ILE A 540      33.229  32.426  11.650  1.00 53.49           C  
ANISOU 3880  CG1 ILE A 540     6418   7479   6428   -145   -116    291       C  
ATOM   3881  CG2 ILE A 540      31.909  34.246  12.826  1.00 53.60           C  
ANISOU 3881  CG2 ILE A 540     6424   7521   6419   -178    -83    232       C  
ATOM   3882  CD1 ILE A 540      33.283  33.128  10.297  1.00 52.17           C  
ANISOU 3882  CD1 ILE A 540     6240   7285   6297   -118   -101    280       C  
ATOM   3883  N   LEU A 541      34.823  34.615  15.281  1.00 46.44           N  
ANISOU 3883  N   LEU A 541     5506   6673   5466   -207   -142    230       N  
ATOM   3884  CA  LEU A 541      34.916  35.408  16.506  1.00 48.12           C  
ANISOU 3884  CA  LEU A 541     5712   6921   5651   -229   -144    198       C  
ATOM   3885  C   LEU A 541      35.849  36.636  16.341  1.00 49.58           C  
ANISOU 3885  C   LEU A 541     5871   7097   5871   -224   -145    165       C  
ATOM   3886  O   LEU A 541      35.470  37.759  16.721  1.00 48.84           O  
ANISOU 3886  O   LEU A 541     5763   7011   5781   -236   -129    124       O  
ATOM   3887  CB  LEU A 541      35.324  34.525  17.700  1.00 46.71           C  
ANISOU 3887  CB  LEU A 541     5547   6778   5423   -242   -172    220       C  
ATOM   3888  CG  LEU A 541      35.560  35.236  19.039  1.00 50.80           C  
ANISOU 3888  CG  LEU A 541     6059   7340   5904   -262   -181    187       C  
ATOM   3889  CD1 LEU A 541      34.311  35.949  19.532  1.00 52.04           C  
ANISOU 3889  CD1 LEU A 541     6216   7514   6042   -282   -151    152       C  
ATOM   3890  CD2 LEU A 541      36.071  34.283  20.111  1.00 50.51           C  
ANISOU 3890  CD2 LEU A 541     6037   7340   5817   -269   -211    216       C  
ATOM   3891  N   TYR A 542      37.036  36.438  15.745  1.00 48.18           N  
ANISOU 3891  N   TYR A 542     5685   6899   5723   -206   -162    182       N  
ATOM   3892  CA  TYR A 542      37.983  37.562  15.538  1.00 48.52           C  
ANISOU 3892  CA  TYR A 542     5700   6928   5807   -201   -161    153       C  
ATOM   3893  C   TYR A 542      37.301  38.644  14.738  1.00 47.44           C  
ANISOU 3893  C   TYR A 542     5551   6765   5707   -195   -125    129       C  
ATOM   3894  O   TYR A 542      37.442  39.834  15.038  1.00 44.22           O  
ANISOU 3894  O   TYR A 542     5122   6358   5322   -203   -114     90       O  
ATOM   3895  CB  TYR A 542      39.250  37.145  14.784  1.00 48.74           C  
ANISOU 3895  CB  TYR A 542     5719   6931   5869   -180   -177    178       C  
ATOM   3896  CG  TYR A 542      40.014  36.024  15.412  1.00 48.22           C  
ANISOU 3896  CG  TYR A 542     5663   6884   5774   -182   -214    205       C  
ATOM   3897  CD1 TYR A 542      40.192  35.965  16.795  1.00 49.19           C  
ANISOU 3897  CD1 TYR A 542     5787   7048   5853   -201   -238    193       C  
ATOM   3898  CD2 TYR A 542      40.582  35.023  14.621  1.00 50.00           C  
ANISOU 3898  CD2 TYR A 542     5894   7086   6016   -163   -226    244       C  
ATOM   3899  CE1 TYR A 542      40.893  34.927  17.379  1.00 50.35           C  
ANISOU 3899  CE1 TYR A 542     5944   7214   5973   -200   -273    223       C  
ATOM   3900  CE2 TYR A 542      41.289  33.976  15.196  1.00 50.80           C  
ANISOU 3900  CE2 TYR A 542     6004   7203   6097   -163   -261    272       C  
ATOM   3901  CZ  TYR A 542      41.439  33.946  16.574  1.00 51.66           C  
ANISOU 3901  CZ  TYR A 542     6115   7353   6161   -181   -284    262       C  
ATOM   3902  OH  TYR A 542      42.113  32.917  17.155  1.00 58.91           O  
ANISOU 3902  OH  TYR A 542     7041   8286   7057   -180   -319    293       O  
ATOM   3903  N   ASP A 543      36.555  38.210  13.721  1.00 47.31           N  
ANISOU 3903  N   ASP A 543     5548   6726   5701   -179   -109    153       N  
ATOM   3904  CA  ASP A 543      35.779  39.126  12.894  1.00 46.63           C  
ANISOU 3904  CA  ASP A 543     5454   6616   5646   -170    -76    136       C  
ATOM   3905  C   ASP A 543      34.740  39.894  13.710  1.00 45.54           C  
ANISOU 3905  C   ASP A 543     5312   6498   5492   -192    -60     99       C  
ATOM   3906  O   ASP A 543      34.602  41.095  13.554  1.00 46.36           O  
ANISOU 3906  O   ASP A 543     5397   6589   5629   -193    -39     69       O  
ATOM   3907  CB  ASP A 543      35.176  38.401  11.701  1.00 45.64           C  
ANISOU 3907  CB  ASP A 543     5344   6469   5528   -148    -67    167       C  
ATOM   3908  CG  ASP A 543      36.220  38.064  10.640  1.00 50.19           C  
ANISOU 3908  CG  ASP A 543     5917   7019   6135   -121    -73    194       C  
ATOM   3909  OD1 ASP A 543      37.353  38.604  10.705  1.00 51.28           O  
ANISOU 3909  OD1 ASP A 543     6037   7149   6298   -119    -78    187       O  
ATOM   3910  OD2 ASP A 543      35.918  37.256   9.732  1.00 50.75           O  
ANISOU 3910  OD2 ASP A 543     6000   7076   6205   -102    -73    220       O  
ATOM   3911  N   ALA A 544      34.062  39.215  14.623  1.00 46.82           N  
ANISOU 3911  N   ALA A 544     5492   6691   5607   -211    -68    100       N  
ATOM   3912  CA  ALA A 544      33.108  39.885  15.512  1.00 47.73           C  
ANISOU 3912  CA  ALA A 544     5604   6830   5703   -235    -52     63       C  
ATOM   3913  C   ALA A 544      33.795  40.905  16.430  1.00 46.59           C  
ANISOU 3913  C   ALA A 544     5437   6704   5562   -251    -58     21       C  
ATOM   3914  O   ALA A 544      33.290  42.024  16.611  1.00 47.58           O  
ANISOU 3914  O   ALA A 544     5544   6827   5706   -260    -36    -19       O  
ATOM   3915  CB  ALA A 544      32.313  38.866  16.322  1.00 44.54           C  
ANISOU 3915  CB  ALA A 544     5223   6455   5244   -252    -58     77       C  
ATOM   3916  N   ILE A 545      34.943  40.527  16.999  1.00 49.54           N  
ANISOU 3916  N   ILE A 545     5809   7095   5919   -253    -87     29       N  
ATOM   3917  CA  ILE A 545      35.768  41.480  17.792  1.00 50.46           C  
ANISOU 3917  CA  ILE A 545     5899   7228   6045   -264    -97    -14       C  
ATOM   3918  C   ILE A 545      36.228  42.652  16.920  1.00 47.25           C  
ANISOU 3918  C   ILE A 545     5464   6781   5709   -251    -77    -35       C  
ATOM   3919  O   ILE A 545      36.134  43.826  17.309  1.00 46.08           O  
ANISOU 3919  O   ILE A 545     5291   6633   5585   -262    -63    -82       O  
ATOM   3920  CB  ILE A 545      37.039  40.833  18.379  1.00 50.64           C  
ANISOU 3920  CB  ILE A 545     5923   7273   6047   -263   -135      0       C  
ATOM   3921  CG1 ILE A 545      36.762  39.433  18.950  1.00 51.97           C  
ANISOU 3921  CG1 ILE A 545     6123   7471   6154   -268   -155     40       C  
ATOM   3922  CG2 ILE A 545      37.690  41.772  19.387  1.00 50.16           C  
ANISOU 3922  CG2 ILE A 545     5835   7238   5986   -278   -147    -52       C  
ATOM   3923  CD1 ILE A 545      36.268  39.395  20.369  1.00 53.18           C  
ANISOU 3923  CD1 ILE A 545     6284   7676   6245   -292   -162     19       C  
ATOM   3924  N   GLY A 546      36.722  42.325  15.735  1.00 45.57           N  
ANISOU 3924  N   GLY A 546     5253   6532   5531   -227    -75      1       N  
ATOM   3925  CA  GLY A 546      37.183  43.359  14.800  1.00 46.72           C  
ANISOU 3925  CA  GLY A 546     5373   6635   5743   -211    -53     -9       C  
ATOM   3926  C   GLY A 546      36.102  44.381  14.550  1.00 46.56           C  
ANISOU 3926  C   GLY A 546     5343   6600   5747   -214    -19    -35       C  
ATOM   3927  O   GLY A 546      36.316  45.592  14.721  1.00 46.80           O  
ANISOU 3927  O   GLY A 546     5345   6619   5820   -220     -4    -74       O  
ATOM   3928  N   THR A 547      34.910  43.902  14.178  1.00 48.97           N  
ANISOU 3928  N   THR A 547     5671   6906   6030   -211     -8    -18       N  
ATOM   3929  CA  THR A 547      33.800  44.833  13.902  1.00 46.29           C  
ANISOU 3929  CA  THR A 547     5322   6552   5714   -212     24    -42       C  
ATOM   3930  C   THR A 547      33.343  45.556  15.173  1.00 43.72           C  
ANISOU 3930  C   THR A 547     4983   6255   5375   -241     28    -94       C  
ATOM   3931  O   THR A 547      33.066  46.756  15.139  1.00 41.55           O  
ANISOU 3931  O   THR A 547     4683   5963   5142   -245     50   -129       O  
ATOM   3932  CB  THR A 547      32.689  44.255  12.957  1.00 50.94           C  
ANISOU 3932  CB  THR A 547     5933   7126   6294   -195     36    -11       C  
ATOM   3933  OG1 THR A 547      31.386  44.658  13.392  1.00 54.79           O  
ANISOU 3933  OG1 THR A 547     6421   7625   6772   -210     54    -40       O  
ATOM   3934  CG2 THR A 547      32.741  42.766  12.834  1.00 46.45           C  
ANISOU 3934  CG2 THR A 547     5393   6572   5685   -189     14     29       C  
ATOM   3935  N   LEU A 548      33.383  44.868  16.312  1.00 44.10           N  
ANISOU 3935  N   LEU A 548     5043   6346   5365   -262      5   -101       N  
ATOM   3936  CA  LEU A 548      33.125  45.555  17.577  1.00 46.98           C  
ANISOU 3936  CA  LEU A 548     5393   6745   5712   -289      7   -154       C  
ATOM   3937  C   LEU A 548      34.045  46.772  17.770  1.00 51.80           C  
ANISOU 3937  C   LEU A 548     5965   7342   6373   -291      9   -197       C  
ATOM   3938  O   LEU A 548      33.575  47.894  18.059  1.00 51.53           O  
ANISOU 3938  O   LEU A 548     5906   7303   6369   -302     30   -244       O  
ATOM   3939  CB  LEU A 548      33.242  44.603  18.761  1.00 46.60           C  
ANISOU 3939  CB  LEU A 548     5365   6748   5592   -306    -20   -150       C  
ATOM   3940  CG  LEU A 548      33.065  45.227  20.159  1.00 49.04           C  
ANISOU 3940  CG  LEU A 548     5661   7102   5871   -333    -22   -206       C  
ATOM   3941  CD1 LEU A 548      31.776  46.029  20.304  1.00 50.63           C  
ANISOU 3941  CD1 LEU A 548     5854   7301   6084   -347     11   -244       C  
ATOM   3942  CD2 LEU A 548      33.117  44.178  21.253  1.00 48.59           C  
ANISOU 3942  CD2 LEU A 548     5629   7097   5735   -347    -47   -191       C  
ATOM   3943  N   ALA A 549      35.352  46.549  17.606  1.00 52.12           N  
ANISOU 3943  N   ALA A 549     5999   7376   6429   -281    -13   -182       N  
ATOM   3944  CA  ALA A 549      36.334  47.625  17.745  1.00 50.91           C  
ANISOU 3944  CA  ALA A 549     5807   7207   6331   -282    -12   -220       C  
ATOM   3945  C   ALA A 549      36.035  48.769  16.790  1.00 49.66           C  
ANISOU 3945  C   ALA A 549     5625   6998   6247   -270     25   -230       C  
ATOM   3946  O   ALA A 549      36.103  49.920  17.186  1.00 50.95           O  
ANISOU 3946  O   ALA A 549     5754   7153   6452   -281     39   -280       O  
ATOM   3947  CB  ALA A 549      37.750  47.100  17.535  1.00 52.65           C  
ANISOU 3947  CB  ALA A 549     6024   7421   6560   -269    -39   -196       C  
ATOM   3948  N   ASP A 550      35.686  48.456  15.545  1.00 48.78           N  
ANISOU 3948  N   ASP A 550     5530   6852   6152   -247     42   -182       N  
ATOM   3949  CA  ASP A 550      35.271  49.490  14.600  1.00 51.67           C  
ANISOU 3949  CA  ASP A 550     5877   7172   6583   -232     78   -184       C  
ATOM   3950  C   ASP A 550      33.993  50.228  15.039  1.00 59.17           C  
ANISOU 3950  C   ASP A 550     6819   8128   7534   -248     99   -223       C  
ATOM   3951  O   ASP A 550      33.901  51.451  14.882  1.00 60.12           O  
ANISOU 3951  O   ASP A 550     6908   8220   7716   -248    124   -253       O  
ATOM   3952  CB  ASP A 550      35.051  48.893  13.215  1.00 53.15           C  
ANISOU 3952  CB  ASP A 550     6089   7332   6775   -202     88   -125       C  
ATOM   3953  CG  ASP A 550      36.341  48.489  12.537  1.00 57.36           C  
ANISOU 3953  CG  ASP A 550     6621   7845   7328   -183     77    -90       C  
ATOM   3954  OD1 ASP A 550      37.431  48.690  13.126  1.00 61.06           O  
ANISOU 3954  OD1 ASP A 550     7069   8319   7811   -192     62   -111       O  
ATOM   3955  OD2 ASP A 550      36.268  47.989  11.392  1.00 57.80           O  
ANISOU 3955  OD2 ASP A 550     6695   7881   7386   -157     85    -44       O  
ATOM   3956  N   SER A 551      33.012  49.493  15.581  1.00 58.10           N  
ANISOU 3956  N   SER A 551     6710   8028   7338   -261     91   -222       N  
ATOM   3957  CA  SER A 551      31.753  50.105  16.006  1.00 58.93           C  
ANISOU 3957  CA  SER A 551     6808   8139   7442   -276    112   -259       C  
ATOM   3958  C   SER A 551      31.900  51.049  17.202  1.00 62.10           C  
ANISOU 3958  C   SER A 551     7178   8562   7855   -303    114   -327       C  
ATOM   3959  O   SER A 551      31.352  52.156  17.182  1.00 62.30           O  
ANISOU 3959  O   SER A 551     7177   8567   7928   -308    139   -363       O  
ATOM   3960  CB  SER A 551      30.695  49.043  16.297  1.00 56.65           C  
ANISOU 3960  CB  SER A 551     6554   7882   7088   -284    105   -241       C  
ATOM   3961  OG  SER A 551      30.222  48.506  15.084  1.00 57.90           O  
ANISOU 3961  OG  SER A 551     6733   8013   7253   -259    113   -193       O  
ATOM   3962  N   VAL A 552      32.631  50.626  18.232  1.00 60.82           N  
ANISOU 3962  N   VAL A 552     7018   8442   7650   -319     86   -344       N  
ATOM   3963  CA  VAL A 552      32.703  51.420  19.461  1.00 62.56           C  
ANISOU 3963  CA  VAL A 552     7209   8692   7869   -344     84   -413       C  
ATOM   3964  C   VAL A 552      33.919  52.336  19.559  1.00 67.52           C  
ANISOU 3964  C   VAL A 552     7797   9301   8557   -343     79   -448       C  
ATOM   3965  O   VAL A 552      34.053  53.071  20.546  1.00 69.79           O  
ANISOU 3965  O   VAL A 552     8055   9612   8851   -363     77   -512       O  
ATOM   3966  CB  VAL A 552      32.688  50.545  20.728  1.00 62.85           C  
ANISOU 3966  CB  VAL A 552     7269   8795   7818   -364     56   -424       C  
ATOM   3967  CG1 VAL A 552      31.411  49.715  20.804  1.00 61.57           C  
ANISOU 3967  CG1 VAL A 552     7142   8652   7600   -370     64   -398       C  
ATOM   3968  CG2 VAL A 552      33.926  49.665  20.785  1.00 63.02           C  
ANISOU 3968  CG2 VAL A 552     7303   8830   7812   -355     20   -390       C  
ATOM   3969  N   GLY A 553      34.806  52.279  18.563  1.00 66.82           N  
ANISOU 3969  N   GLY A 553     7704   9172   8513   -320     79   -409       N  
ATOM   3970  CA  GLY A 553      36.041  53.068  18.568  1.00 63.25           C  
ANISOU 3970  CA  GLY A 553     7212   8696   8123   -317     76   -436       C  
ATOM   3971  C   GLY A 553      36.719  53.158  19.929  1.00 64.90           C  
ANISOU 3971  C   GLY A 553     7402   8952   8304   -339     46   -493       C  
ATOM   3972  O   GLY A 553      36.910  52.145  20.616  1.00 62.11           O  
ANISOU 3972  O   GLY A 553     7076   8648   7875   -345     13   -480       O  
ATOM   3973  N   HIS A 554      37.053  54.385  20.331  1.00 66.63           N  
ANISOU 3973  N   HIS A 554     7574   9158   8585   -349     57   -556       N  
ATOM   3974  CA  HIS A 554      37.890  54.629  21.513  1.00 69.62           C  
ANISOU 3974  CA  HIS A 554     7925   9576   8952   -365     28   -617       C  
ATOM   3975  C   HIS A 554      37.283  54.191  22.812  1.00 69.61           C  
ANISOU 3975  C   HIS A 554     7942   9645   8861   -387      7   -650       C  
ATOM   3976  O   HIS A 554      38.011  53.997  23.789  1.00 71.06           O  
ANISOU 3976  O   HIS A 554     8117   9875   9008   -395    -27   -684       O  
ATOM   3977  CB  HIS A 554      38.342  56.095  21.587  1.00 79.06           C  
ANISOU 3977  CB  HIS A 554     9061  10735  10244   -371     48   -681       C  
ATOM   3978  CG  HIS A 554      38.889  56.639  20.276  1.00 88.54           C  
ANISOU 3978  CG  HIS A 554    10242  11861  11540   -349     76   -646       C  
ATOM   3979  ND1 HIS A 554      39.872  56.020  19.581  1.00 90.65           N  
ANISOU 3979  ND1 HIS A 554    10520  12108  11816   -330     64   -595       N  
ATOM   3980  CD2 HIS A 554      38.548  57.780  19.542  1.00 91.32           C  
ANISOU 3980  CD2 HIS A 554    10563  12153  11983   -343    120   -654       C  
ATOM   3981  CE1 HIS A 554      40.139  56.722  18.459  1.00 91.24           C  
ANISOU 3981  CE1 HIS A 554    10573  12116  11979   -313     99   -571       C  
ATOM   3982  NE2 HIS A 554      39.329  57.799  18.437  1.00 93.13           N  
ANISOU 3982  NE2 HIS A 554    10787  12331  12269   -320    133   -606       N  
ATOM   3983  N   HIS A 555      35.962  53.999  22.838  1.00 66.63           N  
ANISOU 3983  N   HIS A 555     7590   9281   8447   -394     27   -640       N  
ATOM   3984  CA  HIS A 555      35.273  53.509  24.036  1.00 65.65           C  
ANISOU 3984  CA  HIS A 555     7487   9224   8233   -414     13   -664       C  
ATOM   3985  C   HIS A 555      35.832  52.198  24.474  1.00 62.84           C  
ANISOU 3985  C   HIS A 555     7168   8914   7796   -411    -26   -623       C  
ATOM   3986  O   HIS A 555      35.682  51.815  25.628  1.00 66.68           O  
ANISOU 3986  O   HIS A 555     7665   9463   8207   -426    -47   -647       O  
ATOM   3987  CB  HIS A 555      33.766  53.361  23.816  1.00 68.93           C  
ANISOU 3987  CB  HIS A 555     7928   9638   8626   -420     43   -648       C  
ATOM   3988  CG  HIS A 555      33.052  54.656  23.517  1.00 68.92           C  
ANISOU 3988  CG  HIS A 555     7891   9597   8699   -426     81   -692       C  
ATOM   3989  ND1 HIS A 555      32.555  54.945  22.292  1.00 70.21           N  
ANISOU 3989  ND1 HIS A 555     8055   9701   8921   -409    111   -655       N  
ATOM   3990  CD2 HIS A 555      32.752  55.745  24.329  1.00 69.44           C  
ANISOU 3990  CD2 HIS A 555     7918   9675   8791   -446     94   -773       C  
ATOM   3991  CE1 HIS A 555      31.973  56.162  22.317  1.00 67.98           C  
ANISOU 3991  CE1 HIS A 555     7736   9392   8701   -418    141   -706       C  
ATOM   3992  NE2 HIS A 555      32.092  56.651  23.563  1.00 70.75           N  
ANISOU 3992  NE2 HIS A 555     8062   9786   9035   -441    131   -780       N  
ATOM   3993  N   LEU A 556      36.482  51.496  23.553  1.00 63.52           N  
ANISOU 3993  N   LEU A 556     7271   8969   7895   -390    -37   -560       N  
ATOM   3994  CA  LEU A 556      37.128  50.214  23.854  1.00 64.36           C  
ANISOU 3994  CA  LEU A 556     7410   9111   7935   -383    -75   -515       C  
ATOM   3995  C   LEU A 556      38.381  50.355  24.732  1.00 66.09           C  
ANISOU 3995  C   LEU A 556     7604   9363   8146   -386   -114   -555       C  
ATOM   3996  O   LEU A 556      38.851  49.377  25.327  1.00 64.20           O  
ANISOU 3996  O   LEU A 556     7388   9167   7839   -385   -150   -531       O  
ATOM   3997  CB  LEU A 556      37.456  49.456  22.553  1.00 62.99           C  
ANISOU 3997  CB  LEU A 556     7258   8890   7785   -359    -73   -439       C  
ATOM   3998  CG  LEU A 556      37.943  47.992  22.630  1.00 62.60           C  
ANISOU 3998  CG  LEU A 556     7245   8866   7673   -350   -108   -381       C  
ATOM   3999  CD1 LEU A 556      37.008  47.090  23.438  1.00 62.77           C  
ANISOU 3999  CD1 LEU A 556     7306   8941   7605   -363   -114   -364       C  
ATOM   4000  CD2 LEU A 556      38.195  47.401  21.244  1.00 59.71           C  
ANISOU 4000  CD2 LEU A 556     6895   8450   7341   -326   -100   -315       C  
ATOM   4001  N   ASN A 557      38.903  51.576  24.827  1.00 67.97           N  
ANISOU 4001  N   ASN A 557     7793   9580   8454   -390   -106   -617       N  
ATOM   4002  CA  ASN A 557      40.161  51.812  25.514  1.00 69.71           C  
ANISOU 4002  CA  ASN A 557     7982   9823   8683   -391   -142   -661       C  
ATOM   4003  C   ASN A 557      39.996  51.896  27.030  1.00 73.14           C  
ANISOU 4003  C   ASN A 557     8412  10332   9045   -409   -167   -721       C  
ATOM   4004  O   ASN A 557      39.995  52.984  27.608  1.00 75.29           O  
ANISOU 4004  O   ASN A 557     8643  10613   9351   -422   -160   -799       O  
ATOM   4005  CB  ASN A 557      40.830  53.075  24.959  1.00 71.83           C  
ANISOU 4005  CB  ASN A 557     8196  10033   9064   -387   -123   -703       C  
ATOM   4006  CG  ASN A 557      42.278  53.212  25.383  1.00 71.11           C  
ANISOU 4006  CG  ASN A 557     8071   9951   8997   -382   -160   -737       C  
ATOM   4007  OD1 ASN A 557      42.916  52.252  25.835  1.00 72.44           O  
ANISOU 4007  OD1 ASN A 557     8261  10159   9105   -376   -201   -713       O  
ATOM   4008  ND2 ASN A 557      42.811  54.416  25.233  1.00 72.14           N  
ANISOU 4008  ND2 ASN A 557     8147  10042   9221   -384   -144   -793       N  
ATOM   4009  N   LYS A 558      39.846  50.740  27.669  1.00 72.64           N  
ANISOU 4009  N   LYS A 558     8390  10325   8883   -410   -195   -684       N  
ATOM   4010  CA  LYS A 558      39.770  50.678  29.121  1.00 73.35           C  
ANISOU 4010  CA  LYS A 558     8481  10494   8892   -424   -221   -732       C  
ATOM   4011  C   LYS A 558      40.623  49.534  29.612  1.00 72.00           C  
ANISOU 4011  C   LYS A 558     8336  10367   8653   -413   -271   -693       C  
ATOM   4012  O   LYS A 558      40.582  48.450  29.039  1.00 76.96           O  
ANISOU 4012  O   LYS A 558     9003  10981   9258   -401   -275   -614       O  
ATOM   4013  CB  LYS A 558      38.327  50.509  29.605  1.00 76.42           C  
ANISOU 4013  CB  LYS A 558     8900  10918   9218   -441   -194   -732       C  
ATOM   4014  CG  LYS A 558      37.370  51.552  29.050  1.00 81.34           C  
ANISOU 4014  CG  LYS A 558     9502  11496   9910   -450   -144   -764       C  
ATOM   4015  CD  LYS A 558      36.518  52.208  30.127  1.00 87.44           C  
ANISOU 4015  CD  LYS A 558    10261  12316  10645   -473   -130   -835       C  
ATOM   4016  CE  LYS A 558      35.737  53.382  29.548  1.00 89.37           C  
ANISOU 4016  CE  LYS A 558    10474  12508  10974   -481    -83   -873       C  
ATOM   4017  NZ  LYS A 558      36.594  54.312  28.753  1.00 88.74           N  
ANISOU 4017  NZ  LYS A 558    10349  12364  11006   -471    -78   -895       N  
ATOM   4018  N   PRO A 559      41.404  49.770  30.675  1.00 71.85           N  
ANISOU 4018  N   PRO A 559     8294  10401   8604   -415   -310   -748       N  
ATOM   4019  CA  PRO A 559      42.355  48.773  31.186  1.00 73.10           C  
ANISOU 4019  CA  PRO A 559     8471  10601   8704   -401   -362   -716       C  
ATOM   4020  C   PRO A 559      41.754  47.375  31.371  1.00 72.45           C  
ANISOU 4020  C   PRO A 559     8449  10552   8528   -398   -369   -635       C  
ATOM   4021  O   PRO A 559      42.383  46.377  31.013  1.00 71.92           O  
ANISOU 4021  O   PRO A 559     8403  10474   8448   -382   -394   -572       O  
ATOM   4022  CB  PRO A 559      42.789  49.367  32.529  1.00 69.60           C  
ANISOU 4022  CB  PRO A 559     7998  10227   8222   -409   -395   -801       C  
ATOM   4023  CG  PRO A 559      42.676  50.837  32.318  1.00 69.60           C  
ANISOU 4023  CG  PRO A 559     7944  10190   8311   -421   -365   -881       C  
ATOM   4024  CD  PRO A 559      41.479  51.036  31.428  1.00 70.70           C  
ANISOU 4024  CD  PRO A 559     8100  10277   8486   -429   -308   -849       C  
ATOM   4025  N   GLU A 560      40.542  47.306  31.909  1.00 76.18           N  
ANISOU 4025  N   GLU A 560     8945  11060   8939   -414   -343   -638       N  
ATOM   4026  CA  GLU A 560      39.877  46.020  32.098  1.00 75.72           C  
ANISOU 4026  CA  GLU A 560     8941  11029   8798   -413   -343   -563       C  
ATOM   4027  C   GLU A 560      39.626  45.332  30.744  1.00 70.63           C  
ANISOU 4027  C   GLU A 560     8321  10316   8200   -402   -320   -485       C  
ATOM   4028  O   GLU A 560      39.955  44.157  30.574  1.00 66.90           O  
ANISOU 4028  O   GLU A 560     7880   9846   7695   -389   -342   -416       O  
ATOM   4029  CB  GLU A 560      38.594  46.169  32.938  1.00 78.86           C  
ANISOU 4029  CB  GLU A 560     9357  11477   9129   -433   -314   -587       C  
ATOM   4030  CG  GLU A 560      37.504  47.078  32.360  1.00 88.34           C  
ANISOU 4030  CG  GLU A 560    10543  12635  10389   -448   -260   -620       C  
ATOM   4031  CD  GLU A 560      37.593  48.549  32.781  1.00 95.58           C  
ANISOU 4031  CD  GLU A 560    11408  13558  11351   -460   -252   -720       C  
ATOM   4032  OE1 GLU A 560      38.711  49.070  33.037  1.00 97.06           O  
ANISOU 4032  OE1 GLU A 560    11560  13752  11568   -453   -284   -766       O  
ATOM   4033  OE2 GLU A 560      36.519  49.198  32.837  1.00 92.91           O  
ANISOU 4033  OE2 GLU A 560    11064  13215  11025   -477   -212   -755       O  
ATOM   4034  N   TYR A 561      39.092  46.085  29.780  1.00 68.30           N  
ANISOU 4034  N   TYR A 561     8008   9961   7982   -406   -279   -498       N  
ATOM   4035  CA  TYR A 561      38.780  45.544  28.449  1.00 66.10           C  
ANISOU 4035  CA  TYR A 561     7750   9618   7748   -394   -256   -432       C  
ATOM   4036  C   TYR A 561      40.033  45.048  27.756  1.00 65.08           C  
ANISOU 4036  C   TYR A 561     7615   9455   7657   -373   -285   -393       C  
ATOM   4037  O   TYR A 561      40.051  43.937  27.231  1.00 63.37           O  
ANISOU 4037  O   TYR A 561     7430   9224   7425   -362   -291   -323       O  
ATOM   4038  CB  TYR A 561      38.075  46.577  27.564  1.00 65.87           C  
ANISOU 4038  CB  TYR A 561     7698   9533   7797   -399   -209   -459       C  
ATOM   4039  CG  TYR A 561      36.758  47.107  28.107  1.00 67.97           C  
ANISOU 4039  CG  TYR A 561     7966   9822   8037   -420   -176   -497       C  
ATOM   4040  CD1 TYR A 561      36.019  46.397  29.066  1.00 68.04           C  
ANISOU 4040  CD1 TYR A 561     8008   9890   7953   -432   -178   -484       C  
ATOM   4041  CD2 TYR A 561      36.232  48.309  27.635  1.00 69.18           C  
ANISOU 4041  CD2 TYR A 561     8089   9936   8261   -426   -140   -543       C  
ATOM   4042  CE1 TYR A 561      34.821  46.891  29.556  1.00 68.06           C  
ANISOU 4042  CE1 TYR A 561     8011   9914   7935   -451   -145   -521       C  
ATOM   4043  CE2 TYR A 561      35.029  48.809  28.116  1.00 69.94           C  
ANISOU 4043  CE2 TYR A 561     8184  10052   8338   -445   -109   -581       C  
ATOM   4044  CZ  TYR A 561      34.329  48.098  29.074  1.00 69.70           C  
ANISOU 4044  CZ  TYR A 561     8186  10081   8216   -458   -111   -571       C  
ATOM   4045  OH  TYR A 561      33.131  48.599  29.539  1.00 71.14           O  
ANISOU 4045  OH  TYR A 561     8366  10282   8383   -477    -78   -610       O  
ATOM   4046  N   ILE A 562      41.079  45.878  27.779  1.00 63.89           N  
ANISOU 4046  N   ILE A 562     7422   9292   7561   -369   -302   -443       N  
ATOM   4047  CA  ILE A 562      42.379  45.531  27.217  1.00 62.97           C  
ANISOU 4047  CA  ILE A 562     7294   9146   7486   -350   -330   -417       C  
ATOM   4048  C   ILE A 562      42.924  44.246  27.847  1.00 63.98           C  
ANISOU 4048  C   ILE A 562     7452   9319   7540   -341   -376   -371       C  
ATOM   4049  O   ILE A 562      43.406  43.359  27.140  1.00 63.13           O  
ANISOU 4049  O   ILE A 562     7360   9182   7445   -326   -387   -311       O  
ATOM   4050  CB  ILE A 562      43.395  46.692  27.367  1.00 64.51           C  
ANISOU 4050  CB  ILE A 562     7434   9328   7749   -350   -342   -489       C  
ATOM   4051  CG1 ILE A 562      42.910  47.930  26.590  1.00 67.42           C  
ANISOU 4051  CG1 ILE A 562     7772   9641   8204   -356   -293   -525       C  
ATOM   4052  CG2 ILE A 562      44.765  46.271  26.868  1.00 58.44           C  
ANISOU 4052  CG2 ILE A 562     6652   8531   7020   -331   -372   -463       C  
ATOM   4053  CD1 ILE A 562      43.641  49.226  26.898  1.00 66.20           C  
ANISOU 4053  CD1 ILE A 562     7560   9477   8117   -361   -296   -607       C  
ATOM   4054  N   GLN A 563      42.809  44.130  29.166  1.00 65.38           N  
ANISOU 4054  N   GLN A 563     7636   9568   7638   -351   -400   -398       N  
ATOM   4055  CA  GLN A 563      43.363  42.981  29.870  1.00 69.70           C  
ANISOU 4055  CA  GLN A 563     8209  10162   8112   -341   -446   -355       C  
ATOM   4056  C   GLN A 563      42.638  41.669  29.570  1.00 70.49           C  
ANISOU 4056  C   GLN A 563     8360  10258   8165   -337   -435   -270       C  
ATOM   4057  O   GLN A 563      43.271  40.626  29.451  1.00 74.10           O  
ANISOU 4057  O   GLN A 563     8835  10714   8606   -322   -465   -214       O  
ATOM   4058  CB  GLN A 563      43.438  43.242  31.382  1.00 76.16           C  
ANISOU 4058  CB  GLN A 563     9022  11063   8853   -349   -476   -407       C  
ATOM   4059  CG  GLN A 563      44.249  42.209  32.161  1.00 83.64           C  
ANISOU 4059  CG  GLN A 563     9988  12061   9731   -335   -531   -371       C  
ATOM   4060  CD  GLN A 563      45.631  41.946  31.563  1.00 89.73           C  
ANISOU 4060  CD  GLN A 563    10738  12794  10561   -315   -566   -355       C  
ATOM   4061  OE1 GLN A 563      46.408  42.876  31.326  1.00 91.90           O  
ANISOU 4061  OE1 GLN A 563    10968  13044  10906   -313   -573   -412       O  
ATOM   4062  NE2 GLN A 563      45.944  40.670  31.325  1.00 89.07           N  
ANISOU 4062  NE2 GLN A 563    10685  12704  10453   -301   -587   -277       N  
ATOM   4063  N   MET A 564      41.317  41.709  29.453  1.00 69.47           N  
ANISOU 4063  N   MET A 564     8250  10126   8018   -351   -393   -262       N  
ATOM   4064  CA  MET A 564      40.575  40.495  29.115  1.00 68.18           C  
ANISOU 4064  CA  MET A 564     8132   9954   7821   -348   -379   -185       C  
ATOM   4065  C   MET A 564      40.695  40.140  27.622  1.00 64.65           C  
ANISOU 4065  C   MET A 564     7686   9432   7446   -335   -362   -139       C  
ATOM   4066  O   MET A 564      40.687  38.961  27.249  1.00 61.86           O  
ANISOU 4066  O   MET A 564     7360   9065   7078   -324   -370    -72       O  
ATOM   4067  CB  MET A 564      39.111  40.589  29.580  1.00 69.94           C  
ANISOU 4067  CB  MET A 564     8375  10202   7996   -368   -341   -192       C  
ATOM   4068  CG  MET A 564      38.301  41.743  28.995  1.00 73.26           C  
ANISOU 4068  CG  MET A 564     8774  10587   8474   -380   -296   -241       C  
ATOM   4069  SD  MET A 564      36.790  42.153  29.913  1.00 77.71           S  
ANISOU 4069  SD  MET A 564     9349  11197   8980   -405   -259   -277       S  
ATOM   4070  CE  MET A 564      35.771  40.711  29.584  1.00 73.90           C  
ANISOU 4070  CE  MET A 564     8917  10705   8459   -405   -238   -190       C  
ATOM   4071  N   LEU A 565      40.849  41.159  26.782  1.00 62.05           N  
ANISOU 4071  N   LEU A 565     7326   9055   7197   -333   -341   -176       N  
ATOM   4072  CA  LEU A 565      40.852  40.969  25.331  1.00 64.52           C  
ANISOU 4072  CA  LEU A 565     7639   9299   7576   -319   -319   -139       C  
ATOM   4073  C   LEU A 565      42.208  40.563  24.731  1.00 65.03           C  
ANISOU 4073  C   LEU A 565     7692   9334   7683   -299   -348   -113       C  
ATOM   4074  O   LEU A 565      42.295  39.633  23.921  1.00 60.63           O  
ANISOU 4074  O   LEU A 565     7153   8746   7138   -286   -348    -56       O  
ATOM   4075  CB  LEU A 565      40.359  42.245  24.666  1.00 65.01           C  
ANISOU 4075  CB  LEU A 565     7675   9323   7704   -325   -279   -184       C  
ATOM   4076  CG  LEU A 565      40.004  42.216  23.190  1.00 64.93           C  
ANISOU 4076  CG  LEU A 565     7669   9249   7754   -312   -246   -150       C  
ATOM   4077  CD1 LEU A 565      39.068  41.058  22.861  1.00 64.20           C  
ANISOU 4077  CD1 LEU A 565     7617   9154   7623   -310   -235    -91       C  
ATOM   4078  CD2 LEU A 565      39.375  43.554  22.845  1.00 65.05           C  
ANISOU 4078  CD2 LEU A 565     7659   9238   7820   -320   -208   -199       C  
ATOM   4079  N   MET A 566      43.263  41.267  25.134  1.00 66.20           N  
ANISOU 4079  N   MET A 566     7806   9492   7857   -298   -373   -160       N  
ATOM   4080  CA  MET A 566      44.578  41.104  24.509  1.00 63.23           C  
ANISOU 4080  CA  MET A 566     7409   9080   7534   -280   -396   -147       C  
ATOM   4081  C   MET A 566      45.242  39.738  24.680  1.00 62.44           C  
ANISOU 4081  C   MET A 566     7332   8995   7398   -266   -436    -90       C  
ATOM   4082  O   MET A 566      45.649  39.143  23.686  1.00 63.59           O  
ANISOU 4082  O   MET A 566     7482   9097   7583   -251   -433    -47       O  
ATOM   4083  CB  MET A 566      45.513  42.240  24.908  1.00 64.43           C  
ANISOU 4083  CB  MET A 566     7514   9235   7730   -282   -411   -217       C  
ATOM   4084  CG  MET A 566      45.183  43.550  24.214  1.00 64.93           C  
ANISOU 4084  CG  MET A 566     7548   9255   7868   -288   -367   -260       C  
ATOM   4085  SD  MET A 566      45.341  43.385  22.429  1.00 68.86           S  
ANISOU 4085  SD  MET A 566     8047   9672   8445   -269   -333   -209       S  
ATOM   4086  CE  MET A 566      43.788  42.612  22.044  1.00 73.07           C  
ANISOU 4086  CE  MET A 566     8629  10207   8927   -272   -304   -157       C  
ATOM   4087  N   PRO A 567      45.338  39.226  25.922  1.00 63.45           N  
ANISOU 4087  N   PRO A 567     7474   9184   7450   -271   -471    -89       N  
ATOM   4088  CA  PRO A 567      46.038  37.945  26.114  1.00 64.15           C  
ANISOU 4088  CA  PRO A 567     7581   9285   7508   -257   -512    -33       C  
ATOM   4089  C   PRO A 567      45.602  36.799  25.193  1.00 67.31           C  
ANISOU 4089  C   PRO A 567     8013   9648   7916   -247   -496     41       C  
ATOM   4090  O   PRO A 567      46.468  36.149  24.599  1.00 73.64           O  
ANISOU 4090  O   PRO A 567     8810  10419   8751   -231   -515     74       O  
ATOM   4091  CB  PRO A 567      45.776  37.623  27.583  1.00 63.85           C  
ANISOU 4091  CB  PRO A 567     7561   9322   7376   -265   -540    -37       C  
ATOM   4092  CG  PRO A 567      45.697  38.977  28.210  1.00 62.22           C  
ANISOU 4092  CG  PRO A 567     7325   9143   7173   -278   -533   -119       C  
ATOM   4093  CD  PRO A 567      44.963  39.832  27.215  1.00 61.87           C  
ANISOU 4093  CD  PRO A 567     7269   9046   7192   -287   -480   -141       C  
ATOM   4094  N   PRO A 568      44.284  36.555  25.044  1.00 67.46           N  
ANISOU 4094  N   PRO A 568     8059   9666   7907   -258   -460     62       N  
ATOM   4095  CA  PRO A 568      43.932  35.452  24.140  1.00 63.54           C  
ANISOU 4095  CA  PRO A 568     7587   9131   7423   -248   -447    127       C  
ATOM   4096  C   PRO A 568      44.166  35.749  22.644  1.00 60.16           C  
ANISOU 4096  C   PRO A 568     7143   8638   7077   -235   -422    130       C  
ATOM   4097  O   PRO A 568      44.307  34.821  21.846  1.00 57.03           O  
ANISOU 4097  O   PRO A 568     6759   8209   6701   -222   -423    178       O  
ATOM   4098  CB  PRO A 568      42.451  35.210  24.438  1.00 64.15           C  
ANISOU 4098  CB  PRO A 568     7693   9227   7453   -263   -415    141       C  
ATOM   4099  CG  PRO A 568      41.960  36.497  24.998  1.00 64.22           C  
ANISOU 4099  CG  PRO A 568     7686   9261   7452   -279   -397     76       C  
ATOM   4100  CD  PRO A 568      43.103  37.099  25.742  1.00 65.22           C  
ANISOU 4100  CD  PRO A 568     7785   9417   7577   -278   -434     33       C  
ATOM   4101  N   LEU A 569      44.222  37.023  22.272  1.00 60.04           N  
ANISOU 4101  N   LEU A 569     7100   8603   7109   -239   -400     78       N  
ATOM   4102  CA  LEU A 569      44.536  37.393  20.886  1.00 60.99           C  
ANISOU 4102  CA  LEU A 569     7204   8663   7305   -225   -375     81       C  
ATOM   4103  C   LEU A 569      45.996  37.084  20.526  1.00 62.11           C  
ANISOU 4103  C   LEU A 569     7327   8784   7489   -209   -405     92       C  
ATOM   4104  O   LEU A 569      46.279  36.476  19.492  1.00 61.71           O  
ANISOU 4104  O   LEU A 569     7280   8693   7473   -193   -399    129       O  
ATOM   4105  CB  LEU A 569      44.200  38.864  20.619  1.00 57.71           C  
ANISOU 4105  CB  LEU A 569     6763   8231   6932   -233   -341     27       C  
ATOM   4106  CG  LEU A 569      42.729  39.224  20.350  1.00 58.95           C  
ANISOU 4106  CG  LEU A 569     6936   8384   7078   -243   -300     22       C  
ATOM   4107  CD1 LEU A 569      42.619  40.663  19.866  1.00 57.54           C  
ANISOU 4107  CD1 LEU A 569     6727   8176   6958   -246   -267    -25       C  
ATOM   4108  CD2 LEU A 569      42.081  38.303  19.320  1.00 57.35           C  
ANISOU 4108  CD2 LEU A 569     6760   8151   6879   -231   -282     76       C  
ATOM   4109  N   ILE A 570      46.906  37.497  21.401  1.00 65.08           N  
ANISOU 4109  N   ILE A 570     7679   9187   7860   -212   -438     56       N  
ATOM   4110  CA  ILE A 570      48.330  37.194  21.275  1.00 70.05           C  
ANISOU 4110  CA  ILE A 570     8287   9803   8525   -197   -472     61       C  
ATOM   4111  C   ILE A 570      48.595  35.690  21.381  1.00 69.24           C  
ANISOU 4111  C   ILE A 570     8210   9709   8388   -187   -504    122       C  
ATOM   4112  O   ILE A 570      49.443  35.144  20.658  1.00 65.57           O  
ANISOU 4112  O   ILE A 570     7738   9210   7966   -171   -515    148       O  
ATOM   4113  CB  ILE A 570      49.151  37.931  22.354  1.00 73.51           C  
ANISOU 4113  CB  ILE A 570     8695  10277   8958   -203   -506      5       C  
ATOM   4114  CG1 ILE A 570      48.838  39.431  22.322  1.00 74.00           C  
ANISOU 4114  CG1 ILE A 570     8729  10331   9058   -216   -474    -58       C  
ATOM   4115  CG2 ILE A 570      50.648  37.682  22.166  1.00 73.22           C  
ANISOU 4115  CG2 ILE A 570     8632  10222   8967   -188   -541      6       C  
ATOM   4116  CD1 ILE A 570      49.013  40.112  23.663  1.00 75.83           C  
ANISOU 4116  CD1 ILE A 570     8941  10615   9254   -228   -500   -118       C  
ATOM   4117  N   GLN A 571      47.871  35.022  22.276  1.00 66.91           N  
ANISOU 4117  N   GLN A 571     7946   9458   8019   -195   -516    145       N  
ATOM   4118  CA  GLN A 571      48.039  33.594  22.425  1.00 68.03           C  
ANISOU 4118  CA  GLN A 571     8112   9607   8130   -186   -543    206       C  
ATOM   4119  C   GLN A 571      47.925  32.876  21.078  1.00 68.65           C  
ANISOU 4119  C   GLN A 571     8200   9630   8254   -173   -521    249       C  
ATOM   4120  O   GLN A 571      48.786  32.064  20.752  1.00 70.53           O  
ANISOU 4120  O   GLN A 571     8434   9849   8516   -158   -546    281       O  
ATOM   4121  CB  GLN A 571      47.066  33.021  23.436  1.00 70.77           C  
ANISOU 4121  CB  GLN A 571     8492  10002   8395   -198   -547    230       C  
ATOM   4122  CG  GLN A 571      47.289  31.539  23.686  1.00 77.73           C  
ANISOU 4122  CG  GLN A 571     9397  10891   9247   -187   -576    295       C  
ATOM   4123  CD  GLN A 571      46.171  30.905  24.489  1.00 84.60           C  
ANISOU 4123  CD  GLN A 571    10303  11799  10044   -199   -567    327       C  
ATOM   4124  OE1 GLN A 571      45.680  31.485  25.462  1.00 85.65           O  
ANISOU 4124  OE1 GLN A 571    10440  11979  10123   -213   -565    298       O  
ATOM   4125  NE2 GLN A 571      45.763  29.706  24.088  1.00 85.91           N  
ANISOU 4125  NE2 GLN A 571    10491  11942  10208   -193   -561    387       N  
ATOM   4126  N   LYS A 572      46.893  33.193  20.292  1.00 67.96           N  
ANISOU 4126  N   LYS A 572     8123   9519   8182   -177   -476    248       N  
ATOM   4127  CA  LYS A 572      46.684  32.538  18.990  1.00 68.79           C  
ANISOU 4127  CA  LYS A 572     8236   9576   8326   -163   -453    285       C  
ATOM   4128  C   LYS A 572      47.647  33.058  17.929  1.00 63.64           C  
ANISOU 4128  C   LYS A 572     7556   8880   7746   -149   -445    269       C  
ATOM   4129  O   LYS A 572      47.986  32.356  16.977  1.00 63.03           O  
ANISOU 4129  O   LYS A 572     7479   8767   7702   -133   -441    300       O  
ATOM   4130  CB  LYS A 572      45.237  32.690  18.503  1.00 72.77           C  
ANISOU 4130  CB  LYS A 572     8760  10071   8819   -171   -410    288       C  
ATOM   4131  CG  LYS A 572      44.185  32.259  19.517  1.00 81.88           C  
ANISOU 4131  CG  LYS A 572     9940  11266   9904   -187   -410    301       C  
ATOM   4132  CD  LYS A 572      44.047  30.747  19.661  1.00 87.10           C  
ANISOU 4132  CD  LYS A 572    10626  11929  10540   -182   -428    359       C  
ATOM   4133  CE  LYS A 572      43.232  30.404  20.904  1.00 90.15           C  
ANISOU 4133  CE  LYS A 572    11035  12363  10855   -199   -432    371       C  
ATOM   4134  NZ  LYS A 572      43.370  28.977  21.312  1.00 91.32           N  
ANISOU 4134  NZ  LYS A 572    11203  12518  10977   -193   -456    429       N  
ATOM   4135  N   TRP A 573      48.052  34.308  18.097  1.00 64.16           N  
ANISOU 4135  N   TRP A 573     7594   8946   7837   -154   -438    219       N  
ATOM   4136  CA  TRP A 573      49.121  34.929  17.316  1.00 65.28           C  
ANISOU 4136  CA  TRP A 573     7703   9050   8049   -142   -432    199       C  
ATOM   4137  C   TRP A 573      50.410  34.131  17.390  1.00 65.41           C  
ANISOU 4137  C   TRP A 573     7708   9061   8084   -129   -472    219       C  
ATOM   4138  O   TRP A 573      51.055  33.881  16.361  1.00 60.01           O  
ANISOU 4138  O   TRP A 573     7013   8336   7452   -114   -463    235       O  
ATOM   4139  CB  TRP A 573      49.312  36.339  17.848  1.00 67.36           C  
ANISOU 4139  CB  TRP A 573     7939   9325   8329   -154   -425    140       C  
ATOM   4140  CG  TRP A 573      50.547  37.061  17.398  1.00 71.96           C  
ANISOU 4140  CG  TRP A 573     8482   9876   8983   -145   -425    111       C  
ATOM   4141  CD1 TRP A 573      51.827  36.962  17.924  1.00 73.95           C  
ANISOU 4141  CD1 TRP A 573     8708  10135   9253   -141   -465     96       C  
ATOM   4142  CD2 TRP A 573      50.648  38.067  16.340  1.00 71.39           C  
ANISOU 4142  CD2 TRP A 573     8388   9759   8980   -139   -381     92       C  
ATOM   4143  NE1 TRP A 573      52.685  37.797  17.265  1.00 74.87           N  
ANISOU 4143  NE1 TRP A 573     8789  10213   9446   -134   -447     68       N  
ATOM   4144  CE2 TRP A 573      52.045  38.485  16.308  1.00 71.10           C  
ANISOU 4144  CE2 TRP A 573     8312   9702   9001   -133   -396     67       C  
ATOM   4145  CE3 TRP A 573      49.755  38.631  15.441  1.00 70.60           C  
ANISOU 4145  CE3 TRP A 573     8296   9633   8898   -137   -332     96       C  
ATOM   4146  CZ2 TRP A 573      52.505  39.436  15.418  1.00 73.33           C  
ANISOU 4146  CZ2 TRP A 573     8565   9939   9358   -126   -359     48       C  
ATOM   4147  CZ3 TRP A 573      50.232  39.591  14.546  1.00 69.95           C  
ANISOU 4147  CZ3 TRP A 573     8185   9506   8886   -128   -298     79       C  
ATOM   4148  CH2 TRP A 573      51.575  39.978  14.534  1.00 71.97           C  
ANISOU 4148  CH2 TRP A 573     8403   9742   9198   -123   -309     57       C  
ATOM   4149  N   ASN A 574      50.774  33.716  18.607  1.00 63.46           N  
ANISOU 4149  N   ASN A 574     7464   8856   7793   -135   -516    219       N  
ATOM   4150  CA  ASN A 574      51.936  32.862  18.844  1.00 64.69           C  
ANISOU 4150  CA  ASN A 574     7610   9011   7958   -123   -561    241       C  
ATOM   4151  C   ASN A 574      51.805  31.429  18.321  1.00 66.53           C  
ANISOU 4151  C   ASN A 574     7867   9226   8185   -111   -567    301       C  
ATOM   4152  O   ASN A 574      52.811  30.781  18.073  1.00 70.84           O  
ANISOU 4152  O   ASN A 574     8400   9753   8762    -97   -592    320       O  
ATOM   4153  CB  ASN A 574      52.287  32.824  20.334  1.00 64.33           C  
ANISOU 4153  CB  ASN A 574     7562   9020   7859   -130   -608    225       C  
ATOM   4154  CG  ASN A 574      52.684  34.183  20.881  1.00 66.64           C  
ANISOU 4154  CG  ASN A 574     7823   9330   8168   -139   -611    158       C  
ATOM   4155  OD1 ASN A 574      53.099  35.086  20.142  1.00 66.29           O  
ANISOU 4155  OD1 ASN A 574     7749   9248   8188   -137   -585    125       O  
ATOM   4156  ND2 ASN A 574      52.554  34.339  22.192  1.00 68.21           N  
ANISOU 4156  ND2 ASN A 574     8026   9586   8306   -148   -641    137       N  
ATOM   4157  N   MET A 575      50.586  30.924  18.158  1.00 68.23           N  
ANISOU 4157  N   MET A 575     8114   9445   8365   -116   -544    330       N  
ATOM   4158  CA  MET A 575      50.406  29.553  17.669  1.00 69.07           C  
ANISOU 4158  CA  MET A 575     8241   9533   8471   -106   -548    385       C  
ATOM   4159  C   MET A 575      50.529  29.494  16.167  1.00 68.45           C  
ANISOU 4159  C   MET A 575     8153   9402   8451    -92   -517    391       C  
ATOM   4160  O   MET A 575      50.895  28.463  15.614  1.00 73.87           O  
ANISOU 4160  O   MET A 575     8842  10065   9160    -78   -526    425       O  
ATOM   4161  CB  MET A 575      49.025  29.006  18.014  1.00 75.10           C  
ANISOU 4161  CB  MET A 575     9037  10316   9180   -117   -533    412       C  
ATOM   4162  CG  MET A 575      48.757  28.718  19.474  1.00 81.40           C  
ANISOU 4162  CG  MET A 575     9852  11167   9910   -129   -561    422       C  
ATOM   4163  SD  MET A 575      46.995  28.345  19.659  1.00 85.03           S  
ANISOU 4163  SD  MET A 575    10348  11641  10319   -143   -526    445       S  
ATOM   4164  CE  MET A 575      46.900  28.213  21.445  1.00 83.59           C  
ANISOU 4164  CE  MET A 575    10181  11526  10054   -156   -559    451       C  
ATOM   4165  N   LEU A 576      50.172  30.584  15.502  1.00 65.23           N  
ANISOU 4165  N   LEU A 576     7736   8979   8069    -93   -478    359       N  
ATOM   4166  CA  LEU A 576      50.026  30.547  14.056  1.00 66.51           C  
ANISOU 4166  CA  LEU A 576     7898   9099   8275    -79   -442    368       C  
ATOM   4167  C   LEU A 576      51.345  30.840  13.363  1.00 68.32           C  
ANISOU 4167  C   LEU A 576     8096   9295   8567    -65   -444    356       C  
ATOM   4168  O   LEU A 576      52.086  31.738  13.764  1.00 67.30           O  
ANISOU 4168  O   LEU A 576     7941   9170   8459    -69   -451    321       O  
ATOM   4169  CB  LEU A 576      48.937  31.524  13.583  1.00 63.04           C  
ANISOU 4169  CB  LEU A 576     7464   8655   7831    -85   -398    345       C  
ATOM   4170  CG  LEU A 576      47.463  31.298  13.961  1.00 62.03           C  
ANISOU 4170  CG  LEU A 576     7366   8550   7652    -98   -384    355       C  
ATOM   4171  CD1 LEU A 576      46.602  32.387  13.337  1.00 59.34           C  
ANISOU 4171  CD1 LEU A 576     7024   8198   7322    -99   -341    329       C  
ATOM   4172  CD2 LEU A 576      46.936  29.925  13.559  1.00 57.36           C  
ANISOU 4172  CD2 LEU A 576     6797   7949   7048    -90   -387    398       C  
ATOM   4173  N   LYS A 577      51.621  30.079  12.315  1.00 71.79           N  
ANISOU 4173  N   LYS A 577     8536   9702   9037    -48   -435    381       N  
ATOM   4174  CA  LYS A 577      52.843  30.240  11.554  1.00 74.73           C  
ANISOU 4174  CA  LYS A 577     8880  10042   9471    -33   -432    374       C  
ATOM   4175  C   LYS A 577      52.604  31.172  10.383  1.00 73.25           C  
ANISOU 4175  C   LYS A 577     8687   9828   9318    -24   -381    358       C  
ATOM   4176  O   LYS A 577      51.470  31.310   9.909  1.00 69.96           O  
ANISOU 4176  O   LYS A 577     8291   9413   8880    -24   -352    363       O  
ATOM   4177  CB  LYS A 577      53.343  28.878  11.076  1.00 84.78           C  
ANISOU 4177  CB  LYS A 577    10156  11297  10761    -18   -451    409       C  
ATOM   4178  CG  LYS A 577      54.082  28.077  12.149  1.00 93.70           C  
ANISOU 4178  CG  LYS A 577    11280  12444  11877    -22   -504    424       C  
ATOM   4179  CD  LYS A 577      53.761  26.581  12.104  1.00103.70           C  
ANISOU 4179  CD  LYS A 577    12566  13707  13128    -16   -522    468       C  
ATOM   4180  CE  LYS A 577      53.840  25.970  10.700  1.00110.65           C  
ANISOU 4180  CE  LYS A 577    13443  14548  14049      3   -497    482       C  
ATOM   4181  NZ  LYS A 577      55.232  25.795  10.184  1.00115.18           N  
ANISOU 4181  NZ  LYS A 577    13988  15094  14682     17   -508    478       N  
ATOM   4182  N   ASP A 578      53.686  31.800   9.920  1.00 69.48           N  
ANISOU 4182  N   ASP A 578     8179   9325   8896    -16   -371    339       N  
ATOM   4183  CA  ASP A 578      53.646  32.826   8.874  1.00 65.30           C  
ANISOU 4183  CA  ASP A 578     7639   8769   8405     -7   -322    325       C  
ATOM   4184  C   ASP A 578      53.015  32.395   7.559  1.00 62.40           C  
ANISOU 4184  C   ASP A 578     7289   8382   8037     11   -288    350       C  
ATOM   4185  O   ASP A 578      52.730  33.232   6.709  1.00 57.79           O  
ANISOU 4185  O   ASP A 578     6703   7782   7473     20   -246    344       O  
ATOM   4186  CB  ASP A 578      55.055  33.360   8.594  1.00 68.08           C  
ANISOU 4186  CB  ASP A 578     7953   9093   8821      0   -318    307       C  
ATOM   4187  CG  ASP A 578      55.522  34.363   9.636  1.00 72.22           C  
ANISOU 4187  CG  ASP A 578     8451   9630   9358    -16   -333    267       C  
ATOM   4188  OD1 ASP A 578      54.757  34.638  10.587  1.00 74.07           O  
ANISOU 4188  OD1 ASP A 578     8699   9898   9547    -33   -347    253       O  
ATOM   4189  OD2 ASP A 578      56.655  34.880   9.504  1.00 70.02           O  
ANISOU 4189  OD2 ASP A 578     8139   9329   9137    -13   -331    246       O  
ATOM   4190  N   GLU A 579      52.814  31.097   7.384  1.00 63.56           N  
ANISOU 4190  N   GLU A 579     7453   8532   8165     18   -307    379       N  
ATOM   4191  CA  GLU A 579      52.238  30.585   6.139  1.00 66.70           C  
ANISOU 4191  CA  GLU A 579     7866   8914   8562     37   -279    398       C  
ATOM   4192  C   GLU A 579      50.756  30.203   6.298  1.00 65.14           C  
ANISOU 4192  C   GLU A 579     7699   8738   8313     31   -277    409       C  
ATOM   4193  O   GLU A 579      50.112  29.817   5.323  1.00 61.53           O  
ANISOU 4193  O   GLU A 579     7255   8272   7850     46   -255    420       O  
ATOM   4194  CB  GLU A 579      53.073  29.423   5.552  1.00 68.63           C  
ANISOU 4194  CB  GLU A 579     8103   9139   8833     53   -294    418       C  
ATOM   4195  CG  GLU A 579      53.653  28.435   6.568  1.00 72.70           C  
ANISOU 4195  CG  GLU A 579     8615   9666   9343     43   -345    430       C  
ATOM   4196  CD  GLU A 579      54.879  28.973   7.304  1.00 79.16           C  
ANISOU 4196  CD  GLU A 579     9404  10481  10191     36   -367    411       C  
ATOM   4197  OE1 GLU A 579      55.589  29.851   6.758  1.00 79.79           O  
ANISOU 4197  OE1 GLU A 579     9461  10540  10314     42   -342    392       O  
ATOM   4198  OE2 GLU A 579      55.136  28.520   8.441  1.00 81.71           O  
ANISOU 4198  OE2 GLU A 579     9727  10824  10494     24   -410    415       O  
ATOM   4199  N   ASP A 580      50.226  30.334   7.516  1.00 63.78           N  
ANISOU 4199  N   ASP A 580     7536   8593   8103      9   -298    402       N  
ATOM   4200  CA  ASP A 580      48.824  29.989   7.814  1.00 65.05           C  
ANISOU 4200  CA  ASP A 580     7725   8775   8217      0   -295    410       C  
ATOM   4201  C   ASP A 580      47.812  31.113   7.504  1.00 63.02           C  
ANISOU 4201  C   ASP A 580     7475   8521   7948     -2   -258    391       C  
ATOM   4202  O   ASP A 580      47.823  32.160   8.160  1.00 62.89           O  
ANISOU 4202  O   ASP A 580     7450   8516   7930    -16   -254    367       O  
ATOM   4203  CB  ASP A 580      48.688  29.564   9.280  1.00 65.57           C  
ANISOU 4203  CB  ASP A 580     7799   8871   8244    -21   -332    415       C  
ATOM   4204  CG  ASP A 580      47.395  28.800   9.558  1.00 69.04           C  
ANISOU 4204  CG  ASP A 580     8266   9326   8641    -29   -333    433       C  
ATOM   4205  OD1 ASP A 580      46.460  28.833   8.718  1.00 68.58           O  
ANISOU 4205  OD1 ASP A 580     8219   9259   8580    -20   -304    433       O  
ATOM   4206  OD2 ASP A 580      47.323  28.154  10.626  1.00 67.74           O  
ANISOU 4206  OD2 ASP A 580     8110   9183   8446    -42   -363    448       O  
ATOM   4207  N   LYS A 581      46.931  30.872   6.528  1.00 60.89           N  
ANISOU 4207  N   LYS A 581     7219   8243   7672     12   -234    400       N  
ATOM   4208  CA  LYS A 581      45.906  31.846   6.107  1.00 62.11           C  
ANISOU 4208  CA  LYS A 581     7381   8400   7818     14   -200    385       C  
ATOM   4209  C   LYS A 581      45.002  32.310   7.266  1.00 59.89           C  
ANISOU 4209  C   LYS A 581     7110   8146   7501    -11   -206    370       C  
ATOM   4210  O   LYS A 581      44.487  33.438   7.254  1.00 57.47           O  
ANISOU 4210  O   LYS A 581     6800   7840   7195    -16   -181    349       O  
ATOM   4211  CB  LYS A 581      45.029  31.293   4.971  1.00 67.37           C  
ANISOU 4211  CB  LYS A 581     8063   9058   8477     34   -182    398       C  
ATOM   4212  CG  LYS A 581      45.751  30.564   3.842  1.00 73.41           C  
ANISOU 4212  CG  LYS A 581     8823   9803   9269     60   -179    413       C  
ATOM   4213  CD  LYS A 581      46.521  31.498   2.926  1.00 75.87           C  
ANISOU 4213  CD  LYS A 581     9118  10095   9616     78   -149    408       C  
ATOM   4214  CE  LYS A 581      47.524  30.728   2.071  1.00 81.41           C  
ANISOU 4214  CE  LYS A 581     9809  10777  10346     98   -151    421       C  
ATOM   4215  NZ  LYS A 581      47.104  30.575   0.648  1.00 79.50           N  
ANISOU 4215  NZ  LYS A 581     9575  10528  10103    128   -124    427       N  
ATOM   4216  N   ASP A 582      44.827  31.456   8.269  1.00 51.58           N  
ANISOU 4216  N   ASP A 582     6068   7113   6417    -27   -236    380       N  
ATOM   4217  CA  ASP A 582      44.085  31.840   9.451  1.00 52.37           C  
ANISOU 4217  CA  ASP A 582     6177   7243   6479    -52   -242    366       C  
ATOM   4218  C   ASP A 582      44.623  33.074  10.152  1.00 53.05           C  
ANISOU 4218  C   ASP A 582     6244   7338   6574    -65   -241    335       C  
ATOM   4219  O   ASP A 582      43.981  33.588  11.074  1.00 52.95           O  
ANISOU 4219  O   ASP A 582     6236   7350   6532    -84   -241    316       O  
ATOM   4220  CB  ASP A 582      43.962  30.667  10.413  1.00 54.65           C  
ANISOU 4220  CB  ASP A 582     6480   7552   6733    -65   -274    388       C  
ATOM   4221  CG  ASP A 582      43.144  29.534   9.824  1.00 58.01           C  
ANISOU 4221  CG  ASP A 582     6922   7968   7151    -56   -270    413       C  
ATOM   4222  OD1 ASP A 582      42.743  29.617   8.636  1.00 59.51           O  
ANISOU 4222  OD1 ASP A 582     7113   8138   7360    -38   -246    411       O  
ATOM   4223  OD2 ASP A 582      42.898  28.557  10.543  1.00 63.04           O  
ANISOU 4223  OD2 ASP A 582     7571   8618   7763    -66   -291    435       O  
ATOM   4224  N   LEU A 583      45.777  33.567   9.702  1.00 51.13           N  
ANISOU 4224  N   LEU A 583     5978   7074   6374    -54   -238    327       N  
ATOM   4225  CA  LEU A 583      46.272  34.876  10.141  1.00 51.76           C  
ANISOU 4225  CA  LEU A 583     6035   7154   6476    -63   -230    293       C  
ATOM   4226  C   LEU A 583      45.401  36.023   9.654  1.00 50.82           C  
ANISOU 4226  C   LEU A 583     5915   7026   6367    -63   -191    274       C  
ATOM   4227  O   LEU A 583      45.255  37.015  10.373  1.00 56.33           O  
ANISOU 4227  O   LEU A 583     6600   7736   7066    -78   -186    242       O  
ATOM   4228  CB  LEU A 583      47.711  35.137   9.682  1.00 50.89           C  
ANISOU 4228  CB  LEU A 583     5898   7019   6419    -51   -232    290       C  
ATOM   4229  CG  LEU A 583      48.857  34.479  10.447  1.00 53.43           C  
ANISOU 4229  CG  LEU A 583     6209   7351   6743    -56   -275    293       C  
ATOM   4230  CD1 LEU A 583      50.162  34.830   9.737  1.00 52.26           C  
ANISOU 4230  CD1 LEU A 583     6031   7169   6656    -41   -267    288       C  
ATOM   4231  CD2 LEU A 583      48.911  34.881  11.927  1.00 49.97           C  
ANISOU 4231  CD2 LEU A 583     5763   6947   6275    -78   -303    266       C  
ATOM   4232  N   PHE A 584      44.837  35.902   8.451  1.00 47.09           N  
ANISOU 4232  N   PHE A 584     5453   6534   5904    -43   -164    291       N  
ATOM   4233  CA  PHE A 584      44.067  37.009   7.856  1.00 51.35           C  
ANISOU 4233  CA  PHE A 584     5991   7062   6458    -37   -125    277       C  
ATOM   4234  C   PHE A 584      43.020  37.583   8.812  1.00 51.23           C  
ANISOU 4234  C   PHE A 584     5981   7071   6413    -60   -123    252       C  
ATOM   4235  O   PHE A 584      43.003  38.793   9.039  1.00 52.20           O  
ANISOU 4235  O   PHE A 584     6086   7189   6558    -68   -105    224       O  
ATOM   4236  CB  PHE A 584      43.409  36.634   6.519  1.00 49.70           C  
ANISOU 4236  CB  PHE A 584     5797   6837   6249    -12   -103    301       C  
ATOM   4237  CG  PHE A 584      44.366  36.099   5.488  1.00 54.47           C  
ANISOU 4237  CG  PHE A 584     6397   7420   6881     12   -100    323       C  
ATOM   4238  CD1 PHE A 584      45.751  36.253   5.629  1.00 58.50           C  
ANISOU 4238  CD1 PHE A 584     6884   7916   7426     12   -108    321       C  
ATOM   4239  CD2 PHE A 584      43.886  35.471   4.345  1.00 57.43           C  
ANISOU 4239  CD2 PHE A 584     6785   7786   7248     36    -88    344       C  
ATOM   4240  CE1 PHE A 584      46.629  35.766   4.669  1.00 57.86           C  
ANISOU 4240  CE1 PHE A 584     6798   7815   7373     34   -103    340       C  
ATOM   4241  CE2 PHE A 584      44.759  34.980   3.380  1.00 59.54           C  
ANISOU 4241  CE2 PHE A 584     7048   8035   7540     59    -84    363       C  
ATOM   4242  CZ  PHE A 584      46.133  35.131   3.541  1.00 59.04           C  
ANISOU 4242  CZ  PHE A 584     6963   7958   7511     58    -90    361       C  
ATOM   4243  N   PRO A 585      42.156  36.719   9.385  1.00 51.18           N  
ANISOU 4243  N   PRO A 585     5998   7090   6360    -72   -140    261       N  
ATOM   4244  CA  PRO A 585      41.121  37.260  10.255  1.00 51.19           C  
ANISOU 4244  CA  PRO A 585     6004   7114   6333    -93   -134    236       C  
ATOM   4245  C   PRO A 585      41.698  37.789  11.557  1.00 50.13           C  
ANISOU 4245  C   PRO A 585     5854   7002   6190   -116   -153    207       C  
ATOM   4246  O   PRO A 585      41.250  38.827  12.043  1.00 49.53           O  
ANISOU 4246  O   PRO A 585     5768   6935   6118   -129   -138    173       O  
ATOM   4247  CB  PRO A 585      40.204  36.050  10.525  1.00 50.38           C  
ANISOU 4247  CB  PRO A 585     5928   7029   6184    -99   -147    257       C  
ATOM   4248  CG  PRO A 585      40.514  35.075   9.436  1.00 50.11           C  
ANISOU 4248  CG  PRO A 585     5901   6974   6163    -75   -150    290       C  
ATOM   4249  CD  PRO A 585      41.964  35.275   9.141  1.00 50.90           C  
ANISOU 4249  CD  PRO A 585     5982   7057   6300    -64   -158    293       C  
ATOM   4250  N   LEU A 586      42.669  37.077  12.122  1.00 49.97           N  
ANISOU 4250  N   LEU A 586     5831   6994   6160   -119   -186    217       N  
ATOM   4251  CA  LEU A 586      43.321  37.528  13.352  1.00 51.36           C  
ANISOU 4251  CA  LEU A 586     5992   7196   6327   -137   -210    188       C  
ATOM   4252  C   LEU A 586      43.999  38.891  13.152  1.00 51.04           C  
ANISOU 4252  C   LEU A 586     5917   7134   6340   -136   -192    152       C  
ATOM   4253  O   LEU A 586      43.859  39.802  13.983  1.00 50.78           O  
ANISOU 4253  O   LEU A 586     5871   7119   6306   -153   -190    112       O  
ATOM   4254  CB  LEU A 586      44.328  36.491  13.842  1.00 50.94           C  
ANISOU 4254  CB  LEU A 586     5941   7155   6260   -136   -250    210       C  
ATOM   4255  CG  LEU A 586      45.074  36.815  15.136  1.00 52.09           C  
ANISOU 4255  CG  LEU A 586     6070   7332   6390   -151   -282    181       C  
ATOM   4256  CD1 LEU A 586      44.135  37.123  16.296  1.00 49.77           C  
ANISOU 4256  CD1 LEU A 586     5786   7080   6043   -174   -283    158       C  
ATOM   4257  CD2 LEU A 586      46.013  35.672  15.474  1.00 51.96           C  
ANISOU 4257  CD2 LEU A 586     6057   7324   6361   -145   -323    210       C  
ATOM   4258  N   LEU A 587      44.691  39.040  12.029  1.00 48.71           N  
ANISOU 4258  N   LEU A 587     5610   6801   6095   -115   -176    167       N  
ATOM   4259  CA  LEU A 587      45.417  40.273  11.770  1.00 51.81           C  
ANISOU 4259  CA  LEU A 587     5970   7169   6547   -112   -156    138       C  
ATOM   4260  C   LEU A 587      44.477  41.427  11.474  1.00 50.60           C  
ANISOU 4260  C   LEU A 587     5811   7003   6410   -115   -118    117       C  
ATOM   4261  O   LEU A 587      44.723  42.566  11.891  1.00 50.71           O  
ANISOU 4261  O   LEU A 587     5797   7012   6458   -125   -107     78       O  
ATOM   4262  CB  LEU A 587      46.420  40.110  10.621  1.00 51.62           C  
ANISOU 4262  CB  LEU A 587     5934   7107   6572    -89   -145    162       C  
ATOM   4263  CG  LEU A 587      47.669  39.233  10.803  1.00 55.35           C  
ANISOU 4263  CG  LEU A 587     6400   7581   7051    -84   -179    176       C  
ATOM   4264  CD1 LEU A 587      48.842  39.852  10.062  1.00 51.20           C  
ANISOU 4264  CD1 LEU A 587     5843   7016   6594    -70   -161    171       C  
ATOM   4265  CD2 LEU A 587      48.026  39.013  12.265  1.00 52.39           C  
ANISOU 4265  CD2 LEU A 587     6019   7242   6643   -105   -222    153       C  
ATOM   4266  N   GLU A 588      43.405  41.135  10.746  1.00 50.62           N  
ANISOU 4266  N   GLU A 588     5837   7000   6394   -105    -98    141       N  
ATOM   4267  CA  GLU A 588      42.421  42.160  10.458  1.00 49.14           C  
ANISOU 4267  CA  GLU A 588     5646   6803   6221   -106    -63    123       C  
ATOM   4268  C   GLU A 588      41.717  42.529  11.746  1.00 47.10           C  
ANISOU 4268  C   GLU A 588     5388   6579   5931   -133    -73     86       C  
ATOM   4269  O   GLU A 588      41.408  43.693  11.985  1.00 47.99           O  
ANISOU 4269  O   GLU A 588     5481   6685   6070   -143    -53     52       O  
ATOM   4270  CB  GLU A 588      41.476  41.723   9.357  1.00 51.44           C  
ANISOU 4270  CB  GLU A 588     5962   7081   6500    -86    -43    156       C  
ATOM   4271  CG  GLU A 588      42.032  42.061   7.990  1.00 54.83           C  
ANISOU 4271  CG  GLU A 588     6382   7473   6976    -57    -16    179       C  
ATOM   4272  CD  GLU A 588      41.322  41.373   6.848  1.00 59.75           C  
ANISOU 4272  CD  GLU A 588     7031   8090   7582    -33     -5    214       C  
ATOM   4273  OE1 GLU A 588      40.508  40.449   7.090  1.00 66.16           O  
ANISOU 4273  OE1 GLU A 588     7866   8923   8348    -38    -22    222       O  
ATOM   4274  OE2 GLU A 588      41.596  41.755   5.690  1.00 63.12           O  
ANISOU 4274  OE2 GLU A 588     7453   8489   8042     -7     21    232       O  
ATOM   4275  N   CYS A 589      41.539  41.551  12.617  1.00 44.84           N  
ANISOU 4275  N   CYS A 589     5121   6328   5588   -147   -105     92       N  
ATOM   4276  CA  CYS A 589      40.968  41.854  13.902  1.00 46.74           C  
ANISOU 4276  CA  CYS A 589     5361   6606   5793   -173   -115     58       C  
ATOM   4277  C   CYS A 589      41.911  42.779  14.676  1.00 49.10           C  
ANISOU 4277  C   CYS A 589     5626   6910   6119   -185   -125     13       C  
ATOM   4278  O   CYS A 589      41.489  43.832  15.190  1.00 46.34           O  
ANISOU 4278  O   CYS A 589     5258   6567   5782   -199   -110    -30       O  
ATOM   4279  CB  CYS A 589      40.678  40.581  14.680  1.00 46.50           C  
ANISOU 4279  CB  CYS A 589     5358   6613   5696   -183   -145     79       C  
ATOM   4280  SG  CYS A 589      40.198  40.945  16.379  1.00 51.77           S  
ANISOU 4280  SG  CYS A 589     6024   7333   6312   -214   -159     36       S  
ATOM   4281  N   LEU A 590      43.193  42.394  14.736  1.00 48.40           N  
ANISOU 4281  N   LEU A 590     5526   6818   6045   -178   -150     21       N  
ATOM   4282  CA  LEU A 590      44.194  43.194  15.439  1.00 47.36           C  
ANISOU 4282  CA  LEU A 590     5359   6692   5945   -187   -164    -23       C  
ATOM   4283  C   LEU A 590      44.268  44.611  14.906  1.00 44.14           C  
ANISOU 4283  C   LEU A 590     4918   6246   5607   -185   -126    -54       C  
ATOM   4284  O   LEU A 590      44.366  45.570  15.667  1.00 43.15           O  
ANISOU 4284  O   LEU A 590     4765   6130   5500   -200   -126   -106       O  
ATOM   4285  CB  LEU A 590      45.554  42.509  15.384  1.00 49.13           C  
ANISOU 4285  CB  LEU A 590     5574   6910   6181   -177   -195     -5       C  
ATOM   4286  CG  LEU A 590      45.667  41.402  16.442  1.00 50.10           C  
ANISOU 4286  CG  LEU A 590     5718   7081   6236   -186   -240      7       C  
ATOM   4287  CD1 LEU A 590      46.854  40.496  16.150  1.00 46.04           C  
ANISOU 4287  CD1 LEU A 590     5202   6556   5734   -171   -269     38       C  
ATOM   4288  CD2 LEU A 590      45.733  41.981  17.856  1.00 47.47           C  
ANISOU 4288  CD2 LEU A 590     5370   6791   5876   -207   -262    -45       C  
ATOM   4289  N   SER A 591      44.164  44.747  13.593  1.00 44.58           N  
ANISOU 4289  N   SER A 591     4977   6260   5703   -164    -94    -22       N  
ATOM   4290  CA  SER A 591      44.183  46.052  12.992  1.00 45.68           C  
ANISOU 4290  CA  SER A 591     5087   6359   5910   -159    -55    -42       C  
ATOM   4291  C   SER A 591      43.133  46.970  13.613  1.00 49.28           C  
ANISOU 4291  C   SER A 591     5536   6828   6361   -177    -38    -83       C  
ATOM   4292  O   SER A 591      43.433  48.109  13.999  1.00 53.58           O  
ANISOU 4292  O   SER A 591     6044   7360   6954   -187    -26   -129       O  
ATOM   4293  CB  SER A 591      43.977  45.925  11.497  1.00 49.10           C  
ANISOU 4293  CB  SER A 591     5535   6754   6368   -132    -23      5       C  
ATOM   4294  OG  SER A 591      44.214  47.171  10.870  1.00 56.49           O  
ANISOU 4294  OG  SER A 591     6439   7647   7376   -124     16     -7       O  
ATOM   4295  N   SER A 592      41.903  46.474  13.720  1.00 48.88           N  
ANISOU 4295  N   SER A 592     5517   6800   6256   -182    -37    -70       N  
ATOM   4296  CA  SER A 592      40.805  47.269  14.250  1.00 47.88           C  
ANISOU 4296  CA  SER A 592     5384   6685   6123   -198    -19   -106       C  
ATOM   4297  C   SER A 592      41.011  47.549  15.726  1.00 46.67           C  
ANISOU 4297  C   SER A 592     5215   6573   5945   -224    -45   -160       C  
ATOM   4298  O   SER A 592      40.773  48.656  16.186  1.00 47.93           O  
ANISOU 4298  O   SER A 592     5346   6729   6135   -238    -29   -209       O  
ATOM   4299  CB  SER A 592      39.456  46.555  14.027  1.00 47.61           C  
ANISOU 4299  CB  SER A 592     5389   6667   6036   -197    -14    -79       C  
ATOM   4300  OG  SER A 592      39.035  46.649  12.669  1.00 46.40           O  
ANISOU 4300  OG  SER A 592     5244   6475   5912   -172     15    -43       O  
ATOM   4301  N   VAL A 593      41.447  46.542  16.470  1.00 46.08           N  
ANISOU 4301  N   VAL A 593     5157   6536   5814   -231    -84   -151       N  
ATOM   4302  CA  VAL A 593      41.674  46.721  17.893  1.00 48.66           C  
ANISOU 4302  CA  VAL A 593     5472   6910   6108   -253   -111   -199       C  
ATOM   4303  C   VAL A 593      42.734  47.800  18.117  1.00 53.34           C  
ANISOU 4303  C   VAL A 593     6015   7484   6766   -255   -112   -248       C  
ATOM   4304  O   VAL A 593      42.574  48.658  18.992  1.00 56.16           O  
ANISOU 4304  O   VAL A 593     6348   7861   7128   -273   -112   -307       O  
ATOM   4305  CB  VAL A 593      42.124  45.411  18.557  1.00 48.41           C  
ANISOU 4305  CB  VAL A 593     5466   6920   6009   -254   -155   -172       C  
ATOM   4306  CG1 VAL A 593      42.328  45.608  20.045  1.00 50.51           C  
ANISOU 4306  CG1 VAL A 593     5719   7239   6232   -274   -185   -222       C  
ATOM   4307  CG2 VAL A 593      41.097  44.326  18.328  1.00 48.77           C  
ANISOU 4307  CG2 VAL A 593     5554   6978   5997   -252   -152   -124       C  
ATOM   4308  N   ALA A 594      43.803  47.765  17.315  1.00 51.61           N  
ANISOU 4308  N   ALA A 594     5782   7227   6599   -238   -111   -226       N  
ATOM   4309  CA  ALA A 594      44.926  48.689  17.500  1.00 53.92           C  
ANISOU 4309  CA  ALA A 594     6026   7499   6960   -239   -113   -271       C  
ATOM   4310  C   ALA A 594      44.466  50.126  17.321  1.00 55.07           C  
ANISOU 4310  C   ALA A 594     6140   7614   7171   -246    -72   -313       C  
ATOM   4311  O   ALA A 594      44.727  50.977  18.173  1.00 55.24           O  
ANISOU 4311  O   ALA A 594     6125   7647   7216   -261    -78   -376       O  
ATOM   4312  CB  ALA A 594      46.063  48.355  16.542  1.00 51.73           C  
ANISOU 4312  CB  ALA A 594     5742   7182   6732   -218   -112   -234       C  
ATOM   4313  N   THR A 595      43.751  50.375  16.224  1.00 55.65           N  
ANISOU 4313  N   THR A 595     6224   7648   7271   -233    -32   -277       N  
ATOM   4314  CA  THR A 595      43.189  51.692  15.926  1.00 57.09           C  
ANISOU 4314  CA  THR A 595     6379   7796   7516   -236     10   -306       C  
ATOM   4315  C   THR A 595      42.265  52.185  17.050  1.00 57.96           C  
ANISOU 4315  C   THR A 595     6483   7944   7594   -260      6   -362       C  
ATOM   4316  O   THR A 595      42.213  53.378  17.357  1.00 60.02           O  
ANISOU 4316  O   THR A 595     6705   8188   7911   -271     25   -415       O  
ATOM   4317  CB  THR A 595      42.391  51.660  14.607  1.00 57.22           C  
ANISOU 4317  CB  THR A 595     6420   7776   7546   -215     47   -251       C  
ATOM   4318  OG1 THR A 595      43.212  51.136  13.557  1.00 59.12           O  
ANISOU 4318  OG1 THR A 595     6668   7986   7808   -191     51   -200       O  
ATOM   4319  CG2 THR A 595      41.920  53.046  14.222  1.00 59.62           C  
ANISOU 4319  CG2 THR A 595     6693   8038   7923   -214     91   -276       C  
ATOM   4320  N   ALA A 596      41.530  51.263  17.656  1.00 57.19           N  
ANISOU 4320  N   ALA A 596     6425   7897   7409   -270    -17   -350       N  
ATOM   4321  CA  ALA A 596      40.555  51.647  18.660  1.00 57.35           C  
ANISOU 4321  CA  ALA A 596     6444   7955   7393   -292    -16   -398       C  
ATOM   4322  C   ALA A 596      41.271  51.910  19.974  1.00 56.97           C  
ANISOU 4322  C   ALA A 596     6368   7947   7329   -310    -49   -460       C  
ATOM   4323  O   ALA A 596      40.959  52.873  20.665  1.00 58.80           O  
ANISOU 4323  O   ALA A 596     6569   8189   7581   -327    -39   -524       O  
ATOM   4324  CB  ALA A 596      39.488  50.571  18.807  1.00 53.10           C  
ANISOU 4324  CB  ALA A 596     5955   7452   6769   -295    -24   -361       C  
ATOM   4325  N   LEU A 597      42.253  51.069  20.286  1.00 57.05           N  
ANISOU 4325  N   LEU A 597     6387   7982   7308   -305    -88   -444       N  
ATOM   4326  CA  LEU A 597      43.026  51.169  21.532  1.00 61.69           C  
ANISOU 4326  CA  LEU A 597     6951   8614   7873   -318   -126   -499       C  
ATOM   4327  C   LEU A 597      44.042  52.316  21.638  1.00 65.20           C  
ANISOU 4327  C   LEU A 597     7338   9031   8405   -320   -124   -559       C  
ATOM   4328  O   LEU A 597      44.358  52.768  22.750  1.00 68.00           O  
ANISOU 4328  O   LEU A 597     7665   9423   8750   -335   -147   -625       O  
ATOM   4329  CB  LEU A 597      43.740  49.847  21.806  1.00 60.14           C  
ANISOU 4329  CB  LEU A 597     6784   8451   7615   -310   -171   -458       C  
ATOM   4330  CG  LEU A 597      43.116  48.931  22.857  1.00 63.59           C  
ANISOU 4330  CG  LEU A 597     7258   8957   7945   -322   -200   -451       C  
ATOM   4331  CD1 LEU A 597      41.607  48.787  22.689  1.00 65.37           C  
ANISOU 4331  CD1 LEU A 597     7515   9188   8134   -329   -169   -430       C  
ATOM   4332  CD2 LEU A 597      43.793  47.575  22.842  1.00 60.37           C  
ANISOU 4332  CD2 LEU A 597     6880   8567   7490   -309   -237   -395       C  
ATOM   4333  N   GLN A 598      44.563  52.774  20.502  1.00 65.54           N  
ANISOU 4333  N   GLN A 598     7361   9008   8534   -305    -95   -536       N  
ATOM   4334  CA  GLN A 598      45.620  53.803  20.481  1.00 66.81           C  
ANISOU 4334  CA  GLN A 598     7463   9132   8788   -304    -89   -585       C  
ATOM   4335  C   GLN A 598      46.746  53.465  21.469  1.00 66.52           C  
ANISOU 4335  C   GLN A 598     7409   9138   8730   -309   -141   -624       C  
ATOM   4336  O   GLN A 598      47.266  52.345  21.446  1.00 62.98           O  
ANISOU 4336  O   GLN A 598     6989   8710   8233   -299   -174   -580       O  
ATOM   4337  CB  GLN A 598      45.027  55.182  20.757  1.00 66.37           C  
ANISOU 4337  CB  GLN A 598     7369   9060   8790   -319    -56   -648       C  
ATOM   4338  CG  GLN A 598      43.855  55.493  19.862  1.00 66.97           C  
ANISOU 4338  CG  GLN A 598     7463   9099   8882   -313     -9   -611       C  
ATOM   4339  CD  GLN A 598      43.156  56.774  20.234  1.00 71.47           C  
ANISOU 4339  CD  GLN A 598     7998   9657   9501   -329     20   -674       C  
ATOM   4340  OE1 GLN A 598      42.572  56.899  21.317  1.00 71.65           O  
ANISOU 4340  OE1 GLN A 598     8019   9730   9476   -349      5   -726       O  
ATOM   4341  NE2 GLN A 598      43.184  57.733  19.321  1.00 74.48           N  
ANISOU 4341  NE2 GLN A 598     8349   9970   9979   -319     64   -667       N  
ATOM   4342  N   SER A 599      47.083  54.414  22.347  1.00 68.80           N  
ANISOU 4342  N   SER A 599     7649   9439   9053   -323   -150   -707       N  
ATOM   4343  CA  SER A 599      48.137  54.234  23.363  1.00 70.74           C  
ANISOU 4343  CA  SER A 599     7870   9727   9280   -327   -202   -755       C  
ATOM   4344  C   SER A 599      48.010  52.941  24.164  1.00 68.75           C  
ANISOU 4344  C   SER A 599     7666   9548   8908   -327   -251   -728       C  
ATOM   4345  O   SER A 599      49.018  52.348  24.541  1.00 70.31           O  
ANISOU 4345  O   SER A 599     7859   9768   9086   -320   -295   -728       O  
ATOM   4346  CB  SER A 599      48.210  55.439  24.314  1.00 74.30           C  
ANISOU 4346  CB  SER A 599     8267  10194   9770   -345   -205   -856       C  
ATOM   4347  OG  SER A 599      46.917  55.835  24.749  1.00 80.60           O  
ANISOU 4347  OG  SER A 599     9077  11017  10531   -360   -184   -880       O  
ATOM   4348  N   GLY A 600      46.779  52.498  24.405  1.00 67.94           N  
ANISOU 4348  N   GLY A 600     7607   9480   8728   -335   -242   -704       N  
ATOM   4349  CA  GLY A 600      46.540  51.235  25.102  1.00 65.71           C  
ANISOU 4349  CA  GLY A 600     7373   9263   8333   -335   -281   -668       C  
ATOM   4350  C   GLY A 600      47.223  50.058  24.431  1.00 64.85           C  
ANISOU 4350  C   GLY A 600     7292   9138   8210   -316   -301   -593       C  
ATOM   4351  O   GLY A 600      47.516  49.044  25.074  1.00 65.55           O  
ANISOU 4351  O   GLY A 600     7407   9276   8224   -313   -345   -570       O  
ATOM   4352  N   PHE A 601      47.483  50.187  23.134  1.00 61.47           N  
ANISOU 4352  N   PHE A 601     6858   8641   7855   -303   -269   -553       N  
ATOM   4353  CA  PHE A 601      48.165  49.131  22.403  1.00 62.89           C  
ANISOU 4353  CA  PHE A 601     7061   8802   8032   -284   -284   -486       C  
ATOM   4354  C   PHE A 601      49.690  49.128  22.597  1.00 66.08           C  
ANISOU 4354  C   PHE A 601     7429   9199   8478   -275   -319   -509       C  
ATOM   4355  O   PHE A 601      50.359  48.162  22.224  1.00 64.07           O  
ANISOU 4355  O   PHE A 601     7192   8939   8213   -261   -342   -460       O  
ATOM   4356  CB  PHE A 601      47.819  49.182  20.914  1.00 60.68           C  
ANISOU 4356  CB  PHE A 601     6794   8458   7806   -271   -236   -431       C  
ATOM   4357  CG  PHE A 601      47.901  47.846  20.247  1.00 61.24           C  
ANISOU 4357  CG  PHE A 601     6907   8524   7838   -255   -247   -354       C  
ATOM   4358  CD1 PHE A 601      46.878  46.909  20.411  1.00 62.59           C  
ANISOU 4358  CD1 PHE A 601     7127   8728   7926   -257   -252   -312       C  
ATOM   4359  CD2 PHE A 601      49.006  47.501  19.480  1.00 59.48           C  
ANISOU 4359  CD2 PHE A 601     6673   8264   7663   -237   -252   -325       C  
ATOM   4360  CE1 PHE A 601      46.957  45.660  19.803  1.00 64.51           C  
ANISOU 4360  CE1 PHE A 601     7407   8966   8140   -243   -262   -244       C  
ATOM   4361  CE2 PHE A 601      49.092  46.258  18.872  1.00 60.28           C  
ANISOU 4361  CE2 PHE A 601     6811   8361   7732   -222   -263   -257       C  
ATOM   4362  CZ  PHE A 601      48.069  45.335  19.033  1.00 62.84           C  
ANISOU 4362  CZ  PHE A 601     7182   8717   7976   -225   -268   -217       C  
ATOM   4363  N   LEU A 602      50.234  50.189  23.198  1.00 69.09           N  
ANISOU 4363  N   LEU A 602     7758   9582   8910   -285   -326   -587       N  
ATOM   4364  CA  LEU A 602      51.692  50.307  23.390  1.00 67.78           C  
ANISOU 4364  CA  LEU A 602     7550   9406   8795   -277   -358   -619       C  
ATOM   4365  C   LEU A 602      52.369  49.023  23.864  1.00 65.59           C  
ANISOU 4365  C   LEU A 602     7298   9171   8451   -267   -415   -585       C  
ATOM   4366  O   LEU A 602      53.348  48.598  23.259  1.00 62.80           O  
ANISOU 4366  O   LEU A 602     6936   8785   8140   -252   -425   -557       O  
ATOM   4367  CB  LEU A 602      52.056  51.459  24.336  1.00 73.57           C  
ANISOU 4367  CB  LEU A 602     8229  10158   9567   -290   -370   -717       C  
ATOM   4368  CG  LEU A 602      52.759  52.719  23.815  1.00 76.22           C  
ANISOU 4368  CG  LEU A 602     8501  10429  10031   -291   -339   -766       C  
ATOM   4369  CD1 LEU A 602      53.828  52.368  22.786  1.00 78.00           C  
ANISOU 4369  CD1 LEU A 602     8716  10597  10323   -273   -332   -721       C  
ATOM   4370  CD2 LEU A 602      51.776  53.722  23.240  1.00 77.57           C  
ANISOU 4370  CD2 LEU A 602     8664  10557  10252   -300   -277   -774       C  
ATOM   4371  N   PRO A 603      51.841  48.383  24.928  1.00 64.70           N  
ANISOU 4371  N   PRO A 603     7218   9132   8235   -273   -450   -585       N  
ATOM   4372  CA  PRO A 603      52.559  47.222  25.457  1.00 62.66           C  
ANISOU 4372  CA  PRO A 603     6979   8913   7916   -262   -507   -556       C  
ATOM   4373  C   PRO A 603      52.615  46.046  24.495  1.00 62.14           C  
ANISOU 4373  C   PRO A 603     6952   8817   7841   -247   -502   -466       C  
ATOM   4374  O   PRO A 603      53.271  45.046  24.788  1.00 63.48           O  
ANISOU 4374  O   PRO A 603     7136   9010   7974   -235   -546   -435       O  
ATOM   4375  CB  PRO A 603      51.748  46.844  26.711  1.00 65.30           C  
ANISOU 4375  CB  PRO A 603     7343   9328   8138   -273   -534   -567       C  
ATOM   4376  CG  PRO A 603      50.994  48.085  27.081  1.00 63.72           C  
ANISOU 4376  CG  PRO A 603     7120   9134   7957   -291   -502   -635       C  
ATOM   4377  CD  PRO A 603      50.672  48.729  25.762  1.00 65.46           C  
ANISOU 4377  CD  PRO A 603     7329   9276   8267   -291   -442   -617       C  
ATOM   4378  N   TYR A 604      51.950  46.168  23.352  1.00 61.37           N  
ANISOU 4378  N   TYR A 604     6870   8668   7778   -245   -449   -426       N  
ATOM   4379  CA  TYR A 604      51.775  45.031  22.448  1.00 61.06           C  
ANISOU 4379  CA  TYR A 604     6872   8606   7721   -232   -441   -344       C  
ATOM   4380  C   TYR A 604      52.382  45.240  21.058  1.00 58.84           C  
ANISOU 4380  C   TYR A 604     6574   8252   7531   -217   -407   -318       C  
ATOM   4381  O   TYR A 604      52.584  44.277  20.323  1.00 58.45           O  
ANISOU 4381  O   TYR A 604     6548   8182   7476   -203   -408   -258       O  
ATOM   4382  CB  TYR A 604      50.273  44.682  22.331  1.00 60.38           C  
ANISOU 4382  CB  TYR A 604     6833   8536   7574   -239   -413   -307       C  
ATOM   4383  CG  TYR A 604      49.624  44.450  23.676  1.00 62.77           C  
ANISOU 4383  CG  TYR A 604     7155   8910   7784   -253   -440   -328       C  
ATOM   4384  CD1 TYR A 604      49.802  43.242  24.360  1.00 63.77           C  
ANISOU 4384  CD1 TYR A 604     7313   9084   7834   -248   -485   -291       C  
ATOM   4385  CD2 TYR A 604      48.861  45.448  24.289  1.00 61.75           C  
ANISOU 4385  CD2 TYR A 604     7013   8803   7646   -271   -421   -385       C  
ATOM   4386  CE1 TYR A 604      49.229  43.027  25.609  1.00 62.14           C  
ANISOU 4386  CE1 TYR A 604     7125   8945   7539   -260   -508   -307       C  
ATOM   4387  CE2 TYR A 604      48.287  45.241  25.540  1.00 63.27           C  
ANISOU 4387  CE2 TYR A 604     7223   9066   7752   -283   -445   -406       C  
ATOM   4388  CZ  TYR A 604      48.477  44.029  26.191  1.00 62.92           C  
ANISOU 4388  CZ  TYR A 604     7211   9068   7627   -277   -487   -365       C  
ATOM   4389  OH  TYR A 604      47.917  43.812  27.425  1.00 62.94           O  
ANISOU 4389  OH  TYR A 604     7233   9141   7540   -288   -508   -381       O  
ATOM   4390  N   CYS A 605      52.668  46.491  20.710  1.00 58.76           N  
ANISOU 4390  N   CYS A 605     6520   8202   7605   -221   -375   -364       N  
ATOM   4391  CA  CYS A 605      53.006  46.851  19.335  1.00 61.71           C  
ANISOU 4391  CA  CYS A 605     6880   8506   8063   -208   -329   -338       C  
ATOM   4392  C   CYS A 605      54.276  46.199  18.777  1.00 64.10           C  
ANISOU 4392  C   CYS A 605     7171   8780   8405   -191   -347   -309       C  
ATOM   4393  O   CYS A 605      54.245  45.666  17.665  1.00 64.36           O  
ANISOU 4393  O   CYS A 605     7225   8777   8452   -177   -322   -252       O  
ATOM   4394  CB  CYS A 605      53.025  48.372  19.130  1.00 63.12           C  
ANISOU 4394  CB  CYS A 605     7011   8645   8326   -216   -289   -392       C  
ATOM   4395  SG  CYS A 605      54.004  49.312  20.324  1.00 69.07           S  
ANISOU 4395  SG  CYS A 605     7703   9419   9123   -228   -323   -488       S  
ATOM   4396  N   GLU A 606      55.368  46.212  19.539  1.00 66.42           N  
ANISOU 4396  N   GLU A 606     7431   9091   8713   -192   -391   -350       N  
ATOM   4397  CA  GLU A 606      56.675  45.819  18.983  1.00 68.73           C  
ANISOU 4397  CA  GLU A 606     7702   9348   9063   -177   -403   -334       C  
ATOM   4398  C   GLU A 606      56.643  44.500  18.195  1.00 62.85           C  
ANISOU 4398  C   GLU A 606     7000   8595   8287   -161   -406   -256       C  
ATOM   4399  O   GLU A 606      56.890  44.509  16.983  1.00 59.25           O  
ANISOU 4399  O   GLU A 606     6542   8087   7885   -149   -367   -222       O  
ATOM   4400  CB  GLU A 606      57.801  45.832  20.037  1.00 75.99           C  
ANISOU 4400  CB  GLU A 606     8583  10297   9991   -178   -461   -388       C  
ATOM   4401  CG  GLU A 606      59.153  45.389  19.480  1.00 87.07           C  
ANISOU 4401  CG  GLU A 606     9963  11664  11457   -163   -475   -373       C  
ATOM   4402  CD  GLU A 606      60.315  45.570  20.450  1.00 96.49           C  
ANISOU 4402  CD  GLU A 606    11110  12879  12672   -163   -529   -433       C  
ATOM   4403  OE1 GLU A 606      60.244  45.060  21.592  1.00 98.88           O  
ANISOU 4403  OE1 GLU A 606    11427  13246  12898   -166   -585   -448       O  
ATOM   4404  OE2 GLU A 606      61.315  46.213  20.056  1.00 97.46           O  
ANISOU 4404  OE2 GLU A 606    11182  12955  12892   -159   -516   -466       O  
ATOM   4405  N   PRO A 607      56.326  43.372  18.861  1.00 60.25           N  
ANISOU 4405  N   PRO A 607     6709   8315   7869   -161   -449   -227       N  
ATOM   4406  CA  PRO A 607      56.329  42.115  18.100  1.00 58.48           C  
ANISOU 4406  CA  PRO A 607     6520   8078   7622   -146   -450   -156       C  
ATOM   4407  C   PRO A 607      55.373  42.140  16.902  1.00 59.61           C  
ANISOU 4407  C   PRO A 607     6691   8186   7771   -141   -394   -113       C  
ATOM   4408  O   PRO A 607      55.694  41.594  15.845  1.00 64.27           O  
ANISOU 4408  O   PRO A 607     7289   8740   8390   -126   -376    -69       O  
ATOM   4409  CB  PRO A 607      55.886  41.063  19.125  1.00 57.35           C  
ANISOU 4409  CB  PRO A 607     6414   7996   7381   -150   -499   -134       C  
ATOM   4410  CG  PRO A 607      55.281  41.818  20.252  1.00 57.92           C  
ANISOU 4410  CG  PRO A 607     6480   8114   7413   -167   -509   -186       C  
ATOM   4411  CD  PRO A 607      55.918  43.179  20.264  1.00 59.61           C  
ANISOU 4411  CD  PRO A 607     6639   8302   7706   -173   -493   -253       C  
ATOM   4412  N   VAL A 608      54.223  42.787  17.068  1.00 57.72           N  
ANISOU 4412  N   VAL A 608     6465   7960   7507   -153   -367   -127       N  
ATOM   4413  CA  VAL A 608      53.228  42.901  16.005  1.00 58.27           C  
ANISOU 4413  CA  VAL A 608     6560   8001   7580   -148   -315    -91       C  
ATOM   4414  C   VAL A 608      53.826  43.643  14.814  1.00 55.40           C  
ANISOU 4414  C   VAL A 608     6167   7576   7307   -136   -270    -90       C  
ATOM   4415  O   VAL A 608      53.753  43.171  13.664  1.00 52.99           O  
ANISOU 4415  O   VAL A 608     5880   7240   7013   -119   -244    -42       O  
ATOM   4416  CB  VAL A 608      51.946  43.629  16.497  1.00 57.37           C  
ANISOU 4416  CB  VAL A 608     6456   7910   7431   -164   -295   -117       C  
ATOM   4417  CG1 VAL A 608      50.992  43.883  15.344  1.00 54.62           C  
ANISOU 4417  CG1 VAL A 608     6127   7528   7097   -157   -242    -85       C  
ATOM   4418  CG2 VAL A 608      51.260  42.833  17.601  1.00 55.81           C  
ANISOU 4418  CG2 VAL A 608     6292   7774   7141   -176   -333   -111       C  
ATOM   4419  N   TYR A 609      54.422  44.801  15.106  1.00 54.82           N  
ANISOU 4419  N   TYR A 609     6048   7485   7297   -143   -261   -143       N  
ATOM   4420  CA  TYR A 609      55.161  45.580  14.112  1.00 53.60           C  
ANISOU 4420  CA  TYR A 609     5858   7271   7237   -132   -218   -146       C  
ATOM   4421  C   TYR A 609      56.232  44.741  13.397  1.00 53.57           C  
ANISOU 4421  C   TYR A 609     5852   7242   7261   -114   -227   -110       C  
ATOM   4422  O   TYR A 609      56.277  44.699  12.159  1.00 53.75           O  
ANISOU 4422  O   TYR A 609     5882   7224   7317    -98   -185    -71       O  
ATOM   4423  CB  TYR A 609      55.787  46.825  14.740  1.00 53.23           C  
ANISOU 4423  CB  TYR A 609     5756   7212   7257   -145   -217   -215       C  
ATOM   4424  CG  TYR A 609      56.459  47.700  13.706  1.00 54.16           C  
ANISOU 4424  CG  TYR A 609     5837   7264   7476   -134   -165   -216       C  
ATOM   4425  CD1 TYR A 609      55.787  48.785  13.155  1.00 51.57           C  
ANISOU 4425  CD1 TYR A 609     5501   6904   7191   -136   -110   -220       C  
ATOM   4426  CD2 TYR A 609      57.763  47.418  13.249  1.00 52.83           C  
ANISOU 4426  CD2 TYR A 609     5643   7064   7365   -123   -169   -208       C  
ATOM   4427  CE1 TYR A 609      56.385  49.579  12.191  1.00 54.35           C  
ANISOU 4427  CE1 TYR A 609     5820   7194   7636   -125    -60   -214       C  
ATOM   4428  CE2 TYR A 609      58.372  48.202  12.279  1.00 51.64           C  
ANISOU 4428  CE2 TYR A 609     5459   6852   7309   -113   -117   -205       C  
ATOM   4429  CZ  TYR A 609      57.685  49.279  11.752  1.00 54.13           C  
ANISOU 4429  CZ  TYR A 609     5767   7136   7662   -114    -62   -206       C  
ATOM   4430  OH  TYR A 609      58.268  50.078  10.791  1.00 54.95           O  
ANISOU 4430  OH  TYR A 609     5839   7178   7860   -103     -7   -198       O  
ATOM   4431  N   GLN A 610      57.069  44.057  14.169  1.00 53.49           N  
ANISOU 4431  N   GLN A 610     5833   7257   7234   -116   -280   -123       N  
ATOM   4432  CA  GLN A 610      58.159  43.300  13.569  1.00 58.93           C  
ANISOU 4432  CA  GLN A 610     6513   7921   7956   -100   -291    -96       C  
ATOM   4433  C   GLN A 610      57.640  42.246  12.617  1.00 56.58           C  
ANISOU 4433  C   GLN A 610     6260   7617   7620    -85   -276    -29       C  
ATOM   4434  O   GLN A 610      58.099  42.165  11.468  1.00 53.84           O  
ANISOU 4434  O   GLN A 610     5908   7228   7320    -70   -243     -1       O  
ATOM   4435  CB  GLN A 610      59.088  42.681  14.619  1.00 66.48           C  
ANISOU 4435  CB  GLN A 610     7454   8909   8897   -103   -356   -119       C  
ATOM   4436  CG  GLN A 610      60.449  43.366  14.698  1.00 76.32           C  
ANISOU 4436  CG  GLN A 610     8641  10124  10232   -102   -361   -165       C  
ATOM   4437  CD  GLN A 610      60.615  44.250  15.926  1.00 83.26           C  
ANISOU 4437  CD  GLN A 610     9485  11031  11118   -119   -389   -237       C  
ATOM   4438  OE1 GLN A 610      60.669  43.757  17.060  1.00 87.97           O  
ANISOU 4438  OE1 GLN A 610    10089  11680  11656   -124   -446   -255       O  
ATOM   4439  NE2 GLN A 610      60.724  45.561  15.706  1.00 84.24           N  
ANISOU 4439  NE2 GLN A 610     9570  11120  11317   -125   -348   -279       N  
ATOM   4440  N   ARG A 611      56.665  41.462  13.082  1.00 55.19           N  
ANISOU 4440  N   ARG A 611     6127   7483   7360    -90   -300     -6       N  
ATOM   4441  CA  ARG A 611      56.158  40.339  12.294  1.00 52.58           C  
ANISOU 4441  CA  ARG A 611     5837   7151   6991    -77   -293     53       C  
ATOM   4442  C   ARG A 611      55.552  40.828  10.980  1.00 51.23           C  
ANISOU 4442  C   ARG A 611     5677   6944   6846    -65   -232     77       C  
ATOM   4443  O   ARG A 611      55.740  40.193   9.931  1.00 50.91           O  
ANISOU 4443  O   ARG A 611     5648   6879   6816    -47   -215    116       O  
ATOM   4444  CB  ARG A 611      55.145  39.510  13.086  1.00 53.92           C  
ANISOU 4444  CB  ARG A 611     6047   7369   7070    -86   -325     70       C  
ATOM   4445  CG  ARG A 611      54.680  38.269  12.348  1.00 53.47           C  
ANISOU 4445  CG  ARG A 611     6028   7309   6978    -73   -323    126       C  
ATOM   4446  CD  ARG A 611      53.967  37.296  13.261  1.00 55.37           C  
ANISOU 4446  CD  ARG A 611     6302   7596   7139    -82   -362    144       C  
ATOM   4447  NE  ARG A 611      53.676  36.040  12.568  1.00 56.62           N  
ANISOU 4447  NE  ARG A 611     6490   7747   7276    -69   -363    195       N  
ATOM   4448  CZ  ARG A 611      52.934  35.054  13.063  1.00 55.46           C  
ANISOU 4448  CZ  ARG A 611     6376   7631   7068    -73   -385    223       C  
ATOM   4449  NH1 ARG A 611      52.377  35.155  14.263  1.00 58.70           N  
ANISOU 4449  NH1 ARG A 611     6797   8083   7425    -91   -408    208       N  
ATOM   4450  NH2 ARG A 611      52.749  33.959  12.351  1.00 57.99           N  
ANISOU 4450  NH2 ARG A 611     6716   7937   7380    -61   -384    265       N  
ATOM   4451  N   CYS A 612      54.862  41.967  11.031  1.00 47.14           N  
ANISOU 4451  N   CYS A 612     5151   6420   6340    -74   -200     52       N  
ATOM   4452  CA  CYS A 612      54.194  42.483   9.845  1.00 48.81           C  
ANISOU 4452  CA  CYS A 612     5373   6600   6571    -61   -144     77       C  
ATOM   4453  C   CYS A 612      55.173  42.892   8.771  1.00 49.39           C  
ANISOU 4453  C   CYS A 612     5420   6624   6722    -44   -106     87       C  
ATOM   4454  O   CYS A 612      55.037  42.490   7.601  1.00 45.80           O  
ANISOU 4454  O   CYS A 612     4984   6149   6268    -25    -77    129       O  
ATOM   4455  CB  CYS A 612      53.298  43.665  10.191  1.00 53.18           C  
ANISOU 4455  CB  CYS A 612     5920   7158   7128    -75   -119     46       C  
ATOM   4456  SG  CYS A 612      51.769  43.169  10.999  1.00 58.35           S  
ANISOU 4456  SG  CYS A 612     6618   7865   7688    -89   -141     49       S  
ATOM   4457  N   VAL A 613      56.149  43.716   9.167  1.00 50.11           N  
ANISOU 4457  N   VAL A 613     5466   6696   6879    -52   -106     47       N  
ATOM   4458  CA  VAL A 613      57.222  44.120   8.254  1.00 48.83           C  
ANISOU 4458  CA  VAL A 613     5271   6483   6797    -38    -70     53       C  
ATOM   4459  C   VAL A 613      57.847  42.865   7.661  1.00 47.49           C  
ANISOU 4459  C   VAL A 613     5117   6311   6616    -22    -86     91       C  
ATOM   4460  O   VAL A 613      57.997  42.724   6.425  1.00 44.12           O  
ANISOU 4460  O   VAL A 613     4697   5854   6211     -2    -46    127       O  
ATOM   4461  CB  VAL A 613      58.290  44.987   8.961  1.00 50.12           C  
ANISOU 4461  CB  VAL A 613     5380   6630   7033    -50    -79     -2       C  
ATOM   4462  CG1 VAL A 613      59.391  45.361   7.988  1.00 46.67           C  
ANISOU 4462  CG1 VAL A 613     4910   6139   6683    -36    -39      7       C  
ATOM   4463  CG2 VAL A 613      57.650  46.249   9.541  1.00 49.90           C  
ANISOU 4463  CG2 VAL A 613     5334   6604   7021    -67    -62    -44       C  
ATOM   4464  N   ASN A 614      58.150  41.928   8.544  1.00 49.26           N  
ANISOU 4464  N   ASN A 614     5348   6569   6801    -29   -144     84       N  
ATOM   4465  CA  ASN A 614      58.759  40.686   8.114  1.00 54.80           C  
ANISOU 4465  CA  ASN A 614     6061   7268   7493    -16   -165    116       C  
ATOM   4466  C   ASN A 614      57.934  39.926   7.071  1.00 55.76           C  
ANISOU 4466  C   ASN A 614     6225   7390   7572      1   -142    167       C  
ATOM   4467  O   ASN A 614      58.497  39.445   6.073  1.00 54.63           O  
ANISOU 4467  O   ASN A 614     6081   7222   7455     19   -122    193       O  
ATOM   4468  CB  ASN A 614      59.095  39.791   9.301  1.00 59.80           C  
ANISOU 4468  CB  ASN A 614     6697   7939   8085    -26   -233    104       C  
ATOM   4469  CG  ASN A 614      60.304  38.922   9.022  1.00 68.39           C  
ANISOU 4469  CG  ASN A 614     7770   9011   9206    -15   -255    117       C  
ATOM   4470  OD1 ASN A 614      61.431  39.414   8.989  1.00 76.30           O  
ANISOU 4470  OD1 ASN A 614     8729   9984  10277    -13   -251     90       O  
ATOM   4471  ND2 ASN A 614      60.077  37.634   8.789  1.00 67.19           N  
ANISOU 4471  ND2 ASN A 614     7648   8872   9009     -6   -277    155       N  
ATOM   4472  N   LEU A 615      56.613  39.841   7.292  1.00 52.55           N  
ANISOU 4472  N   LEU A 615     5852   7011   7102     -5   -143    177       N  
ATOM   4473  CA  LEU A 615      55.719  39.162   6.358  1.00 49.86           C  
ANISOU 4473  CA  LEU A 615     5551   6675   6720     11   -123    219       C  
ATOM   4474  C   LEU A 615      55.719  39.843   4.998  1.00 48.85           C  
ANISOU 4474  C   LEU A 615     5417   6509   6633     31    -63    236       C  
ATOM   4475  O   LEU A 615      55.653  39.183   3.956  1.00 47.81           O  
ANISOU 4475  O   LEU A 615     5304   6369   6492     51    -45    270       O  
ATOM   4476  CB  LEU A 615      54.286  39.121   6.894  1.00 52.33           C  
ANISOU 4476  CB  LEU A 615     5896   7022   6967     -1   -133    219       C  
ATOM   4477  CG  LEU A 615      53.881  38.020   7.873  1.00 55.20           C  
ANISOU 4477  CG  LEU A 615     6283   7425   7266    -13   -185    225       C  
ATOM   4478  CD1 LEU A 615      52.545  38.378   8.509  1.00 53.48           C  
ANISOU 4478  CD1 LEU A 615     6086   7236   6996    -28   -184    214       C  
ATOM   4479  CD2 LEU A 615      53.793  36.666   7.186  1.00 54.61           C  
ANISOU 4479  CD2 LEU A 615     6233   7350   7166      3   -194    265       C  
ATOM   4480  N   VAL A 616      55.752  41.170   5.015  1.00 48.29           N  
ANISOU 4480  N   VAL A 616     5323   6419   6607     25    -30    214       N  
ATOM   4481  CA  VAL A 616      55.864  41.939   3.781  1.00 50.47           C  
ANISOU 4481  CA  VAL A 616     5591   6658   6929     45     31    233       C  
ATOM   4482  C   VAL A 616      57.193  41.618   3.090  1.00 51.24           C  
ANISOU 4482  C   VAL A 616     5665   6724   7079     59     44    244       C  
ATOM   4483  O   VAL A 616      57.236  41.400   1.878  1.00 51.03           O  
ANISOU 4483  O   VAL A 616     5650   6681   7058     83     80    278       O  
ATOM   4484  CB  VAL A 616      55.731  43.461   4.036  1.00 47.99           C  
ANISOU 4484  CB  VAL A 616     5248   6322   6662     35     64    205       C  
ATOM   4485  CG1 VAL A 616      55.949  44.246   2.749  1.00 46.19           C  
ANISOU 4485  CG1 VAL A 616     5010   6053   6488     57    129    230       C  
ATOM   4486  CG2 VAL A 616      54.374  43.780   4.643  1.00 48.03           C  
ANISOU 4486  CG2 VAL A 616     5276   6356   6616     21     55    193       C  
ATOM   4487  N   GLN A 617      58.264  41.570   3.877  1.00 53.32           N  
ANISOU 4487  N   GLN A 617     5896   6982   7380     46     13    214       N  
ATOM   4488  CA  GLN A 617      59.599  41.296   3.349  1.00 55.78           C  
ANISOU 4488  CA  GLN A 617     6180   7263   7749     57     22    218       C  
ATOM   4489  C   GLN A 617      59.656  39.939   2.658  1.00 53.53           C  
ANISOU 4489  C   GLN A 617     5922   6988   7428     74     10    254       C  
ATOM   4490  O   GLN A 617      60.050  39.832   1.488  1.00 52.67           O  
ANISOU 4490  O   GLN A 617     5814   6855   7345     95     50    279       O  
ATOM   4491  CB  GLN A 617      60.634  41.358   4.477  1.00 58.42           C  
ANISOU 4491  CB  GLN A 617     6477   7598   8122     39    -21    175       C  
ATOM   4492  CG  GLN A 617      62.065  41.611   4.015  1.00 62.48           C  
ANISOU 4492  CG  GLN A 617     6947   8070   8721     46      0    166       C  
ATOM   4493  CD  GLN A 617      62.996  41.862   5.185  1.00 61.80           C  
ANISOU 4493  CD  GLN A 617     6820   7984   8677     28    -43    116       C  
ATOM   4494  OE1 GLN A 617      63.393  40.931   5.879  1.00 60.53           O  
ANISOU 4494  OE1 GLN A 617     6661   7848   8490     23   -100    108       O  
ATOM   4495  NE2 GLN A 617      63.340  43.131   5.416  1.00 63.29           N  
ANISOU 4495  NE2 GLN A 617     6969   8147   8931     19    -16     80       N  
ATOM   4496  N   LYS A 618      59.244  38.902   3.371  1.00 52.08           N  
ANISOU 4496  N   LYS A 618     5763   6841   7186     66    -43    256       N  
ATOM   4497  CA  LYS A 618      59.339  37.566   2.803  1.00 55.29           C  
ANISOU 4497  CA  LYS A 618     6190   7254   7565     80    -59    285       C  
ATOM   4498  C   LYS A 618      58.415  37.354   1.586  1.00 55.08           C  
ANISOU 4498  C   LYS A 618     6197   7228   7503    102    -20    320       C  
ATOM   4499  O   LYS A 618      58.763  36.617   0.662  1.00 59.92           O  
ANISOU 4499  O   LYS A 618     6816   7832   8120    121     -8    342       O  
ATOM   4500  CB  LYS A 618      59.215  36.476   3.876  1.00 54.65           C  
ANISOU 4500  CB  LYS A 618     6122   7205   7436     67   -124    282       C  
ATOM   4501  CG  LYS A 618      57.855  36.355   4.524  1.00 64.49           C  
ANISOU 4501  CG  LYS A 618     7402   8489   8613     55   -144    285       C  
ATOM   4502  CD  LYS A 618      57.691  35.021   5.252  1.00 66.69           C  
ANISOU 4502  CD  LYS A 618     7700   8796   8843     49   -199    297       C  
ATOM   4503  CE  LYS A 618      58.419  35.007   6.589  1.00 63.12           C  
ANISOU 4503  CE  LYS A 618     7225   8358   8398     31   -249    270       C  
ATOM   4504  NZ  LYS A 618      58.152  33.701   7.237  1.00 66.05           N  
ANISOU 4504  NZ  LYS A 618     7620   8758   8719     28   -299    290       N  
ATOM   4505  N   THR A 619      57.266  38.029   1.565  1.00 52.61           N  
ANISOU 4505  N   THR A 619     5904   6928   7159     99      0    322       N  
ATOM   4506  CA  THR A 619      56.385  38.005   0.402  1.00 50.73           C  
ANISOU 4506  CA  THR A 619     5694   6691   6891    122     38    352       C  
ATOM   4507  C   THR A 619      57.074  38.591  -0.827  1.00 48.47           C  
ANISOU 4507  C   THR A 619     5392   6370   6655    144     95    368       C  
ATOM   4508  O   THR A 619      57.095  37.968  -1.897  1.00 51.79           O  
ANISOU 4508  O   THR A 619     5827   6790   7063    168    114    393       O  
ATOM   4509  CB  THR A 619      55.039  38.734   0.680  1.00 49.58           C  
ANISOU 4509  CB  THR A 619     5568   6562   6707    114     48    348       C  
ATOM   4510  OG1 THR A 619      54.382  38.101   1.779  1.00 48.36           O  
ANISOU 4510  OG1 THR A 619     5431   6441   6504     94     -2    336       O  
ATOM   4511  CG2 THR A 619      54.127  38.663  -0.523  1.00 46.32           C  
ANISOU 4511  CG2 THR A 619     5184   6153   6263    140     83    378       C  
ATOM   4512  N   LEU A 620      57.614  39.795  -0.676  1.00 47.73           N  
ANISOU 4512  N   LEU A 620     5268   6250   6619    138    124    352       N  
ATOM   4513  CA  LEU A 620      58.410  40.423  -1.733  1.00 51.51           C  
ANISOU 4513  CA  LEU A 620     5726   6692   7156    157    181    367       C  
ATOM   4514  C   LEU A 620      59.551  39.524  -2.202  1.00 51.59           C  
ANISOU 4514  C   LEU A 620     5723   6689   7191    167    176    374       C  
ATOM   4515  O   LEU A 620      59.791  39.380  -3.416  1.00 50.65           O  
ANISOU 4515  O   LEU A 620     5608   6557   7078    193    217    401       O  
ATOM   4516  CB  LEU A 620      58.945  41.773  -1.272  1.00 51.03           C  
ANISOU 4516  CB  LEU A 620     5626   6600   7164    143    206    343       C  
ATOM   4517  CG  LEU A 620      57.800  42.774  -1.058  1.00 55.08           C  
ANISOU 4517  CG  LEU A 620     6150   7120   7660    137    223    340       C  
ATOM   4518  CD1 LEU A 620      58.319  44.106  -0.524  1.00 54.13           C  
ANISOU 4518  CD1 LEU A 620     5987   6967   7613    121    245    311       C  
ATOM   4519  CD2 LEU A 620      57.009  42.978  -2.347  1.00 51.71           C  
ANISOU 4519  CD2 LEU A 620     5752   6692   7205    166    271    382       C  
ATOM   4520  N   ALA A 621      60.226  38.894  -1.242  1.00 49.36           N  
ANISOU 4520  N   ALA A 621     5423   6412   6919    149    124    350       N  
ATOM   4521  CA  ALA A 621      61.302  37.961  -1.574  1.00 53.34           C  
ANISOU 4521  CA  ALA A 621     5913   6904   7449    158    113    353       C  
ATOM   4522  C   ALA A 621      60.771  36.821  -2.437  1.00 53.65           C  
ANISOU 4522  C   ALA A 621     5986   6962   7434    178    111    382       C  
ATOM   4523  O   ALA A 621      61.254  36.600  -3.563  1.00 52.73           O  
ANISOU 4523  O   ALA A 621     5868   6831   7336    201    148    400       O  
ATOM   4524  CB  ALA A 621      61.974  37.420  -0.311  1.00 51.76           C  
ANISOU 4524  CB  ALA A 621     5693   6713   7262    136     50    324       C  
ATOM   4525  N   GLN A 622      59.748  36.134  -1.924  1.00 53.74           N  
ANISOU 4525  N   GLN A 622     6029   7009   7382    171     71    384       N  
ATOM   4526  CA  GLN A 622      59.168  34.999  -2.622  1.00 54.12           C  
ANISOU 4526  CA  GLN A 622     6108   7076   7381    189     63    406       C  
ATOM   4527  C   GLN A 622      58.739  35.369  -4.034  1.00 50.74           C  
ANISOU 4527  C   GLN A 622     5694   6643   6940    217    120    430       C  
ATOM   4528  O   GLN A 622      58.969  34.595  -4.962  1.00 51.13           O  
ANISOU 4528  O   GLN A 622     5751   6693   6982    238    132    443       O  
ATOM   4529  CB  GLN A 622      58.026  34.382  -1.821  1.00 62.59           C  
ANISOU 4529  CB  GLN A 622     7209   8182   8390    175     18    404       C  
ATOM   4530  CG  GLN A 622      58.493  33.595  -0.596  1.00 73.07           C  
ANISOU 4530  CG  GLN A 622     8526   9519   9718    153    -43    390       C  
ATOM   4531  CD  GLN A 622      57.442  33.474   0.520  1.00 85.40           C  
ANISOU 4531  CD  GLN A 622    10109  11112  11227    133    -82    384       C  
ATOM   4532  OE1 GLN A 622      56.268  33.841   0.355  1.00 84.33           O  
ANISOU 4532  OE1 GLN A 622     9998  10992  11052    134    -66    389       O  
ATOM   4533  NE2 GLN A 622      57.874  32.956   1.675  1.00 88.18           N  
ANISOU 4533  NE2 GLN A 622    10452  11475  11579    115   -132    372       N  
ATOM   4534  N   ALA A 623      58.165  36.561  -4.207  1.00 47.17           N  
ANISOU 4534  N   ALA A 623     5247   6188   6489    219    157    434       N  
ATOM   4535  CA  ALA A 623      57.740  37.003  -5.532  1.00 48.91           C  
ANISOU 4535  CA  ALA A 623     5483   6405   6695    249    212    461       C  
ATOM   4536  C   ALA A 623      58.915  37.150  -6.494  1.00 53.21           C  
ANISOU 4536  C   ALA A 623     6006   6922   7291    268    257    472       C  
ATOM   4537  O   ALA A 623      58.835  36.715  -7.647  1.00 55.81           O  
ANISOU 4537  O   ALA A 623     6349   7258   7597    296    284    493       O  
ATOM   4538  CB  ALA A 623      56.938  38.292  -5.460  1.00 45.13           C  
ANISOU 4538  CB  ALA A 623     5009   5924   6213    247    241    465       C  
ATOM   4539  N   MET A 624      60.004  37.763  -6.025  1.00 55.44           N  
ANISOU 4539  N   MET A 624     6250   7172   7641    253    266    457       N  
ATOM   4540  CA  MET A 624      61.208  37.905  -6.849  1.00 54.00           C  
ANISOU 4540  CA  MET A 624     6043   6960   7516    269    310    466       C  
ATOM   4541  C   MET A 624      61.753  36.535  -7.232  1.00 49.91           C  
ANISOU 4541  C   MET A 624     5527   6450   6988    278    287    465       C  
ATOM   4542  O   MET A 624      62.105  36.300  -8.388  1.00 52.20           O  
ANISOU 4542  O   MET A 624     5819   6734   7279    304    327    484       O  
ATOM   4543  CB  MET A 624      62.274  38.721  -6.118  1.00 54.82           C  
ANISOU 4543  CB  MET A 624     6102   7028   7700    247    315    442       C  
ATOM   4544  CG  MET A 624      62.051  40.224  -6.174  1.00 59.49           C  
ANISOU 4544  CG  MET A 624     6682   7597   8325    246    363    448       C  
ATOM   4545  SD  MET A 624      63.141  41.077  -5.009  1.00 63.38           S  
ANISOU 4545  SD  MET A 624     7120   8052   8908    215    352    406       S  
ATOM   4546  CE  MET A 624      62.807  42.787  -5.403  1.00 62.51           C  
ANISOU 4546  CE  MET A 624     6998   7912   8841    220    421    420       C  
ATOM   4547  N   LEU A 625      61.798  35.635  -6.257  1.00 48.43           N  
ANISOU 4547  N   LEU A 625     5339   6276   6788    259    224    445       N  
ATOM   4548  CA  LEU A 625      62.291  34.281  -6.485  1.00 53.31           C  
ANISOU 4548  CA  LEU A 625     5956   6900   7402    265    195    443       C  
ATOM   4549  C   LEU A 625      61.462  33.548  -7.542  1.00 57.50           C  
ANISOU 4549  C   LEU A 625     6520   7455   7872    292    208    462       C  
ATOM   4550  O   LEU A 625      62.013  32.892  -8.439  1.00 59.44           O  
ANISOU 4550  O   LEU A 625     6762   7697   8127    312    226    468       O  
ATOM   4551  CB  LEU A 625      62.281  33.492  -5.181  1.00 53.73           C  
ANISOU 4551  CB  LEU A 625     6006   6965   7445    240    124    423       C  
ATOM   4552  CG  LEU A 625      63.491  32.613  -4.855  1.00 58.62           C  
ANISOU 4552  CG  LEU A 625     6596   7567   8108    234     91    409       C  
ATOM   4553  CD1 LEU A 625      63.105  31.509  -3.876  1.00 54.72           C  
ANISOU 4553  CD1 LEU A 625     6115   7097   7580    219     22    403       C  
ATOM   4554  CD2 LEU A 625      64.155  32.035  -6.101  1.00 57.98           C  
ANISOU 4554  CD2 LEU A 625     6509   7474   8049    259    126    419       C  
ATOM   4555  N   ASN A 626      60.137  33.660  -7.427  1.00 58.09           N  
ANISOU 4555  N   ASN A 626     6627   7558   7888    292    198    469       N  
ATOM   4556  CA  ASN A 626      59.234  33.093  -8.415  1.00 56.43           C  
ANISOU 4556  CA  ASN A 626     6447   7373   7620    319    209    484       C  
ATOM   4557  C   ASN A 626      59.405  33.761  -9.772  1.00 60.01           C  
ANISOU 4557  C   ASN A 626     6903   7820   8077    350    276    505       C  
ATOM   4558  O   ASN A 626      59.398  33.091 -10.805  1.00 61.61           O  
ANISOU 4558  O   ASN A 626     7116   8036   8257    376    292    513       O  
ATOM   4559  CB  ASN A 626      57.784  33.220  -7.961  1.00 57.81           C  
ANISOU 4559  CB  ASN A 626     6652   7576   7738    312    186    485       C  
ATOM   4560  CG  ASN A 626      56.812  33.062  -9.111  1.00 56.08           C  
ANISOU 4560  CG  ASN A 626     6462   7381   7465    343    211    501       C  
ATOM   4561  OD1 ASN A 626      56.532  31.943  -9.537  1.00 58.35           O  
ANISOU 4561  OD1 ASN A 626     6761   7686   7723    355    191    497       O  
ATOM   4562  ND2 ASN A 626      56.328  34.183  -9.648  1.00 52.80           N  
ANISOU 4562  ND2 ASN A 626     6056   6966   7039    357    254    517       N  
ATOM   4563  N   ASN A 627      59.542  35.085  -9.774  1.00 59.66           N  
ANISOU 4563  N   ASN A 627     6849   7757   8062    348    316    515       N  
ATOM   4564  CA  ASN A 627      59.796  35.804 -11.010  1.00 60.99           C  
ANISOU 4564  CA  ASN A 627     7018   7917   8240    378    384    541       C  
ATOM   4565  C   ASN A 627      61.068  35.326 -11.722  1.00 63.33           C  
ANISOU 4565  C   ASN A 627     7292   8195   8576    391    410    542       C  
ATOM   4566  O   ASN A 627      61.116  35.288 -12.955  1.00 61.93           O  
ANISOU 4566  O   ASN A 627     7125   8026   8380    423    455    561       O  
ATOM   4567  CB  ASN A 627      59.865  37.306 -10.767  1.00 64.36           C  
ANISOU 4567  CB  ASN A 627     7431   8317   8705    370    423    551       C  
ATOM   4568  CG  ASN A 627      60.129  38.080 -12.042  1.00 70.43           C  
ANISOU 4568  CG  ASN A 627     8200   9075   9486    402    497    584       C  
ATOM   4569  OD1 ASN A 627      59.298  38.107 -12.945  1.00 75.83           O  
ANISOU 4569  OD1 ASN A 627     8914   9784  10114    431    518    607       O  
ATOM   4570  ND2 ASN A 627      61.301  38.702 -12.129  1.00 74.01           N  
ANISOU 4570  ND2 ASN A 627     8619   9489  10011    398    536    586       N  
ATOM   4571  N   ALA A 628      62.090  34.964 -10.949  1.00 60.39           N  
ANISOU 4571  N   ALA A 628     6888   7799   8258    368    382    519       N  
ATOM   4572  CA  ALA A 628      63.334  34.462 -11.540  1.00 62.98           C  
ANISOU 4572  CA  ALA A 628     7192   8107   8631    378    404    515       C  
ATOM   4573  C   ALA A 628      63.161  33.049 -12.103  1.00 64.21           C  
ANISOU 4573  C   ALA A 628     7363   8289   8745    394    379    510       C  
ATOM   4574  O   ALA A 628      63.391  32.817 -13.286  1.00 65.04           O  
ANISOU 4574  O   ALA A 628     7472   8400   8839    423    420    521       O  
ATOM   4575  CB  ALA A 628      64.472  34.503 -10.528  1.00 58.83           C  
ANISOU 4575  CB  ALA A 628     6626   7549   8179    349    378    491       C  
ATOM   4576  N   GLN A 629      62.770  32.106 -11.251  1.00 65.44           N  
ANISOU 4576  N   GLN A 629     7525   8458   8881    376    314    492       N  
ATOM   4577  CA  GLN A 629      62.523  30.740 -11.697  1.00 68.65           C  
ANISOU 4577  CA  GLN A 629     7945   8888   9254    389    287    484       C  
ATOM   4578  C   GLN A 629      61.116  30.229 -11.345  1.00 67.13           C  
ANISOU 4578  C   GLN A 629     7784   8728   8995    386    245    482       C  
ATOM   4579  O   GLN A 629      60.941  29.532 -10.334  1.00 64.80           O  
ANISOU 4579  O   GLN A 629     7487   8435   8698    363    189    469       O  
ATOM   4580  CB  GLN A 629      63.626  29.792 -11.219  1.00 74.01           C  
ANISOU 4580  CB  GLN A 629     8592   9544   9983    375    252    463       C  
ATOM   4581  CG  GLN A 629      64.585  29.392 -12.343  1.00 82.78           C  
ANISOU 4581  CG  GLN A 629     9686  10644  11123    398    293    462       C  
ATOM   4582  CD  GLN A 629      65.892  30.165 -12.335  1.00 87.76           C  
ANISOU 4582  CD  GLN A 629    10280  11237  11828    392    330    461       C  
ATOM   4583  OE1 GLN A 629      66.662  30.090 -11.375  1.00 98.78           O  
ANISOU 4583  OE1 GLN A 629    11648  12608  13277    368    297    445       O  
ATOM   4584  NE2 GLN A 629      66.167  30.888 -13.421  1.00 85.86           N  
ANISOU 4584  NE2 GLN A 629    10040  10991  11593    415    400    479       N  
ATOM   4585  N   PRO A 630      60.115  30.565 -12.196  1.00 66.25           N  
ANISOU 4585  N   PRO A 630     7702   8643   8828    411    274    497       N  
ATOM   4586  CA  PRO A 630      58.697  30.205 -11.978  1.00 67.10           C  
ANISOU 4586  CA  PRO A 630     7840   8782   8874    411    241    495       C  
ATOM   4587  C   PRO A 630      58.494  28.697 -11.849  1.00 71.14           C  
ANISOU 4587  C   PRO A 630     8353   9305   9371    409    193    477       C  
ATOM   4588  O   PRO A 630      57.625  28.253 -11.096  1.00 67.34           O  
ANISOU 4588  O   PRO A 630     7886   8837   8862    393    150    470       O  
ATOM   4589  CB  PRO A 630      57.991  30.726 -13.240  1.00 64.88           C  
ANISOU 4589  CB  PRO A 630     7582   8523   8546    446    288    513       C  
ATOM   4590  CG  PRO A 630      58.934  31.711 -13.858  1.00 66.26           C  
ANISOU 4590  CG  PRO A 630     7741   8676   8758    459    348    531       C  
ATOM   4591  CD  PRO A 630      60.313  31.230 -13.501  1.00 65.01           C  
ANISOU 4591  CD  PRO A 630     7548   8487   8664    443    340    517       C  
ATOM   4592  N   ASP A 631      59.326  27.925 -12.552  1.00 76.00           N  
ANISOU 4592  N   ASP A 631     8954   9915  10009    424    203    468       N  
ATOM   4593  CA  ASP A 631      59.184  26.471 -12.622  1.00 77.29           C  
ANISOU 4593  CA  ASP A 631     9116  10087  10165    427    164    450       C  
ATOM   4594  C   ASP A 631      59.701  25.755 -11.385  1.00 76.99           C  
ANISOU 4594  C   ASP A 631     9059  10028  10166    395    111    440       C  
ATOM   4595  O   ASP A 631      59.630  24.534 -11.310  1.00 80.66           O  
ANISOU 4595  O   ASP A 631     9520  10495  10633    395     76    427       O  
ATOM   4596  CB  ASP A 631      59.873  25.912 -13.875  1.00 81.86           C  
ANISOU 4596  CB  ASP A 631     9683  10667  10753    456    196    442       C  
ATOM   4597  CG  ASP A 631      59.452  26.634 -15.157  1.00 90.39           C  
ANISOU 4597  CG  ASP A 631    10783  11772  11791    491    252    455       C  
ATOM   4598  OD1 ASP A 631      58.344  27.216 -15.203  1.00 93.40           O  
ANISOU 4598  OD1 ASP A 631    11189  12175  12123    498    256    466       O  
ATOM   4599  OD2 ASP A 631      60.238  26.620 -16.129  1.00 95.61           O  
ANISOU 4599  OD2 ASP A 631    11431  12430  12464    514    294    455       O  
ATOM   4600  N   GLN A 632      60.211  26.503 -10.413  1.00 76.59           N  
ANISOU 4600  N   GLN A 632     8996   9958  10148    370    103    445       N  
ATOM   4601  CA  GLN A 632      60.816  25.886  -9.230  1.00 77.78           C  
ANISOU 4601  CA  GLN A 632     9126  10090  10337    343     52    437       C  
ATOM   4602  C   GLN A 632      60.361  26.514  -7.921  1.00 74.11           C  
ANISOU 4602  C   GLN A 632     8669   9628   9862    315     23    442       C  
ATOM   4603  O   GLN A 632      60.456  25.892  -6.860  1.00 72.81           O  
ANISOU 4603  O   GLN A 632     8498   9460   9706    293    -28    438       O  
ATOM   4604  CB  GLN A 632      62.343  25.960  -9.310  1.00 88.62           C  
ANISOU 4604  CB  GLN A 632    10464  11432  11777    342     66    431       C  
ATOM   4605  CG  GLN A 632      62.969  25.191 -10.464  1.00 98.00           C  
ANISOU 4605  CG  GLN A 632    11638  12614  12982    366     90    423       C  
ATOM   4606  CD  GLN A 632      64.291  25.788 -10.901  1.00103.47           C  
ANISOU 4606  CD  GLN A 632    12301  13279  13732    372    132    421       C  
ATOM   4607  OE1 GLN A 632      64.477  26.109 -12.078  1.00108.04           O  
ANISOU 4607  OE1 GLN A 632    12883  13863  14307    397    186    425       O  
ATOM   4608  NE2 GLN A 632      65.214  25.954  -9.954  1.00104.44           N  
ANISOU 4608  NE2 GLN A 632    12397  13376  13911    349    107    414       N  
ATOM   4609  N   TYR A 633      59.900  27.756  -7.984  1.00 72.03           N  
ANISOU 4609  N   TYR A 633     8417   9370   9581    315     54    450       N  
ATOM   4610  CA  TYR A 633      59.460  28.445  -6.780  1.00 72.15           C  
ANISOU 4610  CA  TYR A 633     8438   9390   9588    288     31    449       C  
ATOM   4611  C   TYR A 633      58.044  28.985  -6.951  1.00 72.19           C  
ANISOU 4611  C   TYR A 633     8474   9419   9535    293     44    457       C  
ATOM   4612  O   TYR A 633      57.731  29.687  -7.923  1.00 68.78           O  
ANISOU 4612  O   TYR A 633     8052   8993   9089    315     90    467       O  
ATOM   4613  CB  TYR A 633      60.461  29.530  -6.362  1.00 72.43           C  
ANISOU 4613  CB  TYR A 633     8446   9400   9675    276     49    445       C  
ATOM   4614  CG  TYR A 633      61.885  29.023  -6.334  1.00 72.43           C  
ANISOU 4614  CG  TYR A 633     8412   9373   9734    275     41    435       C  
ATOM   4615  CD1 TYR A 633      62.732  29.228  -7.420  1.00 74.43           C  
ANISOU 4615  CD1 TYR A 633     8648   9608  10023    295     89    437       C  
ATOM   4616  CD2 TYR A 633      62.374  28.298  -5.237  1.00 72.36           C  
ANISOU 4616  CD2 TYR A 633     8388   9359   9746    254    -16    425       C  
ATOM   4617  CE1 TYR A 633      64.039  28.754  -7.408  1.00 78.38           C  
ANISOU 4617  CE1 TYR A 633     9116  10083  10584    294     82    426       C  
ATOM   4618  CE2 TYR A 633      63.676  27.814  -5.213  1.00 72.79           C  
ANISOU 4618  CE2 TYR A 633     8410   9389   9858    254    -26    415       C  
ATOM   4619  CZ  TYR A 633      64.509  28.044  -6.303  1.00 79.46           C  
ANISOU 4619  CZ  TYR A 633     9236  10213  10742    273     23    414       C  
ATOM   4620  OH  TYR A 633      65.813  27.572  -6.309  1.00 82.31           O  
ANISOU 4620  OH  TYR A 633     9562  10547  11165    273     15    403       O  
ATOM   4621  N   GLU A 634      57.202  28.604  -5.993  1.00 71.64           N  
ANISOU 4621  N   GLU A 634     8419   9366   9435    274      1    455       N  
ATOM   4622  CA  GLU A 634      55.792  28.934  -5.958  1.00 74.98           C  
ANISOU 4622  CA  GLU A 634     8871   9813   9805    274      3    459       C  
ATOM   4623  C   GLU A 634      55.628  30.438  -5.817  1.00 71.38           C  
ANISOU 4623  C   GLU A 634     8415   9353   9353    270     35    461       C  
ATOM   4624  O   GLU A 634      56.297  31.051  -4.983  1.00 71.77           O  
ANISOU 4624  O   GLU A 634     8446   9388   9436    249     28    455       O  
ATOM   4625  CB  GLU A 634      55.176  28.256  -4.733  1.00 82.99           C  
ANISOU 4625  CB  GLU A 634     9895  10840  10798    249    -49    455       C  
ATOM   4626  CG  GLU A 634      53.680  28.023  -4.796  1.00 92.70           C  
ANISOU 4626  CG  GLU A 634    11153  12093  11974    252    -56    456       C  
ATOM   4627  CD  GLU A 634      53.342  26.591  -5.145  1.00 99.65           C  
ANISOU 4627  CD  GLU A 634    12039  12980  12842    261    -79    455       C  
ATOM   4628  OE1 GLU A 634      53.627  26.170  -6.288  1.00103.30           O  
ANISOU 4628  OE1 GLU A 634    12498  13441  13312    287    -59    453       O  
ATOM   4629  OE2 GLU A 634      52.792  25.890  -4.270  1.00105.31           O  
ANISOU 4629  OE2 GLU A 634    12763  13704  13544    243   -117    455       O  
ATOM   4630  N   ALA A 635      54.746  31.032  -6.621  1.00 65.20           N  
ANISOU 4630  N   ALA A 635     7652   8583   8538    289     69    470       N  
ATOM   4631  CA  ALA A 635      54.340  32.421  -6.400  1.00 62.49           C  
ANISOU 4631  CA  ALA A 635     7311   8238   8194    283     96    474       C  
ATOM   4632  C   ALA A 635      53.738  32.542  -5.002  1.00 61.65           C  
ANISOU 4632  C   ALA A 635     7210   8141   8074    251     57    462       C  
ATOM   4633  O   ALA A 635      53.066  31.619  -4.534  1.00 68.33           O  
ANISOU 4633  O   ALA A 635     8071   9005   8888    242     19    458       O  
ATOM   4634  CB  ALA A 635      53.359  32.894  -7.460  1.00 58.02           C  
ANISOU 4634  CB  ALA A 635     6768   7687   7590    311    131    487       C  
ATOM   4635  N   PRO A 636      54.006  33.660  -4.311  1.00 60.68           N  
ANISOU 4635  N   PRO A 636     7072   8006   7977    233     66    455       N  
ATOM   4636  CA  PRO A 636      53.442  33.849  -2.967  1.00 59.63           C  
ANISOU 4636  CA  PRO A 636     6943   7886   7828    203     31    440       C  
ATOM   4637  C   PRO A 636      51.962  34.311  -2.987  1.00 57.60           C  
ANISOU 4637  C   PRO A 636     6711   7648   7525    204     40    442       C  
ATOM   4638  O   PRO A 636      51.476  34.843  -3.997  1.00 52.36           O  
ANISOU 4638  O   PRO A 636     6057   6984   6852    227     77    454       O  
ATOM   4639  CB  PRO A 636      54.323  34.959  -2.399  1.00 58.69           C  
ANISOU 4639  CB  PRO A 636     6796   7745   7760    188     44    427       C  
ATOM   4640  CG  PRO A 636      54.633  35.799  -3.613  1.00 56.16           C  
ANISOU 4640  CG  PRO A 636     6469   7405   7467    213    103    442       C  
ATOM   4641  CD  PRO A 636      54.817  34.819  -4.737  1.00 54.39           C  
ANISOU 4641  CD  PRO A 636     6255   7184   7229    240    111    458       C  
ATOM   4642  N   ASP A 637      51.271  34.104  -1.870  1.00 55.19           N  
ANISOU 4642  N   ASP A 637     6416   7361   7193    179      4    430       N  
ATOM   4643  CA  ASP A 637      49.936  34.640  -1.672  1.00 52.75           C  
ANISOU 4643  CA  ASP A 637     6126   7069   6849    175     10    427       C  
ATOM   4644  C   ASP A 637      50.075  36.061  -1.165  1.00 50.93           C  
ANISOU 4644  C   ASP A 637     5879   6826   6646    161     31    414       C  
ATOM   4645  O   ASP A 637      50.451  36.285  -0.002  1.00 47.79           O  
ANISOU 4645  O   ASP A 637     5467   6430   6261    135      7    396       O  
ATOM   4646  CB  ASP A 637      49.175  33.798  -0.645  1.00 54.16           C  
ANISOU 4646  CB  ASP A 637     6319   7271   6989    153    -33    419       C  
ATOM   4647  CG  ASP A 637      47.700  34.159  -0.551  1.00 59.66           C  
ANISOU 4647  CG  ASP A 637     7036   7985   7647    150    -27    415       C  
ATOM   4648  OD1 ASP A 637      47.274  35.253  -0.989  1.00 60.54           O  
ANISOU 4648  OD1 ASP A 637     7148   8091   7764    159      6    414       O  
ATOM   4649  OD2 ASP A 637      46.948  33.323  -0.014  1.00 66.00           O  
ANISOU 4649  OD2 ASP A 637     7854   8806   8417    139    -56    413       O  
ATOM   4650  N   LYS A 638      49.729  37.023  -2.019  1.00 48.48           N  
ANISOU 4650  N   LYS A 638     5570   6506   6344    180     74    423       N  
ATOM   4651  CA  LYS A 638      49.914  38.430  -1.678  1.00 48.61           C  
ANISOU 4651  CA  LYS A 638     5567   6505   6397    170    100    413       C  
ATOM   4652  C   LYS A 638      48.979  38.947  -0.593  1.00 48.59           C  
ANISOU 4652  C   LYS A 638     5569   6517   6374    144     84    391       C  
ATOM   4653  O   LYS A 638      49.133  40.074  -0.132  1.00 46.89           O  
ANISOU 4653  O   LYS A 638     5334   6289   6192    132    100    375       O  
ATOM   4654  CB  LYS A 638      49.837  39.316  -2.924  1.00 48.83           C  
ANISOU 4654  CB  LYS A 638     5595   6515   6443    199    154    434       C  
ATOM   4655  CG  LYS A 638      51.026  39.138  -3.863  1.00 51.69           C  
ANISOU 4655  CG  LYS A 638     5944   6856   6840    220    180    451       C  
ATOM   4656  CD  LYS A 638      50.870  39.989  -5.108  1.00 53.25           C  
ANISOU 4656  CD  LYS A 638     6145   7040   7049    252    236    478       C  
ATOM   4657  CE  LYS A 638      52.077  39.859  -6.013  1.00 54.43           C  
ANISOU 4657  CE  LYS A 638     6279   7168   7232    272    266    495       C  
ATOM   4658  NZ  LYS A 638      51.944  40.778  -7.177  1.00 56.99           N  
ANISOU 4658  NZ  LYS A 638     6607   7480   7567    303    324    525       N  
ATOM   4659  N   ASP A 639      48.012  38.138  -0.184  1.00 49.18           N  
ANISOU 4659  N   ASP A 639     5667   6619   6399    136     54    388       N  
ATOM   4660  CA  ASP A 639      47.099  38.561   0.862  1.00 52.91           C  
ANISOU 4660  CA  ASP A 639     6145   7109   6850    111     39    367       C  
ATOM   4661  C   ASP A 639      47.835  38.719   2.180  1.00 50.48           C  
ANISOU 4661  C   ASP A 639     5817   6804   6559     82     11    343       C  
ATOM   4662  O   ASP A 639      47.510  39.609   2.949  1.00 53.04           O  
ANISOU 4662  O   ASP A 639     6131   7131   6890     63     14    319       O  
ATOM   4663  CB  ASP A 639      45.910  37.606   1.002  1.00 57.72           C  
ANISOU 4663  CB  ASP A 639     6782   7745   7404    109     15    371       C  
ATOM   4664  CG  ASP A 639      45.015  37.590  -0.240  1.00 63.69           C  
ANISOU 4664  CG  ASP A 639     7556   8501   8140    139     40    388       C  
ATOM   4665  OD1 ASP A 639      44.913  38.616  -0.951  1.00 65.84           O  
ANISOU 4665  OD1 ASP A 639     7824   8759   8434    156     77    395       O  
ATOM   4666  OD2 ASP A 639      44.401  36.541  -0.505  1.00 67.26           O  
ANISOU 4666  OD2 ASP A 639     8027   8969   8558    147     22    395       O  
ATOM   4667  N   PHE A 640      48.826  37.868   2.426  1.00 49.38           N  
ANISOU 4667  N   PHE A 640     5670   6665   6428     79    -15    346       N  
ATOM   4668  CA  PHE A 640      49.715  37.998   3.600  1.00 51.11           C  
ANISOU 4668  CA  PHE A 640     5866   6886   6667     55    -44    323       C  
ATOM   4669  C   PHE A 640      50.329  39.391   3.671  1.00 51.34           C  
ANISOU 4669  C   PHE A 640     5864   6891   6751     51    -16    302       C  
ATOM   4670  O   PHE A 640      50.473  39.977   4.745  1.00 50.61           O  
ANISOU 4670  O   PHE A 640     5756   6807   6668     28    -31    271       O  
ATOM   4671  CB  PHE A 640      50.845  36.958   3.550  1.00 47.28           C  
ANISOU 4671  CB  PHE A 640     5373   6395   6195     60    -70    334       C  
ATOM   4672  CG  PHE A 640      50.393  35.573   3.887  1.00 46.71           C  
ANISOU 4672  CG  PHE A 640     5325   6347   6077     56   -107    348       C  
ATOM   4673  CD1 PHE A 640      50.296  35.165   5.214  1.00 46.24           C  
ANISOU 4673  CD1 PHE A 640     5269   6313   5989     33   -149    337       C  
ATOM   4674  CD2 PHE A 640      50.039  34.680   2.880  1.00 47.11           C  
ANISOU 4674  CD2 PHE A 640     5394   6395   6111     78   -100    373       C  
ATOM   4675  CE1 PHE A 640      49.858  33.883   5.534  1.00 47.03           C  
ANISOU 4675  CE1 PHE A 640     5389   6430   6048     30   -180    355       C  
ATOM   4676  CE2 PHE A 640      49.604  33.402   3.193  1.00 46.60           C  
ANISOU 4676  CE2 PHE A 640     5348   6347   6010     74   -133    385       C  
ATOM   4677  CZ  PHE A 640      49.518  33.003   4.522  1.00 46.61           C  
ANISOU 4677  CZ  PHE A 640     5352   6370   5987     50   -171    378       C  
ATOM   4678  N   MET A 641      50.668  39.917   2.506  1.00 51.80           N  
ANISOU 4678  N   MET A 641     5914   6920   6846     73     27    318       N  
ATOM   4679  CA  MET A 641      51.266  41.226   2.409  1.00 55.30           C  
ANISOU 4679  CA  MET A 641     6326   7334   7350     72     61    304       C  
ATOM   4680  C   MET A 641      50.216  42.316   2.620  1.00 54.50           C  
ANISOU 4680  C   MET A 641     6227   7235   7246     65     83    291       C  
ATOM   4681  O   MET A 641      50.450  43.289   3.336  1.00 56.30           O  
ANISOU 4681  O   MET A 641     6428   7453   7509     47     88    260       O  
ATOM   4682  CB  MET A 641      51.942  41.353   1.054  1.00 55.23           C  
ANISOU 4682  CB  MET A 641     6311   7295   7379    101    103    332       C  
ATOM   4683  CG  MET A 641      52.400  42.753   0.714  1.00 61.59           C  
ANISOU 4683  CG  MET A 641     7087   8065   8250    105    150    326       C  
ATOM   4684  SD  MET A 641      53.762  42.674  -0.458  1.00 59.68           S  
ANISOU 4684  SD  MET A 641     6825   7786   8062    130    187    351       S  
ATOM   4685  CE  MET A 641      52.938  42.354  -2.020  1.00 59.71           C  
ANISOU 4685  CE  MET A 641     6866   7797   8025    167    223    398       C  
ATOM   4686  N   ILE A 642      49.049  42.139   2.011  1.00 54.88           N  
ANISOU 4686  N   ILE A 642     6304   7294   7252     79     95    311       N  
ATOM   4687  CA  ILE A 642      47.945  43.103   2.139  1.00 50.65           C  
ANISOU 4687  CA  ILE A 642     5773   6760   6711     74    116    300       C  
ATOM   4688  C   ILE A 642      47.493  43.246   3.598  1.00 48.42           C  
ANISOU 4688  C   ILE A 642     5487   6503   6409     41     83    262       C  
ATOM   4689  O   ILE A 642      47.380  44.335   4.138  1.00 48.22           O  
ANISOU 4689  O   ILE A 642     5439   6468   6413     27     96    234       O  
ATOM   4690  CB  ILE A 642      46.781  42.700   1.221  1.00 52.42           C  
ANISOU 4690  CB  ILE A 642     6029   6996   6890     97    127    328       C  
ATOM   4691  CG1 ILE A 642      47.218  42.870  -0.239  1.00 50.07           C  
ANISOU 4691  CG1 ILE A 642     5733   6675   6617    132    168    363       C  
ATOM   4692  CG2 ILE A 642      45.520  43.512   1.534  1.00 50.61           C  
ANISOU 4692  CG2 ILE A 642     5807   6774   6649     89    138    314       C  
ATOM   4693  CD1 ILE A 642      46.328  42.178  -1.245  1.00 53.60           C  
ANISOU 4693  CD1 ILE A 642     6212   7138   7016    159    171    390       C  
ATOM   4694  N   VAL A 643      47.281  42.126   4.251  1.00 48.14           N  
ANISOU 4694  N   VAL A 643     5470   6499   6323     29     41    261       N  
ATOM   4695  CA  VAL A 643      46.853  42.143   5.623  1.00 48.67           C  
ANISOU 4695  CA  VAL A 643     5537   6594   6362      0     10    229       C  
ATOM   4696  C   VAL A 643      47.934  42.767   6.515  1.00 48.35           C  
ANISOU 4696  C   VAL A 643     5460   6547   6362    -18     -2    195       C  
ATOM   4697  O   VAL A 643      47.621  43.552   7.419  1.00 48.94           O  
ANISOU 4697  O   VAL A 643     5521   6632   6441    -39     -5    158       O  
ATOM   4698  CB  VAL A 643      46.450  40.721   6.059  1.00 51.00           C  
ANISOU 4698  CB  VAL A 643     5860   6921   6595     -6    -30    243       C  
ATOM   4699  CG1 VAL A 643      46.177  40.663   7.540  1.00 52.11           C  
ANISOU 4699  CG1 VAL A 643     6000   7094   6704    -36    -63    213       C  
ATOM   4700  CG2 VAL A 643      45.208  40.277   5.291  1.00 54.00           C  
ANISOU 4700  CG2 VAL A 643     6271   7309   6940      9    -17    266       C  
ATOM   4701  N   ALA A 644      49.203  42.453   6.246  1.00 47.54           N  
ANISOU 4701  N   ALA A 644     5341   6427   6294    -10     -8    202       N  
ATOM   4702  CA  ALA A 644      50.308  43.008   7.055  1.00 45.77           C  
ANISOU 4702  CA  ALA A 644     5080   6196   6114    -26    -22    167       C  
ATOM   4703  C   ALA A 644      50.433  44.516   6.902  1.00 44.03           C  
ANISOU 4703  C   ALA A 644     4827   5944   5957    -28     18    142       C  
ATOM   4704  O   ALA A 644      50.562  45.239   7.899  1.00 43.33           O  
ANISOU 4704  O   ALA A 644     4714   5863   5887    -48      7     98       O  
ATOM   4705  CB  ALA A 644      51.623  42.314   6.739  1.00 46.85           C  
ANISOU 4705  CB  ALA A 644     5204   6319   6278    -15    -36    180       C  
ATOM   4706  N   LEU A 645      50.369  45.002   5.666  1.00 43.71           N  
ANISOU 4706  N   LEU A 645     4786   5870   5952     -5     65    170       N  
ATOM   4707  CA  LEU A 645      50.384  46.456   5.432  1.00 47.95           C  
ANISOU 4707  CA  LEU A 645     5294   6373   6552     -5    109    154       C  
ATOM   4708  C   LEU A 645      49.209  47.097   6.151  1.00 51.83           C  
ANISOU 4708  C   LEU A 645     5789   6883   7020    -22    108    126       C  
ATOM   4709  O   LEU A 645      49.367  48.100   6.861  1.00 50.24           O  
ANISOU 4709  O   LEU A 645     5556   6673   6861    -40    113     84       O  
ATOM   4710  CB  LEU A 645      50.316  46.799   3.933  1.00 47.02           C  
ANISOU 4710  CB  LEU A 645     5183   6221   6463     26    162    197       C  
ATOM   4711  CG  LEU A 645      51.510  46.355   3.074  1.00 48.12           C  
ANISOU 4711  CG  LEU A 645     5313   6336   6635     45    175    225       C  
ATOM   4712  CD1 LEU A 645      51.247  46.477   1.575  1.00 49.05           C  
ANISOU 4712  CD1 LEU A 645     5448   6433   6758     78    223    273       C  
ATOM   4713  CD2 LEU A 645      52.751  47.131   3.449  1.00 46.92           C  
ANISOU 4713  CD2 LEU A 645     5113   6152   6563     34    186    195       C  
ATOM   4714  N   ASP A 646      48.033  46.487   5.988  1.00 53.71           N  
ANISOU 4714  N   ASP A 646     6066   7148   7194    -18    100    146       N  
ATOM   4715  CA  ASP A 646      46.818  47.031   6.552  1.00 54.14           C  
ANISOU 4715  CA  ASP A 646     6127   7218   7224    -32    102    124       C  
ATOM   4716  C   ASP A 646      46.935  47.033   8.076  1.00 50.10           C  
ANISOU 4716  C   ASP A 646     5603   6739   6694    -63     63     75       C  
ATOM   4717  O   ASP A 646      46.540  47.997   8.722  1.00 48.13           O  
ANISOU 4717  O   ASP A 646     5333   6490   6464    -80     72     36       O  
ATOM   4718  CB  ASP A 646      45.582  46.285   6.018  1.00 63.05           C  
ANISOU 4718  CB  ASP A 646     7298   8367   8290    -20    101    156       C  
ATOM   4719  CG  ASP A 646      44.462  46.179   7.047  1.00 77.37           C  
ANISOU 4719  CG  ASP A 646     9126  10217  10053    -43     78    129       C  
ATOM   4720  OD1 ASP A 646      43.678  47.160   7.199  1.00 79.08           O  
ANISOU 4720  OD1 ASP A 646     9333  10427  10286    -49    100    108       O  
ATOM   4721  OD2 ASP A 646      44.365  45.099   7.697  1.00 85.67           O  
ANISOU 4721  OD2 ASP A 646    10197  11303  11050    -54     40    130       O  
ATOM   4722  N   LEU A 647      47.531  46.001   8.659  1.00 44.95           N  
ANISOU 4722  N   LEU A 647     4959   6113   6007    -71     21     75       N  
ATOM   4723  CA  LEU A 647      47.756  46.050  10.093  1.00 45.27           C  
ANISOU 4723  CA  LEU A 647     4985   6186   6029    -97    -17     30       C  
ATOM   4724  C   LEU A 647      48.791  47.146  10.475  1.00 51.80           C  
ANISOU 4724  C   LEU A 647     5762   6989   6931   -105     -9    -14       C  
ATOM   4725  O   LEU A 647      48.616  47.853  11.487  1.00 52.51           O  
ANISOU 4725  O   LEU A 647     5831   7096   7026   -126    -18    -64       O  
ATOM   4726  CB  LEU A 647      48.138  44.680  10.626  1.00 44.29           C  
ANISOU 4726  CB  LEU A 647     4882   6096   5851   -100    -65     45       C  
ATOM   4727  CG  LEU A 647      48.558  44.566  12.092  1.00 48.23           C  
ANISOU 4727  CG  LEU A 647     5368   6633   6325   -123   -109      4       C  
ATOM   4728  CD1 LEU A 647      47.693  45.407  13.023  1.00 48.88           C  
ANISOU 4728  CD1 LEU A 647     5444   6740   6390   -144   -106    -41       C  
ATOM   4729  CD2 LEU A 647      48.536  43.109  12.534  1.00 47.63           C  
ANISOU 4729  CD2 LEU A 647     5323   6593   6181   -124   -152     32       C  
ATOM   4730  N   LEU A 648      49.845  47.320   9.672  1.00 49.28           N  
ANISOU 4730  N   LEU A 648     5422   6630   6673    -90     11      1       N  
ATOM   4731  CA  LEU A 648      50.808  48.389   9.970  1.00 49.33           C  
ANISOU 4731  CA  LEU A 648     5377   6607   6759    -97     23    -41       C  
ATOM   4732  C   LEU A 648      50.129  49.764   9.905  1.00 51.08           C  
ANISOU 4732  C   LEU A 648     5577   6805   7025   -103     64    -66       C  
ATOM   4733  O   LEU A 648      50.390  50.645  10.728  1.00 52.12           O  
ANISOU 4733  O   LEU A 648     5671   6935   7196   -121     60   -121       O  
ATOM   4734  CB  LEU A 648      52.034  48.314   9.060  1.00 46.28           C  
ANISOU 4734  CB  LEU A 648     4971   6180   6434    -79     42    -17       C  
ATOM   4735  CG  LEU A 648      52.971  47.117   9.330  1.00 46.88           C  
ANISOU 4735  CG  LEU A 648     5053   6275   6484    -77     -3     -7       C  
ATOM   4736  CD1 LEU A 648      53.826  46.823   8.110  1.00 43.06           C  
ANISOU 4736  CD1 LEU A 648     4565   5752   6043    -53     24     33       C  
ATOM   4737  CD2 LEU A 648      53.814  47.252  10.598  1.00 42.32           C  
ANISOU 4737  CD2 LEU A 648     4443   5717   5921    -96    -46    -62       C  
ATOM   4738  N   SER A 649      49.221  49.919   8.952  1.00 51.35           N  
ANISOU 4738  N   SER A 649     5636   6824   7052    -87    101    -27       N  
ATOM   4739  CA  SER A 649      48.403  51.125   8.842  1.00 53.22           C  
ANISOU 4739  CA  SER A 649     5859   7040   7324    -90    138    -44       C  
ATOM   4740  C   SER A 649      47.612  51.420  10.133  1.00 54.58           C  
ANISOU 4740  C   SER A 649     6027   7249   7460   -117    113    -96       C  
ATOM   4741  O   SER A 649      47.616  52.556  10.649  1.00 51.96           O  
ANISOU 4741  O   SER A 649     5657   6903   7182   -131    128   -144       O  
ATOM   4742  CB  SER A 649      47.440  50.960   7.685  1.00 52.98           C  
ANISOU 4742  CB  SER A 649     5863   6998   7269    -67    169     10       C  
ATOM   4743  OG  SER A 649      47.173  52.200   7.092  1.00 59.22           O  
ANISOU 4743  OG  SER A 649     6630   7746   8124    -58    219     12       O  
ATOM   4744  N   GLY A 650      46.959  50.385  10.659  1.00 52.43           N  
ANISOU 4744  N   GLY A 650     5793   7026   7102   -125     77    -88       N  
ATOM   4745  CA  GLY A 650      46.165  50.508  11.874  1.00 52.52           C  
ANISOU 4745  CA  GLY A 650     5808   7080   7068   -150     53   -133       C  
ATOM   4746  C   GLY A 650      47.035  50.864  13.059  1.00 53.58           C  
ANISOU 4746  C   GLY A 650     5905   7231   7221   -170     24   -193       C  
ATOM   4747  O   GLY A 650      46.711  51.759  13.839  1.00 54.98           O  
ANISOU 4747  O   GLY A 650     6056   7417   7417   -188     27   -247       O  
ATOM   4748  N   LEU A 651      48.153  50.159  13.180  1.00 55.43           N  
ANISOU 4748  N   LEU A 651     6135   7472   7452   -166     -6   -185       N  
ATOM   4749  CA  LEU A 651      49.164  50.451  14.184  1.00 57.34           C  
ANISOU 4749  CA  LEU A 651     6340   7728   7720   -180    -37   -240       C  
ATOM   4750  C   LEU A 651      49.591  51.917  14.138  1.00 55.17           C  
ANISOU 4750  C   LEU A 651     6010   7410   7542   -185     -4   -286       C  
ATOM   4751  O   LEU A 651      49.602  52.595  15.163  1.00 55.52           O  
ANISOU 4751  O   LEU A 651     6025   7474   7598   -205    -18   -351       O  
ATOM   4752  CB  LEU A 651      50.368  49.547  13.953  1.00 58.82           C  
ANISOU 4752  CB  LEU A 651     6527   7912   7908   -169    -64   -214       C  
ATOM   4753  CG  LEU A 651      51.122  49.005  15.163  1.00 61.24           C  
ANISOU 4753  CG  LEU A 651     6824   8263   8181   -181   -122   -249       C  
ATOM   4754  CD1 LEU A 651      50.170  48.571  16.259  1.00 62.34           C  
ANISOU 4754  CD1 LEU A 651     6992   8464   8229   -197   -154   -264       C  
ATOM   4755  CD2 LEU A 651      51.993  47.833  14.733  1.00 63.93           C  
ANISOU 4755  CD2 LEU A 651     7181   8602   8508   -165   -147   -204       C  
ATOM   4756  N   ALA A 652      49.917  52.399  12.941  1.00 55.34           N  
ANISOU 4756  N   ALA A 652     6019   7374   7634   -167     42   -254       N  
ATOM   4757  CA  ALA A 652      50.354  53.789  12.743  1.00 58.37           C  
ANISOU 4757  CA  ALA A 652     6350   7707   8122   -169     81   -289       C  
ATOM   4758  C   ALA A 652      49.258  54.814  13.049  1.00 59.73           C  
ANISOU 4758  C   ALA A 652     6511   7876   8307   -182    106   -322       C  
ATOM   4759  O   ALA A 652      49.537  55.864  13.636  1.00 61.72           O  
ANISOU 4759  O   ALA A 652     6715   8113   8623   -196    114   -383       O  
ATOM   4760  CB  ALA A 652      50.896  53.987  11.329  1.00 54.72           C  
ANISOU 4760  CB  ALA A 652     5882   7185   7724   -145    128   -236       C  
ATOM   4761  N   GLU A 653      48.024  54.511  12.646  1.00 61.05           N  
ANISOU 4761  N   GLU A 653     6720   8056   8420   -176    119   -285       N  
ATOM   4762  CA  GLU A 653      46.880  55.357  12.986  1.00 61.32           C  
ANISOU 4762  CA  GLU A 653     6748   8092   8458   -188    139   -315       C  
ATOM   4763  C   GLU A 653      46.642  55.394  14.495  1.00 59.12           C  
ANISOU 4763  C   GLU A 653     6459   7867   8137   -216     99   -384       C  
ATOM   4764  O   GLU A 653      46.487  56.465  15.075  1.00 57.37           O  
ANISOU 4764  O   GLU A 653     6199   7637   7964   -231    111   -443       O  
ATOM   4765  CB  GLU A 653      45.613  54.883  12.277  1.00 65.31           C  
ANISOU 4765  CB  GLU A 653     7303   8606   8908   -175    154   -261       C  
ATOM   4766  CG  GLU A 653      44.438  55.839  12.439  1.00 66.90           C  
ANISOU 4766  CG  GLU A 653     7494   8798   9125   -184    181   -288       C  
ATOM   4767  CD  GLU A 653      43.204  55.427  11.651  1.00 71.00           C  
ANISOU 4767  CD  GLU A 653     8058   9320   9597   -168    198   -235       C  
ATOM   4768  OE1 GLU A 653      43.218  54.388  10.954  1.00 72.86           O  
ANISOU 4768  OE1 GLU A 653     8332   9565   9785   -150    189   -179       O  
ATOM   4769  OE2 GLU A 653      42.199  56.155  11.734  1.00 75.37           O  
ANISOU 4769  OE2 GLU A 653     8605   9866  10164   -174    219   -253       O  
ATOM   4770  N   GLY A 654      46.617  54.220  15.116  1.00 55.14           N  
ANISOU 4770  N   GLY A 654     5989   7418   7542   -221     53   -375       N  
ATOM   4771  CA  GLY A 654      46.450  54.111  16.556  1.00 56.99           C  
ANISOU 4771  CA  GLY A 654     6220   7711   7723   -245     12   -433       C  
ATOM   4772  C   GLY A 654      47.505  54.867  17.338  1.00 57.70           C  
ANISOU 4772  C   GLY A 654     6254   7798   7871   -257     -3   -504       C  
ATOM   4773  O   GLY A 654      47.189  55.812  18.062  1.00 58.55           O  
ANISOU 4773  O   GLY A 654     6328   7912   8005   -274      3   -568       O  
ATOM   4774  N   LEU A 655      48.764  54.466  17.167  1.00 57.22           N  
ANISOU 4774  N   LEU A 655     6179   7726   7835   -247    -23   -494       N  
ATOM   4775  CA  LEU A 655      49.870  55.009  17.959  1.00 56.21           C  
ANISOU 4775  CA  LEU A 655     5999   7601   7758   -257    -47   -562       C  
ATOM   4776  C   LEU A 655      50.319  56.413  17.573  1.00 55.44           C  
ANISOU 4776  C   LEU A 655     5842   7440   7784   -258     -4   -600       C  
ATOM   4777  O   LEU A 655      50.857  57.136  18.409  1.00 58.26           O  
ANISOU 4777  O   LEU A 655     6149   7802   8184   -272    -19   -676       O  
ATOM   4778  CB  LEU A 655      51.067  54.062  17.901  1.00 57.56           C  
ANISOU 4778  CB  LEU A 655     6175   7780   7917   -246    -84   -538       C  
ATOM   4779  CG  LEU A 655      50.774  52.614  18.298  1.00 56.98           C  
ANISOU 4779  CG  LEU A 655     6156   7765   7729   -244   -128   -497       C  
ATOM   4780  CD1 LEU A 655      51.902  51.726  17.800  1.00 58.16           C  
ANISOU 4780  CD1 LEU A 655     6311   7901   7887   -227   -149   -456       C  
ATOM   4781  CD2 LEU A 655      50.574  52.469  19.802  1.00 53.76           C  
ANISOU 4781  CD2 LEU A 655     5747   7427   7251   -262   -176   -553       C  
ATOM   4782  N   GLY A 656      50.115  56.802  16.319  1.00 53.67           N  
ANISOU 4782  N   GLY A 656     5621   7156   7617   -243     49   -550       N  
ATOM   4783  CA  GLY A 656      50.610  58.095  15.834  1.00 56.83           C  
ANISOU 4783  CA  GLY A 656     5964   7488   8140   -241     95   -575       C  
ATOM   4784  C   GLY A 656      52.113  58.258  16.045  1.00 59.57           C  
ANISOU 4784  C   GLY A 656     6263   7815   8556   -241     79   -611       C  
ATOM   4785  O   GLY A 656      52.898  57.354  15.723  1.00 59.58           O  
ANISOU 4785  O   GLY A 656     6281   7821   8536   -228     58   -573       O  
ATOM   4786  N   GLY A 657      52.504  59.404  16.600  1.00 61.68           N  
ANISOU 4786  N   GLY A 657     6468   8060   8909   -254     89   -686       N  
ATOM   4787  CA  GLY A 657      53.891  59.674  16.993  1.00 60.14           C  
ANISOU 4787  CA  GLY A 657     6218   7849   8784   -257     69   -738       C  
ATOM   4788  C   GLY A 657      54.615  58.527  17.695  1.00 62.73           C  
ANISOU 4788  C   GLY A 657     6563   8235   9037   -257      2   -745       C  
ATOM   4789  O   GLY A 657      55.812  58.324  17.482  1.00 63.22           O  
ANISOU 4789  O   GLY A 657     6601   8274   9147   -249     -8   -745       O  
ATOM   4790  N   ASN A 658      53.904  57.753  18.511  1.00 61.62           N  
ANISOU 4790  N   ASN A 658     6466   8167   8779   -265    -42   -747       N  
ATOM   4791  CA  ASN A 658      54.538  56.663  19.245  1.00 60.98           C  
ANISOU 4791  CA  ASN A 658     6403   8144   8623   -264   -107   -752       C  
ATOM   4792  C   ASN A 658      54.977  55.472  18.408  1.00 61.14           C  
ANISOU 4792  C   ASN A 658     6465   8156   8610   -245   -114   -670       C  
ATOM   4793  O   ASN A 658      55.515  54.509  18.954  1.00 62.08           O  
ANISOU 4793  O   ASN A 658     6600   8319   8670   -242   -167   -666       O  
ATOM   4794  CB  ASN A 658      53.649  56.200  20.387  1.00 66.03           C  
ANISOU 4794  CB  ASN A 658     7075   8863   9149   -278   -148   -776       C  
ATOM   4795  CG  ASN A 658      53.710  57.135  21.570  1.00 69.17           C  
ANISOU 4795  CG  ASN A 658     7423   9288   9570   -297   -167   -878       C  
ATOM   4796  OD1 ASN A 658      54.755  57.300  22.194  1.00 73.18           O  
ANISOU 4796  OD1 ASN A 658     7888   9806  10111   -299   -202   -935       O  
ATOM   4797  ND2 ASN A 658      52.594  57.765  21.876  1.00 73.62           N  
ANISOU 4797  ND2 ASN A 658     7990   9863  10119   -310   -145   -904       N  
ATOM   4798  N   ILE A 659      54.756  55.523  17.094  1.00 58.07           N  
ANISOU 4798  N   ILE A 659     6092   7713   8258   -230    -61   -604       N  
ATOM   4799  CA  ILE A 659      55.281  54.475  16.225  1.00 54.93           C  
ANISOU 4799  CA  ILE A 659     5726   7302   7841   -211    -64   -532       C  
ATOM   4800  C   ILE A 659      56.698  54.807  15.705  1.00 55.73           C  
ANISOU 4800  C   ILE A 659     5779   7349   8046   -202    -49   -540       C  
ATOM   4801  O   ILE A 659      57.359  53.959  15.097  1.00 51.94           O  
ANISOU 4801  O   ILE A 659     5317   6859   7561   -187    -56   -492       O  
ATOM   4802  CB  ILE A 659      54.321  54.138  15.066  1.00 51.63           C  
ANISOU 4802  CB  ILE A 659     5359   6865   7394   -197    -21   -452       C  
ATOM   4803  CG1 ILE A 659      54.561  52.698  14.607  1.00 51.34           C  
ANISOU 4803  CG1 ILE A 659     5370   6847   7290   -181    -46   -387       C  
ATOM   4804  CG2 ILE A 659      54.445  55.144  13.921  1.00 52.12           C  
ANISOU 4804  CG2 ILE A 659     5394   6852   7558   -185     48   -432       C  
ATOM   4805  CD1 ILE A 659      53.392  52.059  13.894  1.00 52.08           C  
ANISOU 4805  CD1 ILE A 659     5522   6951   7315   -171    -27   -321       C  
ATOM   4806  N   GLU A 660      57.138  56.041  15.955  1.00 58.73           N  
ANISOU 4806  N   GLU A 660     6098   7693   8525   -211    -28   -603       N  
ATOM   4807  CA  GLU A 660      58.435  56.559  15.496  1.00 60.80           C  
ANISOU 4807  CA  GLU A 660     6304   7896   8901   -205     -6   -620       C  
ATOM   4808  C   GLU A 660      59.604  55.619  15.792  1.00 59.18           C  
ANISOU 4808  C   GLU A 660     6094   7710   8680   -199    -57   -623       C  
ATOM   4809  O   GLU A 660      60.314  55.212  14.882  1.00 58.55           O  
ANISOU 4809  O   GLU A 660     6017   7594   8637   -183    -38   -575       O  
ATOM   4810  CB  GLU A 660      58.691  57.940  16.098  1.00 63.97           C  
ANISOU 4810  CB  GLU A 660     6637   8271   9399   -221      8   -705       C  
ATOM   4811  CG  GLU A 660      59.795  58.729  15.420  1.00 68.45           C  
ANISOU 4811  CG  GLU A 660     7144   8761  10104   -215     52   -716       C  
ATOM   4812  CD  GLU A 660      61.182  58.309  15.877  1.00 70.34           C  
ANISOU 4812  CD  GLU A 660     7348   9006  10373   -214      7   -754       C  
ATOM   4813  OE1 GLU A 660      61.364  58.052  17.091  1.00 71.35           O  
ANISOU 4813  OE1 GLU A 660     7464   9191  10453   -225    -57   -816       O  
ATOM   4814  OE2 GLU A 660      62.084  58.229  15.016  1.00 68.64           O  
ANISOU 4814  OE2 GLU A 660     7115   8738  10226   -201     36   -721       O  
ATOM   4815  N   GLN A 661      59.782  55.262  17.056  1.00 62.78           N  
ANISOU 4815  N   GLN A 661     6544   8228   9081   -210   -123   -677       N  
ATOM   4816  CA  GLN A 661      60.874  54.390  17.460  1.00 67.09           C  
ANISOU 4816  CA  GLN A 661     7083   8797   9610   -204   -179   -684       C  
ATOM   4817  C   GLN A 661      60.946  53.099  16.648  1.00 66.76           C  
ANISOU 4817  C   GLN A 661     7096   8758   9513   -186   -182   -597       C  
ATOM   4818  O   GLN A 661      62.033  52.633  16.305  1.00 70.12           O  
ANISOU 4818  O   GLN A 661     7504   9161   9976   -175   -194   -585       O  
ATOM   4819  CB  GLN A 661      60.794  54.076  18.952  1.00 75.59           C  
ANISOU 4819  CB  GLN A 661     8160   9952  10608   -215   -251   -743       C  
ATOM   4820  CG  GLN A 661      61.290  55.209  19.845  1.00 89.24           C  
ANISOU 4820  CG  GLN A 661     9819  11679  12408   -229   -264   -846       C  
ATOM   4821  CD  GLN A 661      61.225  54.868  21.328  1.00 95.44           C  
ANISOU 4821  CD  GLN A 661    10607  12549  13107   -238   -338   -904       C  
ATOM   4822  OE1 GLN A 661      61.641  53.785  21.751  1.00 97.56           O  
ANISOU 4822  OE1 GLN A 661    10901  12863  13305   -230   -393   -884       O  
ATOM   4823  NE2 GLN A 661      60.703  55.799  22.127  1.00 96.49           N  
ANISOU 4823  NE2 GLN A 661    10713  12704  13247   -254   -338   -977       N  
ATOM   4824  N   LEU A 662      59.792  52.527  16.329  1.00 63.49           N  
ANISOU 4824  N   LEU A 662     6742   8367   9012   -183   -172   -540       N  
ATOM   4825  CA  LEU A 662      59.755  51.261  15.607  1.00 60.01           C  
ANISOU 4825  CA  LEU A 662     6354   7934   8515   -167   -178   -461       C  
ATOM   4826  C   LEU A 662      60.140  51.430  14.134  1.00 56.65           C  
ANISOU 4826  C   LEU A 662     5923   7439   8163   -150   -116   -409       C  
ATOM   4827  O   LEU A 662      60.845  50.589  13.563  1.00 55.15           O  
ANISOU 4827  O   LEU A 662     5744   7237   7975   -136   -124   -369       O  
ATOM   4828  CB  LEU A 662      58.374  50.622  15.746  1.00 59.16           C  
ANISOU 4828  CB  LEU A 662     6309   7872   8297   -169   -185   -422       C  
ATOM   4829  CG  LEU A 662      58.014  50.154  17.160  1.00 61.23           C  
ANISOU 4829  CG  LEU A 662     6586   8209   8468   -183   -248   -457       C  
ATOM   4830  CD1 LEU A 662      56.505  50.166  17.396  1.00 59.09           C  
ANISOU 4830  CD1 LEU A 662     6358   7972   8121   -192   -237   -444       C  
ATOM   4831  CD2 LEU A 662      58.600  48.779  17.437  1.00 58.71           C  
ANISOU 4831  CD2 LEU A 662     6292   7924   8090   -173   -303   -426       C  
ATOM   4832  N   VAL A 663      59.669  52.520  13.536  1.00 53.89           N  
ANISOU 4832  N   VAL A 663     5558   7046   7873   -151    -56   -410       N  
ATOM   4833  CA  VAL A 663      59.934  52.840  12.135  1.00 55.95           C  
ANISOU 4833  CA  VAL A 663     5814   7242   8203   -134     10   -360       C  
ATOM   4834  C   VAL A 663      61.407  53.214  11.954  1.00 54.86           C  
ANISOU 4834  C   VAL A 663     5617   7056   8171   -131     19   -388       C  
ATOM   4835  O   VAL A 663      62.016  52.900  10.925  1.00 54.15           O  
ANISOU 4835  O   VAL A 663     5529   6927   8117   -115     50   -341       O  
ATOM   4836  CB  VAL A 663      58.995  53.973  11.643  1.00 56.27           C  
ANISOU 4836  CB  VAL A 663     5851   7250   8281   -136     70   -354       C  
ATOM   4837  CG1 VAL A 663      59.481  54.584  10.337  1.00 56.41           C  
ANISOU 4837  CG1 VAL A 663     5848   7195   8391   -119    140   -315       C  
ATOM   4838  CG2 VAL A 663      57.585  53.439  11.459  1.00 57.38           C  
ANISOU 4838  CG2 VAL A 663     6054   7427   8320   -133     70   -309       C  
ATOM   4839  N   ALA A 664      61.961  53.860  12.978  1.00 53.48           N  
ANISOU 4839  N   ALA A 664     5390   6888   8043   -147    -10   -467       N  
ATOM   4840  CA  ALA A 664      63.380  54.203  13.038  1.00 55.82           C  
ANISOU 4840  CA  ALA A 664     5625   7146   8440   -147    -12   -508       C  
ATOM   4841  C   ALA A 664      64.267  52.974  12.917  1.00 54.81           C  
ANISOU 4841  C   ALA A 664     5510   7031   8282   -135    -52   -481       C  
ATOM   4842  O   ALA A 664      65.348  53.061  12.371  1.00 56.11           O  
ANISOU 4842  O   ALA A 664     5640   7149   8530   -127    -31   -480       O  
ATOM   4843  CB  ALA A 664      63.693  54.948  14.322  1.00 53.35           C  
ANISOU 4843  CB  ALA A 664     5258   6851   8160   -166    -50   -604       C  
ATOM   4844  N   ARG A 665      63.789  51.831  13.401  1.00 54.61           N  
ANISOU 4844  N   ARG A 665     5537   7068   8144   -134   -106   -457       N  
ATOM   4845  CA  ARG A 665      64.570  50.601  13.416  1.00 54.83           C  
ANISOU 4845  CA  ARG A 665     5579   7116   8140   -123   -151   -433       C  
ATOM   4846  C   ARG A 665      64.219  49.691  12.257  1.00 52.26           C  
ANISOU 4846  C   ARG A 665     5306   6779   7771   -106   -123   -348       C  
ATOM   4847  O   ARG A 665      64.513  48.502  12.292  1.00 54.18           O  
ANISOU 4847  O   ARG A 665     5577   7048   7962    -97   -163   -318       O  
ATOM   4848  CB  ARG A 665      64.373  49.852  14.743  1.00 58.60           C  
ANISOU 4848  CB  ARG A 665     6075   7667   8522   -132   -232   -462       C  
ATOM   4849  CG  ARG A 665      64.955  50.577  15.947  1.00 66.20           C  
ANISOU 4849  CG  ARG A 665     6982   8648   9523   -145   -272   -552       C  
ATOM   4850  CD  ARG A 665      65.044  49.694  17.181  1.00 74.44           C  
ANISOU 4850  CD  ARG A 665     8042   9765  10476   -148   -356   -574       C  
ATOM   4851  NE  ARG A 665      63.920  49.883  18.098  1.00 86.24           N  
ANISOU 4851  NE  ARG A 665     9563  11317  11887   -161   -377   -597       N  
ATOM   4852  CZ  ARG A 665      62.892  49.041  18.216  1.00 93.06           C  
ANISOU 4852  CZ  ARG A 665    10490  12226  12641   -161   -390   -546       C  
ATOM   4853  NH1 ARG A 665      62.827  47.934  17.475  1.00 95.02           N  
ANISOU 4853  NH1 ARG A 665    10782  12469  12850   -147   -388   -471       N  
ATOM   4854  NH2 ARG A 665      61.920  49.304  19.080  1.00 94.83           N  
ANISOU 4854  NH2 ARG A 665    10732  12500  12797   -174   -405   -573       N  
ATOM   4855  N   SER A 666      63.635  50.250  11.206  1.00 51.75           N  
ANISOU 4855  N   SER A 666     5255   6676   7733    -99    -54   -308       N  
ATOM   4856  CA  SER A 666      62.903  49.430  10.238  1.00 51.42           C  
ANISOU 4856  CA  SER A 666     5272   6639   7626    -83    -32   -231       C  
ATOM   4857  C   SER A 666      63.196  49.774   8.783  1.00 49.07           C  
ANISOU 4857  C   SER A 666     4970   6282   7394    -65     41   -184       C  
ATOM   4858  O   SER A 666      63.523  50.911   8.474  1.00 49.40           O  
ANISOU 4858  O   SER A 666     4970   6275   7527    -67     89   -204       O  
ATOM   4859  CB  SER A 666      61.389  49.600  10.495  1.00 50.85           C  
ANISOU 4859  CB  SER A 666     5242   6602   7478    -90    -29   -221       C  
ATOM   4860  OG  SER A 666      60.646  48.630   9.775  1.00 52.06           O  
ANISOU 4860  OG  SER A 666     5453   6772   7554    -77    -23   -154       O  
ATOM   4861  N   ASN A 667      63.030  48.795   7.893  1.00 49.16           N  
ANISOU 4861  N   ASN A 667     5024   6297   7358    -47     50   -121       N  
ATOM   4862  CA  ASN A 667      63.107  49.040   6.444  1.00 50.26           C  
ANISOU 4862  CA  ASN A 667     5169   6388   7538    -27    121    -69       C  
ATOM   4863  C   ASN A 667      61.738  49.159   5.766  1.00 51.03           C  
ANISOU 4863  C   ASN A 667     5314   6496   7578    -18    156    -22       C  
ATOM   4864  O   ASN A 667      61.636  49.087   4.524  1.00 49.11           O  
ANISOU 4864  O   ASN A 667     5090   6227   7341      4    206     31       O  
ATOM   4865  CB  ASN A 667      63.921  47.944   5.756  1.00 48.37           C  
ANISOU 4865  CB  ASN A 667     4940   6142   7295    -11    115    -33       C  
ATOM   4866  CG  ASN A 667      63.274  46.575   5.877  1.00 49.46           C  
ANISOU 4866  CG  ASN A 667     5133   6332   7326     -6     68      0       C  
ATOM   4867  OD1 ASN A 667      62.669  46.241   6.894  1.00 49.73           O  
ANISOU 4867  OD1 ASN A 667     5186   6412   7296    -20     16    -21       O  
ATOM   4868  ND2 ASN A 667      63.418  45.766   4.841  1.00 50.59           N  
ANISOU 4868  ND2 ASN A 667     5302   6466   7452     14     87     50       N  
ATOM   4869  N   ILE A 668      60.688  49.344   6.571  1.00 52.78           N  
ANISOU 4869  N   ILE A 668     5555   6755   7744    -32    130    -43       N  
ATOM   4870  CA  ILE A 668      59.320  49.389   6.034  1.00 50.83           C  
ANISOU 4870  CA  ILE A 668     5353   6521   7437    -24    155     -3       C  
ATOM   4871  C   ILE A 668      59.202  50.288   4.790  1.00 51.06           C  
ANISOU 4871  C   ILE A 668     5376   6500   7525     -6    233     33       C  
ATOM   4872  O   ILE A 668      58.617  49.891   3.781  1.00 50.31           O  
ANISOU 4872  O   ILE A 668     5319   6406   7389     15    260     88       O  
ATOM   4873  CB  ILE A 668      58.253  49.709   7.123  1.00 52.30           C  
ANISOU 4873  CB  ILE A 668     5551   6748   7573    -44    125    -39       C  
ATOM   4874  CG1 ILE A 668      56.819  49.484   6.600  1.00 50.78           C  
ANISOU 4874  CG1 ILE A 668     5411   6577   7309    -35    141      3       C  
ATOM   4875  CG2 ILE A 668      58.404  51.126   7.658  1.00 53.05           C  
ANISOU 4875  CG2 ILE A 668     5595   6815   7746    -60    146    -94       C  
ATOM   4876  CD1 ILE A 668      56.581  48.189   5.850  1.00 46.95           C  
ANISOU 4876  CD1 ILE A 668     4973   6111   6756    -16    131     59       C  
ATOM   4877  N   LEU A 669      59.809  51.466   4.832  1.00 50.75           N  
ANISOU 4877  N   LEU A 669     5285   6415   7584    -12    268      3       N  
ATOM   4878  CA  LEU A 669      59.753  52.363   3.685  1.00 51.62           C  
ANISOU 4878  CA  LEU A 669     5385   6473   7754      6    344     41       C  
ATOM   4879  C   LEU A 669      60.414  51.830   2.411  1.00 53.03           C  
ANISOU 4879  C   LEU A 669     5576   6627   7946     32    382     97       C  
ATOM   4880  O   LEU A 669      59.949  52.117   1.301  1.00 50.46           O  
ANISOU 4880  O   LEU A 669     5271   6283   7619     54    435    149       O  
ATOM   4881  CB  LEU A 669      60.338  53.717   4.055  1.00 54.48           C  
ANISOU 4881  CB  LEU A 669     5685   6788   8228     -7    375     -5       C  
ATOM   4882  CG  LEU A 669      59.382  54.570   4.887  1.00 56.58           C  
ANISOU 4882  CG  LEU A 669     5942   7066   8489    -26    367    -46       C  
ATOM   4883  CD1 LEU A 669      60.160  55.541   5.746  1.00 57.16           C  
ANISOU 4883  CD1 LEU A 669     5949   7111   8660    -47    364   -118       C  
ATOM   4884  CD2 LEU A 669      58.398  55.310   3.986  1.00 59.57           C  
ANISOU 4884  CD2 LEU A 669     6340   7420   8873    -10    426      0       C  
ATOM   4885  N   THR A 670      61.492  51.058   2.552  1.00 51.60           N  
ANISOU 4885  N   THR A 670     5381   6448   7777     31    353     86       N  
ATOM   4886  CA  THR A 670      62.127  50.535   1.355  1.00 53.43           C  
ANISOU 4886  CA  THR A 670     5622   6658   8021     55    389    136       C  
ATOM   4887  C   THR A 670      61.276  49.389   0.816  1.00 52.54           C  
ANISOU 4887  C   THR A 670     5572   6589   7802     72    371    182       C  
ATOM   4888  O   THR A 670      61.210  49.178  -0.392  1.00 53.89           O  
ANISOU 4888  O   THR A 670     5765   6748   7961     97    414    234       O  
ATOM   4889  CB  THR A 670      63.649  50.180   1.503  1.00 55.90           C  
ANISOU 4889  CB  THR A 670     5893   6947   8397     51    377    111       C  
ATOM   4890  OG1 THR A 670      63.858  48.760   1.415  1.00 54.85           O  
ANISOU 4890  OG1 THR A 670     5792   6849   8200     59    333    129       O  
ATOM   4891  CG2 THR A 670      64.302  50.782   2.798  1.00 54.12           C  
ANISOU 4891  CG2 THR A 670     5614   6714   8235     24    341     36       C  
ATOM   4892  N   LEU A 671      60.612  48.666   1.712  1.00 50.83           N  
ANISOU 4892  N   LEU A 671     5382   6423   7508     58    308    163       N  
ATOM   4893  CA  LEU A 671      59.617  47.668   1.314  1.00 50.70           C  
ANISOU 4893  CA  LEU A 671     5424   6448   7393     71    289    202       C  
ATOM   4894  C   LEU A 671      58.397  48.307   0.619  1.00 55.15           C  
ANISOU 4894  C   LEU A 671     6014   7009   7930     84    332    235       C  
ATOM   4895  O   LEU A 671      57.945  47.831  -0.434  1.00 53.04           O  
ANISOU 4895  O   LEU A 671     5783   6749   7621    109    355    283       O  
ATOM   4896  CB  LEU A 671      59.178  46.854   2.522  1.00 49.06           C  
ANISOU 4896  CB  LEU A 671     5233   6290   7116     50    216    172       C  
ATOM   4897  CG  LEU A 671      60.297  46.052   3.187  1.00 48.98           C  
ANISOU 4897  CG  LEU A 671     5204   6289   7119     41    166    146       C  
ATOM   4898  CD1 LEU A 671      59.731  45.210   4.321  1.00 47.12           C  
ANISOU 4898  CD1 LEU A 671     4992   6106   6804     24     97    128       C  
ATOM   4899  CD2 LEU A 671      61.059  45.190   2.181  1.00 46.26           C  
ANISOU 4899  CD2 LEU A 671     4866   5930   6782     62    181    183       C  
ATOM   4900  N   MET A 672      57.893  49.403   1.193  1.00 54.47           N  
ANISOU 4900  N   MET A 672     5910   6914   7873     70    343    207       N  
ATOM   4901  CA  MET A 672      56.773  50.139   0.608  1.00 53.81           C  
ANISOU 4901  CA  MET A 672     5845   6823   7775     82    383    234       C  
ATOM   4902  C   MET A 672      57.030  50.553  -0.814  1.00 55.54           C  
ANISOU 4902  C   MET A 672     6065   7005   8031    112    451    287       C  
ATOM   4903  O   MET A 672      56.124  50.559  -1.635  1.00 53.98           O  
ANISOU 4903  O   MET A 672     5903   6817   7791    134    475    329       O  
ATOM   4904  CB  MET A 672      56.494  51.388   1.408  1.00 55.85           C  
ANISOU 4904  CB  MET A 672     6069   7064   8085     61    392    192       C  
ATOM   4905  CG  MET A 672      55.368  51.210   2.389  1.00 59.78           C  
ANISOU 4905  CG  MET A 672     6590   7607   8516     42    346    163       C  
ATOM   4906  SD  MET A 672      55.113  52.734   3.302  1.00 68.95           S  
ANISOU 4906  SD  MET A 672     7706   8746   9746     18    360    107       S  
ATOM   4907  CE  MET A 672      55.986  52.183   4.746  1.00 55.68           C  
ANISOU 4907  CE  MET A 672     5999   7094   8062    -11    291     42       C  
ATOM   4908  N   TYR A 673      58.278  50.904  -1.100  1.00 58.89           N  
ANISOU 4908  N   TYR A 673     6451   7388   8536    115    482    284       N  
ATOM   4909  CA  TYR A 673      58.623  51.406  -2.406  1.00 57.75           C  
ANISOU 4909  CA  TYR A 673     6303   7204   8436    143    553    334       C  
ATOM   4910  C   TYR A 673      58.294  50.352  -3.470  1.00 55.86           C  
ANISOU 4910  C   TYR A 673     6113   6994   8119    172    556    386       C  
ATOM   4911  O   TYR A 673      57.815  50.694  -4.543  1.00 55.47           O  
ANISOU 4911  O   TYR A 673     6084   6935   8057    200    604    434       O  
ATOM   4912  CB  TYR A 673      60.088  51.875  -2.427  1.00 60.81           C  
ANISOU 4912  CB  TYR A 673     6637   7542   8926    137    582    317       C  
ATOM   4913  CG  TYR A 673      60.493  52.693  -3.640  1.00 62.12           C  
ANISOU 4913  CG  TYR A 673     6789   7659   9157    162    665    364       C  
ATOM   4914  CD1 TYR A 673      59.657  53.690  -4.166  1.00 62.64           C  
ANISOU 4914  CD1 TYR A 673     6862   7705   9234    176    714    396       C  
ATOM   4915  CD2 TYR A 673      61.721  52.483  -4.253  1.00 62.72           C  
ANISOU 4915  CD2 TYR A 673     6842   7704   9284    172    697    378       C  
ATOM   4916  CE1 TYR A 673      60.040  54.438  -5.272  1.00 64.09           C  
ANISOU 4916  CE1 TYR A 673     7033   7844   9476    201    792    445       C  
ATOM   4917  CE2 TYR A 673      62.116  53.223  -5.363  1.00 63.05           C  
ANISOU 4917  CE2 TYR A 673     6871   7700   9385    196    777    425       C  
ATOM   4918  CZ  TYR A 673      61.278  54.195  -5.872  1.00 65.99           C  
ANISOU 4918  CZ  TYR A 673     7253   8056   9765    211    825    460       C  
ATOM   4919  OH  TYR A 673      61.684  54.925  -6.971  1.00 63.96           O  
ANISOU 4919  OH  TYR A 673     6984   7754   9566    236    907    511       O  
ATOM   4920  N   GLN A 674      58.497  49.075  -3.154  1.00 56.29           N  
ANISOU 4920  N   GLN A 674     6186   7084   8119    167    503    375       N  
ATOM   4921  CA  GLN A 674      58.141  47.993  -4.090  1.00 59.67           C  
ANISOU 4921  CA  GLN A 674     6659   7542   8472    193    500    416       C  
ATOM   4922  C   GLN A 674      56.659  47.663  -4.100  1.00 58.78           C  
ANISOU 4922  C   GLN A 674     6591   7470   8272    199    476    429       C  
ATOM   4923  O   GLN A 674      56.121  47.308  -5.144  1.00 59.49           O  
ANISOU 4923  O   GLN A 674     6714   7574   8315    228    497    470       O  
ATOM   4924  CB  GLN A 674      58.950  46.712  -3.848  1.00 64.60           C  
ANISOU 4924  CB  GLN A 674     7283   8183   9078    187    455    403       C  
ATOM   4925  CG  GLN A 674      60.026  46.469  -4.902  1.00 70.85           C  
ANISOU 4925  CG  GLN A 674     8064   8949   9908    209    498    430       C  
ATOM   4926  CD  GLN A 674      61.182  47.436  -4.756  1.00 73.69           C  
ANISOU 4926  CD  GLN A 674     8369   9256  10373    199    535    413       C  
ATOM   4927  OE1 GLN A 674      61.736  47.576  -3.668  1.00 81.54           O  
ANISOU 4927  OE1 GLN A 674     9330  10242  11408    172    500    365       O  
ATOM   4928  NE2 GLN A 674      61.546  48.116  -5.839  1.00 73.48           N  
ANISOU 4928  NE2 GLN A 674     8333   9195  10391    222    607    450       N  
ATOM   4929  N   CYS A 675      56.026  47.753  -2.930  1.00 55.58           N  
ANISOU 4929  N   CYS A 675     6186   7086   7847    172    432    391       N  
ATOM   4930  CA  CYS A 675      54.588  47.567  -2.777  1.00 53.09           C  
ANISOU 4930  CA  CYS A 675     5908   6806   7459    173    410    396       C  
ATOM   4931  C   CYS A 675      53.817  48.581  -3.608  1.00 54.86           C  
ANISOU 4931  C   CYS A 675     6139   7012   7692    194    463    428       C  
ATOM   4932  O   CYS A 675      52.831  48.237  -4.261  1.00 53.35           O  
ANISOU 4932  O   CYS A 675     5986   6846   7440    215    465    457       O  
ATOM   4933  CB  CYS A 675      54.194  47.729  -1.321  1.00 49.82           C  
ANISOU 4933  CB  CYS A 675     5483   6410   7037    138    363    346       C  
ATOM   4934  SG  CYS A 675      54.827  46.405  -0.293  1.00 52.79           S  
ANISOU 4934  SG  CYS A 675     5860   6818   7381    116    292    314       S  
ATOM   4935  N   MET A 676      54.284  49.825  -3.585  1.00 53.24           N  
ANISOU 4935  N   MET A 676     5897   6764   7569    190    506    423       N  
ATOM   4936  CA  MET A 676      53.622  50.903  -4.292  1.00 55.43           C  
ANISOU 4936  CA  MET A 676     6176   7018   7867    210    559    454       C  
ATOM   4937  C   MET A 676      53.668  50.672  -5.798  1.00 56.42           C  
ANISOU 4937  C   MET A 676     6327   7141   7970    251    603    515       C  
ATOM   4938  O   MET A 676      52.886  51.261  -6.547  1.00 56.61           O  
ANISOU 4938  O   MET A 676     6367   7161   7982    275    638    551       O  
ATOM   4939  CB  MET A 676      54.273  52.238  -3.949  1.00 58.25           C  
ANISOU 4939  CB  MET A 676     6483   7323   8327    196    597    435       C  
ATOM   4940  CG  MET A 676      53.954  52.775  -2.559  1.00 61.51           C  
ANISOU 4940  CG  MET A 676     6871   7739   8763    160    563    376       C  
ATOM   4941  SD  MET A 676      54.974  54.205  -2.107  1.00 66.63           S  
ANISOU 4941  SD  MET A 676     7451   8324   9543    142    604    342       S  
ATOM   4942  CE  MET A 676      55.368  54.874  -3.717  1.00 58.67           C  
ANISOU 4942  CE  MET A 676     6439   7266   8586    181    690    414       C  
ATOM   4943  N   GLN A 677      54.585  49.810  -6.228  1.00 57.56           N  
ANISOU 4943  N   GLN A 677     6473   7290   8109    260    600    525       N  
ATOM   4944  CA  GLN A 677      54.790  49.547  -7.647  1.00 59.62           C  
ANISOU 4944  CA  GLN A 677     6754   7549   8349    299    643    578       C  
ATOM   4945  C   GLN A 677      54.246  48.193  -8.064  1.00 58.41           C  
ANISOU 4945  C   GLN A 677     6644   7445   8103    314    605    588       C  
ATOM   4946  O   GLN A 677      54.412  47.796  -9.213  1.00 59.56           O  
ANISOU 4946  O   GLN A 677     6808   7599   8222    347    633    626       O  
ATOM   4947  CB  GLN A 677      56.273  49.631  -7.999  1.00 59.02           C  
ANISOU 4947  CB  GLN A 677     6645   7436   8343    301    679    584       C  
ATOM   4948  CG  GLN A 677      56.883  50.983  -7.702  1.00 61.97           C  
ANISOU 4948  CG  GLN A 677     6972   7755   8819    288    723    575       C  
ATOM   4949  CD  GLN A 677      58.365  51.042  -8.014  1.00 63.69           C  
ANISOU 4949  CD  GLN A 677     7155   7935   9111    289    758    577       C  
ATOM   4950  OE1 GLN A 677      58.761  51.126  -9.175  1.00 65.03           O  
ANISOU 4950  OE1 GLN A 677     7330   8090   9289    319    813    624       O  
ATOM   4951  NE2 GLN A 677      59.195  51.018  -6.972  1.00 64.67           N  
ANISOU 4951  NE2 GLN A 677     7240   8043   9289    256    727    526       N  
ATOM   4952  N   ASP A 678      53.598  47.497  -7.130  1.00 57.14           N  
ANISOU 4952  N   ASP A 678     6498   7319   7895    291    543    554       N  
ATOM   4953  CA  ASP A 678      53.035  46.165  -7.380  1.00 59.60           C  
ANISOU 4953  CA  ASP A 678     6847   7675   8123    302    503    557       C  
ATOM   4954  C   ASP A 678      51.932  46.148  -8.442  1.00 61.91           C  
ANISOU 4954  C   ASP A 678     7176   7991   8356    337    521    594       C  
ATOM   4955  O   ASP A 678      51.170  47.117  -8.564  1.00 62.77           O  
ANISOU 4955  O   ASP A 678     7287   8091   8472    345    545    607       O  
ATOM   4956  CB  ASP A 678      52.489  45.586  -6.079  1.00 58.70           C  
ANISOU 4956  CB  ASP A 678     6739   7589   7977    268    438    515       C  
ATOM   4957  CG  ASP A 678      52.298  44.082  -6.145  1.00 62.76           C  
ANISOU 4957  CG  ASP A 678     7280   8140   8426    272    393    512       C  
ATOM   4958  OD1 ASP A 678      51.245  43.635  -6.652  1.00 65.08           O  
ANISOU 4958  OD1 ASP A 678     7607   8463   8659    290    385    527       O  
ATOM   4959  OD2 ASP A 678      53.200  43.345  -5.686  1.00 59.61           O  
ANISOU 4959  OD2 ASP A 678     6867   7740   8041    257    366    495       O  
ATOM   4960  N   LYS A 679      51.830  45.038  -9.181  1.00 62.85           N  
ANISOU 4960  N   LYS A 679     7322   8141   8419    360    508    608       N  
ATOM   4961  CA  LYS A 679      50.776  44.859 -10.197  1.00 65.40           C  
ANISOU 4961  CA  LYS A 679     7679   8491   8677    396    518    637       C  
ATOM   4962  C   LYS A 679      49.368  44.764  -9.584  1.00 62.85           C  
ANISOU 4962  C   LYS A 679     7377   8196   8309    384    478    618       C  
ATOM   4963  O   LYS A 679      48.393  45.127 -10.223  1.00 59.98           O  
ANISOU 4963  O   LYS A 679     7033   7845   7911    410    492    639       O  
ATOM   4964  CB  LYS A 679      51.045  43.637 -11.099  1.00 70.00           C  
ANISOU 4964  CB  LYS A 679     8282   9102   9213    422    510    649       C  
ATOM   4965  CG  LYS A 679      51.127  42.294 -10.365  1.00 79.01           C  
ANISOU 4965  CG  LYS A 679     9428  10265  10327    398    450    614       C  
ATOM   4966  CD  LYS A 679      50.590  41.104 -11.172  1.00 83.87           C  
ANISOU 4966  CD  LYS A 679    10072  10919  10875    425    430    620       C  
ATOM   4967  CE  LYS A 679      49.194  40.653 -10.714  1.00 84.03           C  
ANISOU 4967  CE  LYS A 679    10116  10971  10841    417    386    601       C  
ATOM   4968  NZ  LYS A 679      49.177  39.966  -9.384  1.00 79.44           N  
ANISOU 4968  NZ  LYS A 679     9529  10394  10263    377    332    566       N  
ATOM   4969  N   MET A 680      49.277  44.276  -8.348  1.00 61.27           N  
ANISOU 4969  N   MET A 680     7170   8003   8105    347    429    578       N  
ATOM   4970  CA  MET A 680      47.996  44.046  -7.696  1.00 60.91           C  
ANISOU 4970  CA  MET A 680     7142   7984   8015    333    390    557       C  
ATOM   4971  C   MET A 680      47.443  45.297  -7.022  1.00 62.49           C  
ANISOU 4971  C   MET A 680     7329   8167   8248    316    402    546       C  
ATOM   4972  O   MET A 680      48.046  45.812  -6.078  1.00 63.49           O  
ANISOU 4972  O   MET A 680     7427   8271   8424    285    399    521       O  
ATOM   4973  CB  MET A 680      48.122  42.925  -6.672  1.00 62.35           C  
ANISOU 4973  CB  MET A 680     7327   8187   8178    302    334    524       C  
ATOM   4974  CG  MET A 680      46.837  42.600  -5.941  1.00 60.40           C  
ANISOU 4974  CG  MET A 680     7097   7966   7885    286    295    502       C  
ATOM   4975  SD  MET A 680      46.910  40.982  -5.166  1.00 64.76           S  
ANISOU 4975  SD  MET A 680     7660   8546   8399    264    235    479       S  
ATOM   4976  CE  MET A 680      47.071  39.904  -6.594  1.00 67.63           C  
ANISOU 4976  CE  MET A 680     8043   8925   8730    303    242    504       C  
ATOM   4977  N   PRO A 681      46.266  45.768  -7.480  1.00 62.94           N  
ANISOU 4977  N   PRO A 681     7403   8233   8277    335    414    560       N  
ATOM   4978  CA  PRO A 681      45.685  47.023  -6.979  1.00 60.14           C  
ANISOU 4978  CA  PRO A 681     7034   7859   7957    322    431    552       C  
ATOM   4979  C   PRO A 681      45.595  47.101  -5.459  1.00 55.82           C  
ANISOU 4979  C   PRO A 681     6470   7313   7427    277    395    504       C  
ATOM   4980  O   PRO A 681      45.948  48.137  -4.883  1.00 53.91           O  
ANISOU 4980  O   PRO A 681     6198   7041   7243    258    414    489       O  
ATOM   4981  CB  PRO A 681      44.294  47.046  -7.622  1.00 57.52           C  
ANISOU 4981  CB  PRO A 681     6730   7550   7574    349    430    568       C  
ATOM   4982  CG  PRO A 681      44.489  46.300  -8.899  1.00 61.26           C  
ANISOU 4982  CG  PRO A 681     7226   8042   8008    389    440    601       C  
ATOM   4983  CD  PRO A 681      45.444  45.180  -8.557  1.00 60.65           C  
ANISOU 4983  CD  PRO A 681     7145   7973   7926    372    413    584       C  
ATOM   4984  N   GLU A 682      45.161  46.017  -4.822  1.00 52.63           N  
ANISOU 4984  N   GLU A 682     6083   6942   6973    259    346    480       N  
ATOM   4985  CA  GLU A 682      44.968  46.000  -3.370  1.00 55.32           C  
ANISOU 4985  CA  GLU A 682     6413   7291   7316    218    311    437       C  
ATOM   4986  C   GLU A 682      46.273  46.187  -2.600  1.00 55.05           C  
ANISOU 4986  C   GLU A 682     6347   7237   7333    192    307    416       C  
ATOM   4987  O   GLU A 682      46.273  46.753  -1.498  1.00 54.64           O  
ANISOU 4987  O   GLU A 682     6274   7180   7306    162    295    381       O  
ATOM   4988  CB  GLU A 682      44.285  44.709  -2.909  1.00 60.53           C  
ANISOU 4988  CB  GLU A 682     7099   7989   7912    207    262    423       C  
ATOM   4989  CG  GLU A 682      42.919  44.452  -3.513  1.00 67.36           C  
ANISOU 4989  CG  GLU A 682     7991   8875   8727    227    259    434       C  
ATOM   4990  CD  GLU A 682      42.961  43.547  -4.743  1.00 75.54           C  
ANISOU 4990  CD  GLU A 682     9049   9925   9728    263    261    464       C  
ATOM   4991  OE1 GLU A 682      43.685  43.846  -5.733  1.00 71.57           O  
ANISOU 4991  OE1 GLU A 682     8542   9406   9246    291    295    493       O  
ATOM   4992  OE2 GLU A 682      42.241  42.521  -4.717  1.00 81.38           O  
ANISOU 4992  OE2 GLU A 682     9810  10693  10419    264    230    456       O  
ATOM   4993  N   VAL A 683      47.379  45.706  -3.172  1.00 52.90           N  
ANISOU 4993  N   VAL A 683     6069   6953   7076    205    316    434       N  
ATOM   4994  CA  VAL A 683      48.699  45.910  -2.569  1.00 51.80           C  
ANISOU 4994  CA  VAL A 683     5897   6792   6993    186    314    415       C  
ATOM   4995  C   VAL A 683      49.056  47.402  -2.595  1.00 51.46           C  
ANISOU 4995  C   VAL A 683     5820   6708   7023    184    359    412       C  
ATOM   4996  O   VAL A 683      49.458  47.981  -1.576  1.00 52.25           O  
ANISOU 4996  O   VAL A 683     5891   6796   7165    155    350    375       O  
ATOM   4997  CB  VAL A 683      49.797  45.055  -3.257  1.00 52.50           C  
ANISOU 4997  CB  VAL A 683     5985   6876   7085    202    317    435       C  
ATOM   4998  CG1 VAL A 683      51.181  45.472  -2.790  1.00 50.61           C  
ANISOU 4998  CG1 VAL A 683     5708   6607   6916    185    324    417       C  
ATOM   4999  CG2 VAL A 683      49.578  43.573  -2.986  1.00 48.37           C  
ANISOU 4999  CG2 VAL A 683     5487   6389   6502    197    267    429       C  
ATOM   5000  N   ARG A 684      48.882  48.027  -3.753  1.00 49.96           N  
ANISOU 5000  N   ARG A 684     5636   6499   6849    215    408    451       N  
ATOM   5001  CA  ARG A 684      49.127  49.459  -3.874  1.00 53.15           C  
ANISOU 5001  CA  ARG A 684     6009   6860   7325    217    456    455       C  
ATOM   5002  C   ARG A 684      48.234  50.215  -2.906  1.00 52.96           C  
ANISOU 5002  C   ARG A 684     5975   6838   7309    192    444    420       C  
ATOM   5003  O   ARG A 684      48.697  51.100  -2.185  1.00 54.36           O  
ANISOU 5003  O   ARG A 684     6116   6989   7551    170    453    389       O  
ATOM   5004  CB  ARG A 684      48.911  49.957  -5.314  1.00 50.70           C  
ANISOU 5004  CB  ARG A 684     5712   6534   7019    259    510    509       C  
ATOM   5005  CG  ARG A 684      49.693  49.166  -6.341  1.00 49.79           C  
ANISOU 5005  CG  ARG A 684     5609   6423   6887    285    525    543       C  
ATOM   5006  CD  ARG A 684      49.915  49.962  -7.616  1.00 51.45           C  
ANISOU 5006  CD  ARG A 684     5818   6605   7127    322    590    595       C  
ATOM   5007  NE  ARG A 684      48.672  50.251  -8.321  1.00 50.28           N  
ANISOU 5007  NE  ARG A 684     5697   6472   6934    351    602    625       N  
ATOM   5008  CZ  ARG A 684      48.002  49.376  -9.071  1.00 50.43           C  
ANISOU 5008  CZ  ARG A 684     5754   6530   6876    378    586    645       C  
ATOM   5009  NH1 ARG A 684      48.443  48.132  -9.214  1.00 47.83           N  
ANISOU 5009  NH1 ARG A 684     5439   6227   6507    379    557    638       N  
ATOM   5010  NH2 ARG A 684      46.873  49.746  -9.672  1.00 51.87           N  
ANISOU 5010  NH2 ARG A 684     5959   6726   7025    404    596    669       N  
ATOM   5011  N   GLN A 685      46.964  49.831  -2.880  1.00 52.45           N  
ANISOU 5011  N   GLN A 685     5942   6806   7181    196    421    421       N  
ATOM   5012  CA  GLN A 685      45.953  50.473  -2.052  1.00 52.08           C  
ANISOU 5012  CA  GLN A 685     5890   6765   7133    175    410    390       C  
ATOM   5013  C   GLN A 685      46.320  50.452  -0.567  1.00 50.51           C  
ANISOU 5013  C   GLN A 685     5668   6574   6949    133    373    334       C  
ATOM   5014  O   GLN A 685      46.117  51.430   0.153  1.00 49.14           O  
ANISOU 5014  O   GLN A 685     5468   6385   6817    113    381    301       O  
ATOM   5015  CB  GLN A 685      44.605  49.781  -2.277  1.00 54.36           C  
ANISOU 5015  CB  GLN A 685     6218   7092   7345    186    385    399       C  
ATOM   5016  CG  GLN A 685      43.513  50.172  -1.290  1.00 58.74           C  
ANISOU 5016  CG  GLN A 685     6771   7660   7887    161    365    361       C  
ATOM   5017  CD  GLN A 685      42.400  49.137  -1.196  1.00 61.94           C  
ANISOU 5017  CD  GLN A 685     7213   8108   8214    161    328    359       C  
ATOM   5018  OE1 GLN A 685      41.672  49.075  -0.192  1.00 62.26           O  
ANISOU 5018  OE1 GLN A 685     7254   8168   8233    135    302    324       O  
ATOM   5019  NE2 GLN A 685      42.261  48.318  -2.241  1.00 58.82           N  
ANISOU 5019  NE2 GLN A 685     6845   7727   7777    192    328    395       N  
ATOM   5020  N   SER A 686      46.859  49.332  -0.111  1.00 49.76           N  
ANISOU 5020  N   SER A 686     5582   6504   6819    121    333    323       N  
ATOM   5021  CA  SER A 686      47.286  49.213   1.265  1.00 50.82           C  
ANISOU 5021  CA  SER A 686     5697   6652   6961     85    296    273       C  
ATOM   5022  C   SER A 686      48.538  50.050   1.534  1.00 52.17           C  
ANISOU 5022  C   SER A 686     5822   6785   7215     75    316    253       C  
ATOM   5023  O   SER A 686      48.704  50.602   2.625  1.00 54.46           O  
ANISOU 5023  O   SER A 686     6084   7075   7534     47    301    205       O  
ATOM   5024  CB  SER A 686      47.573  47.759   1.578  1.00 51.81           C  
ANISOU 5024  CB  SER A 686     5844   6812   7029     80    249    274       C  
ATOM   5025  OG  SER A 686      46.399  47.099   1.972  1.00 56.98           O  
ANISOU 5025  OG  SER A 686     6530   7504   7615     72    219    269       O  
ATOM   5026  N   SER A 687      49.412  50.149   0.542  1.00 49.21           N  
ANISOU 5026  N   SER A 687     5438   6380   6880     98    351    286       N  
ATOM   5027  CA  SER A 687      50.689  50.818   0.760  1.00 51.38           C  
ANISOU 5027  CA  SER A 687     5668   6617   7238     89    370    267       C  
ATOM   5028  C   SER A 687      50.523  52.334   0.782  1.00 49.72           C  
ANISOU 5028  C   SER A 687     5423   6366   7101     86    414    255       C  
ATOM   5029  O   SER A 687      51.119  53.019   1.615  1.00 51.40           O  
ANISOU 5029  O   SER A 687     5595   6561   7374     62    411    210       O  
ATOM   5030  CB  SER A 687      51.755  50.348  -0.236  1.00 51.28           C  
ANISOU 5030  CB  SER A 687     5653   6584   7245    112    393    304       C  
ATOM   5031  OG  SER A 687      51.483  50.804  -1.539  1.00 55.25           O  
ANISOU 5031  OG  SER A 687     6168   7064   7759    145    446    355       O  
ATOM   5032  N   PHE A 688      49.657  52.852  -0.085  1.00 49.51           N  
ANISOU 5032  N   PHE A 688     5414   6329   7070    109    451    292       N  
ATOM   5033  CA  PHE A 688      49.339  54.271  -0.057  1.00 47.17           C  
ANISOU 5033  CA  PHE A 688     5088   5994   6841    107    491    283       C  
ATOM   5034  C   PHE A 688      48.660  54.661   1.256  1.00 45.89           C  
ANISOU 5034  C   PHE A 688     4912   5850   6674     74    459    224       C  
ATOM   5035  O   PHE A 688      48.892  55.740   1.766  1.00 47.23           O  
ANISOU 5035  O   PHE A 688     5039   5988   6916     58    478    190       O  
ATOM   5036  CB  PHE A 688      48.495  54.682  -1.259  1.00 49.61           C  
ANISOU 5036  CB  PHE A 688     5420   6290   7139    141    534    339       C  
ATOM   5037  CG  PHE A 688      49.176  54.479  -2.587  1.00 52.58           C  
ANISOU 5037  CG  PHE A 688     5807   6647   7525    176    574    397       C  
ATOM   5038  CD1 PHE A 688      50.526  54.804  -2.762  1.00 52.14           C  
ANISOU 5038  CD1 PHE A 688     5716   6553   7542    175    603    399       C  
ATOM   5039  CD2 PHE A 688      48.458  53.997  -3.684  1.00 51.82           C  
ANISOU 5039  CD2 PHE A 688     5752   6571   7365    211    584    449       C  
ATOM   5040  CE1 PHE A 688      51.145  54.639  -3.996  1.00 52.07           C  
ANISOU 5040  CE1 PHE A 688     5716   6527   7542    208    644    454       C  
ATOM   5041  CE2 PHE A 688      49.071  53.833  -4.923  1.00 54.20           C  
ANISOU 5041  CE2 PHE A 688     6064   6859   7672    245    623    502       C  
ATOM   5042  CZ  PHE A 688      50.419  54.158  -5.079  1.00 53.51           C  
ANISOU 5042  CZ  PHE A 688     5943   6733   7656    243    654    506       C  
ATOM   5043  N   ALA A 689      47.845  53.775   1.810  1.00 45.19           N  
ANISOU 5043  N   ALA A 689     4857   5811   6502     63    412    210       N  
ATOM   5044  CA  ALA A 689      47.246  54.022   3.114  1.00 46.04           C  
ANISOU 5044  CA  ALA A 689     4955   5944   6597     31    380    153       C  
ATOM   5045  C   ALA A 689      48.315  54.104   4.206  1.00 45.99           C  
ANISOU 5045  C   ALA A 689     4910   5937   6628      2    354     99       C  
ATOM   5046  O   ALA A 689      48.339  55.052   4.977  1.00 46.05           O  
ANISOU 5046  O   ALA A 689     4880   5930   6686    -18    359     51       O  
ATOM   5047  CB  ALA A 689      46.212  52.955   3.454  1.00 44.48           C  
ANISOU 5047  CB  ALA A 689     4801   5799   6301     26    337    154       C  
ATOM   5048  N   LEU A 690      49.203  53.115   4.268  1.00 47.88           N  
ANISOU 5048  N   LEU A 690     5158   6193   6843      2    326    105       N  
ATOM   5049  CA  LEU A 690      50.308  53.171   5.219  1.00 46.73           C  
ANISOU 5049  CA  LEU A 690     4974   6046   6735    -20    300     56       C  
ATOM   5050  C   LEU A 690      51.163  54.426   4.988  1.00 47.22           C  
ANISOU 5050  C   LEU A 690     4983   6050   6908    -20    345     41       C  
ATOM   5051  O   LEU A 690      51.578  55.084   5.941  1.00 46.17           O  
ANISOU 5051  O   LEU A 690     4808   5910   6823    -43    334    -18       O  
ATOM   5052  CB  LEU A 690      51.148  51.906   5.142  1.00 47.54           C  
ANISOU 5052  CB  LEU A 690     5093   6169   6800    -15    266     73       C  
ATOM   5053  CG  LEU A 690      52.316  51.777   6.131  1.00 48.07           C  
ANISOU 5053  CG  LEU A 690     5126   6242   6898    -36    230     25       C  
ATOM   5054  CD1 LEU A 690      51.917  52.077   7.568  1.00 46.58           C  
ANISOU 5054  CD1 LEU A 690     4922   6085   6689    -66    192    -37       C  
ATOM   5055  CD2 LEU A 690      52.904  50.380   6.029  1.00 48.10           C  
ANISOU 5055  CD2 LEU A 690     5154   6270   6851    -29    193     49       C  
ATOM   5056  N   LEU A 691      51.375  54.792   3.729  1.00 46.45           N  
ANISOU 5056  N   LEU A 691     4886   5911   6852      8    398     92       N  
ATOM   5057  CA  LEU A 691      52.171  55.974   3.444  1.00 48.78           C  
ANISOU 5057  CA  LEU A 691     5131   6148   7258     10    447     84       C  
ATOM   5058  C   LEU A 691      51.563  57.192   4.096  1.00 52.03           C  
ANISOU 5058  C   LEU A 691     5510   6542   7718     -8    460     40       C  
ATOM   5059  O   LEU A 691      52.270  57.967   4.750  1.00 52.68           O  
ANISOU 5059  O   LEU A 691     5540   6597   7878    -26    465    -11       O  
ATOM   5060  CB  LEU A 691      52.321  56.184   1.940  1.00 49.39           C  
ANISOU 5060  CB  LEU A 691     5218   6185   7361     44    506    154       C  
ATOM   5061  CG  LEU A 691      52.979  57.472   1.444  1.00 49.53           C  
ANISOU 5061  CG  LEU A 691     5188   6136   7494     52    569    161       C  
ATOM   5062  CD1 LEU A 691      54.300  57.763   2.140  1.00 51.22           C  
ANISOU 5062  CD1 LEU A 691     5348   6325   7788     30    562    109       C  
ATOM   5063  CD2 LEU A 691      53.171  57.400  -0.066  1.00 49.17           C  
ANISOU 5063  CD2 LEU A 691     5164   6065   7455     89    622    238       C  
ATOM   5064  N   GLY A 692      50.245  57.348   3.929  1.00 53.72           N  
ANISOU 5064  N   GLY A 692     5753   6770   7886     -2    466     57       N  
ATOM   5065  CA  GLY A 692      49.511  58.461   4.521  1.00 51.99           C  
ANISOU 5065  CA  GLY A 692     5508   6538   7709    -18    479     16       C  
ATOM   5066  C   GLY A 692      49.610  58.457   6.035  1.00 51.97           C  
ANISOU 5066  C   GLY A 692     5481   6568   7697    -54    430    -63       C  
ATOM   5067  O   GLY A 692      49.810  59.502   6.659  1.00 54.05           O  
ANISOU 5067  O   GLY A 692     5695   6805   8035    -71    442   -116       O  
ATOM   5068  N   ASP A 693      49.503  57.276   6.628  1.00 50.86           N  
ANISOU 5068  N   ASP A 693     5374   6484   7465    -63    375    -73       N  
ATOM   5069  CA  ASP A 693      49.601  57.145   8.079  1.00 55.72           C  
ANISOU 5069  CA  ASP A 693     5973   7141   8059    -95    325   -144       C  
ATOM   5070  C   ASP A 693      50.984  57.504   8.648  1.00 57.16           C  
ANISOU 5070  C   ASP A 693     6103   7302   8313   -108    316   -192       C  
ATOM   5071  O   ASP A 693      51.084  58.147   9.700  1.00 56.43           O  
ANISOU 5071  O   ASP A 693     5972   7216   8252   -131    300   -262       O  
ATOM   5072  CB  ASP A 693      49.218  55.727   8.504  1.00 59.17           C  
ANISOU 5072  CB  ASP A 693     6460   7641   8381    -99    271   -132       C  
ATOM   5073  CG  ASP A 693      47.718  55.465   8.406  1.00 62.81           C  
ANISOU 5073  CG  ASP A 693     6964   8130   8771    -96    270   -111       C  
ATOM   5074  OD1 ASP A 693      46.903  56.396   8.643  1.00 59.22           O  
ANISOU 5074  OD1 ASP A 693     6494   7665   8342   -104    290   -137       O  
ATOM   5075  OD2 ASP A 693      47.360  54.315   8.091  1.00 62.95           O  
ANISOU 5075  OD2 ASP A 693     7028   8180   8710    -86    248    -72       O  
ATOM   5076  N   LEU A 694      52.046  57.087   7.960  1.00 55.09           N  
ANISOU 5076  N   LEU A 694     5837   7017   8078    -92    326   -159       N  
ATOM   5077  CA  LEU A 694      53.404  57.336   8.448  1.00 54.06           C  
ANISOU 5077  CA  LEU A 694     5656   6867   8018   -103    315   -203       C  
ATOM   5078  C   LEU A 694      53.795  58.789   8.242  1.00 53.96           C  
ANISOU 5078  C   LEU A 694     5584   6789   8129   -105    368   -229       C  
ATOM   5079  O   LEU A 694      54.579  59.360   9.016  1.00 53.19           O  
ANISOU 5079  O   LEU A 694     5434   6679   8098   -123    357   -293       O  
ATOM   5080  CB  LEU A 694      54.401  56.398   7.781  1.00 52.24           C  
ANISOU 5080  CB  LEU A 694     5438   6630   7778    -86    309   -161       C  
ATOM   5081  CG  LEU A 694      54.247  54.942   8.209  1.00 51.31           C  
ANISOU 5081  CG  LEU A 694     5367   6575   7552    -88    250   -149       C  
ATOM   5082  CD1 LEU A 694      55.178  54.082   7.376  1.00 51.86           C  
ANISOU 5082  CD1 LEU A 694     5450   6633   7623    -69    252   -102       C  
ATOM   5083  CD2 LEU A 694      54.513  54.759   9.698  1.00 49.33           C  
ANISOU 5083  CD2 LEU A 694     5098   6368   7276   -115    189   -219       C  
ATOM   5084  N   THR A 695      53.206  59.381   7.211  1.00 53.21           N  
ANISOU 5084  N   THR A 695     5499   6655   8063    -86    424   -178       N  
ATOM   5085  CA  THR A 695      53.368  60.792   6.926  1.00 55.78           C  
ANISOU 5085  CA  THR A 695     5773   6916   8505    -86    481   -191       C  
ATOM   5086  C   THR A 695      52.882  61.650   8.092  1.00 58.52           C  
ANISOU 5086  C   THR A 695     6083   7271   8880   -113    465   -270       C  
ATOM   5087  O   THR A 695      53.561  62.589   8.517  1.00 59.71           O  
ANISOU 5087  O   THR A 695     6172   7383   9132   -126    481   -324       O  
ATOM   5088  CB  THR A 695      52.656  61.136   5.617  1.00 54.08           C  
ANISOU 5088  CB  THR A 695     5585   6667   8296    -57    539   -113       C  
ATOM   5089  OG1 THR A 695      53.333  60.449   4.556  1.00 55.32           O  
ANISOU 5089  OG1 THR A 695     5766   6813   8441    -32    557    -49       O  
ATOM   5090  CG2 THR A 695      52.683  62.617   5.340  1.00 53.92           C  
ANISOU 5090  CG2 THR A 695     5514   6580   8395    -56    599   -122       C  
ATOM   5091  N   LYS A 696      51.721  61.301   8.623  1.00 60.46           N  
ANISOU 5091  N   LYS A 696     6366   7568   9039   -122    434   -281       N  
ATOM   5092  CA  LYS A 696      51.167  61.996   9.770  1.00 61.25           C  
ANISOU 5092  CA  LYS A 696     6436   7685   9151   -148    415   -357       C  
ATOM   5093  C   LYS A 696      51.952  61.680  11.030  1.00 60.39           C  
ANISOU 5093  C   LYS A 696     6301   7615   9030   -172    359   -432       C  
ATOM   5094  O   LYS A 696      52.209  62.571  11.828  1.00 60.06           O  
ANISOU 5094  O   LYS A 696     6205   7561   9056   -191    358   -507       O  
ATOM   5095  CB  LYS A 696      49.694  61.616   9.988  1.00 61.95           C  
ANISOU 5095  CB  LYS A 696     6575   7822   9143   -151    397   -346       C  
ATOM   5096  CG  LYS A 696      48.759  62.080   8.889  1.00 64.22           C  
ANISOU 5096  CG  LYS A 696     6883   8074   9444   -129    448   -284       C  
ATOM   5097  CD  LYS A 696      47.372  62.357   9.433  1.00 66.83           C  
ANISOU 5097  CD  LYS A 696     7228   8433   9732   -141    439   -310       C  
ATOM   5098  CE  LYS A 696      46.687  61.094   9.918  1.00 69.10           C  
ANISOU 5098  CE  LYS A 696     7571   8793   9890   -148    387   -303       C  
ATOM   5099  NZ  LYS A 696      45.419  61.434  10.621  1.00 70.07           N  
ANISOU 5099  NZ  LYS A 696     7700   8944   9980   -164    378   -342       N  
ATOM   5100  N   ALA A 697      52.320  60.411  11.205  1.00 57.73           N  
ANISOU 5100  N   ALA A 697     6001   7326   8609   -170    313   -414       N  
ATOM   5101  CA  ALA A 697      52.862  59.935  12.475  1.00 57.95           C  
ANISOU 5101  CA  ALA A 697     6015   7404   8598   -190    250   -479       C  
ATOM   5102  C   ALA A 697      54.350  60.285  12.703  1.00 61.71           C  
ANISOU 5102  C   ALA A 697     6433   7849   9165   -194    246   -522       C  
ATOM   5103  O   ALA A 697      54.730  60.678  13.802  1.00 63.51           O  
ANISOU 5103  O   ALA A 697     6619   8096   9415   -214    214   -603       O  
ATOM   5104  CB  ALA A 697      52.644  58.438  12.608  1.00 54.97           C  
ANISOU 5104  CB  ALA A 697     5699   7089   8099   -185    202   -441       C  
ATOM   5105  N   CYS A 698      55.187  60.119  11.681  1.00 59.68           N  
ANISOU 5105  N   CYS A 698     6172   7547   8957   -175    277   -471       N  
ATOM   5106  CA  CYS A 698      56.623  60.373  11.823  1.00 59.69           C  
ANISOU 5106  CA  CYS A 698     6118   7515   9046   -177    274   -508       C  
ATOM   5107  C   CYS A 698      57.200  60.728  10.469  1.00 56.84           C  
ANISOU 5107  C   CYS A 698     5745   7083   8770   -156    340   -448       C  
ATOM   5108  O   CYS A 698      57.864  59.921   9.812  1.00 55.29           O  
ANISOU 5108  O   CYS A 698     5568   6881   8557   -140    339   -399       O  
ATOM   5109  CB  CYS A 698      57.337  59.161  12.428  1.00 60.01           C  
ANISOU 5109  CB  CYS A 698     6176   7609   9017   -180    208   -519       C  
ATOM   5110  SG  CYS A 698      56.941  57.590  11.625  1.00 64.17           S  
ANISOU 5110  SG  CYS A 698     6785   8171   9425   -159    193   -424       S  
ATOM   5111  N   PHE A 699      56.917  61.946  10.045  1.00 56.69           N  
ANISOU 5111  N   PHE A 699     5692   7006   8840   -155    398   -449       N  
ATOM   5112  CA  PHE A 699      57.317  62.385   8.725  1.00 59.81           C  
ANISOU 5112  CA  PHE A 699     6078   7333   9314   -133    468   -385       C  
ATOM   5113  C   PHE A 699      58.839  62.415   8.478  1.00 62.08           C  
ANISOU 5113  C   PHE A 699     6320   7578   9690   -129    481   -395       C  
ATOM   5114  O   PHE A 699      59.290  62.270   7.328  1.00 61.50           O  
ANISOU 5114  O   PHE A 699     6256   7464   9644   -107    527   -328       O  
ATOM   5115  CB  PHE A 699      56.701  63.741   8.406  1.00 58.75           C  
ANISOU 5115  CB  PHE A 699     5913   7144   9264   -132    528   -386       C  
ATOM   5116  CG  PHE A 699      56.904  64.154   6.985  1.00 58.79           C  
ANISOU 5116  CG  PHE A 699     5919   7084   9333   -106    603   -307       C  
ATOM   5117  CD1 PHE A 699      56.406  63.371   5.950  1.00 57.57           C  
ANISOU 5117  CD1 PHE A 699     5830   6946   9098    -80    616   -219       C  
ATOM   5118  CD2 PHE A 699      57.611  65.299   6.678  1.00 59.63           C  
ANISOU 5118  CD2 PHE A 699     5962   7115   9580   -106    660   -321       C  
ATOM   5119  CE1 PHE A 699      56.599  63.732   4.630  1.00 57.85           C  
ANISOU 5119  CE1 PHE A 699     5869   6927   9183    -53    685   -144       C  
ATOM   5120  CE2 PHE A 699      57.802  65.668   5.359  1.00 60.76           C  
ANISOU 5120  CE2 PHE A 699     6108   7199   9778    -79    732   -242       C  
ATOM   5121  CZ  PHE A 699      57.303  64.876   4.334  1.00 59.12           C  
ANISOU 5121  CZ  PHE A 699     5968   7013   9481    -52    744   -153       C  
ATOM   5122  N   GLN A 700      59.628  62.606   9.535  1.00 61.85           N  
ANISOU 5122  N   GLN A 700     6240   7557   9704   -150    441   -479       N  
ATOM   5123  CA  GLN A 700      61.081  62.710   9.348  1.00 66.29           C  
ANISOU 5123  CA  GLN A 700     6752   8075  10361   -148    454   -497       C  
ATOM   5124  C   GLN A 700      61.638  61.497   8.579  1.00 66.06           C  
ANISOU 5124  C   GLN A 700     6766   8059  10275   -128    446   -429       C  
ATOM   5125  O   GLN A 700      62.563  61.644   7.776  1.00 65.57           O  
ANISOU 5125  O   GLN A 700     6679   7943  10292   -116    490   -400       O  
ATOM   5126  CB  GLN A 700      61.837  62.964  10.665  1.00 65.80           C  
ANISOU 5126  CB  GLN A 700     6631   8030  10341   -171    401   -602       C  
ATOM   5127  CG  GLN A 700      61.797  61.830  11.680  1.00 68.06           C  
ANISOU 5127  CG  GLN A 700     6950   8401  10508   -180    313   -633       C  
ATOM   5128  CD  GLN A 700      60.636  61.939  12.660  1.00 74.60           C  
ANISOU 5128  CD  GLN A 700     7799   9289  11258   -196    276   -675       C  
ATOM   5129  OE1 GLN A 700      59.521  62.378  12.313  1.00 73.40           O  
ANISOU 5129  OE1 GLN A 700     7671   9129  11087   -195    310   -645       O  
ATOM   5130  NE2 GLN A 700      60.891  61.527  13.903  1.00 76.59           N  
ANISOU 5130  NE2 GLN A 700     8041   9600  11459   -211    204   -743       N  
ATOM   5131  N   HIS A 701      61.044  60.318   8.782  1.00 63.27           N  
ANISOU 5131  N   HIS A 701     6476   7774   9789   -125    395   -402       N  
ATOM   5132  CA  HIS A 701      61.495  59.121   8.062  1.00 60.51           C  
ANISOU 5132  CA  HIS A 701     6168   7438   9384   -107    386   -340       C  
ATOM   5133  C   HIS A 701      60.967  59.006   6.667  1.00 59.72           C  
ANISOU 5133  C   HIS A 701     6112   7314   9265    -81    444   -248       C  
ATOM   5134  O   HIS A 701      61.492  58.236   5.864  1.00 61.66           O  
ANISOU 5134  O   HIS A 701     6381   7555   9492    -63    454   -197       O  
ATOM   5135  CB  HIS A 701      61.174  57.872   8.844  1.00 58.91           C  
ANISOU 5135  CB  HIS A 701     6012   7314   9057   -113    307   -349       C  
ATOM   5136  CG  HIS A 701      61.745  57.880  10.226  1.00 62.09           C  
ANISOU 5136  CG  HIS A 701     6376   7750   9467   -135    244   -436       C  
ATOM   5137  ND1 HIS A 701      63.061  57.737  10.462  1.00 62.28           N  
ANISOU 5137  ND1 HIS A 701     6356   7757   9551   -136    225   -471       N  
ATOM   5138  CD2 HIS A 701      61.135  58.054  11.466  1.00 63.82           C  
ANISOU 5138  CD2 HIS A 701     6592   8019   9640   -154    197   -499       C  
ATOM   5139  CE1 HIS A 701      63.283  57.791  11.788  1.00 65.80           C  
ANISOU 5139  CE1 HIS A 701     6774   8243   9986   -155    164   -551       C  
ATOM   5140  NE2 HIS A 701      62.104  57.988  12.402  1.00 66.41           N  
ANISOU 5140  NE2 HIS A 701     6877   8362   9996   -166    148   -567       N  
ATOM   5141  N   VAL A 702      59.943  59.787   6.358  1.00 56.94           N  
ANISOU 5141  N   VAL A 702     5769   6946   8918    -78    483   -229       N  
ATOM   5142  CA  VAL A 702      59.264  59.691   5.083  1.00 56.77           C  
ANISOU 5142  CA  VAL A 702     5794   6910   8865    -52    534   -143       C  
ATOM   5143  C   VAL A 702      59.853  60.716   4.120  1.00 56.64           C  
ANISOU 5143  C   VAL A 702     5738   6815   8969    -37    615   -112       C  
ATOM   5144  O   VAL A 702      60.099  60.402   2.957  1.00 54.67           O  
ANISOU 5144  O   VAL A 702     5511   6544   8715    -12    656    -42       O  
ATOM   5145  CB  VAL A 702      57.730  59.899   5.247  1.00 57.77           C  
ANISOU 5145  CB  VAL A 702     5958   7068   8924    -53    529   -134       C  
ATOM   5146  CG1 VAL A 702      57.003  59.802   3.913  1.00 55.89           C  
ANISOU 5146  CG1 VAL A 702     5768   6818   8652    -23    577    -46       C  
ATOM   5147  CG2 VAL A 702      57.146  58.900   6.238  1.00 55.95           C  
ANISOU 5147  CG2 VAL A 702     5765   6914   8578    -68    452   -163       C  
ATOM   5148  N   LYS A 703      60.079  61.935   4.612  1.00 58.28           N  
ANISOU 5148  N   LYS A 703     5883   6977   9282    -53    639   -166       N  
ATOM   5149  CA  LYS A 703      60.637  63.032   3.798  1.00 61.27           C  
ANISOU 5149  CA  LYS A 703     6217   7275   9790    -42    720   -141       C  
ATOM   5150  C   LYS A 703      61.739  62.646   2.782  1.00 62.75           C  
ANISOU 5150  C   LYS A 703     6400   7427  10015    -22    759    -89       C  
ATOM   5151  O   LYS A 703      61.671  63.063   1.627  1.00 64.22           O  
ANISOU 5151  O   LYS A 703     6595   7570  10235      2    829    -20       O  
ATOM   5152  CB  LYS A 703      61.090  64.203   4.683  1.00 62.40           C  
ANISOU 5152  CB  LYS A 703     6281   7376  10052    -67    726   -226       C  
ATOM   5153  CG  LYS A 703      61.483  65.441   3.888  1.00 63.46           C  
ANISOU 5153  CG  LYS A 703     6366   7422  10324    -57    814   -199       C  
ATOM   5154  CD  LYS A 703      61.592  66.683   4.749  1.00 63.32           C  
ANISOU 5154  CD  LYS A 703     6275   7364  10420    -81    822   -282       C  
ATOM   5155  CE  LYS A 703      61.905  67.864   3.856  1.00 65.67           C  
ANISOU 5155  CE  LYS A 703     6528   7570  10852    -68    915   -243       C  
ATOM   5156  NZ  LYS A 703      61.687  69.167   4.534  1.00 66.71           N  
ANISOU 5156  NZ  LYS A 703     6595   7659  11091    -88    933   -310       N  
ATOM   5157  N   PRO A 704      62.754  61.860   3.205  1.00 63.28           N  
ANISOU 5157  N   PRO A 704     6454   7512  10076    -31    716   -122       N  
ATOM   5158  CA  PRO A 704      63.770  61.409   2.253  1.00 64.06           C  
ANISOU 5158  CA  PRO A 704     6552   7582  10205    -12    752    -75       C  
ATOM   5159  C   PRO A 704      63.232  60.698   1.010  1.00 66.05           C  
ANISOU 5159  C   PRO A 704     6872   7852  10371     19    780     20       C  
ATOM   5160  O   PRO A 704      63.915  60.671  -0.008  1.00 63.86           O  
ANISOU 5160  O   PRO A 704     6591   7537  10135     39    834     71       O  
ATOM   5161  CB  PRO A 704      64.590  60.412   3.070  1.00 65.04           C  
ANISOU 5161  CB  PRO A 704     6670   7747  10297    -26    678   -126       C  
ATOM   5162  CG  PRO A 704      64.470  60.884   4.470  1.00 63.41           C  
ANISOU 5162  CG  PRO A 704     6424   7558  10110    -55    627   -217       C  
ATOM   5163  CD  PRO A 704      63.108  61.499   4.594  1.00 62.53           C  
ANISOU 5163  CD  PRO A 704     6336   7459   9964    -58    638   -210       C  
ATOM   5164  N   CYS A 705      62.031  60.126   1.094  1.00 66.47           N  
ANISOU 5164  N   CYS A 705     6986   7963  10308     24    744     41       N  
ATOM   5165  CA  CYS A 705      61.496  59.258   0.031  1.00 61.79           C  
ANISOU 5165  CA  CYS A 705     6460   7399   9619     52    755    121       C  
ATOM   5166  C   CYS A 705      60.555  59.960  -0.932  1.00 60.57           C  
ANISOU 5166  C   CYS A 705     6329   7222   9461     76    817    185       C  
ATOM   5167  O   CYS A 705      60.254  59.435  -2.004  1.00 61.68           O  
ANISOU 5167  O   CYS A 705     6517   7377   9543    105    841    255       O  
ATOM   5168  CB  CYS A 705      60.770  58.071   0.641  1.00 61.46           C  
ANISOU 5168  CB  CYS A 705     6471   7435   9448     45    678    108       C  
ATOM   5169  SG  CYS A 705      61.808  57.099   1.740  1.00 69.08           S  
ANISOU 5169  SG  CYS A 705     7415   8432  10399     22    600     43       S  
ATOM   5170  N   ILE A 706      60.099  61.142  -0.540  1.00 58.44           N  
ANISOU 5170  N   ILE A 706     6027   6922   9257     65    839    159       N  
ATOM   5171  CA  ILE A 706      59.091  61.882  -1.281  1.00 59.24           C  
ANISOU 5171  CA  ILE A 706     6148   7004   9357     85    890    213       C  
ATOM   5172  C   ILE A 706      59.395  62.003  -2.776  1.00 61.92           C  
ANISOU 5172  C   ILE A 706     6503   7308   9717    121    964    300       C  
ATOM   5173  O   ILE A 706      58.541  61.705  -3.615  1.00 64.89           O  
ANISOU 5173  O   ILE A 706     6931   7707  10015    149    977    363       O  
ATOM   5174  CB  ILE A 706      58.846  63.257  -0.627  1.00 59.53           C  
ANISOU 5174  CB  ILE A 706     6130   6996   9493     66    911    166       C  
ATOM   5175  CG1 ILE A 706      58.241  63.079   0.779  1.00 58.91           C  
ANISOU 5175  CG1 ILE A 706     6049   6966   9367     34    837     86       C  
ATOM   5176  CG2 ILE A 706      57.992  64.153  -1.514  1.00 61.65           C  
ANISOU 5176  CG2 ILE A 706     6410   7230   9784     90    975    228       C  
ATOM   5177  CD1 ILE A 706      56.973  62.241   0.845  1.00 60.69           C  
ANISOU 5177  CD1 ILE A 706     6343   7261   9456     40    791    107       C  
ATOM   5178  N   ALA A 707      60.619  62.405  -3.104  1.00 65.14           N  
ANISOU 5178  N   ALA A 707     6864   7660  10225    122   1011    303       N  
ATOM   5179  CA  ALA A 707      61.023  62.575  -4.494  1.00 62.19           C  
ANISOU 5179  CA  ALA A 707     6501   7250   9878    156   1087    384       C  
ATOM   5180  C   ALA A 707      60.848  61.302  -5.328  1.00 59.92           C  
ANISOU 5180  C   ALA A 707     6279   7016   9472    183   1071    439       C  
ATOM   5181  O   ALA A 707      60.587  61.381  -6.526  1.00 61.41           O  
ANISOU 5181  O   ALA A 707     6499   7198   9638    217   1124    516       O  
ATOM   5182  CB  ALA A 707      62.444  63.095  -4.568  1.00 61.34           C  
ANISOU 5182  CB  ALA A 707     6329   7077   9899    148   1133    368       C  
ATOM   5183  N   ASP A 708      60.977  60.141  -4.691  1.00 58.64           N  
ANISOU 5183  N   ASP A 708     6138   6909   9235    168    998    400       N  
ATOM   5184  CA  ASP A 708      60.694  58.853  -5.333  1.00 62.43           C  
ANISOU 5184  CA  ASP A 708     6679   7444   9598    189    972    441       C  
ATOM   5185  C   ASP A 708      59.190  58.529  -5.288  1.00 61.40           C  
ANISOU 5185  C   ASP A 708     6603   7366   9359    197    935    456       C  
ATOM   5186  O   ASP A 708      58.594  58.075  -6.271  1.00 61.12           O  
ANISOU 5186  O   ASP A 708     6617   7357   9248    228    951    517       O  
ATOM   5187  CB  ASP A 708      61.451  57.715  -4.625  1.00 67.34           C  
ANISOU 5187  CB  ASP A 708     7298   8099  10189    169    906    392       C  
ATOM   5188  CG  ASP A 708      62.968  57.845  -4.719  1.00 70.00           C  
ANISOU 5188  CG  ASP A 708     7584   8389  10625    164    936    377       C  
ATOM   5189  OD1 ASP A 708      63.458  58.446  -5.694  1.00 72.16           O  
ANISOU 5189  OD1 ASP A 708     7841   8613  10961    184   1013    424       O  
ATOM   5190  OD2 ASP A 708      63.668  57.322  -3.816  1.00 69.70           O  
ANISOU 5190  OD2 ASP A 708     7521   8363  10598    139    882    317       O  
ATOM   5191  N   PHE A 709      58.592  58.765  -4.131  1.00 56.86           N  
ANISOU 5191  N   PHE A 709     6018   6809   8779    169    887    398       N  
ATOM   5192  CA  PHE A 709      57.187  58.460  -3.901  1.00 58.37           C  
ANISOU 5192  CA  PHE A 709     6254   7050   8875    171    848    401       C  
ATOM   5193  C   PHE A 709      56.186  59.249  -4.757  1.00 59.32           C  
ANISOU 5193  C   PHE A 709     6394   7154   8991    198    898    458       C  
ATOM   5194  O   PHE A 709      55.212  58.676  -5.263  1.00 57.34           O  
ANISOU 5194  O   PHE A 709     6196   6945   8645    218    883    494       O  
ATOM   5195  CB  PHE A 709      56.891  58.611  -2.417  1.00 55.18           C  
ANISOU 5195  CB  PHE A 709     5827   6664   8475    132    790    322       C  
ATOM   5196  CG  PHE A 709      57.395  57.459  -1.590  1.00 53.80           C  
ANISOU 5196  CG  PHE A 709     5660   6534   8250    112    720    277       C  
ATOM   5197  CD1 PHE A 709      58.163  56.449  -2.169  1.00 52.47           C  
ANISOU 5197  CD1 PHE A 709     5509   6377   8052    126    715    305       C  
ATOM   5198  CD2 PHE A 709      57.122  57.392  -0.224  1.00 54.07           C  
ANISOU 5198  CD2 PHE A 709     5681   6597   8268     80    660    208       C  
ATOM   5199  CE1 PHE A 709      58.626  55.378  -1.413  1.00 53.82           C  
ANISOU 5199  CE1 PHE A 709     5685   6586   8179    108    650    267       C  
ATOM   5200  CE2 PHE A 709      57.582  56.325   0.545  1.00 55.15           C  
ANISOU 5200  CE2 PHE A 709     5824   6775   8355     63    596    172       C  
ATOM   5201  CZ  PHE A 709      58.337  55.316  -0.049  1.00 54.39           C  
ANISOU 5201  CZ  PHE A 709     5746   6688   8233     78    590    202       C  
ATOM   5202  N   MET A 710      56.434  60.543  -4.951  1.00 61.00           N  
ANISOU 5202  N   MET A 710     6564   7304   9308    200    958    467       N  
ATOM   5203  CA  MET A 710      55.460  61.393  -5.650  1.00 62.71           C  
ANISOU 5203  CA  MET A 710     6796   7503   9530    225   1004    518       C  
ATOM   5204  C   MET A 710      55.154  60.952  -7.083  1.00 64.88           C  
ANISOU 5204  C   MET A 710     7121   7795   9737    270   1038    604       C  
ATOM   5205  O   MET A 710      53.986  60.858  -7.452  1.00 64.79           O  
ANISOU 5205  O   MET A 710     7150   7814   9654    289   1029    634       O  
ATOM   5206  CB  MET A 710      55.881  62.858  -5.630  1.00 62.93           C  
ANISOU 5206  CB  MET A 710     6764   7455   9692    219   1067    516       C  
ATOM   5207  CG  MET A 710      55.655  63.529  -4.296  1.00 64.77           C  
ANISOU 5207  CG  MET A 710     6953   7675   9980    181   1035    435       C  
ATOM   5208  SD  MET A 710      53.922  63.484  -3.796  1.00 67.21           S  
ANISOU 5208  SD  MET A 710     7301   8034  10201    176    988    420       S  
ATOM   5209  CE  MET A 710      53.062  64.153  -5.226  1.00 61.20           C  
ANISOU 5209  CE  MET A 710     6570   7249   9435    224   1055    517       C  
ATOM   5210  N   PRO A 711      56.196  60.681  -7.899  1.00 65.31           N  
ANISOU 5210  N   PRO A 711     7171   7830   9814    288   1079    641       N  
ATOM   5211  CA  PRO A 711      55.876  60.288  -9.280  1.00 64.52           C  
ANISOU 5211  CA  PRO A 711     7120   7751   9645    333   1112    722       C  
ATOM   5212  C   PRO A 711      55.036  59.010  -9.360  1.00 63.76           C  
ANISOU 5212  C   PRO A 711     7083   7730   9414    343   1050    722       C  
ATOM   5213  O   PRO A 711      54.334  58.786 -10.354  1.00 64.60           O  
ANISOU 5213  O   PRO A 711     7232   7862   9450    380   1065    779       O  
ATOM   5214  CB  PRO A 711      57.255  60.087  -9.942  1.00 65.88           C  
ANISOU 5214  CB  PRO A 711     7273   7894   9864    344   1158    747       C  
ATOM   5215  CG  PRO A 711      58.270  60.207  -8.849  1.00 67.14           C  
ANISOU 5215  CG  PRO A 711     7378   8025  10108    303   1137    675       C  
ATOM   5216  CD  PRO A 711      57.633  60.960  -7.719  1.00 65.11           C  
ANISOU 5216  CD  PRO A 711     7094   7757   9890    272   1108    619       C  
ATOM   5217  N   ILE A 712      55.104  58.185  -8.320  1.00 58.86           N  
ANISOU 5217  N   ILE A 712     6462   7143   8758    310    980    659       N  
ATOM   5218  CA  ILE A 712      54.322  56.971  -8.295  1.00 58.83           C  
ANISOU 5218  CA  ILE A 712     6510   7207   8636    315    920    654       C  
ATOM   5219  C   ILE A 712      52.887  57.296  -7.900  1.00 60.03           C  
ANISOU 5219  C   ILE A 712     6682   7381   8747    312    894    644       C  
ATOM   5220  O   ILE A 712      51.950  56.824  -8.540  1.00 57.56           O  
ANISOU 5220  O   ILE A 712     6414   7106   8350    339    883    678       O  
ATOM   5221  CB  ILE A 712      54.926  55.923  -7.365  1.00 58.75           C  
ANISOU 5221  CB  ILE A 712     6494   7225   8603    284    857    597       C  
ATOM   5222  CG1 ILE A 712      56.246  55.430  -7.965  1.00 59.37           C  
ANISOU 5222  CG1 ILE A 712     6562   7288   8708    295    883    615       C  
ATOM   5223  CG2 ILE A 712      53.943  54.775  -7.160  1.00 57.41           C  
ANISOU 5223  CG2 ILE A 712     6373   7120   8318    285    794    588       C  
ATOM   5224  CD1 ILE A 712      57.084  54.619  -7.009  1.00 59.09           C  
ANISOU 5224  CD1 ILE A 712     6508   7265   8679    263    829    558       C  
ATOM   5225  N   LEU A 713      52.721  58.122  -6.869  1.00 58.53           N  
ANISOU 5225  N   LEU A 713     6455   7166   8618    281    884    596       N  
ATOM   5226  CA  LEU A 713      51.405  58.613  -6.516  1.00 59.48           C  
ANISOU 5226  CA  LEU A 713     6586   7298   8715    278    869    586       C  
ATOM   5227  C   LEU A 713      50.754  59.261  -7.738  1.00 60.84           C  
ANISOU 5227  C   LEU A 713     6778   7454   8883    321    923    658       C  
ATOM   5228  O   LEU A 713      49.577  59.042  -8.001  1.00 63.59           O  
ANISOU 5228  O   LEU A 713     7164   7837   9161    337    903    675       O  
ATOM   5229  CB  LEU A 713      51.490  59.593  -5.350  1.00 59.04           C  
ANISOU 5229  CB  LEU A 713     6480   7208   8744    241    865    526       C  
ATOM   5230  CG  LEU A 713      51.832  58.923  -4.019  1.00 60.97           C  
ANISOU 5230  CG  LEU A 713     6712   7482   8971    200    800    451       C  
ATOM   5231  CD1 LEU A 713      52.475  59.882  -3.032  1.00 58.23           C  
ANISOU 5231  CD1 LEU A 713     6303   7093   8729    167    807    392       C  
ATOM   5232  CD2 LEU A 713      50.604  58.272  -3.411  1.00 56.34           C  
ANISOU 5232  CD2 LEU A 713     6163   6953   8291    189    741    426       C  
ATOM   5233  N   GLY A 714      51.536  60.022  -8.499  1.00 61.03           N  
ANISOU 5233  N   GLY A 714     6779   7428   8983    340    991    702       N  
ATOM   5234  CA  GLY A 714      51.049  60.690  -9.702  1.00 61.23           C  
ANISOU 5234  CA  GLY A 714     6821   7435   9011    383   1049    777       C  
ATOM   5235  C   GLY A 714      50.559  59.763 -10.803  1.00 63.26           C  
ANISOU 5235  C   GLY A 714     7135   7743   9157    424   1041    830       C  
ATOM   5236  O   GLY A 714      49.681  60.132 -11.578  1.00 66.19           O  
ANISOU 5236  O   GLY A 714     7531   8121   9497    459   1062    880       O  
ATOM   5237  N   THR A 715      51.122  58.559 -10.877  1.00 66.12           N  
ANISOU 5237  N   THR A 715     7517   8142   9463    422   1011    818       N  
ATOM   5238  CA  THR A 715      50.714  57.572 -11.893  1.00 67.08           C  
ANISOU 5238  CA  THR A 715     7692   8316   9481    459   1000    860       C  
ATOM   5239  C   THR A 715      49.582  56.648 -11.407  1.00 65.86           C  
ANISOU 5239  C   THR A 715     7572   8220   9230    451    927    825       C  
ATOM   5240  O   THR A 715      49.082  55.827 -12.179  1.00 65.20           O  
ANISOU 5240  O   THR A 715     7532   8183   9060    481    911    852       O  
ATOM   5241  CB  THR A 715      51.908  56.726 -12.398  1.00 68.47           C  
ANISOU 5241  CB  THR A 715     7871   8499   9647    467   1011    871       C  
ATOM   5242  OG1 THR A 715      52.619  56.188 -11.277  1.00 70.00           O  
ANISOU 5242  OG1 THR A 715     8039   8692   9865    423    967    806       O  
ATOM   5243  CG2 THR A 715      52.861  57.573 -13.229  1.00 68.86           C  
ANISOU 5243  CG2 THR A 715     7895   8496   9773    488   1093    923       C  
ATOM   5244  N   ASN A 716      49.186  56.802 -10.139  1.00 62.73           N  
ANISOU 5244  N   ASN A 716     7158   7823   8853    410    885    765       N  
ATOM   5245  CA  ASN A 716      48.075  56.055  -9.535  1.00 60.99           C  
ANISOU 5245  CA  ASN A 716     6967   7654   8555    397    820    729       C  
ATOM   5246  C   ASN A 716      46.810  56.910  -9.235  1.00 61.68           C  
ANISOU 5246  C   ASN A 716     7052   7734   8648    396    817    724       C  
ATOM   5247  O   ASN A 716      45.947  56.521  -8.437  1.00 56.44           O  
ANISOU 5247  O   ASN A 716     6400   7101   7943    374    767    681       O  
ATOM   5248  CB  ASN A 716      48.536  55.327  -8.262  1.00 59.87           C  
ANISOU 5248  CB  ASN A 716     6811   7528   8411    351    765    662       C  
ATOM   5249  CG  ASN A 716      49.399  54.108  -8.551  1.00 61.24           C  
ANISOU 5249  CG  ASN A 716     6998   7724   8545    355    746    664       C  
ATOM   5250  OD1 ASN A 716      48.914  52.973  -8.583  1.00 61.41           O  
ANISOU 5250  OD1 ASN A 716     7053   7793   8485    359    702    657       O  
ATOM   5251  ND2 ASN A 716      50.686  54.334  -8.751  1.00 61.36           N  
ANISOU 5251  ND2 ASN A 716     6986   7705   8624    354    781    673       N  
ATOM   5252  N   LEU A 717      46.701  58.074  -9.868  1.00 62.29           N  
ANISOU 5252  N   LEU A 717     7115   7770   8780    420    874    767       N  
ATOM   5253  CA  LEU A 717      45.457  58.842  -9.798  1.00 64.29           C  
ANISOU 5253  CA  LEU A 717     7372   8020   9036    427    875    771       C  
ATOM   5254  C   LEU A 717      44.511  58.408 -10.922  1.00 67.71           C  
ANISOU 5254  C   LEU A 717     7852   8492   9382    475    872    822       C  
ATOM   5255  O   LEU A 717      44.047  59.224 -11.726  1.00 73.43           O  
ANISOU 5255  O   LEU A 717     8580   9197  10122    509    912    873       O  
ATOM   5256  CB  LEU A 717      45.725  60.347  -9.831  1.00 62.22           C  
ANISOU 5256  CB  LEU A 717     7068   7692   8882    428    934    790       C  
ATOM   5257  CG  LEU A 717      46.590  60.932  -8.709  1.00 60.68           C  
ANISOU 5257  CG  LEU A 717     6819   7454   8783    383    939    734       C  
ATOM   5258  CD1 LEU A 717      46.769  62.417  -8.949  1.00 63.31           C  
ANISOU 5258  CD1 LEU A 717     7111   7719   9223    391   1003    762       C  
ATOM   5259  CD2 LEU A 717      46.009  60.693  -7.325  1.00 58.65           C  
ANISOU 5259  CD2 LEU A 717     6553   7221   8511    339    879    657       C  
ATOM   5260  N   ASN A 718      44.246  57.104 -10.965  1.00 68.26           N  
ANISOU 5260  N   ASN A 718     7957   8617   9363    476    823    806       N  
ATOM   5261  CA  ASN A 718      43.338  56.514 -11.926  1.00 69.65           C  
ANISOU 5261  CA  ASN A 718     8177   8837   9450    518    809    840       C  
ATOM   5262  C   ASN A 718      42.032  56.063 -11.263  1.00 72.23           C  
ANISOU 5262  C   ASN A 718     8520   9200   9724    502    751    797       C  
ATOM   5263  O   ASN A 718      42.014  55.100 -10.482  1.00 68.75           O  
ANISOU 5263  O   ASN A 718     8086   8789   9246    471    702    749       O  
ATOM   5264  CB  ASN A 718      44.011  55.345 -12.633  1.00 69.74           C  
ANISOU 5264  CB  ASN A 718     8213   8882   9402    536    801    857       C  
ATOM   5265  CG  ASN A 718      43.154  54.756 -13.736  1.00 72.41           C  
ANISOU 5265  CG  ASN A 718     8595   9268   9651    584    790    892       C  
ATOM   5266  OD1 ASN A 718      42.039  55.217 -14.012  1.00 73.85           O  
ANISOU 5266  OD1 ASN A 718     8788   9457   9813    605    787    907       O  
ATOM   5267  ND2 ASN A 718      43.674  53.724 -14.374  1.00 70.36           N  
ANISOU 5267  ND2 ASN A 718     8356   9040   9338    601    782    902       N  
ATOM   5268  N   PRO A 719      40.929  56.755 -11.583  1.00 72.77           N  
ANISOU 5268  N   PRO A 719     8596   9266   9789    524    759    817       N  
ATOM   5269  CA  PRO A 719      39.653  56.492 -10.923  1.00 74.34           C  
ANISOU 5269  CA  PRO A 719     8805   9492   9949    508    711    775       C  
ATOM   5270  C   PRO A 719      39.095  55.088 -11.203  1.00 75.20           C  
ANISOU 5270  C   PRO A 719     8952   9660   9960    519    661    763       C  
ATOM   5271  O   PRO A 719      38.201  54.642 -10.492  1.00 74.78           O  
ANISOU 5271  O   PRO A 719     8906   9631   9875    497    617    720       O  
ATOM   5272  CB  PRO A 719      38.736  57.587 -11.478  1.00 73.04           C  
ANISOU 5272  CB  PRO A 719     8637   9307   9807    539    739    811       C  
ATOM   5273  CG  PRO A 719      39.345  57.967 -12.785  1.00 75.31           C  
ANISOU 5273  CG  PRO A 719     8933   9580  10101    587    791    884       C  
ATOM   5274  CD  PRO A 719      40.824  57.829 -12.586  1.00 73.22           C  
ANISOU 5274  CD  PRO A 719     8649   9293   9879    566    815    881       C  
ATOM   5275  N   GLU A 720      39.637  54.397 -12.207  1.00 77.33           N  
ANISOU 5275  N   GLU A 720     9245   9952  10186    552    670    799       N  
ATOM   5276  CA  GLU A 720      39.300  52.994 -12.465  1.00 78.13           C  
ANISOU 5276  CA  GLU A 720     9377  10106  10202    561    625    783       C  
ATOM   5277  C   GLU A 720      39.551  52.114 -11.233  1.00 74.37           C  
ANISOU 5277  C   GLU A 720     8894   9642   9720    510    580    723       C  
ATOM   5278  O   GLU A 720      38.829  51.153 -10.994  1.00 72.63           O  
ANISOU 5278  O   GLU A 720     8693   9459   9443    504    534    694       O  
ATOM   5279  CB  GLU A 720      40.084  52.469 -13.674  1.00 89.26           C  
ANISOU 5279  CB  GLU A 720    10806  11532  11578    600    649    827       C  
ATOM   5280  CG  GLU A 720      39.719  51.052 -14.117  1.00101.72           C  
ANISOU 5280  CG  GLU A 720    12414  13164  13070    616    606    813       C  
ATOM   5281  CD  GLU A 720      40.361  50.651 -15.445  1.00111.40           C  
ANISOU 5281  CD  GLU A 720    13658  14408  14259    662    633    858       C  
ATOM   5282  OE1 GLU A 720      40.175  51.378 -16.451  1.00112.01           O  
ANISOU 5282  OE1 GLU A 720    13744  14482  14331    707    671    909       O  
ATOM   5283  OE2 GLU A 720      41.051  49.602 -15.486  1.00112.23           O  
ANISOU 5283  OE2 GLU A 720    13770  14532  14340    655    616    842       O  
ATOM   5284  N   PHE A 721      40.575  52.448 -10.455  1.00 71.56           N  
ANISOU 5284  N   PHE A 721     8510   9255   9426    475    593    705       N  
ATOM   5285  CA  PHE A 721      40.844  51.752  -9.199  1.00 66.85           C  
ANISOU 5285  CA  PHE A 721     7904   8668   8828    427    551    650       C  
ATOM   5286  C   PHE A 721      40.504  52.682  -8.050  1.00 65.18           C  
ANISOU 5286  C   PHE A 721     7664   8430   8671    390    549    613       C  
ATOM   5287  O   PHE A 721      41.363  53.392  -7.535  1.00 64.54           O  
ANISOU 5287  O   PHE A 721     7551   8313   8657    368    573    603       O  
ATOM   5288  CB  PHE A 721      42.306  51.302  -9.134  1.00 67.02           C  
ANISOU 5288  CB  PHE A 721     7913   8678   8873    415    559    650       C  
ATOM   5289  CG  PHE A 721      42.749  50.529 -10.340  1.00 65.87           C  
ANISOU 5289  CG  PHE A 721     7791   8553   8683    453    570    688       C  
ATOM   5290  CD1 PHE A 721      42.480  49.164 -10.448  1.00 67.09           C  
ANISOU 5290  CD1 PHE A 721     7971   8751   8769    456    527    673       C  
ATOM   5291  CD2 PHE A 721      43.410  51.164 -11.386  1.00 69.07           C  
ANISOU 5291  CD2 PHE A 721     8192   8935   9116    487    624    739       C  
ATOM   5292  CE1 PHE A 721      42.875  48.444 -11.571  1.00 65.62           C  
ANISOU 5292  CE1 PHE A 721     7805   8585   8543    492    536    703       C  
ATOM   5293  CE2 PHE A 721      43.811  50.450 -12.511  1.00 68.40           C  
ANISOU 5293  CE2 PHE A 721     8129   8873   8986    524    635    771       C  
ATOM   5294  CZ  PHE A 721      43.541  49.087 -12.604  1.00 67.25           C  
ANISOU 5294  CZ  PHE A 721     8008   8772   8773    526    590    751       C  
ATOM   5295  N   ILE A 722      39.235  52.668  -7.658  1.00 64.12           N  
ANISOU 5295  N   ILE A 722     7540   8315   8507    383    523    590       N  
ATOM   5296  CA  ILE A 722      38.695  53.652  -6.728  1.00 61.20           C  
ANISOU 5296  CA  ILE A 722     7145   7923   8186    355    526    558       C  
ATOM   5297  C   ILE A 722      39.508  53.805  -5.443  1.00 58.14           C  
ANISOU 5297  C   ILE A 722     6727   7519   7845    307    516    512       C  
ATOM   5298  O   ILE A 722      39.885  54.910  -5.071  1.00 58.77           O  
ANISOU 5298  O   ILE A 722     6773   7559   7997    294    545    503       O  
ATOM   5299  CB  ILE A 722      37.216  53.350  -6.388  1.00 61.79           C  
ANISOU 5299  CB  ILE A 722     7237   8026   8213    350    491    532       C  
ATOM   5300  CG1 ILE A 722      36.334  53.534  -7.629  1.00 64.26           C  
ANISOU 5300  CG1 ILE A 722     7571   8348   8496    400    504    576       C  
ATOM   5301  CG2 ILE A 722      36.712  54.218  -5.234  1.00 57.66           C  
ANISOU 5301  CG2 ILE A 722     6687   7485   7737    314    489    488       C  
ATOM   5302  CD1 ILE A 722      36.295  54.947  -8.167  1.00 69.07           C  
ANISOU 5302  CD1 ILE A 722     8162   8916   9166    423    552    611       C  
ATOM   5303  N   SER A 723      39.773  52.703  -4.765  1.00 54.93           N  
ANISOU 5303  N   SER A 723     6331   7143   7397    282    475    481       N  
ATOM   5304  CA  SER A 723      40.359  52.795  -3.444  1.00 56.48           C  
ANISOU 5304  CA  SER A 723     6501   7333   7625    237    457    432       C  
ATOM   5305  C   SER A 723      41.869  53.038  -3.495  1.00 55.27           C  
ANISOU 5305  C   SER A 723     6323   7151   7527    232    481    440       C  
ATOM   5306  O   SER A 723      42.438  53.583  -2.542  1.00 52.36           O  
ANISOU 5306  O   SER A 723     5921   6762   7210    201    481    402       O  
ATOM   5307  CB  SER A 723      40.002  51.566  -2.610  1.00 58.14           C  
ANISOU 5307  CB  SER A 723     6732   7588   7773    211    404    398       C  
ATOM   5308  OG  SER A 723      40.342  50.396  -3.315  1.00 66.05           O  
ANISOU 5308  OG  SER A 723     7760   8612   8725    231    389    424       O  
ATOM   5309  N   VAL A 724      42.495  52.659  -4.610  1.00 53.77           N  
ANISOU 5309  N   VAL A 724     6146   6957   7327    265    501    485       N  
ATOM   5310  CA  VAL A 724      43.902  52.969  -4.860  1.00 55.92           C  
ANISOU 5310  CA  VAL A 724     6394   7197   7657    267    532    499       C  
ATOM   5311  C   VAL A 724      44.001  54.467  -5.123  1.00 56.21           C  
ANISOU 5311  C   VAL A 724     6399   7183   7774    275    585    516       C  
ATOM   5312  O   VAL A 724      44.790  55.190  -4.499  1.00 55.73           O  
ANISOU 5312  O   VAL A 724     6299   7088   7786    251    602    491       O  
ATOM   5313  CB  VAL A 724      44.460  52.189  -6.081  1.00 57.07           C  
ANISOU 5313  CB  VAL A 724     6563   7353   7768    302    546    547       C  
ATOM   5314  CG1 VAL A 724      45.853  52.669  -6.450  1.00 53.14           C  
ANISOU 5314  CG1 VAL A 724     6037   6815   7337    307    588    566       C  
ATOM   5315  CG2 VAL A 724      44.479  50.692  -5.809  1.00 55.08           C  
ANISOU 5315  CG2 VAL A 724     6336   7144   7448    293    495    529       C  
ATOM   5316  N   CYS A 725      43.179  54.923  -6.053  1.00 54.37           N  
ANISOU 5316  N   CYS A 725     6182   6947   7528    310    611    557       N  
ATOM   5317  CA  CYS A 725      43.091  56.325  -6.377  1.00 54.97           C  
ANISOU 5317  CA  CYS A 725     6234   6977   7677    322    662    579       C  
ATOM   5318  C   CYS A 725      42.793  57.155  -5.135  1.00 53.59           C  
ANISOU 5318  C   CYS A 725     6024   6782   7557    283    653    524       C  
ATOM   5319  O   CYS A 725      43.429  58.166  -4.881  1.00 53.58           O  
ANISOU 5319  O   CYS A 725     5982   6734   7641    271    687    516       O  
ATOM   5320  CB  CYS A 725      41.995  56.532  -7.403  1.00 53.78           C  
ANISOU 5320  CB  CYS A 725     6110   6836   7486    364    676    625       C  
ATOM   5321  SG  CYS A 725      41.985  58.198  -8.040  1.00 59.67           S  
ANISOU 5321  SG  CYS A 725     6829   7523   8322    388    744    669       S  
ATOM   5322  N   ASN A 726      41.816  56.710  -4.362  1.00 52.39           N  
ANISOU 5322  N   ASN A 726     5886   6665   7355    262    608    484       N  
ATOM   5323  CA  ASN A 726      41.453  57.382  -3.132  1.00 51.18           C  
ANISOU 5323  CA  ASN A 726     5703   6502   7242    224    596    427       C  
ATOM   5324  C   ASN A 726      42.638  57.511  -2.201  1.00 49.90           C  
ANISOU 5324  C   ASN A 726     5505   6323   7132    189    591    384       C  
ATOM   5325  O   ASN A 726      42.955  58.602  -1.748  1.00 54.04           O  
ANISOU 5325  O   ASN A 726     5987   6807   7738    174    616    360       O  
ATOM   5326  CB  ASN A 726      40.330  56.637  -2.415  1.00 46.67           C  
ANISOU 5326  CB  ASN A 726     5157   5978   6598    205    545    390       C  
ATOM   5327  CG  ASN A 726      39.884  57.341  -1.145  1.00 49.01           C  
ANISOU 5327  CG  ASN A 726     5423   6268   6931    167    534    329       C  
ATOM   5328  OD1 ASN A 726      40.262  56.947  -0.034  1.00 46.76           O  
ANISOU 5328  OD1 ASN A 726     5128   6002   6637    131    502    279       O  
ATOM   5329  ND2 ASN A 726      39.074  58.393  -1.302  1.00 49.42           N  
ANISOU 5329  ND2 ASN A 726     5461   6294   7024    175    560    332       N  
ATOM   5330  N   ASN A 727      43.276  56.390  -1.904  1.00 47.83           N  
ANISOU 5330  N   ASN A 727     5257   6091   6824    178    556    372       N  
ATOM   5331  CA  ASN A 727      44.351  56.375  -0.922  1.00 48.53           C  
ANISOU 5331  CA  ASN A 727     5313   6173   6952    144    541    325       C  
ATOM   5332  C   ASN A 727      45.591  57.139  -1.375  1.00 49.37           C  
ANISOU 5332  C   ASN A 727     5383   6227   7147    153    587    343       C  
ATOM   5333  O   ASN A 727      46.204  57.830  -0.572  1.00 49.93           O  
ANISOU 5333  O   ASN A 727     5411   6272   7287    126    592    299       O  
ATOM   5334  CB  ASN A 727      44.676  54.948  -0.512  1.00 48.28           C  
ANISOU 5334  CB  ASN A 727     5309   6188   6849    132    490    312       C  
ATOM   5335  CG  ASN A 727      43.560  54.324   0.310  1.00 46.29           C  
ANISOU 5335  CG  ASN A 727     5080   5982   6526    113    444    280       C  
ATOM   5336  OD1 ASN A 727      42.580  54.988   0.637  1.00 47.84           O  
ANISOU 5336  OD1 ASN A 727     5272   6177   6730    106    448    262       O  
ATOM   5337  ND2 ASN A 727      43.717  53.067   0.671  1.00 44.05           N  
ANISOU 5337  ND2 ASN A 727     4820   5737   6178    103    400    272       N  
ATOM   5338  N   ALA A 728      45.912  57.052  -2.666  1.00 49.47           N  
ANISOU 5338  N   ALA A 728     5413   6225   7160    190    624    405       N  
ATOM   5339  CA  ALA A 728      46.958  57.863  -3.262  1.00 50.11           C  
ANISOU 5339  CA  ALA A 728     5460   6252   7326    203    679    432       C  
ATOM   5340  C   ALA A 728      46.617  59.322  -3.029  1.00 52.99           C  
ANISOU 5340  C   ALA A 728     5787   6571   7776    196    716    420       C  
ATOM   5341  O   ALA A 728      47.438  60.075  -2.487  1.00 55.09           O  
ANISOU 5341  O   ALA A 728     6006   6798   8130    175    734    388       O  
ATOM   5342  CB  ALA A 728      47.105  57.566  -4.751  1.00 47.47           C  
ANISOU 5342  CB  ALA A 728     5155   5916   6966    248    714    506       C  
ATOM   5343  N   THR A 729      45.388  59.698  -3.391  1.00 51.83           N  
ANISOU 5343  N   THR A 729     5660   6430   7604    213    723    442       N  
ATOM   5344  CA  THR A 729      44.905  61.066  -3.225  1.00 50.96           C  
ANISOU 5344  CA  THR A 729     5516   6276   7572    210    757    434       C  
ATOM   5345  C   THR A 729      45.021  61.518  -1.780  1.00 50.13           C  
ANISOU 5345  C   THR A 729     5369   6164   7513    164    733    353       C  
ATOM   5346  O   THR A 729      45.542  62.602  -1.511  1.00 51.56           O  
ANISOU 5346  O   THR A 729     5501   6294   7795    153    767    333       O  
ATOM   5347  CB  THR A 729      43.449  61.212  -3.698  1.00 51.83           C  
ANISOU 5347  CB  THR A 729     5656   6402   7634    233    756    461       C  
ATOM   5348  OG1 THR A 729      43.366  60.860  -5.080  1.00 54.74           O  
ANISOU 5348  OG1 THR A 729     6061   6778   7961    279    779    535       O  
ATOM   5349  CG2 THR A 729      42.942  62.644  -3.529  1.00 52.25           C  
ANISOU 5349  CG2 THR A 729     5673   6408   7774    231    792    453       C  
ATOM   5350  N   TRP A 730      44.542  60.698  -0.850  1.00 47.61           N  
ANISOU 5350  N   TRP A 730     5069   5897   7124    139    675    305       N  
ATOM   5351  CA  TRP A 730      44.600  61.077   0.555  1.00 47.27           C  
ANISOU 5351  CA  TRP A 730     4991   5857   7114     96    649    226       C  
ATOM   5352  C   TRP A 730      46.040  61.286   0.931  1.00 49.84           C  
ANISOU 5352  C   TRP A 730     5274   6155   7508     80    658    199       C  
ATOM   5353  O   TRP A 730      46.388  62.324   1.473  1.00 52.29           O  
ANISOU 5353  O   TRP A 730     5533   6425   7908     62    678    159       O  
ATOM   5354  CB  TRP A 730      43.956  60.013   1.426  1.00 44.00           C  
ANISOU 5354  CB  TRP A 730     4608   5507   6603     74    587    188       C  
ATOM   5355  CG  TRP A 730      44.131  60.229   2.914  1.00 42.02           C  
ANISOU 5355  CG  TRP A 730     4324   5270   6371     32    555    106       C  
ATOM   5356  CD1 TRP A 730      43.618  61.265   3.691  1.00 42.60           C  
ANISOU 5356  CD1 TRP A 730     4362   5327   6497     10    562     54       C  
ATOM   5357  CD2 TRP A 730      44.859  59.365   3.862  1.00 40.40           C  
ANISOU 5357  CD2 TRP A 730     4118   5102   6128      6    507     64       C  
ATOM   5358  NE1 TRP A 730      43.967  61.107   5.016  1.00 41.72           N  
ANISOU 5358  NE1 TRP A 730     4229   5243   6380    -26    523    -18       N  
ATOM   5359  CE2 TRP A 730      44.715  59.988   5.182  1.00 40.31           C  
ANISOU 5359  CE2 TRP A 730     4071   5097   6146    -30    488    -14       C  
ATOM   5360  CE3 TRP A 730      45.606  58.192   3.744  1.00 40.20           C  
ANISOU 5360  CE3 TRP A 730     4117   5105   6051      9    478     81       C  
ATOM   5361  CZ2 TRP A 730      45.297  59.449   6.316  1.00 39.72           C  
ANISOU 5361  CZ2 TRP A 730     3987   5058   6046    -58    443    -68       C  
ATOM   5362  CZ3 TRP A 730      46.181  57.650   4.895  1.00 39.94           C  
ANISOU 5362  CZ3 TRP A 730     4074   5104   5996    -20    432     28       C  
ATOM   5363  CH2 TRP A 730      46.040  58.271   6.152  1.00 41.32           C  
ANISOU 5363  CH2 TRP A 730     4215   5287   6196    -52    414    -44       C  
ATOM   5364  N   ALA A 731      46.886  60.305   0.602  1.00 49.17           N  
ANISOU 5364  N   ALA A 731     5208   6088   7386     87    643    221       N  
ATOM   5365  CA  ALA A 731      48.314  60.342   0.890  1.00 48.32           C  
ANISOU 5365  CA  ALA A 731     5064   5957   7338     74    647    198       C  
ATOM   5366  C   ALA A 731      48.981  61.639   0.432  1.00 49.74           C  
ANISOU 5366  C   ALA A 731     5195   6065   7640     82    711    210       C  
ATOM   5367  O   ALA A 731      49.707  62.270   1.203  1.00 46.62           O  
ANISOU 5367  O   ALA A 731     4747   5642   7323     57    714    156       O  
ATOM   5368  CB  ALA A 731      49.004  59.144   0.259  1.00 47.96           C  
ANISOU 5368  CB  ALA A 731     5052   5935   7237     91    634    237       C  
ATOM   5369  N   ILE A 732      48.709  62.049  -0.806  1.00 50.06           N  
ANISOU 5369  N   ILE A 732     5250   6076   7696    118    763    281       N  
ATOM   5370  CA  ILE A 732      49.354  63.229  -1.331  1.00 53.39           C  
ANISOU 5370  CA  ILE A 732     5627   6428   8233    129    829    303       C  
ATOM   5371  C   ILE A 732      48.878  64.486  -0.652  1.00 56.18           C  
ANISOU 5371  C   ILE A 732     5934   6744   8667    109    845    258       C  
ATOM   5372  O   ILE A 732      49.630  65.452  -0.545  1.00 55.77           O  
ANISOU 5372  O   ILE A 732     5828   6635   8728    101    884    241       O  
ATOM   5373  CB  ILE A 732      49.365  63.337  -2.874  1.00 56.58           C  
ANISOU 5373  CB  ILE A 732     6056   6808   8636    174    885    396       C  
ATOM   5374  CG1 ILE A 732      48.096  62.861  -3.552  1.00 60.90           C  
ANISOU 5374  CG1 ILE A 732     6660   7395   9085    203    872    443       C  
ATOM   5375  CG2 ILE A 732      50.443  62.435  -3.424  1.00 63.42           C  
ANISOU 5375  CG2 ILE A 732     6937   7684   9476    186    886    424       C  
ATOM   5376  CD1 ILE A 732      48.329  62.491  -5.017  1.00 57.07           C  
ANISOU 5376  CD1 ILE A 732     6209   6908   8566    248    910    528       C  
ATOM   5377  N   GLY A 733      47.653  64.455  -0.141  1.00 53.16           N  
ANISOU 5377  N   GLY A 733     5572   6396   8232    100    813    234       N  
ATOM   5378  CA  GLY A 733      47.161  65.556   0.652  1.00 51.83           C  
ANISOU 5378  CA  GLY A 733     5359   6199   8133     78    820    180       C  
ATOM   5379  C   GLY A 733      47.899  65.632   1.973  1.00 49.97           C  
ANISOU 5379  C   GLY A 733     5080   5970   7937     37    787     90       C  
ATOM   5380  O   GLY A 733      48.302  66.704   2.399  1.00 52.31           O  
ANISOU 5380  O   GLY A 733     5318   6217   8340     21    814     49       O  
ATOM   5381  N   GLU A 734      48.084  64.503   2.631  1.00 48.77           N  
ANISOU 5381  N   GLU A 734     4953   5877   7699     20    729     59       N  
ATOM   5382  CA  GLU A 734      48.802  64.519   3.900  1.00 54.59           C  
ANISOU 5382  CA  GLU A 734     5650   6626   8465    -16    692    -25       C  
ATOM   5383  C   GLU A 734      50.303  64.914   3.738  1.00 57.80           C  
ANISOU 5383  C   GLU A 734     6008   6982   8971    -17    722    -33       C  
ATOM   5384  O   GLU A 734      50.864  65.592   4.604  1.00 55.70           O  
ANISOU 5384  O   GLU A 734     5685   6694   8783    -43    718   -103       O  
ATOM   5385  CB  GLU A 734      48.694  63.167   4.600  1.00 55.28           C  
ANISOU 5385  CB  GLU A 734     5779   6788   8436    -31    623    -49       C  
ATOM   5386  CG  GLU A 734      47.273  62.712   4.914  1.00 62.77           C  
ANISOU 5386  CG  GLU A 734     6771   7788   9289    -34    591    -51       C  
ATOM   5387  CD  GLU A 734      46.653  63.434   6.100  1.00 65.04           C  
ANISOU 5387  CD  GLU A 734     7027   8085   9600    -65    575   -128       C  
ATOM   5388  OE1 GLU A 734      47.392  64.047   6.897  1.00 69.00           O  
ANISOU 5388  OE1 GLU A 734     7476   8568  10172    -87    572   -192       O  
ATOM   5389  OE2 GLU A 734      45.416  63.394   6.234  1.00 66.36           O  
ANISOU 5389  OE2 GLU A 734     7221   8278   9715    -66    565   -128       O  
ATOM   5390  N   ILE A 735      50.952  64.489   2.650  1.00 55.90           N  
ANISOU 5390  N   ILE A 735     5787   6725   8729     10    750     36       N  
ATOM   5391  CA  ILE A 735      52.359  64.811   2.508  1.00 58.26           C  
ANISOU 5391  CA  ILE A 735     6039   6976   9120      8    779     28       C  
ATOM   5392  C   ILE A 735      52.533  66.321   2.226  1.00 61.37           C  
ANISOU 5392  C   ILE A 735     6375   7291   9651     10    845     27       C  
ATOM   5393  O   ILE A 735      53.453  66.942   2.756  1.00 60.65           O  
ANISOU 5393  O   ILE A 735     6224   7161   9659     -9    856    -26       O  
ATOM   5394  CB  ILE A 735      53.142  63.912   1.515  1.00 57.62           C  
ANISOU 5394  CB  ILE A 735     5990   6899   9005     33    791     92       C  
ATOM   5395  CG1 ILE A 735      52.973  64.384   0.090  1.00 58.76           C  
ANISOU 5395  CG1 ILE A 735     6149   7000   9179     70    860    180       C  
ATOM   5396  CG2 ILE A 735      52.816  62.428   1.657  1.00 54.15           C  
ANISOU 5396  CG2 ILE A 735     5609   6533   8431     34    729    102       C  
ATOM   5397  CD1 ILE A 735      54.318  64.540  -0.572  1.00 65.41           C  
ANISOU 5397  CD1 ILE A 735     6960   7792  10098     82    907    208       C  
ATOM   5398  N   SER A 736      51.624  66.898   1.434  1.00 61.35           N  
ANISOU 5398  N   SER A 736     6390   7265   9655     34    888     84       N  
ATOM   5399  CA  SER A 736      51.548  68.349   1.222  1.00 62.80           C  
ANISOU 5399  CA  SER A 736     6523   7376   9964     37    949     86       C  
ATOM   5400  C   SER A 736      51.720  69.136   2.504  1.00 64.18           C  
ANISOU 5400  C   SER A 736     6633   7533  10218     -1    931    -15       C  
ATOM   5401  O   SER A 736      52.593  70.008   2.601  1.00 66.81           O  
ANISOU 5401  O   SER A 736     6903   7805  10677    -10    969    -41       O  
ATOM   5402  CB  SER A 736      50.203  68.739   0.616  1.00 64.38           C  
ANISOU 5402  CB  SER A 736     6755   7574  10132     59    970    137       C  
ATOM   5403  OG  SER A 736      50.264  68.701  -0.793  1.00 70.96           O  
ANISOU 5403  OG  SER A 736     7618   8385  10960    100   1021    236       O  
ATOM   5404  N   ILE A 737      50.876  68.819   3.481  1.00 64.23           N  
ANISOU 5404  N   ILE A 737     6655   7595  10153    -23    875    -71       N  
ATOM   5405  CA  ILE A 737      50.853  69.509   4.765  1.00 65.31           C  
ANISOU 5405  CA  ILE A 737     6738   7730  10348    -58    852   -172       C  
ATOM   5406  C   ILE A 737      52.201  69.416   5.461  1.00 65.12           C  
ANISOU 5406  C   ILE A 737     6666   7699  10377    -80    832   -236       C  
ATOM   5407  O   ILE A 737      52.621  70.342   6.140  1.00 66.61           O  
ANISOU 5407  O   ILE A 737     6788   7850  10670   -101    842   -306       O  
ATOM   5408  CB  ILE A 737      49.711  68.977   5.661  1.00 66.21           C  
ANISOU 5408  CB  ILE A 737     6888   7917  10354    -76    792   -215       C  
ATOM   5409  CG1 ILE A 737      48.345  69.388   5.078  1.00 68.78           C  
ANISOU 5409  CG1 ILE A 737     7242   8234  10659    -58    817   -168       C  
ATOM   5410  CG2 ILE A 737      49.861  69.427   7.114  1.00 64.43           C  
ANISOU 5410  CG2 ILE A 737     6610   7705  10165   -114    756   -327       C  
ATOM   5411  CD1 ILE A 737      48.304  70.751   4.394  1.00 68.48           C  
ANISOU 5411  CD1 ILE A 737     7159   8112  10749    -43    890   -138       C  
ATOM   5412  N   GLN A 738      52.883  68.299   5.277  1.00 65.11           N  
ANISOU 5412  N   GLN A 738     6698   7733  10306    -74    802   -213       N  
ATOM   5413  CA  GLN A 738      54.189  68.129   5.884  1.00 65.72           C  
ANISOU 5413  CA  GLN A 738     6733   7807  10431    -91    780   -269       C  
ATOM   5414  C   GLN A 738      55.321  68.827   5.088  1.00 65.63           C  
ANISOU 5414  C   GLN A 738     6673   7714  10549    -79    847   -240       C  
ATOM   5415  O   GLN A 738      56.242  69.353   5.692  1.00 62.35           O  
ANISOU 5415  O   GLN A 738     6193   7266  10230    -98    847   -306       O  
ATOM   5416  CB  GLN A 738      54.465  66.642   6.128  1.00 66.01           C  
ANISOU 5416  CB  GLN A 738     6820   7915  10345    -92    718   -263       C  
ATOM   5417  CG  GLN A 738      53.485  65.962   7.086  1.00 65.44           C  
ANISOU 5417  CG  GLN A 738     6788   7922  10154   -109    651   -302       C  
ATOM   5418  CD  GLN A 738      53.705  66.304   8.553  1.00 66.19           C  
ANISOU 5418  CD  GLN A 738     6835   8041  10273   -143    606   -410       C  
ATOM   5419  OE1 GLN A 738      53.661  65.428   9.413  1.00 69.48           O  
ANISOU 5419  OE1 GLN A 738     7276   8525  10599   -157    542   -447       O  
ATOM   5420  NE2 GLN A 738      53.934  67.574   8.845  1.00 67.13           N  
ANISOU 5420  NE2 GLN A 738     6887   8105  10514   -155    640   -461       N  
ATOM   5421  N   MET A 739      55.207  68.855   3.753  1.00 66.31           N  
ANISOU 5421  N   MET A 739     6789   7767  10639    -46    903   -143       N  
ATOM   5422  CA  MET A 739      56.162  69.520   2.837  1.00 68.30           C  
ANISOU 5422  CA  MET A 739     7002   7940  11008    -29    976    -98       C  
ATOM   5423  C   MET A 739      56.146  71.057   2.853  1.00 68.44           C  
ANISOU 5423  C   MET A 739     6953   7878  11175    -35   1036   -119       C  
ATOM   5424  O   MET A 739      57.171  71.688   2.590  1.00 73.69           O  
ANISOU 5424  O   MET A 739     7562   8476  11961    -35   1084   -122       O  
ATOM   5425  CB  MET A 739      55.938  69.059   1.382  1.00 66.10           C  
ANISOU 5425  CB  MET A 739     6782   7658  10675     10   1019     17       C  
ATOM   5426  CG  MET A 739      56.401  67.649   1.050  1.00 66.42           C  
ANISOU 5426  CG  MET A 739     6874   7751  10610     21    982     48       C  
ATOM   5427  SD  MET A 739      58.196  67.443   0.871  1.00 68.69           S  
ANISOU 5427  SD  MET A 739     7118   8001  10980     18   1002     38       S  
ATOM   5428  CE  MET A 739      58.626  67.145   2.571  1.00 66.86           C  
ANISOU 5428  CE  MET A 739     6849   7811  10745    -24    918    -85       C  
ATOM   5429  N   GLY A 740      54.989  71.656   3.124  1.00 66.52           N  
ANISOU 5429  N   GLY A 740     6712   7637  10926    -39   1037   -131       N  
ATOM   5430  CA  GLY A 740      54.835  73.104   3.023  1.00 64.87           C  
ANISOU 5430  CA  GLY A 740     6443   7350  10854    -40   1097   -140       C  
ATOM   5431  C   GLY A 740      55.116  73.542   1.596  1.00 66.62           C  
ANISOU 5431  C   GLY A 740     6670   7507  11137     -4   1180    -35       C  
ATOM   5432  O   GLY A 740      54.782  72.824   0.648  1.00 62.42           O  
ANISOU 5432  O   GLY A 740     6203   7003  10511     25   1187     52       O  
ATOM   5433  N   ILE A 741      55.761  74.699   1.431  1.00 68.81           N  
ANISOU 5433  N   ILE A 741     6877   7697  11572     -7   1244    -43       N  
ATOM   5434  CA  ILE A 741      56.062  75.204   0.082  1.00 71.29           C  
ANISOU 5434  CA  ILE A 741     7191   7944  11952     28   1330     60       C  
ATOM   5435  C   ILE A 741      57.057  74.298  -0.691  1.00 70.62           C  
ANISOU 5435  C   ILE A 741     7136   7870  11826     46   1341    116       C  
ATOM   5436  O   ILE A 741      57.111  74.328  -1.934  1.00 66.75           O  
ANISOU 5436  O   ILE A 741     6675   7354  11334     81   1400    217       O  
ATOM   5437  CB  ILE A 741      56.486  76.695   0.088  1.00 73.58           C  
ANISOU 5437  CB  ILE A 741     7395   8132  12429     21   1400     41       C  
ATOM   5438  CG1 ILE A 741      56.227  77.326  -1.294  1.00 76.49           C  
ANISOU 5438  CG1 ILE A 741     7778   8441  12843     61   1487    160       C  
ATOM   5439  CG2 ILE A 741      57.935  76.851   0.546  1.00 76.07           C  
ANISOU 5439  CG2 ILE A 741     7643   8408  12851     -2   1408    -23       C  
ATOM   5440  CD1 ILE A 741      56.238  78.846  -1.330  1.00 77.04           C  
ANISOU 5440  CD1 ILE A 741     7773   8413  13084     58   1557    154       C  
ATOM   5441  N   GLU A 742      57.803  73.471   0.044  1.00 69.89           N  
ANISOU 5441  N   GLU A 742     7039   7821  11695     23   1283     51       N  
ATOM   5442  CA  GLU A 742      58.727  72.508  -0.572  1.00 73.60           C  
ANISOU 5442  CA  GLU A 742     7537   8308  12119     37   1284     94       C  
ATOM   5443  C   GLU A 742      57.998  71.574  -1.539  1.00 71.71           C  
ANISOU 5443  C   GLU A 742     7387   8123  11736     71   1278    187       C  
ATOM   5444  O   GLU A 742      58.624  70.852  -2.311  1.00 72.35           O  
ANISOU 5444  O   GLU A 742     7498   8215  11778     90   1293    241       O  
ATOM   5445  CB  GLU A 742      59.481  71.698   0.488  1.00 73.52           C  
ANISOU 5445  CB  GLU A 742     7513   8345  12076      8   1210      5       C  
ATOM   5446  CG  GLU A 742      60.437  72.515   1.343  1.00 77.67           C  
ANISOU 5446  CG  GLU A 742     7947   8818  12746    -22   1216    -87       C  
ATOM   5447  CD  GLU A 742      61.313  71.643   2.222  1.00 82.83           C  
ANISOU 5447  CD  GLU A 742     8589   9517  13365    -45   1146   -163       C  
ATOM   5448  OE1 GLU A 742      61.338  71.865   3.449  1.00 84.93           O  
ANISOU 5448  OE1 GLU A 742     8815   9801  13652    -75   1095   -263       O  
ATOM   5449  OE2 GLU A 742      61.972  70.722   1.692  1.00 85.21           O  
ANISOU 5449  OE2 GLU A 742     8922   9838  13616    -31   1141   -122       O  
ATOM   5450  N   MET A 743      56.669  71.622  -1.504  1.00 71.31           N  
ANISOU 5450  N   MET A 743     7376   8106  11613     78   1258    203       N  
ATOM   5451  CA  MET A 743      55.827  70.777  -2.337  1.00 65.79           C  
ANISOU 5451  CA  MET A 743     6758   7462  10777    109   1247    281       C  
ATOM   5452  C   MET A 743      55.754  71.275  -3.785  1.00 66.11           C  
ANISOU 5452  C   MET A 743     6816   7456  10848    151   1329    391       C  
ATOM   5453  O   MET A 743      55.346  70.525  -4.678  1.00 64.09           O  
ANISOU 5453  O   MET A 743     6625   7241  10487    183   1329    464       O  
ATOM   5454  CB  MET A 743      54.429  70.717  -1.724  1.00 67.13           C  
ANISOU 5454  CB  MET A 743     6957   7680  10868    100   1196    252       C  
ATOM   5455  CG  MET A 743      53.504  69.663  -2.312  1.00 65.52           C  
ANISOU 5455  CG  MET A 743     6837   7546  10511    125   1164    310       C  
ATOM   5456  SD  MET A 743      53.935  68.019  -1.732  1.00 64.87           S  
ANISOU 5456  SD  MET A 743     6796   7547  10305    109   1082    270       S  
ATOM   5457  CE  MET A 743      52.947  67.028  -2.847  1.00 64.47           C  
ANISOU 5457  CE  MET A 743     6834   7554  10108    149   1073    361       C  
ATOM   5458  N   GLN A 744      56.169  72.523  -4.022  1.00 66.22           N  
ANISOU 5458  N   GLN A 744     6770   7385  11006    153   1400    403       N  
ATOM   5459  CA  GLN A 744      55.947  73.162  -5.328  1.00 70.23           C  
ANISOU 5459  CA  GLN A 744     7291   7845  11548    195   1481    509       C  
ATOM   5460  C   GLN A 744      56.349  72.321  -6.559  1.00 71.03           C  
ANISOU 5460  C   GLN A 744     7447   7971  11570    232   1507    599       C  
ATOM   5461  O   GLN A 744      55.541  72.206  -7.483  1.00 69.30           O  
ANISOU 5461  O   GLN A 744     7281   7773  11277    269   1526    680       O  
ATOM   5462  CB  GLN A 744      56.473  74.613  -5.377  1.00 75.69           C  
ANISOU 5462  CB  GLN A 744     7905   8436  12419    190   1558    508       C  
ATOM   5463  CG  GLN A 744      57.873  74.818  -5.932  1.00 84.24           C  
ANISOU 5463  CG  GLN A 744     8949   9459  13600    196   1622    536       C  
ATOM   5464  CD  GLN A 744      58.574  76.015  -5.310  1.00 90.66           C  
ANISOU 5464  CD  GLN A 744     9668  10186  14594    168   1662    475       C  
ATOM   5465  OE1 GLN A 744      58.018  77.116  -5.241  1.00 94.05           O  
ANISOU 5465  OE1 GLN A 744    10062  10562  15109    168   1698    477       O  
ATOM   5466  NE2 GLN A 744      59.804  75.803  -4.846  1.00 89.53           N  
ANISOU 5466  NE2 GLN A 744     9479  10025  14511    144   1656    416       N  
ATOM   5467  N   PRO A 745      57.562  71.705  -6.564  1.00 70.87           N  
ANISOU 5467  N   PRO A 745     7415   7951  11560    223   1506    583       N  
ATOM   5468  CA  PRO A 745      57.967  70.949  -7.768  1.00 70.48           C  
ANISOU 5468  CA  PRO A 745     7414   7923  11441    259   1536    668       C  
ATOM   5469  C   PRO A 745      57.072  69.745  -8.096  1.00 71.76           C  
ANISOU 5469  C   PRO A 745     7659   8175  11430    278   1479    697       C  
ATOM   5470  O   PRO A 745      56.993  69.329  -9.255  1.00 69.24           O  
ANISOU 5470  O   PRO A 745     7388   7875  11046    317   1510    780       O  
ATOM   5471  CB  PRO A 745      59.383  70.468  -7.432  1.00 69.43           C  
ANISOU 5471  CB  PRO A 745     7247   7779  11355    237   1530    622       C  
ATOM   5472  CG  PRO A 745      59.473  70.508  -5.944  1.00 68.79           C  
ANISOU 5472  CG  PRO A 745     7123   7708  11306    191   1463    507       C  
ATOM   5473  CD  PRO A 745      58.588  71.634  -5.504  1.00 68.95           C  
ANISOU 5473  CD  PRO A 745     7115   7695  11388    182   1475    487       C  
ATOM   5474  N   TYR A 746      56.396  69.205  -7.087  1.00 72.36           N  
ANISOU 5474  N   TYR A 746     7751   8307  11435    252   1397    627       N  
ATOM   5475  CA  TYR A 746      55.584  68.002  -7.266  1.00 74.16           C  
ANISOU 5475  CA  TYR A 746     8052   8619  11505    266   1337    643       C  
ATOM   5476  C   TYR A 746      54.148  68.285  -7.710  1.00 73.34           C  
ANISOU 5476  C   TYR A 746     7990   8537  11341    291   1338    690       C  
ATOM   5477  O   TYR A 746      53.473  67.403  -8.235  1.00 73.87           O  
ANISOU 5477  O   TYR A 746     8119   8664  11286    314   1308    726       O  
ATOM   5478  CB  TYR A 746      55.615  67.156  -5.991  1.00 74.35           C  
ANISOU 5478  CB  TYR A 746     8076   8697  11475    226   1249    551       C  
ATOM   5479  CG  TYR A 746      57.021  66.879  -5.515  1.00 75.32           C  
ANISOU 5479  CG  TYR A 746     8157   8801  11659    202   1243    502       C  
ATOM   5480  CD1 TYR A 746      57.862  66.026  -6.233  1.00 76.46           C  
ANISOU 5480  CD1 TYR A 746     8325   8960  11769    219   1254    540       C  
ATOM   5481  CD2 TYR A 746      57.520  67.481  -4.360  1.00 76.25           C  
ANISOU 5481  CD2 TYR A 746     8212   8889  11873    164   1226    416       C  
ATOM   5482  CE1 TYR A 746      59.158  65.770  -5.810  1.00 78.20           C  
ANISOU 5482  CE1 TYR A 746     8505   9162  12048    198   1248    495       C  
ATOM   5483  CE2 TYR A 746      58.815  67.232  -3.927  1.00 79.26           C  
ANISOU 5483  CE2 TYR A 746     8551   9253  12311    143   1218    369       C  
ATOM   5484  CZ  TYR A 746      59.631  66.377  -4.657  1.00 80.35           C  
ANISOU 5484  CZ  TYR A 746     8712   9402  12414    161   1229    410       C  
ATOM   5485  OH  TYR A 746      60.922  66.118  -4.243  1.00 82.77           O  
ANISOU 5485  OH  TYR A 746     8978   9692  12781    141   1220    363       O  
ATOM   5486  N   ILE A 747      53.701  69.521  -7.536  1.00 71.46           N  
ANISOU 5486  N   ILE A 747     7714   8245  11194    288   1373    688       N  
ATOM   5487  CA  ILE A 747      52.325  69.880  -7.860  1.00 72.99           C  
ANISOU 5487  CA  ILE A 747     7938   8453  11341    310   1372    725       C  
ATOM   5488  C   ILE A 747      51.881  69.577  -9.297  1.00 74.85           C  
ANISOU 5488  C   ILE A 747     8233   8710  11498    364   1405    830       C  
ATOM   5489  O   ILE A 747      50.821  68.978  -9.478  1.00 76.13           O  
ANISOU 5489  O   ILE A 747     8447   8930  11549    379   1363    844       O  
ATOM   5490  CB  ILE A 747      51.999  71.326  -7.444  1.00 72.57           C  
ANISOU 5490  CB  ILE A 747     7828   8331  11413    298   1409    705       C  
ATOM   5491  CG1 ILE A 747      51.815  71.362  -5.933  1.00 70.51           C  
ANISOU 5491  CG1 ILE A 747     7534   8086  11172    249   1347    593       C  
ATOM   5492  CG2 ILE A 747      50.745  71.835  -8.144  1.00 72.65           C  
ANISOU 5492  CG2 ILE A 747     7869   8341  11394    333   1430    770       C  
ATOM   5493  CD1 ILE A 747      51.838  72.750  -5.367  1.00 72.31           C  
ANISOU 5493  CD1 ILE A 747     7690   8240  11543    229   1383    554       C  
ATOM   5494  N   PRO A 748      52.683  69.966 -10.313  1.00 76.90           N  
ANISOU 5494  N   PRO A 748     8483   8925  11813    392   1480    902       N  
ATOM   5495  CA  PRO A 748      52.248  69.749 -11.700  1.00 77.08           C  
ANISOU 5495  CA  PRO A 748     8559   8969  11758    447   1515   1003       C  
ATOM   5496  C   PRO A 748      52.002  68.283 -12.046  1.00 76.44           C  
ANISOU 5496  C   PRO A 748     8545   8974  11526    461   1459   1010       C  
ATOM   5497  O   PRO A 748      51.130  67.990 -12.864  1.00 79.97           O  
ANISOU 5497  O   PRO A 748     9042   9460  11881    500   1455   1067       O  
ATOM   5498  CB  PRO A 748      53.422  70.285 -12.533  1.00 77.22           C  
ANISOU 5498  CB  PRO A 748     8549   8925  11865    466   1602   1063       C  
ATOM   5499  CG  PRO A 748      54.128  71.231 -11.633  1.00 77.22           C  
ANISOU 5499  CG  PRO A 748     8471   8852  12016    426   1625   1003       C  
ATOM   5500  CD  PRO A 748      53.994  70.640 -10.261  1.00 78.18           C  
ANISOU 5500  CD  PRO A 748     8583   9014  12108    378   1539    895       C  
ATOM   5501  N   MET A 749      52.746  67.373 -11.421  1.00 75.05           N  
ANISOU 5501  N   MET A 749     8364   8826  11326    431   1415    950       N  
ATOM   5502  CA  MET A 749      52.615  65.946 -11.727  1.00 75.21           C  
ANISOU 5502  CA  MET A 749     8441   8922  11212    442   1365    954       C  
ATOM   5503  C   MET A 749      51.329  65.332 -11.168  1.00 73.10           C  
ANISOU 5503  C   MET A 749     8212   8718  10845    434   1288    916       C  
ATOM   5504  O   MET A 749      51.063  64.147 -11.337  1.00 73.90           O  
ANISOU 5504  O   MET A 749     8360   8884  10836    442   1241    913       O  
ATOM   5505  CB  MET A 749      53.865  65.174 -11.269  1.00 77.18           C  
ANISOU 5505  CB  MET A 749     8673   9177  11475    415   1345    906       C  
ATOM   5506  CG  MET A 749      53.940  64.787  -9.798  1.00 80.64           C  
ANISOU 5506  CG  MET A 749     9087   9634  11918    364   1273    806       C  
ATOM   5507  SD  MET A 749      55.591  64.317  -9.198  1.00 90.60           S  
ANISOU 5507  SD  MET A 749    10306  10876  13241    331   1265    751       S  
ATOM   5508  CE  MET A 749      56.374  63.630 -10.660  1.00 89.09           C  
ANISOU 5508  CE  MET A 749    10148  10695  13008    372   1314    831       C  
ATOM   5509  N   VAL A 750      50.514  66.165 -10.537  1.00 71.28           N  
ANISOU 5509  N   VAL A 750     7960   8466  10656    419   1280    888       N  
ATOM   5510  CA  VAL A 750      49.393  65.689  -9.750  1.00 69.34           C  
ANISOU 5510  CA  VAL A 750     7738   8272  10336    400   1208    836       C  
ATOM   5511  C   VAL A 750      48.110  66.525  -9.929  1.00 69.37           C  
ANISOU 5511  C   VAL A 750     7747   8265  10345    418   1218    861       C  
ATOM   5512  O   VAL A 750      47.015  65.971  -9.919  1.00 71.11           O  
ANISOU 5512  O   VAL A 750     8008   8537  10473    427   1172    857       O  
ATOM   5513  CB  VAL A 750      49.838  65.544  -8.272  1.00 65.62           C  
ANISOU 5513  CB  VAL A 750     7228   7801   9904    345   1160    738       C  
ATOM   5514  CG1 VAL A 750      48.975  66.342  -7.316  1.00 64.16           C  
ANISOU 5514  CG1 VAL A 750     7016   7602   9762    319   1141    685       C  
ATOM   5515  CG2 VAL A 750      49.931  64.085  -7.884  1.00 64.68           C  
ANISOU 5515  CG2 VAL A 750     7145   7749   9680    331   1093    702       C  
ATOM   5516  N   LEU A 751      48.255  67.835 -10.136  1.00 69.17           N  
ANISOU 5516  N   LEU A 751     7681   8170  10431    425   1281    889       N  
ATOM   5517  CA  LEU A 751      47.118  68.762 -10.157  1.00 69.65           C  
ANISOU 5517  CA  LEU A 751     7735   8209  10518    437   1292    904       C  
ATOM   5518  C   LEU A 751      46.069  68.531 -11.261  1.00 73.92           C  
ANISOU 5518  C   LEU A 751     8333   8788  10967    489   1293    979       C  
ATOM   5519  O   LEU A 751      44.876  68.394 -10.953  1.00 74.96           O  
ANISOU 5519  O   LEU A 751     8485   8953  11043    488   1249    957       O  
ATOM   5520  CB  LEU A 751      47.588  70.225 -10.171  1.00 67.91           C  
ANISOU 5520  CB  LEU A 751     7455   7901  10448    435   1362    920       C  
ATOM   5521  CG  LEU A 751      46.447  71.246 -10.004  1.00 68.26           C  
ANISOU 5521  CG  LEU A 751     7482   7916  10536    440   1371    923       C  
ATOM   5522  CD1 LEU A 751      45.850  71.167  -8.607  1.00 65.77           C  
ANISOU 5522  CD1 LEU A 751     7149   7623  10219    393   1307    822       C  
ATOM   5523  CD2 LEU A 751      46.881  72.671 -10.311  1.00 66.78           C  
ANISOU 5523  CD2 LEU A 751     7241   7638  10493    449   1450    961       C  
ATOM   5524  N   HIS A 752      46.501  68.510 -12.525  1.00 76.15           N  
ANISOU 5524  N   HIS A 752     8637   9064  11232    534   1344   1064       N  
ATOM   5525  CA  HIS A 752      45.590  68.309 -13.659  1.00 80.07           C  
ANISOU 5525  CA  HIS A 752     9186   9598  11640    588   1348   1139       C  
ATOM   5526  C   HIS A 752      44.676  67.135 -13.449  1.00 78.87           C  
ANISOU 5526  C   HIS A 752     9083   9525  11359    586   1270   1103       C  
ATOM   5527  O   HIS A 752      43.471  67.224 -13.697  1.00 82.63           O  
ANISOU 5527  O   HIS A 752     9584  10026  11786    609   1248   1119       O  
ATOM   5528  CB  HIS A 752      46.354  68.149 -14.975  1.00 87.18           C  
ANISOU 5528  CB  HIS A 752    10109  10496  12519    633   1404   1225       C  
ATOM   5529  CG  HIS A 752      46.591  69.452 -15.717  1.00 99.76           C  
ANISOU 5529  CG  HIS A 752    11676  12020  14208    664   1489   1302       C  
ATOM   5530  ND1 HIS A 752      47.830  69.927 -15.980  1.00104.28           N  
ANISOU 5530  ND1 HIS A 752    12214  12537  14870    661   1555   1330       N  
ATOM   5531  CD2 HIS A 752      45.693  70.377 -16.263  1.00102.02           C  
ANISOU 5531  CD2 HIS A 752    11964  12282  14515    699   1518   1361       C  
ATOM   5532  CE1 HIS A 752      47.731  71.094 -16.655  1.00103.66           C  
ANISOU 5532  CE1 HIS A 752    12117  12401  14866    693   1626   1404       C  
ATOM   5533  NE2 HIS A 752      46.425  71.370 -16.822  1.00103.22           N  
ANISOU 5533  NE2 HIS A 752    12085  12366  14768    717   1602   1424       N  
ATOM   5534  N   GLN A 753      45.240  66.031 -12.967  1.00 74.84           N  
ANISOU 5534  N   GLN A 753     8583   9055  10798    559   1227   1054       N  
ATOM   5535  CA  GLN A 753      44.484  64.809 -12.730  1.00 73.19           C  
ANISOU 5535  CA  GLN A 753     8419   8920  10471    555   1154   1018       C  
ATOM   5536  C   GLN A 753      43.454  64.937 -11.614  1.00 70.95           C  
ANISOU 5536  C   GLN A 753     8125   8648  10187    521   1102    950       C  
ATOM   5537  O   GLN A 753      42.335  64.438 -11.744  1.00 71.22           O  
ANISOU 5537  O   GLN A 753     8194   8728  10138    535   1060    948       O  
ATOM   5538  CB  GLN A 753      45.432  63.658 -12.429  1.00 72.04           C  
ANISOU 5538  CB  GLN A 753     8281   8806  10286    532   1124    982       C  
ATOM   5539  CG  GLN A 753      46.328  63.330 -13.600  1.00 73.36           C  
ANISOU 5539  CG  GLN A 753     8466   8975  10434    568   1169   1047       C  
ATOM   5540  CD  GLN A 753      47.569  62.588 -13.176  1.00 72.55           C  
ANISOU 5540  CD  GLN A 753     8350   8875  10342    539   1158   1010       C  
ATOM   5541  OE1 GLN A 753      47.648  61.371 -13.330  1.00 74.53           O  
ANISOU 5541  OE1 GLN A 753     8634   9179  10505    542   1119    998       O  
ATOM   5542  NE2 GLN A 753      48.541  63.311 -12.621  1.00 70.41           N  
ANISOU 5542  NE2 GLN A 753     8027   8545  10181    510   1192    987       N  
ATOM   5543  N   LEU A 754      43.830  65.596 -10.522  1.00 66.62           N  
ANISOU 5543  N   LEU A 754     7526   8057   9730    476   1104    892       N  
ATOM   5544  CA  LEU A 754      42.921  65.766  -9.401  1.00 67.15           C  
ANISOU 5544  CA  LEU A 754     7579   8133   9800    442   1059    823       C  
ATOM   5545  C   LEU A 754      41.708  66.586  -9.822  1.00 68.46           C  
ANISOU 5545  C   LEU A 754     7750   8284   9976    469   1074    857       C  
ATOM   5546  O   LEU A 754      40.569  66.303  -9.421  1.00 64.61           O  
ANISOU 5546  O   LEU A 754     7281   7833   9435    463   1028    826       O  
ATOM   5547  CB  LEU A 754      43.627  66.446  -8.236  1.00 66.19           C  
ANISOU 5547  CB  LEU A 754     7399   7966   9784    393   1066    757       C  
ATOM   5548  CG  LEU A 754      44.649  65.626  -7.458  1.00 66.02           C  
ANISOU 5548  CG  LEU A 754     7368   7964   9752    356   1034    700       C  
ATOM   5549  CD1 LEU A 754      45.399  66.550  -6.520  1.00 65.71           C  
ANISOU 5549  CD1 LEU A 754     7265   7870   9833    318   1054    646       C  
ATOM   5550  CD2 LEU A 754      43.984  64.514  -6.668  1.00 64.49           C  
ANISOU 5550  CD2 LEU A 754     7206   7838   9459    332    959    644       C  
ATOM   5551  N   VAL A 755      41.971  67.600 -10.640  1.00 68.58           N  
ANISOU 5551  N   VAL A 755     7748   8247  10063    501   1139    923       N  
ATOM   5552  CA  VAL A 755      40.931  68.462 -11.176  1.00 70.04           C  
ANISOU 5552  CA  VAL A 755     7935   8411  10266    534   1161    968       C  
ATOM   5553  C   VAL A 755      40.040  67.669 -12.131  1.00 73.25           C  
ANISOU 5553  C   VAL A 755     8402   8879  10550    579   1134   1015       C  
ATOM   5554  O   VAL A 755      38.819  67.844 -12.128  1.00 75.84           O  
ANISOU 5554  O   VAL A 755     8742   9222  10850    591   1109   1013       O  
ATOM   5555  CB  VAL A 755      41.534  69.699 -11.878  1.00 68.55           C  
ANISOU 5555  CB  VAL A 755     7713   8148  10184    559   1242   1036       C  
ATOM   5556  CG1 VAL A 755      40.475  70.462 -12.663  1.00 64.98           C  
ANISOU 5556  CG1 VAL A 755     7272   7681   9735    604   1265   1099       C  
ATOM   5557  CG2 VAL A 755      42.206  70.606 -10.858  1.00 66.18           C  
ANISOU 5557  CG2 VAL A 755     7347   7784  10016    513   1266    979       C  
ATOM   5558  N   GLU A 756      40.648  66.792 -12.931  1.00 74.81           N  
ANISOU 5558  N   GLU A 756     8634   9112  10678    604   1137   1054       N  
ATOM   5559  CA  GLU A 756      39.893  65.915 -13.826  1.00 78.09           C  
ANISOU 5559  CA  GLU A 756     9106   9591  10972    647   1106   1091       C  
ATOM   5560  C   GLU A 756      38.964  64.997 -13.019  1.00 76.79           C  
ANISOU 5560  C   GLU A 756     8963   9483  10733    619   1030   1019       C  
ATOM   5561  O   GLU A 756      37.789  64.831 -13.362  1.00 77.94           O  
ANISOU 5561  O   GLU A 756     9135   9661  10819    645   1002   1029       O  
ATOM   5562  CB  GLU A 756      40.846  65.094 -14.695  1.00 83.04           C  
ANISOU 5562  CB  GLU A 756     9761  10246  11545    671   1123   1132       C  
ATOM   5563  CG  GLU A 756      40.293  64.708 -16.062  1.00 91.17           C  
ANISOU 5563  CG  GLU A 756    10840  11319  12482    734   1127   1203       C  
ATOM   5564  CD  GLU A 756      41.372  64.150 -16.986  1.00101.70           C  
ANISOU 5564  CD  GLU A 756    12193  12668  13781    761   1160   1251       C  
ATOM   5565  OE1 GLU A 756      41.297  62.954 -17.362  1.00101.34           O  
ANISOU 5565  OE1 GLU A 756    12185  12683  13634    774   1122   1243       O  
ATOM   5566  OE2 GLU A 756      42.310  64.903 -17.330  1.00103.05           O  
ANISOU 5566  OE2 GLU A 756    12339  12788  14029    768   1225   1295       O  
ATOM   5567  N   ILE A 757      39.489  64.442 -11.928  1.00 71.74           N  
ANISOU 5567  N   ILE A 757     8307   8851  10100    568    997    948       N  
ATOM   5568  CA  ILE A 757      38.753  63.496 -11.096  1.00 69.26           C  
ANISOU 5568  CA  ILE A 757     8011   8588   9716    538    928    881       C  
ATOM   5569  C   ILE A 757      37.592  64.146 -10.338  1.00 71.40           C  
ANISOU 5569  C   ILE A 757     8264   8848  10017    519    908    840       C  
ATOM   5570  O   ILE A 757      36.533  63.527 -10.156  1.00 71.22           O  
ANISOU 5570  O   ILE A 757     8268   8870   9924    519    860    814       O  
ATOM   5571  CB  ILE A 757      39.701  62.755 -10.124  1.00 69.04           C  
ANISOU 5571  CB  ILE A 757     7971   8572   9690    490    901    820       C  
ATOM   5572  CG1 ILE A 757      40.506  61.691 -10.881  1.00 67.77           C  
ANISOU 5572  CG1 ILE A 757     7841   8443   9464    511    900    852       C  
ATOM   5573  CG2 ILE A 757      38.937  62.119  -8.967  1.00 65.14           C  
ANISOU 5573  CG2 ILE A 757     7482   8115   9153    450    838    745       C  
ATOM   5574  CD1 ILE A 757      41.775  61.260 -10.171  1.00 67.27           C  
ANISOU 5574  CD1 ILE A 757     7757   8373   9431    473    895    812       C  
ATOM   5575  N   ILE A 758      37.785  65.387  -9.902  1.00 68.35           N  
ANISOU 5575  N   ILE A 758     7832   8401   9737    503    946    832       N  
ATOM   5576  CA  ILE A 758      36.755  66.080  -9.128  1.00 65.51           C  
ANISOU 5576  CA  ILE A 758     7449   8026   9416    483    931    788       C  
ATOM   5577  C   ILE A 758      35.614  66.612 -10.013  1.00 67.23           C  
ANISOU 5577  C   ILE A 758     7683   8241   9620    530    942    842       C  
ATOM   5578  O   ILE A 758      34.552  66.968  -9.513  1.00 67.78           O  
ANISOU 5578  O   ILE A 758     7744   8310   9700    519    921    808       O  
ATOM   5579  CB  ILE A 758      37.353  67.202  -8.247  1.00 63.82           C  
ANISOU 5579  CB  ILE A 758     7175   7749   9326    445    963    749       C  
ATOM   5580  CG1 ILE A 758      36.432  67.508  -7.060  1.00 62.47           C  
ANISOU 5580  CG1 ILE A 758     6981   7580   9174    406    929    673       C  
ATOM   5581  CG2 ILE A 758      37.667  68.441  -9.081  1.00 63.10           C  
ANISOU 5581  CG2 ILE A 758     7058   7593   9325    478   1032    818       C  
ATOM   5582  CD1 ILE A 758      36.967  68.564  -6.115  1.00 63.18           C  
ANISOU 5582  CD1 ILE A 758     7009   7613   9382    367    956    623       C  
ATOM   5583  N   ASN A 759      35.836  66.672 -11.322  1.00 68.51           N  
ANISOU 5583  N   ASN A 759     7869   8402   9761    582    975    925       N  
ATOM   5584  CA  ASN A 759      34.775  67.036 -12.258  1.00 70.38           C  
ANISOU 5584  CA  ASN A 759     8127   8646   9969    634    980    980       C  
ATOM   5585  C   ASN A 759      34.159  65.806 -12.933  1.00 72.98           C  
ANISOU 5585  C   ASN A 759     8511   9048  10170    665    935    993       C  
ATOM   5586  O   ASN A 759      33.423  65.937 -13.908  1.00 74.75           O  
ANISOU 5586  O   ASN A 759     8760   9288  10355    715    937   1047       O  
ATOM   5587  CB  ASN A 759      35.295  68.028 -13.309  1.00 69.50           C  
ANISOU 5587  CB  ASN A 759     8005   8485   9917    678   1050   1069       C  
ATOM   5588  CG  ASN A 759      35.381  69.452 -12.780  1.00 70.70           C  
ANISOU 5588  CG  ASN A 759     8101   8559  10201    658   1093   1062       C  
ATOM   5589  OD1 ASN A 759      34.383  70.162 -12.705  1.00 71.64           O  
ANISOU 5589  OD1 ASN A 759     8208   8659  10351    668   1091   1063       O  
ATOM   5590  ND2 ASN A 759      36.583  69.876 -12.416  1.00 72.14           N  
ANISOU 5590  ND2 ASN A 759     8247   8695  10466    632   1133   1054       N  
ATOM   5591  N   ARG A 760      34.446  64.619 -12.401  1.00 73.36           N  
ANISOU 5591  N   ARG A 760     8576   9141  10156    635    892    943       N  
ATOM   5592  CA  ARG A 760      34.097  63.376 -13.079  1.00 78.60           C  
ANISOU 5592  CA  ARG A 760     9288   9870  10705    663    853    955       C  
ATOM   5593  C   ARG A 760      32.754  62.819 -12.607  1.00 80.91           C  
ANISOU 5593  C   ARG A 760     9597  10204  10942    653    794    904       C  
ATOM   5594  O   ARG A 760      32.551  62.636 -11.405  1.00 78.53           O  
ANISOU 5594  O   ARG A 760     9278   9903  10657    602    765    834       O  
ATOM   5595  CB  ARG A 760      35.201  62.336 -12.881  1.00 81.06           C  
ANISOU 5595  CB  ARG A 760     9611  10207  10982    640    842    935       C  
ATOM   5596  CG  ARG A 760      35.382  61.356 -14.034  1.00 84.00           C  
ANISOU 5596  CG  ARG A 760    10027  10628  11262    685    834    978       C  
ATOM   5597  CD  ARG A 760      36.332  60.226 -13.649  1.00 83.77           C  
ANISOU 5597  CD  ARG A 760    10006  10625  11199    655    813    944       C  
ATOM   5598  NE  ARG A 760      35.710  59.315 -12.687  1.00 82.55           N  
ANISOU 5598  NE  ARG A 760     9859  10506  11000    617    751    873       N  
ATOM   5599  CZ  ARG A 760      35.527  58.011 -12.883  1.00 79.75           C  
ANISOU 5599  CZ  ARG A 760     9537  10206  10560    623    709    857       C  
ATOM   5600  NH1 ARG A 760      35.945  57.432 -14.001  1.00 79.44           N  
ANISOU 5600  NH1 ARG A 760     9524  10192  10466    664    719    902       N  
ATOM   5601  NH2 ARG A 760      34.942  57.282 -11.944  1.00 76.75           N  
ANISOU 5601  NH2 ARG A 760     9160   9852  10149    587    658    795       N  
ATOM   5602  N   PRO A 761      31.834  62.545 -13.557  1.00 85.63           N  
ANISOU 5602  N   PRO A 761    10226  10836  11473    702    777    939       N  
ATOM   5603  CA  PRO A 761      30.514  62.001 -13.221  1.00 85.16           C  
ANISOU 5603  CA  PRO A 761    10180  10815  11361    697    723    894       C  
ATOM   5604  C   PRO A 761      30.607  60.552 -12.751  1.00 86.66           C  
ANISOU 5604  C   PRO A 761    10393  11056  11478    669    674    843       C  
ATOM   5605  O   PRO A 761      31.509  59.819 -13.175  1.00 85.91           O  
ANISOU 5605  O   PRO A 761    10316  10982  11346    677    678    861       O  
ATOM   5606  CB  PRO A 761      29.760  62.073 -14.552  1.00 84.69           C  
ANISOU 5606  CB  PRO A 761    10148  10779  11250    764    723    954       C  
ATOM   5607  CG  PRO A 761      30.826  61.963 -15.593  1.00 86.40           C  
ANISOU 5607  CG  PRO A 761    10382  10999  11446    801    760   1020       C  
ATOM   5608  CD  PRO A 761      32.016  62.685 -15.018  1.00 86.11           C  
ANISOU 5608  CD  PRO A 761    10311  10906  11501    766    808   1022       C  
ATOM   5609  N   ASN A 762      29.679  60.151 -11.884  1.00 87.16           N  
ANISOU 5609  N   ASN A 762    10454  11139  11525    638    630    780       N  
ATOM   5610  CA  ASN A 762      29.631  58.784 -11.355  1.00 89.19           C  
ANISOU 5610  CA  ASN A 762    10731  11442  11717    610    583    731       C  
ATOM   5611  C   ASN A 762      30.905  58.422 -10.587  1.00 89.51           C  
ANISOU 5611  C   ASN A 762    10759  11473  11778    566    590    706       C  
ATOM   5612  O   ASN A 762      31.467  57.333 -10.755  1.00 93.53           O  
ANISOU 5612  O   ASN A 762    11289  12013  12233    565    572    704       O  
ATOM   5613  CB  ASN A 762      29.341  57.760 -12.473  1.00 93.13           C  
ANISOU 5613  CB  ASN A 762    11269  11992  12125    656    559    758       C  
ATOM   5614  CG  ASN A 762      28.127  58.135 -13.319  1.00 97.61           C  
ANISOU 5614  CG  ASN A 762    11847  12571  12670    705    551    784       C  
ATOM   5615  OD1 ASN A 762      27.103  58.580 -12.796  1.00 95.06           O  
ANISOU 5615  OD1 ASN A 762    11509  12237  12371    693    536    754       O  
ATOM   5616  ND2 ASN A 762      28.240  57.953 -14.633  1.00 95.81           N  
ANISOU 5616  ND2 ASN A 762    11644  12366  12394    763    560    840       N  
ATOM   5617  N   THR A 763      31.361  59.357  -9.757  1.00 80.63           N  
ANISOU 5617  N   THR A 763     9598  10302  10734    531    616    687       N  
ATOM   5618  CA  THR A 763      32.527  59.143  -8.914  1.00 72.26           C  
ANISOU 5618  CA  THR A 763     8522   9231   9704    488    621    657       C  
ATOM   5619  C   THR A 763      32.078  59.098  -7.455  1.00 66.32           C  
ANISOU 5619  C   THR A 763     7750   8481   8968    433    592    583       C  
ATOM   5620  O   THR A 763      31.394  60.006  -6.989  1.00 69.10           O  
ANISOU 5620  O   THR A 763     8078   8808   9369    421    600    562       O  
ATOM   5621  CB  THR A 763      33.596  60.224  -9.163  1.00 71.17           C  
ANISOU 5621  CB  THR A 763     8354   9039   9648    493    677    694       C  
ATOM   5622  OG1 THR A 763      34.034  60.142 -10.525  1.00 73.85           O  
ANISOU 5622  OG1 THR A 763     8715   9382   9961    545    705    764       O  
ATOM   5623  CG2 THR A 763      34.792  60.027  -8.261  1.00 69.47           C  
ANISOU 5623  CG2 THR A 763     8118   8811   9467    448    679    657       C  
ATOM   5624  N   PRO A 764      32.442  58.024  -6.737  1.00 61.94           N  
ANISOU 5624  N   PRO A 764     7205   7958   8370    400    557    543       N  
ATOM   5625  CA  PRO A 764      31.981  57.833  -5.366  1.00 61.63           C  
ANISOU 5625  CA  PRO A 764     7153   7930   8332    350    527    475       C  
ATOM   5626  C   PRO A 764      32.177  59.062  -4.492  1.00 63.88           C  
ANISOU 5626  C   PRO A 764     7396   8173   8704    319    552    443       C  
ATOM   5627  O   PRO A 764      33.161  59.786  -4.642  1.00 66.64           O  
ANISOU 5627  O   PRO A 764     7722   8484   9115    321    588    463       O  
ATOM   5628  CB  PRO A 764      32.851  56.678  -4.855  1.00 59.70           C  
ANISOU 5628  CB  PRO A 764     6922   7715   8047    324    501    453       C  
ATOM   5629  CG  PRO A 764      33.195  55.904  -6.080  1.00 58.57           C  
ANISOU 5629  CG  PRO A 764     6809   7592   7852    366    501    504       C  
ATOM   5630  CD  PRO A 764      33.299  56.912  -7.193  1.00 60.43           C  
ANISOU 5630  CD  PRO A 764     7039   7795   8127    409    546    562       C  
ATOM   5631  N   LYS A 765      31.225  59.274  -3.589  1.00 65.61           N  
ANISOU 5631  N   LYS A 765     7603   8398   8928    291    534    392       N  
ATOM   5632  CA  LYS A 765      31.243  60.357  -2.613  1.00 65.59           C  
ANISOU 5632  CA  LYS A 765     7558   8360   9001    257    551    349       C  
ATOM   5633  C   LYS A 765      32.621  60.495  -1.944  1.00 62.95           C  
ANISOU 5633  C   LYS A 765     7199   8010   8709    227    562    327       C  
ATOM   5634  O   LYS A 765      33.163  61.591  -1.872  1.00 61.60           O  
ANISOU 5634  O   LYS A 765     6992   7793   8621    223    598    328       O  
ATOM   5635  CB  LYS A 765      30.118  60.117  -1.584  1.00 70.72           C  
ANISOU 5635  CB  LYS A 765     8207   9037   9625    224    519    288       C  
ATOM   5636  CG  LYS A 765      29.949  61.157  -0.478  1.00 76.31           C  
ANISOU 5636  CG  LYS A 765     8873   9718  10404    187    532    231       C  
ATOM   5637  CD  LYS A 765      28.906  60.742   0.575  1.00 82.47           C  
ANISOU 5637  CD  LYS A 765     9656  10533  11146    153    499    170       C  
ATOM   5638  CE  LYS A 765      29.282  59.492   1.382  1.00 81.56           C  
ANISOU 5638  CE  LYS A 765     9562  10465  10962    122    462    139       C  
ATOM   5639  NZ  LYS A 765      30.502  59.641   2.229  1.00 83.74           N  
ANISOU 5639  NZ  LYS A 765     9815  10735  11267     90    465    109       N  
ATOM   5640  N   THR A 766      33.194  59.381  -1.492  1.00 60.97           N  
ANISOU 5640  N   THR A 766     6966   7795   8403    207    531    309       N  
ATOM   5641  CA  THR A 766      34.440  59.412  -0.725  1.00 58.74           C  
ANISOU 5641  CA  THR A 766     6661   7505   8155    175    533    281       C  
ATOM   5642  C   THR A 766      35.660  59.812  -1.560  1.00 54.60           C  
ANISOU 5642  C   THR A 766     6124   6943   7678    199    570    328       C  
ATOM   5643  O   THR A 766      36.481  60.612  -1.123  1.00 49.95           O  
ANISOU 5643  O   THR A 766     5497   6318   7164    181    594    309       O  
ATOM   5644  CB  THR A 766      34.673  58.086   0.011  1.00 60.76           C  
ANISOU 5644  CB  THR A 766     6939   7809   8338    149    487    250       C  
ATOM   5645  OG1 THR A 766      33.542  57.818   0.838  1.00 60.89           O  
ANISOU 5645  OG1 THR A 766     6963   7855   8316    125    458    206       O  
ATOM   5646  CG2 THR A 766      35.903  58.165   0.902  1.00 64.31           C  
ANISOU 5646  CG2 THR A 766     7361   8251   8821    116    484    215       C  
ATOM   5647  N   LEU A 767      35.763  59.302  -2.774  1.00 53.07           N  
ANISOU 5647  N   LEU A 767     5961   6757   7445    240    578    389       N  
ATOM   5648  CA  LEU A 767      36.852  59.740  -3.627  1.00 54.33           C  
ANISOU 5648  CA  LEU A 767     6109   6881   7651    264    620    438       C  
ATOM   5649  C   LEU A 767      36.783  61.248  -3.867  1.00 55.25           C  
ANISOU 5649  C   LEU A 767     6190   6941   7861    275    669    454       C  
ATOM   5650  O   LEU A 767      37.816  61.928  -3.871  1.00 54.86           O  
ANISOU 5650  O   LEU A 767     6109   6850   7887    270    704    461       O  
ATOM   5651  CB  LEU A 767      36.886  58.966  -4.946  1.00 54.55           C  
ANISOU 5651  CB  LEU A 767     6178   6931   7616    310    622    500       C  
ATOM   5652  CG  LEU A 767      38.008  59.285  -5.950  1.00 56.03           C  
ANISOU 5652  CG  LEU A 767     6360   7088   7840    340    668    558       C  
ATOM   5653  CD1 LEU A 767      39.398  59.275  -5.317  1.00 55.29           C  
ANISOU 5653  CD1 LEU A 767     6239   6975   7794    309    675    532       C  
ATOM   5654  CD2 LEU A 767      37.971  58.328  -7.132  1.00 54.57           C  
ANISOU 5654  CD2 LEU A 767     6219   6938   7578    381    661    608       C  
ATOM   5655  N   LEU A 768      35.568  61.775  -4.040  1.00 55.60           N  
ANISOU 5655  N   LEU A 768     6237   6982   7908    288    671    458       N  
ATOM   5656  CA  LEU A 768      35.408  63.193  -4.350  1.00 55.00           C  
ANISOU 5656  CA  LEU A 768     6127   6849   7921    303    718    479       C  
ATOM   5657  C   LEU A 768      35.765  64.059  -3.159  1.00 53.76           C  
ANISOU 5657  C   LEU A 768     5920   6658   7849    259    727    417       C  
ATOM   5658  O   LEU A 768      36.390  65.108  -3.323  1.00 53.74           O  
ANISOU 5658  O   LEU A 768     5880   6601   7939    262    773    431       O  
ATOM   5659  CB  LEU A 768      33.996  63.512  -4.836  1.00 58.31           C  
ANISOU 5659  CB  LEU A 768     6562   7274   8321    330    714    499       C  
ATOM   5660  CG  LEU A 768      33.562  63.062  -6.237  1.00 60.47           C  
ANISOU 5660  CG  LEU A 768     6877   7568   8532    385    717    570       C  
ATOM   5661  CD1 LEU A 768      32.067  63.317  -6.421  1.00 58.45           C  
ANISOU 5661  CD1 LEU A 768     6629   7321   8256    403    702    569       C  
ATOM   5662  CD2 LEU A 768      34.363  63.740  -7.338  1.00 59.05           C  
ANISOU 5662  CD2 LEU A 768     6690   7348   8399    424    771    643       C  
ATOM   5663  N   GLU A 769      35.375  63.609  -1.968  1.00 51.01           N  
ANISOU 5663  N   GLU A 769     5569   6343   7470    218    686    347       N  
ATOM   5664  CA  GLU A 769      35.742  64.279  -0.726  1.00 53.01           C  
ANISOU 5664  CA  GLU A 769     5776   6575   7790    173    687    277       C  
ATOM   5665  C   GLU A 769      37.264  64.356  -0.522  1.00 55.38           C  
ANISOU 5665  C   GLU A 769     6051   6854   8139    159    703    271       C  
ATOM   5666  O   GLU A 769      37.796  65.429  -0.220  1.00 56.73           O  
ANISOU 5666  O   GLU A 769     6173   6974   8407    147    736    251       O  
ATOM   5667  CB  GLU A 769      35.061  63.615   0.467  1.00 54.26           C  
ANISOU 5667  CB  GLU A 769     5944   6784   7889    136    638    209       C  
ATOM   5668  CG  GLU A 769      33.551  63.818   0.446  1.00 62.54           C  
ANISOU 5668  CG  GLU A 769     7004   7843   8917    143    629    202       C  
ATOM   5669  CD  GLU A 769      32.778  62.972   1.458  1.00 62.82           C  
ANISOU 5669  CD  GLU A 769     7058   7933   8879    111    581    146       C  
ATOM   5670  OE1 GLU A 769      33.354  62.056   2.083  1.00 63.80           O  
ANISOU 5670  OE1 GLU A 769     7195   8093   8952     87    551    121       O  
ATOM   5671  OE2 GLU A 769      31.567  63.239   1.629  1.00 64.09           O  
ANISOU 5671  OE2 GLU A 769     7219   8099   9033    110    575    127       O  
ATOM   5672  N   ASN A 770      37.953  63.225  -0.685  1.00 51.68           N  
ANISOU 5672  N   ASN A 770     5611   6419   7605    161    679    285       N  
ATOM   5673  CA  ASN A 770      39.389  63.197  -0.536  1.00 50.71           C  
ANISOU 5673  CA  ASN A 770     5465   6278   7523    150    691    280       C  
ATOM   5674  C   ASN A 770      40.042  64.055  -1.608  1.00 52.33           C  
ANISOU 5674  C   ASN A 770     5652   6425   7806    182    751    340       C  
ATOM   5675  O   ASN A 770      40.914  64.867  -1.291  1.00 51.91           O  
ANISOU 5675  O   ASN A 770     5552   6326   7845    168    780    320       O  
ATOM   5676  CB  ASN A 770      39.930  61.766  -0.527  1.00 50.30           C  
ANISOU 5676  CB  ASN A 770     5450   6275   7386    147    653    285       C  
ATOM   5677  CG  ASN A 770      39.812  61.116   0.839  1.00 54.19           C  
ANISOU 5677  CG  ASN A 770     5943   6812   7835    105    601    214       C  
ATOM   5678  OD1 ASN A 770      40.194  61.706   1.855  1.00 56.26           O  
ANISOU 5678  OD1 ASN A 770     6165   7060   8150     72    598    155       O  
ATOM   5679  ND2 ASN A 770      39.261  59.897   0.880  1.00 53.39           N  
ANISOU 5679  ND2 ASN A 770     5886   6764   7635    106    559    218       N  
ATOM   5680  N   THR A 771      39.581  63.931  -2.853  1.00 52.29           N  
ANISOU 5680  N   THR A 771     5680   6421   7766    227    770    412       N  
ATOM   5681  CA  THR A 771      40.092  64.784  -3.925  1.00 53.90           C  
ANISOU 5681  CA  THR A 771     5869   6571   8039    261    831    478       C  
ATOM   5682  C   THR A 771      39.964  66.275  -3.602  1.00 58.05           C  
ANISOU 5682  C   THR A 771     6342   7035   8680    252    871    461       C  
ATOM   5683  O   THR A 771      40.911  67.042  -3.826  1.00 58.18           O  
ANISOU 5683  O   THR A 771     6322   6998   8788    254    918    477       O  
ATOM   5684  CB  THR A 771      39.434  64.493  -5.274  1.00 53.71           C  
ANISOU 5684  CB  THR A 771     5889   6563   7954    313    843    555       C  
ATOM   5685  OG1 THR A 771      39.542  63.098  -5.559  1.00 55.61           O  
ANISOU 5685  OG1 THR A 771     6176   6861   8093    321    805    565       O  
ATOM   5686  CG2 THR A 771      40.125  65.274  -6.384  1.00 56.45           C  
ANISOU 5686  CG2 THR A 771     6223   6859   8366    350    908    628       C  
ATOM   5687  N   ALA A 772      38.808  66.674  -3.070  1.00 56.07           N  
ANISOU 5687  N   ALA A 772     6084   6789   8429    240    854    426       N  
ATOM   5688  CA  ALA A 772      38.579  68.066  -2.702  1.00 57.17           C  
ANISOU 5688  CA  ALA A 772     6172   6871   8678    230    889    403       C  
ATOM   5689  C   ALA A 772      39.526  68.515  -1.599  1.00 58.10           C  
ANISOU 5689  C   ALA A 772     6238   6964   8875    186    891    332       C  
ATOM   5690  O   ALA A 772      40.179  69.545  -1.737  1.00 60.54           O  
ANISOU 5690  O   ALA A 772     6501   7210   9293    187    939    340       O  
ATOM   5691  CB  ALA A 772      37.132  68.305  -2.291  1.00 56.89           C  
ANISOU 5691  CB  ALA A 772     6143   6853   8622    224    865    374       C  
ATOM   5692  N   ILE A 773      39.594  67.755  -0.512  1.00 55.39           N  
ANISOU 5692  N   ILE A 773     5899   6668   8477    148    839    263       N  
ATOM   5693  CA  ILE A 773      40.517  68.064   0.576  1.00 58.06           C  
ANISOU 5693  CA  ILE A 773     6189   6992   8878    108    834    190       C  
ATOM   5694  C   ILE A 773      41.968  68.211   0.102  1.00 59.11           C  
ANISOU 5694  C   ILE A 773     6300   7086   9072    116    869    219       C  
ATOM   5695  O   ILE A 773      42.654  69.181   0.434  1.00 58.31           O  
ANISOU 5695  O   ILE A 773     6141   6931   9081    101    901    190       O  
ATOM   5696  CB  ILE A 773      40.436  66.997   1.673  1.00 59.28           C  
ANISOU 5696  CB  ILE A 773     6365   7215   8945     74    770    126       C  
ATOM   5697  CG1 ILE A 773      39.183  67.251   2.511  1.00 59.83           C  
ANISOU 5697  CG1 ILE A 773     6430   7306   8996     52    745     72       C  
ATOM   5698  CG2 ILE A 773      41.684  67.013   2.554  1.00 58.27           C  
ANISOU 5698  CG2 ILE A 773     6197   7081   8861     42    759     68       C  
ATOM   5699  CD1 ILE A 773      38.775  66.052   3.323  1.00 61.99           C  
ANISOU 5699  CD1 ILE A 773     6741   7654   9159     30    685     32       C  
ATOM   5700  N   THR A 774      42.420  67.256  -0.694  1.00 58.83           N  
ANISOU 5700  N   THR A 774     6307   7077   8969    140    863    274       N  
ATOM   5701  CA  THR A 774      43.795  67.257  -1.176  1.00 57.79           C  
ANISOU 5701  CA  THR A 774     6159   6914   8886    148    895    303       C  
ATOM   5702  C   THR A 774      44.083  68.495  -2.035  1.00 59.90           C  
ANISOU 5702  C   THR A 774     6392   7105   9263    174    968    356       C  
ATOM   5703  O   THR A 774      45.107  69.154  -1.847  1.00 61.22           O  
ANISOU 5703  O   THR A 774     6509   7222   9530    162   1001    338       O  
ATOM   5704  CB  THR A 774      44.110  65.934  -1.889  1.00 54.56           C  
ANISOU 5704  CB  THR A 774     5804   6551   8375    170    874    351       C  
ATOM   5705  OG1 THR A 774      44.215  64.909  -0.894  1.00 50.74           O  
ANISOU 5705  OG1 THR A 774     5335   6123   7820    139    812    292       O  
ATOM   5706  CG2 THR A 774      45.410  66.015  -2.697  1.00 55.49           C  
ANISOU 5706  CG2 THR A 774     5909   6630   8543    189    919    399       C  
ATOM   5707  N   ILE A 775      43.162  68.827  -2.939  1.00 60.83           N  
ANISOU 5707  N   ILE A 775     6535   7214   9365    210    992    419       N  
ATOM   5708  CA  ILE A 775      43.284  70.036  -3.754  1.00 63.36           C  
ANISOU 5708  CA  ILE A 775     6824   7462   9786    237   1062    476       C  
ATOM   5709  C   ILE A 775      43.345  71.267  -2.861  1.00 62.54           C  
ANISOU 5709  C   ILE A 775     6652   7303   9806    206   1082    413       C  
ATOM   5710  O   ILE A 775      44.173  72.141  -3.064  1.00 63.66           O  
ANISOU 5710  O   ILE A 775     6748   7380  10061    207   1135    425       O  
ATOM   5711  CB  ILE A 775      42.123  70.177  -4.759  1.00 65.97           C  
ANISOU 5711  CB  ILE A 775     7195   7801  10071    281   1076    548       C  
ATOM   5712  CG1 ILE A 775      42.280  69.153  -5.890  1.00 67.26           C  
ANISOU 5712  CG1 ILE A 775     7417   8005  10134    320   1073    621       C  
ATOM   5713  CG2 ILE A 775      42.065  71.600  -5.305  1.00 64.89           C  
ANISOU 5713  CG2 ILE A 775     7018   7586  10051    302   1143    592       C  
ATOM   5714  CD1 ILE A 775      41.188  69.193  -6.943  1.00 68.02           C  
ANISOU 5714  CD1 ILE A 775     7555   8115  10175    367   1082    693       C  
ATOM   5715  N   GLY A 776      42.468  71.308  -1.864  1.00 61.38           N  
ANISOU 5715  N   GLY A 776     6499   7183   9638    177   1040    343       N  
ATOM   5716  CA  GLY A 776      42.493  72.339  -0.840  1.00 59.56           C  
ANISOU 5716  CA  GLY A 776     6204   6912   9513    142   1048    266       C  
ATOM   5717  C   GLY A 776      43.838  72.442  -0.155  1.00 57.18           C  
ANISOU 5717  C   GLY A 776     5856   6590   9280    112   1051    210       C  
ATOM   5718  O   GLY A 776      44.344  73.537   0.061  1.00 57.24           O  
ANISOU 5718  O   GLY A 776     5801   6531   9415    101   1092    186       O  
ATOM   5719  N   ARG A 777      44.414  71.296   0.178  1.00 57.37           N  
ANISOU 5719  N   ARG A 777     5908   6668   9221     99   1006    189       N  
ATOM   5720  CA  ARG A 777      45.695  71.235   0.892  1.00 59.08           C  
ANISOU 5720  CA  ARG A 777     6084   6875   9489     70    998    131       C  
ATOM   5721  C   ARG A 777      46.889  71.696   0.045  1.00 61.11           C  
ANISOU 5721  C   ARG A 777     6312   7068   9837     89   1059    183       C  
ATOM   5722  O   ARG A 777      47.738  72.465   0.516  1.00 61.58           O  
ANISOU 5722  O   ARG A 777     6308   7077  10011     69   1083    137       O  
ATOM   5723  CB  ARG A 777      45.921  69.829   1.448  1.00 55.52           C  
ANISOU 5723  CB  ARG A 777     5674   6502   8920     54    932    101       C  
ATOM   5724  CG  ARG A 777      45.149  69.596   2.737  1.00 54.50           C  
ANISOU 5724  CG  ARG A 777     5545   6423   8738     19    874     17       C  
ATOM   5725  CD  ARG A 777      45.216  68.164   3.240  1.00 52.93           C  
ANISOU 5725  CD  ARG A 777     5393   6304   8415      6    810     -3       C  
ATOM   5726  NE  ARG A 777      45.060  68.162   4.689  1.00 54.08           N  
ANISOU 5726  NE  ARG A 777     5514   6483   8550    -34    764    -99       N  
ATOM   5727  CZ  ARG A 777      44.978  67.080   5.458  1.00 54.94           C  
ANISOU 5727  CZ  ARG A 777     5655   6662   8558    -53    704   -134       C  
ATOM   5728  NH1 ARG A 777      45.008  65.853   4.934  1.00 54.53           N  
ANISOU 5728  NH1 ARG A 777     5660   6652   8407    -36    680    -83       N  
ATOM   5729  NH2 ARG A 777      44.842  67.236   6.772  1.00 54.69           N  
ANISOU 5729  NH2 ARG A 777     5596   6657   8525    -88    669   -222       N  
ATOM   5730  N   LEU A 778      46.934  71.238  -1.203  1.00 61.95           N  
ANISOU 5730  N   LEU A 778     6464   7178   9895    128   1085    277       N  
ATOM   5731  CA  LEU A 778      47.959  71.671  -2.152  1.00 63.52           C  
ANISOU 5731  CA  LEU A 778     6643   7318  10173    152   1150    339       C  
ATOM   5732  C   LEU A 778      47.939  73.186  -2.321  1.00 66.27           C  
ANISOU 5732  C   LEU A 778     6933   7582  10666    156   1215    349       C  
ATOM   5733  O   LEU A 778      48.990  73.833  -2.380  1.00 66.49           O  
ANISOU 5733  O   LEU A 778     6909   7548  10807    150   1260    344       O  
ATOM   5734  CB  LEU A 778      47.749  71.006  -3.512  1.00 62.42           C  
ANISOU 5734  CB  LEU A 778     6567   7202   9948    198   1168    442       C  
ATOM   5735  CG  LEU A 778      47.994  69.502  -3.642  1.00 62.34           C  
ANISOU 5735  CG  LEU A 778     6613   7264   9811    202   1118    450       C  
ATOM   5736  CD1 LEU A 778      47.452  69.035  -4.984  1.00 63.00           C  
ANISOU 5736  CD1 LEU A 778     6756   7370   9811    250   1137    546       C  
ATOM   5737  CD2 LEU A 778      49.466  69.147  -3.519  1.00 59.97           C  
ANISOU 5737  CD2 LEU A 778     6288   6950   9547    189   1125    432       C  
ATOM   5738  N   GLY A 779      46.733  73.744  -2.390  1.00 65.32           N  
ANISOU 5738  N   GLY A 779     6819   7456  10543    166   1218    360       N  
ATOM   5739  CA  GLY A 779      46.565  75.173  -2.539  1.00 66.17           C  
ANISOU 5739  CA  GLY A 779     6873   7484  10786    172   1277    371       C  
ATOM   5740  C   GLY A 779      47.009  75.956  -1.321  1.00 67.11           C  
ANISOU 5740  C   GLY A 779     6917   7566  11018    127   1273    268       C  
ATOM   5741  O   GLY A 779      47.415  77.105  -1.439  1.00 66.87           O  
ANISOU 5741  O   GLY A 779     6826   7456  11126    127   1331    270       O  
ATOM   5742  N   TYR A 780      46.923  75.337  -0.149  1.00 65.08           N  
ANISOU 5742  N   TYR A 780     6661   7366  10701     90   1206    177       N  
ATOM   5743  CA  TYR A 780      47.257  76.014   1.096  1.00 65.22           C  
ANISOU 5743  CA  TYR A 780     6608   7360  10811     48   1193     69       C  
ATOM   5744  C   TYR A 780      48.762  76.260   1.168  1.00 67.02           C  
ANISOU 5744  C   TYR A 780     6785   7542  11137     37   1222     48       C  
ATOM   5745  O   TYR A 780      49.200  77.350   1.528  1.00 66.07           O  
ANISOU 5745  O   TYR A 780     6593   7355  11157     21   1258      4       O  
ATOM   5746  CB  TYR A 780      46.765  75.172   2.272  1.00 62.89           C  
ANISOU 5746  CB  TYR A 780     6337   7149  10409     16   1112    -15       C  
ATOM   5747  CG  TYR A 780      47.039  75.705   3.656  1.00 63.28           C  
ANISOU 5747  CG  TYR A 780     6322   7193  10527    -28   1087   -134       C  
ATOM   5748  CD1 TYR A 780      46.783  77.036   3.992  1.00 64.28           C  
ANISOU 5748  CD1 TYR A 780     6384   7257  10784    -39   1123   -176       C  
ATOM   5749  CD2 TYR A 780      47.515  74.857   4.651  1.00 64.62           C  
ANISOU 5749  CD2 TYR A 780     6498   7426  10630    -57   1025   -207       C  
ATOM   5750  CE1 TYR A 780      47.024  77.504   5.279  1.00 63.14           C  
ANISOU 5750  CE1 TYR A 780     6179   7113  10698    -79   1098   -292       C  
ATOM   5751  CE2 TYR A 780      47.757  75.311   5.933  1.00 64.23           C  
ANISOU 5751  CE2 TYR A 780     6392   7380  10634    -95    998   -319       C  
ATOM   5752  CZ  TYR A 780      47.509  76.631   6.239  1.00 64.41           C  
ANISOU 5752  CZ  TYR A 780     6349   7341  10783   -106   1035   -363       C  
ATOM   5753  OH  TYR A 780      47.745  77.063   7.516  1.00 67.32           O  
ANISOU 5753  OH  TYR A 780     6660   7717  11201   -143   1006   -479       O  
ATOM   5754  N   VAL A 781      49.539  75.242   0.799  1.00 67.48           N  
ANISOU 5754  N   VAL A 781     6879   7634  11125     45   1206     79       N  
ATOM   5755  CA  VAL A 781      51.000  75.306   0.853  1.00 66.23           C  
ANISOU 5755  CA  VAL A 781     6677   7439  11047     35   1227     59       C  
ATOM   5756  C   VAL A 781      51.594  75.981  -0.386  1.00 67.92           C  
ANISOU 5756  C   VAL A 781     6874   7576  11358     67   1314    150       C  
ATOM   5757  O   VAL A 781      52.657  76.597  -0.308  1.00 69.80           O  
ANISOU 5757  O   VAL A 781     7050   7752  11719     57   1353    127       O  
ATOM   5758  CB  VAL A 781      51.647  73.913   1.088  1.00 64.50           C  
ANISOU 5758  CB  VAL A 781     6499   7290  10718     27   1171     45       C  
ATOM   5759  CG1 VAL A 781      51.246  73.348   2.446  1.00 63.10           C  
ANISOU 5759  CG1 VAL A 781     6327   7184  10466     -8   1090    -52       C  
ATOM   5760  CG2 VAL A 781      51.315  72.931  -0.028  1.00 61.39           C  
ANISOU 5760  CG2 VAL A 781     6184   6937  10204     64   1171    144       C  
ATOM   5761  N   CYS A 782      50.897  75.875  -1.518  1.00 68.65           N  
ANISOU 5761  N   CYS A 782     7019   7670  11393    107   1343    251       N  
ATOM   5762  CA  CYS A 782      51.359  76.453  -2.777  1.00 65.65           C  
ANISOU 5762  CA  CYS A 782     6632   7224  11087    143   1426    349       C  
ATOM   5763  C   CYS A 782      50.246  77.142  -3.556  1.00 64.59           C  
ANISOU 5763  C   CYS A 782     6518   7065  10959    177   1465    424       C  
ATOM   5764  O   CYS A 782      49.923  76.742  -4.677  1.00 65.26           O  
ANISOU 5764  O   CYS A 782     6659   7168  10969    218   1486    521       O  
ATOM   5765  CB  CYS A 782      51.999  75.388  -3.654  1.00 65.97           C  
ANISOU 5765  CB  CYS A 782     6727   7301  11040    168   1429    417       C  
ATOM   5766  SG  CYS A 782      53.428  74.570  -2.924  1.00 72.05           S  
ANISOU 5766  SG  CYS A 782     7473   8092  11810    136   1390    344       S  
ATOM   5767  N   PRO A 783      49.686  78.215  -2.989  1.00 64.05           N  
ANISOU 5767  N   PRO A 783     6400   6952  10986    161   1478    380       N  
ATOM   5768  CA  PRO A 783      48.573  78.893  -3.644  1.00 67.51           C  
ANISOU 5768  CA  PRO A 783     6852   7365  11432    192   1510    446       C  
ATOM   5769  C   PRO A 783      48.884  79.269  -5.078  1.00 71.95           C  
ANISOU 5769  C   PRO A 783     7429   7878  12031    239   1588    569       C  
ATOM   5770  O   PRO A 783      47.986  79.277  -5.921  1.00 73.93           O  
ANISOU 5770  O   PRO A 783     7727   8142  12223    277   1600    649       O  
ATOM   5771  CB  PRO A 783      48.384  80.162  -2.801  1.00 67.11           C  
ANISOU 5771  CB  PRO A 783     6723   7251  11525    163   1528    372       C  
ATOM   5772  CG  PRO A 783      49.631  80.291  -1.988  1.00 64.63           C  
ANISOU 5772  CG  PRO A 783     6346   6910  11299    126   1526    288       C  
ATOM   5773  CD  PRO A 783      50.082  78.888  -1.743  1.00 63.25           C  
ANISOU 5773  CD  PRO A 783     6221   6818  10992    116   1464    267       C  
ATOM   5774  N   GLN A 784      50.151  79.564  -5.353  1.00 75.09           N  
ANISOU 5774  N   GLN A 784     7787   8221  12523    237   1640    583       N  
ATOM   5775  CA  GLN A 784      50.530  80.087  -6.656  1.00 77.98           C  
ANISOU 5775  CA  GLN A 784     8155   8528  12945    280   1725    698       C  
ATOM   5776  C   GLN A 784      50.373  79.061  -7.781  1.00 77.89           C  
ANISOU 5776  C   GLN A 784     8229   8579  12788    323   1720    793       C  
ATOM   5777  O   GLN A 784      50.023  79.421  -8.905  1.00 78.39           O  
ANISOU 5777  O   GLN A 784     8318   8620  12847    369   1773    898       O  
ATOM   5778  CB  GLN A 784      51.946  80.671  -6.618  1.00 78.87           C  
ANISOU 5778  CB  GLN A 784     8200   8565  13204    265   1784    684       C  
ATOM   5779  CG  GLN A 784      52.033  82.082  -7.193  1.00 81.38           C  
ANISOU 5779  CG  GLN A 784     8464   8778  13679    284   1876    742       C  
ATOM   5780  CD  GLN A 784      51.295  83.125  -6.352  1.00 82.82           C  
ANISOU 5780  CD  GLN A 784     8590   8918  13961    261   1870    676       C  
ATOM   5781  OE1 GLN A 784      50.484  83.902  -6.868  1.00 79.84           O  
ANISOU 5781  OE1 GLN A 784     8213   8502  13622    287   1908    736       O  
ATOM   5782  NE2 GLN A 784      51.567  83.139  -5.049  1.00 84.15           N  
ANISOU 5782  NE2 GLN A 784     8709   9093  14169    211   1822    549       N  
ATOM   5783  N   GLU A 785      50.606  77.787  -7.473  1.00 79.29           N  
ANISOU 5783  N   GLU A 785     8448   8833  12844    310   1657    756       N  
ATOM   5784  CA  GLU A 785      50.545  76.731  -8.488  1.00 82.53           C  
ANISOU 5784  CA  GLU A 785     8934   9305  13117    347   1649    836       C  
ATOM   5785  C   GLU A 785      49.120  76.264  -8.777  1.00 83.88           C  
ANISOU 5785  C   GLU A 785     9170   9541  13160    372   1604    866       C  
ATOM   5786  O   GLU A 785      48.810  75.822  -9.891  1.00 81.64           O  
ANISOU 5786  O   GLU A 785     8944   9287  12789    417   1619    955       O  
ATOM   5787  CB  GLU A 785      51.429  75.544  -8.091  1.00 84.82           C  
ANISOU 5787  CB  GLU A 785     9241   9647  13339    325   1603    787       C  
ATOM   5788  CG  GLU A 785      52.904  75.691  -8.476  1.00 90.31           C  
ANISOU 5788  CG  GLU A 785     9901  10292  14123    324   1661    807       C  
ATOM   5789  CD  GLU A 785      53.630  76.791  -7.709  1.00 92.52           C  
ANISOU 5789  CD  GLU A 785    10090  10489  14576    290   1695    743       C  
ATOM   5790  OE1 GLU A 785      53.212  77.118  -6.573  1.00 94.74           O  
ANISOU 5790  OE1 GLU A 785    10337  10771  14889    254   1651    652       O  
ATOM   5791  OE2 GLU A 785      54.624  77.330  -8.243  1.00 93.63           O  
ANISOU 5791  OE2 GLU A 785    10193  10562  14821    299   1767    782       O  
ATOM   5792  N   VAL A 786      48.254  76.382  -7.776  1.00 81.35           N  
ANISOU 5792  N   VAL A 786     8839   9240  12829    343   1551    789       N  
ATOM   5793  CA  VAL A 786      46.919  75.798  -7.850  1.00 80.19           C  
ANISOU 5793  CA  VAL A 786     8750   9161  12556    358   1497    798       C  
ATOM   5794  C   VAL A 786      45.791  76.830  -8.023  1.00 78.51           C  
ANISOU 5794  C   VAL A 786     8525   8912  12393    376   1519    825       C  
ATOM   5795  O   VAL A 786      44.844  76.577  -8.764  1.00 78.14           O  
ANISOU 5795  O   VAL A 786     8530   8900  12260    413   1510    887       O  
ATOM   5796  CB  VAL A 786      46.681  74.798  -6.683  1.00 82.27           C  
ANISOU 5796  CB  VAL A 786     9031   9498  12731    316   1408    699       C  
ATOM   5797  CG1 VAL A 786      47.190  75.360  -5.369  1.00 80.98           C  
ANISOU 5797  CG1 VAL A 786     8797   9301  12671    265   1396    594       C  
ATOM   5798  CG2 VAL A 786      45.218  74.377  -6.582  1.00 79.34           C  
ANISOU 5798  CG2 VAL A 786     8706   9186  12253    325   1356    695       C  
ATOM   5799  N   ALA A 787      45.911  77.996  -7.388  1.00 76.17           N  
ANISOU 5799  N   ALA A 787     8159   8545  12238    351   1549    780       N  
ATOM   5800  CA  ALA A 787      44.897  79.049  -7.505  1.00 74.34           C  
ANISOU 5800  CA  ALA A 787     7906   8270  12069    366   1573    802       C  
ATOM   5801  C   ALA A 787      44.461  79.421  -8.940  1.00 75.98           C  
ANISOU 5801  C   ALA A 787     8147   8456  12264    427   1627    930       C  
ATOM   5802  O   ALA A 787      43.298  79.759  -9.148  1.00 77.49           O  
ANISOU 5802  O   ALA A 787     8355   8653  12435    448   1618    955       O  
ATOM   5803  CB  ALA A 787      45.298  80.292  -6.719  1.00 73.84           C  
ANISOU 5803  CB  ALA A 787     7755   8123  12177    332   1609    740       C  
ATOM   5804  N   PRO A 788      45.374  79.374  -9.932  1.00 77.60           N  
ANISOU 5804  N   PRO A 788     8363   8639  12482    457   1684   1013       N  
ATOM   5805  CA  PRO A 788      44.864  79.610 -11.295  1.00 80.02           C  
ANISOU 5805  CA  PRO A 788     8712   8940  12753    519   1727   1135       C  
ATOM   5806  C   PRO A 788      43.757  78.639 -11.725  1.00 81.37           C  
ANISOU 5806  C   PRO A 788     8959   9201  12757    547   1667   1161       C  
ATOM   5807  O   PRO A 788      42.934  78.975 -12.576  1.00 83.43           O  
ANISOU 5807  O   PRO A 788     9248   9461  12991    594   1685   1239       O  
ATOM   5808  CB  PRO A 788      46.099  79.431 -12.194  1.00 77.76           C  
ANISOU 5808  CB  PRO A 788     8431   8633  12480    542   1787   1207       C  
ATOM   5809  CG  PRO A 788      47.274  79.306 -11.287  1.00 78.74           C  
ANISOU 5809  CG  PRO A 788     8507   8736  12675    491   1783   1122       C  
ATOM   5810  CD  PRO A 788      46.840  79.498  -9.864  1.00 78.16           C  
ANISOU 5810  CD  PRO A 788     8393   8664  12639    439   1727   1002       C  
ATOM   5811  N   MET A 789      43.731  77.455 -11.126  1.00 82.74           N  
ANISOU 5811  N   MET A 789     9165   9450  12823    521   1595   1094       N  
ATOM   5812  CA  MET A 789      42.774  76.417 -11.502  1.00 83.21           C  
ANISOU 5812  CA  MET A 789     9295   9596  12724    545   1536   1110       C  
ATOM   5813  C   MET A 789      41.399  76.554 -10.820  1.00 80.28           C  
ANISOU 5813  C   MET A 789     8926   9247  12328    531   1483   1057       C  
ATOM   5814  O   MET A 789      40.467  75.809 -11.139  1.00 75.42           O  
ANISOU 5814  O   MET A 789     8366   8698  11593    553   1436   1071       O  
ATOM   5815  CB  MET A 789      43.369  75.046 -11.192  1.00 87.76           C  
ANISOU 5815  CB  MET A 789     9905  10241  13199    523   1486   1066       C  
ATOM   5816  CG  MET A 789      43.085  73.995 -12.246  1.00 94.14           C  
ANISOU 5816  CG  MET A 789    10787  11119  13864    568   1467   1132       C  
ATOM   5817  SD  MET A 789      44.495  73.736 -13.332  1.00 95.16           S  
ANISOU 5817  SD  MET A 789    10927  11233  13997    597   1530   1211       S  
ATOM   5818  CE  MET A 789      43.779  72.645 -14.560  1.00 96.57           C  
ANISOU 5818  CE  MET A 789    11191  11499  14003    654   1502   1283       C  
ATOM   5819  N   LEU A 790      41.286  77.518  -9.904  1.00 77.91           N  
ANISOU 5819  N   LEU A 790     8565   8892  12146    496   1493    995       N  
ATOM   5820  CA  LEU A 790      40.104  77.721  -9.056  1.00 75.43           C  
ANISOU 5820  CA  LEU A 790     8241   8593  11827    473   1445    928       C  
ATOM   5821  C   LEU A 790      38.747  77.645  -9.771  1.00 76.69           C  
ANISOU 5821  C   LEU A 790     8446   8785  11908    517   1427    984       C  
ATOM   5822  O   LEU A 790      37.855  76.918  -9.326  1.00 76.59           O  
ANISOU 5822  O   LEU A 790     8465   8835  11801    506   1362    937       O  
ATOM   5823  CB  LEU A 790      40.239  79.049  -8.313  1.00 75.46           C  
ANISOU 5823  CB  LEU A 790     8166   8514  11992    444   1482    880       C  
ATOM   5824  CG  LEU A 790      39.558  79.219  -6.959  1.00 74.54           C  
ANISOU 5824  CG  LEU A 790     8017   8407  11896    395   1433    767       C  
ATOM   5825  CD1 LEU A 790      39.848  78.061  -6.018  1.00 71.05           C  
ANISOU 5825  CD1 LEU A 790     7595   8038  11364    353   1366    681       C  
ATOM   5826  CD2 LEU A 790      40.015  80.530  -6.345  1.00 73.50           C  
ANISOU 5826  CD2 LEU A 790     7801   8187  11937    368   1479    724       C  
ATOM   5827  N   GLN A 791      38.607  78.381 -10.875  1.00 78.94           N  
ANISOU 5827  N   GLN A 791     8734   9027  12233    567   1483   1084       N  
ATOM   5828  CA  GLN A 791      37.383  78.369 -11.691  1.00 79.38           C  
ANISOU 5828  CA  GLN A 791     8832   9111  12218    617   1469   1147       C  
ATOM   5829  C   GLN A 791      36.964  76.959 -12.097  1.00 76.03           C  
ANISOU 5829  C   GLN A 791     8481   8783  11625    635   1410   1155       C  
ATOM   5830  O   GLN A 791      35.787  76.678 -12.267  1.00 75.96           O  
ANISOU 5830  O   GLN A 791     8504   8815  11543    655   1369   1158       O  
ATOM   5831  CB  GLN A 791      37.550  79.204 -12.972  1.00 82.15           C  
ANISOU 5831  CB  GLN A 791     9184   9410  12621    675   1542   1268       C  
ATOM   5832  CG  GLN A 791      37.917  80.669 -12.772  1.00 88.42           C  
ANISOU 5832  CG  GLN A 791     9907  10100  13589    666   1610   1279       C  
ATOM   5833  CD  GLN A 791      39.421  80.940 -12.834  1.00 93.72           C  
ANISOU 5833  CD  GLN A 791    10543  10720  14347    651   1670   1293       C  
ATOM   5834  OE1 GLN A 791      40.246  80.082 -12.494  1.00 89.97           O  
ANISOU 5834  OE1 GLN A 791    10079  10282  13825    624   1648   1250       O  
ATOM   5835  NE2 GLN A 791      39.783  82.150 -13.265  1.00 95.77           N  
ANISOU 5835  NE2 GLN A 791    10758  10892  14740    670   1747   1353       N  
ATOM   5836  N   GLN A 792      37.932  76.071 -12.260  1.00 75.06           N  
ANISOU 5836  N   GLN A 792     8381   8693  11444    629   1406   1157       N  
ATOM   5837  CA  GLN A 792      37.651  74.761 -12.825  1.00 74.08           C  
ANISOU 5837  CA  GLN A 792     8325   8655  11168    653   1360   1176       C  
ATOM   5838  C   GLN A 792      37.205  73.737 -11.773  1.00 70.97           C  
ANISOU 5838  C   GLN A 792     7946   8324  10695    609   1281   1077       C  
ATOM   5839  O   GLN A 792      36.667  72.682 -12.122  1.00 72.50           O  
ANISOU 5839  O   GLN A 792     8193   8588  10765    627   1234   1083       O  
ATOM   5840  CB  GLN A 792      38.861  74.252 -13.626  1.00 77.76           C  
ANISOU 5840  CB  GLN A 792     8813   9130  11605    674   1395   1232       C  
ATOM   5841  CG  GLN A 792      39.414  75.251 -14.640  1.00 80.08           C  
ANISOU 5841  CG  GLN A 792     9090   9359  11980    716   1480   1332       C  
ATOM   5842  CD  GLN A 792      40.650  74.739 -15.364  1.00 83.82           C  
ANISOU 5842  CD  GLN A 792     9581   9841  12427    732   1517   1381       C  
ATOM   5843  OE1 GLN A 792      40.593  73.741 -16.079  1.00 86.54           O  
ANISOU 5843  OE1 GLN A 792     9980  10251  12649    762   1494   1413       O  
ATOM   5844  NE2 GLN A 792      41.771  75.426 -15.187  1.00 83.66           N  
ANISOU 5844  NE2 GLN A 792     9512   9752  12524    713   1576   1385       N  
ATOM   5845  N   PHE A 793      37.403  74.044 -10.493  1.00 65.61           N  
ANISOU 5845  N   PHE A 793     7221   7620  10086    553   1267    988       N  
ATOM   5846  CA  PHE A 793      37.103  73.051  -9.456  1.00 64.52           C  
ANISOU 5846  CA  PHE A 793     7098   7543   9875    509   1197    897       C  
ATOM   5847  C   PHE A 793      36.173  73.495  -8.330  1.00 62.30           C  
ANISOU 5847  C   PHE A 793     6787   7256   9630    472   1165    816       C  
ATOM   5848  O   PHE A 793      35.636  72.665  -7.607  1.00 61.38           O  
ANISOU 5848  O   PHE A 793     6690   7195   9438    445   1106    752       O  
ATOM   5849  CB  PHE A 793      38.396  72.385  -8.900  1.00 62.26           C  
ANISOU 5849  CB  PHE A 793     6803   7269   9585    473   1190    853       C  
ATOM   5850  CG  PHE A 793      39.269  73.283  -8.033  1.00 61.91           C  
ANISOU 5850  CG  PHE A 793     6690   7159   9673    432   1222    801       C  
ATOM   5851  CD1 PHE A 793      38.915  73.588  -6.717  1.00 61.56           C  
ANISOU 5851  CD1 PHE A 793     6609   7110   9672    383   1191    706       C  
ATOM   5852  CD2 PHE A 793      40.486  73.767  -8.512  1.00 60.97           C  
ANISOU 5852  CD2 PHE A 793     6544   6987   9633    441   1282    844       C  
ATOM   5853  CE1 PHE A 793      39.730  74.394  -5.922  1.00 61.44           C  
ANISOU 5853  CE1 PHE A 793     6529   7038   9777    346   1218    652       C  
ATOM   5854  CE2 PHE A 793      41.308  74.561  -7.717  1.00 60.03           C  
ANISOU 5854  CE2 PHE A 793     6361   6809   9640    403   1310    791       C  
ATOM   5855  CZ  PHE A 793      40.933  74.879  -6.423  1.00 59.71           C  
ANISOU 5855  CZ  PHE A 793     6281   6764   9641    356   1277    693       C  
ATOM   5856  N   ILE A 794      35.988  74.803  -8.202  1.00 63.33           N  
ANISOU 5856  N   ILE A 794     6866   7316   9879    472   1207    819       N  
ATOM   5857  CA  ILE A 794      35.303  75.386  -7.055  1.00 64.45           C  
ANISOU 5857  CA  ILE A 794     6968   7441  10080    431   1186    735       C  
ATOM   5858  C   ILE A 794      33.886  74.855  -6.820  1.00 64.85           C  
ANISOU 5858  C   ILE A 794     7052   7547  10042    433   1130    706       C  
ATOM   5859  O   ILE A 794      33.518  74.580  -5.672  1.00 63.45           O  
ANISOU 5859  O   ILE A 794     6862   7396   9850    388   1088    616       O  
ATOM   5860  CB  ILE A 794      35.339  76.937  -7.093  1.00 63.75           C  
ANISOU 5860  CB  ILE A 794     6818   7262  10143    436   1246    752       C  
ATOM   5861  CG1 ILE A 794      34.769  77.541  -5.800  1.00 62.55           C  
ANISOU 5861  CG1 ILE A 794     6616   7091  10059    389   1226    652       C  
ATOM   5862  CG2 ILE A 794      34.647  77.478  -8.337  1.00 63.37           C  
ANISOU 5862  CG2 ILE A 794     6790   7191  10098    496   1278    853       C  
ATOM   5863  CD1 ILE A 794      35.592  77.250  -4.560  1.00 61.13           C  
ANISOU 5863  CD1 ILE A 794     6406   6922   9899    331   1204    554       C  
ATOM   5864  N   ARG A 795      33.116  74.688  -7.898  1.00 65.98           N  
ANISOU 5864  N   ARG A 795     7236   7710  10124    485   1128    780       N  
ATOM   5865  CA  ARG A 795      31.768  74.112  -7.811  1.00 67.16           C  
ANISOU 5865  CA  ARG A 795     7419   7913  10185    492   1074    758       C  
ATOM   5866  C   ARG A 795      31.764  72.739  -7.122  1.00 64.36           C  
ANISOU 5866  C   ARG A 795     7098   7633   9722    459   1013    695       C  
ATOM   5867  O   ARG A 795      31.240  72.611  -6.007  1.00 63.46           O  
ANISOU 5867  O   ARG A 795     6969   7537   9606    416    978    611       O  
ATOM   5868  CB  ARG A 795      31.126  73.985  -9.191  1.00 73.85           C  
ANISOU 5868  CB  ARG A 795     8311   8779  10972    557   1079    852       C  
ATOM   5869  CG  ARG A 795      30.553  75.253  -9.779  1.00 80.05           C  
ANISOU 5869  CG  ARG A 795     9070   9503  11842    593   1120    908       C  
ATOM   5870  CD  ARG A 795      29.711  74.873 -10.980  1.00 89.26           C  
ANISOU 5870  CD  ARG A 795    10287  10708  12919    655   1105    983       C  
ATOM   5871  NE  ARG A 795      29.344  76.022 -11.803  1.00102.46           N  
ANISOU 5871  NE  ARG A 795    11942  12325  14663    702   1150   1060       N  
ATOM   5872  CZ  ARG A 795      28.222  76.110 -12.520  1.00107.67           C  
ANISOU 5872  CZ  ARG A 795    12626  13003  15282    749   1132   1104       C  
ATOM   5873  NH1 ARG A 795      27.332  75.119 -12.509  1.00105.96           N  
ANISOU 5873  NH1 ARG A 795    12449  12856  14955    754   1071   1073       N  
ATOM   5874  NH2 ARG A 795      27.980  77.200 -13.241  1.00107.73           N  
ANISOU 5874  NH2 ARG A 795    12615  12956  15362    792   1177   1178       N  
ATOM   5875  N   PRO A 796      32.356  71.710  -7.772  1.00 61.75           N  
ANISOU 5875  N   PRO A 796     6813   7347   9303    478   1002    734       N  
ATOM   5876  CA  PRO A 796      32.318  70.386  -7.143  1.00 60.37           C  
ANISOU 5876  CA  PRO A 796     6670   7240   9029    449    945    678       C  
ATOM   5877  C   PRO A 796      33.091  70.336  -5.828  1.00 59.90           C  
ANISOU 5877  C   PRO A 796     6575   7174   9009    389    935    595       C  
ATOM   5878  O   PRO A 796      32.708  69.602  -4.910  1.00 61.89           O  
ANISOU 5878  O   PRO A 796     6838   7472   9206    353    887    527       O  
ATOM   5879  CB  PRO A 796      32.942  69.462  -8.197  1.00 57.53           C  
ANISOU 5879  CB  PRO A 796     6357   6916   8586    485    946    743       C  
ATOM   5880  CG  PRO A 796      33.728  70.356  -9.088  1.00 58.10           C  
ANISOU 5880  CG  PRO A 796     6411   6931   8732    518   1011    818       C  
ATOM   5881  CD  PRO A 796      33.030  71.679  -9.085  1.00 59.22           C  
ANISOU 5881  CD  PRO A 796     6517   7017   8968    528   1041    830       C  
ATOM   5882  N   TRP A 797      34.145  71.137  -5.725  1.00 58.37           N  
ANISOU 5882  N   TRP A 797     6339   6924   8914    378    981    600       N  
ATOM   5883  CA  TRP A 797      34.893  71.239  -4.480  1.00 59.77           C  
ANISOU 5883  CA  TRP A 797     6477   7091   9142    324    974    519       C  
ATOM   5884  C   TRP A 797      33.946  71.572  -3.359  1.00 58.92           C  
ANISOU 5884  C   TRP A 797     6345   6990   9053    288    945    438       C  
ATOM   5885  O   TRP A 797      33.941  70.909  -2.318  1.00 59.01           O  
ANISOU 5885  O   TRP A 797     6359   7043   9019    247    903    365       O  
ATOM   5886  CB  TRP A 797      36.013  72.287  -4.604  1.00 59.03           C  
ANISOU 5886  CB  TRP A 797     6332   6924   9172    322   1034    537       C  
ATOM   5887  CG  TRP A 797      36.952  72.315  -3.423  1.00 57.49           C  
ANISOU 5887  CG  TRP A 797     6097   6721   9027    270   1025    455       C  
ATOM   5888  CD1 TRP A 797      38.172  71.649  -3.292  1.00 57.51           C  
ANISOU 5888  CD1 TRP A 797     6103   6739   9010    256   1020    447       C  
ATOM   5889  CD2 TRP A 797      36.782  73.049  -2.158  1.00 56.18           C  
ANISOU 5889  CD2 TRP A 797     5876   6532   8937    225   1018    364       C  
ATOM   5890  NE1 TRP A 797      38.745  71.914  -2.071  1.00 58.07           N  
ANISOU 5890  NE1 TRP A 797     6128   6799   9139    208   1008    361       N  
ATOM   5891  CE2 TRP A 797      37.962  72.745  -1.344  1.00 56.99           C  
ANISOU 5891  CE2 TRP A 797     5955   6640   9059    188   1007    307       C  
ATOM   5892  CE3 TRP A 797      35.810  73.898  -1.641  1.00 58.66           C  
ANISOU 5892  CE3 TRP A 797     6159   6822   9306    213   1020    324       C  
ATOM   5893  CZ2 TRP A 797      38.134  73.271  -0.076  1.00 57.12           C  
ANISOU 5893  CZ2 TRP A 797     5920   6643   9140    142    997    213       C  
ATOM   5894  CZ3 TRP A 797      35.995  74.428  -0.355  1.00 57.04           C  
ANISOU 5894  CZ3 TRP A 797     5901   6602   9169    165   1012    228       C  
ATOM   5895  CH2 TRP A 797      37.130  74.120   0.406  1.00 58.49           C  
ANISOU 5895  CH2 TRP A 797     6064   6796   9365    131   1000    173       C  
ATOM   5896  N   CYS A 798      33.132  72.603  -3.583  1.00 58.85           N  
ANISOU 5896  N   CYS A 798     6312   6938   9110    304    970    453       N  
ATOM   5897  CA  CYS A 798      32.149  73.070  -2.607  1.00 59.43           C  
ANISOU 5897  CA  CYS A 798     6358   7010   9213    273    950    379       C  
ATOM   5898  C   CYS A 798      31.017  72.068  -2.367  1.00 57.63           C  
ANISOU 5898  C   CYS A 798     6174   6851   8870    270    894    354       C  
ATOM   5899  O   CYS A 798      30.695  71.754  -1.216  1.00 55.23           O  
ANISOU 5899  O   CYS A 798     5862   6578   8544    227    860    272       O  
ATOM   5900  CB  CYS A 798      31.590  74.431  -3.025  1.00 58.43           C  
ANISOU 5900  CB  CYS A 798     6194   6816   9192    296    994    409       C  
ATOM   5901  SG  CYS A 798      32.767  75.796  -2.819  1.00 65.43           S  
ANISOU 5901  SG  CYS A 798     7007   7611  10241    281   1058    403       S  
ATOM   5902  N   THR A 799      30.438  71.563  -3.452  1.00 57.90           N  
ANISOU 5902  N   THR A 799     6256   6911   8834    315    886    423       N  
ATOM   5903  CA  THR A 799      29.373  70.563  -3.387  1.00 60.05           C  
ANISOU 5903  CA  THR A 799     6572   7247   8999    318    835    406       C  
ATOM   5904  C   THR A 799      29.799  69.393  -2.499  1.00 59.01           C  
ANISOU 5904  C   THR A 799     6460   7171   8791    278    792    348       C  
ATOM   5905  O   THR A 799      29.069  68.988  -1.601  1.00 56.95           O  
ANISOU 5905  O   THR A 799     6201   6945   8492    246    756    285       O  
ATOM   5906  CB  THR A 799      29.029  70.032  -4.797  1.00 63.04           C  
ANISOU 5906  CB  THR A 799     6999   7647   9305    376    832    493       C  
ATOM   5907  OG1 THR A 799      28.743  71.137  -5.664  1.00 64.75           O  
ANISOU 5907  OG1 THR A 799     7198   7811   9592    417    874    555       O  
ATOM   5908  CG2 THR A 799      27.823  69.083  -4.758  1.00 60.54           C  
ANISOU 5908  CG2 THR A 799     6722   7391   8890    380    780    472       C  
ATOM   5909  N   SER A 800      31.001  68.878  -2.742  1.00 58.95           N  
ANISOU 5909  N   SER A 800     6463   7170   8764    279    799    372       N  
ATOM   5910  CA  SER A 800      31.521  67.741  -1.994  1.00 55.80           C  
ANISOU 5910  CA  SER A 800     6084   6823   8295    245    760    327       C  
ATOM   5911  C   SER A 800      31.761  68.033  -0.500  1.00 56.12           C  
ANISOU 5911  C   SER A 800     6085   6861   8377    189    748    236       C  
ATOM   5912  O   SER A 800      31.331  67.274   0.366  1.00 54.67           O  
ANISOU 5912  O   SER A 800     5917   6727   8130    159    706    181       O  
ATOM   5913  CB  SER A 800      32.787  67.218  -2.669  1.00 56.68           C  
ANISOU 5913  CB  SER A 800     6213   6936   8387    262    773    377       C  
ATOM   5914  OG  SER A 800      33.417  66.238  -1.870  1.00 60.87           O  
ANISOU 5914  OG  SER A 800     6754   7507   8865    228    738    331       O  
ATOM   5915  N   LEU A 801      32.397  69.156  -0.197  1.00 56.56           N  
ANISOU 5915  N   LEU A 801     6089   6861   8541    176    785    218       N  
ATOM   5916  CA  LEU A 801      32.824  69.432   1.178  1.00 58.80           C  
ANISOU 5916  CA  LEU A 801     6331   7144   8865    124    775    130       C  
ATOM   5917  C   LEU A 801      31.778  70.054   2.094  1.00 60.80           C  
ANISOU 5917  C   LEU A 801     6556   7394   9150     97    766     62       C  
ATOM   5918  O   LEU A 801      31.904  69.986   3.328  1.00 60.39           O  
ANISOU 5918  O   LEU A 801     6484   7365   9098     54    745    -19       O  
ATOM   5919  CB  LEU A 801      34.124  70.262   1.186  1.00 58.26           C  
ANISOU 5919  CB  LEU A 801     6216   7019   8901    118    816    130       C  
ATOM   5920  CG  LEU A 801      35.428  69.499   1.459  1.00 57.59           C  
ANISOU 5920  CG  LEU A 801     6138   6957   8787    103    801    120       C  
ATOM   5921  CD1 LEU A 801      35.423  68.053   0.953  1.00 54.81           C  
ANISOU 5921  CD1 LEU A 801     5849   6664   8311    119    766    161       C  
ATOM   5922  CD2 LEU A 801      36.619  70.265   0.903  1.00 54.59           C  
ANISOU 5922  CD2 LEU A 801     5723   6515   8505    116    852    156       C  
ATOM   5923  N   ARG A 802      30.751  70.668   1.513  1.00 64.40           N  
ANISOU 5923  N   ARG A 802     7010   7825   9633    123    783     91       N  
ATOM   5924  CA  ARG A 802      29.678  71.234   2.337  1.00 63.48           C  
ANISOU 5924  CA  ARG A 802     6868   7707   9546     99    775     26       C  
ATOM   5925  C   ARG A 802      29.032  70.124   3.145  1.00 61.79           C  
ANISOU 5925  C   ARG A 802     6687   7565   9226     72    724    -24       C  
ATOM   5926  O   ARG A 802      28.583  70.343   4.272  1.00 61.80           O  
ANISOU 5926  O   ARG A 802     6664   7580   9238     34    711   -102       O  
ATOM   5927  CB  ARG A 802      28.658  72.044   1.513  1.00 63.29           C  
ANISOU 5927  CB  ARG A 802     6837   7643   9568    135    799     71       C  
ATOM   5928  CG  ARG A 802      28.032  71.330   0.319  1.00 64.42           C  
ANISOU 5928  CG  ARG A 802     7036   7812   9630    183    787    149       C  
ATOM   5929  CD  ARG A 802      26.638  70.826   0.632  1.00 64.50           C  
ANISOU 5929  CD  ARG A 802     7068   7864   9574    177    750    118       C  
ATOM   5930  NE  ARG A 802      25.693  71.928   0.794  1.00 65.33           N  
ANISOU 5930  NE  ARG A 802     7135   7928   9758    178    768     95       N  
ATOM   5931  CZ  ARG A 802      24.499  71.827   1.379  1.00 64.07           C  
ANISOU 5931  CZ  ARG A 802     6974   7792   9576    161    744     45       C  
ATOM   5932  NH1 ARG A 802      24.077  70.671   1.875  1.00 60.65           N  
ANISOU 5932  NH1 ARG A 802     6578   7423   9043    142    702     12       N  
ATOM   5933  NH2 ARG A 802      23.720  72.895   1.468  1.00 60.71           N  
ANISOU 5933  NH2 ARG A 802     6511   7323   9232    164    764     27       N  
ATOM   5934  N   ASN A 803      29.063  68.919   2.589  1.00 60.80           N  
ANISOU 5934  N   ASN A 803     6616   7485   9000     91    697     20       N  
ATOM   5935  CA  ASN A 803      28.460  67.763   3.242  1.00 63.23           C  
ANISOU 5935  CA  ASN A 803     6959   7860   9206     69    651    -17       C  
ATOM   5936  C   ASN A 803      29.320  67.009   4.273  1.00 64.58           C  
ANISOU 5936  C   ASN A 803     7133   8071   9332     30    624    -66       C  
ATOM   5937  O   ASN A 803      28.847  66.020   4.838  1.00 66.41           O  
ANISOU 5937  O   ASN A 803     7396   8358   9479     12    587    -93       O  
ATOM   5938  CB  ASN A 803      27.869  66.795   2.195  1.00 62.95           C  
ANISOU 5938  CB  ASN A 803     6979   7855   9083    107    632     48       C  
ATOM   5939  CG  ASN A 803      26.616  67.350   1.534  1.00 63.70           C  
ANISOU 5939  CG  ASN A 803     7074   7930   9199    137    642     73       C  
ATOM   5940  OD1 ASN A 803      26.507  67.398   0.304  1.00 62.87           O  
ANISOU 5940  OD1 ASN A 803     6988   7810   9090    184    654    145       O  
ATOM   5941  ND2 ASN A 803      25.681  67.816   2.350  1.00 63.78           N  
ANISOU 5941  ND2 ASN A 803     7060   7939   9235    112    637     12       N  
ATOM   5942  N   ILE A 804      30.550  67.460   4.545  1.00 60.53           N  
ANISOU 5942  N   ILE A 804     6589   7532   8878     17    641    -80       N  
ATOM   5943  CA  ILE A 804      31.376  66.737   5.525  1.00 59.02           C  
ANISOU 5943  CA  ILE A 804     6401   7382   8644    -18    612   -127       C  
ATOM   5944  C   ILE A 804      31.425  67.361   6.914  1.00 61.50           C  
ANISOU 5944  C   ILE A 804     6669   7698   9001    -62    608   -219       C  
ATOM   5945  O   ILE A 804      31.225  68.565   7.078  1.00 61.84           O  
ANISOU 5945  O   ILE A 804     6666   7695   9137    -67    637   -247       O  
ATOM   5946  CB  ILE A 804      32.803  66.386   5.025  1.00 59.70           C  
ANISOU 5946  CB  ILE A 804     6492   7458   8735     -6    619    -86       C  
ATOM   5947  CG1 ILE A 804      33.682  67.636   4.908  1.00 60.46           C  
ANISOU 5947  CG1 ILE A 804     6533   7487   8950     -5    662    -90       C  
ATOM   5948  CG2 ILE A 804      32.744  65.601   3.720  1.00 56.96           C  
ANISOU 5948  CG2 ILE A 804     6194   7120   8328     37    618     -1       C  
ATOM   5949  CD1 ILE A 804      35.145  67.333   4.669  1.00 63.86           C  
ANISOU 5949  CD1 ILE A 804     6961   7910   9394     -1    668    -68       C  
ATOM   5950  N   ARG A 805      31.681  66.510   7.902  1.00 65.03           N  
ANISOU 5950  N   ARG A 805     7131   8201   9378    -93    570   -265       N  
ATOM   5951  CA  ARG A 805      31.761  66.882   9.305  1.00 70.60           C  
ANISOU 5951  CA  ARG A 805     7800   8925  10101   -135    558   -355       C  
ATOM   5952  C   ARG A 805      32.877  67.908   9.506  1.00 69.85           C  
ANISOU 5952  C   ARG A 805     7649   8781  10111   -143    585   -384       C  
ATOM   5953  O   ARG A 805      33.858  67.917   8.763  1.00 70.14           O  
ANISOU 5953  O   ARG A 805     7684   8788  10179   -123    600   -336       O  
ATOM   5954  CB  ARG A 805      32.044  65.618  10.129  1.00 80.06           C  
ANISOU 5954  CB  ARG A 805     9032  10193  11195   -158    513   -379       C  
ATOM   5955  CG  ARG A 805      31.752  65.701  11.624  1.00 91.45           C  
ANISOU 5955  CG  ARG A 805    10455  11676  12617   -200    492   -469       C  
ATOM   5956  CD  ARG A 805      31.713  64.307  12.254  1.00101.49           C  
ANISOU 5956  CD  ARG A 805    11772  13020  13771   -215    448   -473       C  
ATOM   5957  NE  ARG A 805      30.479  63.584  11.912  1.00111.64           N  
ANISOU 5957  NE  ARG A 805    13101  14330  14986   -205    439   -442       N  
ATOM   5958  CZ  ARG A 805      30.314  62.262  11.986  1.00113.60           C  
ANISOU 5958  CZ  ARG A 805    13397  14628  15136   -205    408   -417       C  
ATOM   5959  NH1 ARG A 805      31.305  61.471  12.386  1.00115.24           N  
ANISOU 5959  NH1 ARG A 805    13619  14868  15298   -214    381   -415       N  
ATOM   5960  NH2 ARG A 805      29.147  61.724  11.650  1.00113.30           N  
ANISOU 5960  NH2 ARG A 805    13392  14607  15049   -196    403   -393       N  
ATOM   5961  N   ASP A 806      32.719  68.769  10.504  1.00 67.72           N  
ANISOU 5961  N   ASP A 806     7330   8503   9896   -173    590   -465       N  
ATOM   5962  CA  ASP A 806      33.752  69.730  10.858  1.00 68.51           C  
ANISOU 5962  CA  ASP A 806     7371   8561  10100   -186    611   -507       C  
ATOM   5963  C   ASP A 806      34.882  69.015  11.592  1.00 70.31           C  
ANISOU 5963  C   ASP A 806     7602   8831  10283   -206    578   -539       C  
ATOM   5964  O   ASP A 806      34.732  68.611  12.748  1.00 75.50           O  
ANISOU 5964  O   ASP A 806     8261   9543  10882   -236    544   -605       O  
ATOM   5965  CB  ASP A 806      33.194  70.844  11.753  1.00 65.97           C  
ANISOU 5965  CB  ASP A 806     6995   8222   9850   -212    625   -592       C  
ATOM   5966  CG  ASP A 806      32.197  71.753  11.035  1.00 65.28           C  
ANISOU 5966  CG  ASP A 806     6892   8080   9832   -192    662   -564       C  
ATOM   5967  OD1 ASP A 806      31.998  71.620   9.799  1.00 62.89           O  
ANISOU 5967  OD1 ASP A 806     6619   7751   9528   -155    680   -476       O  
ATOM   5968  OD2 ASP A 806      31.618  72.614  11.734  1.00 61.95           O  
ANISOU 5968  OD2 ASP A 806     6427   7645   9466   -213    673   -632       O  
ATOM   5969  N   ASN A 807      36.007  68.850  10.914  1.00 66.47           N  
ANISOU 5969  N   ASN A 807     7116   8318   9821   -188    588   -492       N  
ATOM   5970  CA  ASN A 807      37.180  68.235  11.526  1.00 66.81           C  
ANISOU 5970  CA  ASN A 807     7157   8393   9834   -204    557   -520       C  
ATOM   5971  C   ASN A 807      38.461  68.895  11.018  1.00 66.24           C  
ANISOU 5971  C   ASN A 807     7043   8260   9864   -193    588   -506       C  
ATOM   5972  O   ASN A 807      38.405  69.900  10.295  1.00 64.75           O  
ANISOU 5972  O   ASN A 807     6824   8005   9773   -176    635   -479       O  
ATOM   5973  CB  ASN A 807      37.184  66.728  11.259  1.00 62.49           C  
ANISOU 5973  CB  ASN A 807     6677   7902   9164   -193    521   -468       C  
ATOM   5974  CG  ASN A 807      37.084  66.401   9.785  1.00 64.42           C  
ANISOU 5974  CG  ASN A 807     6958   8119   9400   -154    544   -370       C  
ATOM   5975  OD1 ASN A 807      37.490  67.192   8.923  1.00 66.18           O  
ANISOU 5975  OD1 ASN A 807     7157   8280   9710   -132    586   -332       O  
ATOM   5976  ND2 ASN A 807      36.552  65.227   9.479  1.00 66.44           N  
ANISOU 5976  ND2 ASN A 807     7272   8420   9552   -143    517   -327       N  
ATOM   5977  N   GLU A 808      39.603  68.314  11.378  1.00 67.69           N  
ANISOU 5977  N   GLU A 808     7225   8466  10026   -202    563   -520       N  
ATOM   5978  CA  GLU A 808      40.908  68.851  11.004  1.00 67.03           C  
ANISOU 5978  CA  GLU A 808     7100   8329  10038   -195    589   -514       C  
ATOM   5979  C   GLU A 808      41.097  68.944   9.485  1.00 65.98           C  
ANISOU 5979  C   GLU A 808     6986   8144   9941   -156    632   -414       C  
ATOM   5980  O   GLU A 808      41.584  69.962   8.966  1.00 64.01           O  
ANISOU 5980  O   GLU A 808     6692   7825   9806   -146    680   -402       O  
ATOM   5981  CB  GLU A 808      42.015  68.018  11.658  1.00 70.31           C  
ANISOU 5981  CB  GLU A 808     7519   8787  10407   -209    547   -543       C  
ATOM   5982  CG  GLU A 808      43.443  68.474  11.367  1.00 80.36           C  
ANISOU 5982  CG  GLU A 808     8747  10009  11775   -204    568   -544       C  
ATOM   5983  CD  GLU A 808      43.743  69.898  11.818  1.00 82.59           C  
ANISOU 5983  CD  GLU A 808     8951  10236  12191   -220    600   -613       C  
ATOM   5984  OE1 GLU A 808      43.246  70.321  12.887  1.00 87.70           O  
ANISOU 5984  OE1 GLU A 808     9572  10909  12840   -246    581   -695       O  
ATOM   5985  OE2 GLU A 808      44.490  70.595  11.100  1.00 85.63           O  
ANISOU 5985  OE2 GLU A 808     9300  10553  12682   -206    644   -586       O  
ATOM   5986  N   GLU A 809      40.688  67.895   8.777  1.00 64.13           N  
ANISOU 5986  N   GLU A 809     6815   7942   9610   -134    618   -345       N  
ATOM   5987  CA  GLU A 809      40.872  67.832   7.329  1.00 65.08           C  
ANISOU 5987  CA  GLU A 809     6959   8024   9745    -95    654   -250       C  
ATOM   5988  C   GLU A 809      40.123  68.953   6.625  1.00 64.39           C  
ANISOU 5988  C   GLU A 809     6852   7879   9736    -76    704   -219       C  
ATOM   5989  O   GLU A 809      40.680  69.637   5.770  1.00 66.28           O  
ANISOU 5989  O   GLU A 809     7068   8057  10059    -54    751   -173       O  
ATOM   5990  CB  GLU A 809      40.430  66.479   6.771  1.00 67.52           C  
ANISOU 5990  CB  GLU A 809     7339   8385   9930    -76    625   -190       C  
ATOM   5991  CG  GLU A 809      41.230  65.287   7.274  1.00 71.78           C  
ANISOU 5991  CG  GLU A 809     7902   8976  10394    -89    579   -204       C  
ATOM   5992  CD  GLU A 809      40.743  64.755   8.616  1.00 74.33           C  
ANISOU 5992  CD  GLU A 809     8233   9362  10645   -123    529   -274       C  
ATOM   5993  OE1 GLU A 809      39.587  65.021   8.989  1.00 76.40           O  
ANISOU 5993  OE1 GLU A 809     8500   9639  10888   -132    525   -298       O  
ATOM   5994  OE2 GLU A 809      41.519  64.060   9.304  1.00 75.24           O  
ANISOU 5994  OE2 GLU A 809     8351   9514  10722   -140    492   -304       O  
ATOM   5995  N   LYS A 810      38.861  69.138   7.000  1.00 64.42           N  
ANISOU 5995  N   LYS A 810     6863   7901   9711    -84    693   -244       N  
ATOM   5996  CA  LYS A 810      38.017  70.182   6.417  1.00 62.84           C  
ANISOU 5996  CA  LYS A 810     6645   7650   9581    -66    735   -219       C  
ATOM   5997  C   LYS A 810      38.607  71.560   6.705  1.00 58.55           C  
ANISOU 5997  C   LYS A 810     6027   7039   9180    -78    775   -261       C  
ATOM   5998  O   LYS A 810      38.695  72.418   5.822  1.00 54.56           O  
ANISOU 5998  O   LYS A 810     5500   6468   8763    -53    826   -211       O  
ATOM   5999  CB  LYS A 810      36.577  70.071   6.951  1.00 63.68           C  
ANISOU 5999  CB  LYS A 810     6769   7795   9632    -78    711   -252       C  
ATOM   6000  CG  LYS A 810      35.529  70.879   6.184  1.00 63.13           C  
ANISOU 6000  CG  LYS A 810     6696   7683   9609    -52    746   -212       C  
ATOM   6001  CD  LYS A 810      34.143  70.608   6.750  1.00 65.21           C  
ANISOU 6001  CD  LYS A 810     6980   7989   9808    -66    717   -248       C  
ATOM   6002  CE  LYS A 810      33.063  71.509   6.161  1.00 64.71           C  
ANISOU 6002  CE  LYS A 810     6904   7883   9801    -44    749   -222       C  
ATOM   6003  NZ  LYS A 810      31.828  71.413   6.992  1.00 60.69           N  
ANISOU 6003  NZ  LYS A 810     6399   7411   9249    -67    723   -281       N  
ATOM   6004  N   ASP A 811      39.016  71.751   7.951  1.00 58.62           N  
ANISOU 6004  N   ASP A 811     5997   7065   9211   -116    753   -354       N  
ATOM   6005  CA  ASP A 811      39.697  72.963   8.357  1.00 60.29           C  
ANISOU 6005  CA  ASP A 811     6133   7217   9557   -131    784   -408       C  
ATOM   6006  C   ASP A 811      40.866  73.235   7.409  1.00 61.03           C  
ANISOU 6006  C   ASP A 811     6210   7252   9725   -108    826   -348       C  
ATOM   6007  O   ASP A 811      40.927  74.278   6.747  1.00 60.68           O  
ANISOU 6007  O   ASP A 811     6131   7135   9791    -91    880   -316       O  
ATOM   6008  CB  ASP A 811      40.189  72.813   9.793  1.00 61.70           C  
ANISOU 6008  CB  ASP A 811     6282   7438   9723   -172    743   -513       C  
ATOM   6009  CG  ASP A 811      41.152  73.910  10.192  1.00 65.49           C  
ANISOU 6009  CG  ASP A 811     6684   7860  10341   -187    771   -572       C  
ATOM   6010  OD1 ASP A 811      40.679  74.979  10.632  1.00 65.45           O  
ANISOU 6010  OD1 ASP A 811     6628   7820  10420   -201    792   -627       O  
ATOM   6011  OD2 ASP A 811      42.384  73.698  10.062  1.00 70.36           O  
ANISOU 6011  OD2 ASP A 811     7287   8464  10983   -186    772   -565       O  
ATOM   6012  N   SER A 812      41.773  72.269   7.343  1.00 60.22           N  
ANISOU 6012  N   SER A 812     6135   7182   9563   -107    801   -331       N  
ATOM   6013  CA  SER A 812      42.938  72.341   6.486  1.00 59.96           C  
ANISOU 6013  CA  SER A 812     6092   7104   9587    -86    836   -275       C  
ATOM   6014  C   SER A 812      42.579  72.740   5.047  1.00 60.11           C  
ANISOU 6014  C   SER A 812     6129   7073   9637    -44    890   -173       C  
ATOM   6015  O   SER A 812      43.204  73.638   4.477  1.00 60.80           O  
ANISOU 6015  O   SER A 812     6175   7087   9838    -31    944   -145       O  
ATOM   6016  CB  SER A 812      43.664  70.998   6.536  1.00 59.04           C  
ANISOU 6016  CB  SER A 812     6018   7044   9371    -87    794   -262       C  
ATOM   6017  OG  SER A 812      44.568  70.853   5.465  1.00 61.63           O  
ANISOU 6017  OG  SER A 812     6354   7336   9727    -60    828   -188       O  
ATOM   6018  N   ALA A 813      41.564  72.089   4.477  1.00 58.16           N  
ANISOU 6018  N   ALA A 813     5943   6863   9292    -22    875   -118       N  
ATOM   6019  CA  ALA A 813      41.172  72.311   3.070  1.00 59.14           C  
ANISOU 6019  CA  ALA A 813     6094   6953   9424     22    918    -16       C  
ATOM   6020  C   ALA A 813      40.560  73.685   2.821  1.00 57.83           C  
ANISOU 6020  C   ALA A 813     5886   6720   9366     32    966     -9       C  
ATOM   6021  O   ALA A 813      40.709  74.251   1.738  1.00 58.08           O  
ANISOU 6021  O   ALA A 813     5914   6698   9457     66   1018     68       O  
ATOM   6022  CB  ALA A 813      40.203  71.224   2.606  1.00 57.88           C  
ANISOU 6022  CB  ALA A 813     6008   6856   9128     42    883     30       C  
ATOM   6023  N   PHE A 814      39.856  74.206   3.816  1.00 56.67           N  
ANISOU 6023  N   PHE A 814     5708   6578   9246      3    949    -88       N  
ATOM   6024  CA  PHE A 814      39.239  75.521   3.702  1.00 60.15           C  
ANISOU 6024  CA  PHE A 814     6104   6956   9796      8    991    -91       C  
ATOM   6025  C   PHE A 814      40.263  76.641   3.844  1.00 61.36           C  
ANISOU 6025  C   PHE A 814     6182   7032  10100     -2   1039   -118       C  
ATOM   6026  O   PHE A 814      40.132  77.680   3.199  1.00 62.26           O  
ANISOU 6026  O   PHE A 814     6264   7074  10317     18   1093    -76       O  
ATOM   6027  CB  PHE A 814      38.117  75.684   4.727  1.00 58.64           C  
ANISOU 6027  CB  PHE A 814     5902   6796   9581    -20    958   -170       C  
ATOM   6028  CG  PHE A 814      36.757  75.250   4.226  1.00 59.58           C  
ANISOU 6028  CG  PHE A 814     6076   6949   9613      3    942   -124       C  
ATOM   6029  CD1 PHE A 814      36.397  73.910   4.211  1.00 57.57           C  
ANISOU 6029  CD1 PHE A 814     5887   6771   9217      6    894   -109       C  
ATOM   6030  CD2 PHE A 814      35.822  76.197   3.798  1.00 60.43           C  
ANISOU 6030  CD2 PHE A 814     6165   7010   9786     21    974   -101       C  
ATOM   6031  CE1 PHE A 814      35.145  73.515   3.770  1.00 58.60           C  
ANISOU 6031  CE1 PHE A 814     6062   6931   9272     26    878    -73       C  
ATOM   6032  CE2 PHE A 814      34.565  75.812   3.357  1.00 57.99           C  
ANISOU 6032  CE2 PHE A 814     5902   6732   9399     42    956    -64       C  
ATOM   6033  CZ  PHE A 814      34.227  74.467   3.341  1.00 58.98           C  
ANISOU 6033  CZ  PHE A 814     6092   6934   9384     44    908    -51       C  
ATOM   6034  N   ARG A 815      41.273  76.436   4.692  1.00 62.48           N  
ANISOU 6034  N   ARG A 815     6295   7187  10259    -34   1018   -188       N  
ATOM   6035  CA  ARG A 815      42.415  77.365   4.762  1.00 63.78           C  
ANISOU 6035  CA  ARG A 815     6389   7280  10566    -42   1062   -211       C  
ATOM   6036  C   ARG A 815      43.018  77.511   3.376  1.00 62.40           C  
ANISOU 6036  C   ARG A 815     6226   7052  10432     -2   1118   -103       C  
ATOM   6037  O   ARG A 815      43.273  78.620   2.919  1.00 65.66           O  
ANISOU 6037  O   ARG A 815     6590   7384  10974      9   1177    -77       O  
ATOM   6038  CB  ARG A 815      43.474  76.902   5.759  1.00 62.06           C  
ANISOU 6038  CB  ARG A 815     6147   7094  10339    -76   1024   -293       C  
ATOM   6039  CG  ARG A 815      42.934  76.717   7.162  1.00 64.24           C  
ANISOU 6039  CG  ARG A 815     6412   7428  10566   -115    968   -401       C  
ATOM   6040  CD  ARG A 815      43.978  76.964   8.227  1.00 67.49           C  
ANISOU 6040  CD  ARG A 815     6764   7838  11039   -149    951   -500       C  
ATOM   6041  NE  ARG A 815      43.355  77.662   9.349  1.00 71.34           N  
ANISOU 6041  NE  ARG A 815     7207   8332  11566   -180    935   -602       N  
ATOM   6042  CZ  ARG A 815      43.064  77.097  10.516  1.00 72.34           C  
ANISOU 6042  CZ  ARG A 815     7344   8534  11606   -209    877   -683       C  
ATOM   6043  NH1 ARG A 815      43.384  75.833  10.732  1.00 73.35           N  
ANISOU 6043  NH1 ARG A 815     7525   8735  11611   -211    827   -674       N  
ATOM   6044  NH2 ARG A 815      42.473  77.800  11.477  1.00 71.05           N  
ANISOU 6044  NH2 ARG A 815     7138   8375  11484   -235    869   -774       N  
ATOM   6045  N   GLY A 816      43.189  76.384   2.696  1.00 61.56           N  
ANISOU 6045  N   GLY A 816     6186   6993  10213     20   1099    -36       N  
ATOM   6046  CA  GLY A 816      43.675  76.364   1.323  1.00 62.69           C  
ANISOU 6046  CA  GLY A 816     6351   7100  10370     61   1148     72       C  
ATOM   6047  C   GLY A 816      42.827  77.137   0.335  1.00 65.47           C  
ANISOU 6047  C   GLY A 816     6709   7405  10761     98   1197    152       C  
ATOM   6048  O   GLY A 816      43.358  77.880  -0.503  1.00 68.78           O  
ANISOU 6048  O   GLY A 816     7103   7754  11275    123   1261    215       O  
ATOM   6049  N   ILE A 817      41.509  76.974   0.430  1.00 64.37           N  
ANISOU 6049  N   ILE A 817     6603   7303  10552    103   1167    150       N  
ATOM   6050  CA  ILE A 817      40.612  77.622  -0.515  1.00 63.46           C  
ANISOU 6050  CA  ILE A 817     6498   7150  10462    142   1205    227       C  
ATOM   6051  C   ILE A 817      40.577  79.122  -0.278  1.00 64.76           C  
ANISOU 6051  C   ILE A 817     6589   7231  10788    133   1255    202       C  
ATOM   6052  O   ILE A 817      40.362  79.890  -1.213  1.00 65.21           O  
ANISOU 6052  O   ILE A 817     6638   7230  10911    168   1309    280       O  
ATOM   6053  CB  ILE A 817      39.187  77.022  -0.499  1.00 63.96           C  
ANISOU 6053  CB  ILE A 817     6615   7276  10409    151   1159    231       C  
ATOM   6054  CG1 ILE A 817      38.529  77.180  -1.870  1.00 64.32           C  
ANISOU 6054  CG1 ILE A 817     6700   7306  10434    205   1191    342       C  
ATOM   6055  CG2 ILE A 817      38.326  77.654   0.580  1.00 62.70           C  
ANISOU 6055  CG2 ILE A 817     6417   7113  10292    118   1139    142       C  
ATOM   6056  CD1 ILE A 817      38.950  76.125  -2.870  1.00 64.99           C  
ANISOU 6056  CD1 ILE A 817     6847   7432  10416    238   1186    421       C  
ATOM   6057  N   CYS A 818      40.808  79.534   0.967  1.00 64.35           N  
ANISOU 6057  N   CYS A 818     6480   7170  10798     88   1238     93       N  
ATOM   6058  CA  CYS A 818      40.870  80.950   1.290  1.00 65.78           C  
ANISOU 6058  CA  CYS A 818     6584   7270  11142     76   1284     56       C  
ATOM   6059  C   CYS A 818      42.133  81.584   0.712  1.00 66.81           C  
ANISOU 6059  C   CYS A 818     6670   7323  11393     87   1347     97       C  
ATOM   6060  O   CYS A 818      42.081  82.643   0.078  1.00 67.44           O  
ANISOU 6060  O   CYS A 818     6714   7322  11587    109   1410    148       O  
ATOM   6061  CB  CYS A 818      40.783  81.158   2.799  1.00 67.02           C  
ANISOU 6061  CB  CYS A 818     6692   7446  11325     25   1244    -78       C  
ATOM   6062  SG  CYS A 818      39.131  80.804   3.456  1.00 67.26           S  
ANISOU 6062  SG  CYS A 818     6759   7544  11254     12   1188   -125       S  
ATOM   6063  N   THR A 819      43.263  80.915   0.907  1.00 66.79           N  
ANISOU 6063  N   THR A 819     6670   7343  11363     73   1333     77       N  
ATOM   6064  CA  THR A 819      44.527  81.406   0.399  1.00 66.24           C  
ANISOU 6064  CA  THR A 819     6561   7206  11403     81   1391    111       C  
ATOM   6065  C   THR A 819      44.416  81.550  -1.111  1.00 66.64           C  
ANISOU 6065  C   THR A 819     6647   7221  11452    134   1447    247       C  
ATOM   6066  O   THR A 819      44.808  82.569  -1.676  1.00 70.24           O  
ANISOU 6066  O   THR A 819     7058   7592  12038    150   1517    293       O  
ATOM   6067  CB  THR A 819      45.688  80.473   0.772  1.00 66.51           C  
ANISOU 6067  CB  THR A 819     6604   7281  11387     62   1359     76       C  
ATOM   6068  OG1 THR A 819      45.573  80.094   2.144  1.00 64.38           O  
ANISOU 6068  OG1 THR A 819     6320   7066  11075     19   1293    -41       O  
ATOM   6069  CG2 THR A 819      47.018  81.184   0.588  1.00 70.32           C  
ANISOU 6069  CG2 THR A 819     7021   7684  12013     58   1417     76       C  
ATOM   6070  N   MET A 820      43.852  80.542  -1.760  1.00 66.34           N  
ANISOU 6070  N   MET A 820     6690   7250  11267    162   1417    311       N  
ATOM   6071  CA  MET A 820      43.669  80.593  -3.207  1.00 68.82           C  
ANISOU 6071  CA  MET A 820     7044   7544  11560    215   1465    440       C  
ATOM   6072  C   MET A 820      42.754  81.738  -3.674  1.00 69.90           C  
ANISOU 6072  C   MET A 820     7159   7620  11779    240   1508    486       C  
ATOM   6073  O   MET A 820      43.034  82.397  -4.683  1.00 74.48           O  
ANISOU 6073  O   MET A 820     7730   8139  12431    276   1576    577       O  
ATOM   6074  CB  MET A 820      43.187  79.249  -3.739  1.00 63.33           C  
ANISOU 6074  CB  MET A 820     6437   6938  10688    239   1417    487       C  
ATOM   6075  CG  MET A 820      44.238  78.172  -3.617  1.00 63.98           C  
ANISOU 6075  CG  MET A 820     6543   7065  10702    226   1391    471       C  
ATOM   6076  SD  MET A 820      43.758  76.650  -4.439  1.00 67.87           S  
ANISOU 6076  SD  MET A 820     7135   7651  11001    259   1346    538       S  
ATOM   6077  CE  MET A 820      42.677  75.886  -3.228  1.00 64.62           C  
ANISOU 6077  CE  MET A 820     6748   7321  10484    224   1257    443       C  
ATOM   6078  N   ILE A 821      41.673  81.983  -2.944  1.00 70.01           N  
ANISOU 6078  N   ILE A 821     7164   7651  11784    222   1472    425       N  
ATOM   6079  CA  ILE A 821      40.782  83.099  -3.281  1.00 70.88           C  
ANISOU 6079  CA  ILE A 821     7248   7703  11981    243   1510    459       C  
ATOM   6080  C   ILE A 821      41.527  84.442  -3.165  1.00 72.16           C  
ANISOU 6080  C   ILE A 821     7323   7759  12334    233   1578    447       C  
ATOM   6081  O   ILE A 821      41.380  85.320  -4.022  1.00 70.82           O  
ANISOU 6081  O   ILE A 821     7137   7521  12250    267   1640    530       O  
ATOM   6082  CB  ILE A 821      39.490  83.078  -2.437  1.00 67.34           C  
ANISOU 6082  CB  ILE A 821     6803   7294  11489    222   1455    386       C  
ATOM   6083  CG1 ILE A 821      38.605  81.906  -2.870  1.00 68.31           C  
ANISOU 6083  CG1 ILE A 821     7011   7506  11438    245   1402    426       C  
ATOM   6084  CG2 ILE A 821      38.715  84.378  -2.597  1.00 69.71           C  
ANISOU 6084  CG2 ILE A 821     7057   7521  11908    235   1497    402       C  
ATOM   6085  CD1 ILE A 821      37.526  81.519  -1.875  1.00 66.00           C  
ANISOU 6085  CD1 ILE A 821     6731   7273  11075    215   1338    339       C  
ATOM   6086  N   SER A 822      42.342  84.580  -2.118  1.00 71.94           N  
ANISOU 6086  N   SER A 822     7240   7719  12374    186   1567    345       N  
ATOM   6087  CA  SER A 822      43.162  85.774  -1.931  1.00 75.04           C  
ANISOU 6087  CA  SER A 822     7546   8014  12952    172   1629    320       C  
ATOM   6088  C   SER A 822      44.111  85.984  -3.121  1.00 76.17           C  
ANISOU 6088  C   SER A 822     7691   8101  13148    208   1701    430       C  
ATOM   6089  O   SER A 822      44.388  87.115  -3.502  1.00 77.75           O  
ANISOU 6089  O   SER A 822     7835   8208  13497    220   1771    466       O  
ATOM   6090  CB  SER A 822      43.953  85.693  -0.624  1.00 74.50           C  
ANISOU 6090  CB  SER A 822     7425   7957  12926    118   1596    189       C  
ATOM   6091  OG  SER A 822      45.131  84.927  -0.801  1.00 78.15           O  
ANISOU 6091  OG  SER A 822     7905   8442  13348    115   1593    201       O  
ATOM   6092  N   VAL A 823      44.582  84.889  -3.712  1.00 74.39           N  
ANISOU 6092  N   VAL A 823     7529   7933  12802    226   1685    484       N  
ATOM   6093  CA  VAL A 823      45.495  84.958  -4.854  1.00 74.59           C  
ANISOU 6093  CA  VAL A 823     7564   7917  12862    261   1751    587       C  
ATOM   6094  C   VAL A 823      44.769  85.106  -6.205  1.00 76.27           C  
ANISOU 6094  C   VAL A 823     7828   8122  13031    320   1789    722       C  
ATOM   6095  O   VAL A 823      45.275  85.764  -7.118  1.00 76.20           O  
ANISOU 6095  O   VAL A 823     7801   8043  13106    351   1866    812       O  
ATOM   6096  CB  VAL A 823      46.465  83.750  -4.857  1.00 72.77           C  
ANISOU 6096  CB  VAL A 823     7370   7746  12533    252   1721    578       C  
ATOM   6097  CG1 VAL A 823      47.216  83.642  -6.178  1.00 70.01           C  
ANISOU 6097  CG1 VAL A 823     7048   7370  12184    294   1784    697       C  
ATOM   6098  CG2 VAL A 823      47.433  83.845  -3.681  1.00 68.43           C  
ANISOU 6098  CG2 VAL A 823     6755   7181  12062    200   1702    459       C  
ATOM   6099  N   ASN A 824      43.591  84.494  -6.330  1.00 77.10           N  
ANISOU 6099  N   ASN A 824     7994   8297  13002    336   1736    737       N  
ATOM   6100  CA  ASN A 824      42.805  84.574  -7.572  1.00 76.47           C  
ANISOU 6100  CA  ASN A 824     7966   8220  12868    394   1762    858       C  
ATOM   6101  C   ASN A 824      41.290  84.748  -7.308  1.00 74.65           C  
ANISOU 6101  C   ASN A 824     7752   8015  12597    400   1720    839       C  
ATOM   6102  O   ASN A 824      40.497  83.835  -7.542  1.00 74.46           O  
ANISOU 6102  O   ASN A 824     7795   8071  12425    416   1667    855       O  
ATOM   6103  CB  ASN A 824      43.123  83.359  -8.472  1.00 74.96           C  
ANISOU 6103  CB  ASN A 824     7854   8099  12527    427   1747    931       C  
ATOM   6104  CG  ASN A 824      42.321  83.340  -9.772  1.00 75.45           C  
ANISOU 6104  CG  ASN A 824     7974   8176  12517    489   1767   1053       C  
ATOM   6105  OD1 ASN A 824      41.965  84.378 -10.327  1.00 72.29           O  
ANISOU 6105  OD1 ASN A 824     7550   7711  12207    519   1821   1118       O  
ATOM   6106  ND2 ASN A 824      42.039  82.137 -10.264  1.00 75.05           N  
ANISOU 6106  ND2 ASN A 824     7999   8213  12303    511   1722   1084       N  
ATOM   6107  N   PRO A 825      40.879  85.931  -6.821  1.00 76.04           N  
ANISOU 6107  N   PRO A 825     7863   8122  12909    385   1745    803       N  
ATOM   6108  CA  PRO A 825      39.461  86.108  -6.470  1.00 74.71           C  
ANISOU 6108  CA  PRO A 825     7703   7975  12707    386   1704    773       C  
ATOM   6109  C   PRO A 825      38.505  86.031  -7.647  1.00 76.83           C  
ANISOU 6109  C   PRO A 825     8030   8262  12901    445   1711    886       C  
ATOM   6110  O   PRO A 825      37.373  85.584  -7.470  1.00 78.94           O  
ANISOU 6110  O   PRO A 825     8334   8586  13073    449   1655    865       O  
ATOM   6111  CB  PRO A 825      39.401  87.494  -5.831  1.00 73.88           C  
ANISOU 6111  CB  PRO A 825     7509   7778  12784    361   1743    720       C  
ATOM   6112  CG  PRO A 825      40.657  88.194  -6.264  1.00 77.57           C  
ANISOU 6112  CG  PRO A 825     7928   8162  13385    367   1821    764       C  
ATOM   6113  CD  PRO A 825      41.696  87.113  -6.495  1.00 76.20           C  
ANISOU 6113  CD  PRO A 825     7795   8040  13117    365   1809    776       C  
ATOM   6114  N   SER A 826      38.934  86.449  -8.836  1.00 78.62           N  
ANISOU 6114  N   SER A 826     8265   8443  13165    493   1777   1004       N  
ATOM   6115  CA  SER A 826      38.058  86.356 -10.013  1.00 81.46           C  
ANISOU 6115  CA  SER A 826     8683   8825  13444    555   1782   1116       C  
ATOM   6116  C   SER A 826      37.780  84.891 -10.342  1.00 81.29           C  
ANISOU 6116  C   SER A 826     8745   8912  13228    569   1719   1128       C  
ATOM   6117  O   SER A 826      36.899  84.572 -11.143  1.00 81.34           O  
ANISOU 6117  O   SER A 826     8807   8960  13139    615   1701   1196       O  
ATOM   6118  CB  SER A 826      38.647  87.089 -11.222  1.00 84.35           C  
ANISOU 6118  CB  SER A 826     9042   9122  13887    604   1869   1244       C  
ATOM   6119  OG  SER A 826      39.795  86.417 -11.708  1.00 87.31           O  
ANISOU 6119  OG  SER A 826     9442   9518  14214    610   1891   1281       O  
ATOM   6120  N   GLY A 827      38.540  84.011  -9.697  1.00 80.73           N  
ANISOU 6120  N   GLY A 827     8682   8887  13104    530   1685   1057       N  
ATOM   6121  CA  GLY A 827      38.336  82.574  -9.790  1.00 80.08           C  
ANISOU 6121  CA  GLY A 827     8672   8906  12847    533   1620   1047       C  
ATOM   6122  C   GLY A 827      37.090  82.043  -9.099  1.00 78.26           C  
ANISOU 6122  C   GLY A 827     8467   8741  12529    515   1544    977       C  
ATOM   6123  O   GLY A 827      36.626  80.959  -9.438  1.00 75.49           O  
ANISOU 6123  O   GLY A 827     8180   8469  12033    532   1495    992       O  
ATOM   6124  N   VAL A 828      36.551  82.791  -8.133  1.00 79.37           N  
ANISOU 6124  N   VAL A 828     8554   8846  12757    481   1534    898       N  
ATOM   6125  CA  VAL A 828      35.332  82.363  -7.422  1.00 81.62           C  
ANISOU 6125  CA  VAL A 828     8857   9187  12968    462   1466    828       C  
ATOM   6126  C   VAL A 828      34.087  83.173  -7.745  1.00 84.71           C  
ANISOU 6126  C   VAL A 828     9239   9547  13399    490   1474    861       C  
ATOM   6127  O   VAL A 828      32.974  82.666  -7.619  1.00 85.88           O  
ANISOU 6127  O   VAL A 828     9422   9750  13457    495   1421    840       O  
ATOM   6128  CB  VAL A 828      35.492  82.330  -5.878  1.00 80.81           C  
ANISOU 6128  CB  VAL A 828     8711   9093  12902    394   1430    692       C  
ATOM   6129  CG1 VAL A 828      36.271  81.101  -5.451  1.00 82.45           C  
ANISOU 6129  CG1 VAL A 828     8950   9367  13009    367   1389    649       C  
ATOM   6130  CG2 VAL A 828      36.132  83.600  -5.338  1.00 78.25           C  
ANISOU 6130  CG2 VAL A 828     8301   8676  12754    368   1483    653       C  
ATOM   6131  N   ILE A 829      34.285  84.427  -8.149  1.00 88.11           N  
ANISOU 6131  N   ILE A 829     9621   9888  13968    509   1540    911       N  
ATOM   6132  CA  ILE A 829      33.198  85.398  -8.325  1.00 86.68           C  
ANISOU 6132  CA  ILE A 829     9416   9662  13859    532   1554    934       C  
ATOM   6133  C   ILE A 829      31.966  84.792  -8.986  1.00 83.60           C  
ANISOU 6133  C   ILE A 829     9089   9334  13340    574   1510    982       C  
ATOM   6134  O   ILE A 829      30.869  84.889  -8.449  1.00 85.02           O  
ANISOU 6134  O   ILE A 829     9262   9529  13511    561   1471    928       O  
ATOM   6135  CB  ILE A 829      33.665  86.663  -9.101  1.00 90.43           C  
ANISOU 6135  CB  ILE A 829     9847  10036  14477    565   1639   1024       C  
ATOM   6136  CG1 ILE A 829      34.878  87.330  -8.416  1.00 93.28           C  
ANISOU 6136  CG1 ILE A 829    10135  10326  14980    522   1686    970       C  
ATOM   6137  CG2 ILE A 829      32.518  87.658  -9.289  1.00 88.81           C  
ANISOU 6137  CG2 ILE A 829     9616   9782  14346    590   1652   1050       C  
ATOM   6138  CD1 ILE A 829      34.717  87.675  -6.941  1.00 93.28           C  
ANISOU 6138  CD1 ILE A 829    10075  10313  15053    459   1657    830       C  
ATOM   6139  N   GLN A 830      32.163  84.147 -10.131  1.00 84.46           N  
ANISOU 6139  N   GLN A 830     9259   9482  13349    622   1515   1078       N  
ATOM   6140  CA  GLN A 830      31.063  83.592 -10.909  1.00 88.06           C  
ANISOU 6140  CA  GLN A 830     9777   9997  13686    670   1476   1132       C  
ATOM   6141  C   GLN A 830      30.277  82.493 -10.177  1.00 87.86           C  
ANISOU 6141  C   GLN A 830     9785  10057  13539    640   1394   1045       C  
ATOM   6142  O   GLN A 830      29.093  82.289 -10.454  1.00 91.42           O  
ANISOU 6142  O   GLN A 830    10265  10543  13927    666   1357   1056       O  
ATOM   6143  CB  GLN A 830      31.580  83.077 -12.253  1.00 94.51           C  
ANISOU 6143  CB  GLN A 830    10649  10842  14419    726   1499   1246       C  
ATOM   6144  CG  GLN A 830      30.536  83.063 -13.363  1.00103.05           C  
ANISOU 6144  CG  GLN A 830    11776  11950  15429    793   1488   1335       C  
ATOM   6145  CD  GLN A 830      31.059  82.450 -14.652  1.00109.00           C  
ANISOU 6145  CD  GLN A 830    12587  12742  16084    847   1507   1439       C  
ATOM   6146  OE1 GLN A 830      32.018  82.951 -15.254  1.00108.59           O  
ANISOU 6146  OE1 GLN A 830    12522  12642  16093    867   1573   1511       O  
ATOM   6147  NE2 GLN A 830      30.426  81.360 -15.087  1.00107.67           N  
ANISOU 6147  NE2 GLN A 830    12482  12661  15766    872   1449   1445       N  
ATOM   6148  N   ASP A 831      30.934  81.802  -9.243  1.00 85.21           N  
ANISOU 6148  N   ASP A 831     9446   9755  13175    587   1367    959       N  
ATOM   6149  CA  ASP A 831      30.334  80.669  -8.526  1.00 79.37           C  
ANISOU 6149  CA  ASP A 831     8741   9098  12317    557   1293    879       C  
ATOM   6150  C   ASP A 831      30.319  80.879  -7.004  1.00 75.49           C  
ANISOU 6150  C   ASP A 831     8200   8598  11885    489   1272    754       C  
ATOM   6151  O   ASP A 831      30.475  79.921  -6.239  1.00 70.25           O  
ANISOU 6151  O   ASP A 831     7556   7994  11142    451   1225    683       O  
ATOM   6152  CB  ASP A 831      31.081  79.374  -8.870  1.00 81.35           C  
ANISOU 6152  CB  ASP A 831     9047   9416  12446    561   1270    897       C  
ATOM   6153  CG  ASP A 831      31.146  79.112 -10.368  1.00 85.19           C  
ANISOU 6153  CG  ASP A 831     9584   9919  12867    628   1291   1016       C  
ATOM   6154  OD1 ASP A 831      30.176  78.542 -10.909  1.00 86.67           O  
ANISOU 6154  OD1 ASP A 831     9817  10159  12954    661   1252   1042       O  
ATOM   6155  OD2 ASP A 831      32.169  79.466 -11.000  1.00 85.50           O  
ANISOU 6155  OD2 ASP A 831     9615   9919  12953    647   1346   1081       O  
ATOM   6156  N   PHE A 832      30.106  82.125  -6.575  1.00 71.99           N  
ANISOU 6156  N   PHE A 832     7694   8082  11579    476   1305    728       N  
ATOM   6157  CA  PHE A 832      30.204  82.494  -5.158  1.00 70.00           C  
ANISOU 6157  CA  PHE A 832     7385   7812  11399    414   1294    609       C  
ATOM   6158  C   PHE A 832      29.149  81.859  -4.255  1.00 70.34           C  
ANISOU 6158  C   PHE A 832     7445   7919  11363    382   1229    521       C  
ATOM   6159  O   PHE A 832      29.413  81.610  -3.072  1.00 70.07           O  
ANISOU 6159  O   PHE A 832     7388   7907  11329    329   1204    421       O  
ATOM   6160  CB  PHE A 832      30.175  84.015  -4.986  1.00 68.98           C  
ANISOU 6160  CB  PHE A 832     7181   7586  11442    410   1348    604       C  
ATOM   6161  CG  PHE A 832      30.849  84.494  -3.725  1.00 69.72           C  
ANISOU 6161  CG  PHE A 832     7210   7648  11634    350   1356    496       C  
ATOM   6162  CD1 PHE A 832      32.232  84.367  -3.560  1.00 70.03           C  
ANISOU 6162  CD1 PHE A 832     7232   7673  11702    331   1379    486       C  
ATOM   6163  CD2 PHE A 832      30.114  85.086  -2.707  1.00 68.48           C  
ANISOU 6163  CD2 PHE A 832     7004   7474  11540    315   1341    403       C  
ATOM   6164  CE1 PHE A 832      32.856  84.815  -2.402  1.00 69.15           C  
ANISOU 6164  CE1 PHE A 832     7058   7535  11682    278   1383    384       C  
ATOM   6165  CE2 PHE A 832      30.735  85.532  -1.545  1.00 69.63           C  
ANISOU 6165  CE2 PHE A 832     7089   7595  11774    261   1347    299       C  
ATOM   6166  CZ  PHE A 832      32.108  85.402  -1.394  1.00 69.43           C  
ANISOU 6166  CZ  PHE A 832     7046   7556  11776    244   1367    290       C  
ATOM   6167  N   ILE A 833      27.960  81.608  -4.805  1.00 71.35           N  
ANISOU 6167  N   ILE A 833     7610   8076  11424    416   1203