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***  sirk1_2020  ***

elNémo ID: 20012713215889478

Job options:

ID        	=	 20012713215889478
JOBID     	=	 sirk1_2020
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 sirk1_2020

HEADER    TRANSFERASE                             17-FEB-17   5UV4              
TITLE     CRYSTAL STRUCTURE OF MAIZE SIRK1 (SUCROSE-INDUCED RECEPTOR KINASE 1)  
TITLE    2 KINASE DOMAIN BOUND TO AMP-PNP                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE LEUCINE-RICH REPEAT PROTEIN KINASE FAMILY PROTEIN;
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 737-1045;                                     
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ZEA MAYS;                                       
SOURCE   3 ORGANISM_COMMON: MAIZE;                                              
SOURCE   4 ORGANISM_TAXID: 4577;                                                
SOURCE   5 GENE: ZEAMMB73_708518;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 DE3 R3                                
KEYWDS    RECEPTOR-LIKE KINASE, LEUCINE-RICH REPEAT, SUCROSE-INDUCED KINASE,    
KEYWDS   2 STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC,            
KEYWDS   3 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.M.COUNAGO,B.AQUINO,K.B.MASSIRER,O.GILEADI,P.ARRUDA,STRUCTURAL       
AUTHOR   2 GENOMICS CONSORTIUM (SGC)                                            
REVDAT   1   26-APR-17 5UV4    0                                                
JRNL        AUTH   B.AQUINO,R.M.COUNAGO,K.B.MASSIRER,O.GILEADI,P.ARRUDA,        
JRNL        AUTH 2 STRUCTURAL GENOMICS CONSORTIUM (SGC)                         
JRNL        TITL   CRYSTAL STRUCTURE OF MAIZE SIRK1 (SUCROSE-INDUCED RECEPTOR   
JRNL        TITL 2 KINASE 1) KINASE DOMAIN BOUND TO AMP-PNP                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.3                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.87                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 14160                          
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)  : 0.184                          
REMARK   3   R VALUE            (WORKING SET)  : 0.182                          
REMARK   3   FREE R VALUE                      : 0.211                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.600                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 652                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 7                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.30                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.48                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 96.71                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2885                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2056                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2755                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2040                   
REMARK   3   BIN FREE R VALUE                        : 0.2411                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.51                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 130                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2180                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 32                                      
REMARK   3   SOLVENT ATOMS            : 65                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 55.34                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 66.92                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 24.09650                                             
REMARK   3    B22 (A**2) : -12.70820                                            
REMARK   3    B33 (A**2) : -11.38830                                            
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : NULL                
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.296               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.197               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.284               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.196               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.929                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.913                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 2258   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 3076   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 753    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 40     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 336    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 2258   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 303    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 2577   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.06                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.06                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 17.74                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: {A|744 - 791}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):   16.9251   27.1041   44.9567           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2331 T22:   -0.2656                                    
REMARK   3     T33:   -0.0254 T12:    0.0657                                    
REMARK   3     T13:   -0.0452 T23:   -0.0422                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.3148 L22:    6.0770                                    
REMARK   3     L33:    6.3413 L12:   -0.3412                                    
REMARK   3     L13:   -1.9987 L23:    3.1408                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1194 S12:    0.1548 S13:   -0.7099                     
REMARK   3     S21:    0.1439 S22:    0.0213 S23:   -0.4948                     
REMARK   3     S31:    0.7060 S32:    0.1824 S33:   -0.1407                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: {A|792 - 810}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):    0.7589   31.5774   43.4059           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2400 T22:   -0.0427                                    
REMARK   3     T33:    0.0386 T12:   -0.0860                                    
REMARK   3     T13:   -0.0210 T23:   -0.0756                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.2921 L22:    4.9123                                    
REMARK   3     L33:    0.0355 L12:    2.9932                                    
REMARK   3     L13:   -1.7225 L23:   -0.3739                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0364 S12:   -0.0759 S13:   -0.4016                     
REMARK   3     S21:    0.0056 S22:   -0.2471 S23:    0.5493                     
REMARK   3     S31:    0.2011 S32:   -0.1801 S33:    0.2108                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: {A|811 - 860}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):   17.9826   37.5845   47.3062           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2461 T22:   -0.1582                                    
REMARK   3     T33:   -0.1284 T12:    0.0433                                    
REMARK   3     T13:   -0.0135 T23:   -0.0102                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.4910 L22:    3.0735                                    
REMARK   3     L33:    1.4471 L12:    0.2424                                    
REMARK   3     L13:    0.1555 L23:    0.2997                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1319 S12:   -0.0281 S13:   -0.4598                     
REMARK   3     S21:    0.2276 S22:   -0.0728 S23:   -0.2547                     
REMARK   3     S31:    0.3442 S32:    0.1477 S33:   -0.0592                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: {A|861 - 962}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):    9.8746   48.2166   47.6202           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2968 T22:   -0.1078                                    
REMARK   3     T33:   -0.1727 T12:   -0.0074                                    
REMARK   3     T13:    0.0492 T23:   -0.0681                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.4636 L22:    2.7957                                    
REMARK   3     L33:    1.4021 L12:    0.6044                                    
REMARK   3     L13:   -0.2721 L23:   -0.2649                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1864 S12:   -0.2214 S13:    0.0681                     
REMARK   3     S21:    0.2181 S22:   -0.2020 S23:    0.2208                     
REMARK   3     S31:    0.0202 S32:   -0.0522 S33:    0.0156                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: {A|963 - 1023}                                         
REMARK   3    ORIGIN FOR THE GROUP (A):   16.4457   63.0974   57.7091           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0898 T22:   -0.1023                                    
REMARK   3     T33:   -0.1365 T12:   -0.0666                                    
REMARK   3     T13:    0.0971 T23:   -0.2052                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.5891 L22:    4.7121                                    
REMARK   3     L33:    4.7757 L12:    0.8324                                    
REMARK   3     L13:    2.3435 L23:   -0.9762                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1351 S12:   -0.6391 S13:    0.4499                     
REMARK   3     S21:    0.9111 S22:   -0.1655 S23:    0.1635                     
REMARK   3     S31:   -0.4522 S32:   -0.2268 S33:    0.0304                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: {A|1024 - 1045}                                        
REMARK   3    ORIGIN FOR THE GROUP (A):    9.9324   61.3587   42.3465           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2449 T22:   -0.1102                                    
REMARK   3     T33:   -0.0040 T12:    0.0352                                    
REMARK   3     T13:    0.0135 T23:   -0.0622                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.8735 L22:    2.8661                                    
REMARK   3     L33:    0.0230 L12:   -0.0519                                    
REMARK   3     L13:   -0.5134 L23:    1.6991                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0222 S12:    0.0676 S13:    0.4852                     
REMARK   3     S21:   -0.0343 S22:   -0.2120 S23:    0.4802                     
REMARK   3     S31:   -0.0551 S32:   -0.1317 S33:    0.2342                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5UV4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000226460.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-NOV-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979200                           
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS MAY 1, 2016 BUILT=20160617     
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.5.31                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14190                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.870                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.04900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.8000                            
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) : 2.39                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4L68                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12.5% W/V PEG1000, 12.5% W/V PEG3350,    
REMARK 280  12.5% V/V MPD, 0,02M OF EACH MONOSSACHARIDE (D-GLUCOSE, D-          
REMARK 280  MANNOSE, D-GALACTOSE, L-FUCOSE, D-XYLOSE, N-ACETYL-D-GLUCOSAMINE)   
REMARK 280  , 0.1M MOPS/HEPES-NA PH 7.5, VAPOR DIFFUSION, SITTING DROP,         
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       26.72200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       39.87100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.26600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       39.87100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.72200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.26600            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     SER A   735                                                      
REMARK 465     MET A   736                                                      
REMARK 465     SER A   737                                                      
REMARK 465     PRO A   738                                                      
REMARK 465     ASP A   739                                                      
REMARK 465     LYS A   740                                                      
REMARK 465     LEU A   741                                                      
REMARK 465     VAL A   742                                                      
REMARK 465     GLY A   743                                                      
REMARK 465     ASN A   973                                                      
REMARK 465     ASP A   974                                                      
REMARK 465     GLY A   975                                                      
REMARK 465     VAL A   976                                                      
REMARK 465     THR A  1001                                                      
REMARK 465     GLY A  1002                                                      
REMARK 465     VAL A  1003                                                      
REMARK 465     GLU A  1004                                                      
REMARK 465     SER A  1005                                                      
REMARK 465     SER A  1006                                                      
REMARK 465     GLU A  1007                                                      
REMARK 465     GLY A  1008                                                      
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     ASP A 749    CG   OD1  OD2                                       
REMARK 470     ASN A 750    CG   OD1  ND2                                       
REMARK 470     THR A 755    OG1  CG2                                            
REMARK 470     GLU A 757    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 758    CG   CD   OE1  OE2                                  
REMARK 470     CYS A 761    SG                                                  
REMARK 470     ASP A 781    CG   OD1  OD2                                       
REMARK 470     LYS A 800    CG   CD   CE   NZ                                   
REMARK 470     LYS A 807    CG   CD   CE   NZ                                   
REMARK 470     LYS A 828    CG   CD   CE   NZ                                   
REMARK 470     GLU A 829    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 852    CG   OD1  OD2                                       
REMARK 470     GLU A 853    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 855    CG   OD1  ND2                                       
REMARK 470     ASN A 898    CG   OD1  ND2                                       
REMARK 470     SER A 899    OG                                                  
REMARK 470     SER A 902    OG                                                  
REMARK 470     ILE A 917    CG1  CG2  CD1                                       
REMARK 470     VAL A 923    CG1  CG2                                            
REMARK 470     SER A 938    OG                                                  
REMARK 470     THR A 939    OG1  CG2                                            
REMARK 470     SER A 940    OG                                                  
REMARK 470     LYS A 941    CG   CD   CE   NZ                                   
REMARK 470     ILE A 965    CG1  CG2  CD1                                       
REMARK 470     ILE A 969    CG1  CG2  CD1                                       
REMARK 470     ILE A 970    CG1  CG2  CD1                                       
REMARK 470     VAL A 977    CG1  CG2                                            
REMARK 470     MET A 985    CG   SD   CE                                        
REMARK 470     LEU A 988    CG   CD1  CD2                                       
REMARK 470     GLU A 989    CG   CD   OE1  OE2                                  
REMARK 470     VAL A 992    CG1  CG2                                            
REMARK 470     SER A 993    OG                                                  
REMARK 470     ARG A 998    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A 856      135.03    -36.79                                   
REMARK 500    CYS A 971       96.89    -69.40                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1265        DISTANCE =  6.61 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1102  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 893   OD1                                                    
REMARK 620 2 ASP A 907   OD2  89.3                                              
REMARK 620 3 ANP A1101   O1G  86.7  88.7                                        
REMARK 620 4 ANP A1101   O1B  79.5 167.4  85.1                                  
REMARK 620 5 ANP A1101   O1A 167.7 102.0  88.6  88.8                            
REMARK 620 6 HOH A1212   O    90.2  93.8 175.9  91.8  94.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP A 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1102                 
DBREF  5UV4 A  737  1045  UNP    K7VIQ3   K7VIQ3_MAIZE   737   1045             
SEQADV 5UV4 SER A  735  UNP  K7VIQ3              EXPRESSION TAG                 
SEQADV 5UV4 MET A  736  UNP  K7VIQ3              EXPRESSION TAG                 
SEQRES   1 A  311  SER MET SER PRO ASP LYS LEU VAL GLY ASP LEU HIS LEU          
SEQRES   2 A  311  PHE ASP ASN SER VAL VAL PHE THR ALA GLU GLU LEU SER          
SEQRES   3 A  311  CYS ALA PRO ALA GLU ILE ILE GLY ARG SER CYS HIS GLY          
SEQRES   4 A  311  THR SER TYR LYS ALA THR LEU ASP ASN GLY TYR MET LEU          
SEQRES   5 A  311  THR VAL LYS TRP LEU LYS GLU GLY PHE ALA LYS SER LYS          
SEQRES   6 A  311  LYS GLU PHE SER ARG GLU ILE LYS LYS LEU GLY SER VAL          
SEQRES   7 A  311  ARG HIS PRO ASN LEU VAL PRO LEU ARG GLY TYR TYR TRP          
SEQRES   8 A  311  GLY PRO LYS GLU HIS GLU ARG ILE MET ILE SER ASP TYR          
SEQRES   9 A  311  ALA ASP ALA THR SER LEU SER THR TYR LEU SER GLU PHE          
SEQRES  10 A  311  ASP GLU ARG ASN LEU PRO PRO LEU SER ALA GLY GLN ARG          
SEQRES  11 A  311  LEU ASN ILE ALA ILE ASP ILE ALA ARG CYS LEU ASP TYR          
SEQRES  12 A  311  LEU HIS ASN GLU ARG VAL ILE PRO HIS GLY ASN ILE LYS          
SEQRES  13 A  311  SER SER ASN VAL LEU ILE GLN ASN SER THR PRO SER ALA          
SEQRES  14 A  311  LEU VAL THR ASP TYR SER LEU HIS ARG LEU MET THR PRO          
SEQRES  15 A  311  ILE GLY MET ALA GLU GLN VAL LEU ASN ALA GLY ALA LEU          
SEQRES  16 A  311  GLY TYR SER PRO PRO GLU PHE SER SER THR SER LYS PRO          
SEQRES  17 A  311  CYS PRO SER LEU LYS SER ASP VAL TYR ALA PHE GLY VAL          
SEQRES  18 A  311  ILE LEU LEU GLU LEU LEU THR GLY LYS ILE ALA GLY GLU          
SEQRES  19 A  311  ILE ILE CYS MET ASN ASP GLY VAL VAL ASP LEU THR ASP          
SEQRES  20 A  311  TRP VAL ARG MET LEU ASP LEU GLU GLU ARG VAL SER GLU          
SEQRES  21 A  311  CYS TYR ASP ARG HIS ILE THR GLY VAL GLU SER SER GLU          
SEQRES  22 A  311  GLY ALA PRO GLN ALA LEU ASP GLY MET LEU ARG ILE ALA          
SEQRES  23 A  311  LEU ARG CYS ILE ARG SER ALA SER GLU ARG PRO GLU VAL          
SEQRES  24 A  311  ARG THR VAL PHE GLU ASP LEU LEU SER LEU SER SER              
HET    ANP  A1101      31                                                       
HET     MG  A1102       1                                                       
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   2  ANP    C10 H17 N6 O12 P3                                            
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  HOH   *65(H2 O)                                                     
HELIX    1 AA1 THR A  755  CYS A  761  1                                   7    
HELIX    2 AA2 SER A  798  SER A  811  1                                  14    
HELIX    3 AA3 LEU A  844  PHE A  851  1                                   8    
HELIX    4 AA4 SER A  860  GLU A  881  1                                  22    
HELIX    5 AA5 LYS A  890  SER A  892  5                                   3    
HELIX    6 AA6 SER A  909  MET A  914  5                                   6    
HELIX    7 AA7 THR A  915  LEU A  929  1                                  15    
HELIX    8 AA8 PRO A  933  SER A  937  5                                   5    
HELIX    9 AA9 SER A  945  GLY A  963  1                                  19    
HELIX   10 AB1 ASP A  978  GLU A  989  1                                  12    
HELIX   11 AB2 ARG A  991  TYR A  996  5                                   6    
HELIX   12 AB3 PRO A 1010  ILE A 1024  1                                  15    
HELIX   13 AB4 GLU A 1032  LEU A 1043  1                                  12    
SHEET    1 AA1 6 LEU A 745  LEU A 747  0                                        
SHEET    2 AA1 6 LEU A 820  TRP A 825 -1  O  TYR A 823   N  HIS A 746           
SHEET    3 AA1 6 ARG A 832  ASP A 837 -1  O  ILE A 835   N  ARG A 821           
SHEET    4 AA1 6 MET A 785  LEU A 791 -1  N  LEU A 791   O  ARG A 832           
SHEET    5 AA1 6 GLY A 773  THR A 779 -1  N  ALA A 778   O  LEU A 786           
SHEET    6 AA1 6 ALA A 764  ARG A 769 -1  N  ILE A 767   O  SER A 775           
SHEET    1 AA2 3 THR A 842  SER A 843  0                                        
SHEET    2 AA2 3 VAL A 894  ILE A 896 -1  O  ILE A 896   N  THR A 842           
SHEET    3 AA2 3 ALA A 903  VAL A 905 -1  O  LEU A 904   N  LEU A 895           
LINK         OD1 ASN A 893                MG    MG A1102     1555   1555  2.14  
LINK         OD2 ASP A 907                MG    MG A1102     1555   1555  1.99  
LINK         O1G ANP A1101                MG    MG A1102     1555   1555  2.20  
LINK         O1B ANP A1101                MG    MG A1102     1555   1555  2.33  
LINK         O1A ANP A1101                MG    MG A1102     1555   1555  1.75  
LINK        MG    MG A1102                 O   HOH A1212     1555   1555  2.18  
CISPEP   1 THR A  900    PRO A  901          0         6.44                     
SITE     1 AC1 23 ILE A 767  GLY A 768  SER A 770  HIS A 772                    
SITE     2 AC1 23 SER A 775  LYS A 789  TYR A 838  ALA A 839                    
SITE     3 AC1 23 ALA A 841  SER A 843  ASN A 888  LYS A 890                    
SITE     4 AC1 23 SER A 892  ASN A 893  LEU A 895  ASP A 907                    
SITE     5 AC1 23  MG A1102  HOH A1201  HOH A1208  HOH A1210                    
SITE     6 AC1 23 HOH A1212  HOH A1227  HOH A1235                               
SITE     1 AC2  4 ASN A 893  ASP A 907  ANP A1101  HOH A1212                    
CRYST1   53.444   74.532   79.742  90.00  90.00  90.00 P 21 21 21    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      0.018711  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013417  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012540        0.00000                         
ATOM      1  N   ASP A 744       7.259  18.314  41.197  1.00 85.52           N  
ANISOU    1  N   ASP A 744    10448   9143  12903  -1717    294  -2784       N  
ATOM      2  CA  ASP A 744       6.902  19.276  40.165  1.00 84.09           C  
ANISOU    2  CA  ASP A 744     9924   9541  12484  -1523     44  -2963       C  
ATOM      3  C   ASP A 744       7.767  20.533  40.219  1.00 81.40           C  
ANISOU    3  C   ASP A 744     9586   9406  11936  -1102   -118  -2574       C  
ATOM      4  O   ASP A 744       7.672  21.337  41.141  1.00 79.62           O  
ANISOU    4  O   ASP A 744     9307   9285  11660  -1055   -135  -2301       O  
ATOM      5  CB  ASP A 744       5.424  19.642  40.269  1.00 88.67           C  
ANISOU    5  CB  ASP A 744    10117  10533  13039  -1783     -2  -3271       C  
ATOM      6  CG  ASP A 744       4.945  20.469  39.095  1.00105.92           C  
ANISOU    6  CG  ASP A 744    11962  13339  14944  -1534   -303  -3443       C  
ATOM      7  OD1 ASP A 744       5.712  20.632  38.129  1.00106.98           O  
ANISOU    7  OD1 ASP A 744    12177  13587  14883  -1260   -441  -3468       O  
ATOM      8  OD2 ASP A 744       3.799  20.959  39.138  1.00114.76           O  
ANISOU    8  OD2 ASP A 744    12747  14826  16031  -1608   -389  -3576       O  
ATOM      9  N   LEU A 745       8.606  20.683  39.206  1.00 74.45           N  
ANISOU    9  N   LEU A 745     8767   8582  10938   -830   -200  -2595       N  
ATOM     10  CA  LEU A 745       9.527  21.812  39.057  1.00 69.70           C  
ANISOU   10  CA  LEU A 745     8177   8151  10156   -478   -293  -2304       C  
ATOM     11  C   LEU A 745       9.273  22.515  37.709  1.00 72.52           C  
ANISOU   11  C   LEU A 745     8390   8957  10208   -312   -440  -2496       C  
ATOM     12  O   LEU A 745       9.294  21.860  36.666  1.00 73.71           O  
ANISOU   12  O   LEU A 745     8562   9150  10296   -336   -449  -2813       O  
ATOM     13  CB  LEU A 745      10.988  21.332  39.150  1.00 68.70           C  
ANISOU   13  CB  LEU A 745     8273   7671  10160   -293   -206  -2151       C  
ATOM     14  CG  LEU A 745      12.064  22.366  38.755  1.00 70.56           C  
ANISOU   14  CG  LEU A 745     8488   8079  10242     19   -241  -1964       C  
ATOM     15  CD1 LEU A 745      12.120  23.537  39.731  1.00 66.27           C  
ANISOU   15  CD1 LEU A 745     7892   7644   9644     92   -285  -1626       C  
ATOM     16  CD2 LEU A 745      13.429  21.709  38.595  1.00 74.50           C  
ANISOU   16  CD2 LEU A 745     9114   8285  10909    188   -150  -1963       C  
ATOM     17  N   HIS A 746       9.040  23.839  37.738  1.00 66.56           N  
ANISOU   17  N   HIS A 746     7534   8515   9242   -130   -546  -2302       N  
ATOM     18  CA  HIS A 746       8.771  24.619  36.535  1.00 67.29           C  
ANISOU   18  CA  HIS A 746     7569   9012   8987     87   -695  -2408       C  
ATOM     19  C   HIS A 746       9.850  25.659  36.295  1.00 68.08           C  
ANISOU   19  C   HIS A 746     7835   9117   8914    370   -629  -2103       C  
ATOM     20  O   HIS A 746      10.234  26.385  37.202  1.00 65.36           O  
ANISOU   20  O   HIS A 746     7513   8664   8655    420   -564  -1798       O  
ATOM     21  CB  HIS A 746       7.371  25.263  36.602  1.00 69.75           C  
ANISOU   21  CB  HIS A 746     7624   9697   9181     84   -879  -2502       C  
ATOM     22  CG  HIS A 746       6.945  25.963  35.338  1.00 75.81           C  
ANISOU   22  CG  HIS A 746     8355  10898   9551    356  -1094  -2628       C  
ATOM     23  ND1 HIS A 746       7.120  27.333  35.168  1.00 76.58           N  
ANISOU   23  ND1 HIS A 746     8555  11151   9389    684  -1146  -2328       N  
ATOM     24  CD2 HIS A 746       6.365  25.462  34.225  1.00 81.22           C  
ANISOU   24  CD2 HIS A 746     8953  11871  10037    353  -1269  -3019       C  
ATOM     25  CE1 HIS A 746       6.652  27.612  33.963  1.00 78.72           C  
ANISOU   25  CE1 HIS A 746     8838  11784   9290    904  -1355  -2502       C  
ATOM     26  NE2 HIS A 746       6.197  26.520  33.353  1.00 82.18           N  
ANISOU   26  NE2 HIS A 746     9146  12344   9734    721  -1457  -2930       N  
ATOM     27  N   LEU A 747      10.352  25.720  35.079  1.00 65.83           N  
ANISOU   27  N   LEU A 747     7679   8951   8382    524   -614  -2213       N  
ATOM     28  CA  LEU A 747      11.355  26.704  34.698  1.00 64.20           C  
ANISOU   28  CA  LEU A 747     7652   8749   7992    747   -484  -1970       C  
ATOM     29  C   LEU A 747      10.771  27.581  33.593  1.00 71.50           C  
ANISOU   29  C   LEU A 747     8671  10039   8456    971   -610  -1989       C  
ATOM     30  O   LEU A 747      10.242  27.062  32.605  1.00 73.46           O  
ANISOU   30  O   LEU A 747     8923  10509   8480    986   -746  -2286       O  
ATOM     31  CB  LEU A 747      12.654  26.026  34.236  1.00 64.48           C  
ANISOU   31  CB  LEU A 747     7813   8560   8127    746   -277  -2060       C  
ATOM     32  CG  LEU A 747      13.360  25.070  35.222  1.00 67.97           C  
ANISOU   32  CG  LEU A 747     8200   8620   9004    619   -183  -2044       C  
ATOM     33  CD1 LEU A 747      14.516  24.365  34.536  1.00 69.73           C  
ANISOU   33  CD1 LEU A 747     8508   8678   9308    677     -2  -2216       C  
ATOM     34  CD2 LEU A 747      13.867  25.800  36.475  1.00 65.43           C  
ANISOU   34  CD2 LEU A 747     7833   8165   8861    645   -145  -1707       C  
ATOM     35  N   PHE A 748      10.858  28.906  33.759  1.00 68.16           N  
ANISOU   35  N   PHE A 748     8353   9670   7875   1158   -573  -1680       N  
ATOM     36  CA  PHE A 748      10.314  29.868  32.785  1.00 70.63           C  
ANISOU   36  CA  PHE A 748     8838  10280   7720   1444   -693  -1617       C  
ATOM     37  C   PHE A 748      11.067  29.879  31.449  1.00 78.04           C  
ANISOU   37  C   PHE A 748    10092  11268   8292   1567   -547  -1674       C  
ATOM     38  O   PHE A 748      10.413  29.850  30.409  1.00 81.53           O  
ANISOU   38  O   PHE A 748    10632  12013   8332   1731   -745  -1836       O  
ATOM     39  CB  PHE A 748      10.224  31.269  33.404  1.00 70.34           C  
ANISOU   39  CB  PHE A 748     8880  10198   7650   1608   -642  -1259       C  
ATOM     40  CG  PHE A 748       9.527  31.248  34.746  1.00 68.90           C  
ANISOU   40  CG  PHE A 748     8401   9967   7812   1469   -740  -1225       C  
ATOM     41  CD1 PHE A 748       8.225  30.762  34.868  1.00 72.12           C  
ANISOU   41  CD1 PHE A 748     8523  10617   8262   1426  -1006  -1463       C  
ATOM     42  CD2 PHE A 748      10.175  31.690  35.888  1.00 67.16           C  
ANISOU   42  CD2 PHE A 748     8174   9477   7867   1357   -550   -995       C  
ATOM     43  CE1 PHE A 748       7.589  30.725  36.106  1.00 71.25           C  
ANISOU   43  CE1 PHE A 748     8157  10456   8461   1263  -1029  -1449       C  
ATOM     44  CE2 PHE A 748       9.527  31.679  37.125  1.00 68.48           C  
ANISOU   44  CE2 PHE A 748     8116   9608   8296   1224   -614   -966       C  
ATOM     45  CZ  PHE A 748       8.244  31.185  37.228  1.00 68.12           C  
ANISOU   45  CZ  PHE A 748     7817   9778   8288   1170   -828  -1184       C  
ATOM     46  N   ASP A 749      12.433  29.868  31.475  1.00 72.77           N  
ANISOU   46  N   ASP A 749     9561  10328   7759   1481   -204  -1581       N  
ATOM     47  CA  ASP A 749      13.281  29.834  30.266  1.00 73.88           C  
ANISOU   47  CA  ASP A 749     9995  10481   7595   1545     33  -1660       C  
ATOM     48  C   ASP A 749      14.136  28.563  30.238  1.00 76.20           C  
ANISOU   48  C   ASP A 749    10163  10590   8198   1346    191  -1937       C  
ATOM     49  O   ASP A 749      14.149  27.798  31.209  1.00 72.13           O  
ANISOU   49  O   ASP A 749     9385   9895   8128   1185    124  -2004       O  
ATOM     50  CB  ASP A 749      14.186  31.088  30.196  1.00 74.68           C  
ANISOU   50  CB  ASP A 749    10372  10429   7572   1627    377  -1340       C  
ATOM     51  N   ASN A 750      14.879  28.356  29.135  1.00 76.26           N  
ANISOU   51  N   ASN A 750    10394  10619   7961   1376    429  -2088       N  
ATOM     52  CA  ASN A 750      15.786  27.217  28.972  1.00 76.75           C  
ANISOU   52  CA  ASN A 750    10361  10498   8304   1240    625  -2374       C  
ATOM     53  C   ASN A 750      17.235  27.644  29.310  1.00 80.74           C  
ANISOU   53  C   ASN A 750    10844  10765   9068   1202   1017  -2240       C  
ATOM     54  O   ASN A 750      18.171  26.847  29.197  1.00 80.97           O  
ANISOU   54  O   ASN A 750    10767  10636   9360   1140   1222  -2462       O  
ATOM     55  CB  ASN A 750      15.671  26.654  27.548  1.00 81.91           C  
ANISOU   55  CB  ASN A 750    11234  11349   8539   1280    656  -2699       C  
ATOM     56  N   SER A 751      17.398  28.912  29.741  1.00 77.51           N  
ANISOU   56  N   SER A 751    10512  10333   8607   1241   1122  -1910       N  
ATOM     57  CA  SER A 751      18.667  29.551  30.102  1.00 77.86           C  
ANISOU   57  CA  SER A 751    10510  10195   8879   1168   1492  -1796       C  
ATOM     58  C   SER A 751      19.362  28.890  31.289  1.00 81.85           C  
ANISOU   58  C   SER A 751    10623  10496   9980   1074   1451  -1864       C  
ATOM     59  O   SER A 751      20.588  28.795  31.298  1.00 84.27           O  
ANISOU   59  O   SER A 751    10792  10692  10534   1024   1739  -1982       O  
ATOM     60  CB  SER A 751      18.446  31.031  30.392  1.00 80.47           C  
ANISOU   60  CB  SER A 751    11022  10524   9027   1210   1566  -1447       C  
ATOM     61  OG  SER A 751      17.492  31.182  31.429  1.00 89.33           O  
ANISOU   61  OG  SER A 751    11982  11662  10297   1236   1209  -1288       O  
ATOM     62  N   VAL A 752      18.590  28.479  32.300  1.00 75.60           N  
ANISOU   62  N   VAL A 752     9657   9664   9403   1061   1103  -1790       N  
ATOM     63  CA  VAL A 752      19.080  27.819  33.516  1.00 74.09           C  
ANISOU   63  CA  VAL A 752     9173   9274   9703   1015    997  -1801       C  
ATOM     64  C   VAL A 752      18.233  26.568  33.695  1.00 79.09           C  
ANISOU   64  C   VAL A 752     9768   9851  10434    995    724  -1945       C  
ATOM     65  O   VAL A 752      17.025  26.671  33.965  1.00 77.51           O  
ANISOU   65  O   VAL A 752     9601   9747  10102    958    491  -1859       O  
ATOM     66  CB  VAL A 752      19.041  28.707  34.795  1.00 74.82           C  
ANISOU   66  CB  VAL A 752     9151   9324   9953    976    908  -1524       C  
ATOM     67  CG1 VAL A 752      19.921  28.095  35.881  1.00 74.15           C  
ANISOU   67  CG1 VAL A 752     8796   9061  10315    973    848  -1562       C  
ATOM     68  CG2 VAL A 752      19.464  30.148  34.504  1.00 74.60           C  
ANISOU   68  CG2 VAL A 752     9252   9356   9736    956   1179  -1369       C  
ATOM     69  N   VAL A 753      18.870  25.396  33.518  1.00 77.42           N  
ANISOU   69  N   VAL A 753     9480   9468  10467   1015    787  -2190       N  
ATOM     70  CA  VAL A 753      18.226  24.084  33.534  1.00 78.27           C  
ANISOU   70  CA  VAL A 753     9602   9442  10694    968    621  -2386       C  
ATOM     71  C   VAL A 753      18.836  23.148  34.578  1.00 83.04           C  
ANISOU   71  C   VAL A 753    10077   9715  11758   1014    564  -2376       C  
ATOM     72  O   VAL A 753      20.062  23.008  34.651  1.00 83.94           O  
ANISOU   72  O   VAL A 753    10069   9719  12106   1142    707  -2435       O  
ATOM     73  CB  VAL A 753      18.259  23.471  32.100  1.00 85.02           C  
ANISOU   73  CB  VAL A 753    10596  10378  11330    974    762  -2734       C  
ATOM     74  CG1 VAL A 753      17.783  22.018  32.080  1.00 86.75           C  
ANISOU   74  CG1 VAL A 753    10830  10392  11739    897    659  -3009       C  
ATOM     75  CG2 VAL A 753      17.444  24.310  31.125  1.00 85.35           C  
ANISOU   75  CG2 VAL A 753    10823  10765  10841    969    729  -2720       C  
ATOM     76  N   PHE A 754      17.955  22.478  35.355  1.00 78.35           N  
ANISOU   76  N   PHE A 754     9520   8964  11286    918    363  -2320       N  
ATOM     77  CA  PHE A 754      18.298  21.495  36.392  1.00 77.68           C  
ANISOU   77  CA  PHE A 754     9431   8515  11570    971    284  -2264       C  
ATOM     78  C   PHE A 754      17.086  20.645  36.732  1.00 81.01           C  
ANISOU   78  C   PHE A 754     9988   8771  12021    777    174  -2311       C  
ATOM     79  O   PHE A 754      15.965  20.993  36.364  1.00 79.79           O  
ANISOU   79  O   PHE A 754     9839   8848  11628    603    113  -2368       O  
ATOM     80  CB  PHE A 754      18.847  22.175  37.665  1.00 76.87           C  
ANISOU   80  CB  PHE A 754     9214   8391  11600   1061    185  -1948       C  
ATOM     81  CG  PHE A 754      17.934  23.231  38.233  1.00 75.00           C  
ANISOU   81  CG  PHE A 754     8978   8367  11153    918     80  -1709       C  
ATOM     82  CD1 PHE A 754      16.951  22.899  39.158  1.00 76.95           C  
ANISOU   82  CD1 PHE A 754     9312   8499  11426    780    -59  -1574       C  
ATOM     83  CD2 PHE A 754      18.045  24.556  37.834  1.00 74.77           C  
ANISOU   83  CD2 PHE A 754     8884   8622  10902    919    160  -1630       C  
ATOM     84  CE1 PHE A 754      16.089  23.867  39.657  1.00 74.84           C  
ANISOU   84  CE1 PHE A 754     9017   8436  10983    662   -131  -1395       C  
ATOM     85  CE2 PHE A 754      17.173  25.519  38.323  1.00 74.74           C  
ANISOU   85  CE2 PHE A 754     8893   8783  10721    825     73  -1428       C  
ATOM     86  CZ  PHE A 754      16.198  25.168  39.226  1.00 72.35           C  
ANISOU   86  CZ  PHE A 754     8626   8400  10463    706    -79  -1327       C  
ATOM     87  N   THR A 755      17.310  19.555  37.466  1.00 79.82           N  
ANISOU   87  N   THR A 755     9947   8215  12167    815    156  -2289       N  
ATOM     88  CA  THR A 755      16.266  18.649  37.933  1.00 81.04           C  
ANISOU   88  CA  THR A 755    10275   8112  12404    591    128  -2325       C  
ATOM     89  C   THR A 755      15.814  19.037  39.350  1.00 83.64           C  
ANISOU   89  C   THR A 755    10646   8386  12748    516     13  -1970       C  
ATOM     90  O   THR A 755      16.540  19.735  40.073  1.00 81.04           O  
ANISOU   90  O   THR A 755    10240   8122  12428    696    -70  -1709       O  
ATOM     91  CB  THR A 755      16.799  17.211  37.926  1.00 88.87           C  
ANISOU   91  CB  THR A 755    11460   8608  13697    689    228  -2479       C  
ATOM     92  N   ALA A 756      14.613  18.557  39.748  1.00 81.47           N  
ANISOU   92  N   ALA A 756    10484   7994  12475    224     32  -2002       N  
ATOM     93  CA  ALA A 756      14.063  18.716  41.100  1.00 79.75           C  
ANISOU   93  CA  ALA A 756    10366   7667  12266     97     -8  -1706       C  
ATOM     94  C   ALA A 756      14.955  17.897  42.069  1.00 83.40           C  
ANISOU   94  C   ALA A 756    11100   7653  12936    307    -15  -1475       C  
ATOM     95  O   ALA A 756      15.273  18.373  43.160  1.00 80.91           O  
ANISOU   95  O   ALA A 756    10831   7336  12576    419   -121  -1157       O  
ATOM     96  CB  ALA A 756      12.626  18.208  41.140  1.00 81.89           C  
ANISOU   96  CB  ALA A 756    10685   7891  12537   -298     90  -1886       C  
ATOM     97  N   GLU A 757      15.405  16.694  41.624  1.00 82.66           N  
ANISOU   97  N   GLU A 757    11190   7167  13052    401     82  -1653       N  
ATOM     98  CA  GLU A 757      16.305  15.815  42.373  1.00 85.45           C  
ANISOU   98  CA  GLU A 757    11824   7035  13610    693     57  -1461       C  
ATOM     99  C   GLU A 757      17.703  16.441  42.482  1.00 88.95           C  
ANISOU   99  C   GLU A 757    12048   7666  14082   1122   -121  -1338       C  
ATOM    100  O   GLU A 757      18.388  16.224  43.483  1.00 90.57           O  
ANISOU  100  O   GLU A 757    12396   7660  14358   1400   -264  -1072       O  
ATOM    101  CB  GLU A 757      16.375  14.409  41.752  1.00 91.06           C  
ANISOU  101  CB  GLU A 757    12781   7264  14556    693    235  -1728       C  
ATOM    102  N   GLU A 758      18.111  17.238  41.474  1.00 83.06           N  
ANISOU  102  N   GLU A 758    10961   7332  13266   1166   -108  -1543       N  
ATOM    103  CA  GLU A 758      19.396  17.933  41.481  1.00 82.13           C  
ANISOU  103  CA  GLU A 758    10571   7439  13196   1487   -209  -1500       C  
ATOM    104  C   GLU A 758      19.374  19.079  42.500  1.00 82.62           C  
ANISOU  104  C   GLU A 758    10522   7775  13095   1464   -371  -1203       C  
ATOM    105  O   GLU A 758      20.349  19.272  43.221  1.00 82.79           O  
ANISOU  105  O   GLU A 758    10448   7805  13202   1739   -531  -1066       O  
ATOM    106  CB  GLU A 758      19.760  18.438  40.075  1.00 82.87           C  
ANISOU  106  CB  GLU A 758    10404   7851  13231   1475    -61  -1810       C  
ATOM    107  N   LEU A 759      18.253  19.816  42.574  1.00 77.06           N  
ANISOU  107  N   LEU A 759     9815   7299  12164   1150   -339  -1134       N  
ATOM    108  CA  LEU A 759      18.046  20.929  43.513  1.00 74.04           C  
ANISOU  108  CA  LEU A 759     9357   7160  11615   1082   -449   -884       C  
ATOM    109  C   LEU A 759      18.020  20.449  44.974  1.00 78.13           C  
ANISOU  109  C   LEU A 759    10137   7406  12144   1145   -584   -596       C  
ATOM    110  O   LEU A 759      18.656  21.060  45.833  1.00 76.22           O  
ANISOU  110  O   LEU A 759     9819   7289  11853   1297   -746   -422       O  
ATOM    111  CB  LEU A 759      16.742  21.683  43.169  1.00 71.63           C  
ANISOU  111  CB  LEU A 759     9002   7121  11093    766   -367   -918       C  
ATOM    112  CG  LEU A 759      16.485  22.993  43.941  1.00 73.48           C  
ANISOU  112  CG  LEU A 759     9134   7631  11156    696   -433   -714       C  
ATOM    113  CD1 LEU A 759      17.494  24.094  43.557  1.00 72.07           C  
ANISOU  113  CD1 LEU A 759     8711   7719  10953    848   -433   -740       C  
ATOM    114  CD2 LEU A 759      15.061  23.460  43.747  1.00 73.29           C  
ANISOU  114  CD2 LEU A 759     9090   7790  10966    429   -367   -752       C  
ATOM    115  N   SER A 760      17.296  19.347  45.240  1.00 77.10           N  
ANISOU  115  N   SER A 760    10339   6896  12059   1014   -499   -562       N  
ATOM    116  CA  SER A 760      17.183  18.732  46.561  1.00 78.88           C  
ANISOU  116  CA  SER A 760    10939   6782  12252   1058   -565   -268       C  
ATOM    117  C   SER A 760      18.500  18.113  47.067  1.00 85.57           C  
ANISOU  117  C   SER A 760    11901   7381  13230   1526   -767   -139       C  
ATOM    118  O   SER A 760      18.731  18.115  48.277  1.00 87.45           O  
ANISOU  118  O   SER A 760    12356   7529  13344   1673   -936    150       O  
ATOM    119  CB  SER A 760      16.063  17.696  46.576  1.00 83.96           C  
ANISOU  119  CB  SER A 760    11928   7043  12932    748   -339   -306       C  
ATOM    120  OG  SER A 760      16.358  16.608  45.717  1.00 94.08           O  
ANISOU  120  OG  SER A 760    13309   7999  14440    838   -236   -529       O  
ATOM    121  N   CYS A 761      19.356  17.592  46.162  1.00 82.55           N  
ANISOU  121  N   CYS A 761    11375   6910  13081   1784   -762   -366       N  
ATOM    122  CA  CYS A 761      20.638  16.988  46.558  1.00 86.25           C  
ANISOU  122  CA  CYS A 761    11880   7170  13721   2292   -973   -298       C  
ATOM    123  C   CYS A 761      21.815  17.970  46.442  1.00 90.45           C  
ANISOU  123  C   CYS A 761    11909   8156  14303   2542  -1158   -409       C  
ATOM    124  O   CYS A 761      22.972  17.555  46.529  1.00 94.09           O  
ANISOU  124  O   CYS A 761    12243   8546  14960   2979  -1331   -467       O  
ATOM    125  CB  CYS A 761      20.904  15.685  45.802  1.00 89.99           C  
ANISOU  125  CB  CYS A 761    12531   7197  14465   2465   -837   -489       C  
ATOM    126  N   ALA A 762      21.518  19.268  46.289  1.00 83.13           N  
ANISOU  126  N   ALA A 762    10695   7679  13214   2268  -1111   -450       N  
ATOM    127  CA  ALA A 762      22.518  20.327  46.142  1.00 82.16           C  
ANISOU  127  CA  ALA A 762    10104   7978  13135   2387  -1200   -586       C  
ATOM    128  C   ALA A 762      22.985  20.881  47.489  1.00 87.77           C  
ANISOU  128  C   ALA A 762    10775   8851  13723   2536  -1498   -378       C  
ATOM    129  O   ALA A 762      22.151  21.059  48.392  1.00 85.58           O  
ANISOU  129  O   ALA A 762    10787   8527  13202   2355  -1545   -122       O  
ATOM    130  CB  ALA A 762      21.949  21.471  45.298  1.00 78.59           C  
ANISOU  130  CB  ALA A 762     9441   7870  12551   2024   -971   -719       C  
ATOM    131  N   PRO A 763      24.299  21.224  47.625  1.00 87.24           N  
ANISOU  131  N   PRO A 763    10316   9017  13812   2835  -1687   -529       N  
ATOM    132  CA  PRO A 763      24.763  21.851  48.874  1.00 88.11           C  
ANISOU  132  CA  PRO A 763    10337   9360  13782   2953  -1999   -398       C  
ATOM    133  C   PRO A 763      23.934  23.113  49.119  1.00 90.29           C  
ANISOU  133  C   PRO A 763    10606   9896  13805   2515  -1862   -324       C  
ATOM    134  O   PRO A 763      23.848  23.994  48.249  1.00 86.71           O  
ANISOU  134  O   PRO A 763     9893   9662  13392   2260  -1610   -510       O  
ATOM    135  CB  PRO A 763      26.239  22.169  48.591  1.00 91.94           C  
ANISOU  135  CB  PRO A 763    10258  10135  14541   3234  -2124   -718       C  
ATOM    136  CG  PRO A 763      26.626  21.273  47.484  1.00 97.77           C  
ANISOU  136  CG  PRO A 763    10921  10657  15570   3418  -1952   -928       C  
ATOM    137  CD  PRO A 763      25.405  21.090  46.650  1.00 90.40           C  
ANISOU  137  CD  PRO A 763    10306   9517  14526   3051  -1607   -873       C  
ATOM    138  N   ALA A 764      23.209  23.123  50.247  1.00 88.50           N  
ANISOU  138  N   ALA A 764    10738   9589  13301   2426  -1984    -35       N  
ATOM    139  CA  ALA A 764      22.309  24.217  50.615  1.00 84.46           C  
ANISOU  139  CA  ALA A 764    10272   9274  12547   2039  -1852     50       C  
ATOM    140  C   ALA A 764      22.678  24.835  51.955  1.00 89.16           C  
ANISOU  140  C   ALA A 764    10865  10081  12931   2103  -2126    151       C  
ATOM    141  O   ALA A 764      22.990  24.115  52.906  1.00 93.64           O  
ANISOU  141  O   ALA A 764    11686  10513  13380   2385  -2414    332       O  
ATOM    142  CB  ALA A 764      20.875  23.718  50.650  1.00 83.69           C  
ANISOU  142  CB  ALA A 764    10597   8906  12297   1778  -1651    243       C  
ATOM    143  N   GLU A 765      22.647  26.165  52.032  1.00 81.33           N  
ANISOU  143  N   GLU A 765     9624   9406  11871   1854  -2038     33       N  
ATOM    144  CA  GLU A 765      22.933  26.882  53.278  1.00 80.87           C  
ANISOU  144  CA  GLU A 765     9549   9582  11595   1849  -2268     69       C  
ATOM    145  C   GLU A 765      21.904  27.979  53.509  1.00 78.47           C  
ANISOU  145  C   GLU A 765     9336   9385  11095   1450  -2026    115       C  
ATOM    146  O   GLU A 765      21.554  28.684  52.569  1.00 75.21           O  
ANISOU  146  O   GLU A 765     8750   9030  10797   1229  -1734    -11       O  
ATOM    147  CB  GLU A 765      24.390  27.391  53.361  1.00 84.40           C  
ANISOU  147  CB  GLU A 765     9499  10350  12218   2041  -2495   -227       C  
ATOM    148  CG  GLU A 765      24.891  28.187  52.167  1.00 93.13           C  
ANISOU  148  CG  GLU A 765    10151  11621  13613   1870  -2208   -546       C  
ATOM    149  CD  GLU A 765      26.396  28.161  51.967  1.00115.67           C  
ANISOU  149  CD  GLU A 765    12493  14698  16759   2118  -2382   -878       C  
ATOM    150  OE1 GLU A 765      27.097  28.986  52.597  1.00113.77           O  
ANISOU  150  OE1 GLU A 765    11941  14769  16517   2066  -2531  -1088       O  
ATOM    151  OE2 GLU A 765      26.874  27.329  51.162  1.00108.03           O  
ANISOU  151  OE2 GLU A 765    11403  13603  16038   2348  -2350   -971       O  
ATOM    152  N   ILE A 766      21.396  28.090  54.744  1.00 74.79           N  
ANISOU  152  N   ILE A 766     9174   8927  10315   1383  -2137    301       N  
ATOM    153  CA  ILE A 766      20.393  29.080  55.127  1.00 72.57           C  
ANISOU  153  CA  ILE A 766     8997   8735   9843   1037  -1912    336       C  
ATOM    154  C   ILE A 766      20.920  30.535  54.970  1.00 73.64           C  
ANISOU  154  C   ILE A 766     8750   9168  10062    881  -1835     70       C  
ATOM    155  O   ILE A 766      22.004  30.866  55.437  1.00 74.58           O  
ANISOU  155  O   ILE A 766     8630   9501  10205    998  -2071   -102       O  
ATOM    156  CB  ILE A 766      19.783  28.796  56.534  1.00 78.04           C  
ANISOU  156  CB  ILE A 766    10133   9360  10157   1000  -2016    578       C  
ATOM    157  CG1 ILE A 766      18.527  29.655  56.796  1.00 75.86           C  
ANISOU  157  CG1 ILE A 766     9972   9123   9727    634  -1703    603       C  
ATOM    158  CG2 ILE A 766      20.803  28.939  57.663  1.00 83.03           C  
ANISOU  158  CG2 ILE A 766    10752  10206  10588   1218  -2411    548       C  
ATOM    159  CD1 ILE A 766      17.494  28.983  57.682  1.00 87.27           C  
ANISOU  159  CD1 ILE A 766    11905  10367  10885    520  -1607    858       C  
ATOM    160  N   ILE A 767      20.159  31.357  54.239  1.00 66.45           N  
ANISOU  160  N   ILE A 767     7780   8252   9215    632  -1497     18       N  
ATOM    161  CA  ILE A 767      20.449  32.772  54.009  1.00 64.49           C  
ANISOU  161  CA  ILE A 767     7279   8181   9041    448  -1322   -194       C  
ATOM    162  C   ILE A 767      19.775  33.518  55.166  1.00 69.50           C  
ANISOU  162  C   ILE A 767     8105   8888   9412    264  -1296   -144       C  
ATOM    163  O   ILE A 767      20.402  34.327  55.838  1.00 71.07           O  
ANISOU  163  O   ILE A 767     8173   9270   9561    190  -1375   -318       O  
ATOM    164  CB  ILE A 767      19.922  33.261  52.618  1.00 63.78           C  
ANISOU  164  CB  ILE A 767     7117   8010   9106    336   -976   -233       C  
ATOM    165  CG1 ILE A 767      20.506  32.456  51.460  1.00 63.08           C  
ANISOU  165  CG1 ILE A 767     6887   7848   9233    501   -970   -294       C  
ATOM    166  CG2 ILE A 767      20.155  34.754  52.442  1.00 65.33           C  
ANISOU  166  CG2 ILE A 767     7162   8308   9353    147   -747   -407       C  
ATOM    167  CD1 ILE A 767      20.159  32.974  50.060  1.00 66.00           C  
ANISOU  167  CD1 ILE A 767     7209   8176   9693    417   -653   -349       C  
ATOM    168  N   GLY A 768      18.506  33.211  55.398  1.00 66.91           N  
ANISOU  168  N   GLY A 768     8070   8426   8926    175  -1169     54       N  
ATOM    169  CA  GLY A 768      17.745  33.825  56.477  1.00 67.35           C  
ANISOU  169  CA  GLY A 768     8327   8535   8729     -3  -1090     97       C  
ATOM    170  C   GLY A 768      16.277  33.475  56.510  1.00 68.31           C  
ANISOU  170  C   GLY A 768     8689   8514   8752   -125   -875    262       C  
ATOM    171  O   GLY A 768      15.783  32.723  55.666  1.00 66.80           O  
ANISOU  171  O   GLY A 768     8510   8183   8689    -87   -799    338       O  
ATOM    172  N   ARG A 769      15.587  34.021  57.519  1.00 64.43           N  
ANISOU  172  N   ARG A 769     8369   8075   8035   -291   -766    274       N  
ATOM    173  CA  ARG A 769      14.173  33.808  57.769  1.00 63.45           C  
ANISOU  173  CA  ARG A 769     8433   7861   7812   -449   -525    372       C  
ATOM    174  C   ARG A 769      13.432  35.139  57.749  1.00 64.12           C  
ANISOU  174  C   ARG A 769     8401   8033   7928   -590   -260    229       C  
ATOM    175  O   ARG A 769      13.995  36.174  58.104  1.00 63.31           O  
ANISOU  175  O   ARG A 769     8222   8036   7799   -620   -266     88       O  
ATOM    176  CB  ARG A 769      13.958  33.114  59.120  1.00 66.29           C  
ANISOU  176  CB  ARG A 769     9173   8176   7837   -510   -589    529       C  
ATOM    177  CG  ARG A 769      14.393  31.665  59.150  1.00 78.53           C  
ANISOU  177  CG  ARG A 769    10947   9547   9344   -349   -793    727       C  
ATOM    178  CD  ARG A 769      14.222  31.066  60.540  1.00 87.22           C  
ANISOU  178  CD  ARG A 769    12519  10577  10044   -389   -841    920       C  
ATOM    179  NE  ARG A 769      14.623  29.657  60.585  1.00102.76           N  
ANISOU  179  NE  ARG A 769    14782  12301  11962   -196  -1020   1147       N  
ATOM    180  CZ  ARG A 769      15.849  29.231  60.884  1.00122.12           C  
ANISOU  180  CZ  ARG A 769    17295  14778  14325    121  -1416   1215       C  
ATOM    181  NH1 ARG A 769      16.818  30.103  61.150  1.00110.04           N  
ANISOU  181  NH1 ARG A 769    15501  13547  12762    237  -1678   1034       N  
ATOM    182  NH2 ARG A 769      16.119  27.932  60.906  1.00107.83           N  
ANISOU  182  NH2 ARG A 769    15797  12692  12483    332  -1550   1437       N  
ATOM    183  N   SER A 770      12.159  35.104  57.348  1.00 58.56           N  
ANISOU  183  N   SER A 770     7674   7281   7296   -670    -24    238       N  
ATOM    184  CA  SER A 770      11.322  36.289  57.292  1.00 57.78           C  
ANISOU  184  CA  SER A 770     7463   7246   7246   -736    223    109       C  
ATOM    185  C   SER A 770       9.845  35.930  57.512  1.00 62.12           C  
ANISOU  185  C   SER A 770     8042   7788   7774   -866    449    109       C  
ATOM    186  O   SER A 770       9.510  34.762  57.777  1.00 61.58           O  
ANISOU  186  O   SER A 770     8119   7641   7636   -960    446    211       O  
ATOM    187  CB  SER A 770      11.514  37.010  55.958  1.00 58.31           C  
ANISOU  187  CB  SER A 770     7301   7307   7548   -586    257     38       C  
ATOM    188  OG  SER A 770      10.990  36.235  54.891  1.00 64.07           O  
ANISOU  188  OG  SER A 770     7933   8003   8408   -502    240     86       O  
ATOM    189  N   CYS A 771       8.968  36.946  57.352  1.00 58.84           N  
ANISOU  189  N   CYS A 771     7476   7438   7445   -863    664    -25       N  
ATOM    190  CA  CYS A 771       7.520  36.837  57.478  1.00 60.69           C  
ANISOU  190  CA  CYS A 771     7617   7722   7720   -964    899   -110       C  
ATOM    191  C   CYS A 771       6.978  35.925  56.395  1.00 67.02           C  
ANISOU  191  C   CYS A 771     8247   8521   8698   -918    846   -105       C  
ATOM    192  O   CYS A 771       5.980  35.262  56.638  1.00 70.85           O  
ANISOU  192  O   CYS A 771     8693   9026   9201  -1088   1003   -167       O  
ATOM    193  CB  CYS A 771       6.867  38.213  57.424  1.00 61.63           C  
ANISOU  193  CB  CYS A 771     7578   7910   7929   -873   1088   -270       C  
ATOM    194  SG  CYS A 771       7.269  39.159  55.933  1.00 64.46           S  
ANISOU  194  SG  CYS A 771     7761   8237   8492   -551    985   -275       S  
ATOM    195  N   HIS A 772       7.584  35.980  55.217  1.00 60.41           N  
ANISOU  195  N   HIS A 772     7312   7660   7980   -721    651    -62       N  
ATOM    196  CA  HIS A 772       7.250  35.118  54.093  1.00 59.21           C  
ANISOU  196  CA  HIS A 772     7008   7521   7970   -664    569    -89       C  
ATOM    197  C   HIS A 772       7.635  33.651  54.280  1.00 60.21           C  
ANISOU  197  C   HIS A 772     7306   7504   8067   -802    490      7       C  
ATOM    198  O   HIS A 772       6.913  32.758  53.865  1.00 59.63           O  
ANISOU  198  O   HIS A 772     7142   7421   8094   -895    533    -72       O  
ATOM    199  CB  HIS A 772       7.840  35.675  52.806  1.00 58.43           C  
ANISOU  199  CB  HIS A 772     6798   7443   7958   -403    431    -83       C  
ATOM    200  CG  HIS A 772       7.235  36.976  52.393  1.00 61.68           C  
ANISOU  200  CG  HIS A 772     7080   7948   8409   -224    524   -161       C  
ATOM    201  ND1 HIS A 772       7.868  38.181  52.582  1.00 62.69           N  
ANISOU  201  ND1 HIS A 772     7306   8005   8507   -126    574   -123       N  
ATOM    202  CD2 HIS A 772       6.046  37.262  51.818  1.00 64.43           C  
ANISOU  202  CD2 HIS A 772     7211   8438   8829   -118    579   -290       C  
ATOM    203  CE1 HIS A 772       7.100  39.154  52.131  1.00 63.12           C  
ANISOU  203  CE1 HIS A 772     7263   8112   8609     62    669   -188       C  
ATOM    204  NE2 HIS A 772       5.988  38.623  51.663  1.00 64.41           N  
ANISOU  204  NE2 HIS A 772     7215   8427   8829    101    649   -291       N  
ATOM    205  N   GLY A 773       8.790  33.416  54.892  1.00 54.08           N  
ANISOU  205  N   GLY A 773     6771   6615   7162   -798    370    154       N  
ATOM    206  CA  GLY A 773       9.294  32.070  55.090  1.00 53.77           C  
ANISOU  206  CA  GLY A 773     6963   6392   7073   -842    263    288       C  
ATOM    207  C   GLY A 773      10.796  32.071  55.288  1.00 58.25           C  
ANISOU  207  C   GLY A 773     7637   6919   7576   -666     17    394       C  
ATOM    208  O   GLY A 773      11.312  32.845  56.078  1.00 58.16           O  
ANISOU  208  O   GLY A 773     7685   6990   7422   -659    -23    401       O  
ATOM    209  N   THR A 774      11.490  31.163  54.609  1.00 55.49           N  
ANISOU  209  N   THR A 774     7272   6464   7349   -522   -147    428       N  
ATOM    210  CA  THR A 774      12.942  31.070  54.700  1.00 56.47           C  
ANISOU  210  CA  THR A 774     7435   6559   7463   -329   -395    488       C  
ATOM    211  C   THR A 774      13.676  30.958  53.345  1.00 61.11           C  
ANISOU  211  C   THR A 774     7792   7155   8272   -153   -479    394       C  
ATOM    212  O   THR A 774      13.220  30.275  52.439  1.00 61.82           O  
ANISOU  212  O   THR A 774     7840   7167   8483   -158   -419    352       O  
ATOM    213  CB  THR A 774      13.348  29.903  55.618  1.00 69.04           C  
ANISOU  213  CB  THR A 774     9379   7950   8903   -304   -516    673       C  
ATOM    214  OG1 THR A 774      14.735  29.611  55.447  1.00 71.74           O  
ANISOU  214  OG1 THR A 774     9712   8302   9244    -54   -810    706       O  
ATOM    215  CG2 THR A 774      12.542  28.673  55.291  1.00 71.01           C  
ANISOU  215  CG2 THR A 774     9773   7954   9255   -377   -408    720       C  
ATOM    216  N   SER A 775      14.817  31.636  53.238  1.00 56.04           N  
ANISOU  216  N   SER A 775     6999   6620   7675    -29   -591    327       N  
ATOM    217  CA  SER A 775      15.687  31.656  52.063  1.00 55.28           C  
ANISOU  217  CA  SER A 775     6694   6541   7767    118   -627    220       C  
ATOM    218  C   SER A 775      16.927  30.771  52.250  1.00 60.24           C  
ANISOU  218  C   SER A 775     7317   7103   8468    308   -862    229       C  
ATOM    219  O   SER A 775      17.570  30.817  53.305  1.00 60.55           O  
ANISOU  219  O   SER A 775     7407   7195   8403    364  -1046    263       O  
ATOM    220  CB  SER A 775      16.163  33.071  51.764  1.00 56.24           C  
ANISOU  220  CB  SER A 775     6631   6808   7928     95   -523     98       C  
ATOM    221  OG  SER A 775      15.131  33.765  51.087  1.00 70.19           O  
ANISOU  221  OG  SER A 775     8386   8600   9683     35   -317     85       O  
ATOM    222  N   TYR A 776      17.285  30.023  51.190  1.00 56.55           N  
ANISOU  222  N   TYR A 776     6770   6542   8174    432   -866    170       N  
ATOM    223  CA  TYR A 776      18.479  29.179  51.128  1.00 58.82           C  
ANISOU  223  CA  TYR A 776     6996   6759   8594    667  -1064    134       C  
ATOM    224  C   TYR A 776      19.269  29.476  49.874  1.00 63.86           C  
ANISOU  224  C   TYR A 776     7349   7477   9436    743   -966    -66       C  
ATOM    225  O   TYR A 776      18.713  29.920  48.866  1.00 62.90           O  
ANISOU  225  O   TYR A 776     7189   7387   9324    639   -751   -125       O  
ATOM    226  CB  TYR A 776      18.142  27.679  51.143  1.00 61.69           C  
ANISOU  226  CB  TYR A 776     7617   6843   8980    759  -1125    253       C  
ATOM    227  CG  TYR A 776      17.532  27.171  52.428  1.00 65.96           C  
ANISOU  227  CG  TYR A 776     8516   7240   9307    699  -1194    474       C  
ATOM    228  CD1 TYR A 776      16.172  27.322  52.685  1.00 67.33           C  
ANISOU  228  CD1 TYR A 776     8854   7380   9349    424   -986    543       C  
ATOM    229  CD2 TYR A 776      18.293  26.464  53.350  1.00 70.65           C  
ANISOU  229  CD2 TYR A 776     9303   7720   9820    935  -1453    608       C  
ATOM    230  CE1 TYR A 776      15.600  26.848  53.860  1.00 71.25           C  
ANISOU  230  CE1 TYR A 776     9709   7729   9633    326   -975    735       C  
ATOM    231  CE2 TYR A 776      17.731  25.974  54.526  1.00 74.48           C  
ANISOU  231  CE2 TYR A 776    10209   8042  10047    880  -1483    844       C  
ATOM    232  CZ  TYR A 776      16.378  26.159  54.771  1.00 85.46           C  
ANISOU  232  CZ  TYR A 776    11775   9388  11308    546  -1210    906       C  
ATOM    233  OH  TYR A 776      15.795  25.674  55.919  1.00 94.27           O  
ANISOU  233  OH  TYR A 776    13332  10329  12156    446  -1162   1127       O  
ATOM    234  N   LYS A 777      20.581  29.281  49.966  1.00 62.25           N  
ANISOU  234  N   LYS A 777     6944   7330   9377    933  -1123   -184       N  
ATOM    235  CA  LYS A 777      21.515  29.373  48.863  1.00 62.41           C  
ANISOU  235  CA  LYS A 777     6680   7413   9619   1015  -1012   -406       C  
ATOM    236  C   LYS A 777      21.802  27.906  48.461  1.00 69.51           C  
ANISOU  236  C   LYS A 777     7645   8106  10659   1256  -1119   -410       C  
ATOM    237  O   LYS A 777      22.225  27.103  49.295  1.00 70.63           O  
ANISOU  237  O   LYS A 777     7869   8151  10816   1475  -1386   -327       O  
ATOM    238  CB  LYS A 777      22.809  30.084  49.299  1.00 65.12           C  
ANISOU  238  CB  LYS A 777     6687   7974  10080   1059  -1104   -604       C  
ATOM    239  CG  LYS A 777      23.839  30.197  48.189  1.00 67.36           C  
ANISOU  239  CG  LYS A 777     6645   8331  10618   1105   -926   -875       C  
ATOM    240  CD  LYS A 777      25.218  30.232  48.762  1.00 71.35           C  
ANISOU  240  CD  LYS A 777     6772   9023  11313   1257  -1136  -1105       C  
ATOM    241  CE  LYS A 777      26.264  30.374  47.694  1.00 75.70           C  
ANISOU  241  CE  LYS A 777     6952   9663  12146   1264   -900  -1423       C  
ATOM    242  NZ  LYS A 777      27.584  30.766  48.274  1.00 78.00           N  
ANISOU  242  NZ  LYS A 777     6769  10219  12647   1318  -1052  -1734       N  
ATOM    243  N   ALA A 778      21.497  27.563  47.212  1.00 67.20           N  
ANISOU  243  N   ALA A 778     7367   7729  10436   1224   -912   -496       N  
ATOM    244  CA  ALA A 778      21.728  26.241  46.622  1.00 69.19           C  
ANISOU  244  CA  ALA A 778     7683   7764  10843   1416   -938   -559       C  
ATOM    245  C   ALA A 778      22.770  26.380  45.513  1.00 74.69           C  
ANISOU  245  C   ALA A 778     8073   8564  11741   1506   -777   -837       C  
ATOM    246  O   ALA A 778      22.678  27.283  44.679  1.00 73.34           O  
ANISOU  246  O   ALA A 778     7812   8544  11509   1330   -525   -934       O  
ATOM    247  CB  ALA A 778      20.430  25.666  46.063  1.00 68.18           C  
ANISOU  247  CB  ALA A 778     7830   7466  10610   1261   -807   -492       C  
ATOM    248  N   THR A 779      23.767  25.513  45.526  1.00 74.65           N  
ANISOU  248  N   THR A 779     7927   8470  11965   1794   -905   -961       N  
ATOM    249  CA  THR A 779      24.843  25.534  44.537  1.00 77.00           C  
ANISOU  249  CA  THR A 779     7896   8867  12494   1894   -729  -1269       C  
ATOM    250  C   THR A 779      24.761  24.291  43.644  1.00 82.50           C  
ANISOU  250  C   THR A 779     8726   9313  13308   2041   -640  -1373       C  
ATOM    251  O   THR A 779      24.937  23.170  44.125  1.00 83.54           O  
ANISOU  251  O   THR A 779     8978   9199  13563   2309   -848  -1316       O  
ATOM    252  CB  THR A 779      26.222  25.700  45.229  1.00 89.47           C  
ANISOU  252  CB  THR A 779     9075  10622  14299   2121   -932  -1434       C  
ATOM    253  OG1 THR A 779      26.166  26.763  46.186  1.00 84.20           O  
ANISOU  253  OG1 THR A 779     8341  10161  13491   1959  -1045  -1344       O  
ATOM    254  CG2 THR A 779      27.360  25.954  44.233  1.00 92.30           C  
ANISOU  254  CG2 THR A 779     9011  11141  14918   2146   -672  -1809       C  
ATOM    255  N   LEU A 780      24.489  24.506  42.342  1.00 79.61           N  
ANISOU  255  N   LEU A 780     8378   8994  12877   1872   -322  -1526       N  
ATOM    256  CA  LEU A 780      24.392  23.466  41.305  1.00 81.18           C  
ANISOU  256  CA  LEU A 780     8694   9001  13151   1952   -178  -1698       C  
ATOM    257  C   LEU A 780      25.773  22.901  40.999  1.00 87.98           C  
ANISOU  257  C   LEU A 780     9245   9839  14346   2247   -141  -1981       C  
ATOM    258  O   LEU A 780      26.779  23.572  41.251  1.00 88.82           O  
ANISOU  258  O   LEU A 780     8983  10168  14598   2304   -135  -2106       O  
ATOM    259  CB  LEU A 780      23.765  24.048  40.015  1.00 79.68           C  
ANISOU  259  CB  LEU A 780     8606   8948  12719   1695    131  -1794       C  
ATOM    260  CG  LEU A 780      22.274  23.758  39.700  1.00 82.21           C  
ANISOU  260  CG  LEU A 780     9266   9187  12785   1511    115  -1681       C  
ATOM    261  CD1 LEU A 780      21.420  23.597  40.953  1.00 80.47           C  
ANISOU  261  CD1 LEU A 780     9216   8847  12514   1454   -136  -1403       C  
ATOM    262  CD2 LEU A 780      21.697  24.820  38.788  1.00 81.28           C  
ANISOU  262  CD2 LEU A 780     9210   9315  12357   1306    315  -1689       C  
ATOM    263  N   ASP A 781      25.813  21.679  40.437  1.00 85.93           N  
ANISOU  263  N   ASP A 781     9109   9312  14228   2421    -96  -2122       N  
ATOM    264  CA  ASP A 781      27.036  20.951  40.080  1.00 89.65           C  
ANISOU  264  CA  ASP A 781     9308   9708  15049   2754    -48  -2420       C  
ATOM    265  C   ASP A 781      28.025  21.775  39.240  1.00 92.66           C  
ANISOU  265  C   ASP A 781     9275  10406  15525   2676    271  -2741       C  
ATOM    266  O   ASP A 781      29.227  21.708  39.491  1.00 94.67           O  
ANISOU  266  O   ASP A 781     9115  10759  16094   2928    222  -2954       O  
ATOM    267  CB  ASP A 781      26.682  19.630  39.378  1.00 93.52           C  
ANISOU  267  CB  ASP A 781    10077   9841  15618   2859     52  -2549       C  
ATOM    268  N   ASN A 782      27.508  22.581  38.286  1.00 86.14           N  
ANISOU  268  N   ASN A 782     8568   9745  14416   2331    595  -2773       N  
ATOM    269  CA  ASN A 782      28.281  23.430  37.370  1.00 86.54           C  
ANISOU  269  CA  ASN A 782     8361  10050  14471   2175   1000  -3039       C  
ATOM    270  C   ASN A 782      28.754  24.784  37.951  1.00 88.28           C  
ANISOU  270  C   ASN A 782     8314  10538  14692   1997   1038  -2986       C  
ATOM    271  O   ASN A 782      29.413  25.549  37.245  1.00 88.86           O  
ANISOU  271  O   ASN A 782     8195  10789  14779   1819   1429  -3204       O  
ATOM    272  CB  ASN A 782      27.488  23.662  36.077  1.00 86.94           C  
ANISOU  272  CB  ASN A 782     8756  10127  14150   1921   1322  -3064       C  
ATOM    273  CG  ASN A 782      26.256  24.526  36.255  1.00104.54           C  
ANISOU  273  CG  ASN A 782    11304  12433  15983   1667   1238  -2730       C  
ATOM    274  OD1 ASN A 782      25.290  24.149  36.922  1.00 98.42           O  
ANISOU  274  OD1 ASN A 782    10742  11531  15121   1676    933  -2495       O  
ATOM    275  ND2 ASN A 782      26.269  25.710  35.661  1.00 94.30           N  
ANISOU  275  ND2 ASN A 782    10058  11329  14444   1443   1534  -2711       N  
ATOM    276  N   GLY A 783      28.411  25.066  39.205  1.00 82.76           N  
ANISOU  276  N   GLY A 783     7633   9847  13966   2018    675  -2719       N  
ATOM    277  CA  GLY A 783      28.783  26.312  39.870  1.00 82.05           C  
ANISOU  277  CA  GLY A 783     7314   9987  13874   1837    679  -2687       C  
ATOM    278  C   GLY A 783      27.666  27.342  39.957  1.00 82.71           C  
ANISOU  278  C   GLY A 783     7744  10099  13582   1528    741  -2386       C  
ATOM    279  O   GLY A 783      27.814  28.355  40.655  1.00 81.96           O  
ANISOU  279  O   GLY A 783     7529  10141  13469   1373    715  -2327       O  
ATOM    280  N   TYR A 784      26.535  27.099  39.256  1.00 76.59           N  
ANISOU  280  N   TYR A 784     7382   9205  12514   1449    812  -2226       N  
ATOM    281  CA  TYR A 784      25.396  28.018  39.253  1.00 72.67           C  
ANISOU  281  CA  TYR A 784     7203   8744  11666   1223    848  -1958       C  
ATOM    282  C   TYR A 784      24.765  28.111  40.650  1.00 72.56           C  
ANISOU  282  C   TYR A 784     7251   8697  11620   1234    480  -1694       C  
ATOM    283  O   TYR A 784      24.502  27.084  41.275  1.00 72.18           O  
ANISOU  283  O   TYR A 784     7269   8503  11653   1404    189  -1613       O  
ATOM    284  CB  TYR A 784      24.363  27.630  38.182  1.00 73.08           C  
ANISOU  284  CB  TYR A 784     7611   8731  11426   1184    945  -1911       C  
ATOM    285  CG  TYR A 784      23.577  28.824  37.681  1.00 73.06           C  
ANISOU  285  CG  TYR A 784     7867   8832  11062    993   1123  -1743       C  
ATOM    286  CD1 TYR A 784      22.416  29.247  38.334  1.00 70.42           C  
ANISOU  286  CD1 TYR A 784     7714   8501  10540    935    907  -1475       C  
ATOM    287  CD2 TYR A 784      24.018  29.564  36.588  1.00 76.71           C  
ANISOU  287  CD2 TYR A 784     8406   9374  11366    889   1528  -1848       C  
ATOM    288  CE1 TYR A 784      21.719  30.376  37.907  1.00 69.96           C  
ANISOU  288  CE1 TYR A 784     7886   8525  10172    830   1049  -1319       C  
ATOM    289  CE2 TYR A 784      23.317  30.679  36.140  1.00 76.57           C  
ANISOU  289  CE2 TYR A 784     8691   9409  10994    774   1683  -1655       C  
ATOM    290  CZ  TYR A 784      22.163  31.075  36.795  1.00 80.00           C  
ANISOU  290  CZ  TYR A 784     9282   9847  11269    771   1421  -1392       C  
ATOM    291  OH  TYR A 784      21.494  32.181  36.344  1.00 81.89           O  
ANISOU  291  OH  TYR A 784     9816  10123  11174    724   1560  -1206       O  
ATOM    292  N   MET A 785      24.614  29.334  41.171  1.00 66.30           N  
ANISOU  292  N   MET A 785     6454   8016  10719   1054    525  -1577       N  
ATOM    293  CA  MET A 785      24.062  29.531  42.511  1.00 64.40           C  
ANISOU  293  CA  MET A 785     6275   7769  10423   1041    221  -1358       C  
ATOM    294  C   MET A 785      22.659  30.094  42.449  1.00 64.13           C  
ANISOU  294  C   MET A 785     6566   7715  10086    894    248  -1119       C  
ATOM    295  O   MET A 785      22.380  31.045  41.693  1.00 62.99           O  
ANISOU  295  O   MET A 785     6537   7625   9772    763    515  -1102       O  
ATOM    296  CB  MET A 785      24.990  30.376  43.393  1.00 68.38           C  
ANISOU  296  CB  MET A 785     6481   8424  11076    976    185  -1458       C  
ATOM    297  CG  MET A 785      26.393  29.810  43.505  1.00 76.79           C  
ANISOU  297  CG  MET A 785     7136   9569  12472   1162    106  -1744       C  
ATOM    298  SD  MET A 785      27.512  30.838  44.490  1.00 84.31           S  
ANISOU  298  SD  MET A 785     7652  10771  13610   1050     48  -1963       S  
ATOM    299  CE  MET A 785      27.829  32.202  43.347  1.00 81.67           C  
ANISOU  299  CE  MET A 785     7281  10484  13267    676    668  -2142       C  
ATOM    300  N   LEU A 786      21.759  29.483  43.224  1.00 57.52           N  
ANISOU  300  N   LEU A 786     5893   6788   9176    932    -12   -939       N  
ATOM    301  CA  LEU A 786      20.351  29.871  43.233  1.00 53.99           C  
ANISOU  301  CA  LEU A 786     5688   6343   8484    813    -12   -759       C  
ATOM    302  C   LEU A 786      19.864  30.280  44.609  1.00 55.84           C  
ANISOU  302  C   LEU A 786     5969   6588   8661    740   -181   -586       C  
ATOM    303  O   LEU A 786      20.405  29.828  45.619  1.00 55.33           O  
ANISOU  303  O   LEU A 786     5836   6486   8702    816   -382   -564       O  
ATOM    304  CB  LEU A 786      19.490  28.680  42.736  1.00 54.14           C  
ANISOU  304  CB  LEU A 786     5870   6245   8457    854    -91   -762       C  
ATOM    305  CG  LEU A 786      19.846  28.032  41.384  1.00 59.90           C  
ANISOU  305  CG  LEU A 786     6596   6947   9215    929     53   -966       C  
ATOM    306  CD1 LEU A 786      19.337  26.609  41.320  1.00 60.11           C  
ANISOU  306  CD1 LEU A 786     6740   6790   9311    974    -71  -1017       C  
ATOM    307  CD2 LEU A 786      19.261  28.815  40.242  1.00 62.95           C  
ANISOU  307  CD2 LEU A 786     7099   7477   9340    860    242   -985       C  
ATOM    308  N   THR A 787      18.819  31.117  44.653  1.00 53.27           N  
ANISOU  308  N   THR A 787     5774   6318   8147    623   -109   -468       N  
ATOM    309  CA  THR A 787      18.133  31.483  45.893  1.00 53.20           C  
ANISOU  309  CA  THR A 787     5839   6318   8055    535   -223   -323       C  
ATOM    310  C   THR A 787      16.875  30.614  45.901  1.00 58.51           C  
ANISOU  310  C   THR A 787     6662   6921   8650    506   -302   -251       C  
ATOM    311  O   THR A 787      16.129  30.607  44.916  1.00 59.35           O  
ANISOU  311  O   THR A 787     6806   7071   8672    503   -222   -297       O  
ATOM    312  CB  THR A 787      17.790  32.973  45.981  1.00 65.04           C  
ANISOU  312  CB  THR A 787     7366   7905   9441    434    -60   -279       C  
ATOM    313  OG1 THR A 787      18.942  33.761  45.684  1.00 67.40           O  
ANISOU  313  OG1 THR A 787     7539   8237   9832    407    103   -395       O  
ATOM    314  CG2 THR A 787      17.293  33.351  47.365  1.00 67.42           C  
ANISOU  314  CG2 THR A 787     7719   8222   9677    340   -158   -179       C  
ATOM    315  N   VAL A 788      16.681  29.844  46.981  1.00 55.30           N  
ANISOU  315  N   VAL A 788     6346   6404   8260    483   -454   -159       N  
ATOM    316  CA  VAL A 788      15.555  28.914  47.172  1.00 55.92           C  
ANISOU  316  CA  VAL A 788     6578   6368   8301    392   -479   -112       C  
ATOM    317  C   VAL A 788      14.741  29.439  48.365  1.00 59.40           C  
ANISOU  317  C   VAL A 788     7106   6848   8614    246   -472     14       C  
ATOM    318  O   VAL A 788      15.167  29.311  49.528  1.00 59.51           O  
ANISOU  318  O   VAL A 788     7221   6800   8588    250   -572    124       O  
ATOM    319  CB  VAL A 788      16.102  27.467  47.363  1.00 61.94           C  
ANISOU  319  CB  VAL A 788     7456   6889   9191    490   -589   -104       C  
ATOM    320  CG1 VAL A 788      15.027  26.502  47.831  1.00 62.22           C  
ANISOU  320  CG1 VAL A 788     7710   6735   9197    338   -564    -41       C  
ATOM    321  CG2 VAL A 788      16.770  26.965  46.080  1.00 62.39           C  
ANISOU  321  CG2 VAL A 788     7412   6914   9381    623   -548   -280       C  
ATOM    322  N   LYS A 789      13.629  30.142  48.038  1.00 53.13           N  
ANISOU  322  N   LYS A 789     6261   6189   7737    150   -359    -20       N  
ATOM    323  CA  LYS A 789      12.725  30.792  48.982  1.00 51.87           C  
ANISOU  323  CA  LYS A 789     6134   6101   7474     17   -295     43       C  
ATOM    324  C   LYS A 789      11.484  29.931  49.202  1.00 59.07           C  
ANISOU  324  C   LYS A 789     7102   6954   8386   -155   -237     11       C  
ATOM    325  O   LYS A 789      10.669  29.778  48.294  1.00 58.27           O  
ANISOU  325  O   LYS A 789     6881   6943   8317   -176   -201   -127       O  
ATOM    326  CB  LYS A 789      12.321  32.181  48.451  1.00 52.33           C  
ANISOU  326  CB  LYS A 789     6075   6334   7474     70   -195      2       C  
ATOM    327  CG  LYS A 789      11.754  33.095  49.514  1.00 54.25           C  
ANISOU  327  CG  LYS A 789     6341   6635   7636    -21   -114     49       C  
ATOM    328  CD  LYS A 789      11.255  34.423  48.952  1.00 49.11           C  
ANISOU  328  CD  LYS A 789     5614   6100   6944     80     -5     16       C  
ATOM    329  CE  LYS A 789      10.848  35.363  50.078  1.00 51.11           C  
ANISOU  329  CE  LYS A 789     5901   6376   7143     -1    100     36       C  
ATOM    330  NZ  LYS A 789      12.015  35.928  50.804  1.00 51.97           N  
ANISOU  330  NZ  LYS A 789     6083   6426   7237    -46    104     65       N  
ATOM    331  N   TRP A 790      11.345  29.378  50.421  1.00 57.61           N  
ANISOU  331  N   TRP A 790     7110   6628   8150   -288   -219    122       N  
ATOM    332  CA  TRP A 790      10.223  28.539  50.826  1.00 58.44           C  
ANISOU  332  CA  TRP A 790     7314   6630   8260   -521    -86     93       C  
ATOM    333  C   TRP A 790       9.161  29.410  51.461  1.00 61.10           C  
ANISOU  333  C   TRP A 790     7560   7137   8516   -669     66     54       C  
ATOM    334  O   TRP A 790       9.425  30.103  52.442  1.00 60.09           O  
ANISOU  334  O   TRP A 790     7528   7043   8262   -672     81    161       O  
ATOM    335  CB  TRP A 790      10.676  27.512  51.877  1.00 59.57           C  
ANISOU  335  CB  TRP A 790     7807   6485   8342   -577   -100    273       C  
ATOM    336  CG  TRP A 790      11.656  26.481  51.416  1.00 61.37           C  
ANISOU  336  CG  TRP A 790     8160   6486   8673   -405   -238    313       C  
ATOM    337  CD1 TRP A 790      12.971  26.675  51.102  1.00 63.57           C  
ANISOU  337  CD1 TRP A 790     8366   6793   8996   -132   -433    340       C  
ATOM    338  CD2 TRP A 790      11.445  25.064  51.411  1.00 64.05           C  
ANISOU  338  CD2 TRP A 790     8750   6494   9091   -495   -164    332       C  
ATOM    339  NE1 TRP A 790      13.573  25.469  50.819  1.00 65.00           N  
ANISOU  339  NE1 TRP A 790     8700   6706   9290     -5   -506    361       N  
ATOM    340  CE2 TRP A 790      12.666  24.459  51.031  1.00 68.67           C  
ANISOU  340  CE2 TRP A 790     9404   6917   9770   -217   -344    376       C  
ATOM    341  CE3 TRP A 790      10.330  24.242  51.672  1.00 67.55           C  
ANISOU  341  CE3 TRP A 790     9362   6745   9559   -804     74    287       C  
ATOM    342  CZ2 TRP A 790      12.798  23.071  50.888  1.00 70.72           C  
ANISOU  342  CZ2 TRP A 790     9929   6799  10142   -199   -308    397       C  
ATOM    343  CZ3 TRP A 790      10.470  22.866  51.560  1.00 71.92           C  
ANISOU  343  CZ3 TRP A 790    10204   6905  10216   -837    136    311       C  
ATOM    344  CH2 TRP A 790      11.688  22.293  51.169  1.00 73.19           C  
ANISOU  344  CH2 TRP A 790    10465   6881  10464   -518    -60    377       C  
ATOM    345  N   LEU A 791       7.954  29.359  50.933  1.00 58.00           N  
ANISOU  345  N   LEU A 791     6965   6871   8203   -790    175   -135       N  
ATOM    346  CA  LEU A 791       6.871  30.124  51.518  1.00 57.34           C  
ANISOU  346  CA  LEU A 791     6743   6959   8084   -911    336   -217       C  
ATOM    347  C   LEU A 791       6.265  29.330  52.668  1.00 61.65           C  
ANISOU  347  C   LEU A 791     7492   7341   8590  -1231    558   -188       C  
ATOM    348  O   LEU A 791       6.156  28.101  52.575  1.00 62.64           O  
ANISOU  348  O   LEU A 791     7760   7257   8784  -1396    620   -205       O  
ATOM    349  CB  LEU A 791       5.821  30.476  50.454  1.00 57.81           C  
ANISOU  349  CB  LEU A 791     6440   7277   8249   -855    327   -467       C  
ATOM    350  CG  LEU A 791       6.370  31.113  49.150  1.00 61.65           C  
ANISOU  350  CG  LEU A 791     6811   7895   8721   -533    128   -479       C  
ATOM    351  CD1 LEU A 791       5.269  31.266  48.119  1.00 63.66           C  
ANISOU  351  CD1 LEU A 791     6748   8416   9022   -452     66   -727       C  
ATOM    352  CD2 LEU A 791       7.076  32.455  49.414  1.00 59.94           C  
ANISOU  352  CD2 LEU A 791     6664   7702   8408   -330    111   -321       C  
ATOM    353  N   LYS A 792       5.932  30.014  53.784  1.00 67.66           N  
ANISOU  353  N   LYS A 792     7878   9087   8743  -2198   -101   1031       N  
ATOM    354  CA  LYS A 792       5.275  29.375  54.936  1.00 68.70           C  
ANISOU  354  CA  LYS A 792     8174   9131   8798  -2478    -15   1092       C  
ATOM    355  C   LYS A 792       3.993  28.688  54.425  1.00 70.55           C  
ANISOU  355  C   LYS A 792     8300   9246   9261  -2362    163    824       C  
ATOM    356  O   LYS A 792       3.383  29.176  53.460  1.00 66.68           O  
ANISOU  356  O   LYS A 792     7672   8776   8886  -2165    247    566       O  
ATOM    357  CB  LYS A 792       4.903  30.416  56.010  1.00 70.90           C  
ANISOU  357  CB  LYS A 792     8705   9477   8758  -2805    128   1052       C  
ATOM    358  CG  LYS A 792       6.062  30.892  56.862  1.00 78.76           C  
ANISOU  358  CG  LYS A 792     9879  10577   9470  -3045    -49   1358       C  
ATOM    359  CD  LYS A 792       5.546  31.782  57.961  1.00 84.57           C  
ANISOU  359  CD  LYS A 792    10908  11343   9882  -3432    159   1288       C  
ATOM    360  CE  LYS A 792       6.621  32.577  58.639  1.00 83.56           C  
ANISOU  360  CE  LYS A 792    10963  11359   9429  -3675     16   1529       C  
ATOM    361  NZ  LYS A 792       6.054  33.783  59.304  1.00 92.56           N  
ANISOU  361  NZ  LYS A 792    12339  12544  10287  -3977    315   1352       N  
ATOM    362  N   GLU A 793       3.630  27.540  55.025  1.00 69.10           N  
ANISOU  362  N   GLU A 793     8171   8933   9150  -2483    196    900       N  
ATOM    363  CA  GLU A 793       2.428  26.763  54.683  1.00 68.72           C  
ANISOU  363  CA  GLU A 793     8036   8760   9314  -2406    371    662       C  
ATOM    364  C   GLU A 793       1.169  27.644  54.850  1.00 71.14           C  
ANISOU  364  C   GLU A 793     8393   9051   9586  -2499    609    359       C  
ATOM    365  O   GLU A 793       1.102  28.440  55.782  1.00 71.73           O  
ANISOU  365  O   GLU A 793     8668   9146   9439  -2756    707    377       O  
ATOM    366  CB  GLU A 793       2.347  25.513  55.578  1.00 72.42           C  
ANISOU  366  CB  GLU A 793     8617   9097   9804  -2582    382    824       C  
ATOM    367  CG  GLU A 793       1.251  24.532  55.190  1.00 83.70           C  
ANISOU  367  CG  GLU A 793     9941  10391  11470  -2484    555    600       C  
ATOM    368  CD  GLU A 793       1.068  23.322  56.086  1.00104.46           C  
ANISOU  368  CD  GLU A 793    12695  12879  14115  -2657    604    728       C  
ATOM    369  OE1 GLU A 793       2.082  22.765  56.568  1.00 93.45           O  
ANISOU  369  OE1 GLU A 793    11351  11474  12682  -2731    422   1067       O  
ATOM    370  OE2 GLU A 793      -0.097  22.902  56.269  1.00101.22           O  
ANISOU  370  OE2 GLU A 793    12315  12355  13789  -2711    822    492       O  
ATOM    371  N   GLY A 794       0.227  27.524  53.917  1.00 67.10           N  
ANISOU  371  N   GLY A 794     7691   8489   9313  -2304    701     97       N  
ATOM    372  CA  GLY A 794      -0.988  28.330  53.865  1.00 66.25           C  
ANISOU  372  CA  GLY A 794     7544   8334   9294  -2340    906   -179       C  
ATOM    373  C   GLY A 794      -0.799  29.683  53.195  1.00 69.89           C  
ANISOU  373  C   GLY A 794     7916   8920   9718  -2218    863   -248       C  
ATOM    374  O   GLY A 794      -1.791  30.329  52.851  1.00 70.45           O  
ANISOU  374  O   GLY A 794     7873   8942   9954  -2181    994   -464       O  
ATOM    375  N   PHE A 795       0.463  30.133  52.982  1.00 64.21           N  
ANISOU  375  N   PHE A 795     7232   8348   8817  -2150    680    -63       N  
ATOM    376  CA  PHE A 795       0.720  31.438  52.344  1.00 63.04           C  
ANISOU  376  CA  PHE A 795     7019   8322   8611  -2029    646   -129       C  
ATOM    377  C   PHE A 795       0.512  31.442  50.824  1.00 68.44           C  
ANISOU  377  C   PHE A 795     7487   9024   9494  -1734    524   -267       C  
ATOM    378  O   PHE A 795      -0.061  32.403  50.320  1.00 69.17           O  
ANISOU  378  O   PHE A 795     7487   9140   9655  -1664    570   -418       O  
ATOM    379  CB  PHE A 795       2.097  32.020  52.711  1.00 63.34           C  
ANISOU  379  CB  PHE A 795     7186   8501   8378  -2085    519     93       C  
ATOM    380  CG  PHE A 795       2.153  32.692  54.072  1.00 64.59           C  
ANISOU  380  CG  PHE A 795     7581   8682   8277  -2421    668    171       C  
ATOM    381  CD1 PHE A 795       1.214  32.393  55.059  1.00 67.90           C  
ANISOU  381  CD1 PHE A 795     8137   8961   8700  -2689    893     95       C  
ATOM    382  CD2 PHE A 795       3.163  33.592  54.379  1.00 63.97           C  
ANISOU  382  CD2 PHE A 795     7616   8748   7940  -2500    601    313       C  
ATOM    383  CE1 PHE A 795       1.273  33.009  56.310  1.00 69.64           C  
ANISOU  383  CE1 PHE A 795     8628   9178   8654  -3058   1063    154       C  
ATOM    384  CE2 PHE A 795       3.227  34.190  55.638  1.00 66.92           C  
ANISOU  384  CE2 PHE A 795     8246   9142   8039  -2863    749    386       C  
ATOM    385  CZ  PHE A 795       2.286  33.901  56.590  1.00 67.02           C  
ANISOU  385  CZ  PHE A 795     8417   9006   8042  -3155    984    306       C  
ATOM    386  N   ALA A 796       0.933  30.375  50.111  1.00 64.34           N  
ANISOU  386  N   ALA A 796     6897   8475   9076  -1592    387   -213       N  
ATOM    387  CA  ALA A 796       0.764  30.239  48.665  1.00 63.39           C  
ANISOU  387  CA  ALA A 796     6629   8349   9106  -1377    280   -342       C  
ATOM    388  C   ALA A 796      -0.697  30.048  48.285  1.00 69.64           C  
ANISOU  388  C   ALA A 796     7293   9050  10116  -1371    354   -555       C  
ATOM    389  O   ALA A 796      -1.404  29.275  48.935  1.00 72.33           O  
ANISOU  389  O   ALA A 796     7637   9287  10559  -1481    478   -591       O  
ATOM    390  CB  ALA A 796       1.583  29.058  48.153  1.00 64.23           C  
ANISOU  390  CB  ALA A 796     6722   8402   9279  -1292    190   -230       C  
ATOM    391  N   LYS A 797      -1.151  30.744  47.221  1.00 65.20           N  
ANISOU  391  N   LYS A 797     6618   8517   9638  -1250    265   -689       N  
ATOM    392  CA  LYS A 797      -2.507  30.635  46.650  1.00 65.09           C  
ANISOU  392  CA  LYS A 797     6443   8416   9871  -1233    265   -866       C  
ATOM    393  C   LYS A 797      -2.648  29.208  46.059  1.00 71.27           C  
ANISOU  393  C   LYS A 797     7198   9127  10754  -1207    218   -898       C  
ATOM    394  O   LYS A 797      -1.652  28.469  45.981  1.00 70.73           O  
ANISOU  394  O   LYS A 797     7220   9069  10586  -1182    196   -785       O  
ATOM    395  CB  LYS A 797      -2.663  31.649  45.496  1.00 65.75           C  
ANISOU  395  CB  LYS A 797     6437   8560   9984  -1114    101   -936       C  
ATOM    396  CG  LYS A 797      -3.010  33.062  45.929  1.00 68.69           C  
ANISOU  396  CG  LYS A 797     6761   8960  10379  -1137    185   -956       C  
ATOM    397  CD  LYS A 797      -3.071  34.027  44.748  1.00 68.87           C  
ANISOU  397  CD  LYS A 797     6701   9040  10426  -1011     -3   -995       C  
ATOM    398  CE  LYS A 797      -3.541  35.400  45.183  1.00 79.83           C  
ANISOU  398  CE  LYS A 797     8000  10425  11908  -1033    120  -1015       C  
ATOM    399  NZ  LYS A 797      -3.354  36.436  44.129  1.00 83.49           N  
ANISOU  399  NZ  LYS A 797     8418  10963  12342   -905    -61  -1016       N  
ATOM    400  N   SER A 798      -3.865  28.835  45.613  1.00 68.74           N  
ANISOU  400  N   SER A 798     6740   8721  10658  -1220    213  -1046       N  
ATOM    401  CA  SER A 798      -4.143  27.537  44.991  1.00 68.98           C  
ANISOU  401  CA  SER A 798     6741   8684  10784  -1220    191  -1106       C  
ATOM    402  C   SER A 798      -3.332  27.423  43.696  1.00 73.28           C  
ANISOU  402  C   SER A 798     7346   9281  11214  -1143     27  -1084       C  
ATOM    403  O   SER A 798      -3.141  28.430  43.025  1.00 74.18           O  
ANISOU  403  O   SER A 798     7465   9465  11256  -1088   -120  -1091       O  
ATOM    404  CB  SER A 798      -5.633  27.424  44.701  1.00 74.38           C  
ANISOU  404  CB  SER A 798     7252   9277  11732  -1259    182  -1268       C  
ATOM    405  OG  SER A 798      -6.047  28.449  43.812  1.00 84.09           O  
ANISOU  405  OG  SER A 798     8377  10544  13028  -1211    -12  -1310       O  
ATOM    406  N   LYS A 799      -2.840  26.219  43.363  1.00 70.39           N  
ANISOU  406  N   LYS A 799     7040   8862  10842  -1156     81  -1062       N  
ATOM    407  CA  LYS A 799      -1.972  25.897  42.213  1.00 69.27           C  
ANISOU  407  CA  LYS A 799     6993   8710  10617  -1129     16  -1053       C  
ATOM    408  C   LYS A 799      -2.266  26.657  40.909  1.00 73.49           C  
ANISOU  408  C   LYS A 799     7545   9283  11097  -1129   -187  -1155       C  
ATOM    409  O   LYS A 799      -1.333  27.139  40.263  1.00 72.24           O  
ANISOU  409  O   LYS A 799     7503   9146  10798  -1089   -252  -1124       O  
ATOM    410  CB  LYS A 799      -1.975  24.397  41.944  1.00 71.88           C  
ANISOU  410  CB  LYS A 799     7335   8930  11045  -1191    156  -1082       C  
ATOM    411  CG  LYS A 799      -0.722  23.935  41.252  1.00 85.58           C  
ANISOU  411  CG  LYS A 799     9183  10599  12735  -1179    214  -1017       C  
ATOM    412  CD  LYS A 799      -0.978  22.693  40.420  1.00 96.83           C  
ANISOU  412  CD  LYS A 799    10633  11906  14252  -1281    337  -1121       C  
ATOM    413  CE  LYS A 799       0.063  22.497  39.340  1.00100.08           C  
ANISOU  413  CE  LYS A 799    11185  12219  14623  -1317    398  -1129       C  
ATOM    414  NZ  LYS A 799       1.438  22.474  39.892  1.00100.85           N  
ANISOU  414  NZ  LYS A 799    11293  12255  14771  -1225    499   -942       N  
ATOM    415  N   LYS A 800      -3.543  26.764  40.536  1.00 71.10           N  
ANISOU  415  N   LYS A 800     7129   8971  10915  -1184   -295  -1267       N  
ATOM    416  CA  LYS A 800      -3.990  27.444  39.317  1.00 71.27           C  
ANISOU  416  CA  LYS A 800     7156   9018  10905  -1220   -540  -1335       C  
ATOM    417  C   LYS A 800      -3.677  28.937  39.333  1.00 71.91           C  
ANISOU  417  C   LYS A 800     7237   9187  10900  -1127   -664  -1278       C  
ATOM    418  O   LYS A 800      -3.098  29.435  38.373  1.00 71.80           O  
ANISOU  418  O   LYS A 800     7356   9198  10726  -1124   -800  -1281       O  
ATOM    419  CB  LYS A 800      -5.483  27.177  39.052  1.00 75.23           C  
ANISOU  419  CB  LYS A 800     7490   9475  11618  -1309   -649  -1429       C  
ATOM    420  N   GLU A 801      -4.023  29.637  40.424  1.00 66.33           N  
ANISOU  420  N   GLU A 801     6405   8509  10290  -1070   -583  -1237       N  
ATOM    421  CA  GLU A 801      -3.782  31.076  40.571  1.00 64.86           C  
ANISOU  421  CA  GLU A 801     6201   8401  10042   -991   -643  -1188       C  
ATOM    422  C   GLU A 801      -2.292  31.347  40.727  1.00 64.67           C  
ANISOU  422  C   GLU A 801     6357   8447   9767   -920   -574  -1106       C  
ATOM    423  O   GLU A 801      -1.750  32.200  40.023  1.00 63.08           O  
ANISOU  423  O   GLU A 801     6240   8300   9427   -864   -693  -1101       O  
ATOM    424  CB  GLU A 801      -4.524  31.644  41.791  1.00 66.77           C  
ANISOU  424  CB  GLU A 801     6284   8619  10466   -996   -489  -1181       C  
ATOM    425  CG  GLU A 801      -6.028  31.761  41.669  1.00 83.52           C  
ANISOU  425  CG  GLU A 801     8175  10641  12920  -1046   -553  -1255       C  
ATOM    426  CD  GLU A 801      -6.612  32.321  42.955  1.00126.49           C  
ANISOU  426  CD  GLU A 801    13494  16011  18555  -1076   -312  -1265       C  
ATOM    427  OE1 GLU A 801      -6.911  31.522  43.873  1.00121.74           O  
ANISOU  427  OE1 GLU A 801    12900  15329  18028  -1152   -103  -1304       O  
ATOM    428  OE2 GLU A 801      -6.670  33.566  43.085  1.00134.91           O  
ANISOU  428  OE2 GLU A 801    14492  17095  19673  -1041   -297  -1234       O  
ATOM    429  N   PHE A 802      -1.627  30.613  41.636  1.00 59.91           N  
ANISOU  429  N   PHE A 802     5811   7830   9121   -929   -393  -1032       N  
ATOM    430  CA  PHE A 802      -0.190  30.770  41.857  1.00 58.79           C  
ANISOU  430  CA  PHE A 802     5807   7732   8797   -872   -341   -925       C  
ATOM    431  C   PHE A 802       0.595  30.667  40.541  1.00 64.01           C  
ANISOU  431  C   PHE A 802     6601   8359   9359   -842   -435   -965       C  
ATOM    432  O   PHE A 802       1.333  31.599  40.235  1.00 64.24           O  
ANISOU  432  O   PHE A 802     6714   8445   9249   -772   -488   -949       O  
ATOM    433  CB  PHE A 802       0.320  29.763  42.897  1.00 60.52           C  
ANISOU  433  CB  PHE A 802     6048   7906   9041   -915   -181   -809       C  
ATOM    434  CG  PHE A 802       1.765  29.951  43.304  1.00 60.70           C  
ANISOU  434  CG  PHE A 802     6170   7961   8931   -871   -152   -653       C  
ATOM    435  CD1 PHE A 802       2.790  29.339  42.588  1.00 62.36           C  
ANISOU  435  CD1 PHE A 802     6451   8090   9155   -832   -149   -616       C  
ATOM    436  CD2 PHE A 802       2.093  30.662  44.454  1.00 60.69           C  
ANISOU  436  CD2 PHE A 802     6191   8047   8821   -900   -106   -539       C  
ATOM    437  CE1 PHE A 802       4.114  29.474  42.988  1.00 63.04           C  
ANISOU  437  CE1 PHE A 802     6589   8175   9188   -792   -129   -456       C  
ATOM    438  CE2 PHE A 802       3.421  30.811  44.844  1.00 62.88           C  
ANISOU  438  CE2 PHE A 802     6547   8355   8990   -879   -113   -375       C  
ATOM    439  CZ  PHE A 802       4.422  30.225  44.105  1.00 61.54           C  
ANISOU  439  CZ  PHE A 802     6408   8098   8877   -810   -137   -328       C  
ATOM    440  N   SER A 803       0.397  29.582  39.747  1.00 61.38           N  
ANISOU  440  N   SER A 803     6306   7921   9094   -916   -432  -1036       N  
ATOM    441  CA  SER A 803       1.093  29.361  38.465  1.00 61.50           C  
ANISOU  441  CA  SER A 803     6491   7854   9021   -952   -465  -1101       C  
ATOM    442  C   SER A 803       0.855  30.491  37.494  1.00 65.45           C  
ANISOU  442  C   SER A 803     7068   8408   9392   -950   -670  -1179       C  
ATOM    443  O   SER A 803       1.803  30.966  36.869  1.00 64.54           O  
ANISOU  443  O   SER A 803     7115   8268   9137   -922   -677  -1196       O  
ATOM    444  CB  SER A 803       0.659  28.051  37.813  1.00 65.45           C  
ANISOU  444  CB  SER A 803     7023   8232   9614  -1087   -402  -1184       C  
ATOM    445  OG  SER A 803       0.889  26.976  38.702  1.00 76.59           O  
ANISOU  445  OG  SER A 803     8357   9582  11161  -1082   -202  -1102       O  
ATOM    446  N   ARG A 804      -0.419  30.916  37.374  1.00 62.40           N  
ANISOU  446  N   ARG A 804     6555   8073   9080   -985   -835  -1218       N  
ATOM    447  CA  ARG A 804      -0.847  31.991  36.492  1.00 62.87           C  
ANISOU  447  CA  ARG A 804     6646   8176   9067   -995  -1074  -1256       C  
ATOM    448  C   ARG A 804      -0.120  33.291  36.873  1.00 65.85           C  
ANISOU  448  C   ARG A 804     7044   8647   9328   -851  -1058  -1202       C  
ATOM    449  O   ARG A 804       0.541  33.882  36.025  1.00 65.69           O  
ANISOU  449  O   ARG A 804     7201   8623   9135   -839  -1138  -1237       O  
ATOM    450  CB  ARG A 804      -2.362  32.139  36.606  1.00 66.48           C  
ANISOU  450  CB  ARG A 804     6880   8644   9733  -1041  -1224  -1261       C  
ATOM    451  CG  ARG A 804      -3.075  32.799  35.426  1.00 81.88           C  
ANISOU  451  CG  ARG A 804     8844  10591  11675  -1125  -1541  -1280       C  
ATOM    452  CD  ARG A 804      -4.574  32.968  35.684  1.00 89.23           C  
ANISOU  452  CD  ARG A 804     9486  11504  12912  -1155  -1682  -1253       C  
ATOM    453  NE  ARG A 804      -4.864  33.355  37.070  1.00100.85           N  
ANISOU  453  NE  ARG A 804    10740  12996  14584  -1034  -1473  -1216       N  
ATOM    454  CZ  ARG A 804      -4.828  34.602  37.535  1.00117.07           C  
ANISOU  454  CZ  ARG A 804    12696  15096  16688   -927  -1444  -1161       C  
ATOM    455  NH1 ARG A 804      -4.542  35.615  36.722  1.00107.04           N  
ANISOU  455  NH1 ARG A 804    11501  13869  15299   -892  -1634  -1128       N  
ATOM    456  NH2 ARG A 804      -5.078  34.847  38.816  1.00 99.42           N  
ANISOU  456  NH2 ARG A 804    10309  12852  14612   -877  -1203  -1146       N  
ATOM    457  N   GLU A 805      -0.150  33.653  38.164  1.00 61.58           N  
ANISOU  457  N   GLU A 805     6359   8178   8861   -766   -920  -1127       N  
ATOM    458  CA  GLU A 805       0.472  34.857  38.699  1.00 60.08           C  
ANISOU  458  CA  GLU A 805     6179   8088   8562   -657   -864  -1075       C  
ATOM    459  C   GLU A 805       1.977  34.859  38.602  1.00 63.45           C  
ANISOU  459  C   GLU A 805     6789   8518   8802   -598   -775  -1050       C  
ATOM    460  O   GLU A 805       2.529  35.864  38.160  1.00 63.21           O  
ANISOU  460  O   GLU A 805     6853   8536   8628   -527   -823  -1072       O  
ATOM    461  CB  GLU A 805       0.013  35.149  40.137  1.00 61.11           C  
ANISOU  461  CB  GLU A 805     6146   8269   8803   -651   -704  -1010       C  
ATOM    462  CG  GLU A 805      -1.440  35.606  40.253  1.00 68.98           C  
ANISOU  462  CG  GLU A 805     6931   9239  10039   -685   -757  -1041       C  
ATOM    463  CD  GLU A 805      -1.824  36.807  39.406  1.00 95.83           C  
ANISOU  463  CD  GLU A 805    10283  12665  13464   -635   -936  -1057       C  
ATOM    464  OE1 GLU A 805      -1.462  37.950  39.774  1.00 73.89           O  
ANISOU  464  OE1 GLU A 805     7501   9960  10616   -564   -852  -1028       O  
ATOM    465  OE2 GLU A 805      -2.477  36.598  38.357  1.00101.09           O  
ANISOU  465  OE2 GLU A 805    10923  13274  14213   -682  -1168  -1090       O  
ATOM    466  N   ILE A 806       2.644  33.735  38.970  1.00 58.67           N  
ANISOU  466  N   ILE A 806     6224   7838   8230   -627   -645  -1001       N  
ATOM    467  CA  ILE A 806       4.105  33.611  38.958  1.00 55.59           C  
ANISOU  467  CA  ILE A 806     5962   7405   7756   -575   -547   -951       C  
ATOM    468  C   ILE A 806       4.672  33.620  37.531  1.00 62.81           C  
ANISOU  468  C   ILE A 806     7073   8206   8587   -594   -591  -1069       C  
ATOM    469  O   ILE A 806       5.774  34.114  37.352  1.00 61.93           O  
ANISOU  469  O   ILE A 806     7072   8073   8386   -525   -538  -1068       O  
ATOM    470  CB  ILE A 806       4.629  32.419  39.810  1.00 56.62           C  
ANISOU  470  CB  ILE A 806     6040   7460   8012   -606   -403   -825       C  
ATOM    471  CG1 ILE A 806       6.101  32.681  40.294  1.00 54.86           C  
ANISOU  471  CG1 ILE A 806     5866   7234   7743   -536   -330   -699       C  
ATOM    472  CG2 ILE A 806       4.446  31.071  39.101  1.00 53.90           C  
ANISOU  472  CG2 ILE A 806     5725   6950   7803   -696   -350   -885       C  
ATOM    473  CD1 ILE A 806       6.646  31.701  41.329  1.00 59.32           C  
ANISOU  473  CD1 ILE A 806     6352   7742   8446   -571   -238   -508       C  
ATOM    474  N   LYS A 807       3.934  33.116  36.524  1.00 62.58           N  
ANISOU  474  N   LYS A 807     7108   8094   8577   -712   -682  -1177       N  
ATOM    475  CA  LYS A 807       4.442  33.143  35.147  1.00 62.98           C  
ANISOU  475  CA  LYS A 807     7407   8015   8508   -793   -709  -1303       C  
ATOM    476  C   LYS A 807       4.543  34.608  34.671  1.00 66.78           C  
ANISOU  476  C   LYS A 807     7981   8588   8805   -720   -854  -1347       C  
ATOM    477  O   LYS A 807       5.515  34.975  34.015  1.00 65.86           O  
ANISOU  477  O   LYS A 807     8071   8386   8567   -709   -798  -1420       O  
ATOM    478  CB  LYS A 807       3.615  32.249  34.200  1.00 65.59           C  
ANISOU  478  CB  LYS A 807     7820   8239   8864   -994   -778  -1398       C  
ATOM    479  N   LYS A 808       3.604  35.466  35.122  1.00 63.34           N  
ANISOU  479  N   LYS A 808     7376   8308   8384   -659   -999  -1298       N  
ATOM    480  CA  LYS A 808       3.634  36.904  34.834  1.00 61.55           C  
ANISOU  480  CA  LYS A 808     7187   8176   8023   -571  -1112  -1314       C  
ATOM    481  C   LYS A 808       4.889  37.539  35.472  1.00 59.20           C  
ANISOU  481  C   LYS A 808     6930   7935   7630   -426   -938  -1284       C  
ATOM    482  O   LYS A 808       5.531  38.366  34.835  1.00 57.72           O  
ANISOU  482  O   LYS A 808     6910   7740   7281   -376   -956  -1354       O  
ATOM    483  CB  LYS A 808       2.350  37.581  35.334  1.00 64.77           C  
ANISOU  483  CB  LYS A 808     7349   8699   8562   -542  -1239  -1248       C  
ATOM    484  CG  LYS A 808       1.138  37.336  34.424  1.00 67.63           C  
ANISOU  484  CG  LYS A 808     7682   9004   9010   -682  -1495  -1271       C  
ATOM    485  CD  LYS A 808      -0.173  37.227  35.189  1.00 75.99           C  
ANISOU  485  CD  LYS A 808     8433  10098  10344   -689  -1533  -1201       C  
ATOM    486  CE  LYS A 808      -0.743  38.550  35.629  1.00 88.84           C  
ANISOU  486  CE  LYS A 808     9861  11801  12091   -588  -1568  -1136       C  
ATOM    487  NZ  LYS A 808      -2.158  38.418  36.071  1.00102.65           N  
ANISOU  487  NZ  LYS A 808    11315  13513  14175   -634  -1627  -1087       N  
ATOM    488  N   LEU A 809       5.264  37.081  36.688  1.00 52.65           N  
ANISOU  488  N   LEU A 809     5966   7145   6892   -382   -779  -1178       N  
ATOM    489  CA  LEU A 809       6.432  37.534  37.429  1.00 50.17           C  
ANISOU  489  CA  LEU A 809     5667   6886   6507   -282   -639  -1111       C  
ATOM    490  C   LEU A 809       7.742  37.011  36.820  1.00 53.27           C  
ANISOU  490  C   LEU A 809     6233   7110   6896   -278   -539  -1154       C  
ATOM    491  O   LEU A 809       8.753  37.715  36.825  1.00 49.58           O  
ANISOU  491  O   LEU A 809     5849   6654   6335   -189   -474  -1165       O  
ATOM    492  CB  LEU A 809       6.333  37.181  38.930  1.00 50.25           C  
ANISOU  492  CB  LEU A 809     5502   6983   6608   -293   -541   -956       C  
ATOM    493  CG  LEU A 809       5.106  37.696  39.753  1.00 54.35           C  
ANISOU  493  CG  LEU A 809     5851   7626   7174   -324   -550   -921       C  
ATOM    494  CD1 LEU A 809       5.343  37.488  41.238  1.00 53.09           C  
ANISOU  494  CD1 LEU A 809     5615   7533   7025   -373   -417   -779       C  
ATOM    495  CD2 LEU A 809       4.768  39.187  39.450  1.00 52.96           C  
ANISOU  495  CD2 LEU A 809     5669   7552   6901   -254   -592   -982       C  
ATOM    496  N   GLY A 810       7.696  35.795  36.276  1.00 51.53           N  
ANISOU  496  N   GLY A 810     6064   6714   6800   -384   -502  -1189       N  
ATOM    497  CA  GLY A 810       8.814  35.151  35.604  1.00 50.82           C  
ANISOU  497  CA  GLY A 810     6131   6395   6784   -419   -354  -1247       C  
ATOM    498  C   GLY A 810       9.252  35.923  34.373  1.00 54.31           C  
ANISOU  498  C   GLY A 810     6835   6747   7052   -433   -369  -1425       C  
ATOM    499  O   GLY A 810      10.442  36.019  34.111  1.00 54.36           O  
ANISOU  499  O   GLY A 810     6957   6610   7089   -394   -220  -1470       O  
ATOM    500  N   SER A 811       8.309  36.534  33.634  1.00 52.65           N  
ANISOU  500  N   SER A 811     6269   6883   6853    312   -397  -1265       N  
ATOM    501  CA  SER A 811       8.630  37.316  32.428  1.00 52.18           C  
ANISOU  501  CA  SER A 811     6313   6908   6603    364   -409  -1311       C  
ATOM    502  C   SER A 811       9.184  38.702  32.763  1.00 55.26           C  
ANISOU  502  C   SER A 811     6674   7412   6910    391   -322  -1202       C  
ATOM    503  O   SER A 811       9.639  39.397  31.865  1.00 56.01           O  
ANISOU  503  O   SER A 811     6862   7575   6843    432   -299  -1218       O  
ATOM    504  CB  SER A 811       7.396  37.437  31.537  1.00 57.78           C  
ANISOU  504  CB  SER A 811     7060   7615   7278    327   -579  -1381       C  
ATOM    505  OG  SER A 811       6.442  38.331  32.087  1.00 71.06           O  
ANISOU  505  OG  SER A 811     8628   9343   9030    286   -636  -1299       O  
ATOM    506  N   VAL A 812       9.121  39.125  34.047  1.00 50.97           N  
ANISOU  506  N   VAL A 812     6014   6885   6468    362   -271  -1093       N  
ATOM    507  CA  VAL A 812       9.616  40.424  34.482  1.00 48.80           C  
ANISOU  507  CA  VAL A 812     5708   6703   6132    379   -195   -995       C  
ATOM    508  C   VAL A 812      11.131  40.370  34.600  1.00 53.81           C  
ANISOU  508  C   VAL A 812     6365   7358   6724    431    -68   -978       C  
ATOM    509  O   VAL A 812      11.683  39.634  35.441  1.00 52.86           O  
ANISOU  509  O   VAL A 812     6195   7185   6702    435    -21   -956       O  
ATOM    510  CB  VAL A 812       8.929  40.913  35.764  1.00 50.74           C  
ANISOU  510  CB  VAL A 812     5836   6954   6488    327   -191   -903       C  
ATOM    511  CG1 VAL A 812       9.552  42.215  36.254  1.00 49.90           C  
ANISOU  511  CG1 VAL A 812     5710   6929   6319    345   -111   -814       C  
ATOM    512  CG2 VAL A 812       7.438  41.080  35.546  1.00 50.15           C  
ANISOU  512  CG2 VAL A 812     5713   6865   6474    284   -308   -928       C  
ATOM    513  N   ARG A 813      11.811  41.130  33.716  1.00 50.80           N  
ANISOU  513  N   ARG A 813     6057   7046   6197    470    -15   -989       N  
ATOM    514  CA  ARG A 813      13.276  41.153  33.700  1.00 50.35           C  
ANISOU  514  CA  ARG A 813     6002   7016   6111    517    119   -983       C  
ATOM    515  C   ARG A 813      13.827  42.569  33.614  1.00 52.85           C  
ANISOU  515  C   ARG A 813     6322   7424   6333    516    191   -908       C  
ATOM    516  O   ARG A 813      13.421  43.344  32.746  1.00 54.00           O  
ANISOU  516  O   ARG A 813     6555   7613   6352    511    162   -911       O  
ATOM    517  CB  ARG A 813      13.841  40.286  32.555  1.00 48.97           C  
ANISOU  517  CB  ARG A 813     5928   6810   5869    567    160  -1103       C  
ATOM    518  CG  ARG A 813      13.660  38.789  32.747  1.00 61.14           C  
ANISOU  518  CG  ARG A 813     7461   8239   7529    578    116  -1180       C  
ATOM    519  CD  ARG A 813      14.660  38.146  33.713  1.00 65.39           C  
ANISOU  519  CD  ARG A 813     7906   8729   8209    614    189  -1146       C  
ATOM    520  NE  ARG A 813      14.122  36.890  34.243  1.00 80.59           N  
ANISOU  520  NE  ARG A 813     9817  10533  10272    598    112  -1172       N  
ATOM    521  CZ  ARG A 813      14.223  35.709  33.639  1.00 96.36           C  
ANISOU  521  CZ  ARG A 813    11876  12433  12302    634    102  -1286       C  
ATOM    522  NH1 ARG A 813      14.884  35.595  32.494  1.00 88.19           N  
ANISOU  522  NH1 ARG A 813    10926  11416  11166    694    176  -1394       N  
ATOM    523  NH2 ARG A 813      13.669  34.631  34.179  1.00 81.89           N  
ANISOU  523  NH2 ARG A 813    10032  10479  10603    606     27  -1296       N  
ATOM    524  N   HIS A 814      14.796  42.874  34.487  1.00 46.04           N  
ANISOU  524  N   HIS A 814     5373   6584   5534    521    276   -843       N  
ATOM    525  CA  HIS A 814      15.447  44.174  34.556  1.00 44.83           C  
ANISOU  525  CA  HIS A 814     5207   6505   5322    510    351   -772       C  
ATOM    526  C   HIS A 814      16.887  44.010  35.076  1.00 50.24           C  
ANISOU  526  C   HIS A 814     5806   7199   6082    534    457   -755       C  
ATOM    527  O   HIS A 814      17.107  43.185  35.975  1.00 50.02           O  
ANISOU  527  O   HIS A 814     5705   7122   6180    547    431   -748       O  
ATOM    528  CB  HIS A 814      14.621  45.119  35.465  1.00 43.14           C  
ANISOU  528  CB  HIS A 814     4946   6306   5138    462    287   -685       C  
ATOM    529  CG  HIS A 814      15.059  46.538  35.366  1.00 46.38           C  
ANISOU  529  CG  HIS A 814     5371   6776   5476    444    343   -620       C  
ATOM    530  ND1 HIS A 814      16.125  47.028  36.135  1.00 47.41           N  
ANISOU  530  ND1 HIS A 814     5426   6931   5655    431    420   -566       N  
ATOM    531  CD2 HIS A 814      14.647  47.512  34.521  1.00 47.99           C  
ANISOU  531  CD2 HIS A 814     5663   7008   5564    437    327   -602       C  
ATOM    532  CE1 HIS A 814      16.285  48.286  35.759  1.00 46.38           C  
ANISOU  532  CE1 HIS A 814     5337   6840   5445    409    457   -520       C  
ATOM    533  NE2 HIS A 814      15.450  48.613  34.770  1.00 47.39           N  
ANISOU  533  NE2 HIS A 814     5569   6969   5467    415    408   -536       N  
ATOM    534  N   PRO A 815      17.887  44.770  34.575  1.00 49.07           N  
ANISOU  534  N   PRO A 815     5661   7108   5875    538    570   -743       N  
ATOM    535  CA  PRO A 815      19.271  44.590  35.109  1.00 48.42           C  
ANISOU  535  CA  PRO A 815     5463   7033   5902    561    658   -733       C  
ATOM    536  C   PRO A 815      19.365  44.825  36.620  1.00 52.90           C  
ANISOU  536  C   PRO A 815     5926   7591   6584    533    592   -648       C  
ATOM    537  O   PRO A 815      20.140  44.151  37.298  1.00 54.83           O  
ANISOU  537  O   PRO A 815     6079   7804   6950    564    589   -647       O  
ATOM    538  CB  PRO A 815      20.129  45.597  34.312  1.00 50.23           C  
ANISOU  538  CB  PRO A 815     5712   7330   6045    544    794   -723       C  
ATOM    539  CG  PRO A 815      19.286  46.006  33.123  1.00 55.89           C  
ANISOU  539  CG  PRO A 815     6592   8063   6581    530    786   -746       C  
ATOM    540  CD  PRO A 815      17.836  45.788  33.495  1.00 51.51           C  
ANISOU  540  CD  PRO A 815     6076   7471   6025    519    622   -735       C  
ATOM    541  N   ASN A 816      18.517  45.705  37.175  1.00 47.27           N  
ANISOU  541  N   ASN A 816     5234   6894   5831    479    527   -582       N  
ATOM    542  CA  ASN A 816      18.548  45.967  38.615  1.00 46.12           C  
ANISOU  542  CA  ASN A 816     5020   6740   5765    446    471   -510       C  
ATOM    543  C   ASN A 816      17.610  45.068  39.457  1.00 51.48           C  
ANISOU  543  C   ASN A 816     5704   7357   6500    440    378   -502       C  
ATOM    544  O   ASN A 816      17.458  45.292  40.651  1.00 52.54           O  
ANISOU  544  O   ASN A 816     5811   7482   6669    404    336   -442       O  
ATOM    545  CB  ASN A 816      18.285  47.451  38.876  1.00 45.00           C  
ANISOU  545  CB  ASN A 816     4894   6641   5563    391    476   -449       C  
ATOM    546  CG  ASN A 816      19.418  48.302  38.362  1.00 56.24           C  
ANISOU  546  CG  ASN A 816     6293   8111   6964    378    572   -437       C  
ATOM    547  OD1 ASN A 816      19.304  48.984  37.355  1.00 52.12           O  
ANISOU  547  OD1 ASN A 816     5842   7616   6346    369    626   -442       O  
ATOM    548  ND2 ASN A 816      20.551  48.252  39.034  1.00 48.70           N  
ANISOU  548  ND2 ASN A 816     5237   7164   6105    375    591   -420       N  
ATOM    549  N   LEU A 817      16.985  44.072  38.838  1.00 47.77           N  
ANISOU  549  N   LEU A 817     5278   6840   6031    466    352   -564       N  
ATOM    550  CA  LEU A 817      16.051  43.176  39.502  1.00 47.77           C  
ANISOU  550  CA  LEU A 817     5285   6772   6091    447    277   -559       C  
ATOM    551  C   LEU A 817      16.610  41.766  39.416  1.00 53.27           C  
ANISOU  551  C   LEU A 817     5973   7394   6872    498    270   -605       C  
ATOM    552  O   LEU A 817      17.014  41.336  38.325  1.00 53.69           O  
ANISOU  552  O   LEU A 817     6053   7442   6906    547    311   -686       O  
ATOM    553  CB  LEU A 817      14.677  43.264  38.810  1.00 47.92           C  
ANISOU  553  CB  LEU A 817     5360   6787   6061    424    232   -598       C  
ATOM    554  CG  LEU A 817      13.473  42.624  39.551  1.00 53.35           C  
ANISOU  554  CG  LEU A 817     6037   7413   6820    378    168   -586       C  
ATOM    555  CD1 LEU A 817      13.125  43.390  40.853  1.00 52.91           C  
ANISOU  555  CD1 LEU A 817     5946   7378   6779    326    175   -501       C  
ATOM    556  CD2 LEU A 817      12.257  42.557  38.651  1.00 52.46           C  
ANISOU  556  CD2 LEU A 817     5957   7290   6685    365    109   -646       C  
ATOM    557  N   VAL A 818      16.621  41.037  40.546  1.00 48.12           N  
ANISOU  557  N   VAL A 818     5298   6677   6308    488    221   -556       N  
ATOM    558  CA  VAL A 818      17.175  39.684  40.561  1.00 47.74           C  
ANISOU  558  CA  VAL A 818     5244   6537   6358    543    202   -588       C  
ATOM    559  C   VAL A 818      16.246  38.720  39.736  1.00 50.55           C  
ANISOU  559  C   VAL A 818     5664   6821   6722    544    176   -674       C  
ATOM    560  O   VAL A 818      15.055  38.682  40.008  1.00 46.22           O  
ANISOU  560  O   VAL A 818     5143   6252   6168    480    133   -657       O  
ATOM    561  CB  VAL A 818      17.424  39.203  42.019  1.00 51.47           C  
ANISOU  561  CB  VAL A 818     5699   6949   6909    529    140   -495       C  
ATOM    562  CG1 VAL A 818      17.765  37.719  42.071  1.00 52.70           C  
ANISOU  562  CG1 VAL A 818     5866   6981   7178    584     99   -519       C  
ATOM    563  CG2 VAL A 818      18.516  40.029  42.683  1.00 50.69           C  
ANISOU  563  CG2 VAL A 818     5536   6913   6811    538    144   -434       C  
ATOM    564  N   PRO A 819      16.780  37.946  38.737  1.00 50.06           N  
ANISOU  564  N   PRO A 819     5623   6717   6682    613    206   -774       N  
ATOM    565  CA  PRO A 819      15.904  37.052  37.952  1.00 50.98           C  
ANISOU  565  CA  PRO A 819     5813   6759   6799    607    168   -866       C  
ATOM    566  C   PRO A 819      15.321  35.896  38.737  1.00 55.43           C  
ANISOU  566  C   PRO A 819     6388   7194   7477    576     95   -841       C  
ATOM    567  O   PRO A 819      16.025  35.258  39.511  1.00 55.67           O  
ANISOU  567  O   PRO A 819     6393   7154   7604    611     83   -793       O  
ATOM    568  CB  PRO A 819      16.805  36.558  36.811  1.00 52.80           C  
ANISOU  568  CB  PRO A 819     6070   6975   7018    693    237   -982       C  
ATOM    569  CG  PRO A 819      17.965  37.552  36.797  1.00 56.07           C  
ANISOU  569  CG  PRO A 819     6417   7492   7396    727    330   -946       C  
ATOM    570  CD  PRO A 819      18.170  37.877  38.241  1.00 50.12           C  
ANISOU  570  CD  PRO A 819     5586   6742   6715    697    284   -819       C  
ATOM    571  N   LEU A 820      14.010  35.690  38.552  1.00 50.98           N  
ANISOU  571  N   LEU A 820     5862   6600   6908    506     40   -865       N  
ATOM    572  CA  LEU A 820      13.189  34.603  39.061  1.00 50.73           C  
ANISOU  572  CA  LEU A 820     5851   6441   6982    451    -21   -857       C  
ATOM    573  C   LEU A 820      13.233  33.556  37.940  1.00 57.28           C  
ANISOU  573  C   LEU A 820     6744   7179   7839    495    -44   -995       C  
ATOM    574  O   LEU A 820      12.901  33.846  36.794  1.00 56.77           O  
ANISOU  574  O   LEU A 820     6722   7163   7687    502    -51  -1093       O  
ATOM    575  CB  LEU A 820      11.758  35.126  39.300  1.00 49.45           C  
ANISOU  575  CB  LEU A 820     5670   6314   6806    348    -55   -828       C  
ATOM    576  CG  LEU A 820      10.698  34.172  39.845  1.00 53.16           C  
ANISOU  576  CG  LEU A 820     6142   6665   7390    261   -101   -813       C  
ATOM    577  CD1 LEU A 820      11.000  33.758  41.291  1.00 52.58           C  
ANISOU  577  CD1 LEU A 820     6070   6527   7381    232    -77   -688       C  
ATOM    578  CD2 LEU A 820       9.326  34.828  39.771  1.00 54.86           C  
ANISOU  578  CD2 LEU A 820     6309   6935   7600    175   -126   -817       C  
ATOM    579  N   ARG A 821      13.742  32.369  38.258  1.00 56.91           N  
ANISOU  579  N   ARG A 821     6719   6998   7908    535    -56  -1004       N  
ATOM    580  CA  ARG A 821      13.968  31.287  37.297  1.00 57.11           C  
ANISOU  580  CA  ARG A 821     6810   6914   7976    593    -66  -1143       C  
ATOM    581  C   ARG A 821      12.907  30.213  37.261  1.00 62.19           C  
ANISOU  581  C   ARG A 821     7505   7411   8711    519   -147  -1188       C  
ATOM    582  O   ARG A 821      12.721  29.563  36.238  1.00 65.05           O  
ANISOU  582  O   ARG A 821     7937   7707   9071    538   -174  -1329       O  
ATOM    583  CB  ARG A 821      15.334  30.652  37.540  1.00 55.29           C  
ANISOU  583  CB  ARG A 821     6562   6610   7835    706    -25  -1144       C  
ATOM    584  CG  ARG A 821      16.489  31.618  37.418  1.00 53.51           C  
ANISOU  584  CG  ARG A 821     6269   6518   7545    780     61  -1124       C  
ATOM    585  CD  ARG A 821      16.770  32.042  35.999  1.00 51.33           C  
ANISOU  585  CD  ARG A 821     6031   6325   7148    825    140  -1258       C  
ATOM    586  NE  ARG A 821      17.941  32.921  35.966  1.00 58.80           N  
ANISOU  586  NE  ARG A 821     6898   7385   8057    885    239  -1229       N  
ATOM    587  CZ  ARG A 821      18.262  33.718  34.954  1.00 67.09           C  
ANISOU  587  CZ  ARG A 821     7970   8549   8973    902    333  -1293       C  
ATOM    588  NH1 ARG A 821      17.509  33.754  33.864  1.00 58.33           N  
ANISOU  588  NH1 ARG A 821     6972   7457   7734    872    326  -1391       N  
ATOM    589  NH2 ARG A 821      19.325  34.497  35.030  1.00 58.65           N  
ANISOU  589  NH2 ARG A 821     6815   7573   7895    942    428  -1257       N  
ATOM    590  N   GLY A 822      12.217  30.029  38.363  1.00 56.84           N  
ANISOU  590  N   GLY A 822     6802   6684   8112    429   -181  -1075       N  
ATOM    591  CA  GLY A 822      11.178  29.027  38.431  1.00 56.09           C  
ANISOU  591  CA  GLY A 822     6743   6444   8124    338   -247  -1103       C  
ATOM    592  C   GLY A 822      10.581  28.892  39.797  1.00 56.55           C  
ANISOU  592  C   GLY A 822     6774   6454   8260    237   -247   -954       C  
ATOM    593  O   GLY A 822      10.680  29.789  40.639  1.00 52.08           O  
ANISOU  593  O   GLY A 822     6160   5992   7635    219   -203   -838       O  
ATOM    594  N   TYR A 823       9.949  27.752  40.000  1.00 56.08           N  
ANISOU  594  N   TYR A 823     6755   6224   8327    165   -290   -963       N  
ATOM    595  CA  TYR A 823       9.322  27.402  41.256  1.00 57.62           C  
ANISOU  595  CA  TYR A 823     6949   6340   8604     52   -276   -826       C  
ATOM    596  C   TYR A 823       9.143  25.899  41.378  1.00 62.97           C  
ANISOU  596  C   TYR A 823     7705   6787   9434     14   -320   -840       C  
ATOM    597  O   TYR A 823       9.066  25.172  40.371  1.00 61.94           O  
ANISOU  597  O   TYR A 823     7614   6563   9359     39   -374   -984       O  
ATOM    598  CB  TYR A 823       7.967  28.144  41.461  1.00 58.91           C  
ANISOU  598  CB  TYR A 823     7031   6597   8756    -79   -256   -803       C  
ATOM    599  CG  TYR A 823       6.872  27.722  40.515  1.00 62.95           C  
ANISOU  599  CG  TYR A 823     7519   7057   9343   -154   -324   -934       C  
ATOM    600  CD1 TYR A 823       6.731  28.325  39.269  1.00 65.26           C  
ANISOU  600  CD1 TYR A 823     7788   7454   9552   -106   -377  -1066       C  
ATOM    601  CD2 TYR A 823       5.961  26.729  40.868  1.00 65.61           C  
ANISOU  601  CD2 TYR A 823     7859   7235   9833   -282   -343   -924       C  
ATOM    602  CE1 TYR A 823       5.733  27.925  38.379  1.00 67.81           C  
ANISOU  602  CE1 TYR A 823     8098   7727   9940   -175   -470  -1192       C  
ATOM    603  CE2 TYR A 823       4.962  26.315  39.983  1.00 67.94           C  
ANISOU  603  CE2 TYR A 823     8122   7476  10215   -358   -426  -1055       C  
ATOM    604  CZ  TYR A 823       4.845  26.927  38.744  1.00 73.78           C  
ANISOU  604  CZ  TYR A 823     8841   8325  10865   -301   -500  -1190       C  
ATOM    605  OH  TYR A 823       3.854  26.561  37.871  1.00 74.26           O  
ANISOU  605  OH  TYR A 823     8876   8338  11003   -376   -609  -1321       O  
ATOM    606  N   TYR A 824       9.049  25.449  42.633  1.00 60.13           N  
ANISOU  606  N   TYR A 824     7383   6331   9134    -53   -297   -687       N  
ATOM    607  CA  TYR A 824       8.796  24.061  42.959  1.00 61.16           C  
ANISOU  607  CA  TYR A 824     7599   6227   9413   -112   -332   -662       C  
ATOM    608  C   TYR A 824       7.494  23.999  43.715  1.00 65.14           C  
ANISOU  608  C   TYR A 824     8081   6700   9972   -299   -286   -575       C  
ATOM    609  O   TYR A 824       7.241  24.823  44.616  1.00 62.74           O  
ANISOU  609  O   TYR A 824     7741   6512   9587   -354   -212   -456       O  
ATOM    610  CB  TYR A 824       9.946  23.413  43.759  1.00 62.05           C  
ANISOU  610  CB  TYR A 824     7804   6216   9558    -19   -352   -548       C  
ATOM    611  CG  TYR A 824       9.717  21.940  44.035  1.00 65.91           C  
ANISOU  611  CG  TYR A 824     8398   6438  10207    -73   -397   -521       C  
ATOM    612  CD1 TYR A 824       9.835  20.992  43.020  1.00 69.78           C  
ANISOU  612  CD1 TYR A 824     8928   6779  10807    -20   -456   -678       C  
ATOM    613  CD2 TYR A 824       9.372  21.494  45.307  1.00 66.50           C  
ANISOU  613  CD2 TYR A 824     8550   6400  10316   -181   -375   -339       C  
ATOM    614  CE1 TYR A 824       9.612  19.638  43.263  1.00 72.57           C  
ANISOU  614  CE1 TYR A 824     9385   6869  11320    -72   -500   -656       C  
ATOM    615  CE2 TYR A 824       9.174  20.139  45.569  1.00 68.81           C  
ANISOU  615  CE2 TYR A 824     8955   6432  10759   -236   -415   -301       C  
ATOM    616  CZ  TYR A 824       9.287  19.215  44.541  1.00 78.91           C  
ANISOU  616  CZ  TYR A 824    10260   7556  12164   -181   -481   -461       C  
ATOM    617  OH  TYR A 824       9.052  17.880  44.771  1.00 82.25           O  
ANISOU  617  OH  TYR A 824    10798   7705  12748   -241   -523   -429       O  
ATOM    618  N   TRP A 825       6.666  23.022  43.325  1.00 63.07           N  
ANISOU  618  N   TRP A 825     7835   6275   9852   -399   -324   -646       N  
ATOM    619  CA  TRP A 825       5.377  22.741  43.925  1.00 64.78           C  
ANISOU  619  CA  TRP A 825     8019   6426  10169   -592   -275   -583       C  
ATOM    620  C   TRP A 825       5.386  21.241  44.244  1.00 71.46           C  
ANISOU  620  C   TRP A 825     8987   6998  11168   -649   -307   -543       C  
ATOM    621  O   TRP A 825       5.366  20.421  43.327  1.00 71.82           O  
ANISOU  621  O   TRP A 825     9063   6910  11314   -629   -391   -683       O  
ATOM    622  CB  TRP A 825       4.250  23.116  42.942  1.00 63.89           C  
ANISOU  622  CB  TRP A 825     7779   6391  10103   -669   -311   -734       C  
ATOM    623  CG  TRP A 825       2.891  23.193  43.568  1.00 65.67           C  
ANISOU  623  CG  TRP A 825     7910   6611  10431   -860   -238   -675       C  
ATOM    624  CD1 TRP A 825       2.052  22.154  43.837  1.00 70.37           C  
ANISOU  624  CD1 TRP A 825     8516   7018  11205  -1019   -229   -660       C  
ATOM    625  CD2 TRP A 825       2.203  24.382  43.976  1.00 64.69           C  
ANISOU  625  CD2 TRP A 825     7655   6673  10251   -914   -153   -631       C  
ATOM    626  NE1 TRP A 825       0.897  22.616  44.420  1.00 70.05           N  
ANISOU  626  NE1 TRP A 825     8349   7041  11227  -1173   -130   -606       N  
ATOM    627  CE2 TRP A 825       0.952  23.981  44.501  1.00 70.25           C  
ANISOU  627  CE2 TRP A 825     8283   7295  11113  -1105    -83   -594       C  
ATOM    628  CE3 TRP A 825       2.525  25.752  43.954  1.00 63.93           C  
ANISOU  628  CE3 TRP A 825     7496   6796   9997   -819   -122   -623       C  
ATOM    629  CZ2 TRP A 825       0.027  24.898  45.020  1.00 69.82           C  
ANISOU  629  CZ2 TRP A 825     8086   7375  11068  -1194     25   -554       C  
ATOM    630  CZ3 TRP A 825       1.609  26.662  44.463  1.00 65.53           C  
ANISOU  630  CZ3 TRP A 825     7572   7123  10204   -905    -29   -582       C  
ATOM    631  CH2 TRP A 825       0.375  26.237  44.983  1.00 67.93           C  
ANISOU  631  CH2 TRP A 825     7794   7346  10671  -1084     47   -552       C  
ATOM    632  N   GLY A 826       5.511  20.902  45.525  1.00 70.02           N  
ANISOU  632  N   GLY A 826     8892   6725  10987   -708   -245   -355       N  
ATOM    633  CA  GLY A 826       5.584  19.511  45.968  1.00 72.81           C  
ANISOU  633  CA  GLY A 826     9386   6805  11476   -761   -274   -282       C  
ATOM    634  C   GLY A 826       4.280  18.905  46.455  1.00 80.66           C  
ANISOU  634  C   GLY A 826    10375   7667  12605   -989   -205   -225       C  
ATOM    635  O   GLY A 826       3.305  19.635  46.669  1.00 78.85           O  
ANISOU  635  O   GLY A 826    10025   7575  12361  -1111   -114   -217       O  
ATOM    636  N   PRO A 827       4.242  17.556  46.670  1.00 82.13           N  
ANISOU  636  N   PRO A 827    10691   7576  12940  -1053   -240   -181       N  
ATOM    637  CA  PRO A 827       3.002  16.910  47.158  1.00 84.80           C  
ANISOU  637  CA  PRO A 827    11027   7769  13425  -1291   -161   -118       C  
ATOM    638  C   PRO A 827       2.509  17.412  48.522  1.00 91.01           C  
ANISOU  638  C   PRO A 827    11828   8629  14124  -1426      3     85       C  
ATOM    639  O   PRO A 827       1.301  17.439  48.753  1.00 92.30           O  
ANISOU  639  O   PRO A 827    11898   8793  14381  -1620    110     93       O  
ATOM    640  CB  PRO A 827       3.369  15.421  47.195  1.00 88.55           C  
ANISOU  640  CB  PRO A 827    11675   7924  14047  -1295   -240    -88       C  
ATOM    641  CG  PRO A 827       4.860  15.399  47.295  1.00 91.55           C  
ANISOU  641  CG  PRO A 827    12167   8294  14322  -1066   -322    -45       C  
ATOM    642  CD  PRO A 827       5.314  16.558  46.471  1.00 84.58           C  
ANISOU  642  CD  PRO A 827    11147   7682  13307   -913   -349   -188       C  
ATOM    643  N   LYS A 828       3.435  17.812  49.411  1.00 87.28           N  
ANISOU  643  N   LYS A 828    11469   8218  13476  -1326     23    239       N  
ATOM    644  CA  LYS A 828       3.111  18.345  50.733  1.00 87.76           C  
ANISOU  644  CA  LYS A 828    11580   8357  13407  -1435    176    428       C  
ATOM    645  C   LYS A 828       2.844  19.868  50.689  1.00 90.39           C  
ANISOU  645  C   LYS A 828    11749   8994  13602  -1407    256    373       C  
ATOM    646  O   LYS A 828       3.368  20.568  49.813  1.00 88.58           O  
ANISOU  646  O   LYS A 828    11420   8918  13320  -1251    168    238       O  
ATOM    647  CB  LYS A 828       4.205  17.984  51.743  1.00 91.30           C  
ANISOU  647  CB  LYS A 828    12253   8705  13731  -1350    134    622       C  
ATOM    648  N   GLU A 829       2.012  20.361  51.634  1.00 86.80           N  
ANISOU  648  N   GLU A 829    11273   8614  13092  -1562    435    477       N  
ATOM    649  CA  GLU A 829       1.567  21.755  51.746  1.00 84.86           C  
ANISOU  649  CA  GLU A 829    10876   8626  12740  -1564    540    436       C  
ATOM    650  C   GLU A 829       2.683  22.774  52.047  1.00 86.43           C  
ANISOU  650  C   GLU A 829    11125   9003  12711  -1389    498    474       C  
ATOM    651  O   GLU A 829       2.541  23.957  51.700  1.00 84.19           O  
ANISOU  651  O   GLU A 829    10698   8932  12360  -1333    523    385       O  
ATOM    652  CB  GLU A 829       0.435  21.873  52.780  1.00 87.79           C  
ANISOU  652  CB  GLU A 829    11234   8998  13122  -1778    765    542       C  
ATOM    653  N   HIS A 830       3.775  22.329  52.698  1.00 83.33           N  
ANISOU  653  N   HIS A 830    10933   8517  12213  -1306    425    607       N  
ATOM    654  CA  HIS A 830       4.918  23.192  53.023  1.00 81.22           C  
ANISOU  654  CA  HIS A 830    10715   8396  11750  -1145    362    648       C  
ATOM    655  C   HIS A 830       5.881  23.372  51.835  1.00 81.86           C  
ANISOU  655  C   HIS A 830    10710   8533  11860   -943    197    502       C  
ATOM    656  O   HIS A 830       6.726  24.276  51.878  1.00 80.58           O  
ANISOU  656  O   HIS A 830    10530   8526  11562   -815    155    497       O  
ATOM    657  CB  HIS A 830       5.666  22.661  54.260  1.00 83.36           C  
ANISOU  657  CB  HIS A 830    11230   8543  11899  -1144    335    857       C  
ATOM    658  CG  HIS A 830       6.365  21.358  54.035  1.00 87.88           C  
ANISOU  658  CG  HIS A 830    11925   8878  12587  -1075    185    894       C  
ATOM    659  ND1 HIS A 830       5.707  20.146  54.195  1.00 91.50           N  
ANISOU  659  ND1 HIS A 830    12474   9102  13189  -1214    219    954       N  
ATOM    660  CD2 HIS A 830       7.646  21.119  53.668  1.00 88.64           C  
ANISOU  660  CD2 HIS A 830    12057   8934  12689   -881      9    875       C  
ATOM    661  CE1 HIS A 830       6.611  19.216  53.937  1.00 91.55           C  
ANISOU  661  CE1 HIS A 830    12582   8926  13276  -1093     56    972       C  
ATOM    662  NE2 HIS A 830       7.789  19.755  53.605  1.00 90.39           N  
ANISOU  662  NE2 HIS A 830    12397   8891  13058   -887    -71    921       N  
ATOM    663  N   GLU A 831       5.747  22.517  50.782  1.00 76.99           N  
ANISOU  663  N   GLU A 831    10046   7787  11418   -923    114    379       N  
ATOM    664  CA  GLU A 831       6.612  22.512  49.592  1.00 74.94           C  
ANISOU  664  CA  GLU A 831     9725   7553  11195   -743    -21    229       C  
ATOM    665  C   GLU A 831       6.178  23.514  48.500  1.00 75.13           C  
ANISOU  665  C   GLU A 831     9563   7777  11206   -710    -11     52       C  
ATOM    666  O   GLU A 831       5.762  23.122  47.402  1.00 75.07           O  
ANISOU  666  O   GLU A 831     9485   7725  11315   -713    -64    -99       O  
ATOM    667  CB  GLU A 831       6.757  21.095  49.022  1.00 77.86           C  
ANISOU  667  CB  GLU A 831    10167   7676  11739   -727   -116    177       C  
ATOM    668  CG  GLU A 831       7.449  20.103  49.939  1.00 89.04           C  
ANISOU  668  CG  GLU A 831    11778   8881  13174   -707   -168    345       C  
ATOM    669  CD  GLU A 831       7.500  18.705  49.361  1.00113.30           C  
ANISOU  669  CD  GLU A 831    14920  11690  16438   -697   -255    285       C  
ATOM    670  OE1 GLU A 831       8.615  18.227  49.051  1.00106.13           O  
ANISOU  670  OE1 GLU A 831    14067  10690  15567   -526   -370    258       O  
ATOM    671  OE2 GLU A 831       6.418  18.104  49.173  1.00113.77           O  
ANISOU  671  OE2 GLU A 831    14967  11634  16626   -859   -207    250       O  
ATOM    672  N   ARG A 832       6.307  24.811  48.821  1.00 67.88           N  
ANISOU  672  N   ARG A 832     8582   7071  10138   -678     45     76       N  
ATOM    673  CA  ARG A 832       5.965  25.936  47.960  1.00 65.98           C  
ANISOU  673  CA  ARG A 832     8183   7028   9856   -640     56    -57       C  
ATOM    674  C   ARG A 832       7.216  26.804  47.889  1.00 67.16           C  
ANISOU  674  C   ARG A 832     8338   7318   9862   -477     12    -55       C  
ATOM    675  O   ARG A 832       7.498  27.575  48.802  1.00 66.04           O  
ANISOU  675  O   ARG A 832     8224   7275   9593   -478     65     48       O  
ATOM    676  CB  ARG A 832       4.748  26.715  48.511  1.00 66.65           C  
ANISOU  676  CB  ARG A 832     8177   7220   9927   -781    189    -27       C  
ATOM    677  CG  ARG A 832       3.518  25.856  48.853  1.00 71.75           C  
ANISOU  677  CG  ARG A 832     8813   7722  10726   -968    265      1       C  
ATOM    678  CD  ARG A 832       2.766  25.423  47.626  1.00 71.48           C  
ANISOU  678  CD  ARG A 832     8662   7639  10859  -1001    191   -162       C  
ATOM    679  NE  ARG A 832       1.736  24.433  47.928  1.00 78.83           N  
ANISOU  679  NE  ARG A 832     9588   8400  11963  -1182    245   -136       N  
ATOM    680  CZ  ARG A 832       1.861  23.126  47.723  1.00 91.76           C  
ANISOU  680  CZ  ARG A 832    11321   9822  13721  -1214    177   -140       C  
ATOM    681  NH1 ARG A 832       2.993  22.627  47.243  1.00 77.01           N  
ANISOU  681  NH1 ARG A 832     9561   7880  11819  -1067     55   -172       N  
ATOM    682  NH2 ARG A 832       0.862  22.305  48.014  1.00 85.03           N  
ANISOU  682  NH2 ARG A 832    10454   8818  13035  -1397    237   -114       N  
ATOM    683  N   ILE A 833       8.009  26.600  46.829  1.00 63.14           N  
ANISOU  683  N   ILE A 833     7812   6801   9377   -342    -82   -169       N  
ATOM    684  CA  ILE A 833       9.308  27.237  46.652  1.00 61.62           C  
ANISOU  684  CA  ILE A 833     7614   6713   9084   -186   -124   -177       C  
ATOM    685  C   ILE A 833       9.412  28.164  45.422  1.00 63.92           C  
ANISOU  685  C   ILE A 833     7797   7166   9322   -107   -132   -325       C  
ATOM    686  O   ILE A 833       9.130  27.734  44.308  1.00 63.67           O  
ANISOU  686  O   ILE A 833     7742   7093   9356    -91   -172   -460       O  
ATOM    687  CB  ILE A 833      10.433  26.140  46.621  1.00 65.30           C  
ANISOU  687  CB  ILE A 833     8171   7015   9627    -74   -212   -162       C  
ATOM    688  CG1 ILE A 833      10.333  25.168  47.831  1.00 67.69           C  
ANISOU  688  CG1 ILE A 833     8608   7133   9979   -151   -222      1       C  
ATOM    689  CG2 ILE A 833      11.814  26.788  46.565  1.00 64.75           C  
ANISOU  689  CG2 ILE A 833     8072   7050   9479     81   -249   -159       C  
ATOM    690  CD1 ILE A 833      11.071  23.818  47.685  1.00 75.98           C  
ANISOU  690  CD1 ILE A 833     9750   7960  11159    -65   -319      3       C  
ATOM    691  N   MET A 834       9.913  29.395  45.627  1.00 57.71           N  
ANISOU  691  N   MET A 834     6965   6552   8409    -55   -101   -296       N  
ATOM    692  CA  MET A 834      10.252  30.335  44.558  1.00 55.99           C  
ANISOU  692  CA  MET A 834     6670   6483   8121     30   -106   -408       C  
ATOM    693  C   MET A 834      11.779  30.225  44.323  1.00 60.59           C  
ANISOU  693  C   MET A 834     7271   7064   8688    176   -143   -419       C  
ATOM    694  O   MET A 834      12.543  30.197  45.291  1.00 60.54           O  
ANISOU  694  O   MET A 834     7299   7037   8665    205   -157   -308       O  
ATOM    695  CB  MET A 834       9.900  31.755  44.959  1.00 57.27           C  
ANISOU  695  CB  MET A 834     6772   6816   8173     -7    -45   -366       C  
ATOM    696  CG  MET A 834       8.406  32.032  44.997  1.00 61.44           C  
ANISOU  696  CG  MET A 834     7242   7367   8734   -129     -1   -383       C  
ATOM    697  SD  MET A 834       8.132  33.706  45.606  1.00 63.96           S  
ANISOU  697  SD  MET A 834     7500   7868   8933   -150     78   -331       S  
ATOM    698  CE  MET A 834       8.598  34.651  44.156  1.00 59.10           C  
ANISOU  698  CE  MET A 834     6826   7380   8247    -40     31   -450       C  
ATOM    699  N   ILE A 835      12.222  30.111  43.047  1.00 56.79           N  
ANISOU  699  N   ILE A 835     6767   6595   8215    266   -160   -557       N  
ATOM    700  CA  ILE A 835      13.640  29.953  42.697  1.00 55.34           C  
ANISOU  700  CA  ILE A 835     6577   6405   8043    407   -171   -591       C  
ATOM    701  C   ILE A 835      14.155  31.122  41.839  1.00 57.39           C  
ANISOU  701  C   ILE A 835     6772   6840   8196    470   -123   -665       C  
ATOM    702  O   ILE A 835      13.627  31.396  40.765  1.00 56.38           O  
ANISOU  702  O   ILE A 835     6641   6763   8017    459   -108   -774       O  
ATOM    703  CB  ILE A 835      13.949  28.570  42.070  1.00 59.21           C  
ANISOU  703  CB  ILE A 835     7119   6720   8657    471   -211   -684       C  
ATOM    704  CG1 ILE A 835      13.377  27.427  42.952  1.00 59.76           C  
ANISOU  704  CG1 ILE A 835     7267   6601   8838    393   -259   -596       C  
ATOM    705  CG2 ILE A 835      15.479  28.389  41.875  1.00 60.08           C  
ANISOU  705  CG2 ILE A 835     7201   6816   8810    626   -211   -710       C  
ATOM    706  CD1 ILE A 835      12.995  26.233  42.218  1.00 63.73           C  
ANISOU  706  CD1 ILE A 835     7826   6937   9452    390   -294   -706       C  
ATOM    707  N   SER A 836      15.207  31.787  42.325  1.00 52.52           N  
ANISOU  707  N   SER A 836     6110   6303   7544    531   -106   -600       N  
ATOM    708  CA  SER A 836      15.820  32.950  41.688  1.00 50.53           C  
ANISOU  708  CA  SER A 836     5795   6207   7198    579    -50   -644       C  
ATOM    709  C   SER A 836      17.315  32.761  41.593  1.00 55.60           C  
ANISOU  709  C   SER A 836     6386   6838   7900    700    -39   -659       C  
ATOM    710  O   SER A 836      17.868  31.820  42.180  1.00 57.19           O  
ANISOU  710  O   SER A 836     6597   6916   8216    750    -94   -619       O  
ATOM    711  CB  SER A 836      15.568  34.193  42.550  1.00 49.84           C  
ANISOU  711  CB  SER A 836     5678   6241   7018    511    -35   -539       C  
ATOM    712  OG  SER A 836      14.186  34.461  42.695  1.00 59.40           O  
ANISOU  712  OG  SER A 836     6912   7469   8190    405    -31   -526       O  
ATOM    713  N   ASP A 837      17.992  33.715  40.947  1.00 50.63           N  
ANISOU  713  N   ASP A 837     5695   6337   7203    742     29   -705       N  
ATOM    714  CA  ASP A 837      19.442  33.719  40.918  1.00 52.20           C  
ANISOU  714  CA  ASP A 837     5812   6548   7476    846     55   -716       C  
ATOM    715  C   ASP A 837      19.950  34.129  42.280  1.00 56.54           C  
ANISOU  715  C   ASP A 837     6316   7116   8051    830    -12   -577       C  
ATOM    716  O   ASP A 837      19.269  34.871  43.005  1.00 54.81           O  
ANISOU  716  O   ASP A 837     6126   6958   7740    736    -32   -491       O  
ATOM    717  CB  ASP A 837      19.953  34.757  39.905  1.00 54.89           C  
ANISOU  717  CB  ASP A 837     6101   7028   7727    869    164   -789       C  
ATOM    718  CG  ASP A 837      20.001  34.285  38.469  1.00 62.04           C  
ANISOU  718  CG  ASP A 837     7047   7914   8611    924    245   -943       C  
ATOM    719  OD1 ASP A 837      19.803  33.070  38.235  1.00 63.06           O  
ANISOU  719  OD1 ASP A 837     7229   7910   8822    963    213  -1008       O  
ATOM    720  OD2 ASP A 837      20.227  35.129  37.581  1.00 64.25           O  
ANISOU  720  OD2 ASP A 837     7323   8304   8786    924    340   -997       O  
ATOM    721  N   TYR A 838      21.166  33.671  42.624  1.00 55.66           N  
ANISOU  721  N   TYR A 838     6132   6951   8066    926    -50   -560       N  
ATOM    722  CA  TYR A 838      21.829  34.067  43.847  1.00 54.79           C  
ANISOU  722  CA  TYR A 838     5976   6860   7982    923   -136   -438       C  
ATOM    723  C   TYR A 838      22.885  35.112  43.462  1.00 60.91           C  
ANISOU  723  C   TYR A 838     6619   7765   8761    958    -72   -471       C  
ATOM    724  O   TYR A 838      23.639  34.903  42.517  1.00 62.78           O  
ANISOU  724  O   TYR A 838     6775   8005   9076   1044      9   -574       O  
ATOM    725  CB  TYR A 838      22.449  32.866  44.576  1.00 57.22           C  
ANISOU  725  CB  TYR A 838     6288   7010   8444   1003   -255   -383       C  
ATOM    726  CG  TYR A 838      23.244  33.268  45.805  1.00 58.82           C  
ANISOU  726  CG  TYR A 838     6447   7232   8672   1008   -372   -260       C  
ATOM    727  CD1 TYR A 838      22.607  33.553  47.011  1.00 60.55           C  
ANISOU  727  CD1 TYR A 838     6773   7453   8779    907   -451   -130       C  
ATOM    728  CD2 TYR A 838      24.626  33.432  45.743  1.00 59.45           C  
ANISOU  728  CD2 TYR A 838     6374   7335   8879   1108   -400   -282       C  
ATOM    729  CE1 TYR A 838      23.325  33.974  48.128  1.00 61.07           C  
ANISOU  729  CE1 TYR A 838     6822   7542   8841    905   -572    -24       C  
ATOM    730  CE2 TYR A 838      25.353  33.859  46.852  1.00 60.33           C  
ANISOU  730  CE2 TYR A 838     6441   7468   9012   1107   -531   -175       C  
ATOM    731  CZ  TYR A 838      24.698  34.138  48.039  1.00 70.09           C  
ANISOU  731  CZ  TYR A 838     7811   8706  10115   1004   -624    -47       C  
ATOM    732  OH  TYR A 838      25.405  34.582  49.128  1.00 76.80           O  
ANISOU  732  OH  TYR A 838     8640   9579  10963    997   -767     51       O  
ATOM    733  N   ALA A 839      22.942  36.226  44.191  1.00 57.68           N  
ANISOU  733  N   ALA A 839     6190   7455   8269    888    -98   -390       N  
ATOM    734  CA  ALA A 839      23.948  37.273  43.982  1.00 57.17           C  
ANISOU  734  CA  ALA A 839     5999   7504   8218    901    -50   -406       C  
ATOM    735  C   ALA A 839      24.823  37.328  45.197  1.00 61.58           C  
ANISOU  735  C   ALA A 839     6496   8043   8860    917   -188   -310       C  
ATOM    736  O   ALA A 839      24.332  37.395  46.329  1.00 60.54           O  
ANISOU  736  O   ALA A 839     6458   7889   8656    853   -293   -207       O  
ATOM    737  CB  ALA A 839      23.284  38.630  43.775  1.00 56.61           C  
ANISOU  737  CB  ALA A 839     5965   7560   7984    798     23   -398       C  
ATOM    738  N   ASP A 840      26.121  37.281  44.963  1.00 60.76           N  
ANISOU  738  N   ASP A 840     6234   7944   8907   1003   -188   -348       N  
ATOM    739  CA  ASP A 840      27.137  37.409  45.993  1.00 62.20           C  
ANISOU  739  CA  ASP A 840     6322   8117   9196   1029   -335   -272       C  
ATOM    740  C   ASP A 840      27.120  38.889  46.340  1.00 65.69           C  
ANISOU  740  C   ASP A 840     6752   8689   9519    921   -320   -235       C  
ATOM    741  O   ASP A 840      27.568  39.732  45.565  1.00 66.47           O  
ANISOU  741  O   ASP A 840     6749   8881   9626    906   -197   -299       O  
ATOM    742  CB  ASP A 840      28.493  36.981  45.450  1.00 66.16           C  
ANISOU  742  CB  ASP A 840     6625   8592   9922   1154   -313   -346       C  
ATOM    743  CG  ASP A 840      29.526  36.907  46.532  1.00 85.19           C  
ANISOU  743  CG  ASP A 840     8928  10967  12475   1198   -505   -268       C  
ATOM    744  OD1 ASP A 840      29.199  36.383  47.630  1.00 87.45           O  
ANISOU  744  OD1 ASP A 840     9333  11168  12727   1189   -683   -160       O  
ATOM    745  OD2 ASP A 840      30.663  37.379  46.296  1.00 93.97           O  
ANISOU  745  OD2 ASP A 840     9839  12134  13732   1235   -483   -310       O  
ATOM    746  N   ALA A 841      26.478  39.207  47.449  1.00 60.05           N  
ANISOU  746  N   ALA A 841     6165   7974   8678    837   -425   -138       N  
ATOM    747  CA  ALA A 841      26.213  40.576  47.844  1.00 57.53           C  
ANISOU  747  CA  ALA A 841     5877   7760   8222    727   -408   -108       C  
ATOM    748  C   ALA A 841      26.022  40.669  49.330  1.00 60.52           C  
ANISOU  748  C   ALA A 841     6367   8110   8517    670   -571      1       C  
ATOM    749  O   ALA A 841      26.086  39.673  50.031  1.00 62.71           O  
ANISOU  749  O   ALA A 841     6705   8287   8834    711   -698     64       O  
ATOM    750  CB  ALA A 841      24.922  41.030  47.156  1.00 56.32           C  
ANISOU  750  CB  ALA A 841     5831   7652   7914    660   -264   -145       C  
ATOM    751  N   THR A 842      25.743  41.868  49.803  1.00 55.81           N  
ANISOU  751  N   THR A 842     5818   7595   7793    571   -564     22       N  
ATOM    752  CA  THR A 842      25.418  42.177  51.187  1.00 55.33           C  
ANISOU  752  CA  THR A 842     5896   7523   7602    496   -686    111       C  
ATOM    753  C   THR A 842      24.225  43.080  51.079  1.00 55.57           C  
ANISOU  753  C   THR A 842     6032   7616   7466    401   -556     93       C  
ATOM    754  O   THR A 842      24.172  43.935  50.196  1.00 53.73           O  
ANISOU  754  O   THR A 842     5728   7456   7232    383   -435     27       O  
ATOM    755  CB  THR A 842      26.637  42.697  52.012  1.00 69.76           C  
ANISOU  755  CB  THR A 842     7645   9371   9488    490   -853    145       C  
ATOM    756  OG1 THR A 842      26.197  43.481  53.133  1.00 72.52           O  
ANISOU  756  OG1 THR A 842     8144   9748   9661    388   -919    197       O  
ATOM    757  CG2 THR A 842      27.647  43.471  51.187  1.00 70.92           C  
ANISOU  757  CG2 THR A 842     7584   9591   9771    506   -794     69       C  
ATOM    758  N   SER A 843      23.204  42.827  51.873  1.00 51.24           N  
ANISOU  758  N   SER A 843     5652   7032   6786    345   -564    148       N  
ATOM    759  CA  SER A 843      22.006  43.647  51.787  1.00 48.76           C  
ANISOU  759  CA  SER A 843     5420   6769   6337    265   -436    124       C  
ATOM    760  C   SER A 843      22.236  45.026  52.349  1.00 51.66           C  
ANISOU  760  C   SER A 843     5803   7206   6619    195   -451    120       C  
ATOM    761  O   SER A 843      23.115  45.208  53.184  1.00 51.35           O  
ANISOU  761  O   SER A 843     5766   7164   6581    186   -587    158       O  
ATOM    762  CB  SER A 843      20.855  42.987  52.522  1.00 51.13           C  
ANISOU  762  CB  SER A 843     5881   7009   6537    218   -420    180       C  
ATOM    763  OG  SER A 843      21.008  43.179  53.915  1.00 57.04           O  
ANISOU  763  OG  SER A 843     6755   7743   7174    163   -522    255       O  
ATOM    764  N   LEU A 844      21.406  45.989  51.922  1.00 49.13           N  
ANISOU  764  N   LEU A 844     5502   6940   6226    147   -323     74       N  
ATOM    765  CA  LEU A 844      21.456  47.358  52.421  1.00 48.57           C  
ANISOU  765  CA  LEU A 844     5463   6920   6071     78   -318     60       C  
ATOM    766  C   LEU A 844      21.317  47.425  53.939  1.00 53.15           C  
ANISOU  766  C   LEU A 844     6196   7476   6522     17   -409    115       C  
ATOM    767  O   LEU A 844      22.200  47.991  54.554  1.00 53.91           O  
ANISOU  767  O   LEU A 844     6288   7588   6608    -10   -520    123       O  
ATOM    768  CB  LEU A 844      20.449  48.263  51.706  1.00 46.63           C  
ANISOU  768  CB  LEU A 844     5224   6713   5778     50   -170      6       C  
ATOM    769  CG  LEU A 844      20.548  49.750  52.003  1.00 51.04           C  
ANISOU  769  CG  LEU A 844     5803   7313   6278    -10   -152    -20       C  
ATOM    770  CD1 LEU A 844      22.032  50.278  51.886  1.00 52.36           C  
ANISOU  770  CD1 LEU A 844     5859   7504   6530    -12   -236    -28       C  
ATOM    771  CD2 LEU A 844      19.570  50.544  51.128  1.00 49.03           C  
ANISOU  771  CD2 LEU A 844     5544   7081   6006    -15    -17    -68       C  
ATOM    772  N   SER A 845      20.309  46.766  54.543  1.00 51.58           N  
ANISOU  772  N   SER A 845     6131   7235   6232     -9   -372    155       N  
ATOM    773  CA  SER A 845      20.158  46.774  56.009  1.00 54.59           C  
ANISOU  773  CA  SER A 845     6689   7591   6461    -73   -442    212       C  
ATOM    774  C   SER A 845      21.350  46.137  56.738  1.00 60.06           C  
ANISOU  774  C   SER A 845     7403   8243   7173    -48   -649    281       C  
ATOM    775  O   SER A 845      21.800  46.703  57.740  1.00 62.39           O  
ANISOU  775  O   SER A 845     7793   8547   7364    -98   -757    300       O  
ATOM    776  CB  SER A 845      18.825  46.180  56.466  1.00 59.29           C  
ANISOU  776  CB  SER A 845     7419   8146   6961   -115   -332    244       C  
ATOM    777  OG  SER A 845      18.689  44.824  56.089  1.00 70.58           O  
ANISOU  777  OG  SER A 845     8828   9511   8477    -69   -344    287       O  
ATOM    778  N   THR A 846      21.940  45.102  56.167  1.00 56.02           N  
ANISOU  778  N   THR A 846     6798   7684   6804     34   -718    310       N  
ATOM    779  CA  THR A 846      23.120  44.524  56.773  1.00 58.37           C  
ANISOU  779  CA  THR A 846     7080   7937   7160     78   -934    371       C  
ATOM    780  C   THR A 846      24.295  45.494  56.628  1.00 66.50           C  
ANISOU  780  C   THR A 846     7966   9028   8271     80  -1023    320       C  
ATOM    781  O   THR A 846      25.099  45.633  57.539  1.00 67.45           O  
ANISOU  781  O   THR A 846     8124   9137   8367     65  -1214    360       O  
ATOM    782  CB  THR A 846      23.496  43.188  56.132  1.00 61.70           C  
ANISOU  782  CB  THR A 846     7408   8285   7751    182   -975    396       C  
ATOM    783  OG1 THR A 846      22.628  42.171  56.628  1.00 64.16           O  
ANISOU  783  OG1 THR A 846     7865   8521   7993    166   -918    453       O  
ATOM    784  CG2 THR A 846      24.916  42.828  56.481  1.00 55.10           C  
ANISOU  784  CG2 THR A 846     6512   7400   7025    249  -1207    448       C  
ATOM    785  N   TYR A 847      24.395  46.170  55.486  1.00 63.40           N  
ANISOU  785  N   TYR A 847     7413   8697   7980     94   -891    236       N  
ATOM    786  CA  TYR A 847      25.494  47.108  55.283  1.00 63.86           C  
ANISOU  786  CA  TYR A 847     7326   8806   8132     82   -953    191       C  
ATOM    787  C   TYR A 847      25.394  48.264  56.267  1.00 68.21           C  
ANISOU  787  C   TYR A 847     8001   9386   8530    -20  -1005    184       C  
ATOM    788  O   TYR A 847      26.365  48.548  56.953  1.00 69.40           O  
ANISOU  788  O   TYR A 847     8129   9534   8704    -41  -1183    197       O  
ATOM    789  CB  TYR A 847      25.587  47.601  53.831  1.00 64.63           C  
ANISOU  789  CB  TYR A 847     7254   8955   8348    107   -788    114       C  
ATOM    790  CG  TYR A 847      26.988  48.036  53.443  1.00 69.58           C  
ANISOU  790  CG  TYR A 847     7679   9611   9148    123   -853     81       C  
ATOM    791  CD1 TYR A 847      27.574  49.169  54.008  1.00 71.83           C  
ANISOU  791  CD1 TYR A 847     7950   9927   9417     44   -934     65       C  
ATOM    792  CD2 TYR A 847      27.734  47.311  52.516  1.00 72.04           C  
ANISOU  792  CD2 TYR A 847     7810   9914   9649    214   -826     57       C  
ATOM    793  CE1 TYR A 847      28.876  49.550  53.685  1.00 73.65           C  
ANISOU  793  CE1 TYR A 847     7975  10179   9828     46   -996     35       C  
ATOM    794  CE2 TYR A 847      29.029  47.698  52.165  1.00 74.16           C  
ANISOU  794  CE2 TYR A 847     7871  10209  10097    225   -865     23       C  
ATOM    795  CZ  TYR A 847      29.594  48.819  52.751  1.00 83.20           C  
ANISOU  795  CZ  TYR A 847     8990  11386  11235    136   -951     15       C  
ATOM    796  OH  TYR A 847      30.870  49.196  52.409  1.00 88.51           O  
ANISOU  796  OH  TYR A 847     9441  12083  12107    135   -986    -20       O  
ATOM    797  N   LEU A 848      24.210  48.874  56.388  1.00 63.33           N  
ANISOU  797  N   LEU A 848     7515   8785   7761    -79   -860    160       N  
ATOM    798  CA  LEU A 848      23.969  50.000  57.282  1.00 63.41           C  
ANISOU  798  CA  LEU A 848     7661   8814   7618   -172   -875    136       C  
ATOM    799  C   LEU A 848      24.123  49.677  58.768  1.00 71.70           C  
ANISOU  799  C   LEU A 848     8901   9827   8513   -214  -1043    196       C  
ATOM    800  O   LEU A 848      24.722  50.468  59.498  1.00 72.52           O  
ANISOU  800  O   LEU A 848     9055   9942   8558   -273  -1168    176       O  
ATOM    801  CB  LEU A 848      22.598  50.634  57.013  1.00 61.53           C  
ANISOU  801  CB  LEU A 848     7506   8593   7279   -207   -666     91       C  
ATOM    802  CG  LEU A 848      22.424  51.350  55.679  1.00 63.29           C  
ANISOU  802  CG  LEU A 848     7584   8853   7610   -187   -522     28       C  
ATOM    803  CD1 LEU A 848      20.974  51.642  55.428  1.00 62.66           C  
ANISOU  803  CD1 LEU A 848     7582   8775   7452   -198   -345     -1       C  
ATOM    804  CD2 LEU A 848      23.292  52.602  55.576  1.00 61.61           C  
ANISOU  804  CD2 LEU A 848     7298   8665   7448   -234   -566    -19       C  
ATOM    805  N   SER A 849      23.649  48.527  59.210  1.00 71.26           N  
ANISOU  805  N   SER A 849     8969   9724   8384   -191  -1051    270       N  
ATOM    806  CA  SER A 849      23.757  48.198  60.620  1.00 73.42           C  
ANISOU  806  CA  SER A 849     9462   9956   8480   -236  -1202    343       C  
ATOM    807  C   SER A 849      25.084  47.570  61.052  1.00 80.30           C  
ANISOU  807  C   SER A 849    10286  10789   9436   -189  -1480    408       C  
ATOM    808  O   SER A 849      25.576  47.860  62.134  1.00 83.40           O  
ANISOU  808  O   SER A 849    10842  11163   9683   -240  -1655    445       O  
ATOM    809  CB  SER A 849      22.596  47.302  61.041  1.00 76.01           C  
ANISOU  809  CB  SER A 849     9963  10237   8680   -248  -1086    406       C  
ATOM    810  OG  SER A 849      22.790  45.985  60.578  1.00 86.77           O  
ANISOU  810  OG  SER A 849    11229  11550  10190   -165  -1101    459       O  
ATOM    811  N   GLU A 850      25.657  46.702  60.228  1.00 75.36           N  
ANISOU  811  N   GLU A 850     9445  10146   9043    -91  -1525    417       N  
ATOM    812  CA  GLU A 850      26.890  46.019  60.613  1.00 76.36           C  
ANISOU  812  CA  GLU A 850     9500  10223   9289    -26  -1788    479       C  
ATOM    813  C   GLU A 850      28.162  46.394  59.864  1.00 80.87           C  
ANISOU  813  C   GLU A 850     9777  10827  10122     30  -1869    420       C  
ATOM    814  O   GLU A 850      29.093  45.603  59.833  1.00 83.13           O  
ANISOU  814  O   GLU A 850     9956  11064  10567    116  -2043    465       O  
ATOM    815  CB  GLU A 850      26.704  44.506  60.508  1.00 77.72           C  
ANISOU  815  CB  GLU A 850     9709  10308   9514     59  -1807    567       C  
ATOM    816  CG  GLU A 850      25.518  43.960  61.279  1.00 86.48           C  
ANISOU  816  CG  GLU A 850    11111  11361  10388      4  -1771    654       C  
ATOM    817  CD  GLU A 850      25.130  42.564  60.836  1.00105.53           C  
ANISOU  817  CD  GLU A 850    13532  13697  12867     64  -1667    705       C  
ATOM    818  OE1 GLU A 850      25.926  41.918  60.129  1.00 94.86           O  
ANISOU  818  OE1 GLU A 850    12022  12293  11727    172  -1752    718       O  
ATOM    819  OE2 GLU A 850      24.029  42.110  61.196  1.00106.04           O  
ANISOU  819  OE2 GLU A 850    13757  13749  12783      0  -1494    724       O  
ATOM    820  N   PHE A 851      28.218  47.571  59.257  1.00 74.88           N  
ANISOU  820  N   PHE A 851     8885  10143   9424    -16  -1746    325       N  
ATOM    821  CA  PHE A 851      29.432  47.944  58.538  1.00 74.78           C  
ANISOU  821  CA  PHE A 851     8587  10156   9670     26  -1804    275       C  
ATOM    822  C   PHE A 851      30.659  48.082  59.442  1.00 85.55           C  
ANISOU  822  C   PHE A 851     9907  11497  11101     20  -2114    305       C  
ATOM    823  O   PHE A 851      31.747  47.727  59.035  1.00 86.51           O  
ANISOU  823  O   PHE A 851     9821  11595  11455    108  -2232    314       O  
ATOM    824  CB  PHE A 851      29.231  49.138  57.589  1.00 73.49           C  
ANISOU  824  CB  PHE A 851     8298  10064   9560    -30  -1611    180       C  
ATOM    825  CG  PHE A 851      29.340  50.475  58.248  1.00 73.98           C  
ANISOU  825  CG  PHE A 851     8463  10156   9491   -151  -1651    140       C  
ATOM    826  CD1 PHE A 851      28.242  51.057  58.841  1.00 75.95           C  
ANISOU  826  CD1 PHE A 851     8938  10410   9508   -218  -1528    129       C  
ATOM    827  CD2 PHE A 851      30.543  51.142  58.279  1.00 76.58           C  
ANISOU  827  CD2 PHE A 851     8656  10500   9943   -199  -1808    106       C  
ATOM    828  CE1 PHE A 851      28.342  52.287  59.452  1.00 77.41           C  
ANISOU  828  CE1 PHE A 851     9230  10610   9574   -324  -1563     81       C  
ATOM    829  CE2 PHE A 851      30.653  52.371  58.888  1.00 79.18           C  
ANISOU  829  CE2 PHE A 851     9094  10841  10149   -316  -1858     61       C  
ATOM    830  CZ  PHE A 851      29.550  52.945  59.476  1.00 76.55           C  
ANISOU  830  CZ  PHE A 851     9001  10508   9575   -374  -1731     46       C  
ATOM    831  N   ASP A 852      30.493  48.628  60.644  1.00 86.34           N  
ANISOU  831  N   ASP A 852    10209  11601  10997    -79  -2250    316       N  
ATOM    832  CA  ASP A 852      31.612  48.796  61.568  1.00 90.20           C  
ANISOU  832  CA  ASP A 852    10697  12067  11507   -104  -2573    340       C  
ATOM    833  C   ASP A 852      32.214  47.477  62.044  1.00 97.87           C  
ANISOU  833  C   ASP A 852    11714  12959  12512     -8  -2811    448       C  
ATOM    834  O   ASP A 852      33.428  47.329  62.103  1.00 99.39           O  
ANISOU  834  O   ASP A 852    11721  13130  12911     44  -3046    458       O  
ATOM    835  CB  ASP A 852      31.192  49.638  62.772  1.00 92.79           C  
ANISOU  835  CB  ASP A 852    11280  12410  11566   -235  -2640    318       C  
ATOM    836  N   GLU A 853      31.358  46.513  62.363  1.00 95.96           N  
ANISOU  836  N   GLU A 853    11706  12666  12087     15  -2747    530       N  
ATOM    837  CA  GLU A 853      31.818  45.216  62.840  1.00 98.34           C  
ANISOU  837  CA  GLU A 853    12101  12871  12393    103  -2942    650       C  
ATOM    838  C   GLU A 853      32.628  44.510  61.772  1.00103.45           C  
ANISOU  838  C   GLU A 853    12467  13480  13361    248  -2918    648       C  
ATOM    839  O   GLU A 853      33.652  43.901  62.053  1.00104.45           O  
ANISOU  839  O   GLU A 853    12595  13515  13578    345  -3122    735       O  
ATOM    840  CB  GLU A 853      30.636  44.344  63.259  1.00 99.20           C  
ANISOU  840  CB  GLU A 853    12532  12936  12222     66  -2816    729       C  
ATOM    841  N   ARG A 854      32.155  44.602  60.539  1.00 98.87           N  
ANISOU  841  N   ARG A 854    11664  12961  12940    265  -2664    548       N  
ATOM    842  CA  ARG A 854      32.813  44.000  59.389  1.00 98.33           C  
ANISOU  842  CA  ARG A 854    11321  12871  13169    394  -2591    514       C  
ATOM    843  C   ARG A 854      33.952  44.872  58.871  1.00103.30           C  
ANISOU  843  C   ARG A 854    11639  13560  14050    395  -2648    427       C  
ATOM    844  O   ARG A 854      34.186  45.963  59.366  1.00103.82           O  
ANISOU  844  O   ARG A 854    11724  13669  14055    298  -2778    408       O  
ATOM    845  CB  ARG A 854      31.795  43.697  58.296  1.00 93.22           C  
ANISOU  845  CB  ARG A 854    10675  12249  12497    404  -2257    463       C  
ATOM    846  CG  ARG A 854      30.588  42.940  58.818  1.00 98.72           C  
ANISOU  846  CG  ARG A 854    11615  12868  13027    419  -2206    546       C  
ATOM    847  CD  ARG A 854      29.546  42.689  57.743  1.00105.98           C  
ANISOU  847  CD  ARG A 854    12555  13821  13890    399  -1896    489       C  
ATOM    848  NE  ARG A 854      28.383  41.994  58.284  1.00114.18           N  
ANISOU  848  NE  ARG A 854    13833  14789  14759    383  -1844    565       N  
ATOM    849  CZ  ARG A 854      27.874  40.883  57.770  1.00127.99           C  
ANISOU  849  CZ  ARG A 854    15579  16453  16598    464  -1793    591       C  
ATOM    850  NH1 ARG A 854      28.424  40.344  56.693  1.00122.12           N  
ANISOU  850  NH1 ARG A 854    14610  15687  16103    579  -1779    537       N  
ATOM    851  NH2 ARG A 854      26.817  40.315  58.329  1.00106.23           N  
ANISOU  851  NH2 ARG A 854    13045  13631  13688    427  -1742    664       N  
ATOM    852  N   ASN A 855      34.723  44.357  57.930  1.00 99.33           N  
ANISOU  852  N   ASN A 855    10855  13055  13832    500  -2550    372       N  
ATOM    853  CA  ASN A 855      35.813  45.141  57.373  1.00 99.93           C  
ANISOU  853  CA  ASN A 855    10612  13185  14170    498  -2564    288       C  
ATOM    854  C   ASN A 855      35.339  46.402  56.639  1.00100.27           C  
ANISOU  854  C   ASN A 855    10569  13320  14209    429  -2232    191       C  
ATOM    855  O   ASN A 855      35.950  47.460  56.740  1.00101.25           O  
ANISOU  855  O   ASN A 855    10421  13475  14573    470  -2106    118       O  
ATOM    856  CB  ASN A 855      36.651  44.279  56.432  1.00102.31           C  
ANISOU  856  CB  ASN A 855    10646  13424  14802    655  -2671    284       C  
ATOM    857  N   LEU A 856      34.240  46.270  55.909  1.00 91.45           N  
ANISOU  857  N   LEU A 856     9690  12241  12817    326  -2091    193       N  
ATOM    858  CA  LEU A 856      33.661  47.339  55.090  1.00 87.81           C  
ANISOU  858  CA  LEU A 856     9200  11851  12313    262  -1799    119       C  
ATOM    859  C   LEU A 856      33.689  48.792  55.566  1.00 87.76           C  
ANISOU  859  C   LEU A 856     9207  11903  12236    121  -1803     78       C  
ATOM    860  O   LEU A 856      33.388  49.094  56.711  1.00 87.48           O  
ANISOU  860  O   LEU A 856     9364  11855  12017     45  -1956    111       O  
ATOM    861  CB  LEU A 856      32.218  46.981  54.729  1.00 85.93           C  
ANISOU  861  CB  LEU A 856     9192  11605  11854    264  -1612    139       C  
ATOM    862  CG  LEU A 856      31.910  45.498  54.534  1.00 90.33           C  
ANISOU  862  CG  LEU A 856     9741  12101  12478    389  -1545    160       C  
ATOM    863  CD1 LEU A 856      30.410  45.261  54.516  1.00 88.06           C  
ANISOU  863  CD1 LEU A 856     9710  11791  11959    365  -1437    198       C  
ATOM    864  CD2 LEU A 856      32.558  44.977  53.263  1.00 92.94           C  
ANISOU  864  CD2 LEU A 856     9849  12462  13003    455  -1341     77       C  
ATOM    865  N   PRO A 857      34.049  49.679  54.644  1.00 81.16           N  
ANISOU  865  N   PRO A 857     8187  11121  11530     78  -1626      6       N  
ATOM    866  CA  PRO A 857      34.048  51.136  54.876  1.00 78.60           C  
ANISOU  866  CA  PRO A 857     7901  10834  11129    -64  -1609    -31       C  
ATOM    867  C   PRO A 857      32.597  51.672  54.759  1.00 74.36           C  
ANISOU  867  C   PRO A 857     7617  10311  10327   -118  -1426    -32       C  
ATOM    868  O   PRO A 857      31.782  51.058  54.066  1.00 70.78           O  
ANISOU  868  O   PRO A 857     7221   9857   9816    -52  -1257    -23       O  
ATOM    869  CB  PRO A 857      34.899  51.669  53.722  1.00 80.75           C  
ANISOU  869  CB  PRO A 857     7899  11147  11636    -82  -1449    -95       C  
ATOM    870  CG  PRO A 857      34.675  50.705  52.611  1.00 85.02           C  
ANISOU  870  CG  PRO A 857     8365  11689  12248     36  -1256   -102       C  
ATOM    871  CD  PRO A 857      34.390  49.356  53.237  1.00 81.69           C  
ANISOU  871  CD  PRO A 857     8043  11211  11785    148  -1407    -44       C  
ATOM    872  N   PRO A 858      32.228  52.813  55.379  1.00 67.25           N  
ANISOU  872  N   PRO A 858     6861   9416   9275   -233  -1450    -51       N  
ATOM    873  CA  PRO A 858      30.855  53.314  55.183  1.00 63.40           C  
ANISOU  873  CA  PRO A 858     6580   8936   8573   -268  -1262    -60       C  
ATOM    874  C   PRO A 858      30.571  53.631  53.713  1.00 65.07           C  
ANISOU  874  C   PRO A 858     6691   9179   8855   -252  -1002    -93       C  
ATOM    875  O   PRO A 858      31.500  53.799  52.906  1.00 67.95           O  
ANISOU  875  O   PRO A 858     6840   9564   9415   -250   -947   -119       O  
ATOM    876  CB  PRO A 858      30.809  54.583  56.034  1.00 65.47           C  
ANISOU  876  CB  PRO A 858     6965   9190   8719   -391  -1342    -93       C  
ATOM    877  CG  PRO A 858      32.240  54.968  56.256  1.00 72.21           C  
ANISOU  877  CG  PRO A 858     7623  10044   9768   -440  -1516   -116       C  
ATOM    878  CD  PRO A 858      33.033  53.717  56.236  1.00 68.97           C  
ANISOU  878  CD  PRO A 858     7054   9629   9523   -336  -1646    -76       C  
ATOM    879  N   LEU A 859      29.295  53.669  53.340  1.00 57.86           N  
ANISOU  879  N   LEU A 859     5930   8266   7786   -238   -840    -91       N  
ATOM    880  CA  LEU A 859      28.938  54.004  51.965  1.00 54.71           C  
ANISOU  880  CA  LEU A 859     5472   7893   7422   -225   -615   -117       C  
ATOM    881  C   LEU A 859      29.164  55.510  51.810  1.00 56.40           C  
ANISOU  881  C   LEU A 859     5677   8110   7643   -333   -563   -151       C  
ATOM    882  O   LEU A 859      28.801  56.283  52.703  1.00 55.61           O  
ANISOU  882  O   LEU A 859     5715   7986   7427   -404   -634   -161       O  
ATOM    883  CB  LEU A 859      27.476  53.654  51.651  1.00 52.71           C  
ANISOU  883  CB  LEU A 859     5381   7634   7013   -182   -487   -106       C  
ATOM    884  CG  LEU A 859      27.063  52.168  51.680  1.00 54.20           C  
ANISOU  884  CG  LEU A 859     5598   7806   7190    -85   -509    -74       C  
ATOM    885  CD1 LEU A 859      25.522  52.042  51.751  1.00 49.87           C  
ANISOU  885  CD1 LEU A 859     5230   7245   6473    -80   -416    -66       C  
ATOM    886  CD2 LEU A 859      27.653  51.391  50.481  1.00 51.05           C  
ANISOU  886  CD2 LEU A 859     5029   7420   6947     -3   -424    -90       C  
ATOM    887  N   SER A 860      29.841  55.918  50.723  1.00 50.99           N  
ANISOU  887  N   SER A 860     4831   7445   7098   -350   -441   -169       N  
ATOM    888  CA  SER A 860      30.066  57.332  50.447  1.00 49.16           C  
ANISOU  888  CA  SER A 860     4591   7202   6885   -458   -373   -192       C  
ATOM    889  C   SER A 860      28.731  57.981  50.040  1.00 51.15           C  
ANISOU  889  C   SER A 860     5029   7437   6968   -464   -234   -190       C  
ATOM    890  O   SER A 860      27.771  57.276  49.723  1.00 49.43           O  
ANISOU  890  O   SER A 860     4897   7229   6656   -383   -169   -176       O  
ATOM    891  CB  SER A 860      31.072  57.486  49.316  1.00 49.67           C  
ANISOU  891  CB  SER A 860     4447   7291   7133   -474   -247   -202       C  
ATOM    892  OG  SER A 860      30.558  56.918  48.122  1.00 51.89           O  
ANISOU  892  OG  SER A 860     4736   7596   7382   -395    -66   -195       O  
ATOM    893  N   ALA A 861      28.705  59.310  49.943  1.00 55.14           N  
ANISOU  893  N   ALA A 861     5265   7907   7781  -1023   -196   -422       N  
ATOM    894  CA  ALA A 861      27.530  60.056  49.477  1.00 52.67           C  
ANISOU  894  CA  ALA A 861     5078   7480   7455   -974    -47   -517       C  
ATOM    895  C   ALA A 861      27.095  59.622  48.039  1.00 53.32           C  
ANISOU  895  C   ALA A 861     5147   7519   7594   -787     89   -419       C  
ATOM    896  O   ALA A 861      25.892  59.461  47.784  1.00 53.70           O  
ANISOU  896  O   ALA A 861     5301   7535   7569   -700    164   -460       O  
ATOM    897  CB  ALA A 861      27.831  61.548  49.512  1.00 54.07           C  
ANISOU  897  CB  ALA A 861     5254   7543   7746  -1095    -10   -602       C  
ATOM    898  N   GLY A 862      28.070  59.398  47.157  1.00 46.66           N  
ANISOU  898  N   GLY A 862     4173   6684   6873   -735    117   -295       N  
ATOM    899  CA  GLY A 862      27.856  59.011  45.762  1.00 43.96           C  
ANISOU  899  CA  GLY A 862     3820   6313   6568   -579    245   -204       C  
ATOM    900  C   GLY A 862      27.268  57.634  45.597  1.00 45.49           C  
ANISOU  900  C   GLY A 862     4056   6574   6656   -453    239   -174       C  
ATOM    901  O   GLY A 862      26.370  57.425  44.778  1.00 46.17           O  
ANISOU  901  O   GLY A 862     4220   6627   6696   -344    328   -173       O  
ATOM    902  N   GLN A 863      27.722  56.701  46.415  1.00 42.32           N  
ANISOU  902  N   GLN A 863     3605   6260   6215   -476    121   -148       N  
ATOM    903  CA  GLN A 863      27.245  55.310  46.423  1.00 41.47           C  
ANISOU  903  CA  GLN A 863     3530   6203   6022   -373    100   -115       C  
ATOM    904  C   GLN A 863      25.818  55.224  46.840  1.00 47.10           C  
ANISOU  904  C   GLN A 863     4393   6904   6597   -365    110   -206       C  
ATOM    905  O   GLN A 863      25.067  54.462  46.236  1.00 49.18           O  
ANISOU  905  O   GLN A 863     4709   7160   6817   -255    166   -195       O  
ATOM    906  CB  GLN A 863      28.142  54.432  47.310  1.00 43.78           C  
ANISOU  906  CB  GLN A 863     3727   6581   6326   -411    -45    -45       C  
ATOM    907  CG  GLN A 863      29.557  54.261  46.711  1.00 46.16           C  
ANISOU  907  CG  GLN A 863     3843   6892   6803   -379    -35     66       C  
ATOM    908  CD  GLN A 863      30.511  53.554  47.633  1.00 60.85           C  
ANISOU  908  CD  GLN A 863     5581   8830   8708   -425   -201    148       C  
ATOM    909  OE1 GLN A 863      30.439  53.621  48.870  1.00 50.06           O  
ANISOU  909  OE1 GLN A 863     4255   7521   7245   -541   -353    122       O  
ATOM    910  NE2 GLN A 863      31.452  52.890  47.028  1.00 52.07           N  
ANISOU  910  NE2 GLN A 863     4315   7721   7747   -334   -172    254       N  
ATOM    911  N   ARG A 864      25.421  56.055  47.830  1.00 44.27           N  
ANISOU  911  N   ARG A 864     4104   6538   6177   -487     70   -308       N  
ATOM    912  CA  ARG A 864      24.064  56.215  48.347  1.00 43.69           C  
ANISOU  912  CA  ARG A 864     4163   6445   5991   -500    103   -416       C  
ATOM    913  C   ARG A 864      23.189  56.785  47.238  1.00 47.73           C  
ANISOU  913  C   ARG A 864     4717   6864   6555   -404    232   -438       C  
ATOM    914  O   ARG A 864      22.121  56.240  46.996  1.00 45.91           O  
ANISOU  914  O   ARG A 864     4547   6630   6267   -326    271   -455       O  
ATOM    915  CB  ARG A 864      24.050  57.145  49.584  1.00 43.94           C  
ANISOU  915  CB  ARG A 864     4251   6479   5966   -661     53   -534       C  
ATOM    916  CG  ARG A 864      24.616  56.493  50.843  1.00 47.85           C  
ANISOU  916  CG  ARG A 864     4744   7087   6349   -766    -95   -518       C  
ATOM    917  CD  ARG A 864      25.045  57.515  51.896  1.00 48.46           C  
ANISOU  917  CD  ARG A 864     4852   7174   6385   -948   -165   -625       C  
ATOM    918  NE  ARG A 864      26.091  56.972  52.765  1.00 59.29           N  
ANISOU  918  NE  ARG A 864     6166   8662   7701  -1046   -345   -555       N  
ATOM    919  CZ  ARG A 864      25.934  56.593  54.032  1.00 69.81           C  
ANISOU  919  CZ  ARG A 864     7584  10091   8848  -1154   -451   -588       C  
ATOM    920  NH1 ARG A 864      24.746  56.676  54.617  1.00 58.67           N  
ANISOU  920  NH1 ARG A 864     6325   8678   7287  -1180   -372   -705       N  
ATOM    921  NH2 ARG A 864      26.966  56.132  54.724  1.00 54.85           N  
ANISOU  921  NH2 ARG A 864     5621   8302   6919  -1239   -636   -497       N  
ATOM    922  N   LEU A 865      23.642  57.862  46.531  1.00 45.33           N  
ANISOU  922  N   LEU A 865     4374   6483   6367   -413    292   -424       N  
ATOM    923  CA  LEU A 865      22.863  58.354  45.401  1.00 44.28           C  
ANISOU  923  CA  LEU A 865     4279   6266   6279   -315    397   -410       C  
ATOM    924  C   LEU A 865      22.688  57.239  44.347  1.00 50.62           C  
ANISOU  924  C   LEU A 865     5074   7111   7047   -180    424   -323       C  
ATOM    925  O   LEU A 865      21.597  57.044  43.839  1.00 51.46           O  
ANISOU  925  O   LEU A 865     5242   7196   7113   -101    460   -338       O  
ATOM    926  CB  LEU A 865      23.523  59.582  44.736  1.00 44.26           C  
ANISOU  926  CB  LEU A 865     4234   6174   6407   -346    457   -372       C  
ATOM    927  CG  LEU A 865      22.785  60.138  43.475  1.00 46.85           C  
ANISOU  927  CG  LEU A 865     4604   6416   6779   -244    555   -323       C  
ATOM    928  CD1 LEU A 865      21.277  60.544  43.780  1.00 46.84           C  
ANISOU  928  CD1 LEU A 865     4690   6350   6756   -215    576   -416       C  
ATOM    929  CD2 LEU A 865      23.515  61.281  42.882  1.00 48.13           C  
ANISOU  929  CD2 LEU A 865     4728   6491   7069   -285    614   -264       C  
ATOM    930  N   ASN A 866      23.759  56.512  44.036  1.00 48.30           N  
ANISOU  930  N   ASN A 866     4700   6873   6778   -158    406   -240       N  
ATOM    931  CA  ASN A 866      23.743  55.455  43.031  1.00 47.04           C  
ANISOU  931  CA  ASN A 866     4537   6744   6593    -37    446   -175       C  
ATOM    932  C   ASN A 866      22.820  54.326  43.325  1.00 48.94           C  
ANISOU  932  C   ASN A 866     4838   7018   6739     13    408   -210       C  
ATOM    933  O   ASN A 866      22.109  53.908  42.421  1.00 50.52           O  
ANISOU  933  O   ASN A 866     5089   7206   6899    102    454   -207       O  
ATOM    934  CB  ASN A 866      25.135  54.949  42.771  1.00 53.80           C  
ANISOU  934  CB  ASN A 866     5279   7639   7524    -26    450    -93       C  
ATOM    935  CG  ASN A 866      25.657  55.587  41.531  1.00 93.05           C  
ANISOU  935  CG  ASN A 866    10220  12575  12561     11    563    -30       C  
ATOM    936  OD1 ASN A 866      25.547  55.011  40.444  1.00 97.91           O  
ANISOU  936  OD1 ASN A 866    10863  13199  13141    111    642      6       O  
ATOM    937  ND2 ASN A 866      26.055  56.858  41.646  1.00 82.97           N  
ANISOU  937  ND2 ASN A 866     8913  11248  11364    -76    581    -25       N  
ATOM    938  N   ILE A 867      22.814  53.827  44.571  1.00 44.97           N  
ANISOU  938  N   ILE A 867     4335   6558   6192    -52    321   -240       N  
ATOM    939  CA  ILE A 867      21.899  52.771  45.031  1.00 43.60           C  
ANISOU  939  CA  ILE A 867     4223   6412   5933    -26    287   -267       C  
ATOM    940  C   ILE A 867      20.484  53.232  44.802  1.00 48.44           C  
ANISOU  940  C   ILE A 867     4915   6982   6507     -6    336   -341       C  
ATOM    941  O   ILE A 867      19.692  52.481  44.256  1.00 49.24           O  
ANISOU  941  O   ILE A 867     5052   7080   6576     66    352   -343       O  
ATOM    942  CB  ILE A 867      22.155  52.412  46.519  1.00 46.12           C  
ANISOU  942  CB  ILE A 867     4540   6787   6196   -126    187   -275       C  
ATOM    943  CG1 ILE A 867      23.507  51.650  46.665  1.00 46.51           C  
ANISOU  943  CG1 ILE A 867     4489   6879   6303   -119    115   -173       C  
ATOM    944  CG2 ILE A 867      20.985  51.623  47.124  1.00 44.36           C  
ANISOU  944  CG2 ILE A 867     4399   6580   5876   -127    174   -314       C  
ATOM    945  CD1 ILE A 867      24.142  51.741  48.045  1.00 45.43           C  
ANISOU  945  CD1 ILE A 867     4327   6806   6129   -242     -9   -158       C  
ATOM    946  N   ALA A 868      20.181  54.477  45.194  1.00 45.99           N  
ANISOU  946  N   ALA A 868     4626   6632   6218    -70    358   -402       N  
ATOM    947  CA  ALA A 868      18.869  55.113  45.085  1.00 45.31           C  
ANISOU  947  CA  ALA A 868     4592   6489   6133    -52    409   -473       C  
ATOM    948  C   ALA A 868      18.403  55.174  43.649  1.00 48.31           C  
ANISOU  948  C   ALA A 868     4978   6833   6546     56    452   -424       C  
ATOM    949  O   ALA A 868      17.239  54.888  43.403  1.00 48.09           O  
ANISOU  949  O   ALA A 868     4980   6795   6498    104    458   -452       O  
ATOM    950  CB  ALA A 868      18.930  56.515  45.680  1.00 46.83           C  
ANISOU  950  CB  ALA A 868     4793   6623   6378   -136    436   -542       C  
ATOM    951  N   ILE A 869      19.316  55.465  42.689  1.00 44.79           N  
ANISOU  951  N   ILE A 869     4501   6376   6140     89    478   -346       N  
ATOM    952  CA  ILE A 869      18.977  55.563  41.260  1.00 43.95           C  
ANISOU  952  CA  ILE A 869     4418   6248   6033    181    517   -288       C  
ATOM    953  C   ILE A 869      18.701  54.184  40.661  1.00 48.67           C  
ANISOU  953  C   ILE A 869     5040   6900   6554    253    499   -276       C  
ATOM    954  O   ILE A 869      17.805  54.049  39.852  1.00 50.23           O  
ANISOU  954  O   ILE A 869     5279   7090   6715    312    497   -274       O  
ATOM    955  CB  ILE A 869      20.040  56.346  40.465  1.00 47.32           C  
ANISOU  955  CB  ILE A 869     4815   6649   6515    180    572   -207       C  
ATOM    956  CG1 ILE A 869      20.123  57.815  40.944  1.00 46.54           C  
ANISOU  956  CG1 ILE A 869     4704   6467   6513    108    593   -225       C  
ATOM    957  CG2 ILE A 869      19.834  56.211  38.920  1.00 45.63           C  
ANISOU  957  CG2 ILE A 869     4644   6442   6252    271    615   -132       C  
ATOM    958  CD1 ILE A 869      21.349  58.567  40.336  1.00 50.64           C  
ANISOU  958  CD1 ILE A 869     5177   6957   7107     79    649   -139       C  
ATOM    959  N   ASP A 870      19.470  53.186  41.042  1.00 44.92           N  
ANISOU  959  N   ASP A 870     4535   6469   6063    245    481   -267       N  
ATOM    960  CA  ASP A 870      19.301  51.801  40.622  1.00 45.71           C  
ANISOU  960  CA  ASP A 870     4658   6599   6113    305    469   -268       C  
ATOM    961  C   ASP A 870      17.952  51.247  41.103  1.00 52.44           C  
ANISOU  961  C   ASP A 870     5551   7449   6925    299    424   -330       C  
ATOM    962  O   ASP A 870      17.304  50.479  40.377  1.00 52.13           O  
ANISOU  962  O   ASP A 870     5551   7411   6845    352    416   -346       O  
ATOM    963  CB  ASP A 870      20.456  50.967  41.193  1.00 48.43           C  
ANISOU  963  CB  ASP A 870     4942   6971   6489    293    453   -235       C  
ATOM    964  CG  ASP A 870      21.791  51.138  40.453  1.00 65.14           C  
ANISOU  964  CG  ASP A 870     6997   9092   8660    323    517   -171       C  
ATOM    965  OD1 ASP A 870      21.897  52.063  39.595  1.00 65.68           O  
ANISOU  965  OD1 ASP A 870     7078   9145   8732    334    580   -145       O  
ATOM    966  OD2 ASP A 870      22.718  50.335  40.710  1.00 74.78           O  
ANISOU  966  OD2 ASP A 870     8153  10329   9931    338    511   -136       O  
ATOM    967  N   ILE A 871      17.513  51.647  42.322  1.00 47.80           N  
ANISOU  967  N   ILE A 871     4957   6858   6347    227    399   -373       N  
ATOM    968  CA  ILE A 871      16.227  51.169  42.821  1.00 46.75           C  
ANISOU  968  CA  ILE A 871     4851   6724   6188    214    379   -430       C  
ATOM    969  C   ILE A 871      15.085  51.857  42.061  1.00 48.45           C  
ANISOU  969  C   ILE A 871     5078   6905   6426    256    393   -453       C  
ATOM    970  O   ILE A 871      14.196  51.177  41.572  1.00 47.59           O  
ANISOU  970  O   ILE A 871     4983   6798   6300    292    369   -469       O  
ATOM    971  CB  ILE A 871      16.063  51.290  44.369  1.00 48.55           C  
ANISOU  971  CB  ILE A 871     5079   6969   6398    120    368   -473       C  
ATOM    972  CG1 ILE A 871      17.216  50.606  45.152  1.00 46.95           C  
ANISOU  972  CG1 ILE A 871     4861   6810   6168     74    323   -425       C  
ATOM    973  CG2 ILE A 871      14.683  50.741  44.812  1.00 47.95           C  
ANISOU  973  CG2 ILE A 871     5024   6893   6303    106    373   -526       C  
ATOM    974  CD1 ILE A 871      17.279  51.090  46.599  1.00 44.42           C  
ANISOU  974  CD1 ILE A 871     4556   6520   5803    -37    305   -464       C  
ATOM    975  N   ALA A 872      15.133  53.192  41.942  1.00 46.95           N  
ANISOU  975  N   ALA A 872     4876   6674   6287    251    423   -448       N  
ATOM    976  CA  ALA A 872      14.104  53.971  41.235  1.00 47.15           C  
ANISOU  976  CA  ALA A 872     4900   6654   6360    299    427   -446       C  
ATOM    977  C   ALA A 872      13.959  53.526  39.768  1.00 50.09           C  
ANISOU  977  C   ALA A 872     5301   7047   6684    375    395   -388       C  
ATOM    978  O   ALA A 872      12.837  53.461  39.285  1.00 49.59           O  
ANISOU  978  O   ALA A 872     5235   6978   6629    411    355   -395       O  
ATOM    979  CB  ALA A 872      14.385  55.456  41.339  1.00 47.78           C  
ANISOU  979  CB  ALA A 872     4967   6667   6521    282    469   -436       C  
ATOM    980  N   ARG A 873      15.073  53.148  39.112  1.00 44.71           N  
ANISOU  980  N   ARG A 873     4643   6396   5949    393    412   -339       N  
ATOM    981  CA  ARG A 873      15.128  52.653  37.728  1.00 46.11           C  
ANISOU  981  CA  ARG A 873     4870   6603   6046    454    402   -299       C  
ATOM    982  C   ARG A 873      14.276  51.376  37.579  1.00 53.17           C  
ANISOU  982  C   ARG A 873     5788   7525   6890    467    347   -356       C  
ATOM    983  O   ARG A 873      13.485  51.231  36.642  1.00 54.46           O  
ANISOU  983  O   ARG A 873     5986   7701   7004    501    297   -353       O  
ATOM    984  CB  ARG A 873      16.600  52.362  37.328  1.00 44.19           C  
ANISOU  984  CB  ARG A 873     4633   6384   5772    462    466   -257       C  
ATOM    985  CG  ARG A 873      16.794  51.736  35.930  1.00 50.13           C  
ANISOU  985  CG  ARG A 873     5454   7175   6421    518    487   -237       C  
ATOM    986  CD  ARG A 873      17.970  52.246  35.100  1.00 51.36           C  
ANISOU  986  CD  ARG A 873     5621   7342   6552    535    579   -163       C  
ATOM    987  NE  ARG A 873      19.133  52.652  35.903  1.00 58.36           N  
ANISOU  987  NE  ARG A 873     6425   8211   7538    495    632   -136       N  
ATOM    988  CZ  ARG A 873      19.756  53.815  35.758  1.00 72.22           C  
ANISOU  988  CZ  ARG A 873     8153   9942   9346    470    683    -66       C  
ATOM    989  NH1 ARG A 873      19.368  54.674  34.816  1.00 63.91           N  
ANISOU  989  NH1 ARG A 873     7156   8876   8253    489    698      1       N  
ATOM    990  NH2 ARG A 873      20.801  54.112  36.518  1.00 54.38           N  
ANISOU  990  NH2 ARG A 873     5809   7669   7182    420    713    -51       N  
ATOM    991  N   CYS A 874      14.452  50.464  38.516  1.00 51.26           N  
ANISOU  991  N   CYS A 874     5527   7287   6661    433    347   -401       N  
ATOM    992  CA  CYS A 874      13.750  49.195  38.583  1.00 52.19           C  
ANISOU  992  CA  CYS A 874     5662   7411   6758    430    305   -453       C  
ATOM    993  C   CYS A 874      12.226  49.408  38.843  1.00 53.88           C  
ANISOU  993  C   CYS A 874     5846   7613   7012    411    255   -491       C  
ATOM    994  O   CYS A 874      11.401  48.805  38.173  1.00 54.54           O  
ANISOU  994  O   CYS A 874     5945   7704   7072    425    200   -517       O  
ATOM    995  CB  CYS A 874      14.397  48.331  39.657  1.00 53.48           C  
ANISOU  995  CB  CYS A 874     5806   7570   6942    393    321   -462       C  
ATOM    996  SG  CYS A 874      13.562  46.761  39.922  1.00 58.75           S  
ANISOU  996  SG  CYS A 874     6492   8220   7610    375    280   -514       S  
ATOM    997  N   LEU A 875      11.866  50.264  39.806  1.00 48.85           N  
ANISOU  997  N   LEU A 875     5161   6957   6444    377    279   -500       N  
ATOM    998  CA  LEU A 875      10.474  50.553  40.090  1.00 49.11           C  
ANISOU  998  CA  LEU A 875     5143   6971   6544    367    258   -536       C  
ATOM    999  C   LEU A 875       9.842  51.269  38.930  1.00 52.03           C  
ANISOU  999  C   LEU A 875     5504   7333   6933    425    206   -497       C  
ATOM   1000  O   LEU A 875       8.678  51.019  38.660  1.00 53.05           O  
ANISOU 1000  O   LEU A 875     5592   7463   7100    433    148   -516       O  
ATOM   1001  CB  LEU A 875      10.335  51.393  41.358  1.00 49.80           C  
ANISOU 1001  CB  LEU A 875     5191   7033   6698    321    323   -569       C  
ATOM   1002  CG  LEU A 875      10.776  50.713  42.658  1.00 54.28           C  
ANISOU 1002  CG  LEU A 875     5773   7622   7228    247    360   -601       C  
ATOM   1003  CD1 LEU A 875      10.823  51.730  43.810  1.00 53.43           C  
ANISOU 1003  CD1 LEU A 875     5652   7497   7152    192    428   -644       C  
ATOM   1004  CD2 LEU A 875       9.852  49.501  42.978  1.00 55.25           C  
ANISOU 1004  CD2 LEU A 875     5883   7758   7350    217    342   -631       C  
ATOM   1005  N   ASP A 876      10.609  52.137  38.223  1.00 46.57           N  
ANISOU 1005  N   ASP A 876     4844   6633   6216    462    220   -431       N  
ATOM   1006  CA  ASP A 876      10.110  52.873  37.069  1.00 47.05           C  
ANISOU 1006  CA  ASP A 876     4911   6688   6279    517    163   -363       C  
ATOM   1007  C   ASP A 876       9.582  51.884  36.029  1.00 49.63           C  
ANISOU 1007  C   ASP A 876     5278   7067   6510    533     71   -370       C  
ATOM   1008  O   ASP A 876       8.476  52.066  35.527  1.00 50.06           O  
ANISOU 1008  O   ASP A 876     5297   7126   6599    554    -19   -352       O  
ATOM   1009  CB  ASP A 876      11.212  53.769  36.462  1.00 48.51           C  
ANISOU 1009  CB  ASP A 876     5143   6860   6429    540    209   -279       C  
ATOM   1010  CG  ASP A 876      10.765  54.583  35.269  1.00 61.26           C  
ANISOU 1010  CG  ASP A 876     6778   8467   8032    593    150   -180       C  
ATOM   1011  OD1 ASP A 876       9.875  55.444  35.435  1.00 66.46           O  
ANISOU 1011  OD1 ASP A 876     7372   9068   8810    617    119   -154       O  
ATOM   1012  OD2 ASP A 876      11.263  54.329  34.167  1.00 68.19           O  
ANISOU 1012  OD2 ASP A 876     7735   9394   8779    612    135   -127       O  
ATOM   1013  N   TYR A 877      10.371  50.836  35.754  1.00 45.13           N  
ANISOU 1013  N   TYR A 877     4778   6533   5836    521     92   -401       N  
ATOM   1014  CA  TYR A 877      10.081  49.786  34.791  1.00 46.09           C  
ANISOU 1014  CA  TYR A 877     4964   6697   5852    525     24   -435       C  
ATOM   1015  C   TYR A 877       8.869  48.969  35.221  1.00 50.66           C  
ANISOU 1015  C   TYR A 877     5487   7268   6492    487    -47   -506       C  
ATOM   1016  O   TYR A 877       8.040  48.660  34.381  1.00 51.38           O  
ANISOU 1016  O   TYR A 877     5590   7387   6543    487   -152   -518       O  
ATOM   1017  CB  TYR A 877      11.320  48.892  34.615  1.00 46.66           C  
ANISOU 1017  CB  TYR A 877     5109   6781   5839    525     99   -465       C  
ATOM   1018  CG  TYR A 877      11.041  47.569  33.940  1.00 49.86           C  
ANISOU 1018  CG  TYR A 877     5581   7203   6161    515     54   -543       C  
ATOM   1019  CD1 TYR A 877      10.843  47.491  32.559  1.00 52.21           C  
ANISOU 1019  CD1 TYR A 877     5968   7548   6321    531     -2   -545       C  
ATOM   1020  CD2 TYR A 877      10.976  46.385  34.679  1.00 50.07           C  
ANISOU 1020  CD2 TYR A 877     5592   7193   6241    482     66   -616       C  
ATOM   1021  CE1 TYR A 877      10.528  46.281  31.941  1.00 50.27           C  
ANISOU 1021  CE1 TYR A 877     5794   7311   5996    509    -48   -640       C  
ATOM   1022  CE2 TYR A 877      10.689  45.165  34.063  1.00 51.46           C  
ANISOU 1022  CE2 TYR A 877     5832   7362   6361    466     28   -699       C  
ATOM   1023  CZ  TYR A 877      10.495  45.116  32.693  1.00 62.40           C  
ANISOU 1023  CZ  TYR A 877     7307   8792   7610    478    -26   -723       C  
ATOM   1024  OH  TYR A 877      10.248  43.909  32.086  1.00 75.90           O  
ANISOU 1024  OH  TYR A 877     9093  10487   9259    452    -60   -827       O  
ATOM   1025  N   LEU A 878       8.795  48.602  36.520  1.00 46.39           N  
ANISOU 1025  N   LEU A 878     4890   6696   6041    446      7   -549       N  
ATOM   1026  CA  LEU A 878       7.725  47.811  37.092  1.00 46.58           C  
ANISOU 1026  CA  LEU A 878     4855   6706   6136    398    -29   -609       C  
ATOM   1027  C   LEU A 878       6.442  48.603  36.974  1.00 51.84           C  
ANISOU 1027  C   LEU A 878     5425   7370   6900    410    -94   -591       C  
ATOM   1028  O   LEU A 878       5.430  48.064  36.512  1.00 54.00           O  
ANISOU 1028  O   LEU A 878     5662   7657   7199    390   -189   -618       O  
ATOM   1029  CB  LEU A 878       8.010  47.480  38.594  1.00 46.20           C  
ANISOU 1029  CB  LEU A 878     4776   6632   6147    349     61   -633       C  
ATOM   1030  CG  LEU A 878       9.116  46.446  38.927  1.00 52.59           C  
ANISOU 1030  CG  LEU A 878     5651   7431   6899    333    107   -642       C  
ATOM   1031  CD1 LEU A 878       9.362  46.369  40.450  1.00 51.91           C  
ANISOU 1031  CD1 LEU A 878     5536   7333   6855    280    175   -637       C  
ATOM   1032  CD2 LEU A 878       8.764  45.063  38.426  1.00 56.97           C  
ANISOU 1032  CD2 LEU A 878     6243   7968   7436    313     58   -693       C  
ATOM   1033  N   HIS A 879       6.481  49.890  37.402  1.00 44.62           N  
ANISOU 1033  N   HIS A 879     4462   6430   6060    440    -43   -547       N  
ATOM   1034  CA  HIS A 879       5.310  50.749  37.421  1.00 44.15           C  
ANISOU 1034  CA  HIS A 879     4292   6347   6136    466    -81   -525       C  
ATOM   1035  C   HIS A 879       4.851  51.133  36.052  1.00 50.58           C  
ANISOU 1035  C   HIS A 879     5111   7187   6921    516   -214   -454       C  
ATOM   1036  O   HIS A 879       3.671  51.046  35.798  1.00 49.98           O  
ANISOU 1036  O   HIS A 879     4943   7116   6931    517   -308   -454       O  
ATOM   1037  CB  HIS A 879       5.498  51.999  38.314  1.00 42.92           C  
ANISOU 1037  CB  HIS A 879     4090   6133   6083    483     26   -514       C  
ATOM   1038  CG  HIS A 879       5.618  51.687  39.770  1.00 46.10           C  
ANISOU 1038  CG  HIS A 879     4477   6523   6517    420    142   -590       C  
ATOM   1039  ND1 HIS A 879       5.327  52.641  40.737  1.00 49.38           N  
ANISOU 1039  ND1 HIS A 879     4833   6886   7044    415    242   -623       N  
ATOM   1040  CD2 HIS A 879       5.990  50.536  40.392  1.00 46.94           C  
ANISOU 1040  CD2 HIS A 879     4627   6658   6551    356    172   -635       C  
ATOM   1041  CE1 HIS A 879       5.550  52.049  41.907  1.00 47.74           C  
ANISOU 1041  CE1 HIS A 879     4645   6695   6798    341    326   -687       C  
ATOM   1042  NE2 HIS A 879       5.935  50.775  41.745  1.00 46.84           N  
ANISOU 1042  NE2 HIS A 879     4589   6627   6580    306    281   -683       N  
ATOM   1043  N   ASN A 880       5.764  51.555  35.166  1.00 49.79           N  
ANISOU 1043  N   ASN A 880     5113   7107   6698    552   -224   -387       N  
ATOM   1044  CA  ASN A 880       5.373  52.074  33.849  1.00 50.65           C  
ANISOU 1044  CA  ASN A 880     5244   7247   6755    597   -352   -294       C  
ATOM   1045  C   ASN A 880       5.232  51.050  32.746  1.00 53.48           C  
ANISOU 1045  C   ASN A 880     5689   7683   6949    571   -468   -318       C  
ATOM   1046  O   ASN A 880       4.265  51.133  32.000  1.00 53.91           O  
ANISOU 1046  O   ASN A 880     5704   7769   7008    579   -619   -279       O  
ATOM   1047  CB  ASN A 880       6.323  53.186  33.426  1.00 48.01           C  
ANISOU 1047  CB  ASN A 880     4975   6891   6374    643   -296   -192       C  
ATOM   1048  CG  ASN A 880       6.123  54.390  34.304  1.00 58.26           C  
ANISOU 1048  CG  ASN A 880     6177   8096   7862    672   -221   -164       C  
ATOM   1049  OD1 ASN A 880       6.803  54.585  35.318  1.00 48.79           O  
ANISOU 1049  OD1 ASN A 880     4976   6855   6707    646    -92   -216       O  
ATOM   1050  ND2 ASN A 880       5.053  55.101  34.054  1.00 47.40           N  
ANISOU 1050  ND2 ASN A 880     4704   6685   6619    718   -305   -101       N  
ATOM   1051  N   GLU A 881       6.152  50.094  32.637  1.00 50.87           N  
ANISOU 1051  N   GLU A 881     5468   7377   6483    540   -406   -386       N  
ATOM   1052  CA  GLU A 881       6.098  49.137  31.533  1.00 52.60           C  
ANISOU 1052  CA  GLU A 881     5792   7659   6534    513   -498   -431       C  
ATOM   1053  C   GLU A 881       5.267  47.883  31.822  1.00 53.87           C  
ANISOU 1053  C   GLU A 881     5911   7814   6741    448   -563   -545       C  
ATOM   1054  O   GLU A 881       4.504  47.453  30.951  1.00 54.28           O  
ANISOU 1054  O   GLU A 881     5982   7913   6728    418   -710   -568       O  
ATOM   1055  CB  GLU A 881       7.527  48.777  31.063  1.00 54.45           C  
ANISOU 1055  CB  GLU A 881     6172   7914   6605    522   -387   -448       C  
ATOM   1056  CG  GLU A 881       7.925  49.511  29.779  1.00 72.38           C  
ANISOU 1056  CG  GLU A 881     8548  10244   8711    556   -418   -350       C  
ATOM   1057  CD  GLU A 881       8.200  51.005  29.879  1.00 97.78           C  
ANISOU 1057  CD  GLU A 881    11723  13432  11995    605   -379   -209       C  
ATOM   1058  OE1 GLU A 881       9.318  51.362  30.317  1.00111.43           O  
ANISOU 1058  OE1 GLU A 881    13466  15128  13743    619   -232   -190       O  
ATOM   1059  OE2 GLU A 881       7.322  51.817  29.495  1.00 76.14           O  
ANISOU 1059  OE2 GLU A 881     8933  10696   9301    629   -498   -114       O  
ATOM   1060  N   ARG A 882       5.405  47.307  33.029  1.00 47.67           N  
ANISOU 1060  N   ARG A 882     5073   6974   6064    418   -461   -609       N  
ATOM   1061  CA  ARG A 882       4.726  46.069  33.437  1.00 46.92           C  
ANISOU 1061  CA  ARG A 882     4942   6856   6031    347   -493   -707       C  
ATOM   1062  C   ARG A 882       3.407  46.278  34.196  1.00 52.31           C  
ANISOU 1062  C   ARG A 882     5455   7516   6903    318   -535   -704       C  
ATOM   1063  O   ARG A 882       2.532  45.396  34.187  1.00 51.80           O  
ANISOU 1063  O   ARG A 882     5341   7446   6895    253   -611   -767       O  
ATOM   1064  CB  ARG A 882       5.695  45.178  34.261  1.00 44.89           C  
ANISOU 1064  CB  ARG A 882     4737   6548   5770    327   -358   -762       C  
ATOM   1065  CG  ARG A 882       6.841  44.536  33.446  1.00 52.46           C  
ANISOU 1065  CG  ARG A 882     5846   7514   6572    347   -316   -800       C  
ATOM   1066  CD  ARG A 882       6.365  44.106  32.078  1.00 68.36           C  
ANISOU 1066  CD  ARG A 882     7944   9574   8458    326   -440   -852       C  
ATOM   1067  NE  ARG A 882       7.161  43.043  31.484  1.00 83.95           N  
ANISOU 1067  NE  ARG A 882    10052  11528  10317    319   -389   -944       N  
ATOM   1068  CZ  ARG A 882       6.855  41.752  31.538  1.00 92.20           C  
ANISOU 1068  CZ  ARG A 882    11124  12516  11393    261   -409  -1054       C  
ATOM   1069  NH1 ARG A 882       5.790  41.341  32.215  1.00 69.96           N  
ANISOU 1069  NH1 ARG A 882     8202   9663   8718    197   -475  -1076       N  
ATOM   1070  NH2 ARG A 882       7.619  40.862  30.933  1.00 84.98           N  
ANISOU 1070  NH2 ARG A 882    10336  11569  10382    266   -348  -1145       N  
ATOM   1071  N   VAL A 883       3.283  47.449  34.854  1.00 49.17           N  
ANISOU 1071  N   VAL A 883     4968   7100   6615    363   -474   -638       N  
ATOM   1072  CA  VAL A 883       2.149  47.884  35.670  1.00 48.81           C  
ANISOU 1072  CA  VAL A 883     4753   7025   6766    354   -465   -633       C  
ATOM   1073  C   VAL A 883       1.901  46.847  36.766  1.00 53.91           C  
ANISOU 1073  C   VAL A 883     5362   7639   7482    275   -380   -712       C  
ATOM   1074  O   VAL A 883       0.794  46.300  36.921  1.00 54.48           O  
ANISOU 1074  O   VAL A 883     5328   7706   7666    221   -432   -747       O  
ATOM   1075  CB  VAL A 883       0.884  48.275  34.850  1.00 53.05           C  
ANISOU 1075  CB  VAL A 883     5178   7589   7389    370   -635   -590       C  
ATOM   1076  CG1 VAL A 883      -0.099  49.050  35.716  1.00 52.93           C  
ANISOU 1076  CG1 VAL A 883     4975   7531   7606    392   -584   -570       C  
ATOM   1077  CG2 VAL A 883       1.263  49.079  33.619  1.00 52.85           C  
ANISOU 1077  CG2 VAL A 883     5233   7605   7242    436   -736   -496       C  
ATOM   1078  N   ILE A 884       2.984  46.535  37.483  1.00 50.66           N  
ANISOU 1078  N   ILE A 884     5040   7207   7000    264   -257   -728       N  
ATOM   1079  CA  ILE A 884       3.002  45.569  38.580  1.00 50.86           C  
ANISOU 1079  CA  ILE A 884     5062   7201   7063    192   -168   -774       C  
ATOM   1080  C   ILE A 884       3.769  46.223  39.747  1.00 53.59           C  
ANISOU 1080  C   ILE A 884     5422   7534   7404    202    -25   -751       C  
ATOM   1081  O   ILE A 884       4.902  46.679  39.560  1.00 49.94           O  
ANISOU 1081  O   ILE A 884     5044   7081   6851    245      2   -720       O  
ATOM   1082  CB  ILE A 884       3.676  44.228  38.145  1.00 54.52           C  
ANISOU 1082  CB  ILE A 884     5644   7649   7423    160   -193   -814       C  
ATOM   1083  CG1 ILE A 884       2.873  43.517  36.987  1.00 56.53           C  
ANISOU 1083  CG1 ILE A 884     5898   7913   7667    129   -342   -864       C  
ATOM   1084  CG2 ILE A 884       3.903  43.302  39.369  1.00 54.50           C  
ANISOU 1084  CG2 ILE A 884     5650   7601   7456     95    -94   -829       C  
ATOM   1085  CD1 ILE A 884       3.503  42.147  36.389  1.00 56.58           C  
ANISOU 1085  CD1 ILE A 884     6038   7885   7576     97   -364   -934       C  
ATOM   1086  N   PRO A 885       3.204  46.265  40.968  1.00 49.59           N  
ANISOU 1086  N   PRO A 885     4841   7013   6988    152     70   -770       N  
ATOM   1087  CA  PRO A 885       3.985  46.826  42.076  1.00 48.04           C  
ANISOU 1087  CA  PRO A 885     4683   6815   6755    144    192   -761       C  
ATOM   1088  C   PRO A 885       5.017  45.829  42.594  1.00 50.22           C  
ANISOU 1088  C   PRO A 885     5062   7090   6929    102    222   -749       C  
ATOM   1089  O   PRO A 885       4.815  44.621  42.480  1.00 50.73           O  
ANISOU 1089  O   PRO A 885     5145   7137   6995     61    188   -758       O  
ATOM   1090  CB  PRO A 885       2.917  47.144  43.156  1.00 49.53           C  
ANISOU 1090  CB  PRO A 885     4764   6994   7059     96    292   -796       C  
ATOM   1091  CG  PRO A 885       1.641  46.598  42.653  1.00 54.03           C  
ANISOU 1091  CG  PRO A 885     5226   7557   7744     76    224   -813       C  
ATOM   1092  CD  PRO A 885       1.880  45.785  41.423  1.00 49.79           C  
ANISOU 1092  CD  PRO A 885     4748   7026   7143     89     80   -803       C  
ATOM   1093  N   HIS A 886       6.109  46.323  43.180  1.00 43.98           N  
ANISOU 1093  N   HIS A 886     4331   6311   6067    109    278   -725       N  
ATOM   1094  CA  HIS A 886       7.020  45.447  43.908  1.00 43.78           C  
ANISOU 1094  CA  HIS A 886     4380   6287   5969     66    304   -696       C  
ATOM   1095  C   HIS A 886       6.207  44.989  45.174  1.00 49.28           C  
ANISOU 1095  C   HIS A 886     5045   6985   6696    -26    378   -708       C  
ATOM   1096  O   HIS A 886       5.991  43.805  45.350  1.00 48.50           O  
ANISOU 1096  O   HIS A 886     4960   6861   6605    -73    367   -692       O  
ATOM   1097  CB  HIS A 886       8.301  46.176  44.335  1.00 43.67           C  
ANISOU 1097  CB  HIS A 886     4415   6294   5884     81    334   -664       C  
ATOM   1098  CG  HIS A 886       9.285  45.281  45.020  1.00 46.98           C  
ANISOU 1098  CG  HIS A 886     4893   6718   6241     46    334   -615       C  
ATOM   1099  ND1 HIS A 886       9.086  44.841  46.319  1.00 49.46           N  
ANISOU 1099  ND1 HIS A 886     5220   7045   6527    -39    378   -598       N  
ATOM   1100  CD2 HIS A 886      10.452  44.776  44.566  1.00 49.07           C  
ANISOU 1100  CD2 HIS A 886     5199   6972   6474     87    296   -570       C  
ATOM   1101  CE1 HIS A 886      10.122  44.063  46.605  1.00 48.62           C  
ANISOU 1101  CE1 HIS A 886     5162   6935   6378    -43    345   -530       C  
ATOM   1102  NE2 HIS A 886      10.970  43.986  45.581  1.00 48.85           N  
ANISOU 1102  NE2 HIS A 886     5199   6944   6416     36    299   -516       N  
ATOM   1103  N   GLY A 887       5.849  45.950  46.017  1.00 47.11           N  
ANISOU 1103  N   GLY A 887     4729   6730   6442    -53    465   -740       N  
ATOM   1104  CA  GLY A 887       5.012  45.744  47.182  1.00 47.33           C  
ANISOU 1104  CA  GLY A 887     4725   6768   6489   -140    569   -763       C  
ATOM   1105  C   GLY A 887       5.684  45.186  48.407  1.00 51.26           C  
ANISOU 1105  C   GLY A 887     5312   7298   6867   -223    620   -722       C  
ATOM   1106  O   GLY A 887       5.081  45.085  49.466  1.00 51.48           O  
ANISOU 1106  O   GLY A 887     5333   7347   6879   -307    723   -737       O  
ATOM   1107  N   ASN A 888       6.949  44.834  48.258  1.00 45.46           N  
ANISOU 1107  N   ASN A 888     4656   6568   6047   -202    549   -662       N  
ATOM   1108  CA  ASN A 888       7.724  44.272  49.339  1.00 43.87           C  
ANISOU 1108  CA  ASN A 888     4535   6398   5734   -273    555   -594       C  
ATOM   1109  C   ASN A 888       9.009  45.036  49.550  1.00 47.71           C  
ANISOU 1109  C   ASN A 888     5070   6918   6141   -247    511   -571       C  
ATOM   1110  O   ASN A 888       9.991  44.477  50.003  1.00 47.36           O  
ANISOU 1110  O   ASN A 888     5074   6883   6039   -256    449   -489       O  
ATOM   1111  CB  ASN A 888       8.016  42.802  49.076  1.00 41.16           C  
ANISOU 1111  CB  ASN A 888     4213   6005   5420   -277    497   -521       C  
ATOM   1112  CG  ASN A 888       8.284  42.033  50.342  1.00 55.74           C  
ANISOU 1112  CG  ASN A 888     6132   7865   7184   -353    497   -422       C  
ATOM   1113  OD1 ASN A 888       7.946  42.479  51.427  1.00 46.49           O  
ANISOU 1113  OD1 ASN A 888     4991   6746   5926   -444    570   -411       O  
ATOM   1114  ND2 ASN A 888       8.904  40.877  50.209  1.00 48.52           N  
ANISOU 1114  ND2 ASN A 888     5245   6895   6294   -315    417   -343       N  
ATOM   1115  N   ILE A 889       9.017  46.308  49.190  1.00 44.63           N  
ANISOU 1115  N   ILE A 889     4652   6532   5774   -209    535   -639       N  
ATOM   1116  CA  ILE A 889      10.222  47.096  49.340  1.00 43.93           C  
ANISOU 1116  CA  ILE A 889     4592   6467   5632   -198    505   -633       C  
ATOM   1117  C   ILE A 889      10.651  47.237  50.791  1.00 49.05           C  
ANISOU 1117  C   ILE A 889     5307   7178   6153   -307    532   -628       C  
ATOM   1118  O   ILE A 889       9.884  47.657  51.647  1.00 46.90           O  
ANISOU 1118  O   ILE A 889     5049   6926   5843   -375    630   -700       O  
ATOM   1119  CB  ILE A 889      10.021  48.508  48.779  1.00 46.43           C  
ANISOU 1119  CB  ILE A 889     4867   6755   6020   -143    537   -704       C  
ATOM   1120  CG1 ILE A 889       9.585  48.448  47.319  1.00 43.97           C  
ANISOU 1120  CG1 ILE A 889     4500   6397   5809    -41    493   -697       C  
ATOM   1121  CG2 ILE A 889      11.286  49.331  48.946  1.00 46.14           C  
ANISOU 1121  CG2 ILE A 889     4860   6734   5937   -154    511   -699       C  
ATOM   1122  CD1 ILE A 889      10.547  47.697  46.437  1.00 60.98           C  
ANISOU 1122  CD1 ILE A 889     6676   8547   7945     19    413   -630       C  
ATOM   1123  N   LYS A 890      11.921  46.938  51.024  1.00 46.49           N  
ANISOU 1123  N   LYS A 890     5019   6883   5762   -322    443   -543       N  
ATOM   1124  CA  LYS A 890      12.553  47.017  52.322  1.00 46.97           C  
ANISOU 1124  CA  LYS A 890     5146   7016   5684   -427    422   -515       C  
ATOM   1125  C   LYS A 890      14.041  46.948  52.102  1.00 51.78           C  
ANISOU 1125  C   LYS A 890     5743   7640   6293   -400    304   -432       C  
ATOM   1126  O   LYS A 890      14.486  46.456  51.068  1.00 50.71           O  
ANISOU 1126  O   LYS A 890     5557   7456   6255   -303    259   -380       O  
ATOM   1127  CB  LYS A 890      12.027  45.936  53.305  1.00 49.79           C  
ANISOU 1127  CB  LYS A 890     5560   7407   5952   -511    441   -451       C  
ATOM   1128  CG  LYS A 890      12.171  44.501  52.818  1.00 53.22           C  
ANISOU 1128  CG  LYS A 890     5978   7792   6453   -460    375   -334       C  
ATOM   1129  CD  LYS A 890      11.545  43.509  53.798  1.00 58.71           C  
ANISOU 1129  CD  LYS A 890     6730   8505   7072   -551    409   -263       C  
ATOM   1130  CE  LYS A 890      10.039  43.480  53.755  1.00 39.02           C  
ANISOU 1130  CE  LYS A 890     4211   5986   4628   -576    538   -344       C  
ATOM   1131  NZ  LYS A 890       9.581  42.087  53.808  1.00 49.50           N  
ANISOU 1131  NZ  LYS A 890     5545   7263   5999   -596    534   -249       N  
ATOM   1132  N   SER A 891      14.816  47.477  53.042  1.00 49.54           N  
ANISOU 1132  N   SER A 891     5499   7423   5903   -488    259   -427       N  
ATOM   1133  CA  SER A 891      16.262  47.519  52.874  1.00 49.60           C  
ANISOU 1133  CA  SER A 891     5467   7447   5930   -470    142   -348       C  
ATOM   1134  C   SER A 891      16.882  46.124  52.819  1.00 51.02           C  
ANISOU 1134  C   SER A 891     5625   7620   6139   -429     48   -195       C  
ATOM   1135  O   SER A 891      17.946  45.971  52.230  1.00 48.96           O  
ANISOU 1135  O   SER A 891     5295   7340   5967   -362    -22   -129       O  
ATOM   1136  CB  SER A 891      16.915  48.420  53.919  1.00 53.32           C  
ANISOU 1136  CB  SER A 891     5981   7994   6283   -591     96   -386       C  
ATOM   1137  OG  SER A 891      16.462  48.093  55.218  1.00 60.78           O  
ANISOU 1137  OG  SER A 891     7024   9013   7058   -710    103   -382       O  
ATOM   1138  N   SER A 892      16.166  45.093  53.329  1.00 47.17           N  
ANISOU 1138  N   SER A 892     5187   7129   5604   -458     65   -141       N  
ATOM   1139  CA  SER A 892      16.675  43.730  53.261  1.00 46.07           C  
ANISOU 1139  CA  SER A 892     5030   6955   5520   -412    -15      7       C  
ATOM   1140  C   SER A 892      16.507  43.139  51.842  1.00 48.76           C  
ANISOU 1140  C   SER A 892     5310   7189   6027   -277     21     -7       C  
ATOM   1141  O   SER A 892      17.097  42.095  51.533  1.00 48.52           O  
ANISOU 1141  O   SER A 892     5250   7102   6084   -212    -33     94       O  
ATOM   1142  CB  SER A 892      16.034  42.854  54.327  1.00 47.50           C  
ANISOU 1142  CB  SER A 892     5293   7160   5596   -502    -11     84       C  
ATOM   1143  OG  SER A 892      14.691  42.575  53.977  1.00 58.19           O  
ANISOU 1143  OG  SER A 892     6661   8461   6987   -493    107     11       O  
ATOM   1144  N   ASN A 893      15.722  43.831  50.977  1.00 44.62           N  
ANISOU 1144  N   ASN A 893     4771   6635   5546   -236    110   -134       N  
ATOM   1145  CA  ASN A 893      15.465  43.423  49.595  1.00 43.26           C  
ANISOU 1145  CA  ASN A 893     4561   6382   5494   -126    142   -168       C  
ATOM   1146  C   ASN A 893      16.237  44.305  48.599  1.00 46.04           C  
ANISOU 1146  C   ASN A 893     4861   6731   5900    -51    144   -206       C  
ATOM   1147  O   ASN A 893      15.956  44.317  47.418  1.00 46.32           O  
ANISOU 1147  O   ASN A 893     4880   6721   5997     27    180   -256       O  
ATOM   1148  CB  ASN A 893      13.931  43.328  49.302  1.00 40.41           C  
ANISOU 1148  CB  ASN A 893     4217   5990   5146   -138    219   -254       C  
ATOM   1149  CG  ASN A 893      13.255  42.216  50.068  1.00 47.70           C  
ANISOU 1149  CG  ASN A 893     5179   6894   6049   -202    227   -198       C  
ATOM   1150  OD1 ASN A 893      13.895  41.284  50.515  1.00 45.40           O  
ANISOU 1150  OD1 ASN A 893     4907   6584   5760   -209    170    -87       O  
ATOM   1151  ND2 ASN A 893      11.942  42.259  50.229  1.00 46.11           N  
ANISOU 1151  ND2 ASN A 893     4984   6690   5846   -250    301   -263       N  
ATOM   1152  N   VAL A 894      17.212  45.032  49.092  1.00 44.38           N  
ANISOU 1152  N   VAL A 894     4629   6574   5661    -86    101   -179       N  
ATOM   1153  CA  VAL A 894      18.148  45.815  48.296  1.00 43.21           C  
ANISOU 1153  CA  VAL A 894     4422   6423   5573    -32    102   -188       C  
ATOM   1154  C   VAL A 894      19.527  45.132  48.530  1.00 51.63           C  
ANISOU 1154  C   VAL A 894     5429   7497   6692     -9     20    -69       C  
ATOM   1155  O   VAL A 894      20.003  45.111  49.675  1.00 53.54           O  
ANISOU 1155  O   VAL A 894     5672   7795   6875    -91    -63     -6       O  
ATOM   1156  CB  VAL A 894      18.157  47.318  48.697  1.00 43.89           C  
ANISOU 1156  CB  VAL A 894     4513   6551   5611   -103    120   -259       C  
ATOM   1157  CG1 VAL A 894      19.232  48.055  47.915  1.00 42.37           C  
ANISOU 1157  CG1 VAL A 894     4253   6350   5496    -59    120   -246       C  
ATOM   1158  CG2 VAL A 894      16.776  47.972  48.480  1.00 41.67           C  
ANISOU 1158  CG2 VAL A 894     4271   6247   5313   -109    206   -367       C  
ATOM   1159  N   LEU A 895      20.127  44.532  47.483  1.00 48.49           N  
ANISOU 1159  N   LEU A 895     4978   7042   6402     99     41    -38       N  
ATOM   1160  CA  LEU A 895      21.436  43.880  47.585  1.00 50.51           C  
ANISOU 1160  CA  LEU A 895     5150   7288   6752    143    -19     73       C  
ATOM   1161  C   LEU A 895      22.534  44.722  46.957  1.00 56.28           C  
ANISOU 1161  C   LEU A 895     5789   8037   7556    176      2     76       C  
ATOM   1162  O   LEU A 895      22.338  45.309  45.890  1.00 55.41           O  
ANISOU 1162  O   LEU A 895     5687   7908   7460    223     93      3       O  
ATOM   1163  CB  LEU A 895      21.447  42.442  47.027  1.00 51.05           C  
ANISOU 1163  CB  LEU A 895     5215   7264   6917    241      3    114       C  
ATOM   1164  CG  LEU A 895      20.419  41.451  47.628  1.00 56.55           C  
ANISOU 1164  CG  LEU A 895     5994   7923   7570    205    -16    130       C  
ATOM   1165  CD1 LEU A 895      20.486  40.115  46.926  1.00 56.41           C  
ANISOU 1165  CD1 LEU A 895     5971   7788   7672    304     17    150       C  
ATOM   1166  CD2 LEU A 895      20.586  41.283  49.135  1.00 60.05           C  
ANISOU 1166  CD2 LEU A 895     6451   8425   7941    106   -122    238       C  
ATOM   1167  N   ILE A 896      23.664  44.825  47.668  1.00 54.22           N  
ANISOU 1167  N   ILE A 896     5441   7820   7340    139    -91    168       N  
ATOM   1168  CA  ILE A 896      24.859  45.582  47.285  1.00 55.45           C  
ANISOU 1168  CA  ILE A 896     5481   7998   7589    149    -88    192       C  
ATOM   1169  C   ILE A 896      25.917  44.589  46.855  1.00 59.18           C  
ANISOU 1169  C   ILE A 896     5836   8424   8226    256    -89    290       C  
ATOM   1170  O   ILE A 896      26.313  43.780  47.669  1.00 56.53           O  
ANISOU 1170  O   ILE A 896     5460   8091   7927    251   -196    396       O  
ATOM   1171  CB  ILE A 896      25.448  46.445  48.465  1.00 59.96           C  
ANISOU 1171  CB  ILE A 896     6016   8656   8111     14   -211    223       C  
ATOM   1172  CG1 ILE A 896      24.415  47.412  49.127  1.00 58.76           C  
ANISOU 1172  CG1 ILE A 896     5987   8544   7796   -104   -206    114       C  
ATOM   1173  CG2 ILE A 896      26.724  47.200  48.016  1.00 62.30           C  
ANISOU 1173  CG2 ILE A 896     6170   8966   8535     17   -207    252       C  
ATOM   1174  CD1 ILE A 896      23.357  48.061  48.190  1.00 60.14           C  
ANISOU 1174  CD1 ILE A 896     6237   8669   7944    -65    -68     -7       C  
ATOM   1175  N   GLN A 897      26.423  44.718  45.635  1.00 60.43           N  
ANISOU 1175  N   GLN A 897     5935   8541   8483    350     33    262       N  
ATOM   1176  CA  GLN A 897      27.468  43.841  45.125  1.00 63.43           C  
ANISOU 1176  CA  GLN A 897     6184   8870   9046    462     74    335       C  
ATOM   1177  C   GLN A 897      28.595  44.654  44.492  1.00 74.48           C  
ANISOU 1177  C   GLN A 897     7455  10298  10545    468    139    346       C  
ATOM   1178  O   GLN A 897      28.378  45.759  44.009  1.00 74.00           O  
ANISOU 1178  O   GLN A 897     7440  10266  10409    419    202    276       O  
ATOM   1179  CB  GLN A 897      26.896  42.862  44.103  1.00 63.60           C  
ANISOU 1179  CB  GLN A 897     6271   8795   9098    584    199    277       C  
ATOM   1180  CG  GLN A 897      26.054  43.524  43.035  1.00 62.73           C  
ANISOU 1180  CG  GLN A 897     6297   8683   8856    584    307    145       C  
ATOM   1181  CD  GLN A 897      25.685  42.585  41.916  1.00 77.44           C  
ANISOU 1181  CD  GLN A 897     8215  10460  10746    693    426     78       C  
ATOM   1182  OE1 GLN A 897      25.750  41.374  42.068  1.00 83.63           O  
ANISOU 1182  OE1 GLN A 897     8989  11165  11621    756    418    105       O  
ATOM   1183  NE2 GLN A 897      25.293  43.142  40.782  1.00 58.93           N  
ANISOU 1183  NE2 GLN A 897     5945   8127   8319    712    535    -14       N  
ATOM   1184  N   ASN A 898      29.803  44.104  44.514  1.00 78.09           N  
ANISOU 1184  N   ASN A 898     7741  10738  11190    531    128    444       N  
ATOM   1185  CA  ASN A 898      30.965  44.765  43.931  1.00 79.81           C  
ANISOU 1185  CA  ASN A 898     7796  10974  11554    548    202    476       C  
ATOM   1186  C   ASN A 898      30.817  44.946  42.429  1.00 84.75           C  
ANISOU 1186  C   ASN A 898     8477  11559  12164    629    425    383       C  
ATOM   1187  O   ASN A 898      31.164  45.984  41.880  1.00 86.27           O  
ANISOU 1187  O   ASN A 898     8642  11786  12351    585    502    363       O  
ATOM   1188  CB  ASN A 898      32.233  43.965  44.227  1.00 79.03           C  
ANISOU 1188  CB  ASN A 898     7496  10845  11686    628    156    603       C  
ATOM   1189  N   SER A 899      30.285  43.920  41.780  1.00 78.52           N  
ANISOU 1189  N   SER A 899     7781  10697  11356    736    521    326       N  
ATOM   1190  CA  SER A 899      30.070  43.904  40.340  1.00 76.90           C  
ANISOU 1190  CA  SER A 899     7663  10454  11100    816    719    227       C  
ATOM   1191  C   SER A 899      28.913  44.787  39.899  1.00 77.03           C  
ANISOU 1191  C   SER A 899     7834  10516  10917    747    758    143       C  
ATOM   1192  O   SER A 899      28.113  45.207  40.707  1.00 73.82           O  
ANISOU 1192  O   SER A 899     7448  10160  10439    641    658    155       O  
ATOM   1193  CB  SER A 899      29.814  42.473  39.869  1.00 79.81           C  
ANISOU 1193  CB  SER A 899     8117  10731  11475    915    763    173       C  
ATOM   1194  N   THR A 900      28.871  45.115  38.617  1.00 75.64           N  
ANISOU 1194  N   THR A 900     7763  10318  10659    809    909     61       N  
ATOM   1195  CA  THR A 900      27.787  45.906  38.053  1.00 75.76           C  
ANISOU 1195  CA  THR A 900     7926  10368  10491    761    936     -3       C  
ATOM   1196  C   THR A 900      26.585  44.993  37.761  1.00 81.08           C  
ANISOU 1196  C   THR A 900     8762  11006  11040    787    905    -95       C  
ATOM   1197  O   THR A 900      26.765  43.921  37.189  1.00 82.30           O  
ANISOU 1197  O   THR A 900     8944  11103  11222    870    979   -145       O  
ATOM   1198  CB  THR A 900      28.234  46.578  36.746  1.00 82.11           C  
ANISOU 1198  CB  THR A 900     8731  11196  11269    783   1108     -5       C  
ATOM   1199  OG1 THR A 900      29.563  47.083  36.903  1.00 68.67           O  
ANISOU 1199  OG1 THR A 900     6849   9510   9734    772   1151     81       O  
ATOM   1200  CG2 THR A 900      27.307  47.722  36.390  1.00 87.69           C  
ANISOU 1200  CG2 THR A 900     9547  11942  11829    710   1089    -15       C  
ATOM   1201  N   PRO A 901      25.367  45.387  38.143  1.00 75.97           N  
ANISOU 1201  N   PRO A 901     8210  10382  10272    714    800   -123       N  
ATOM   1202  CA  PRO A 901      25.045  46.701  38.713  1.00 74.58           C  
ANISOU 1202  CA  PRO A 901     8020  10253  10063    617    722    -89       C  
ATOM   1203  C   PRO A 901      25.293  46.721  40.206  1.00 74.88           C  
ANISOU 1203  C   PRO A 901     7968  10305  10178    552    595    -31       C  
ATOM   1204  O   PRO A 901      25.126  45.704  40.858  1.00 77.62           O  
ANISOU 1204  O   PRO A 901     8295  10624  10573    577    538    -12       O  
ATOM   1205  CB  PRO A 901      23.555  46.845  38.425  1.00 74.87           C  
ANISOU 1205  CB  PRO A 901     8197  10293   9958    593    684   -159       C  
ATOM   1206  CG  PRO A 901      23.057  45.446  38.359  1.00 79.61           C  
ANISOU 1206  CG  PRO A 901     8855  10851  10542    638    663   -212       C  
ATOM   1207  CD  PRO A 901      24.161  44.654  37.731  1.00 76.73           C  
ANISOU 1207  CD  PRO A 901     8437  10448  10270    725    761   -205       C  
ATOM   1208  N   SER A 902      25.634  47.882  40.738  1.00 66.73           N  
ANISOU 1208  N   SER A 902     6889   9310   9157    465    549      0       N  
ATOM   1209  CA  SER A 902      26.015  48.000  42.150  1.00 65.42           C  
ANISOU 1209  CA  SER A 902     6651   9173   9033    381    417     47       C  
ATOM   1210  C   SER A 902      24.824  47.576  43.044  1.00 64.20           C  
ANISOU 1210  C   SER A 902     6599   9020   8773    338    324      6       C  
ATOM   1211  O   SER A 902      25.018  46.824  44.003  1.00 64.37           O  
ANISOU 1211  O   SER A 902     6592   9050   8815    317    229     55       O  
ATOM   1212  CB  SER A 902      26.463  49.428  42.465  1.00 68.47           C  
ANISOU 1212  CB  SER A 902     6989   9589   9439    284    400     58       C  
ATOM   1213  N   ALA A 903      23.592  47.961  42.660  1.00 54.85           N  
ANISOU 1213  N   ALA A 903     5529   7825   7486    331    356    -71       N  
ATOM   1214  CA  ALA A 903      22.427  47.570  43.440  1.00 52.80           C  
ANISOU 1214  CA  ALA A 903     5352   7565   7143    290    293   -113       C  
ATOM   1215  C   ALA A 903      21.412  46.692  42.677  1.00 52.74           C  
ANISOU 1215  C   ALA A 903     5427   7517   7094    357    333   -165       C  
ATOM   1216  O   ALA A 903      21.134  46.923  41.489  1.00 49.93           O  
ANISOU 1216  O   ALA A 903     5110   7147   6716    411    404   -203       O  
ATOM   1217  CB  ALA A 903      21.761  48.795  44.027  1.00 53.37           C  
ANISOU 1217  CB  ALA A 903     5465   7660   7154    199    273   -164       C  
ATOM   1218  N   LEU A 904      20.876  45.679  43.394  1.00 49.39           N  
ANISOU 1218  N   LEU A 904     5033   7077   6655    343    278   -160       N  
ATOM   1219  CA  LEU A 904      19.872  44.697  42.956  1.00 48.94           C  
ANISOU 1219  CA  LEU A 904     5048   6974   6574    379    293   -209       C  
ATOM   1220  C   LEU A 904      18.664  44.688  43.894  1.00 53.18           C  
ANISOU 1220  C   LEU A 904     5635   7523   7046    299    247   -238       C  
ATOM   1221  O   LEU A 904      18.821  44.757  45.109  1.00 52.85           O  
ANISOU 1221  O   LEU A 904     5582   7514   6984    227    194   -194       O  
ATOM   1222  CB  LEU A 904      20.462  43.290  42.915  1.00 49.61           C  
ANISOU 1222  CB  LEU A 904     5110   7000   6741    440    290   -165       C  
ATOM   1223  CG  LEU A 904      21.623  43.035  41.937  1.00 55.32           C  
ANISOU 1223  CG  LEU A 904     5777   7694   7549    535    365   -149       C  
ATOM   1224  CD1 LEU A 904      22.245  41.702  42.209  1.00 55.67           C  
ANISOU 1224  CD1 LEU A 904     5779   7666   7708    592    353    -93       C  
ATOM   1225  CD2 LEU A 904      21.149  43.064  40.472  1.00 56.07           C  
ANISOU 1225  CD2 LEU A 904     5945   7769   7590    591    457   -243       C  
ATOM   1226  N   VAL A 905      17.462  44.616  43.326  1.00 47.76           N  
ANISOU 1226  N   VAL A 905     5003   6817   6326    307    269   -310       N  
ATOM   1227  CA  VAL A 905      16.215  44.549  44.074  1.00 46.37           C  
ANISOU 1227  CA  VAL A 905     4860   6647   6113    238    250   -344       C  
ATOM   1228  C   VAL A 905      15.750  43.087  44.017  1.00 48.98           C  
ANISOU 1228  C   VAL A 905     5219   6918   6473    250    237   -342       C  
ATOM   1229  O   VAL A 905      15.794  42.457  42.948  1.00 49.27           O  
ANISOU 1229  O   VAL A 905     5274   6907   6539    316    255   -374       O  
ATOM   1230  CB  VAL A 905      15.179  45.538  43.488  1.00 49.43           C  
ANISOU 1230  CB  VAL A 905     5260   7047   6476    238    275   -416       C  
ATOM   1231  CG1 VAL A 905      13.777  45.293  44.054  1.00 47.99           C  
ANISOU 1231  CG1 VAL A 905     5090   6859   6285    182    273   -460       C  
ATOM   1232  CG2 VAL A 905      15.614  46.980  43.728  1.00 49.47           C  
ANISOU 1232  CG2 VAL A 905     5240   7086   6472    215    293   -414       C  
ATOM   1233  N   THR A 906      15.337  42.551  45.163  1.00 44.61           N  
ANISOU 1233  N   THR A 906     4678   6365   5908    180    212   -305       N  
ATOM   1234  CA  THR A 906      14.876  41.158  45.258  1.00 46.35           C  
ANISOU 1234  CA  THR A 906     4926   6514   6173    175    201   -288       C  
ATOM   1235  C   THR A 906      13.416  41.043  45.757  1.00 50.70           C  
ANISOU 1235  C   THR A 906     5496   7066   6700     95    215   -328       C  
ATOM   1236  O   THR A 906      12.824  42.033  46.152  1.00 50.25           O  
ANISOU 1236  O   THR A 906     5429   7069   6596     49    239   -367       O  
ATOM   1237  CB  THR A 906      15.782  40.364  46.248  1.00 49.48           C  
ANISOU 1237  CB  THR A 906     5313   6891   6595    160    158   -166       C  
ATOM   1238  OG1 THR A 906      15.444  40.693  47.587  1.00 48.53           O  
ANISOU 1238  OG1 THR A 906     5210   6835   6394     58    137   -121       O  
ATOM   1239  CG2 THR A 906      17.237  40.622  46.053  1.00 53.35           C  
ANISOU 1239  CG2 THR A 906     5751   7396   7124    222    138   -110       C  
ATOM   1240  N   ASP A 907      12.895  39.806  45.829  1.00 48.30           N  
ANISOU 1240  N   ASP A 907     5215   6688   6448     75    210   -315       N  
ATOM   1241  CA  ASP A 907      11.614  39.429  46.464  1.00 48.57           C  
ANISOU 1241  CA  ASP A 907     5257   6713   6484    -14    231   -326       C  
ATOM   1242  C   ASP A 907      10.447  40.327  46.088  1.00 52.37           C  
ANISOU 1242  C   ASP A 907     5704   7238   6955    -35    261   -424       C  
ATOM   1243  O   ASP A 907       9.807  40.936  46.959  1.00 52.27           O  
ANISOU 1243  O   ASP A 907     5676   7280   6906   -103    304   -431       O  
ATOM   1244  CB  ASP A 907      11.816  39.361  47.989  1.00 50.70           C  
ANISOU 1244  CB  ASP A 907     5547   7027   6690    -98    235   -226       C  
ATOM   1245  CG  ASP A 907      12.923  38.391  48.390  1.00 59.16           C  
ANISOU 1245  CG  ASP A 907     6638   8047   7791    -74    183   -101       C  
ATOM   1246  OD1 ASP A 907      12.782  37.197  48.110  1.00 62.33           O  
ANISOU 1246  OD1 ASP A 907     7055   8343   8284    -58    176    -74       O  
ATOM   1247  OD2 ASP A 907      13.956  38.848  48.930  1.00 54.15           O  
ANISOU 1247  OD2 ASP A 907     5997   7471   7106    -68    143    -33       O  
ATOM   1248  N   TYR A 908      10.220  40.456  44.762  1.00 48.05           N  
ANISOU 1248  N   TYR A 908     5147   6670   6440     29    239   -500       N  
ATOM   1249  CA  TYR A 908       9.204  41.347  44.218  1.00 47.62           C  
ANISOU 1249  CA  TYR A 908     5049   6653   6392     29    241   -575       C  
ATOM   1250  C   TYR A 908       7.875  40.684  44.031  1.00 54.22           C  
ANISOU 1250  C   TYR A 908     5853   7452   7298    -23    229   -622       C  
ATOM   1251  O   TYR A 908       7.800  39.515  43.652  1.00 56.24           O  
ANISOU 1251  O   TYR A 908     6137   7636   7597    -33    200   -632       O  
ATOM   1252  CB  TYR A 908       9.674  41.995  42.895  1.00 47.86           C  
ANISOU 1252  CB  TYR A 908     5089   6700   6397    117    209   -612       C  
ATOM   1253  CG  TYR A 908       9.938  41.031  41.753  1.00 48.34           C  
ANISOU 1253  CG  TYR A 908     5197   6705   6466    162    173   -648       C  
ATOM   1254  CD1 TYR A 908      11.140  40.326  41.670  1.00 50.55           C  
ANISOU 1254  CD1 TYR A 908     5520   6941   6747    206    190   -614       C  
ATOM   1255  CD2 TYR A 908       8.996  40.836  40.747  1.00 48.72           C  
ANISOU 1255  CD2 TYR A 908     5245   6741   6524    159    122   -722       C  
ATOM   1256  CE1 TYR A 908      11.379  39.418  40.640  1.00 51.37           C  
ANISOU 1256  CE1 TYR A 908     5675   6980   6864    248    181   -668       C  
ATOM   1257  CE2 TYR A 908       9.232  39.946  39.696  1.00 50.21           C  
ANISOU 1257  CE2 TYR A 908     5497   6880   6701    188     94   -778       C  
ATOM   1258  CZ  TYR A 908      10.427  39.244  39.646  1.00 56.47           C  
ANISOU 1258  CZ  TYR A 908     6342   7619   7495    235    136   -759       C  
ATOM   1259  OH  TYR A 908      10.674  38.381  38.611  1.00 56.16           O  
ANISOU 1259  OH  TYR A 908     6372   7520   7447    266    132   -835       O  
ATOM   1260  N   SER A 909       6.824  41.443  44.303  1.00 50.51           N  
ANISOU 1260  N   SER A 909     5315   7022   6856    -57    255   -655       N  
ATOM   1261  CA  SER A 909       5.414  41.159  44.000  1.00 50.12           C  
ANISOU 1261  CA  SER A 909     5193   6955   6897   -102    237   -707       C  
ATOM   1262  C   SER A 909       4.868  39.891  44.629  1.00 53.95           C  
ANISOU 1262  C   SER A 909     5676   7381   7441   -192    261   -687       C  
ATOM   1263  O   SER A 909       3.943  39.276  44.088  1.00 52.47           O  
ANISOU 1263  O   SER A 909     5443   7154   7340   -230    218   -733       O  
ATOM   1264  CB  SER A 909       5.215  41.161  42.485  1.00 50.91           C  
ANISOU 1264  CB  SER A 909     5292   7045   7007    -45    139   -762       C  
ATOM   1265  OG  SER A 909       5.882  42.279  41.922  1.00 49.91           O  
ANISOU 1265  OG  SER A 909     5183   6965   6814     36    126   -754       O  
ATOM   1266  N   LEU A 910       5.402  39.542  45.816  1.00 52.45           N  
ANISOU 1266  N   LEU A 910     5533   7190   7207   -238    325   -613       N  
ATOM   1267  CA  LEU A 910       4.987  38.372  46.599  1.00 53.86           C  
ANISOU 1267  CA  LEU A 910     5723   7310   7430   -332    363   -561       C  
ATOM   1268  C   LEU A 910       3.492  38.375  46.970  1.00 57.42           C  
ANISOU 1268  C   LEU A 910     6077   7769   7970   -420    423   -595       C  
ATOM   1269  O   LEU A 910       2.867  37.299  46.984  1.00 58.68           O  
ANISOU 1269  O   LEU A 910     6220   7856   8220   -492    421   -585       O  
ATOM   1270  CB  LEU A 910       5.879  38.214  47.844  1.00 53.85           C  
ANISOU 1270  CB  LEU A 910     5796   7331   7335   -363    409   -454       C  
ATOM   1271  CG  LEU A 910       7.104  37.297  47.708  1.00 58.52           C  
ANISOU 1271  CG  LEU A 910     6465   7853   7917   -318    350   -377       C  
ATOM   1272  CD1 LEU A 910       7.812  37.458  46.376  1.00 56.18           C  
ANISOU 1272  CD1 LEU A 910     6178   7533   7635   -206    283   -439       C  
ATOM   1273  CD2 LEU A 910       8.060  37.481  48.875  1.00 59.94           C  
ANISOU 1273  CD2 LEU A 910     6698   8085   7990   -337    364   -267       C  
ATOM   1274  N   HIS A 911       2.913  39.579  47.218  1.00 51.00           N  
ANISOU 1274  N   HIS A 911     5189   7032   7157   -413    480   -638       N  
ATOM   1275  CA  HIS A 911       1.480  39.720  47.532  1.00 51.60           C  
ANISOU 1275  CA  HIS A 911     5143   7118   7345   -481    552   -677       C  
ATOM   1276  C   HIS A 911       0.607  39.155  46.394  1.00 58.09           C  
ANISOU 1276  C   HIS A 911     5879   7887   8305   -486    451   -731       C  
ATOM   1277  O   HIS A 911      -0.526  38.780  46.651  1.00 61.12           O  
ANISOU 1277  O   HIS A 911     6160   8254   8810   -568    495   -744       O  
ATOM   1278  CB  HIS A 911       1.117  41.193  47.823  1.00 51.62           C  
ANISOU 1278  CB  HIS A 911     5075   7191   7347   -443    628   -726       C  
ATOM   1279  CG  HIS A 911       1.160  42.086  46.612  1.00 54.26           C  
ANISOU 1279  CG  HIS A 911     5363   7535   7716   -335    527   -776       C  
ATOM   1280  ND1 HIS A 911       0.011  42.390  45.895  1.00 56.82           N  
ANISOU 1280  ND1 HIS A 911     5548   7854   8186   -318    483   -823       N  
ATOM   1281  CD2 HIS A 911       2.216  42.685  46.009  1.00 53.99           C  
ANISOU 1281  CD2 HIS A 911     5404   7516   7593   -246    459   -771       C  
ATOM   1282  CE1 HIS A 911       0.410  43.164  44.897  1.00 55.08           C  
ANISOU 1282  CE1 HIS A 911     5337   7647   7943   -219    385   -836       C  
ATOM   1283  NE2 HIS A 911       1.723  43.373  44.929  1.00 53.68           N  
ANISOU 1283  NE2 HIS A 911     5289   7481   7627   -175    379   -808       N  
ATOM   1284  N   ARG A 912       1.140  39.086  45.148  1.00 55.39           N  
ANISOU 1284  N   ARG A 912     5581   7526   7939   -409    319   -765       N  
ATOM   1285  CA  ARG A 912       0.444  38.580  43.944  1.00 56.77           C  
ANISOU 1285  CA  ARG A 912     5703   7662   8204   -417    196   -829       C  
ATOM   1286  C   ARG A 912       0.217  37.081  44.029  1.00 60.29           C  
ANISOU 1286  C   ARG A 912     6179   8011   8719   -511    184   -825       C  
ATOM   1287  O   ARG A 912      -0.670  36.553  43.371  1.00 60.09           O  
ANISOU 1287  O   ARG A 912     6084   7948   8801   -566    105   -882       O  
ATOM   1288  CB  ARG A 912       1.271  38.857  42.655  1.00 55.94           C  
ANISOU 1288  CB  ARG A 912     5680   7568   8006   -316     79   -864       C  
ATOM   1289  CG  ARG A 912       1.286  40.300  42.140  1.00 56.44           C  
ANISOU 1289  CG  ARG A 912     5701   7710   8032   -225     48   -872       C  
ATOM   1290  CD  ARG A 912      -0.026  40.571  41.473  1.00 62.95           C  
ANISOU 1290  CD  ARG A 912     6390   8555   8974   -243    -40   -913       C  
ATOM   1291  NE  ARG A 912      -0.145  41.900  40.890  1.00 68.04           N  
ANISOU 1291  NE  ARG A 912     6983   9259   9610   -154    -88   -904       N  
ATOM   1292  CZ  ARG A 912       0.014  42.179  39.603  1.00 75.69           C  
ANISOU 1292  CZ  ARG A 912     7990  10255  10516    -97   -223   -915       C  
ATOM   1293  NH1 ARG A 912       0.378  41.227  38.746  1.00 56.98           N  
ANISOU 1293  NH1 ARG A 912     5723   7862   8066   -118   -313   -959       N  
ATOM   1294  NH2 ARG A 912      -0.197  43.410  39.158  1.00 63.61           N  
ANISOU 1294  NH2 ARG A 912     6401   8768   8999    -21   -265   -884       N  
ATOM   1295  N   LEU A 913       1.038  36.399  44.822  1.00 55.80           N  
ANISOU 1295  N   LEU A 913     5713   7394   8096   -531    250   -753       N  
ATOM   1296  CA  LEU A 913       1.053  34.936  44.939  1.00 55.01           C  
ANISOU 1296  CA  LEU A 913     5666   7173   8064   -607    244   -729       C  
ATOM   1297  C   LEU A 913       0.451  34.404  46.230  1.00 59.15           C  
ANISOU 1297  C   LEU A 913     6155   7671   8649   -725    362   -645       C  
ATOM   1298  O   LEU A 913       0.510  33.194  46.480  1.00 58.21           O  
ANISOU 1298  O   LEU A 913     6086   7439   8592   -793    371   -597       O  
ATOM   1299  CB  LEU A 913       2.544  34.525  44.889  1.00 53.08           C  
ANISOU 1299  CB  LEU A 913     5563   6881   7725   -530    230   -681       C  
ATOM   1300  CG  LEU A 913       3.338  34.988  43.666  1.00 56.16           C  
ANISOU 1300  CG  LEU A 913     6006   7294   8037   -412    146   -753       C  
ATOM   1301  CD1 LEU A 913       4.810  34.660  43.817  1.00 55.17           C  
ANISOU 1301  CD1 LEU A 913     5988   7129   7844   -336    162   -692       C  
ATOM   1302  CD2 LEU A 913       2.803  34.375  42.410  1.00 56.72           C  
ANISOU 1302  CD2 LEU A 913     6077   7304   8170   -430     47   -867       C  
ATOM   1303  N   MET A 914      -0.027  35.300  47.102  1.00 56.70           N  
ANISOU 1303  N   MET A 914     5775   7457   8311   -748    468   -619       N  
ATOM   1304  CA  MET A 914      -0.431  34.840  48.420  1.00 58.18           C  
ANISOU 1304  CA  MET A 914     5960   7637   8509   -861    604   -528       C  
ATOM   1305  C   MET A 914      -1.909  34.958  48.776  1.00 65.88           C  
ANISOU 1305  C   MET A 914     6778   8633   9619   -961    697   -557       C  
ATOM   1306  O   MET A 914      -2.625  35.821  48.261  1.00 66.57           O  
ANISOU 1306  O   MET A 914     6738   8779   9777   -924    679   -642       O  
ATOM   1307  CB  MET A 914       0.401  35.541  49.495  1.00 59.40           C  
ANISOU 1307  CB  MET A 914     6201   7879   8489   -836    691   -455       C  
ATOM   1308  CG  MET A 914       1.878  35.176  49.434  1.00 62.77           C  
ANISOU 1308  CG  MET A 914     6770   8273   8807   -765    614   -386       C  
ATOM   1309  SD  MET A 914       2.780  35.724  50.905  1.00 66.75           S  
ANISOU 1309  SD  MET A 914     7376   8875   9109   -782    697   -275       S  
ATOM   1310  CE  MET A 914       2.552  37.531  50.781  1.00 62.20           C  
ANISOU 1310  CE  MET A 914     6731   8430   8474   -718    740   -394       C  
ATOM   1311  N   THR A 915      -2.327  34.095  49.725  1.00 62.81           N  
ANISOU 1311  N   THR A 915     6397   8197   9271  -1088    807   -471       N  
ATOM   1312  CA  THR A 915      -3.643  34.071  50.337  1.00 65.38           C  
ANISOU 1312  CA  THR A 915     6582   8541   9720  -1204    943   -470       C  
ATOM   1313  C   THR A 915      -3.795  35.356  51.192  1.00 71.06           C  
ANISOU 1313  C   THR A 915     7268   9392  10338  -1179   1093   -486       C  
ATOM   1314  O   THR A 915      -2.776  36.014  51.471  1.00 68.61           O  
ANISOU 1314  O   THR A 915     7077   9143   9849  -1100   1085   -471       O  
ATOM   1315  CB  THR A 915      -3.774  32.820  51.245  1.00 73.54           C  
ANISOU 1315  CB  THR A 915     7676   9488  10776  -1344   1038   -344       C  
ATOM   1316  OG1 THR A 915      -2.705  32.798  52.208  1.00 68.64           O  
ANISOU 1316  OG1 THR A 915     7229   8902   9951  -1332   1090   -226       O  
ATOM   1317  CG2 THR A 915      -3.841  31.516  50.451  1.00 69.93           C  
ANISOU 1317  CG2 THR A 915     7231   8872  10467  -1389    915   -345       C  
ATOM   1318  N   PRO A 916      -5.038  35.734  51.624  1.00 69.50           N  
ANISOU 1318  N   PRO A 916     6908   9235  10265  -1247   1237   -522       N  
ATOM   1319  CA  PRO A 916      -5.183  36.915  52.499  1.00 68.80           C  
ANISOU 1319  CA  PRO A 916     6800   9256  10085  -1227   1409   -554       C  
ATOM   1320  C   PRO A 916      -4.309  36.806  53.763  1.00 72.80           C  
ANISOU 1320  C   PRO A 916     7502   9810  10347  -1277   1519   -458       C  
ATOM   1321  O   PRO A 916      -3.788  37.820  54.214  1.00 71.60           O  
ANISOU 1321  O   PRO A 916     7418   9743  10045  -1222   1572   -495       O  
ATOM   1322  CB  PRO A 916      -6.682  36.908  52.847  1.00 72.18           C  
ANISOU 1322  CB  PRO A 916     7023   9689  10714  -1321   1570   -585       C  
ATOM   1323  CG  PRO A 916      -7.333  36.139  51.747  1.00 76.61           C  
ANISOU 1323  CG  PRO A 916     7452  10162  11496  -1345   1412   -607       C  
ATOM   1324  CD  PRO A 916      -6.348  35.075  51.402  1.00 72.14           C  
ANISOU 1324  CD  PRO A 916     7064   9512  10835  -1354   1266   -538       C  
ATOM   1325  N   ILE A 917      -4.141  35.571  54.321  1.00 70.41           N  
ANISOU 1325  N   ILE A 917     7296   9451  10008  -1387   1540   -330       N  
ATOM   1326  CA  ILE A 917      -3.285  35.273  55.474  1.00 70.25           C  
ANISOU 1326  CA  ILE A 917     7468   9469   9754  -1445   1604   -203       C  
ATOM   1327  C   ILE A 917      -1.840  35.732  55.166  1.00 72.89           C  
ANISOU 1327  C   ILE A 917     7939   9831   9924  -1321   1447   -199       C  
ATOM   1328  O   ILE A 917      -1.257  36.524  55.931  1.00 71.79           O  
ANISOU 1328  O   ILE A 917     7896   9794   9588  -1312   1505   -200       O  
ATOM   1329  CB  ILE A 917      -3.326  33.763  55.819  1.00 73.81           C  
ANISOU 1329  CB  ILE A 917     7982   9816  10246  -1562   1602    -49       C  
ATOM   1330  N   GLY A 918      -1.310  35.257  54.030  1.00 68.33           N  
ANISOU 1330  N   GLY A 918     7363   9163   9437  -1235   1258   -209       N  
ATOM   1331  CA  GLY A 918       0.021  35.600  53.541  1.00 66.45           C  
ANISOU 1331  CA  GLY A 918     7224   8934   9090  -1112   1110   -210       C  
ATOM   1332  C   GLY A 918       0.218  37.097  53.443  1.00 69.21           C  
ANISOU 1332  C   GLY A 918     7548   9388   9361  -1027   1128   -319       C  
ATOM   1333  O   GLY A 918       1.167  37.625  54.021  1.00 67.79           O  
ANISOU 1333  O   GLY A 918     7476   9277   9003  -1004   1123   -288       O  
ATOM   1334  N   MET A 919      -0.726  37.788  52.767  1.00 68.16           N  
ANISOU 1334  N   MET A 919     7264   9264   9371   -988   1150   -440       N  
ATOM   1335  CA  MET A 919      -0.737  39.244  52.567  1.00 68.78           C  
ANISOU 1335  CA  MET A 919     7292   9414   9429   -902   1174   -548       C  
ATOM   1336  C   MET A 919      -0.833  40.064  53.867  1.00 69.51           C  
ANISOU 1336  C   MET A 919     7427   9599   9386   -958   1358   -568       C  
ATOM   1337  O   MET A 919      -0.202  41.124  53.958  1.00 68.63           O  
ANISOU 1337  O   MET A 919     7363   9538   9174   -895   1354   -622       O  
ATOM   1338  CB  MET A 919      -1.843  39.655  51.588  1.00 72.59           C  
ANISOU 1338  CB  MET A 919     7588   9871  10124   -855   1149   -645       C  
ATOM   1339  CG  MET A 919      -1.527  40.955  50.868  1.00 77.35           C  
ANISOU 1339  CG  MET A 919     8158  10504  10728   -725   1084   -727       C  
ATOM   1340  SD  MET A 919      -2.722  41.408  49.586  1.00 84.39           S  
ANISOU 1340  SD  MET A 919     8837  11366  11863   -657   1000   -808       S  
ATOM   1341  CE  MET A 919      -4.095  42.017  50.602  1.00 82.98           C  
ANISOU 1341  CE  MET A 919     8494  11219  11815   -720   1237   -860       C  
ATOM   1342  N   ALA A 920      -1.619  39.587  54.851  1.00 64.25           N  
ANISOU 1342  N   ALA A 920     6747   8950   8713  -1085   1526   -530       N  
ATOM   1343  CA  ALA A 920      -1.790  40.254  56.151  1.00 64.74           C  
ANISOU 1343  CA  ALA A 920     6869   9106   8625  -1161   1727   -558       C  
ATOM   1344  C   ALA A 920      -0.461  40.222  56.956  1.00 68.50           C  
ANISOU 1344  C   ALA A 920     7556   9644   8827  -1190   1678   -475       C  
ATOM   1345  O   ALA A 920      -0.095  41.214  57.591  1.00 67.29           O  
ANISOU 1345  O   ALA A 920     7474   9570   8522  -1192   1749   -544       O  
ATOM   1346  CB  ALA A 920      -2.919  39.587  56.956  1.00 66.70           C  
ANISOU 1346  CB  ALA A 920     7061   9358   8926  -1300   1923   -519       C  
ATOM   1347  N   GLU A 921       0.237  39.073  56.922  1.00 66.29           N  
ANISOU 1347  N   GLU A 921     7369   9320   8499  -1215   1550   -329       N  
ATOM   1348  CA  GLU A 921       1.516  38.872  57.589  1.00 67.32           C  
ANISOU 1348  CA  GLU A 921     7674   9499   8406  -1237   1463   -219       C  
ATOM   1349  C   GLU A 921       2.596  39.772  56.978  1.00 67.22           C  
ANISOU 1349  C   GLU A 921     7684   9505   8350  -1115   1322   -283       C  
ATOM   1350  O   GLU A 921       3.400  40.342  57.722  1.00 67.85           O  
ANISOU 1350  O   GLU A 921     7876   9670   8233  -1141   1314   -275       O  
ATOM   1351  CB  GLU A 921       1.933  37.396  57.558  1.00 69.87           C  
ANISOU 1351  CB  GLU A 921     8057   9739   8752  -1271   1357    -41       C  
ATOM   1352  CG  GLU A 921       2.800  36.987  58.744  1.00 88.90           C  
ANISOU 1352  CG  GLU A 921    10641  12214  10923  -1356   1336    119       C  
ATOM   1353  CD  GLU A 921       2.048  36.634  60.019  1.00118.04           C  
ANISOU 1353  CD  GLU A 921    14398  15966  14485  -1521   1523    195       C  
ATOM   1354  OE1 GLU A 921       1.287  37.490  60.531  1.00102.50           O  
ANISOU 1354  OE1 GLU A 921    12404  14084  12458  -1574   1707     72       O  
ATOM   1355  OE2 GLU A 921       2.245  35.504  60.524  1.00117.74           O  
ANISOU 1355  OE2 GLU A 921    14443  15888  14405  -1597   1493    383       O  
ATOM   1356  N   GLN A 922       2.566  39.952  55.645  1.00 59.92           N  
ANISOU 1356  N   GLN A 922     6654   8509   7604   -994   1218   -352       N  
ATOM   1357  CA  GLN A 922       3.499  40.831  54.942  1.00 57.72           C  
ANISOU 1357  CA  GLN A 922     6382   8240   7309   -878   1102   -411       C  
ATOM   1358  C   GLN A 922       3.246  42.313  55.337  1.00 60.06           C  
ANISOU 1358  C   GLN A 922     6661   8606   7553   -873   1215   -546       C  
ATOM   1359  O   GLN A 922       4.188  42.997  55.693  1.00 57.32           O  
ANISOU 1359  O   GLN A 922     6398   8311   7069   -864   1176   -558       O  
ATOM   1360  CB  GLN A 922       3.413  40.631  53.407  1.00 57.54           C  
ANISOU 1360  CB  GLN A 922     6261   8129   7472   -763    981   -448       C  
ATOM   1361  CG  GLN A 922       4.380  41.540  52.631  1.00 58.67           C  
ANISOU 1361  CG  GLN A 922     6413   8283   7596   -647    875   -497       C  
ATOM   1362  CD  GLN A 922       4.282  41.422  51.135  1.00 64.79           C  
ANISOU 1362  CD  GLN A 922     7112   8990   8516   -544    769   -536       C  
ATOM   1363  OE1 GLN A 922       4.493  40.360  50.557  1.00 60.53           O  
ANISOU 1363  OE1 GLN A 922     6586   8384   8030   -529    685   -484       O  
ATOM   1364  NE2 GLN A 922       4.132  42.551  50.460  1.00 48.86           N  
ANISOU 1364  NE2 GLN A 922     5033   6985   6548   -466    761   -623       N  
ATOM   1365  N   VAL A 923       1.991  42.789  55.244  1.00 58.17           N  
ANISOU 1365  N   VAL A 923     6304   8355   7443   -876   1350   -647       N  
ATOM   1366  CA  VAL A 923       1.582  44.161  55.587  1.00 60.35           C  
ANISOU 1366  CA  VAL A 923     6544   8667   7719   -861   1483   -785       C  
ATOM   1367  C   VAL A 923       1.921  44.503  57.058  1.00 66.29           C  
ANISOU 1367  C   VAL A 923     7440   9513   8234   -977   1610   -800       C  
ATOM   1368  O   VAL A 923       2.430  45.601  57.324  1.00 66.75           O  
ANISOU 1368  O   VAL A 923     7552   9603   8208   -960   1630   -892       O  
ATOM   1369  CB  VAL A 923       0.056  44.384  55.302  1.00 66.27           C  
ANISOU 1369  CB  VAL A 923     7116   9378   8686   -849   1618   -868       C  
ATOM   1370  N   LEU A 924       1.624  43.563  57.994  1.00 62.45           N  
ANISOU 1370  N   LEU A 924     7024   9068   7637  -1102   1694   -710       N  
ATOM   1371  CA  LEU A 924       1.903  43.697  59.424  1.00 64.47           C  
ANISOU 1371  CA  LEU A 924     7438   9428   7629  -1234   1807   -701       C  
ATOM   1372  C   LEU A 924       3.397  43.879  59.661  1.00 64.71           C  
ANISOU 1372  C   LEU A 924     7612   9509   7465  -1234   1634   -644       C  
ATOM   1373  O   LEU A 924       3.796  44.772  60.410  1.00 64.75           O  
ANISOU 1373  O   LEU A 924     7715   9589   7298  -1286   1688   -731       O  
ATOM   1374  CB  LEU A 924       1.389  42.463  60.206  1.00 66.80           C  
ANISOU 1374  CB  LEU A 924     7783   9747   7851  -1364   1893   -566       C  
ATOM   1375  CG  LEU A 924       1.411  42.539  61.748  1.00 74.53           C  
ANISOU 1375  CG  LEU A 924     8931  10848   8540  -1524   2048   -551       C  
ATOM   1376  CD1 LEU A 924       0.368  43.523  62.274  1.00 76.53           C  
ANISOU 1376  CD1 LEU A 924     9135  11136   8807  -1561   2321   -739       C  
ATOM   1377  CD2 LEU A 924       1.128  41.184  62.356  1.00 77.09           C  
ANISOU 1377  CD2 LEU A 924     9316  11181   8795  -1641   2081   -365       C  
ATOM   1378  N   ASN A 925       4.213  43.020  59.030  1.00 58.72           N  
ANISOU 1378  N   ASN A 925     6859   8706   6746  -1179   1432   -503       N  
ATOM   1379  CA  ASN A 925       5.658  43.072  59.124  1.00 57.66           C  
ANISOU 1379  CA  ASN A 925     6822   8609   6479  -1164   1251   -428       C  
ATOM   1380  C   ASN A 925       6.188  44.379  58.531  1.00 60.14           C  
ANISOU 1380  C   ASN A 925     7098   8915   6839  -1075   1205   -563       C  
ATOM   1381  O   ASN A 925       7.030  45.012  59.166  1.00 61.28           O  
ANISOU 1381  O   ASN A 925     7339   9131   6814  -1124   1162   -586       O  
ATOM   1382  CB  ASN A 925       6.300  41.853  58.465  1.00 58.56           C  
ANISOU 1382  CB  ASN A 925     6920   8651   6680  -1105   1075   -262       C  
ATOM   1383  CG  ASN A 925       7.799  41.764  58.692  1.00 82.26           C  
ANISOU 1383  CG  ASN A 925    10005  11693   9557  -1096    893   -156       C  
ATOM   1384  OD1 ASN A 925       8.594  41.756  57.746  1.00 71.89           O  
ANISOU 1384  OD1 ASN A 925     8635  10323   8355   -984    756   -139       O  
ATOM   1385  ND2 ASN A 925       8.222  41.748  59.955  1.00 74.99           N  
ANISOU 1385  ND2 ASN A 925     9216  10878   8398  -1219    890    -86       N  
ATOM   1386  N   ALA A 926       5.652  44.824  57.368  1.00 54.39           N  
ANISOU 1386  N   ALA A 926     6232   8101   6332   -957   1215   -651       N  
ATOM   1387  CA  ALA A 926       6.067  46.112  56.771  1.00 53.86           C  
ANISOU 1387  CA  ALA A 926     6126   8012   6325   -872   1185   -768       C  
ATOM   1388  C   ALA A 926       5.703  47.295  57.706  1.00 61.20           C  
ANISOU 1388  C   ALA A 926     7107   8990   7158   -943   1351   -920       C  
ATOM   1389  O   ALA A 926       6.503  48.209  57.858  1.00 61.35           O  
ANISOU 1389  O   ALA A 926     7179   9027   7105   -946   1309   -984       O  
ATOM   1390  CB  ALA A 926       5.454  46.305  55.389  1.00 52.31           C  
ANISOU 1390  CB  ALA A 926     5782   7721   6370   -741   1164   -810       C  
ATOM   1391  N   GLY A 927       4.551  47.217  58.371  1.00 59.55           N  
ANISOU 1391  N   GLY A 927     6885   8799   6944  -1012   1543   -979       N  
ATOM   1392  CA  GLY A 927       4.124  48.203  59.365  1.00 61.21           C  
ANISOU 1392  CA  GLY A 927     7154   9051   7050  -1091   1738  -1135       C  
ATOM   1393  C   GLY A 927       5.089  48.269  60.535  1.00 68.12           C  
ANISOU 1393  C   GLY A 927     8221  10038   7623  -1223   1701  -1118       C  
ATOM   1394  O   GLY A 927       5.509  49.366  60.931  1.00 68.40           O  
ANISOU 1394  O   GLY A 927     8324  10092   7575  -1252   1734  -1252       O  
ATOM   1395  N   ALA A 928       5.509  47.075  61.039  1.00 65.57           N  
ANISOU 1395  N   ALA A 928     7985   9783   7145  -1303   1609   -944       N  
ATOM   1396  CA  ALA A 928       6.451  46.923  62.153  1.00 67.06           C  
ANISOU 1396  CA  ALA A 928     8355  10091   7034  -1436   1531   -878       C  
ATOM   1397  C   ALA A 928       7.813  47.493  61.819  1.00 73.62           C  
ANISOU 1397  C   ALA A 928     9209  10927   7837  -1396   1326   -875       C  
ATOM   1398  O   ALA A 928       8.419  48.150  62.668  1.00 75.65           O  
ANISOU 1398  O   ALA A 928     9590  11268   7886  -1499   1310   -944       O  
ATOM   1399  CB  ALA A 928       6.585  45.463  62.530  1.00 68.26           C  
ANISOU 1399  CB  ALA A 928     8561  10282   7092  -1496   1451   -658       C  
ATOM   1400  N   LEU A 929       8.276  47.272  60.571  1.00 69.04           N  
ANISOU 1400  N   LEU A 929     8508  10257   7467  -1255   1177   -805       N  
ATOM   1401  CA  LEU A 929       9.560  47.745  60.059  1.00 67.90           C  
ANISOU 1401  CA  LEU A 929     8350  10102   7346  -1201    992   -786       C  
ATOM   1402  C   LEU A 929       9.538  49.188  59.562  1.00 69.22           C  
ANISOU 1402  C   LEU A 929     8466  10209   7625  -1144   1051   -967       C  
ATOM   1403  O   LEU A 929      10.584  49.719  59.215  1.00 67.42           O  
ANISOU 1403  O   LEU A 929     8230   9972   7414  -1117    920   -966       O  
ATOM   1404  CB  LEU A 929      10.083  46.800  58.970  1.00 66.66           C  
ANISOU 1404  CB  LEU A 929     8098   9878   7352  -1081    831   -628       C  
ATOM   1405  CG  LEU A 929      10.762  45.544  59.485  1.00 72.43           C  
ANISOU 1405  CG  LEU A 929     8892  10659   7970  -1131    696   -425       C  
ATOM   1406  CD1 LEU A 929      11.096  44.630  58.351  1.00 71.22           C  
ANISOU 1406  CD1 LEU A 929     8639  10412   8010  -1002    584   -306       C  
ATOM   1407  CD2 LEU A 929      12.042  45.885  60.282  1.00 75.19           C  
ANISOU 1407  CD2 LEU A 929     9332  11108   8129  -1218    548   -379       C  
ATOM   1408  N   GLY A 930       8.352  49.789  59.519  1.00 65.35           N  
ANISOU 1408  N   GLY A 930     7930   9668   7231  -1123   1248  -1111       N  
ATOM   1409  CA  GLY A 930       8.151  51.177  59.119  1.00 64.95           C  
ANISOU 1409  CA  GLY A 930     7830   9539   7311  -1067   1332  -1283       C  
ATOM   1410  C   GLY A 930       7.987  51.475  57.644  1.00 67.47           C  
ANISOU 1410  C   GLY A 930     7997   9740   7900   -901   1282  -1270       C  
ATOM   1411  O   GLY A 930       8.183  52.618  57.248  1.00 69.92           O  
ANISOU 1411  O   GLY A 930     8278   9981   8309   -854   1298  -1369       O  
ATOM   1412  N   TYR A 931       7.580  50.500  56.817  1.00 60.64           N  
ANISOU 1412  N   TYR A 931     7041   8844   7155   -819   1229  -1153       N  
ATOM   1413  CA  TYR A 931       7.433  50.740  55.370  1.00 57.00           C  
ANISOU 1413  CA  TYR A 931     6451   8286   6919   -671   1166  -1135       C  
ATOM   1414  C   TYR A 931       6.017  50.989  54.890  1.00 60.82           C  
ANISOU 1414  C   TYR A 931     6814   8700   7593   -601   1293  -1203       C  
ATOM   1415  O   TYR A 931       5.843  51.365  53.728  1.00 59.04           O  
ANISOU 1415  O   TYR A 931     6491   8400   7543   -485   1238  -1194       O  
ATOM   1416  CB  TYR A 931       8.066  49.619  54.568  1.00 53.64           C  
ANISOU 1416  CB  TYR A 931     6003   7863   6514   -615    999   -978       C  
ATOM   1417  CG  TYR A 931       9.560  49.523  54.764  1.00 51.37           C  
ANISOU 1417  CG  TYR A 931     5788   7623   6108   -646    856   -902       C  
ATOM   1418  CD1 TYR A 931      10.430  50.373  54.080  1.00 51.39           C  
ANISOU 1418  CD1 TYR A 931     5765   7589   6173   -587    782   -919       C  
ATOM   1419  CD2 TYR A 931      10.111  48.560  55.603  1.00 51.45           C  
ANISOU 1419  CD2 TYR A 931     5880   7711   5959   -733    790   -797       C  
ATOM   1420  CE1 TYR A 931      11.808  50.275  54.240  1.00 50.79           C  
ANISOU 1420  CE1 TYR A 931     5727   7556   6014   -617    651   -845       C  
ATOM   1421  CE2 TYR A 931      11.492  48.434  55.748  1.00 50.85           C  
ANISOU 1421  CE2 TYR A 931     5842   7676   5802   -753    641   -712       C  
ATOM   1422  CZ  TYR A 931      12.332  49.289  55.057  1.00 54.48           C  
ANISOU 1422  CZ  TYR A 931     6259   8102   6339   -695    575   -741       C  
ATOM   1423  OH  TYR A 931      13.681  49.172  55.197  1.00 54.36           O  
ANISOU 1423  OH  TYR A 931     6256   8128   6269   -716    433   -656       O  
ATOM   1424  N   SER A 932       5.022  50.807  55.772  1.00 59.26           N  
ANISOU 1424  N   SER A 932     6621   8531   7363   -675   1460  -1264       N  
ATOM   1425  CA  SER A 932       3.590  50.995  55.484  1.00 60.41           C  
ANISOU 1425  CA  SER A 932     6630   8618   7706   -622   1599  -1329       C  
ATOM   1426  C   SER A 932       3.172  52.461  55.417  1.00 63.97           C  
ANISOU 1426  C   SER A 932     7025   8988   8294   -564   1718  -1477       C  
ATOM   1427  O   SER A 932       3.439  53.223  56.361  1.00 63.67           O  
ANISOU 1427  O   SER A 932     7084   8965   8141   -638   1830  -1594       O  
ATOM   1428  CB  SER A 932       2.714  50.252  56.491  1.00 66.80           C  
ANISOU 1428  CB  SER A 932     7455   9487   8440   -729   1757  -1336       C  
ATOM   1429  OG  SER A 932       2.509  48.915  56.064  1.00 79.16           O  
ANISOU 1429  OG  SER A 932     8981  11064  10034   -730   1664  -1199       O  
ATOM   1430  N   PRO A 933       2.450  52.833  54.328  1.00 59.37           N  
ANISOU 1430  N   PRO A 933     6283   8314   7959   -435   1697  -1472       N  
ATOM   1431  CA  PRO A 933       1.983  54.223  54.182  1.00 60.14           C  
ANISOU 1431  CA  PRO A 933     6308   8310   8234   -360   1806  -1592       C  
ATOM   1432  C   PRO A 933       0.852  54.592  55.147  1.00 67.33           C  
ANISOU 1432  C   PRO A 933     7171   9205   9207   -402   2063  -1731       C  
ATOM   1433  O   PRO A 933       0.214  53.676  55.691  1.00 69.09           O  
ANISOU 1433  O   PRO A 933     7378   9496   9376   -474   2146  -1710       O  
ATOM   1434  CB  PRO A 933       1.549  54.276  52.721  1.00 61.05           C  
ANISOU 1434  CB  PRO A 933     6270   8353   8575   -218   1676  -1504       C  
ATOM   1435  CG  PRO A 933       1.114  52.883  52.415  1.00 63.87           C  
ANISOU 1435  CG  PRO A 933     6580   8773   8917   -240   1599  -1400       C  
ATOM   1436  CD  PRO A 933       2.043  52.004  53.174  1.00 58.67           C  
ANISOU 1436  CD  PRO A 933     6081   8210   8001   -356   1562  -1355       C  
ATOM   1437  N   PRO A 934       0.542  55.897  55.377  1.00 65.99           N  
ANISOU 1437  N   PRO A 934     6971   8936   9165   -359   2208  -1875       N  
ATOM   1438  CA  PRO A 934      -0.531  56.241  56.346  1.00 67.73           C  
ANISOU 1438  CA  PRO A 934     7147   9140   9449   -398   2487  -2026       C  
ATOM   1439  C   PRO A 934      -1.935  55.732  56.000  1.00 73.20           C  
ANISOU 1439  C   PRO A 934     7628   9813  10370   -338   2566  -1988       C  
ATOM   1440  O   PRO A 934      -2.749  55.535  56.901  1.00 75.36           O  
ANISOU 1440  O   PRO A 934     7878  10120  10638   -407   2790  -2074       O  
ATOM   1441  CB  PRO A 934      -0.473  57.773  56.407  1.00 69.78           C  
ANISOU 1441  CB  PRO A 934     7404   9263   9846   -336   2594  -2177       C  
ATOM   1442  CG  PRO A 934       0.098  58.171  55.099  1.00 72.69           C  
ANISOU 1442  CG  PRO A 934     7719   9553  10347   -215   2370  -2061       C  
ATOM   1443  CD  PRO A 934       1.158  57.128  54.841  1.00 66.80           C  
ANISOU 1443  CD  PRO A 934     7086   8929   9365   -280   2151  -1915       C  
ATOM   1444  N   GLU A 935      -2.212  55.504  54.715  1.00 68.80           N  
ANISOU 1444  N   GLU A 935     6922   9212  10007   -222   2384  -1861       N  
ATOM   1445  CA  GLU A 935      -3.512  55.017  54.257  1.00 69.74           C  
ANISOU 1445  CA  GLU A 935     6822   9314  10361   -168   2412  -1813       C  
ATOM   1446  C   GLU A 935      -3.791  53.567  54.664  1.00 77.06           C  
ANISOU 1446  C   GLU A 935     7766  10355  11158   -284   2415  -1739       C  
ATOM   1447  O   GLU A 935      -4.951  53.162  54.659  1.00 79.54           O  
ANISOU 1447  O   GLU A 935     7907  10664  11649   -282   2507  -1734       O  
ATOM   1448  CB  GLU A 935      -3.679  55.211  52.739  1.00 69.84           C  
ANISOU 1448  CB  GLU A 935     6689   9257  10591    -23   2188  -1696       C  
ATOM   1449  CG  GLU A 935      -2.646  54.478  51.886  1.00 69.79           C  
ANISOU 1449  CG  GLU A 935     6791   9310  10418    -28   1920  -1556       C  
ATOM   1450  CD  GLU A 935      -1.466  55.291  51.377  1.00 89.28           C  
ANISOU 1450  CD  GLU A 935     9376  11734  12813     24   1798  -1537       C  
ATOM   1451  OE1 GLU A 935      -1.199  56.382  51.937  1.00 81.51           O  
ANISOU 1451  OE1 GLU A 935     8446  10684  11841     30   1924  -1647       O  
ATOM   1452  OE2 GLU A 935      -0.786  54.814  50.433  1.00 65.18           O  
ANISOU 1452  OE2 GLU A 935     6366   8712   9688     52   1585  -1419       O  
ATOM   1453  N   PHE A 936      -2.747  52.788  55.017  1.00 73.47           N  
ANISOU 1453  N   PHE A 936     7507   9993  10414   -386   2315  -1674       N  
ATOM   1454  CA  PHE A 936      -2.921  51.389  55.423  1.00 73.02           C  
ANISOU 1454  CA  PHE A 936     7484  10028  10233   -498   2311  -1586       C  
ATOM   1455  C   PHE A 936      -3.619  51.253  56.756  1.00 84.24           C  
ANISOU 1455  C   PHE A 936     8927  11498  11581   -616   2590  -1673       C  
ATOM   1456  O   PHE A 936      -4.344  50.271  56.958  1.00 85.98           O  
ANISOU 1456  O   PHE A 936     9076  11756  11835   -683   2648  -1612       O  
ATOM   1457  CB  PHE A 936      -1.602  50.613  55.381  1.00 71.37           C  
ANISOU 1457  CB  PHE A 936     7462   9886   9769   -556   2119  -1476       C  
ATOM   1458  CG  PHE A 936      -1.226  50.109  54.000  1.00 68.63           C  
ANISOU 1458  CG  PHE A 936     7063   9508   9504   -467   1862  -1356       C  
ATOM   1459  CD1 PHE A 936      -1.850  50.611  52.858  1.00 69.52           C  
ANISOU 1459  CD1 PHE A 936     7006   9545   9864   -340   1785  -1354       C  
ATOM   1460  CD2 PHE A 936      -0.236  49.154  53.840  1.00 66.69           C  
ANISOU 1460  CD2 PHE A 936     6942   9310   9087   -508   1699  -1244       C  
ATOM   1461  CE1 PHE A 936      -1.496  50.156  51.592  1.00 68.56           C  
ANISOU 1461  CE1 PHE A 936     6860   9408   9782   -271   1556  -1253       C  
ATOM   1462  CE2 PHE A 936       0.130  48.718  52.570  1.00 67.50           C  
ANISOU 1462  CE2 PHE A 936     7010   9382   9255   -427   1488  -1156       C  
ATOM   1463  CZ  PHE A 936      -0.501  49.220  51.457  1.00 65.53           C  
ANISOU 1463  CZ  PHE A 936     6611   9070   9218   -316   1420  -1166       C  
ATOM   1464  N   SER A 937      -3.481  52.284  57.626  1.00 84.21           N  
ANISOU 1464  N   SER A 937     9010  11486  11498   -641   2778  -1827       N  
ATOM   1465  CA  SER A 937      -4.154  52.375  58.925  1.00 87.68           C  
ANISOU 1465  CA  SER A 937     9485  11971  11857   -749   3084  -1946       C  
ATOM   1466  C   SER A 937      -5.680  52.427  58.756  1.00 94.51           C  
ANISOU 1466  C   SER A 937    10092  12777  13041   -694   3268  -1988       C  
ATOM   1467  O   SER A 937      -6.387  51.799  59.539  1.00 96.96           O  
ANISOU 1467  O   SER A 937    10383  13148  13309   -799   3464  -1994       O  
ATOM   1468  CB  SER A 937      -3.678  53.607  59.689  1.00 92.76           C  
ANISOU 1468  CB  SER A 937    10268  12593  12382   -769   3230  -2128       C  
ATOM   1469  OG  SER A 937      -2.283  53.553  59.943  1.00 98.57           O  
ANISOU 1469  OG  SER A 937    11231  13395  12825   -840   3062  -2092       O  
ATOM   1470  N   SER A 938      -6.178  53.141  57.716  1.00 91.48           N  
ANISOU 1470  N   SER A 938     9503  12276  12980   -531   3195  -1999       N  
ATOM   1471  CA  SER A 938      -7.606  53.308  57.391  1.00 93.49           C  
ANISOU 1471  CA  SER A 938     9470  12459  13591   -451   3325  -2025       C  
ATOM   1472  C   SER A 938      -8.296  52.075  56.768  1.00 98.39           C  
ANISOU 1472  C   SER A 938     9928  13116  14340   -473   3201  -1875       C  
ATOM   1473  O   SER A 938      -9.512  52.104  56.559  1.00100.73           O  
ANISOU 1473  O   SER A 938     9970  13367  14935   -428   3304  -1888       O  
ATOM   1474  CB  SER A 938      -7.806  54.523  56.489  1.00 96.61           C  
ANISOU 1474  CB  SER A 938     9714  12715  14277   -269   3256  -2065       C  
ATOM   1475  N   THR A 939      -7.539  51.006  56.475  1.00 93.37           N  
ANISOU 1475  N   THR A 939     9427  12550  13500   -544   2984  -1739       N  
ATOM   1476  CA  THR A 939      -8.065  49.778  55.865  1.00 92.56           C  
ANISOU 1476  CA  THR A 939     9202  12468  13498   -579   2847  -1606       C  
ATOM   1477  C   THR A 939      -7.919  48.555  56.773  1.00 96.21           C  
ANISOU 1477  C   THR A 939     9804  13023  13730   -754   2930  -1541       C  
ATOM   1478  O   THR A 939      -6.958  48.464  57.548  1.00 95.56           O  
ANISOU 1478  O   THR A 939     9965  13004  13340   -835   2954  -1542       O  
ATOM   1479  CB  THR A 939      -7.383  49.536  54.507  1.00 95.06           C  
ANISOU 1479  CB  THR A 939     9533  12759  13828   -492   2503  -1497       C  
ATOM   1480  N   SER A 940      -8.947  47.716  56.786  1.00 93.11           N  
ANISOU 1480  N   SER A 940     9252  12632  13492   -817   2958  -1473       N  
ATOM   1481  CA  SER A 940      -8.906  46.476  57.545  1.00 93.24           C  
ANISOU 1481  CA  SER A 940     9380  12717  13332   -985   3032  -1384       C  
ATOM   1482  C   SER A 940      -7.914  45.499  56.919  1.00 92.35           C  
ANISOU 1482  C   SER A 940     9407  12607  13077  -1001   2736  -1245       C  
ATOM   1483  O   SER A 940      -7.148  44.838  57.613  1.00 91.50           O  
ANISOU 1483  O   SER A 940     9525  12554  12686  -1090   2724  -1181       O  
ATOM   1484  CB  SER A 940     -10.298  45.847  57.628  1.00 99.30           C  
ANISOU 1484  CB  SER A 940     9911  13471  14347  -1054   3194  -1368       C  
ATOM   1485  N   LYS A 941      -7.946  45.422  55.591  1.00 84.99           N  
ANISOU 1485  N   LYS A 941     8343  11614  12336   -908   2493  -1201       N  
ATOM   1486  CA  LYS A 941      -7.076  44.526  54.830  1.00 81.36           C  
ANISOU 1486  CA  LYS A 941     8000  11140  11771   -905   2220  -1093       C  
ATOM   1487  C   LYS A 941      -6.416  45.229  53.647  1.00 79.30           C  
ANISOU 1487  C   LYS A 941     7756  10848  11526   -751   2006  -1117       C  
ATOM   1488  O   LYS A 941      -6.776  44.988  52.501  1.00 77.86           O  
ANISOU 1488  O   LYS A 941     7438  10622  11523   -678   1830  -1099       O  
ATOM   1489  CB  LYS A 941      -7.866  43.314  54.338  1.00 83.73           C  
ANISOU 1489  CB  LYS A 941     8161  11401  12252   -967   2129  -1018       C  
ATOM   1490  N   PRO A 942      -5.443  46.084  53.932  1.00 72.71           N  
ANISOU 1490  N   PRO A 942     7081  10037  10509   -706   2021  -1161       N  
ATOM   1491  CA  PRO A 942      -4.741  46.843  52.896  1.00 70.20           C  
ANISOU 1491  CA  PRO A 942     6773   9684  10216   -569   1838  -1174       C  
ATOM   1492  C   PRO A 942      -3.918  45.968  51.957  1.00 70.60           C  
ANISOU 1492  C   PRO A 942     6910   9727  10188   -549   1584  -1077       C  
ATOM   1493  O   PRO A 942      -3.390  44.941  52.362  1.00 69.08           O  
ANISOU 1493  O   PRO A 942     6839   9557   9852   -636   1554  -1004       O  
ATOM   1494  CB  PRO A 942      -3.831  47.756  53.705  1.00 71.44           C  
ANISOU 1494  CB  PRO A 942     7086   9867  10189   -565   1941  -1244       C  
ATOM   1495  CG  PRO A 942      -3.536  46.976  54.930  1.00 76.82           C  
ANISOU 1495  CG  PRO A 942     7922  10619  10648   -709   2058  -1215       C  
ATOM   1496  CD  PRO A 942      -4.752  46.150  55.227  1.00 74.48           C  
ANISOU 1496  CD  PRO A 942     7491  10324  10486   -790   2191  -1195       C  
ATOM   1497  N   CYS A 943      -3.832  46.382  50.701  1.00 66.61           N  
ANISOU 1497  N   CYS A 943     6337   9184   9789   -434   1410  -1072       N  
ATOM   1498  CA  CYS A 943      -3.100  45.652  49.703  1.00 66.94           C  
ANISOU 1498  CA  CYS A 943     6455   9216   9762   -409   1189  -1001       C  
ATOM   1499  C   CYS A 943      -1.904  46.475  49.201  1.00 65.38           C  
ANISOU 1499  C   CYS A 943     6374   9018   9447   -314   1089   -998       C  
ATOM   1500  O   CYS A 943      -2.080  47.653  48.864  1.00 65.26           O  
ANISOU 1500  O   CYS A 943     6292   8981   9523   -225   1098  -1040       O  
ATOM   1501  CB  CYS A 943      -4.024  45.234  48.558  1.00 70.29           C  
ANISOU 1501  CB  CYS A 943     6716   9608  10383   -380   1048   -986       C  
ATOM   1502  SG  CYS A 943      -3.254  44.106  47.364  1.00 74.87           S  
ANISOU 1502  SG  CYS A 943     7404  10172  10871   -375    803   -925       S  
ATOM   1503  N   PRO A 944      -0.693  45.876  49.116  1.00 57.35           N  
ANISOU 1503  N   PRO A 944     5519   8018   8253   -329    995   -943       N  
ATOM   1504  CA  PRO A 944       0.450  46.608  48.522  1.00 55.19           C  
ANISOU 1504  CA  PRO A 944     5337   7743   7890   -242    897   -933       C  
ATOM   1505  C   PRO A 944       0.082  47.099  47.107  1.00 56.71           C  
ANISOU 1505  C   PRO A 944     5433   7904   8211   -136    762   -930       C  
ATOM   1506  O   PRO A 944      -0.691  46.449  46.419  1.00 56.82           O  
ANISOU 1506  O   PRO A 944     5358   7906   8326   -141    679   -917       O  
ATOM   1507  CB  PRO A 944       1.552  45.551  48.464  1.00 55.59           C  
ANISOU 1507  CB  PRO A 944     5525   7805   7790   -274    806   -863       C  
ATOM   1508  CG  PRO A 944       1.179  44.539  49.477  1.00 60.86           C  
ANISOU 1508  CG  PRO A 944     6215   8485   8423   -389    895   -835       C  
ATOM   1509  CD  PRO A 944      -0.319  44.487  49.459  1.00 57.88           C  
ANISOU 1509  CD  PRO A 944     5678   8090   8222   -417    968   -876       C  
ATOM   1510  N   SER A 945       0.558  48.272  46.711  1.00 50.09           N  
ANISOU 1510  N   SER A 945     4609   7052   7373    -51    742   -940       N  
ATOM   1511  CA  SER A 945       0.178  48.878  45.432  1.00 49.13           C  
ANISOU 1511  CA  SER A 945     4401   6902   7364     48    619   -918       C  
ATOM   1512  C   SER A 945       1.292  49.783  44.901  1.00 52.15           C  
ANISOU 1512  C   SER A 945     4877   7273   7663    122    567   -889       C  
ATOM   1513  O   SER A 945       2.306  49.968  45.575  1.00 50.31           O  
ANISOU 1513  O   SER A 945     4756   7052   7306     93    628   -899       O  
ATOM   1514  CB  SER A 945      -1.068  49.733  45.641  1.00 52.45           C  
ANISOU 1514  CB  SER A 945     4651   7286   7992     84    703   -959       C  
ATOM   1515  OG  SER A 945      -0.750  50.774  46.555  1.00 58.28           O  
ANISOU 1515  OG  SER A 945     5423   7999   8720     91    858  -1016       O  
ATOM   1516  N   LEU A 946       1.080  50.358  43.696  1.00 50.06           N  
ANISOU 1516  N   LEU A 946     4562   6989   7471    211    449   -846       N  
ATOM   1517  CA  LEU A 946       1.993  51.294  43.014  1.00 48.54           C  
ANISOU 1517  CA  LEU A 946     4440   6776   7225    285    399   -801       C  
ATOM   1518  C   LEU A 946       2.267  52.475  43.953  1.00 54.15           C  
ANISOU 1518  C   LEU A 946     5158   7440   7977    290    542   -849       C  
ATOM   1519  O   LEU A 946       3.416  52.876  44.110  1.00 54.54           O  
ANISOU 1519  O   LEU A 946     5314   7487   7922    284    561   -841       O  
ATOM   1520  CB  LEU A 946       1.313  51.767  41.708  1.00 49.04           C  
ANISOU 1520  CB  LEU A 946     4418   6823   7391    371    261   -738       C  
ATOM   1521  CG  LEU A 946       1.648  51.077  40.357  1.00 53.97           C  
ANISOU 1521  CG  LEU A 946     5110   7495   7900    387     89   -677       C  
ATOM   1522  CD1 LEU A 946       2.175  49.643  40.482  1.00 53.16           C  
ANISOU 1522  CD1 LEU A 946     5104   7436   7660    312     76   -709       C  
ATOM   1523  CD2 LEU A 946       0.508  51.148  39.419  1.00 57.40           C  
ANISOU 1523  CD2 LEU A 946     5427   7935   8447    427    -49   -637       C  
ATOM   1524  N   LYS A 947       1.212  52.967  44.653  1.00 52.80           N  
ANISOU 1524  N   LYS A 947     4870   7229   7963    290    656   -910       N  
ATOM   1525  CA  LYS A 947       1.282  54.047  45.643  1.00 51.94           C  
ANISOU 1525  CA  LYS A 947     4765   7063   7907    285    820   -990       C  
ATOM   1526  C   LYS A 947       2.073  53.646  46.875  1.00 54.38           C  
ANISOU 1526  C   LYS A 947     5202   7421   8040    177    924  -1053       C  
ATOM   1527  O   LYS A 947       2.873  54.456  47.357  1.00 54.31           O  
ANISOU 1527  O   LYS A 947     5276   7385   7975    162    983  -1093       O  
ATOM   1528  CB  LYS A 947      -0.128  54.490  46.078  1.00 53.05           C  
ANISOU 1528  CB  LYS A 947     4739   7152   8268    311    935  -1051       C  
ATOM   1529  CG  LYS A 947      -0.733  55.538  45.172  1.00 69.96           C  
ANISOU 1529  CG  LYS A 947     6755   9204  10621    435    873  -1000       C  
ATOM   1530  CD  LYS A 947      -0.027  56.907  45.241  1.00 66.79           C  
ANISOU 1530  CD  LYS A 947     6417   8708  10251    486    930  -1015       C  
ATOM   1531  CE  LYS A 947      -0.697  57.835  44.266  1.00 67.40           C  
ANISOU 1531  CE  LYS A 947     6364   8692  10553    615    849   -932       C  
ATOM   1532  NZ  LYS A 947       0.047  59.100  44.111  1.00 73.56           N  
ANISOU 1532  NZ  LYS A 947     7212   9366  11369    666    876   -916       N  
ATOM   1533  N   SER A 948       1.818  52.441  47.433  1.00 50.05           N  
ANISOU 1533  N   SER A 948     4668   6939   7411     93    946  -1059       N  
ATOM   1534  CA  SER A 948       2.559  52.020  48.624  1.00 50.60           C  
ANISOU 1534  CA  SER A 948     4864   7062   7300    -14   1027  -1094       C  
ATOM   1535  C   SER A 948       4.046  51.857  48.338  1.00 55.67           C  
ANISOU 1535  C   SER A 948     5635   7734   7784    -20    919  -1034       C  
ATOM   1536  O   SER A 948       4.857  52.158  49.212  1.00 57.35           O  
ANISOU 1536  O   SER A 948     5944   7970   7877    -83    970  -1068       O  
ATOM   1537  CB  SER A 948       1.957  50.778  49.277  1.00 52.05           C  
ANISOU 1537  CB  SER A 948     5037   7299   7441   -103   1075  -1089       C  
ATOM   1538  OG  SER A 948       2.199  49.626  48.489  1.00 60.72           O  
ANISOU 1538  OG  SER A 948     6151   8421   8501    -98    929  -1002       O  
ATOM   1539  N   ASP A 949       4.407  51.443  47.106  1.00 50.93           N  
ANISOU 1539  N   ASP A 949     5031   7133   7186     44    772   -951       N  
ATOM   1540  CA  ASP A 949       5.804  51.316  46.690  1.00 50.24           C  
ANISOU 1540  CA  ASP A 949     5043   7067   6980     54    684   -892       C  
ATOM   1541  C   ASP A 949       6.580  52.631  46.774  1.00 53.08           C  
ANISOU 1541  C   ASP A 949     5437   7389   7341     73    714   -913       C  
ATOM   1542  O   ASP A 949       7.773  52.612  47.093  1.00 50.93           O  
ANISOU 1542  O   ASP A 949     5246   7146   6960     34    693   -894       O  
ATOM   1543  CB  ASP A 949       5.865  50.864  45.234  1.00 51.45           C  
ANISOU 1543  CB  ASP A 949     5179   7217   7153    130    553   -820       C  
ATOM   1544  CG  ASP A 949       5.966  49.386  45.041  1.00 52.66           C  
ANISOU 1544  CG  ASP A 949     5365   7405   7239     99    490   -787       C  
ATOM   1545  OD1 ASP A 949       5.970  48.656  46.064  1.00 50.44           O  
ANISOU 1545  OD1 ASP A 949     5112   7147   6903     20    542   -798       O  
ATOM   1546  OD2 ASP A 949       6.070  48.953  43.866  1.00 46.86           O  
ANISOU 1546  OD2 ASP A 949     4636   6669   6498    150    390   -748       O  
ATOM   1547  N   VAL A 950       5.933  53.758  46.381  1.00 49.42           N  
ANISOU 1547  N   VAL A 950     4902   6853   7021    138    748   -939       N  
ATOM   1548  CA  VAL A 950       6.608  55.060  46.379  1.00 49.20           C  
ANISOU 1548  CA  VAL A 950     4903   6764   7026    157    779   -956       C  
ATOM   1549  C   VAL A 950       6.911  55.493  47.840  1.00 53.49           C  
ANISOU 1549  C   VAL A 950     5507   7309   7506     58    900  -1065       C  
ATOM   1550  O   VAL A 950       8.015  56.005  48.106  1.00 52.73           O  
ANISOU 1550  O   VAL A 950     5484   7210   7342     16    890  -1073       O  
ATOM   1551  CB  VAL A 950       5.860  56.132  45.518  1.00 51.47           C  
ANISOU 1551  CB  VAL A 950     5101   6954   7501    261    775   -934       C  
ATOM   1552  CG1 VAL A 950       6.509  57.517  45.638  1.00 50.82           C  
ANISOU 1552  CG1 VAL A 950     5052   6781   7477    269    827   -959       C  
ATOM   1553  CG2 VAL A 950       5.813  55.702  44.058  1.00 49.80           C  
ANISOU 1553  CG2 VAL A 950     4866   6764   7291    338    631   -817       C  
ATOM   1554  N   TYR A 951       5.962  55.210  48.772  1.00 49.62           N  
ANISOU 1554  N   TYR A 951     4991   6837   7026      9   1010  -1147       N  
ATOM   1555  CA  TYR A 951       6.106  55.477  50.204  1.00 50.20           C  
ANISOU 1555  CA  TYR A 951     5139   6933   7002   -100   1135  -1260       C  
ATOM   1556  C   TYR A 951       7.322  54.723  50.754  1.00 53.69           C  
ANISOU 1556  C   TYR A 951     5696   7472   7233   -194   1058  -1215       C  
ATOM   1557  O   TYR A 951       8.228  55.342  51.326  1.00 53.88           O  
ANISOU 1557  O   TYR A 951     5798   7500   7174   -259   1062  -1260       O  
ATOM   1558  CB  TYR A 951       4.827  55.141  51.010  1.00 52.03           C  
ANISOU 1558  CB  TYR A 951     5319   7180   7270   -136   1278  -1339       C  
ATOM   1559  CG  TYR A 951       4.966  55.484  52.489  1.00 53.64           C  
ANISOU 1559  CG  TYR A 951     5623   7415   7344   -257   1425  -1467       C  
ATOM   1560  CD1 TYR A 951       5.617  54.617  53.368  1.00 55.51           C  
ANISOU 1560  CD1 TYR A 951     5977   7764   7352   -376   1399  -1442       C  
ATOM   1561  CD2 TYR A 951       4.529  56.707  52.985  1.00 55.15           C  
ANISOU 1561  CD2 TYR A 951     5803   7520   7634   -253   1580  -1610       C  
ATOM   1562  CE1 TYR A 951       5.809  54.947  54.705  1.00 57.42           C  
ANISOU 1562  CE1 TYR A 951     6330   8050   7435   -500   1513  -1554       C  
ATOM   1563  CE2 TYR A 951       4.724  57.057  54.324  1.00 58.42           C  
ANISOU 1563  CE2 TYR A 951     6332   7966   7900   -376   1715  -1747       C  
ATOM   1564  CZ  TYR A 951       5.371  56.171  55.182  1.00 64.28           C  
ANISOU 1564  CZ  TYR A 951     7201   8842   8383   -505   1674  -1717       C  
ATOM   1565  OH  TYR A 951       5.632  56.496  56.495  1.00 60.40           O  
ANISOU 1565  OH  TYR A 951     6843   8402   7706   -641   1784  -1845       O  
ATOM   1566  N   ALA A 952       7.339  53.390  50.554  1.00 49.15           N  
ANISOU 1566  N   ALA A 952     5123   6966   6587   -202    980  -1124       N  
ATOM   1567  CA  ALA A 952       8.406  52.486  50.995  1.00 46.19           C  
ANISOU 1567  CA  ALA A 952     4835   6673   6043   -272    894  -1052       C  
ATOM   1568  C   ALA A 952       9.758  52.878  50.388  1.00 49.31           C  
ANISOU 1568  C   ALA A 952     5254   7059   6423   -242    787   -995       C  
ATOM   1569  O   ALA A 952      10.764  52.896  51.112  1.00 50.23           O  
ANISOU 1569  O   ALA A 952     5438   7225   6421   -322    751   -989       O  
ATOM   1570  CB  ALA A 952       8.026  51.035  50.721  1.00 45.24           C  
ANISOU 1570  CB  ALA A 952     4695   6588   5907   -264    842   -966       C  
ATOM   1571  N   PHE A 953       9.759  53.353  49.118  1.00 44.84           N  
ANISOU 1571  N   PHE A 953     4629   6431   5979   -137    745   -959       N  
ATOM   1572  CA  PHE A 953      10.963  53.875  48.462  1.00 43.29           C  
ANISOU 1572  CA  PHE A 953     4444   6216   5789   -108    674   -906       C  
ATOM   1573  C   PHE A 953      11.495  55.137  49.198  1.00 47.12           C  
ANISOU 1573  C   PHE A 953     4966   6667   6272   -176    727   -990       C  
ATOM   1574  O   PHE A 953      12.689  55.259  49.413  1.00 47.43           O  
ANISOU 1574  O   PHE A 953     5037   6734   6249   -227    669   -963       O  
ATOM   1575  CB  PHE A 953      10.776  54.110  46.936  1.00 44.73           C  
ANISOU 1575  CB  PHE A 953     4571   6345   6078      9    629   -841       C  
ATOM   1576  CG  PHE A 953      12.068  54.542  46.270  1.00 46.99           C  
ANISOU 1576  CG  PHE A 953     4873   6622   6360     29    577   -775       C  
ATOM   1577  CD1 PHE A 953      13.207  53.735  46.330  1.00 48.92           C  
ANISOU 1577  CD1 PHE A 953     5142   6928   6517      3    514   -713       C  
ATOM   1578  CD2 PHE A 953      12.190  55.806  45.707  1.00 50.38           C  
ANISOU 1578  CD2 PHE A 953     5284   6972   6885     66    601   -773       C  
ATOM   1579  CE1 PHE A 953      14.422  54.162  45.792  1.00 49.34           C  
ANISOU 1579  CE1 PHE A 953     5190   6974   6583     14    484   -656       C  
ATOM   1580  CE2 PHE A 953      13.408  56.232  45.169  1.00 52.77           C  
ANISOU 1580  CE2 PHE A 953     5596   7265   7188     68    570   -709       C  
ATOM   1581  CZ  PHE A 953      14.508  55.389  45.177  1.00 49.97           C  
ANISOU 1581  CZ  PHE A 953     5254   6982   6749     44    515   -653       C  
ATOM   1582  N   GLY A 954      10.593  55.982  49.672  1.00 47.33           N  
ANISOU 1582  N   GLY A 954     4982   6632   6368   -186    838  -1099       N  
ATOM   1583  CA  GLY A 954      10.897  57.155  50.493  1.00 48.14           C  
ANISOU 1583  CA  GLY A 954     5132   6687   6472   -262    912  -1216       C  
ATOM   1584  C   GLY A 954      11.603  56.808  51.793  1.00 50.13           C  
ANISOU 1584  C   GLY A 954     5477   7034   6535   -404    897  -1263       C  
ATOM   1585  O   GLY A 954      12.581  57.463  52.159  1.00 50.65           O  
ANISOU 1585  O   GLY A 954     5587   7096   6562   -478    863  -1297       O  
ATOM   1586  N   VAL A 955      11.160  55.721  52.449  1.00 45.13           N  
ANISOU 1586  N   VAL A 955     4873   6492   5782   -448    906  -1247       N  
ATOM   1587  CA  VAL A 955      11.738  55.197  53.689  1.00 45.78           C  
ANISOU 1587  CA  VAL A 955     5052   6683   5659   -583    875  -1257       C  
ATOM   1588  C   VAL A 955      13.190  54.680  53.406  1.00 50.22           C  
ANISOU 1588  C   VAL A 955     5615   7302   6163   -596    704  -1128       C  
ATOM   1589  O   VAL A 955      14.090  54.998  54.186  1.00 51.91           O  
ANISOU 1589  O   VAL A 955     5888   7566   6269   -704    648  -1154       O  
ATOM   1590  CB  VAL A 955      10.801  54.135  54.352  1.00 50.08           C  
ANISOU 1590  CB  VAL A 955     5620   7297   6110   -619    938  -1246       C  
ATOM   1591  CG1 VAL A 955      11.411  53.600  55.642  1.00 51.59           C  
ANISOU 1591  CG1 VAL A 955     5926   7606   6069   -763    895  -1232       C  
ATOM   1592  CG2 VAL A 955       9.405  54.713  54.639  1.00 49.91           C  
ANISOU 1592  CG2 VAL A 955     5573   7217   6173   -606   1124  -1379       C  
ATOM   1593  N   ILE A 956      13.417  53.974  52.241  1.00 44.09           N  
ANISOU 1593  N   ILE A 956     4766   6512   5474   -484    628  -1000       N  
ATOM   1594  CA  ILE A 956      14.734  53.523  51.793  1.00 43.74           C  
ANISOU 1594  CA  ILE A 956     4696   6500   5422   -469    497   -882       C  
ATOM   1595  C   ILE A 956      15.683  54.735  51.640  1.00 49.17           C  
ANISOU 1595  C   ILE A 956     5370   7147   6164   -499    474   -918       C  
ATOM   1596  O   ILE A 956      16.830  54.653  52.064  1.00 50.19           O  
ANISOU 1596  O   ILE A 956     5504   7332   6235   -569    378   -874       O  
ATOM   1597  CB  ILE A 956      14.699  52.714  50.448  1.00 46.03           C  
ANISOU 1597  CB  ILE A 956     4919   6763   5807   -337    458   -775       C  
ATOM   1598  CG1 ILE A 956      13.842  51.429  50.549  1.00 46.83           C  
ANISOU 1598  CG1 ILE A 956     5030   6891   5873   -317    466   -736       C  
ATOM   1599  CG2 ILE A 956      16.163  52.392  49.972  1.00 45.24           C  
ANISOU 1599  CG2 ILE A 956     4781   6686   5721   -316    353   -668       C  
ATOM   1600  CD1 ILE A 956      14.504  50.256  51.290  1.00 51.90           C  
ANISOU 1600  CD1 ILE A 956     5706   7606   6408   -373    383   -643       C  
ATOM   1601  N   LEU A 957      15.224  55.812  50.978  1.00 45.65           N  
ANISOU 1601  N   LEU A 957     4897   6600   5848   -444    553   -980       N  
ATOM   1602  CA  LEU A 957      16.032  57.025  50.778  1.00 48.74           C  
ANISOU 1602  CA  LEU A 957     5276   6926   6317   -475    548  -1012       C  
ATOM   1603  C   LEU A 957      16.417  57.606  52.125  1.00 53.34           C  
ANISOU 1603  C   LEU A 957     5931   7539   6797   -630    547  -1128       C  
ATOM   1604  O   LEU A 957      17.553  58.020  52.302  1.00 52.60           O  
ANISOU 1604  O   LEU A 957     5829   7458   6699   -704    470  -1117       O  
ATOM   1605  CB  LEU A 957      15.274  58.087  49.943  1.00 49.91           C  
ANISOU 1605  CB  LEU A 957     5392   6942   6629   -390    644  -1055       C  
ATOM   1606  CG  LEU A 957      14.903  57.728  48.500  1.00 53.07           C  
ANISOU 1606  CG  LEU A 957     5731   7312   7122   -246    632   -942       C  
ATOM   1607  CD1 LEU A 957      13.997  58.784  47.919  1.00 53.08           C  
ANISOU 1607  CD1 LEU A 957     5707   7188   7272   -174    714   -980       C  
ATOM   1608  CD2 LEU A 957      16.162  57.591  47.634  1.00 56.40           C  
ANISOU 1608  CD2 LEU A 957     6116   7751   7564   -220    558   -822       C  
ATOM   1609  N   LEU A 958      15.495  57.532  53.103  1.00 50.36           N  
ANISOU 1609  N   LEU A 958     5626   7187   6322   -688    628  -1237       N  
ATOM   1610  CA  LEU A 958      15.773  57.993  54.457  1.00 51.52           C  
ANISOU 1610  CA  LEU A 958     5870   7381   6324   -848    635  -1363       C  
ATOM   1611  C   LEU A 958      16.806  57.123  55.182  1.00 55.76           C  
ANISOU 1611  C   LEU A 958     6439   8060   6687   -949    479  -1273       C  
ATOM   1612  O   LEU A 958      17.555  57.644  55.979  1.00 56.07           O  
ANISOU 1612  O   LEU A 958     6531   8137   6635  -1083    417  -1339       O  
ATOM   1613  CB  LEU A 958      14.481  58.154  55.276  1.00 51.82           C  
ANISOU 1613  CB  LEU A 958     5980   7410   6299   -882    793  -1508       C  
ATOM   1614  CG  LEU A 958      13.594  59.324  54.848  1.00 55.49           C  
ANISOU 1614  CG  LEU A 958     6414   7717   6951   -811    948  -1631       C  
ATOM   1615  CD1 LEU A 958      12.408  59.501  55.810  1.00 55.26           C  
ANISOU 1615  CD1 LEU A 958     6450   7684   6861   -857   1124  -1792       C  
ATOM   1616  CD2 LEU A 958      14.409  60.613  54.734  1.00 57.55           C  
ANISOU 1616  CD2 LEU A 958     6683   7876   7306   -860    933  -1705       C  
ATOM   1617  N   GLU A 959      16.849  55.812  54.895  1.00 52.36           N  
ANISOU 1617  N   GLU A 959     5973   7700   6222   -884    408  -1122       N  
ATOM   1618  CA  GLU A 959      17.823  54.885  55.477  1.00 51.72           C  
ANISOU 1618  CA  GLU A 959     5901   7738   6013   -952    250  -1001       C  
ATOM   1619  C   GLU A 959      19.196  55.133  54.838  1.00 52.65           C  
ANISOU 1619  C   GLU A 959     5921   7843   6240   -935    128   -914       C  
ATOM   1620  O   GLU A 959      20.222  54.970  55.492  1.00 52.44           O  
ANISOU 1620  O   GLU A 959     5893   7899   6133  -1032    -11   -863       O  
ATOM   1621  CB  GLU A 959      17.388  53.433  55.217  1.00 51.99           C  
ANISOU 1621  CB  GLU A 959     5915   7810   6028   -868    232   -867       C  
ATOM   1622  CG  GLU A 959      16.161  52.998  55.993  1.00 56.65           C  
ANISOU 1622  CG  GLU A 959     6593   8434   6498   -909    338   -923       C  
ATOM   1623  CD  GLU A 959      15.819  51.552  55.711  1.00 68.67           C  
ANISOU 1623  CD  GLU A 959     8090   9977   8023   -838    310   -782       C  
ATOM   1624  OE1 GLU A 959      15.077  51.320  54.733  1.00 61.02           O  
ANISOU 1624  OE1 GLU A 959     7061   8934   7190   -720    381   -777       O  
ATOM   1625  OE2 GLU A 959      16.323  50.652  56.424  1.00 60.93           O  
ANISOU 1625  OE2 GLU A 959     7149   9082   6919   -900    207   -671       O  
ATOM   1626  N   LEU A 960      19.209  55.531  53.559  1.00 47.34           N  
ANISOU 1626  N   LEU A 960     5165   7072   5752   -815    181   -890       N  
ATOM   1627  CA  LEU A 960      20.446  55.846  52.828  1.00 45.59           C  
ANISOU 1627  CA  LEU A 960     4842   6827   5654   -793    105   -810       C  
ATOM   1628  C   LEU A 960      21.059  57.122  53.337  1.00 54.80           C  
ANISOU 1628  C   LEU A 960     6023   7964   6836   -921     87   -914       C  
ATOM   1629  O   LEU A 960      22.293  57.178  53.491  1.00 57.68           O  
ANISOU 1629  O   LEU A 960     6322   8372   7220   -988    -34   -854       O  
ATOM   1630  CB  LEU A 960      20.175  55.964  51.334  1.00 43.34           C  
ANISOU 1630  CB  LEU A 960     4488   6449   5531   -640    187   -759       C  
ATOM   1631  CG  LEU A 960      20.002  54.626  50.609  1.00 46.29           C  
ANISOU 1631  CG  LEU A 960     4823   6850   5914   -517    172   -639       C  
ATOM   1632  CD1 LEU A 960      19.401  54.836  49.227  1.00 44.17           C  
ANISOU 1632  CD1 LEU A 960     4527   6498   5759   -385    263   -625       C  
ATOM   1633  CD2 LEU A 960      21.328  53.871  50.547  1.00 47.14           C  
ANISOU 1633  CD2 LEU A 960     4851   7018   6042   -514     57   -510       C  
ATOM   1634  N   LEU A 961      20.203  58.125  53.680  1.00 50.24           N  
ANISOU 1634  N   LEU A 961     5526   7310   6254   -964    204  -1078       N  
ATOM   1635  CA  LEU A 961      20.623  59.449  54.160  1.00 52.10           C  
ANISOU 1635  CA  LEU A 961     5794   7484   6519  -1090    214  -1213       C  
ATOM   1636  C   LEU A 961      21.047  59.536  55.623  1.00 59.05           C  
ANISOU 1636  C   LEU A 961     6767   8465   7206  -1280    122  -1309       C  
ATOM   1637  O   LEU A 961      21.949  60.296  55.953  1.00 61.43           O  
ANISOU 1637  O   LEU A 961     7057   8755   7528  -1402     45  -1362       O  
ATOM   1638  CB  LEU A 961      19.510  60.471  53.898  1.00 52.16           C  
ANISOU 1638  CB  LEU A 961     5847   7346   6627  -1044    388  -1352       C  
ATOM   1639  CG  LEU A 961      19.254  60.838  52.427  1.00 54.60           C  
ANISOU 1639  CG  LEU A 961     6070   7531   7144   -887    461  -1269       C  
ATOM   1640  CD1 LEU A 961      17.928  61.559  52.296  1.00 54.40           C  
ANISOU 1640  CD1 LEU A 961     6084   7382   7204   -823    619  -1382       C  
ATOM   1641  CD2 LEU A 961      20.417  61.695  51.847  1.00 55.25           C  
ANISOU 1641  CD2 LEU A 961     6082   7541   7370   -924    417  -1225       C  
ATOM   1642  N   THR A 962      20.366  58.811  56.496  1.00 56.56           N  
ANISOU 1642  N   THR A 962     6548   8244   6699  -1316    134  -1335       N  
ATOM   1643  CA  THR A 962      20.591  58.833  57.943  1.00 58.76           C  
ANISOU 1643  CA  THR A 962     6947   8636   6742  -1502     60  -1427       C  
ATOM   1644  C   THR A 962      21.555  57.728  58.404  1.00 64.10           C  
ANISOU 1644  C   THR A 962     7592   9470   7294  -1553   -152  -1253       C  
ATOM   1645  O   THR A 962      22.205  57.876  59.440  1.00 64.00           O  
ANISOU 1645  O   THR A 962     7644   9557   7116  -1722   -284  -1291       O  
ATOM   1646  CB  THR A 962      19.248  58.680  58.676  1.00 62.89           C  
ANISOU 1646  CB  THR A 962     7603   9177   7115  -1519    215  -1549       C  
ATOM   1647  OG1 THR A 962      18.738  57.394  58.358  1.00 58.37           O  
ANISOU 1647  OG1 THR A 962     6997   8659   6521  -1406    217  -1395       O  
ATOM   1648  CG2 THR A 962      18.229  59.763  58.306  1.00 59.69           C  
ANISOU 1648  CG2 THR A 962     7216   8609   6854  -1461    430  -1722       C  
ATOM   1649  N   GLY A 963      21.597  56.625  57.654  1.00 53.70           N  
ANISOU 1649  N   GLY A 963     6782   7054   6567   -837   -163  -1315       N  
ATOM   1650  CA  GLY A 963      22.407  55.464  57.998  1.00 55.53           C  
ANISOU 1650  CA  GLY A 963     7012   7250   6838   -812   -420  -1204       C  
ATOM   1651  C   GLY A 963      21.721  54.618  59.057  1.00 64.17           C  
ANISOU 1651  C   GLY A 963     8318   8309   7755   -945   -496  -1091       C  
ATOM   1652  O   GLY A 963      22.349  53.727  59.630  1.00 67.58           O  
ANISOU 1652  O   GLY A 963     8807   8684   8185   -970   -755   -967       O  
ATOM   1653  N   LYS A 964      20.424  54.885  59.317  1.00 59.73           N  
ANISOU 1653  N   LYS A 964     7853   7791   7050  -1033   -276  -1112       N  
ATOM   1654  CA  LYS A 964      19.603  54.152  60.282  1.00 61.99           C  
ANISOU 1654  CA  LYS A 964     8313   8104   7137  -1198   -284   -978       C  
ATOM   1655  C   LYS A 964      18.704  53.144  59.589  1.00 68.27           C  
ANISOU 1655  C   LYS A 964     9055   8826   8060  -1164   -266   -885       C  
ATOM   1656  O   LYS A 964      18.207  53.433  58.507  1.00 67.98           O  
ANISOU 1656  O   LYS A 964     8877   8774   8178  -1042   -119   -977       O  
ATOM   1657  CB  LYS A 964      18.729  55.132  61.092  1.00 64.06           C  
ANISOU 1657  CB  LYS A 964     8684   8512   7143  -1318    -20  -1069       C  
ATOM   1658  CG  LYS A 964      19.512  55.938  62.119  1.00 63.67           C  
ANISOU 1658  CG  LYS A 964     8795   8517   6882  -1418    -97  -1148       C  
ATOM   1659  CD  LYS A 964      18.669  57.080  62.663  1.00 69.73           C  
ANISOU 1659  CD  LYS A 964     9661   9394   7439  -1452    196  -1330       C  
ATOM   1660  CE  LYS A 964      19.226  57.716  63.920  1.00 65.51           C  
ANISOU 1660  CE  LYS A 964     9377   8920   6595  -1594    113  -1417       C  
ATOM   1661  NZ  LYS A 964      20.431  58.552  63.670  1.00 76.33           N  
ANISOU 1661  NZ  LYS A 964    10727  10177   8099  -1563    -79  -1520       N  
ATOM   1662  N   ILE A 965      18.467  51.973  60.207  1.00 67.38           N  
ANISOU 1662  N   ILE A 965     9070   8653   7880  -1298   -442   -685       N  
ATOM   1663  CA  ILE A 965      17.521  50.989  59.671  1.00 67.41           C  
ANISOU 1663  CA  ILE A 965     9054   8562   7996  -1329   -464   -571       C  
ATOM   1664  C   ILE A 965      16.105  51.537  59.984  1.00 71.56           C  
ANISOU 1664  C   ILE A 965     9544   9277   8369  -1471   -143   -559       C  
ATOM   1665  O   ILE A 965      15.926  52.193  61.005  1.00 73.15           O  
ANISOU 1665  O   ILE A 965     9825   9657   8313  -1590     16   -573       O  
ATOM   1666  CB  ILE A 965      17.754  49.578  60.266  1.00 72.82           C  
ANISOU 1666  CB  ILE A 965     9902   9085   8680  -1454   -799   -330       C  
ATOM   1667  N   ALA A 966      15.133  51.315  59.096  1.00 66.78           N  
ANISOU 1667  N   ALA A 966     8808   8642   7921  -1442    -49   -552       N  
ATOM   1668  CA  ALA A 966      13.761  51.834  59.205  1.00 66.63           C  
ANISOU 1668  CA  ALA A 966     8671   8810   7836  -1532    254   -542       C  
ATOM   1669  C   ALA A 966      13.024  51.517  60.538  1.00 77.61           C  
ANISOU 1669  C   ALA A 966    10142  10396   8950  -1804    365   -348       C  
ATOM   1670  O   ALA A 966      12.398  52.418  61.116  1.00 79.39           O  
ANISOU 1670  O   ALA A 966    10310  10855   9000  -1824    679   -436       O  
ATOM   1671  CB  ALA A 966      12.933  51.377  58.017  1.00 65.43           C  
ANISOU 1671  CB  ALA A 966     8371   8562   7926  -1490    227   -511       C  
ATOM   1672  N   GLY A 967      13.135  50.277  61.020  1.00 76.85           N  
ANISOU 1672  N   GLY A 967    10186  10205   8809  -2001    107    -94       N  
ATOM   1673  CA  GLY A 967      12.490  49.829  62.254  1.00 79.49           C  
ANISOU 1673  CA  GLY A 967    10611  10735   8855  -2310    179    154       C  
ATOM   1674  C   GLY A 967      13.160  50.194  63.574  1.00 84.72           C  
ANISOU 1674  C   GLY A 967    11487  11549   9154  -2411    195    158       C  
ATOM   1675  O   GLY A 967      12.709  49.732  64.623  1.00 88.31           O  
ANISOU 1675  O   GLY A 967    12053  12182   9320  -2693    231    392       O  
ATOM   1676  N   GLU A 968      14.220  51.014  63.572  1.00 78.69           N  
ANISOU 1676  N   GLU A 968    10790  10734   8375  -2221    156    -77       N  
ATOM   1677  CA  GLU A 968      14.847  51.353  64.849  1.00 80.88           C  
ANISOU 1677  CA  GLU A 968    11296  11146   8289  -2346    125    -72       C  
ATOM   1678  C   GLU A 968      14.173  52.581  65.507  1.00 87.14           C  
ANISOU 1678  C   GLU A 968    12085  12243   8780  -2346    548   -282       C  
ATOM   1679  O   GLU A 968      13.875  53.566  64.832  1.00 85.58           O  
ANISOU 1679  O   GLU A 968    11724  12051   8740  -2129    778   -539       O  
ATOM   1680  CB  GLU A 968      16.387  51.482  64.741  1.00 80.79           C  
ANISOU 1680  CB  GLU A 968    11379  10934   8384  -2207   -198   -165       C  
ATOM   1681  CG  GLU A 968      16.932  52.757  64.125  1.00 83.52           C  
ANISOU 1681  CG  GLU A 968    11616  11258   8861  -1964    -74   -486       C  
ATOM   1682  CD  GLU A 968      18.447  52.836  64.119  1.00101.76           C  
ANISOU 1682  CD  GLU A 968    13975  13421  11266  -1879   -394   -525       C  
ATOM   1683  OE1 GLU A 968      19.074  52.172  63.262  1.00 87.03           O  
ANISOU 1683  OE1 GLU A 968    11993  11362   9714  -1734   -619   -479       O  
ATOM   1684  OE2 GLU A 968      19.006  53.585  64.953  1.00 98.20           O  
ANISOU 1684  OE2 GLU A 968    13670  13060  10583  -1950   -418   -616       O  
ATOM   1685  N   ILE A 969      13.881  52.488  66.810  1.00 87.84           N  
ANISOU 1685  N   ILE A 969    12360  12583   8431  -2586    650   -167       N  
ATOM   1686  CA  ILE A 969      13.242  53.579  67.550  1.00 90.00           C  
ANISOU 1686  CA  ILE A 969    12665  13164   8367  -2570   1064   -395       C  
ATOM   1687  C   ILE A 969      14.285  54.643  67.872  1.00 93.96           C  
ANISOU 1687  C   ILE A 969    13360  13589   8753  -2438    982   -691       C  
ATOM   1688  O   ILE A 969      15.443  54.302  68.131  1.00 93.83           O  
ANISOU 1688  O   ILE A 969    13521  13416   8715  -2508    606   -603       O  
ATOM   1689  CB  ILE A 969      12.507  53.063  68.806  1.00 97.74           C  
ANISOU 1689  CB  ILE A 969    13774  14492   8870  -2886   1239   -165       C  
ATOM   1690  N   ILE A 970      13.895  55.928  67.798  1.00 90.63           N  
ANISOU 1690  N   ILE A 970    12888  13245   8304  -2241   1298  -1036       N  
ATOM   1691  CA  ILE A 970      14.798  57.058  68.049  1.00 90.50           C  
ANISOU 1691  CA  ILE A 970    13059  13119   8207  -2128   1214  -1338       C  
ATOM   1692  C   ILE A 970      14.264  57.958  69.155  1.00 98.05           C  
ANISOU 1692  C   ILE A 970    14217  14331   8704  -2138   1538  -1599       C  
ATOM   1693  O   ILE A 970      13.065  58.243  69.182  1.00 97.61           O  
ANISOU 1693  O   ILE A 970    14007  14485   8597  -2047   1945  -1696       O  
ATOM   1694  CB  ILE A 970      15.104  57.844  66.740  1.00 89.46           C  
ANISOU 1694  CB  ILE A 970    12720  12722   8547  -1853   1181  -1533       C  
ATOM   1695  N   CYS A 971      15.154  58.398  70.066  1.00 99.04           N  
ANISOU 1695  N   CYS A 971    14683  14448   8498  -2240   1349  -1723       N  
ATOM   1696  CA  CYS A 971      14.800  59.276  71.190  1.00104.80           C  
ANISOU 1696  CA  CYS A 971    15690  15400   8729  -2248   1612  -2024       C  
ATOM   1697  C   CYS A 971      14.435  60.678  70.716  1.00108.90           C  
ANISOU 1697  C   CYS A 971    16141  15792   9442  -1931   1857  -2452       C  
ATOM   1698  O   CYS A 971      15.320  61.496  70.446  1.00108.22           O  
ANISOU 1698  O   CYS A 971    16173  15426   9520  -1849   1614  -2647       O  
ATOM   1699  CB  CYS A 971      15.907  59.308  72.237  1.00108.43           C  
ANISOU 1699  CB  CYS A 971    16559  15851   8789  -2470   1266  -2024       C  
ATOM   1700  SG  CYS A 971      15.826  57.958  73.437  1.00116.78           S  
ANISOU 1700  SG  CYS A 971    17835  17225   9310  -2867   1161  -1606       S  
ATOM   1701  N   MET A 972      13.121  60.926  70.569  1.00105.87           N  
ANISOU 1701  N   MET A 972    15538  15605   9084  -1760   2314  -2567       N  
ATOM   1702  CA  MET A 972      12.533  62.190  70.120  1.00119.26           C  
ANISOU 1702  CA  MET A 972    17128  17191  10995  -1422   2582  -2954       C  
ATOM   1703  C   MET A 972      11.050  62.180  70.482  1.00140.38           C  
ANISOU 1703  C   MET A 972    19600  20238  13500  -1310   3115  -3026       C  
ATOM   1704  O   MET A 972      10.523  63.190  70.935  1.00103.67           O  
ANISOU 1704  O   MET A 972    15036  15665   8689  -1082   3420  -3419       O  
ATOM   1705  CB  MET A 972      12.727  62.374  68.598  1.00116.24           C  
ANISOU 1705  CB  MET A 972    16444  16467  11256  -1247   2409  -2886       C  
ATOM   1706  CG  MET A 972      12.193  63.684  68.060  1.00119.90           C  
ANISOU 1706  CG  MET A 972    16810  16756  11991   -911   2605  -3236       C  
ATOM   1707  SD  MET A 972      13.490  64.715  67.362  1.00121.28           S  
ANISOU 1707  SD  MET A 972    17142  16447  12490   -845   2190  -3390       S  
ATOM   1708  CE  MET A 972      12.541  66.137  66.907  1.00119.74           C  
ANISOU 1708  CE  MET A 972    16847  16080  12568   -455   2465  -3768       C  
ATOM   1709  N   VAL A 977       9.986  59.400  67.269  1.00 98.89           N  
ANISOU 1709  N   VAL A 977    13224  14797   9553  -1434   2848  -1971       N  
ATOM   1710  CA  VAL A 977      10.237  58.017  67.655  1.00 98.78           C  
ANISOU 1710  CA  VAL A 977    13311  14905   9315  -1776   2663  -1597       C  
ATOM   1711  C   VAL A 977      10.379  57.151  66.415  1.00 96.40           C  
ANISOU 1711  C   VAL A 977    12831  14350   9446  -1828   2340  -1310       C  
ATOM   1712  O   VAL A 977      11.150  56.198  66.388  1.00 94.90           O  
ANISOU 1712  O   VAL A 977    12802  14019   9237  -2004   1983  -1094       O  
ATOM   1713  CB  VAL A 977       9.100  57.465  68.531  1.00107.68           C  
ANISOU 1713  CB  VAL A 977    14346  16485  10082  -1957   3032  -1445       C  
ATOM   1714  N   ASP A 978       9.615  57.499  65.391  1.00 89.53           N  
ANISOU 1714  N   ASP A 978    11635  13413   8967  -1652   2452  -1331       N  
ATOM   1715  CA  ASP A 978       9.631  56.798  64.119  1.00 84.71           C  
ANISOU 1715  CA  ASP A 978    10844  12567   8776  -1647   2189  -1133       C  
ATOM   1716  C   ASP A 978      10.703  57.433  63.243  1.00 80.56           C  
ANISOU 1716  C   ASP A 978    10389  11713   8507  -1434   1959  -1331       C  
ATOM   1717  O   ASP A 978      10.920  58.628  63.319  1.00 79.88           O  
ANISOU 1717  O   ASP A 978    10408  11593   8351  -1281   2060  -1609       O  
ATOM   1718  CB  ASP A 978       8.258  56.943  63.461  1.00 87.65           C  
ANISOU 1718  CB  ASP A 978    10837  13073   9391  -1565   2444  -1084       C  
ATOM   1719  CG  ASP A 978       8.078  56.038  62.272  1.00 98.69           C  
ANISOU 1719  CG  ASP A 978    12035  14270  11192  -1569   2212   -898       C  
ATOM   1720  OD1 ASP A 978       8.557  54.889  62.320  1.00100.73           O  
ANISOU 1720  OD1 ASP A 978    12386  14421  11464  -1776   1926   -645       O  
ATOM   1721  OD2 ASP A 978       7.444  56.475  61.293  1.00101.79           O  
ANISOU 1721  OD2 ASP A 978    12178  14622  11874  -1375   2313   -993       O  
ATOM   1722  N   LEU A 979      11.375  56.642  62.416  1.00 72.07           N  
ANISOU 1722  N   LEU A 979     9270  10404   7710  -1434   1651  -1193       N  
ATOM   1723  CA  LEU A 979      12.415  57.179  61.543  1.00 67.16           C  
ANISOU 1723  CA  LEU A 979     8678   9530   7309  -1262   1459  -1340       C  
ATOM   1724  C   LEU A 979      11.864  58.280  60.658  1.00 68.02           C  
ANISOU 1724  C   LEU A 979     8606   9578   7659  -1031   1631  -1530       C  
ATOM   1725  O   LEU A 979      12.427  59.362  60.579  1.00 66.74           O  
ANISOU 1725  O   LEU A 979     8536   9311   7513   -910   1632  -1737       O  
ATOM   1726  CB  LEU A 979      13.036  56.080  60.682  1.00 64.46           C  
ANISOU 1726  CB  LEU A 979     8323   8997   7173  -1291   1128  -1168       C  
ATOM   1727  CG  LEU A 979      13.921  56.544  59.523  1.00 65.70           C  
ANISOU 1727  CG  LEU A 979     8445   8954   7565  -1117    966  -1287       C  
ATOM   1728  CD1 LEU A 979      14.929  57.584  59.976  1.00 65.87           C  
ANISOU 1728  CD1 LEU A 979     8628   8941   7458  -1107    899  -1434       C  
ATOM   1729  CD2 LEU A 979      14.627  55.374  58.864  1.00 64.89           C  
ANISOU 1729  CD2 LEU A 979     8313   8708   7633  -1111    695  -1149       C  
ATOM   1730  N   THR A 980      10.742  58.007  60.007  1.00 64.24           N  
ANISOU 1730  N   THR A 980     7877   9150   7380   -989   1741  -1438       N  
ATOM   1731  CA  THR A 980      10.116  58.984  59.130  1.00 63.18           C  
ANISOU 1731  CA  THR A 980     7547   8954   7504   -774   1869  -1569       C  
ATOM   1732  C   THR A 980       9.593  60.170  59.918  1.00 71.34           C  
ANISOU 1732  C   THR A 980     8607  10089   8410   -639   2156  -1812       C  
ATOM   1733  O   THR A 980       9.623  61.297  59.444  1.00 71.27           O  
ANISOU 1733  O   THR A 980     8602   9920   8556   -446   2167  -2001       O  
ATOM   1734  CB  THR A 980       8.972  58.364  58.321  1.00 63.63           C  
ANISOU 1734  CB  THR A 980     7326   9072   7777   -794   1895  -1390       C  
ATOM   1735  OG1 THR A 980       7.862  58.113  59.185  1.00 70.95           O  
ANISOU 1735  OG1 THR A 980     8146  10268   8542   -919   2123  -1294       O  
ATOM   1736  CG2 THR A 980       9.420  57.067  57.710  1.00 58.62           C  
ANISOU 1736  CG2 THR A 980     6715   8304   7253   -908   1597  -1200       C  
ATOM   1737  N   ASP A 981       9.098  59.904  61.120  1.00 71.13           N  
ANISOU 1737  N   ASP A 981     8622  10322   8083   -744   2375  -1810       N  
ATOM   1738  CA  ASP A 981       8.598  60.949  61.986  1.00 74.53           C  
ANISOU 1738  CA  ASP A 981     9110  10896   8312   -610   2684  -2076       C  
ATOM   1739  C   ASP A 981       9.771  61.787  62.468  1.00 78.62           C  
ANISOU 1739  C   ASP A 981     9978  11249   8645   -587   2556  -2305       C  
ATOM   1740  O   ASP A 981       9.672  63.000  62.552  1.00 79.78           O  
ANISOU 1740  O   ASP A 981    10191  11308   8815   -378   2682  -2597       O  
ATOM   1741  CB  ASP A 981       7.836  60.347  63.161  1.00 80.00           C  
ANISOU 1741  CB  ASP A 981     9754  11966   8674   -772   2960  -1975       C  
ATOM   1742  CG  ASP A 981       6.446  59.896  62.776  1.00 88.83           C  
ANISOU 1742  CG  ASP A 981    10468  13288   9995   -783   3144  -1777       C  
ATOM   1743  OD1 ASP A 981       5.946  60.363  61.739  1.00 85.77           O  
ANISOU 1743  OD1 ASP A 981     9842  12744  10003   -618   3078  -1771       O  
ATOM   1744  OD2 ASP A 981       5.852  59.080  63.505  1.00 97.59           O  
ANISOU 1744  OD2 ASP A 981    11494  14728  10859   -979   3345  -1609       O  
ATOM   1745  N   TRP A 982      10.889  61.134  62.761  1.00 73.56           N  
ANISOU 1745  N   TRP A 982     9551  10533   7865   -791   2267  -2171       N  
ATOM   1746  CA  TRP A 982      12.086  61.833  63.213  1.00 73.79           C  
ANISOU 1746  CA  TRP A 982     9887  10404   7746   -816   2077  -2340       C  
ATOM   1747  C   TRP A 982      12.484  62.875  62.186  1.00 74.24           C  
ANISOU 1747  C   TRP A 982     9903  10165   8140   -635   1952  -2480       C  
ATOM   1748  O   TRP A 982      12.606  64.053  62.496  1.00 76.10           O  
ANISOU 1748  O   TRP A 982    10305  10282   8330   -527   1989  -2747       O  
ATOM   1749  CB  TRP A 982      13.238  60.851  63.422  1.00 71.29           C  
ANISOU 1749  CB  TRP A 982     9725  10063   7299  -1052   1757  -2122       C  
ATOM   1750  CG  TRP A 982      14.469  61.453  64.002  1.00 73.04           C  
ANISOU 1750  CG  TRP A 982    10227  10154   7369  -1113   1532  -2261       C  
ATOM   1751  CD1 TRP A 982      14.540  62.320  65.044  1.00 79.22           C  
ANISOU 1751  CD1 TRP A 982    11285  10989   7827  -1132   1611  -2503       C  
ATOM   1752  CD2 TRP A 982      15.817  61.226  63.577  1.00 70.89           C  
ANISOU 1752  CD2 TRP A 982     9976   9690   7270  -1169   1183  -2168       C  
ATOM   1753  NE1 TRP A 982      15.846  62.653  65.295  1.00 78.24           N  
ANISOU 1753  NE1 TRP A 982    11360  10691   7676  -1225   1292  -2550       N  
ATOM   1754  CE2 TRP A 982      16.650  61.993  64.407  1.00 76.73           C  
ANISOU 1754  CE2 TRP A 982    10988  10367   7798  -1250   1037  -2332       C  
ATOM   1755  CE3 TRP A 982      16.399  60.452  62.571  1.00 69.48           C  
ANISOU 1755  CE3 TRP A 982     9601   9399   7397  -1150    987  -1976       C  
ATOM   1756  CZ2 TRP A 982      18.031  62.009  64.265  1.00 75.24           C  
ANISOU 1756  CZ2 TRP A 982    10837  10027   7724  -1335    694  -2268       C  
ATOM   1757  CZ3 TRP A 982      17.769  60.467  62.434  1.00 70.39           C  
ANISOU 1757  CZ3 TRP A 982     9752   9390   7602  -1203    691  -1935       C  
ATOM   1758  CH2 TRP A 982      18.570  61.240  63.276  1.00 73.11           C  
ANISOU 1758  CH2 TRP A 982    10324   9692   7764  -1304    544  -2061       C  
ATOM   1759  N   VAL A 983      12.668  62.426  60.953  1.00 65.76           N  
ANISOU 1759  N   VAL A 983     8619   8976   7390   -607   1811  -2301       N  
ATOM   1760  CA  VAL A 983      13.063  63.311  59.860  1.00 63.82           C  
ANISOU 1760  CA  VAL A 983     8313   8482   7453   -479   1681  -2357       C  
ATOM   1761  C   VAL A 983      12.028  64.424  59.676  1.00 72.97           C  
ANISOU 1761  C   VAL A 983     9379   9572   8775   -248   1890  -2548       C  
ATOM   1762  O   VAL A 983      12.424  65.588  59.564  1.00 74.26           O  
ANISOU 1762  O   VAL A 983     9665   9511   9038   -155   1813  -2720       O  
ATOM   1763  CB  VAL A 983      13.364  62.537  58.545  1.00 62.56           C  
ANISOU 1763  CB  VAL A 983     7969   8269   7532   -511   1503  -2120       C  
ATOM   1764  CG1 VAL A 983      13.756  63.495  57.424  1.00 60.92           C  
ANISOU 1764  CG1 VAL A 983     7706   7850   7592   -410   1388  -2149       C  
ATOM   1765  CG2 VAL A 983      14.460  61.489  58.754  1.00 60.63           C  
ANISOU 1765  CG2 VAL A 983     7815   8060   7163   -682   1284  -1970       C  
ATOM   1766  N   ARG A 984      10.713  64.066  59.674  1.00 71.98           N  
ANISOU 1766  N   ARG A 984     9027   9628   8694   -160   2132  -2508       N  
ATOM   1767  CA  ARG A 984       9.583  65.001  59.541  1.00 75.23           C  
ANISOU 1767  CA  ARG A 984     9280  10013   9292     99   2351  -2677       C  
ATOM   1768  C   ARG A 984       9.548  66.006  60.682  1.00 82.73           C  
ANISOU 1768  C   ARG A 984    10455  10941  10035    230   2521  -3020       C  
ATOM   1769  O   ARG A 984       9.110  67.136  60.469  1.00 84.18           O  
ANISOU 1769  O   ARG A 984    10618  10939  10426    480   2580  -3229       O  
ATOM   1770  CB  ARG A 984       8.219  64.265  59.492  1.00 76.61           C  
ANISOU 1770  CB  ARG A 984     9127  10459   9522    127   2586  -2537       C  
ATOM   1771  CG  ARG A 984       7.804  63.787  58.097  1.00 82.92           C  
ANISOU 1771  CG  ARG A 984     9656  11194  10656    122   2431  -2288       C  
ATOM   1772  CD  ARG A 984       6.371  63.267  58.086  1.00 91.65           C  
ANISOU 1772  CD  ARG A 984    10412  12551  11862    153   2646  -2166       C  
ATOM   1773  NE  ARG A 984       6.259  61.891  58.582  1.00 91.50           N  
ANISOU 1773  NE  ARG A 984    10366  12776  11625   -117   2671  -1946       N  
ATOM   1774  CZ  ARG A 984       5.625  60.917  57.938  1.00102.93           C  
ANISOU 1774  CZ  ARG A 984    11582  14307  13221   -249   2588  -1680       C  
ATOM   1775  NH1 ARG A 984       5.020  61.160  56.781  1.00 97.96           N  
ANISOU 1775  NH1 ARG A 984    10716  13571  12934   -135   2485  -1606       N  
ATOM   1776  NH2 ARG A 984       5.585  59.693  58.447  1.00 81.91           N  
ANISOU 1776  NH2 ARG A 984     8940  11817  10366   -515   2572  -1472       N  
ATOM   1777  N   MET A 985       9.958  65.585  61.897  1.00 80.87           N  
ANISOU 1777  N   MET A 985    10450  10889   9388     71   2587  -3085       N  
ATOM   1778  CA  MET A 985       9.942  66.459  63.075  1.00 85.12           C  
ANISOU 1778  CA  MET A 985    11258  11439   9644    177   2750  -3442       C  
ATOM   1779  C   MET A 985      11.145  67.386  63.048  1.00 89.65           C  
ANISOU 1779  C   MET A 985    12152  11661  10249    149   2445  -3602       C  
ATOM   1780  O   MET A 985      11.026  68.565  63.390  1.00 90.71           O  
ANISOU 1780  O   MET A 985    12464  11600  10402    343   2490  -3930       O  
ATOM   1781  CB  MET A 985       9.911  65.640  64.365  1.00 89.51           C  
ANISOU 1781  CB  MET A 985    11958  12348   9702    -19   2917  -3420       C  
ATOM   1782  N   LEU A 986      12.266  66.864  62.563  1.00 84.91           N  
ANISOU 1782  N   LEU A 986    11607  10971   9683    -90   2122  -3363       N  
ATOM   1783  CA  LEU A 986      13.505  67.616  62.440  1.00 84.68           C  
ANISOU 1783  CA  LEU A 986    11807  10650   9717   -191   1790  -3415       C  
ATOM   1784  C   LEU A 986      13.382  68.650  61.335  1.00 88.97           C  
ANISOU 1784  C   LEU A 986    12250  10871  10683    -23   1689  -3448       C  
ATOM   1785  O   LEU A 986      13.954  69.729  61.418  1.00 89.29           O  
ANISOU 1785  O   LEU A 986    12518  10624  10785    -20   1505  -3618       O  
ATOM   1786  CB  LEU A 986      14.658  66.673  62.118  1.00 81.59           C  
ANISOU 1786  CB  LEU A 986    11383  10320   9298   -455   1522  -3109       C  
ATOM   1787  CG  LEU A 986      15.728  66.466  63.185  1.00 87.54           C  
ANISOU 1787  CG  LEU A 986    12432  11072   9757   -682   1286  -3142       C  
ATOM   1788  CD1 LEU A 986      15.092  66.322  64.554  1.00 91.12           C  
ANISOU 1788  CD1 LEU A 986    13136  11732   9755   -717   1466  -3332       C  
ATOM   1789  CD2 LEU A 986      16.570  65.245  62.856  1.00 86.76           C  
ANISOU 1789  CD2 LEU A 986    12212  11059   9694   -874   1055  -2823       C  
ATOM   1790  N   ASP A 987      12.653  68.303  60.284  1.00 85.05           N  
ANISOU 1790  N   ASP A 987    11431  10412  10473    100   1782  -3275       N  
ATOM   1791  CA  ASP A 987      12.443  69.227  59.169  1.00 84.84           C  
ANISOU 1791  CA  ASP A 987    11298  10099  10839    249   1672  -3255       C  
ATOM   1792  C   ASP A 987      11.632  70.459  59.594  1.00 94.31           C  
ANISOU 1792  C   ASP A 987    12592  11101  12142    539   1808  -3587       C  
ATOM   1793  O   ASP A 987      12.067  71.582  59.318  1.00 95.91           O  
ANISOU 1793  O   ASP A 987    12965  10944  12533    584   1600  -3692       O  
ATOM   1794  CB  ASP A 987      11.818  68.524  57.955  1.00 83.55           C  
ANISOU 1794  CB  ASP A 987    10790  10042  10914    280   1697  -2972       C  
ATOM   1795  CG  ASP A 987      11.629  69.429  56.749  1.00 91.53           C  
ANISOU 1795  CG  ASP A 987    11704  10775  12299    400   1547  -2900       C  
ATOM   1796  OD1 ASP A 987      12.522  70.271  56.484  1.00 89.05           O  
ANISOU 1796  OD1 ASP A 987    11567  10194  12073    321   1316  -2910       O  
ATOM   1797  OD2 ASP A 987      10.591  69.299  56.074  1.00102.79           O  
ANISOU 1797  OD2 ASP A 987    12874  12250  13932    548   1638  -2807       O  
ATOM   1798  N   LEU A 988      10.482  70.255  60.286  1.00 93.62           N  
ANISOU 1798  N   LEU A 988    12393  11244  11933    735   2152  -3753       N  
ATOM   1799  CA  LEU A 988       9.630  71.341  60.788  1.00 98.66           C  
ANISOU 1799  CA  LEU A 988    13091  11743  12653   1074   2340  -4118       C  
ATOM   1800  C   LEU A 988      10.398  72.272  61.746  1.00105.88           C  
ANISOU 1800  C   LEU A 988    14462  12413  13353   1066   2224  -4466       C  
ATOM   1801  O   LEU A 988      10.191  73.483  61.712  1.00108.24           O  
ANISOU 1801  O   LEU A 988    14904  12359  13865   1305   2157  -4731       O  
ATOM   1802  CB  LEU A 988       8.374  70.782  61.468  1.00101.32           C  
ANISOU 1802  CB  LEU A 988    13191  12479  12825   1241   2773  -4210       C  
ATOM   1803  N   GLU A 989      11.297  71.700  62.537  1.00102.60           N  
ANISOU 1803  N   GLU A 989    14289  12148  12545    776   2139  -4446       N  
ATOM   1804  CA  GLU A 989      12.097  72.462  63.482  1.00105.57           C  
ANISOU 1804  CA  GLU A 989    15122  12324  12667    686   1965  -4736       C  
ATOM   1805  C   GLU A 989      13.362  73.030  62.851  1.00109.04           C  
ANISOU 1805  C   GLU A 989    15718  12378  13332    462   1500  -4592       C  
ATOM   1806  O   GLU A 989      14.311  73.345  63.563  1.00110.30           O  
ANISOU 1806  O   GLU A 989    16222  12416  13270    271   1278  -4723       O  
ATOM   1807  CB  GLU A 989      12.484  71.577  64.667  1.00107.37           C  
ANISOU 1807  CB  GLU A 989    15522  12920  12354    462   2069  -4749       C  
ATOM   1808  N   GLU A 990      13.398  73.086  61.524  1.00103.80           N  
ANISOU 1808  N   GLU A 990    14799  11548  13091    463   1348  -4307       N  
ATOM   1809  CA  GLU A 990      14.536  73.641  60.801  1.00102.68           C  
ANISOU 1809  CA  GLU A 990    14731  11096  13187    238    948  -4107       C  
ATOM   1810  C   GLU A 990      15.856  72.946  61.126  1.00104.13           C  
ANISOU 1810  C   GLU A 990    14987  11438  13139   -140    731  -3904       C  
ATOM   1811  O   GLU A 990      16.907  73.582  61.146  1.00103.76           O  
ANISOU 1811  O   GLU A 990    15117  11147  13161   -353    402  -3868       O  
ATOM   1812  CB  GLU A 990      14.666  75.130  61.119  1.00108.49           C  
ANISOU 1812  CB  GLU A 990    15797  11333  14090    343    736  -4402       C  
ATOM   1813  CG  GLU A 990      14.063  76.053  60.078  1.00122.85           C  
ANISOU 1813  CG  GLU A 990    17494  12861  16322    662    770  -4455       C  
ATOM   1814  CD  GLU A 990      14.198  77.514  60.456  1.00153.41           C  
ANISOU 1814  CD  GLU A 990    21717  16176  20397    787    524  -4751       C  
ATOM   1815  OE1 GLU A 990      13.321  78.315  60.076  1.00157.20           O  
ANISOU 1815  OE1 GLU A 990    22108  16372  21250   1064    509  -4785       O  
ATOM   1816  OE2 GLU A 990      15.184  77.863  61.135  1.00150.49           O  
ANISOU 1816  OE2 GLU A 990    21721  15629  19829    608    314  -4947       O  
ATOM   1817  N   ARG A 991      15.819  71.645  61.381  1.00 98.19           N  
ANISOU 1817  N   ARG A 991    14083  11084  12140   -223    895  -3757       N  
ATOM   1818  CA  ARG A 991      17.038  70.910  61.713  1.00 96.05           C  
ANISOU 1818  CA  ARG A 991    13858  10985  11651   -524    706  -3580       C  
ATOM   1819  C   ARG A 991      17.277  69.677  60.847  1.00 95.00           C  
ANISOU 1819  C   ARG A 991    13387  11127  11581   -606    745  -3220       C  
ATOM   1820  O   ARG A 991      17.800  68.675  61.325  1.00 92.85           O  
ANISOU 1820  O   ARG A 991    13120  11087  11072   -752    719  -3114       O  
ATOM   1821  CB  ARG A 991      17.033  70.519  63.188  1.00 96.77           C  
ANISOU 1821  CB  ARG A 991    14229  11253  11286   -568    802  -3812       C  
ATOM   1822  CG  ARG A 991      17.518  71.613  64.119  1.00105.91           C  
ANISOU 1822  CG  ARG A 991    15805  12140  12297   -582    648  -4165       C  
ATOM   1823  CD  ARG A 991      16.905  71.460  65.500  1.00110.79           C  
ANISOU 1823  CD  ARG A 991    16680  12971  12442   -502    893  -4470       C  
ATOM   1824  NE  ARG A 991      17.369  70.257  66.182  1.00105.24           N  
ANISOU 1824  NE  ARG A 991    15989  12616  11382   -738    869  -4276       N  
ATOM   1825  CZ  ARG A 991      16.604  69.507  66.964  1.00115.97           C  
ANISOU 1825  CZ  ARG A 991    17363  14324  12375   -696   1174  -4320       C  
ATOM   1826  NH1 ARG A 991      15.338  69.835  67.163  1.00105.53           N  
ANISOU 1826  NH1 ARG A 991    16006  13098  10992   -414   1567  -4567       N  
ATOM   1827  NH2 ARG A 991      17.105  68.431  67.549  1.00 99.25           N  
ANISOU 1827  NH2 ARG A 991    15280  12470   9961   -941   1082  -4101       N  
ATOM   1828  N   VAL A 992      16.893  69.744  59.580  1.00 89.98           N  
ANISOU 1828  N   VAL A 992    12486  10442  11259   -514    775  -3038       N  
ATOM   1829  CA  VAL A 992      17.026  68.597  58.697  1.00 86.26           C  
ANISOU 1829  CA  VAL A 992    11727  10194  10855   -561    802  -2743       C  
ATOM   1830  C   VAL A 992      18.462  68.100  58.575  1.00 90.23           C  
ANISOU 1830  C   VAL A 992    12189  10758  11335   -795    553  -2542       C  
ATOM   1831  O   VAL A 992      18.699  66.896  58.574  1.00 88.64           O  
ANISOU 1831  O   VAL A 992    11868  10773  11036   -844    567  -2394       O  
ATOM   1832  CB  VAL A 992      16.468  68.895  57.296  1.00 88.13           C  
ANISOU 1832  CB  VAL A 992    11730  10362  11393   -414    870  -2618       C  
ATOM   1833  N   SER A 993      19.424  69.010  58.494  1.00 88.22           N  
ANISOU 1833  N   SER A 993    12037  10307  11175   -940    313  -2540       N  
ATOM   1834  CA  SER A 993      20.808  68.578  58.356  1.00 87.47           C  
ANISOU 1834  CA  SER A 993    11859  10286  11091  -1166     72  -2350       C  
ATOM   1835  C   SER A 993      21.239  67.552  59.407  1.00 90.29           C  
ANISOU 1835  C   SER A 993    12311  10819  11176  -1278    -12  -2363       C  
ATOM   1836  O   SER A 993      22.022  66.661  59.113  1.00 89.31           O  
ANISOU 1836  O   SER A 993    12033  10822  11079  -1402   -173  -2176       O  
ATOM   1837  CB  SER A 993      21.744  69.783  58.397  1.00 93.25           C  
ANISOU 1837  CB  SER A 993    12700  10761  11972  -1334   -179  -2352       C  
ATOM   1838  N   GLU A 994      20.763  67.696  60.635  1.00 86.72           N  
ANISOU 1838  N   GLU A 994    12104  10386  10461  -1228     97  -2577       N  
ATOM   1839  CA  GLU A 994      21.126  66.777  61.710  1.00 86.88           C  
ANISOU 1839  CA  GLU A 994    12265  10572  10172  -1346     19  -2580       C  
ATOM   1840  C   GLU A 994      20.733  65.303  61.516  1.00 87.98           C  
ANISOU 1840  C   GLU A 994    12219  10952  10257  -1285    150  -2400       C  
ATOM   1841  O   GLU A 994      21.177  64.445  62.269  1.00 88.26           O  
ANISOU 1841  O   GLU A 994    12320  11118  10097  -1401     24  -2312       O  
ATOM   1842  CB  GLU A 994      20.581  67.294  63.042  1.00 91.42           C  
ANISOU 1842  CB  GLU A 994    13196  11105  10433  -1325    112  -2883       C  
ATOM   1843  CG  GLU A 994      21.447  68.360  63.689  1.00103.07           C  
ANISOU 1843  CG  GLU A 994    14962  12377  11825  -1499   -179  -3040       C  
ATOM   1844  CD  GLU A 994      20.769  69.015  64.872  1.00126.16           C  
ANISOU 1844  CD  GLU A 994    18276  15244  14414  -1440    -68  -3402       C  
ATOM   1845  OE1 GLU A 994      20.613  70.251  64.860  1.00129.63           O  
ANISOU 1845  OE1 GLU A 994    18879  15412  14965  -1336    -59  -3648       O  
ATOM   1846  OE2 GLU A 994      20.388  68.293  65.813  1.00115.92           O  
ANISOU 1846  OE2 GLU A 994    17131  14176  12736  -1488     15  -3441       O  
ATOM   1847  N   CYS A 995      19.908  65.010  60.519  1.00 81.75           N  
ANISOU 1847  N   CYS A 995    11216  10195   9648  -1117    363  -2335       N  
ATOM   1848  CA  CYS A 995      19.471  63.638  60.253  1.00 78.98           C  
ANISOU 1848  CA  CYS A 995    10706  10023   9279  -1070    458  -2170       C  
ATOM   1849  C   CYS A 995      20.543  62.847  59.516  1.00 76.09           C  
ANISOU 1849  C   CYS A 995    10143   9700   9069  -1112    261  -1958       C  
ATOM   1850  O   CYS A 995      20.601  61.624  59.674  1.00 74.18           O  
ANISOU 1850  O   CYS A 995     9855   9565   8766  -1121    217  -1831       O  
ATOM   1851  CB  CYS A 995      18.126  63.599  59.524  1.00 78.64           C  
ANISOU 1851  CB  CYS A 995    10521   9998   9363   -897    719  -2184       C  
ATOM   1852  SG  CYS A 995      18.236  63.710  57.715  1.00 80.11           S  
ANISOU 1852  SG  CYS A 995    10432  10108   9900   -799    691  -2042       S  
ATOM   1853  N   TYR A 996      21.406  63.553  58.739  1.00 69.00           N  
ANISOU 1853  N   TYR A 996     9128   8718   8373  -1140    139  -1919       N  
ATOM   1854  CA  TYR A 996      22.464  62.948  57.933  1.00 66.39           C  
ANISOU 1854  CA  TYR A 996     8559   8466   8201  -1149      0  -1742       C  
ATOM   1855  C   TYR A 996      23.409  62.101  58.708  1.00 67.05           C  
ANISOU 1855  C   TYR A 996     8651   8634   8192  -1236   -215  -1655       C  
ATOM   1856  O   TYR A 996      23.822  62.473  59.795  1.00 68.97           O  
ANISOU 1856  O   TYR A 996     9081   8844   8279  -1381   -367  -1708       O  
ATOM   1857  CB  TYR A 996      23.257  63.969  57.099  1.00 67.97           C  
ANISOU 1857  CB  TYR A 996     8624   8606   8595  -1215    -79  -1691       C  
ATOM   1858  CG  TYR A 996      22.441  64.702  56.064  1.00 70.58           C  
ANISOU 1858  CG  TYR A 996     8907   8850   9062  -1125     88  -1710       C  
ATOM   1859  CD1 TYR A 996      21.582  64.017  55.209  1.00 71.68           C  
ANISOU 1859  CD1 TYR A 996     8932   9058   9244   -966    258  -1671       C  
ATOM   1860  CD2 TYR A 996      22.547  66.078  55.918  1.00 73.38           C  
ANISOU 1860  CD2 TYR A 996     9339   9029   9513  -1213     30  -1748       C  
ATOM   1861  CE1 TYR A 996      20.852  64.689  54.231  1.00 73.95           C  
ANISOU 1861  CE1 TYR A 996     9172   9269   9659   -894    367  -1660       C  
ATOM   1862  CE2 TYR A 996      21.815  66.762  54.954  1.00 74.48           C  
ANISOU 1862  CE2 TYR A 996     9439   9064   9796  -1133    138  -1731       C  
ATOM   1863  CZ  TYR A 996      20.969  66.066  54.111  1.00 83.53           C  
ANISOU 1863  CZ  TYR A 996    10458  10308  10973   -972    307  -1681       C  
ATOM   1864  OH  TYR A 996      20.244  66.763  53.178  1.00 88.62           O  
ANISOU 1864  OH  TYR A 996    11070  10846  11757   -905    372  -1645       O  
ATOM   1865  N   ASP A 997      23.755  60.954  58.128  1.00 60.30           N  
ANISOU 1865  N   ASP A 997     7605   7871   7436  -1137   -251  -1529       N  
ATOM   1866  CA  ASP A 997      24.691  59.995  58.675  1.00 60.21           C  
ANISOU 1866  CA  ASP A 997     7548   7920   7410  -1165   -484  -1419       C  
ATOM   1867  C   ASP A 997      26.022  60.726  58.951  1.00 68.00           C  
ANISOU 1867  C   ASP A 997     8450   8922   8466  -1310   -711  -1376       C  
ATOM   1868  O   ASP A 997      26.475  61.514  58.109  1.00 66.51           O  
ANISOU 1868  O   ASP A 997     8082   8747   8440  -1327   -672  -1359       O  
ATOM   1869  CB  ASP A 997      24.892  58.859  57.644  1.00 59.00           C  
ANISOU 1869  CB  ASP A 997     7162   7826   7431   -972   -465  -1334       C  
ATOM   1870  CG  ASP A 997      25.671  57.668  58.153  1.00 58.90           C  
ANISOU 1870  CG  ASP A 997     7105   7829   7445   -933   -709  -1226       C  
ATOM   1871  OD1 ASP A 997      26.422  57.819  59.145  1.00 59.96           O  
ANISOU 1871  OD1 ASP A 997     7304   7968   7510  -1073   -938  -1173       O  
ATOM   1872  OD2 ASP A 997      25.526  56.586  57.577  1.00 63.24           O  
ANISOU 1872  OD2 ASP A 997     7574   8365   8090   -763   -703  -1197       O  
ATOM   1873  N   ARG A 998      26.643  60.465  60.128  1.00 68.48           N  
ANISOU 1873  N   ARG A 998     8636   8985   8398  -1444   -970  -1331       N  
ATOM   1874  CA  ARG A 998      27.918  61.096  60.498  1.00 71.01           C  
ANISOU 1874  CA  ARG A 998     8872   9319   8789  -1617  -1244  -1269       C  
ATOM   1875  C   ARG A 998      29.081  60.584  59.611  1.00 76.59           C  
ANISOU 1875  C   ARG A 998     9153  10158   9788  -1515  -1338  -1114       C  
ATOM   1876  O   ARG A 998      30.089  61.269  59.476  1.00 77.80           O  
ANISOU 1876  O   ARG A 998     9116  10364  10080  -1647  -1486  -1039       O  
ATOM   1877  CB  ARG A 998      28.219  60.946  62.005  1.00 71.96           C  
ANISOU 1877  CB  ARG A 998     9264   9413   8665  -1800  -1525  -1258       C  
ATOM   1878  N   HIS A 999      28.905  59.432  58.950  1.00 73.42           N  
ANISOU 1878  N   HIS A 999     8598   9815   9484  -1277  -1236  -1077       N  
ATOM   1879  CA  HIS A 999      29.907  58.866  58.045  1.00 75.07           C  
ANISOU 1879  CA  HIS A 999     8404  10168   9952  -1108  -1265   -983       C  
ATOM   1880  C   HIS A 999      29.931  59.513  56.631  1.00 81.18           C  
ANISOU 1880  C   HIS A 999     8936  11054  10853  -1044   -999  -1002       C  
ATOM   1881  O   HIS A 999      30.659  59.027  55.765  1.00 84.68           O  
ANISOU 1881  O   HIS A 999     9043  11663  11468   -876   -949   -953       O  
ATOM   1882  CB  HIS A 999      29.753  57.343  57.958  1.00 75.50           C  
ANISOU 1882  CB  HIS A 999     8436  10197  10053   -863  -1303   -967       C  
ATOM   1883  CG  HIS A 999      30.090  56.651  59.238  1.00 81.00           C  
ANISOU 1883  CG  HIS A 999     9285  10815  10678   -936  -1633   -870       C  
ATOM   1884  ND1 HIS A 999      31.372  56.190  59.495  1.00 85.70           N  
ANISOU 1884  ND1 HIS A 999     9624  11476  11463   -886  -1926   -745       N  
ATOM   1885  CD2 HIS A 999      29.311  56.400  60.315  1.00 83.05           C  
ANISOU 1885  CD2 HIS A 999     9915  10958  10683  -1071  -1713   -864       C  
ATOM   1886  CE1 HIS A 999      31.331  55.666  60.709  1.00 86.72           C  
ANISOU 1886  CE1 HIS A 999    10002  11498  11451   -997  -2209   -656       C  
ATOM   1887  NE2 HIS A 999      30.112  55.771  61.245  1.00 85.64           N  
ANISOU 1887  NE2 HIS A 999    10255  11264  11021  -1123  -2080   -720       N  
ATOM   1888  N   ILE A1000      29.171  60.605  56.394  1.00 75.26           N  
ANISOU 1888  N   ILE A1000     8353  10223  10017  -1169   -837  -1069       N  
ATOM   1889  CA  ILE A1000      29.152  61.302  55.096  1.00 81.18           C  
ANISOU 1889  CA  ILE A1000     8918  11063  10863  -1156   -624  -1045       C  
ATOM   1890  C   ILE A1000      29.325  62.815  55.273  1.00128.75           C  
ANISOU 1890  C   ILE A1000    15018  17002  16901  -1429   -690  -1011       C  
ATOM   1891  O   ILE A1000      30.443  63.322  55.161  1.00104.17           O  
ANISOU 1891  O   ILE A1000    11666  13998  13917  -1588   -823   -876       O  
ATOM   1892  CB  ILE A1000      27.935  60.938  54.186  1.00 81.18           C  
ANISOU 1892  CB  ILE A1000     9011  11031  10804   -969   -355  -1136       C  
ATOM   1893  CG1 ILE A1000      26.573  61.115  54.905  1.00 79.89           C  
ANISOU 1893  CG1 ILE A1000     9208  10664  10482  -1000   -303  -1253       C  
ATOM   1894  CG2 ILE A1000      28.093  59.532  53.621  1.00 82.02           C  
ANISOU 1894  CG2 ILE A1000     8963  11242  10958   -704   -310  -1153       C  
ATOM   1895  CD1 ILE A1000      25.309  60.834  54.103  1.00 78.93           C  
ANISOU 1895  CD1 ILE A1000     9160  10503  10326   -853    -80  -1318       C  
ATOM   1896  N   ALA A1009      28.097  69.147  53.296  1.00 82.61           N  
ANISOU 1896  N   ALA A1009     9643  10387  11359  -2227   -698   -833       N  
ATOM   1897  CA  ALA A1009      27.279  67.997  52.886  1.00 79.51           C  
ANISOU 1897  CA  ALA A1009     9207  10144  10859  -1918   -439   -924       C  
ATOM   1898  C   ALA A1009      26.870  68.123  51.393  1.00 81.21           C  
ANISOU 1898  C   ALA A1009     9278  10461  11117  -1852   -247   -787       C  
ATOM   1899  O   ALA A1009      26.230  69.127  51.044  1.00 81.83           O  
ANISOU 1899  O   ALA A1009     9516  10314  11261  -1913   -266   -765       O  
ATOM   1900  CB  ALA A1009      26.048  67.868  53.779  1.00 78.78           C  
ANISOU 1900  CB  ALA A1009     9448   9837  10647  -1756   -386  -1180       C  
ATOM   1901  N   PRO A1010      27.254  67.145  50.502  1.00 73.86           N  
ANISOU 1901  N   PRO A1010     8065   9856  10143  -1725    -83   -698       N  
ATOM   1902  CA  PRO A1010      26.963  67.297  49.063  1.00 71.47           C  
ANISOU 1902  CA  PRO A1010     7648   9686   9823  -1697     84   -561       C  
ATOM   1903  C   PRO A1010      25.524  67.633  48.802  1.00 71.37           C  
ANISOU 1903  C   PRO A1010     7886   9436   9794  -1583    145   -650       C  
ATOM   1904  O   PRO A1010      24.663  67.069  49.461  1.00 69.42           O  
ANISOU 1904  O   PRO A1010     7803   9073   9500  -1404    181   -847       O  
ATOM   1905  CB  PRO A1010      27.358  65.951  48.450  1.00 72.03           C  
ANISOU 1905  CB  PRO A1010     7474  10095   9800  -1487    256   -581       C  
ATOM   1906  CG  PRO A1010      28.269  65.360  49.383  1.00 78.13           C  
ANISOU 1906  CG  PRO A1010     8125  10947  10614  -1479    144   -626       C  
ATOM   1907  CD  PRO A1010      28.049  65.923  50.752  1.00 74.60           C  
ANISOU 1907  CD  PRO A1010     7939  10203  10204  -1604    -67   -720       C  
ATOM   1908  N   GLN A1011      25.278  68.574  47.863  1.00 68.56           N  
ANISOU 1908  N   GLN A1011     7546   9016   9488  -1705    139   -478       N  
ATOM   1909  CA  GLN A1011      23.946  69.054  47.461  1.00 67.62           C  
ANISOU 1909  CA  GLN A1011     7627   8664   9403  -1608    157   -511       C  
ATOM   1910  C   GLN A1011      23.009  67.935  47.046  1.00 68.11           C  
ANISOU 1910  C   GLN A1011     7687   8840   9351  -1343    323   -632       C  
ATOM   1911  O   GLN A1011      21.800  68.102  47.149  1.00 66.60           O  
ANISOU 1911  O   GLN A1011     7651   8446   9208  -1218    328   -726       O  
ATOM   1912  CB  GLN A1011      24.068  70.095  46.342  1.00 71.33           C  
ANISOU 1912  CB  GLN A1011     8067   9107   9928  -1808     96   -234       C  
ATOM   1913  CG  GLN A1011      24.375  71.499  46.864  1.00 98.81           C  
ANISOU 1913  CG  GLN A1011    11693  12256  13594  -2052   -145   -149       C  
ATOM   1914  CD  GLN A1011      23.175  72.231  47.446  1.00124.60           C  
ANISOU 1914  CD  GLN A1011    15259  15082  17001  -1922   -250   -326       C  
ATOM   1915  OE1 GLN A1011      22.007  71.933  47.145  1.00121.49           O  
ANISOU 1915  OE1 GLN A1011    14926  14635  16598  -1690   -150   -420       O  
ATOM   1916  NE2 GLN A1011      23.445  73.240  48.268  1.00114.90           N  
ANISOU 1916  NE2 GLN A1011    14215  13526  15917  -2067   -466   -380       N  
ATOM   1917  N   ALA A1012      23.572  66.790  46.609  1.00 65.24           N  
ANISOU 1917  N   ALA A1012     7142   8790   8858  -1252    444   -638       N  
ATOM   1918  CA  ALA A1012      22.847  65.590  46.193  1.00 64.94           C  
ANISOU 1918  CA  ALA A1012     7110   8857   8709  -1022    563   -757       C  
ATOM   1919  C   ALA A1012      22.070  64.990  47.342  1.00 68.34           C  
ANISOU 1919  C   ALA A1012     7686   9117   9165   -885    545   -961       C  
ATOM   1920  O   ALA A1012      20.985  64.483  47.125  1.00 67.74           O  
ANISOU 1920  O   ALA A1012     7685   8989   9066   -751    592  -1031       O  
ATOM   1921  CB  ALA A1012      23.816  64.561  45.634  1.00 66.46           C  
ANISOU 1921  CB  ALA A1012     7093   9379   8780   -944    666   -755       C  
ATOM   1922  N   LEU A1013      22.624  65.051  48.560  1.00 65.50           N  
ANISOU 1922  N   LEU A1013     7361   8688   8838   -943    466  -1034       N  
ATOM   1923  CA  LEU A1013      22.002  64.563  49.782  1.00 64.39           C  
ANISOU 1923  CA  LEU A1013     7372   8419   8675   -860    451  -1203       C  
ATOM   1924  C   LEU A1013      20.730  65.387  50.087  1.00 67.38           C  
ANISOU 1924  C   LEU A1013     7925   8561   9116   -831    472  -1277       C  
ATOM   1925  O   LEU A1013      19.729  64.824  50.545  1.00 66.15           O  
ANISOU 1925  O   LEU A1013     7842   8367   8925   -711    544  -1384       O  
ATOM   1926  CB  LEU A1013      23.011  64.722  50.938  1.00 65.73           C  
ANISOU 1926  CB  LEU A1013     7560   8573   8841   -982    323  -1232       C  
ATOM   1927  CG  LEU A1013      23.905  63.532  51.352  1.00 70.46           C  
ANISOU 1927  CG  LEU A1013     8040   9344   9387   -932    274  -1240       C  
ATOM   1928  CD1 LEU A1013      24.391  62.674  50.145  1.00 69.96           C  
ANISOU 1928  CD1 LEU A1013     7750   9513   9317   -807    363  -1173       C  
ATOM   1929  CD2 LEU A1013      25.069  64.027  52.179  1.00 72.47           C  
ANISOU 1929  CD2 LEU A1013     8260   9599   9676  -1108    100  -1198       C  
ATOM   1930  N   ASP A1014      20.789  66.724  49.846  1.00 62.64           N  
ANISOU 1930  N   ASP A1014     7376   7798   8624   -940    399  -1210       N  
ATOM   1931  CA  ASP A1014      19.670  67.634  50.063  1.00 61.82           C  
ANISOU 1931  CA  ASP A1014     7422   7439   8629   -875    398  -1290       C  
ATOM   1932  C   ASP A1014      18.602  67.363  49.020  1.00 62.79           C  
ANISOU 1932  C   ASP A1014     7475   7592   8791   -745    475  -1222       C  
ATOM   1933  O   ASP A1014      17.418  67.393  49.351  1.00 63.29           O  
ANISOU 1933  O   ASP A1014     7587   7548   8911   -604    537  -1328       O  
ATOM   1934  CB  ASP A1014      20.120  69.101  50.027  1.00 66.14           C  
ANISOU 1934  CB  ASP A1014     8063   7755   9313  -1031    242  -1222       C  
ATOM   1935  CG  ASP A1014      19.188  70.049  50.772  1.00 85.58           C  
ANISOU 1935  CG  ASP A1014    10732   9897  11888   -930    213  -1405       C  
ATOM   1936  OD1 ASP A1014      18.001  70.155  50.377  1.00 84.64           O  
ANISOU 1936  OD1 ASP A1014    10603   9697  11860   -756    287  -1431       O  
ATOM   1937  OD2 ASP A1014      19.656  70.722  51.728  1.00 96.44           O  
ANISOU 1937  OD2 ASP A1014    12277  11097  13271  -1019    101  -1529       O  
ATOM   1938  N   GLY A1015      19.033  67.060  47.792  1.00 56.20           N  
ANISOU 1938  N   GLY A1015     6514   6931   7907   -795    475  -1050       N  
ATOM   1939  CA  GLY A1015      18.160  66.721  46.683  1.00 54.45           C  
ANISOU 1939  CA  GLY A1015     6243   6769   7677   -707    507   -968       C  
ATOM   1940  C   GLY A1015      17.432  65.438  46.994  1.00 58.94           C  
ANISOU 1940  C   GLY A1015     6793   7428   8175   -561    593  -1095       C  
ATOM   1941  O   GLY A1015      16.207  65.362  46.863  1.00 59.53           O  
ANISOU 1941  O   GLY A1015     6870   7426   8321   -462    606  -1115       O  
ATOM   1942  N   MET A1016      18.185  64.447  47.482  1.00 54.94           N  
ANISOU 1942  N   MET A1016     6257   7066   7553   -558    627  -1167       N  
ATOM   1943  CA  MET A1016      17.670  63.141  47.897  1.00 53.07           C  
ANISOU 1943  CA  MET A1016     6026   6887   7251   -458    668  -1264       C  
ATOM   1944  C   MET A1016      16.659  63.292  49.018  1.00 54.11           C  
ANISOU 1944  C   MET A1016     6230   6890   7441   -417    714  -1365       C  
ATOM   1945  O   MET A1016      15.635  62.599  49.024  1.00 51.96           O  
ANISOU 1945  O   MET A1016     5936   6629   7176   -353    750  -1380       O  
ATOM   1946  CB  MET A1016      18.827  62.240  48.358  1.00 54.61           C  
ANISOU 1946  CB  MET A1016     6191   7209   7350   -465    650  -1307       C  
ATOM   1947  CG  MET A1016      19.518  61.522  47.217  1.00 57.66           C  
ANISOU 1947  CG  MET A1016     6478   7775   7653   -415    655  -1267       C  
ATOM   1948  SD  MET A1016      20.931  60.529  47.808  1.00 60.99           S  
ANISOU 1948  SD  MET A1016     6819   8326   8031   -369    617  -1325       S  
ATOM   1949  CE  MET A1016      20.046  59.061  48.438  1.00 55.25           C  
ANISOU 1949  CE  MET A1016     6213   7492   7286   -263    561  -1424       C  
ATOM   1950  N   LEU A1017      16.950  64.202  49.974  1.00 51.88           N  
ANISOU 1950  N   LEU A1017     6031   6495   7186   -465    714  -1437       N  
ATOM   1951  CA  LEU A1017      16.067  64.468  51.116  1.00 52.13           C  
ANISOU 1951  CA  LEU A1017     6144   6434   7227   -410    797  -1571       C  
ATOM   1952  C   LEU A1017      14.715  65.067  50.665  1.00 55.34           C  
ANISOU 1952  C   LEU A1017     6494   6740   7793   -293    853  -1568       C  
ATOM   1953  O   LEU A1017      13.657  64.545  51.052  1.00 53.67           O  
ANISOU 1953  O   LEU A1017     6225   6581   7584   -217    957  -1610       O  
ATOM   1954  CB  LEU A1017      16.769  65.327  52.174  1.00 53.78           C  
ANISOU 1954  CB  LEU A1017     6498   6537   7399   -483    759  -1682       C  
ATOM   1955  CG  LEU A1017      16.009  65.570  53.513  1.00 61.64           C  
ANISOU 1955  CG  LEU A1017     7619   7479   8323   -422    872  -1871       C  
ATOM   1956  CD1 LEU A1017      15.682  64.248  54.265  1.00 60.54           C  
ANISOU 1956  CD1 LEU A1017     7472   7523   8008   -432    960  -1879       C  
ATOM   1957  CD2 LEU A1017      16.834  66.439  54.422  1.00 67.69           C  
ANISOU 1957  CD2 LEU A1017     8573   8120   9026   -512    783  -1994       C  
ATOM   1958  N   ARG A1018      14.748  66.103  49.787  1.00 51.80           N  
ANISOU 1958  N   ARG A1018     6037   6159   7486   -292    767  -1484       N  
ATOM   1959  CA  ARG A1018      13.526  66.723  49.275  1.00 52.60           C  
ANISOU 1959  CA  ARG A1018     6069   6139   7777   -167    767  -1454       C  
ATOM   1960  C   ARG A1018      12.665  65.670  48.534  1.00 55.41           C  
ANISOU 1960  C   ARG A1018     6280   6644   8127   -128    781  -1357       C  
ATOM   1961  O   ARG A1018      11.433  65.656  48.691  1.00 53.96           O  
ANISOU 1961  O   ARG A1018     5990   6445   8067    -14    841  -1380       O  
ATOM   1962  CB  ARG A1018      13.861  67.935  48.391  1.00 56.44           C  
ANISOU 1962  CB  ARG A1018     6597   6445   8404   -213    614  -1327       C  
ATOM   1963  CG  ARG A1018      14.603  69.053  49.135  1.00 69.10           C  
ANISOU 1963  CG  ARG A1018     8362   7840  10055   -273    551  -1421       C  
ATOM   1964  CD  ARG A1018      14.577  70.355  48.343  1.00 90.88           C  
ANISOU 1964  CD  ARG A1018    11171  10343  13018   -302    374  -1282       C  
ATOM   1965  NE  ARG A1018      15.692  71.259  48.670  1.00109.36           N  
ANISOU 1965  NE  ARG A1018    13662  12516  15374   -473    240  -1272       N  
ATOM   1966  CZ  ARG A1018      15.688  72.152  49.660  1.00124.13           C  
ANISOU 1966  CZ  ARG A1018    15710  14116  17338   -428    190  -1469       C  
ATOM   1967  NH1 ARG A1018      14.642  72.251  50.471  1.00114.68           N  
ANISOU 1967  NH1 ARG A1018    14547  12823  16202   -186    314  -1715       N  
ATOM   1968  NH2 ARG A1018      16.741  72.931  49.862  1.00108.90           N  
ANISOU 1968  NH2 ARG A1018    13920  12027  15430   -630     18  -1429       N  
ATOM   1969  N   ILE A1019      13.332  64.740  47.797  1.00 50.78           N  
ANISOU 1969  N   ILE A1019     5686   6210   7397   -218    725  -1265       N  
ATOM   1970  CA  ILE A1019      12.646  63.650  47.109  1.00 50.09           C  
ANISOU 1970  CA  ILE A1019     5518   6236   7278   -204    693  -1199       C  
ATOM   1971  C   ILE A1019      12.020  62.697  48.142  1.00 54.18           C  
ANISOU 1971  C   ILE A1019     6001   6818   7765   -187    790  -1283       C  
ATOM   1972  O   ILE A1019      10.848  62.360  47.992  1.00 53.50           O  
ANISOU 1972  O   ILE A1019     5802   6752   7776   -153    791  -1238       O  
ATOM   1973  CB  ILE A1019      13.569  62.927  46.104  1.00 51.87           C  
ANISOU 1973  CB  ILE A1019     5779   6590   7338   -270    618  -1135       C  
ATOM   1974  CG1 ILE A1019      13.910  63.847  44.908  1.00 54.50           C  
ANISOU 1974  CG1 ILE A1019     6122   6911   7676   -317    534   -995       C  
ATOM   1975  CG2 ILE A1019      12.945  61.628  45.605  1.00 50.06           C  
ANISOU 1975  CG2 ILE A1019     5528   6442   7051   -258    561  -1125       C  
ATOM   1976  CD1 ILE A1019      15.229  63.498  44.251  1.00 65.75           C  
ANISOU 1976  CD1 ILE A1019     7570   8504   8908   -387    539   -964       C  
ATOM   1977  N   ALA A1020      12.801  62.280  49.186  1.00 50.14           N  
ANISOU 1977  N   ALA A1020     5578   6350   7121   -233    850  -1374       N  
ATOM   1978  CA  ALA A1020      12.349  61.353  50.234  1.00 48.75           C  
ANISOU 1978  CA  ALA A1020     5402   6249   6870   -263    927  -1414       C  
ATOM   1979  C   ALA A1020      11.131  61.881  50.934  1.00 54.93           C  
ANISOU 1979  C   ALA A1020     6092   7032   7748   -198   1074  -1460       C  
ATOM   1980  O   ALA A1020      10.169  61.119  51.134  1.00 53.18           O  
ANISOU 1980  O   ALA A1020     5759   6900   7545   -224   1121  -1401       O  
ATOM   1981  CB  ALA A1020      13.441  61.092  51.241  1.00 48.39           C  
ANISOU 1981  CB  ALA A1020     5486   6231   6668   -327    934  -1485       C  
ATOM   1982  N   LEU A1021      11.140  63.212  51.242  1.00 53.47           N  
ANISOU 1982  N   LEU A1021     5939   6737   7642   -108   1139  -1562       N  
ATOM   1983  CA  LEU A1021      10.031  63.884  51.929  1.00 55.17           C  
ANISOU 1983  CA  LEU A1021     6060   6941   7960     21   1307  -1661       C  
ATOM   1984  C   LEU A1021       8.768  63.922  51.087  1.00 59.31           C  
ANISOU 1984  C   LEU A1021     6353   7471   8710    111   1288  -1551       C  
ATOM   1985  O   LEU A1021       7.680  63.783  51.627  1.00 61.37           O  
ANISOU 1985  O   LEU A1021     6442   7840   9036    178   1442  -1572       O  
ATOM   1986  CB  LEU A1021      10.434  65.269  52.444  1.00 56.57           C  
ANISOU 1986  CB  LEU A1021     6375   6945   8175    115   1338  -1832       C  
ATOM   1987  CG  LEU A1021      11.497  65.275  53.587  1.00 60.73           C  
ANISOU 1987  CG  LEU A1021     7127   7483   8464     16   1362  -1967       C  
ATOM   1988  CD1 LEU A1021      11.668  66.683  54.168  1.00 63.58           C  
ANISOU 1988  CD1 LEU A1021     7643   7639   8874    116   1379  -2171       C  
ATOM   1989  CD2 LEU A1021      11.106  64.339  54.752  1.00 59.86           C  
ANISOU 1989  CD2 LEU A1021     7021   7588   8136    -39   1531  -2012       C  
ATOM   1990  N   ARG A1022       8.916  64.037  49.760  1.00 53.96           N  
ANISOU 1990  N   ARG A1022     5657   6712   8133     94   1095  -1416       N  
ATOM   1991  CA  ARG A1022       7.806  64.011  48.812  1.00 53.36           C  
ANISOU 1991  CA  ARG A1022     5381   6635   8259    147   1001  -1277       C  
ATOM   1992  C   ARG A1022       7.198  62.609  48.739  1.00 52.58           C  
ANISOU 1992  C   ARG A1022     5169   6704   8106     30    981  -1174       C  
ATOM   1993  O   ARG A1022       5.995  62.476  48.602  1.00 50.42           O  
ANISOU 1993  O   ARG A1022     4666   6489   8002     65    987  -1092       O  
ATOM   1994  CB  ARG A1022       8.266  64.469  47.428  1.00 51.71           C  
ANISOU 1994  CB  ARG A1022     5242   6312   8092    118    780  -1148       C  
ATOM   1995  CG  ARG A1022       8.047  65.962  47.199  1.00 62.72           C  
ANISOU 1995  CG  ARG A1022     6629   7498   9704    254    728  -1151       C  
ATOM   1996  CD  ARG A1022       8.850  66.510  46.018  1.00 66.55           C  
ANISOU 1996  CD  ARG A1022     7248   7882  10157    164    525  -1005       C  
ATOM   1997  NE  ARG A1022       8.417  65.935  44.737  1.00 73.17           N  
ANISOU 1997  NE  ARG A1022     8022   8805  10976     93    351   -817       N  
ATOM   1998  CZ  ARG A1022       9.242  65.561  43.758  1.00 86.51           C  
ANISOU 1998  CZ  ARG A1022     9836  10579  12456    -47    243   -715       C  
ATOM   1999  NH1 ARG A1022      10.557  65.724  43.885  1.00 74.58           N  
ANISOU 1999  NH1 ARG A1022     8468   9092  10776   -133    297   -754       N  
ATOM   2000  NH2 ARG A1022       8.761  65.024  42.647  1.00 63.19           N  
ANISOU 2000  NH2 ARG A1022     6855   7703   9451   -104     80   -578       N  
ATOM   2001  N   CYS A1023       8.029  61.575  48.858  1.00 49.18           N  
ANISOU 2001  N   CYS A1023     4890   6334   7464   -108    939  -1172       N  
ATOM   2002  CA  CYS A1023       7.602  60.180  48.785  1.00 49.32           C  
ANISOU 2002  CA  CYS A1023     4863   6447   7430   -241    865  -1075       C  
ATOM   2003  C   CYS A1023       6.744  59.722  49.961  1.00 53.34           C  
ANISOU 2003  C   CYS A1023     5230   7093   7944   -292   1039  -1060       C  
ATOM   2004  O   CYS A1023       5.930  58.812  49.803  1.00 54.02           O  
ANISOU 2004  O   CYS A1023     5188   7251   8088   -410    966   -925       O  
ATOM   2005  CB  CYS A1023       8.815  59.273  48.613  1.00 48.85           C  
ANISOU 2005  CB  CYS A1023     5021   6372   7170   -330    755  -1101       C  
ATOM   2006  SG  CYS A1023       9.614  59.388  46.996  1.00 52.10           S  
ANISOU 2006  SG  CYS A1023     5547   6718   7529   -305    560  -1081       S  
ATOM   2007  N   ILE A1024       6.944  60.332  51.148  1.00 54.22           N  
ANISOU 2007  N   ILE A1024     5572   7272   7757    -45   1149  -1525       N  
ATOM   2008  CA  ILE A1024       6.270  59.956  52.389  1.00 53.72           C  
ANISOU 2008  CA  ILE A1024     5525   7307   7578   -131   1370  -1637       C  
ATOM   2009  C   ILE A1024       5.087  60.851  52.720  1.00 59.52           C  
ANISOU 2009  C   ILE A1024     6074   7982   8559   -192   1451  -1923       C  
ATOM   2010  O   ILE A1024       4.514  60.753  53.818  1.00 60.16           O  
ANISOU 2010  O   ILE A1024     6146   8162   8552   -280   1652  -2067       O  
ATOM   2011  CB  ILE A1024       7.251  59.814  53.580  1.00 56.14           C  
ANISOU 2011  CB  ILE A1024     5962   7830   7541   -139   1420  -1582       C  
ATOM   2012  CG1 ILE A1024       7.915  61.177  53.949  1.00 55.42           C  
ANISOU 2012  CG1 ILE A1024     5774   7812   7472   -114   1310  -1750       C  
ATOM   2013  CG2 ILE A1024       8.273  58.684  53.306  1.00 53.36           C  
ANISOU 2013  CG2 ILE A1024     5785   7507   6981    -87   1361  -1294       C  
ATOM   2014  CD1 ILE A1024       8.498  61.244  55.298  1.00 54.25           C  
ANISOU 2014  CD1 ILE A1024     5690   7908   7015   -134   1380  -1818       C  
ATOM   2015  N   ARG A1025       4.667  61.673  51.765  1.00 57.42           N  
ANISOU 2015  N   ARG A1025     5657   7551   8608   -150   1303  -2003       N  
ATOM   2016  CA  ARG A1025       3.473  62.515  51.954  1.00 59.13           C  
ANISOU 2016  CA  ARG A1025     5666   7665   9137   -201   1353  -2284       C  
ATOM   2017  C   ARG A1025       2.236  61.616  51.723  1.00 65.71           C  
ANISOU 2017  C   ARG A1025     6471   8400  10096   -242   1483  -2340       C  
ATOM   2018  O   ARG A1025       2.393  60.420  51.429  1.00 67.27           O  
ANISOU 2018  O   ARG A1025     6801   8613  10144   -227   1530  -2157       O  
ATOM   2019  CB  ARG A1025       3.489  63.696  50.970  1.00 58.72           C  
ANISOU 2019  CB  ARG A1025     5460   7451   9401   -125   1127  -2308       C  
ATOM   2020  CG  ARG A1025       4.482  64.795  51.337  1.00 62.26           C  
ANISOU 2020  CG  ARG A1025     5860   7950   9848   -103   1046  -2343       C  
ATOM   2021  CD  ARG A1025       4.567  65.857  50.251  1.00 78.71           C  
ANISOU 2021  CD  ARG A1025     7809   9843  12253    -19    835  -2289       C  
ATOM   2022  NE  ARG A1025       5.692  66.766  50.489  1.00 98.31           N  
ANISOU 2022  NE  ARG A1025    10256  12353  14744     11    771  -2283       N  
ATOM   2023  CZ  ARG A1025       6.006  67.820  49.735  1.00105.77           C  
ANISOU 2023  CZ  ARG A1025    11083  13136  15969     79    621  -2221       C  
ATOM   2024  NH1 ARG A1025       5.268  68.133  48.676  1.00 76.34           N  
ANISOU 2024  NH1 ARG A1025     7272   9225  12508    131    493  -2136       N  
ATOM   2025  NH2 ARG A1025       7.058  68.570  50.040  1.00 93.25           N  
ANISOU 2025  NH2 ARG A1025     9453  11569  14410    100    598  -2243       N  
ATOM   2026  N   SER A1026       1.030  62.162  51.844  1.00 62.61           N  
ANISOU 2026  N   SER A1026     5887   7890  10013   -294   1542  -2609       N  
ATOM   2027  CA  SER A1026      -0.200  61.391  51.641  1.00 63.70           C  
ANISOU 2027  CA  SER A1026     5962   7910  10330   -332   1672  -2718       C  
ATOM   2028  C   SER A1026      -0.294  60.938  50.195  1.00 66.29           C  
ANISOU 2028  C   SER A1026     6285   8119  10784   -221   1474  -2574       C  
ATOM   2029  O   SER A1026       0.285  61.596  49.318  1.00 64.00           O  
ANISOU 2029  O   SER A1026     5984   7800  10534   -124   1226  -2453       O  
ATOM   2030  CB  SER A1026      -1.431  62.209  52.027  1.00 67.63           C  
ANISOU 2030  CB  SER A1026     6225   8289  11184   -407   1750  -3075       C  
ATOM   2031  OG  SER A1026      -1.968  62.875  50.898  1.00 76.43           O  
ANISOU 2031  OG  SER A1026     7168   9207  12662   -317   1509  -3136       O  
ATOM   2032  N   ALA A1027      -1.032  59.824  49.951  1.00 63.48           N  
ANISOU 2032  N   ALA A1027     5925   7698  10496   -235   1596  -2600       N  
ATOM   2033  CA  ALA A1027      -1.195  59.188  48.638  1.00 62.19           C  
ANISOU 2033  CA  ALA A1027     5739   7457  10434   -136   1438  -2512       C  
ATOM   2034  C   ALA A1027      -1.449  60.224  47.529  1.00 64.94           C  
ANISOU 2034  C   ALA A1027     5949   7710  11016    -29   1136  -2555       C  
ATOM   2035  O   ALA A1027      -0.817  60.180  46.481  1.00 62.19           O  
ANISOU 2035  O   ALA A1027     5657   7397  10574     70    926  -2362       O  
ATOM   2036  CB  ALA A1027      -2.345  58.190  48.692  1.00 63.99           C  
ANISOU 2036  CB  ALA A1027     5875   7578  10859   -181   1635  -2683       C  
ATOM   2037  N   SER A1028      -2.325  61.192  47.816  1.00 63.26           N  
ANISOU 2037  N   SER A1028     5555   7380  11101    -56   1123  -2798       N  
ATOM   2038  CA  SER A1028      -2.750  62.271  46.935  1.00 64.38           C  
ANISOU 2038  CA  SER A1028     5534   7395  11533     39    851  -2855       C  
ATOM   2039  C   SER A1028      -1.639  63.240  46.552  1.00 68.27           C  
ANISOU 2039  C   SER A1028     6091   7933  11915    107    650  -2626       C  
ATOM   2040  O   SER A1028      -1.657  63.756  45.439  1.00 68.89           O  
ANISOU 2040  O   SER A1028     6118   7948  12108    222    394  -2514       O  
ATOM   2041  CB  SER A1028      -3.911  63.025  47.577  1.00 72.26           C  
ANISOU 2041  CB  SER A1028     6306   8242  12907    -33    931  -3197       C  
ATOM   2042  OG  SER A1028      -4.454  63.968  46.670  1.00 88.40           O  
ANISOU 2042  OG  SER A1028     8172  10131  15285     73    652  -3248       O  
ATOM   2043  N   GLU A1029      -0.683  63.490  47.465  1.00 64.01           N  
ANISOU 2043  N   GLU A1029     5659   7505  11157     41    767  -2558       N  
ATOM   2044  CA  GLU A1029       0.436  64.409  47.257  1.00 63.00           C  
ANISOU 2044  CA  GLU A1029     5576   7407  10954     91    622  -2378       C  
ATOM   2045  C   GLU A1029       1.714  63.665  46.863  1.00 66.10           C  
ANISOU 2045  C   GLU A1029     6195   7944  10974    130    593  -2086       C  
ATOM   2046  O   GLU A1029       2.693  64.297  46.466  1.00 66.61           O  
ANISOU 2046  O   GLU A1029     6309   8024  10977    183    467  -1913       O  
ATOM   2047  CB  GLU A1029       0.684  65.235  48.528  1.00 65.04           C  
ANISOU 2047  CB  GLU A1029     5764   7698  11251      0    757  -2553       C  
ATOM   2048  CG  GLU A1029      -0.527  66.029  49.005  1.00 73.97           C  
ANISOU 2048  CG  GLU A1029     6641   8684  12781    -60    806  -2886       C  
ATOM   2049  CD  GLU A1029      -0.419  66.706  50.363  1.00101.25           C  
ANISOU 2049  CD  GLU A1029     9998  12208  16264   -174    981  -3135       C  
ATOM   2050  OE1 GLU A1029      -1.472  66.849  51.028  1.00105.74           O  
ANISOU 2050  OE1 GLU A1029    10405  12722  17050   -271   1128  -3448       O  
ATOM   2051  OE2 GLU A1029       0.697  67.132  50.748  1.00 91.38           O  
ANISOU 2051  OE2 GLU A1029     8811  11069  14841   -168    971  -3050       O  
ATOM   2052  N   ARG A1030       1.698  62.335  46.958  1.00 60.75           N  
ANISOU 2052  N   ARG A1030     5637   7353  10092    101    719  -2041       N  
ATOM   2053  CA  ARG A1030       2.833  61.450  46.665  1.00 58.28           C  
ANISOU 2053  CA  ARG A1030     5517   7164   9462    123    714  -1800       C  
ATOM   2054  C   ARG A1030       3.150  61.422  45.150  1.00 59.69           C  
ANISOU 2054  C   ARG A1030     5713   7332   9636    228    490  -1624       C  
ATOM   2055  O   ARG A1030       2.238  61.212  44.354  1.00 58.99           O  
ANISOU 2055  O   ARG A1030     5525   7184   9705    277    404  -1694       O  
ATOM   2056  CB  ARG A1030       2.513  60.051  47.205  1.00 55.11           C  
ANISOU 2056  CB  ARG A1030     5187   6814   8939     58    925  -1827       C  
ATOM   2057  CG  ARG A1030       3.694  59.164  47.495  1.00 53.23           C  
ANISOU 2057  CG  ARG A1030     5136   6700   8390     45    988  -1620       C  
ATOM   2058  CD  ARG A1030       3.260  57.931  48.263  1.00 49.04           C  
ANISOU 2058  CD  ARG A1030     4653   6188   7791    -28   1229  -1642       C  
ATOM   2059  NE  ARG A1030       2.567  58.301  49.493  1.00 60.85           N  
ANISOU 2059  NE  ARG A1030     6106   7692   9323   -116   1421  -1820       N  
ATOM   2060  CZ  ARG A1030       1.736  57.501  50.150  1.00 69.42           C  
ANISOU 2060  CZ  ARG A1030     7178   8750  10448   -193   1662  -1907       C  
ATOM   2061  NH1 ARG A1030       1.515  56.267  49.721  1.00 50.38           N  
ANISOU 2061  NH1 ARG A1030     4783   6282   8078   -186   1741  -1829       N  
ATOM   2062  NH2 ARG A1030       1.111  57.934  51.241  1.00 54.71           N  
ANISOU 2062  NH2 ARG A1030     5269   6912   8605   -285   1845  -2088       N  
ATOM   2063  N   PRO A1031       4.421  61.677  44.731  1.00 54.92           N  
ANISOU 2063  N   PRO A1031     5221   6791   8854    265    393  -1413       N  
ATOM   2064  CA  PRO A1031       4.740  61.699  43.294  1.00 53.68           C  
ANISOU 2064  CA  PRO A1031     5086   6650   8660    352    202  -1243       C  
ATOM   2065  C   PRO A1031       4.712  60.323  42.650  1.00 56.37           C  
ANISOU 2065  C   PRO A1031     5479   7077   8863    360    219  -1211       C  
ATOM   2066  O   PRO A1031       4.902  59.300  43.322  1.00 54.62           O  
ANISOU 2066  O   PRO A1031     5321   6899   8533    298    382  -1237       O  
ATOM   2067  CB  PRO A1031       6.189  62.234  43.275  1.00 53.63           C  
ANISOU 2067  CB  PRO A1031     5189   6685   8502    358    165  -1061       C  
ATOM   2068  CG  PRO A1031       6.750  61.779  44.558  1.00 56.78           C  
ANISOU 2068  CG  PRO A1031     5668   7147   8758    282    337  -1115       C  
ATOM   2069  CD  PRO A1031       5.636  61.939  45.535  1.00 55.13           C  
ANISOU 2069  CD  PRO A1031     5353   6890   8703    229    457  -1337       C  
ATOM   2070  N   GLU A1032       4.554  60.317  41.328  1.00 52.96           N  
ANISOU 2070  N   GLU A1032     5015   6678   8429    440     46  -1142       N  
ATOM   2071  CA  GLU A1032       4.654  59.111  40.513  1.00 53.22           C  
ANISOU 2071  CA  GLU A1032     5068   6818   8337    455     34  -1130       C  
ATOM   2072  C   GLU A1032       6.143  58.644  40.529  1.00 54.18           C  
ANISOU 2072  C   GLU A1032     5341   7030   8216    414     85   -960       C  
ATOM   2073  O   GLU A1032       7.042  59.458  40.771  1.00 54.08           O  
ANISOU 2073  O   GLU A1032     5408   7005   8135    407     64   -833       O  
ATOM   2074  CB  GLU A1032       4.199  59.422  39.089  1.00 56.63           C  
ANISOU 2074  CB  GLU A1032     5427   7304   8786    558   -187  -1100       C  
ATOM   2075  CG  GLU A1032       3.642  58.198  38.406  1.00 76.28           C  
ANISOU 2075  CG  GLU A1032     7834   9881  11269    580   -192  -1240       C  
ATOM   2076  CD  GLU A1032       2.137  58.194  38.282  1.00 96.72           C  
ANISOU 2076  CD  GLU A1032    10244  12395  14111    633   -246  -1471       C  
ATOM   2077  OE1 GLU A1032       1.475  58.374  39.334  1.00 80.98           O  
ANISOU 2077  OE1 GLU A1032     8195  10257  12316    582   -114  -1608       O  
ATOM   2078  OE2 GLU A1032       1.626  57.977  37.150  1.00 71.63           O  
ANISOU 2078  OE2 GLU A1032     6973   9314  10930    724   -416  -1537       O  
ATOM   2079  N   VAL A1033       6.412  57.358  40.304  1.00 49.65           N  
ANISOU 2079  N   VAL A1033     4783   6526   7555    385    155   -979       N  
ATOM   2080  CA  VAL A1033       7.794  56.867  40.435  1.00 47.91           C  
ANISOU 2080  CA  VAL A1033     4686   6364   7155    340    207   -846       C  
ATOM   2081  C   VAL A1033       8.736  57.364  39.281  1.00 49.41           C  
ANISOU 2081  C   VAL A1033     4932   6642   7199    374     65   -700       C  
ATOM   2082  O   VAL A1033       9.896  57.618  39.574  1.00 47.51           O  
ANISOU 2082  O   VAL A1033     4792   6400   6860    343     90   -588       O  
ATOM   2083  CB  VAL A1033       7.901  55.356  40.695  1.00 50.27           C  
ANISOU 2083  CB  VAL A1033     4973   6676   7452    289    341   -899       C  
ATOM   2084  CG1 VAL A1033       7.820  54.569  39.415  1.00 50.06           C  
ANISOU 2084  CG1 VAL A1033     4858   6742   7422    314    269   -960       C  
ATOM   2085  CG2 VAL A1033       9.196  55.033  41.447  1.00 49.74           C  
ANISOU 2085  CG2 VAL A1033     5034   6611   7255    237    418   -772       C  
ATOM   2086  N   ARG A1034       8.224  57.621  38.051  1.00 48.29           N  
ANISOU 2086  N   ARG A1034     4725   6575   7047    440    -80   -700       N  
ATOM   2087  CA  ARG A1034       9.035  58.170  36.961  1.00 49.51           C  
ANISOU 2087  CA  ARG A1034     4943   6826   7042    468   -194   -538       C  
ATOM   2088  C   ARG A1034       9.623  59.554  37.345  1.00 53.69           C  
ANISOU 2088  C   ARG A1034     5547   7253   7601    477   -213   -379       C  
ATOM   2089  O   ARG A1034      10.771  59.833  37.015  1.00 52.92           O  
ANISOU 2089  O   ARG A1034     5537   7182   7389    454   -204   -245       O  
ATOM   2090  CB  ARG A1034       8.226  58.298  35.658  1.00 50.85           C  
ANISOU 2090  CB  ARG A1034     5032   7115   7174    553   -360   -553       C  
ATOM   2091  CG  ARG A1034       9.071  58.819  34.464  1.00 52.47           C  
ANISOU 2091  CG  ARG A1034     5318   7454   7163    576   -458   -357       C  
ATOM   2092  CD  ARG A1034       8.623  58.242  33.141  1.00 54.29           C  
ANISOU 2092  CD  ARG A1034     5478   7905   7245    628   -579   -424       C  
ATOM   2093  NE  ARG A1034       8.994  56.839  33.060  1.00 53.68           N  
ANISOU 2093  NE  ARG A1034     5352   7925   7120    557   -476   -598       N  
ATOM   2094  CZ  ARG A1034       8.606  56.008  32.109  1.00 62.20           C  
ANISOU 2094  CZ  ARG A1034     6318   9197   8116    581   -538   -757       C  
ATOM   2095  NH1 ARG A1034       7.839  56.438  31.118  1.00 51.72           N  
ANISOU 2095  NH1 ARG A1034     4936   8020   6693    685   -721   -755       N  
ATOM   2096  NH2 ARG A1034       8.994  54.746  32.128  1.00 54.43           N  
ANISOU 2096  NH2 ARG A1034     5262   8264   7157    507   -425   -927       N  
ATOM   2097  N   THR A1035       8.824  60.402  38.030  1.00 50.44           N  
ANISOU 2097  N   THR A1035     5074   6713   7378    504   -226   -424       N  
ATOM   2098  CA  THR A1035       9.232  61.730  38.488  1.00 50.70           C  
ANISOU 2098  CA  THR A1035     5121   6623   7518    513   -234   -327       C  
ATOM   2099  C   THR A1035      10.396  61.601  39.474  1.00 54.90           C  
ANISOU 2099  C   THR A1035     5736   7130   7992    443   -102   -330       C  
ATOM   2100  O   THR A1035      11.375  62.334  39.365  1.00 56.25           O  
ANISOU 2100  O   THR A1035     5954   7262   8157    442   -103   -215       O  
ATOM   2101  CB  THR A1035       8.026  62.467  39.117  1.00 56.61           C  
ANISOU 2101  CB  THR A1035     5745   7243   8522    542   -259   -447       C  
ATOM   2102  OG1 THR A1035       6.956  62.496  38.177  1.00 60.28           O  
ANISOU 2102  OG1 THR A1035     6124   7732   9047    619   -407   -459       O  
ATOM   2103  CG2 THR A1035       8.360  63.893  39.532  1.00 52.96           C  
ANISOU 2103  CG2 THR A1035     5246   6638   8237    554   -272   -378       C  
ATOM   2104  N   VAL A1036      10.272  60.663  40.434  1.00 49.56           N  
ANISOU 2104  N   VAL A1036     5071   6473   7286    391     13   -462       N  
ATOM   2105  CA  VAL A1036      11.259  60.363  41.474  1.00 47.74           C  
ANISOU 2105  CA  VAL A1036     4919   6245   6977    338    119   -476       C  
ATOM   2106  C   VAL A1036      12.555  59.878  40.813  1.00 51.66           C  
ANISOU 2106  C   VAL A1036     5502   6801   7325    319    106   -368       C  
ATOM   2107  O   VAL A1036      13.612  60.411  41.099  1.00 51.41           O  
ANISOU 2107  O   VAL A1036     5517   6737   7281    311    118   -322       O  
ATOM   2108  CB  VAL A1036      10.648  59.311  42.448  1.00 50.36           C  
ANISOU 2108  CB  VAL A1036     5246   6597   7293    295    238   -596       C  
ATOM   2109  CG1 VAL A1036      11.691  58.785  43.431  1.00 49.61           C  
ANISOU 2109  CG1 VAL A1036     5245   6533   7070    254    322   -575       C  
ATOM   2110  CG2 VAL A1036       9.426  59.871  43.175  1.00 49.80           C  
ANISOU 2110  CG2 VAL A1036     5081   6461   7378    295    279   -733       C  
ATOM   2111  N   PHE A1037      12.459  58.898  39.884  1.00 48.93           N  
ANISOU 2111  N   PHE A1037     5155   6543   6895    312     84   -358       N  
ATOM   2112  CA  PHE A1037      13.599  58.380  39.136  1.00 46.82           C  
ANISOU 2112  CA  PHE A1037     4943   6342   6505    281     79   -292       C  
ATOM   2113  C   PHE A1037      14.302  59.553  38.394  1.00 53.27           C  
ANISOU 2113  C   PHE A1037     5797   7141   7304    301     24   -158       C  
ATOM   2114  O   PHE A1037      15.501  59.751  38.596  1.00 53.42           O  
ANISOU 2114  O   PHE A1037     5870   7122   7305    271     65   -122       O  
ATOM   2115  CB  PHE A1037      13.130  57.305  38.143  1.00 48.43           C  
ANISOU 2115  CB  PHE A1037     5089   6659   6654    274     56   -348       C  
ATOM   2116  CG  PHE A1037      14.190  56.819  37.179  1.00 49.66           C  
ANISOU 2116  CG  PHE A1037     5271   6908   6690    233     51   -315       C  
ATOM   2117  CD1 PHE A1037      15.488  56.548  37.617  1.00 50.80           C  
ANISOU 2117  CD1 PHE A1037     5476   7007   6818    178    111   -297       C  
ATOM   2118  CD2 PHE A1037      13.890  56.616  35.841  1.00 52.75           C  
ANISOU 2118  CD2 PHE A1037     5614   7444   6983    247    -17   -324       C  
ATOM   2119  CE1 PHE A1037      16.470  56.082  36.726  1.00 51.65           C  
ANISOU 2119  CE1 PHE A1037     5588   7188   6846    124    120   -301       C  
ATOM   2120  CE2 PHE A1037      14.866  56.139  34.954  1.00 55.30           C  
ANISOU 2120  CE2 PHE A1037     5949   7875   7188    190      0   -326       C  
ATOM   2121  CZ  PHE A1037      16.153  55.870  35.411  1.00 52.45           C  
ANISOU 2121  CZ  PHE A1037     5640   7442   6846    123     77   -320       C  
ATOM   2122  N   GLU A1038      13.540  60.355  37.607  1.00 49.22           N  
ANISOU 2122  N   GLU A1038     5245   6636   6822    359    -65    -81       N  
ATOM   2123  CA  GLU A1038      14.068  61.502  36.870  1.00 49.80           C  
ANISOU 2123  CA  GLU A1038     5349   6673   6901    385   -105     91       C  
ATOM   2124  C   GLU A1038      14.755  62.516  37.788  1.00 53.94           C  
ANISOU 2124  C   GLU A1038     5874   7037   7583    380    -47    106       C  
ATOM   2125  O   GLU A1038      15.817  63.021  37.421  1.00 54.34           O  
ANISOU 2125  O   GLU A1038     5969   7047   7632    362     -8    205       O  
ATOM   2126  CB  GLU A1038      12.953  62.212  36.084  1.00 52.51           C  
ANISOU 2126  CB  GLU A1038     5637   7029   7287    466   -230    185       C  
ATOM   2127  CG  GLU A1038      12.503  61.502  34.817  1.00 65.70           C  
ANISOU 2127  CG  GLU A1038     7304   8894   8765    490   -316    202       C  
ATOM   2128  CD  GLU A1038      11.201  62.006  34.205  1.00 83.71           C  
ANISOU 2128  CD  GLU A1038     9510  11201  11094    589   -473    244       C  
ATOM   2129  OE1 GLU A1038      10.499  62.825  34.846  1.00 77.18           O  
ANISOU 2129  OE1 GLU A1038     8617  10215  10492    632   -510    236       O  
ATOM   2130  OE2 GLU A1038      10.870  61.555  33.084  1.00 67.62           O  
ANISOU 2130  OE2 GLU A1038     7464   9352   8875    625   -568    261       O  
ATOM   2131  N   ASP A1039      14.150  62.809  38.965  1.00 49.78           N  
ANISOU 2131  N   ASP A1039     5285   6426   7202    392    -28    -17       N  
ATOM   2132  CA  ASP A1039      14.691  63.759  39.924  1.00 50.56           C  
ANISOU 2132  CA  ASP A1039     5347   6399   7465    391     22    -65       C  
ATOM   2133  C   ASP A1039      15.953  63.241  40.592  1.00 55.52           C  
ANISOU 2133  C   ASP A1039     6038   7047   8010    345     96   -137       C  
ATOM   2134  O   ASP A1039      16.902  64.008  40.757  1.00 57.87           O  
ANISOU 2134  O   ASP A1039     6322   7257   8410    346    129   -129       O  
ATOM   2135  CB  ASP A1039      13.623  64.192  40.936  1.00 53.42           C  
ANISOU 2135  CB  ASP A1039     5608   6702   7988    407     25   -208       C  
ATOM   2136  CG  ASP A1039      12.512  65.062  40.353  1.00 70.23           C  
ANISOU 2136  CG  ASP A1039     7636   8749  10298    463    -66   -148       C  
ATOM   2137  OD1 ASP A1039      12.687  65.580  39.217  1.00 72.21           O  
ANISOU 2137  OD1 ASP A1039     7904   8975  10558    503   -135     47       O  
ATOM   2138  OD2 ASP A1039      11.461  65.213  41.021  1.00 77.17           O  
ANISOU 2138  OD2 ASP A1039     8421   9591  11310    467    -67   -290       O  
ATOM   2139  N   LEU A1040      16.010  61.936  40.906  1.00 49.82           N  
ANISOU 2139  N   LEU A1040     5372   6425   7133    310    120   -203       N  
ATOM   2140  CA  LEU A1040      17.225  61.342  41.470  1.00 48.53           C  
ANISOU 2140  CA  LEU A1040     5266   6277   6897    277    161   -254       C  
ATOM   2141  C   LEU A1040      18.323  61.363  40.389  1.00 52.49           C  
ANISOU 2141  C   LEU A1040     5807   6769   7368    251    164   -164       C  
ATOM   2142  O   LEU A1040      19.488  61.651  40.684  1.00 51.15           O  
ANISOU 2142  O   LEU A1040     5648   6539   7249    240    193   -201       O  
ATOM   2143  CB  LEU A1040      16.970  59.890  41.932  1.00 47.07           C  
ANISOU 2143  CB  LEU A1040     5118   6177   6588    249    183   -305       C  
ATOM   2144  CG  LEU A1040      16.184  59.703  43.235  1.00 50.79           C  
ANISOU 2144  CG  LEU A1040     5575   6667   7055    256    223   -395       C  
ATOM   2145  CD1 LEU A1040      15.740  58.280  43.382  1.00 49.17           C  
ANISOU 2145  CD1 LEU A1040     5396   6518   6768    228    264   -394       C  
ATOM   2146  CD2 LEU A1040      17.012  60.108  44.480  1.00 52.29           C  
ANISOU 2146  CD2 LEU A1040     5782   6854   7232    268    237   -474       C  
ATOM   2147  N   LEU A1041      17.925  61.106  39.124  1.00 49.49           N  
ANISOU 2147  N   LEU A1041     5439   6458   6908    243    138    -65       N  
ATOM   2148  CA  LEU A1041      18.849  61.063  37.986  1.00 49.51           C  
ANISOU 2148  CA  LEU A1041     5481   6489   6841    203    162     18       C  
ATOM   2149  C   LEU A1041      19.455  62.438  37.672  1.00 54.64           C  
ANISOU 2149  C   LEU A1041     6127   7019   7614    220    196    125       C  
ATOM   2150  O   LEU A1041      20.638  62.498  37.386  1.00 55.69           O  
ANISOU 2150  O   LEU A1041     6286   7112   7763    176    262    125       O  
ATOM   2151  CB  LEU A1041      18.168  60.417  36.781  1.00 49.63           C  
ANISOU 2151  CB  LEU A1041     5498   6655   6705    195    120     70       C  
ATOM   2152  CG  LEU A1041      18.970  59.998  35.578  1.00 54.34           C  
ANISOU 2152  CG  LEU A1041     6126   7353   7167    135    154    108       C  
ATOM   2153  CD1 LEU A1041      20.136  59.058  35.944  1.00 51.83           C  
ANISOU 2153  CD1 LEU A1041     5812   7016   6863     60    217    -23       C  
ATOM   2154  CD2 LEU A1041      18.043  59.320  34.574  1.00 57.25           C  
ANISOU 2154  CD2 LEU A1041     6463   7908   7380    144     92    104       C  
ATOM   2155  N   SER A1042      18.698  63.537  37.863  1.00 51.33           N  
ANISOU 2155  N   SER A1042     5654   6513   7337    280    165    190       N  
ATOM   2156  CA  SER A1042      19.203  64.890  37.632  1.00 52.30           C  
ANISOU 2156  CA  SER A1042     5742   6482   7649    301    210    299       C  
ATOM   2157  C   SER A1042      20.320  65.233  38.630  1.00 56.23           C  
ANISOU 2157  C   SER A1042     6197   6858   8309    286    283    146       C  
ATOM   2158  O   SER A1042      21.239  65.978  38.284  1.00 57.70           O  
ANISOU 2158  O   SER A1042     6366   6923   8635    274    363    200       O  
ATOM   2159  CB  SER A1042      18.071  65.917  37.675  1.00 56.35           C  
ANISOU 2159  CB  SER A1042     6171   6909   8330    370    148    383       C  
ATOM   2160  OG  SER A1042      17.470  65.966  38.957  1.00 63.76           O  
ANISOU 2160  OG  SER A1042     7030   7813   9385    389    128    194       O  
ATOM   2161  N   LEU A1043      20.297  64.597  39.822  1.00 51.30           N  
ANISOU 2161  N   LEU A1043     5561   6279   7652    286    260    -46       N  
ATOM   2162  CA  LEU A1043      21.315  64.763  40.873  1.00 49.71           C  
ANISOU 2162  CA  LEU A1043     5319   6012   7557    288    293   -225       C  
ATOM   2163  C   LEU A1043      22.658  64.140  40.479  1.00 53.01           C  
ANISOU 2163  C   LEU A1043     5794   6429   7920    238    333   -253       C  
ATOM   2164  O   LEU A1043      23.652  64.482  41.100  1.00 55.37           O  
ANISOU 2164  O   LEU A1043     6043   6643   8353    248    360   -392       O  
ATOM   2165  CB  LEU A1043      20.841  64.130  42.189  1.00 48.80           C  
ANISOU 2165  CB  LEU A1043     5200   5993   7351    305    246   -383       C  
ATOM   2166  CG  LEU A1043      19.998  64.953  43.191  1.00 53.72           C  
ANISOU 2166  CG  LEU A1043     5718   6593   8102    346    238   -495       C  
ATOM   2167  CD1 LEU A1043      19.657  66.359  42.719  1.00 54.20           C  
ANISOU 2167  CD1 LEU A1043     5665   6502   8428    373    259   -431       C  
ATOM   2168  CD2 LEU A1043      18.868  64.149  43.755  1.00 50.68           C  
ANISOU 2168  CD2 LEU A1043     5367   6331   7557    341    212   -525       C  
ATOM   2169  N   SER A1044      22.691  63.194  39.512  1.00 46.76           N  
ANISOU 2169  N   SER A1044     5083   5735   6949    186    334   -163       N  
ATOM   2170  CA  SER A1044      23.947  62.580  39.074  1.00 47.36           C  
ANISOU 2170  CA  SER A1044     5191   5803   7002    123    382   -216       C  
ATOM   2171  C   SER A1044      24.607  63.449  37.974  1.00 54.53           C  
ANISOU 2171  C   SER A1044     6099   6619   8002     86    490   -101       C  
ATOM   2172  O   SER A1044      25.611  63.053  37.387  1.00 56.00           O  
ANISOU 2172  O   SER A1044     6306   6795   8177     17    559   -138       O  
ATOM   2173  CB  SER A1044      23.738  61.134  38.624  1.00 48.04           C  
ANISOU 2173  CB  SER A1044     5326   6032   6893     72    348   -220       C  
ATOM   2174  OG  SER A1044      22.925  61.119  37.460  1.00 57.06           O  
ANISOU 2174  OG  SER A1044     6495   7278   7909     57    352    -75       O  
ATOM   2175  N   SER A1045      24.050  64.651  37.730  1.00 52.27           N  
ANISOU 2175  N   SER A1045     5779   6251   7832    131    514     39       N  
ATOM   2176  CA  SER A1045      24.594  65.647  36.811  1.00 71.14           C  
ANISOU 2176  CA  SER A1045     8163   8521  10347    110    633    194       C  
ATOM   2177  C   SER A1045      24.794  66.918  37.619  1.00 84.12           C  
ANISOU 2177  C   SER A1045     9684   9955  12323    168    672    130       C  
ATOM   2178  O   SER A1045      25.638  67.727  37.275  1.00 57.86           O  
ANISOU 2178  O   SER A1045     6312   6462   9209    150    800    165       O  
ATOM   2179  CB  SER A1045      23.640  65.909  35.650  1.00 74.81           C  
ANISOU 2179  CB  SER A1045     8687   9078  10660    121    613    463       C  
ATOM   2180  OG  SER A1045      23.454  64.735  34.881  1.00 82.65           O  
ANISOU 2180  OG  SER A1045     9763  10287  11354     69    578    476       O  
TER    2181      SER A1045                                                      
HETATM 2182  PG  ANP A1101      11.413  38.978  52.546  1.00 50.90           P  
HETATM 2183  O1G ANP A1101      12.300  38.908  51.353  1.00 54.19           O1-
HETATM 2184  O2G ANP A1101      10.832  37.626  52.748  1.00 53.02           O  
HETATM 2185  O3G ANP A1101      10.318  39.947  52.276  1.00 50.46           O1-
HETATM 2186  PB  ANP A1101      13.862  39.340  54.079  1.00 54.72           P  
HETATM 2187  O1B ANP A1101      14.617  40.057  53.001  1.00 53.23           O  
HETATM 2188  O2B ANP A1101      14.234  39.598  55.504  1.00 58.30           O1-
HETATM 2189  N3B ANP A1101      12.256  39.434  53.858  1.00 52.13           N  
HETATM 2190  PA  ANP A1101      15.025  37.005  52.774  1.00 55.67           P  
HETATM 2191  O1A ANP A1101      14.764  37.627  51.447  1.00 52.61           O1-
HETATM 2192  O2A ANP A1101      14.784  35.549  52.943  1.00 57.31           O  
HETATM 2193  O3A ANP A1101      14.177  37.791  53.875  1.00 52.94           O  
HETATM 2194  O5' ANP A1101      16.518  37.342  53.223  1.00 60.54           O  
HETATM 2195  C5' ANP A1101      16.990  36.855  54.498  1.00 62.04           C  
HETATM 2196  C4' ANP A1101      18.077  37.764  55.015  1.00 63.55           C  
HETATM 2197  O4' ANP A1101      19.278  37.563  54.231  1.00 63.72           O  
HETATM 2198  C3' ANP A1101      17.800  39.268  54.941  1.00 64.69           C  
HETATM 2199  O3' ANP A1101      18.463  39.968  55.985  1.00 64.21           O  
HETATM 2200  C2' ANP A1101      18.360  39.637  53.566  1.00 64.65           C  
HETATM 2201  O2' ANP A1101      18.756  40.988  53.503  1.00 61.71           O  
HETATM 2202  C1' ANP A1101      19.554  38.695  53.439  1.00 64.33           C  
HETATM 2203  N9  ANP A1101      19.786  38.217  52.089  1.00 64.82           N  
HETATM 2204  C8  ANP A1101      18.898  37.569  51.276  1.00 64.43           C  
HETATM 2205  N7  ANP A1101      19.413  37.246  50.113  1.00 65.08           N  
HETATM 2206  C5  ANP A1101      20.722  37.701  50.175  1.00 65.50           C  
HETATM 2207  C6  ANP A1101      21.800  37.663  49.265  1.00 64.32           C  
HETATM 2208  N6  ANP A1101      21.719  37.111  48.059  1.00 61.20           N  
HETATM 2209  N1  ANP A1101      22.983  38.211  49.649  1.00 65.49           N  
HETATM 2210  C2  ANP A1101      23.064  38.764  50.870  1.00 65.56           C  
HETATM 2211  N3  ANP A1101      22.116  38.856  51.804  1.00 67.22           N  
HETATM 2212  C4  ANP A1101      20.960  38.300  51.394  1.00 65.61           C  
HETATM 2213 MG    MG A1102      14.414  39.228  50.830  1.00 52.48          MG2+
HETATM 2214  O   HOH A1201      19.255  42.263  56.533  1.00 66.05           O  
HETATM 2215  O   HOH A1202      15.596  40.569  36.294  1.00 48.90           O  
HETATM 2216  O   HOH A1203       9.043  37.695  42.229  1.00 49.22           O  
HETATM 2217  O   HOH A1204      21.577  59.600  61.340  1.00 64.37           O  
HETATM 2218  O   HOH A1205      21.637  37.364  37.917  1.00 88.37           O  
HETATM 2219  O   HOH A1206       6.758  48.134  48.576  1.00 49.12           O  
HETATM 2220  O   HOH A1207       2.126  28.114  51.304  1.00 77.17           O  
HETATM 2221  O   HOH A1208      12.312  34.229  53.632  1.00 59.59           O  
HETATM 2222  O   HOH A1209      10.433  67.993  49.642  1.00 61.93           O  
HETATM 2223  O   HOH A1210      19.774  36.345  45.994  1.00 80.09           O  
HETATM 2224  O   HOH A1211      31.900  52.143  50.769  1.00 57.95           O  
HETATM 2225  O   HOH A1212      16.504  39.681  50.387  1.00 51.70           O  
HETATM 2226  O   HOH A1213      10.822  40.997  56.338  1.00 61.35           O  
HETATM 2227  O   HOH A1214      19.469  56.476  32.736  1.00 71.13           O  
HETATM 2228  O   HOH A1215       4.043  44.838  52.013  1.00 56.05           O  
HETATM 2229  O   HOH A1216      14.864  47.437  57.384  1.00 58.65           O  
HETATM 2230  O   HOH A1217      30.921  60.436  51.185  1.00 52.39           O  
HETATM 2231  O   HOH A1218      13.223  52.364  34.030  1.00 55.04           O  
HETATM 2232  O   HOH A1219       1.235  38.585  39.047  1.00 67.75           O  
HETATM 2233  O   HOH A1220      13.740  37.173  42.159  1.00 47.08           O  
HETATM 2234  O   HOH A1221      25.530  31.646  39.882  1.00 80.84           O  
HETATM 2235  O   HOH A1222       5.803  56.550  37.126  1.00 58.02           O  
HETATM 2236  O   HOH A1223      23.267  33.149  40.050  1.00 66.82           O  
HETATM 2237  O   HOH A1224       4.099  48.750  28.487  1.00 52.40           O  
HETATM 2238  O   HOH A1225       0.734  64.688  53.055  1.00 64.53           O  
HETATM 2239  O   HOH A1226      13.559  33.126  45.108  1.00 49.65           O  
HETATM 2240  O   HOH A1227      15.040  35.790  49.088  1.00 62.72           O  
HETATM 2241  O   HOH A1228      14.568  37.891  44.561  1.00 60.78           O  
HETATM 2242  O   HOH A1229      13.673  39.383  37.615  1.00 53.50           O  
HETATM 2243  O   HOH A1230       4.706  42.170  47.341  1.00 54.42           O  
HETATM 2244  O   HOH A1231       0.041  59.359  35.174  1.00 60.59           O  
HETATM 2245  O   HOH A1232      15.154  50.812  32.925  1.00 69.21           O  
HETATM 2246  O   HOH A1233      16.726  63.532  34.728  1.00 70.30           O  
HETATM 2247  O   HOH A1234      14.125  45.464  30.882  1.00 65.16           O  
HETATM 2248  O   HOH A1235      23.031  40.621  53.947  1.00 56.59           O  
HETATM 2249  O   HOH A1236      12.364  67.449  45.414  1.00 72.52           O  
HETATM 2250  O   HOH A1237      23.163  19.090  42.411  1.00 74.93           O  
HETATM 2251  O   HOH A1238      31.420  52.949  44.085  1.00 59.81           O  
HETATM 2252  O   HOH A1239      27.674  52.519  55.526  1.00 56.69           O  
HETATM 2253  O   HOH A1240      33.278  56.146  52.661  1.00 69.25           O  
HETATM 2254  O   HOH A1241      14.288  70.132  52.502  1.00 71.04           O  
HETATM 2255  O   HOH A1242      15.447  67.276  44.724  1.00 67.57           O  
HETATM 2256  O   HOH A1243       7.278  52.133  62.370  1.00 76.68           O  
HETATM 2257  O   HOH A1244      13.484  42.683  56.812  1.00 66.35           O  
HETATM 2258  O   HOH A1245      11.759  35.672  45.609  1.00 55.48           O  
HETATM 2259  O   HOH A1246      -6.430  31.691  46.964  1.00 78.16           O  
HETATM 2260  O   HOH A1247      14.443  45.265  55.964  1.00 54.72           O  
HETATM 2261  O   HOH A1248      -3.274  39.489  44.986  1.00 88.80           O  
HETATM 2262  O   HOH A1249       7.377  15.226  50.109  1.00 82.44           O  
HETATM 2263  O   HOH A1250      10.349  54.280  59.277  1.00 76.39           O  
HETATM 2264  O   HOH A1251      11.397  37.545  43.652  1.00 60.49           O  
HETATM 2265  O   HOH A1252      14.586  31.358  33.569  1.00 73.01           O  
HETATM 2266  O   HOH A1253      17.337  42.078  32.215  1.00 73.66           O  
HETATM 2267  O   HOH A1254      15.582  21.998  47.438  1.00 78.58           O  
HETATM 2268  O   HOH A1255      25.319  65.350  61.382  1.00 76.51           O  
HETATM 2269  O   HOH A1256      18.793  32.903  59.930  1.00 77.57           O  
HETATM 2270  O   HOH A1257       8.108  63.694  66.052  1.00 87.55           O  
HETATM 2271  O   HOH A1258      21.512  24.576  29.706  1.00 75.36           O  
HETATM 2272  O   HOH A1259      29.973  48.969  47.134  1.00 70.82           O  
HETATM 2273  O   HOH A1260      26.630  35.946  53.137  1.00 86.11           O  
HETATM 2274  O   HOH A1261      27.574  32.026  38.128  1.00 79.51           O  
HETATM 2275  O   HOH A1262      15.495  61.812  32.652  1.00 76.85           O  
HETATM 2276  O   HOH A1263      11.299  35.584  29.364  1.00 95.36           O  
HETATM 2277  O   HOH A1264     -10.112  34.664  49.738  1.00 83.78           O  
HETATM 2278  O   HOH A1265      15.151  37.916  26.310  1.00 85.62           O  
CONECT 1150 2213                                                                
CONECT 1247 2213                                                                
CONECT 2182 2183 2184 2185 2189                                                 
CONECT 2183 2182 2213                                                           
CONECT 2184 2182                                                                
CONECT 2185 2182                                                                
CONECT 2186 2187 2188 2189 2193                                                 
CONECT 2187 2186 2213                                                           
CONECT 2188 2186                                                                
CONECT 2189 2182 2186                                                           
CONECT 2190 2191 2192 2193 2194                                                 
CONECT 2191 2190 2213                                                           
CONECT 2192 2190                                                                
CONECT 2193 2186 2190                                                           
CONECT 2194 2190 2195                                                           
CONECT 2195 2194 2196                                                           
CONECT 2196 2195 2197 2198                                                      
CONECT 2197 2196 2202                                                           
CONECT 2198 2196 2199 2200                                                      
CONECT 2199 2198                                                                
CONECT 2200 2198 2201 2202                                                      
CONECT 2201 2200                                                                
CONECT 2202 2197 2200 2203                                                      
CONECT 2203 2202 2204 2212                                                      
CONECT 2204 2203 2205                                                           
CONECT 2205 2204 2206                                                           
CONECT 2206 2205 2207 2212                                                      
CONECT 2207 2206 2208 2209                                                      
CONECT 2208 2207                                                                
CONECT 2209 2207 2210                                                           
CONECT 2210 2209 2211                                                           
CONECT 2211 2210 2212                                                           
CONECT 2212 2203 2206 2211                                                      
CONECT 2213 1150 1247 2183 2187                                                 
CONECT 2213 2191 2225                                                           
CONECT 2225 2213                                                                
MASTER      435    0    2   13    9    0    7    6 2277    1   36   24          
END                                                                             



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