CNRS Nantes University UFIP UFIP
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***  MEMBRANE PROTEIN 12-JUN-13 4L6R  ***

elNémo ID: 21111011373513307

Job options:

ID        	=	 21111011373513307
JOBID     	=	 MEMBRANE PROTEIN 12-JUN-13 4L6R
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    MEMBRANE PROTEIN                        12-JUN-13   4L6R              
TITLE     STRUCTURE OF THE CLASS B HUMAN GLUCAGON G PROTEIN COUPLED RECEPTOR    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SOLUBLE CYTOCHROME B562 AND GLUCAGON RECEPTOR CHIMERA;     
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 23-128 AND 123-434;                           
COMPND   5 SYNONYM: CYTOCHROME B-562, GL-R;                                     
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI, HOMO SAPIENS;                 
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 562, 9606;                                           
SOURCE   5 GENE: CYBC, GCGR_HUMAN, GCGR;                                        
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 EXPRESSION_SYSTEM_VECTOR: PFASTBAC                                   
KEYWDS    HUMAN GLUCAGON RECEPTOR, DIABETES, GPCR NETWORK, PSI-BIOLOGY,         
KEYWDS   2 MEMBRANE PROTEIN, NOVEL PROTEIN ENGINEERING, STRUCTURAL GENOMICS,    
KEYWDS   3 PROTEIN STRUCTURE INITIATIVE, GPCR, MEMBRANE                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.Y.SIU,M.HE,C.DE GRAAF,G.W.HAN,D.YANG,Z.ZHANG,C.ZHOU,Q.XU,D.WACKER,  
AUTHOR   2 J.S.JOSEPH,W.LIU,J.LAU,V.CHEREZOV,V.KATRITCH,M.W.WANG,R.C.STEVENS,   
AUTHOR   3 GPCR NETWORK (GPCR)                                                  
REVDAT   5   15-NOV-17 4L6R    1       REMARK                                   
REVDAT   4   16-AUG-17 4L6R    1       SOURCE REMARK                            
REVDAT   3   07-AUG-13 4L6R    1       JRNL                                     
REVDAT   2   31-JUL-13 4L6R    1       JRNL                                     
REVDAT   1   24-JUL-13 4L6R    0                                                
JRNL        AUTH   F.Y.SIU,M.HE,C.DE GRAAF,G.W.HAN,D.YANG,Z.ZHANG,C.ZHOU,Q.XU,  
JRNL        AUTH 2 D.WACKER,J.S.JOSEPH,W.LIU,J.LAU,V.CHEREZOV,V.KATRITCH,       
JRNL        AUTH 3 M.W.WANG,R.C.STEVENS                                         
JRNL        TITL   STRUCTURE OF THE HUMAN GLUCAGON CLASS B G-PROTEIN-COUPLED    
JRNL        TITL 2 RECEPTOR.                                                    
JRNL        REF    NATURE                        V. 499   444 2013              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   23863937                                                     
JRNL        DOI    10.1038/NATURE12393                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.0                                        
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) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.12                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 8981                           
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)  : 0.286                          
REMARK   3   R VALUE            (WORKING SET)  : 0.284                          
REMARK   3   FREE R VALUE                      : 0.339                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.790                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 430                            
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               : 5                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.30                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.69                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 91.59                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2308                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2830                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2190                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2812                   
REMARK   3   BIN FREE R VALUE                        : 0.3136                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.11                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 118                      
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            : 3049                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 7                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 110.4                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 126.8                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.12960                                             
REMARK   3    B22 (A**2) : 21.55530                                             
REMARK   3    B33 (A**2) : -20.42560                                            
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) : 1.234               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
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      : 0.883                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.842                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3118   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 4228   ; 2.500  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1432   ; 15.000 ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 65     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 459    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3118   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 403    ; 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   : 3725   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.04                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.79                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 1.81                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|1001 - A|1106 }                                    
REMARK   3    ORIGIN FOR THE GROUP (A):   16.4176    4.5252   -2.0054           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1043 T22:    0.0470                                    
REMARK   3     T33:   -0.5395 T12:   -0.2881                                    
REMARK   3     T13:   -0.1636 T23:    0.1298                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:   16.6309 L22:    6.0851                                    
REMARK   3     L33:   14.8771 L12:    2.3438                                    
REMARK   3     L13:    3.4299 L23:    0.6799                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1704 S12:   -0.1676 S13:   -0.5400                     
REMARK   3     S21:    0.7744 S22:   -0.1591 S23:   -0.9671                     
REMARK   3     S31:   -0.0046 S32:    0.2207 S33:   -0.0112                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { A|123 - A|429 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):   16.1524  -11.4685  -44.8801           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3790 T22:    0.6079                                    
REMARK   3     T33:   -0.6079 T12:   -0.2048                                    
REMARK   3     T13:    0.0527 T23:   -0.1883                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.9466 L22:    1.2789                                    
REMARK   3     L33:    5.4002 L12:    0.6168                                    
REMARK   3     L13:    1.8062 L23:    2.0350                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.3433 S12:    0.0555 S13:   -0.2635                     
REMARK   3     S21:    0.1079 S22:    0.3087 S23:   -0.2990                     
REMARK   3     S31:   -0.3608 S32:    1.0885 S33:   -0.6520                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: 1. THE DIFFRACTION DATA ARE               
REMARK   3  ANISOTROPIC. THE RESOLUTION LIMITS OF A*, B*, AND C* AXES ARE       
REMARK   3  3.3, 3.4 AND 3.3A, RESPECTIVELY. DIFFRAC DATA WERE INCLUDED IN      
REMARK   3  REFINEMENT TO 3.3A IN THE A* AND C* DIRECTIONS, WITH AN OVERALL     
REMARK   3  EFFECTIVE AND REPORTED RESOLUTION OF 3.4A. 2. THE DENSITIES AT      
REMARK   3  THE BOTTOM OF HELIX VI AND VII NEAR LYS349 WERE MODELLED AS A       
REMARK   3  PEG-400 FRAGMENT (PEG) MOLECULE FROM THE CRYSTALLIZATION            
REMARK   3  CONDITION.                                                          
REMARK   4                                                                      
REMARK   4 4L6R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUN-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000080251.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : AUG-12                             
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 14                                 
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0330                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9067                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.9                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : 0.01050                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 22.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.88200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.500                              
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: PDB ENTRY 2Z73                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES PH 6.0, 140-200 MM NAK        
REMARK 280  TARTRATE TETRAHYDRATE, 9-17% (V/V) PEG 400, 0.35-0.55% (V/V)        
REMARK 280  JEFFAMINE M-600 PH 7.0, 200 UM NNC0640, LIPIDIC CUBIC PHASE (LCP)   
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       28.30750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       81.66550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.32550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       81.66550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.30750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.32550            
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 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL UNIT IS UNKNOWN.           
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 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     ARG A   201                                                      
REMARK 465     TYR A   202                                                      
REMARK 465     SER A   203                                                      
REMARK 465     GLN A   204                                                      
REMARK 465     LYS A   205                                                      
REMARK 465     ILE A   206                                                      
REMARK 465     GLY A   207                                                      
REMARK 465     ASP A   208                                                      
REMARK 465     ASP A   209                                                      
REMARK 465     LEU A   210                                                      
REMARK 465     SER A   211                                                      
REMARK 465     VAL A   212                                                      
REMARK 465     SER A   213                                                      
REMARK 465     THR A   214                                                      
REMARK 465     TRP A   215                                                      
REMARK 465     THR A   430                                                      
REMARK 465     SER A   431                                                      
REMARK 465     ASN A   432                                                      
REMARK 465     GLY A   433                                                      
REMARK 465     ARG A   434                                                      
REMARK 465     PRO A   435                                                      
REMARK 465     LEU A   436                                                      
REMARK 465     GLU A   437                                                      
REMARK 465     VAL A   438                                                      
REMARK 465     LEU A   439                                                      
REMARK 465     PHE A   440                                                      
REMARK 465     GLN A   441                                                      
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     TYR A1101    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG A 225    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 235    CG1  CG2  CD1                                       
REMARK 470     GLU A 260    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 261    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE A 263    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE A 270    CG1  CG2  CD1                                       
REMARK 470     LEU A 277    CG   CD1  CD2                                       
REMARK 470     PHE A 278    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     VAL A 280    CG1  CG2                                            
REMARK 470     TRP A 282    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 282    CZ3  CH2                                            
REMARK 470     VAL A 285    CG1  CG2                                            
REMARK 470     LYS A 286    CG   CD   CE   NZ                                   
REMARK 470     CYS A 287    SG                                                  
REMARK 470     LEU A 288    CG   CD1  CD2                                       
REMARK 470     GLU A 290    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 291    CG   OD1  ND2                                       
REMARK 470     VAL A 292    CG1  CG2                                            
REMARK 470     GLN A 293    CG   CD   OE1  NE2                                  
REMARK 470     TRP A 295    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 295    CZ3  CH2                                            
REMARK 470     THR A 296    OG1  CG2                                            
REMARK 470     SER A 297    OG                                                  
REMARK 470     ASN A 298    CG   OD1  ND2                                       
REMARK 470     ASP A 299    CG   OD1  OD2                                       
REMARK 470     ILE A 306    CG1  CG2  CD1                                       
REMARK 470     PHE A 312    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG A 336    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET A 338    CG   SD   CE                                        
REMARK 470     LYS A 344    CG   CD   CE   NZ                                   
REMARK 470     VAL A 363    CG1  CG2                                            
REMARK 470     PHE A 367    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     VAL A 368    CG1  CG2                                            
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 166     -158.71   -165.19                                   
REMARK 500    ASN A 174       44.53    -79.33                                   
REMARK 500    ALA A 175      -39.28   -147.80                                   
REMARK 500    ALA A 220      -33.92   -133.23                                   
REMARK 500    ASN A 238       23.05    -75.58                                   
REMARK 500    LEU A 252      -82.15    -98.63                                   
REMARK 500    ARG A 261      -48.45   -151.72                                   
REMARK 500    LEU A 268      -86.45    -77.59                                   
REMARK 500    VAL A 279      -62.06   -139.61                                   
REMARK 500    TRP A 282        0.52    -67.39                                   
REMARK 500    ALA A 283      -34.72   -136.54                                   
REMARK 500    VAL A 292     -101.01   -135.88                                   
REMARK 500    ASN A 300      -73.42     63.48                                   
REMARK 500    ILE A 306      -79.42    -66.54                                   
REMARK 500    HIS A 340      -19.24    -49.87                                   
REMARK 500    VAL A 368      -41.22   -147.62                                   
REMARK 500    ALA A 373      -85.44     48.21                                   
REMARK 500    PHE A 391       21.77    -73.91                                   
REMARK 500    CYS A 401      -70.08    -95.38                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 1200                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: GPCR-49   RELATED DB: TARGETTRACK                        
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 GLY430-PRO432 ARE CLONING-SITE RESIDUES AND LEU433-GLN438 ARE        
REMARK 999 PRECISION CLEAVAGE-SITE RESIDUES.                                    
DBREF  4L6R A 1001  1106  UNP    P0ABE7   C562_ECOLX      23    128             
DBREF  4L6R A  123   432  UNP    P47871   GLR_HUMAN      123    432             
SEQADV 4L6R TRP A 1007  UNP  P0ABE7    MET    29 ENGINEERED MUTATION            
SEQADV 4L6R ILE A 1102  UNP  P0ABE7    HIS   124 ENGINEERED MUTATION            
SEQADV 4L6R LEU A 1106  UNP  P0ABE7    ARG   128 ENGINEERED MUTATION            
SEQADV 4L6R GLY A  433  UNP  P47871              SEE REMARK 999                 
SEQADV 4L6R ARG A  434  UNP  P47871              SEE REMARK 999                 
SEQADV 4L6R PRO A  435  UNP  P47871              SEE REMARK 999                 
SEQADV 4L6R LEU A  436  UNP  P47871              SEE REMARK 999                 
SEQADV 4L6R GLU A  437  UNP  P47871              SEE REMARK 999                 
SEQADV 4L6R VAL A  438  UNP  P47871              SEE REMARK 999                 
SEQADV 4L6R LEU A  439  UNP  P47871              SEE REMARK 999                 
SEQADV 4L6R PHE A  440  UNP  P47871              SEE REMARK 999                 
SEQADV 4L6R GLN A  441  UNP  P47871              SEE REMARK 999                 
SEQRES   1 A  425  ALA ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN          
SEQRES   2 A  425  LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL          
SEQRES   3 A  425  LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP          
SEQRES   4 A  425  ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER          
SEQRES   5 A  425  PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE          
SEQRES   6 A  425  ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU          
SEQRES   7 A  425  ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA          
SEQRES   8 A  425  GLU GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS          
SEQRES   9 A  425  TYR LEU MET ASP GLY GLU GLU ILE GLU VAL GLN LYS GLU          
SEQRES  10 A  425  VAL ALA LYS MET TYR SER SER PHE GLN VAL MET TYR THR          
SEQRES  11 A  425  VAL GLY TYR SER LEU SER LEU GLY ALA LEU LEU LEU ALA          
SEQRES  12 A  425  LEU ALA ILE LEU GLY GLY LEU SER LYS LEU HIS CYS THR          
SEQRES  13 A  425  ARG ASN ALA ILE HIS ALA ASN LEU PHE ALA SER PHE VAL          
SEQRES  14 A  425  LEU LYS ALA SER SER VAL LEU VAL ILE ASP GLY LEU LEU          
SEQRES  15 A  425  ARG THR ARG TYR SER GLN LYS ILE GLY ASP ASP LEU SER          
SEQRES  16 A  425  VAL SER THR TRP LEU SER ASP GLY ALA VAL ALA GLY CYS          
SEQRES  17 A  425  ARG VAL ALA ALA VAL PHE MET GLN TYR GLY ILE VAL ALA          
SEQRES  18 A  425  ASN TYR CYS TRP LEU LEU VAL GLU GLY LEU TYR LEU HIS          
SEQRES  19 A  425  ASN LEU LEU GLY LEU ALA THR LEU PRO GLU ARG SER PHE          
SEQRES  20 A  425  PHE SER LEU TYR LEU GLY ILE GLY TRP GLY ALA PRO MET          
SEQRES  21 A  425  LEU PHE VAL VAL PRO TRP ALA VAL VAL LYS CYS LEU PHE          
SEQRES  22 A  425  GLU ASN VAL GLN CYS TRP THR SER ASN ASP ASN MET GLY          
SEQRES  23 A  425  PHE TRP TRP ILE LEU ARG PHE PRO VAL PHE LEU ALA ILE          
SEQRES  24 A  425  LEU ILE ASN PHE PHE ILE PHE VAL ARG ILE VAL GLN LEU          
SEQRES  25 A  425  LEU VAL ALA LYS LEU ARG ALA ARG GLN MET HIS HIS THR          
SEQRES  26 A  425  ASP TYR LYS PHE ARG LEU ALA LYS SER THR LEU THR LEU          
SEQRES  27 A  425  ILE PRO LEU LEU GLY VAL HIS GLU VAL VAL PHE ALA PHE          
SEQRES  28 A  425  VAL THR ASP GLU HIS ALA GLN GLY THR LEU ARG SER ALA          
SEQRES  29 A  425  LYS LEU PHE PHE ASP LEU PHE LEU SER SER PHE GLN GLY          
SEQRES  30 A  425  LEU LEU VAL ALA VAL LEU TYR CYS PHE LEU ASN LYS GLU          
SEQRES  31 A  425  VAL GLN SER GLU LEU ARG ARG ARG TRP HIS ARG TRP ARG          
SEQRES  32 A  425  LEU GLY LYS VAL LEU TRP GLU GLU ARG ASN THR SER ASN          
SEQRES  33 A  425  GLY ARG PRO LEU GLU VAL LEU PHE GLN                          
HET    PEG  A1200       7                                                       
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
FORMUL   2  PEG    C4 H10 O3                                                    
HELIX    1   1 ASP A 1002  ALA A 1020  1                                  19    
HELIX    2   2 ASN A 1022  GLN A 1041  1                                  20    
HELIX    3   3 PRO A 1045  GLU A 1049  5                                   5    
HELIX    4   4 SER A 1055  GLU A 1081  1                                  27    
HELIX    5   5 LYS A 1083  GLU A 1092  1                                  10    
HELIX    6   6 GLN A 1093  ILE A 1102  1                                  10    
HELIX    7   7 GLN A 1103  LEU A 1106  5                                   4    
HELIX    8   8 GLU A  126  GLY A  164  1                                  39    
HELIX    9   9 THR A  172  HIS A  177  1                                   6    
HELIX   10  10 ASN A  179  LEU A  198  1                                  20    
HELIX   11  11 SER A  217  ALA A  222  1                                   6    
HELIX   12  12 VAL A  226  TYR A  248  1                                  23    
HELIX   13  13 SER A  262  TYR A  267  5                                   6    
HELIX   14  14 ILE A  270  TRP A  272  5                                   3    
HELIX   15  15 GLY A  273  PHE A  278  1                                   6    
HELIX   16  16 VAL A  280  GLU A  290  1                                  11    
HELIX   17  17 ASN A  300  LEU A  307  1                                   8    
HELIX   18  18 LEU A  307  VAL A  330  1                                  24    
HELIX   19  19 VAL A  330  ALA A  335  1                                   6    
HELIX   20  20 ASP A  342  LEU A  352  1                                  11    
HELIX   21  21 PRO A  356  GLU A  362  1                                   7    
HELIX   22  22 GLN A  374  PHE A  391  1                                  18    
HELIX   23  23 PHE A  391  CYS A  401  1                                  11    
HELIX   24  24 ASN A  404  ASN A  429  1                                  26    
SSBOND   1 CYS A  224    CYS A  294                          1555   1555  2.04  
SITE     1 AC1  4 ARG A 346  SER A 350  LEU A 399  LEU A 403                    
CRYST1   56.615   66.651  163.331  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      0.017663  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015004  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006123        0.00000                         
ATOM      1  N   ALA A1001      13.645  14.436 -11.317  1.00109.57           N  
ANISOU    1  N   ALA A1001    16791  15721   9120  -3009  -1596   4616       N  
ATOM      2  CA  ALA A1001      12.442  15.173 -10.944  1.00112.26           C  
ANISOU    2  CA  ALA A1001    17470  15475   9710  -2347  -1863   4642       C  
ATOM      3  C   ALA A1001      11.253  14.220 -10.760  1.00112.77           C  
ANISOU    3  C   ALA A1001    17195  16177   9476  -1818  -1683   4100       C  
ATOM      4  O   ALA A1001      10.802  14.044  -9.624  1.00110.88           O  
ANISOU    4  O   ALA A1001    17057  15643   9429  -1466  -1658   3512       O  
ATOM      5  CB  ALA A1001      12.122  16.223 -11.992  1.00121.36           C  
ANISOU    5  CB  ALA A1001    18805  16456  10850  -2320  -2162   5565       C  
ATOM      6  N   ASP A1002      10.761  13.586 -11.872  1.00108.91           N  
ANISOU    6  N   ASP A1002    16270  16656   8455  -1849  -1556   4283       N  
ATOM      7  CA  ASP A1002       9.644  12.611 -11.897  1.00105.21           C  
ANISOU    7  CA  ASP A1002    15404  16919   7652  -1531  -1404   3818       C  
ATOM      8  C   ASP A1002       9.969  11.431 -10.986  1.00100.38           C  
ANISOU    8  C   ASP A1002    14688  16356   7097  -1711  -1137   3087       C  
ATOM      9  O   ASP A1002      11.114  11.002 -11.004  1.00 98.40           O  
ANISOU    9  O   ASP A1002    14424  16074   6890  -2140  -1005   3000       O  
ATOM     10  CB  ASP A1002       9.390  12.128 -13.349  1.00109.52           C  
ANISOU   10  CB  ASP A1002    15518  18523   7573  -1749  -1339   4103       C  
ATOM     11  CG  ASP A1002       8.988  13.182 -14.366  1.00132.37           C  
ANISOU   11  CG  ASP A1002    18456  21566  10272  -1601  -1654   4978       C  
ATOM     12  OD1 ASP A1002       8.992  12.866 -15.581  1.00137.42           O  
ANISOU   12  OD1 ASP A1002    18757  23165  10289  -1899  -1609   5278       O  
ATOM     13  OD2 ASP A1002       8.692  14.328 -13.955  1.00143.84           O  
ANISOU   13  OD2 ASP A1002    20297  22167  12187  -1185  -1973   5364       O  
ATOM     14  N   LEU A1003       9.024  10.934 -10.161  1.00 92.07           N  
ANISOU   14  N   LEU A1003    13540  15391   6052  -1401  -1075   2621       N  
ATOM     15  CA  LEU A1003       9.284   9.853  -9.180  1.00 85.70           C  
ANISOU   15  CA  LEU A1003    12707  14541   5312  -1606   -889   2081       C  
ATOM     16  C   LEU A1003       9.676   8.507  -9.850  1.00 85.52           C  
ANISOU   16  C   LEU A1003    12386  15033   5076  -2017   -699   1854       C  
ATOM     17  O   LEU A1003      10.581   7.818  -9.372  1.00 82.39           O  
ANISOU   17  O   LEU A1003    12053  14382   4867  -2260   -623   1621       O  
ATOM     18  CB  LEU A1003       8.013   9.648  -8.329  1.00 85.58           C  
ANISOU   18  CB  LEU A1003    12568  14731   5217  -1270   -850   1760       C  
ATOM     19  CG  LEU A1003       8.021   8.613  -7.197  1.00 86.58           C  
ANISOU   19  CG  LEU A1003    12689  14867   5341  -1501   -701   1354       C  
ATOM     20  CD1 LEU A1003       9.031   8.958  -6.135  1.00 85.63           C  
ANISOU   20  CD1 LEU A1003    12953  14095   5487  -1574   -769   1279       C  
ATOM     21  CD2 LEU A1003       6.648   8.487  -6.586  1.00 91.14           C  
ANISOU   21  CD2 LEU A1003    13007  15923   5698  -1255   -620   1135       C  
ATOM     22  N   GLU A1004       8.997   8.145 -10.938  1.00 83.10           N  
ANISOU   22  N   GLU A1004    11747  15435   4392  -2053   -663   1875       N  
ATOM     23  CA  GLU A1004       9.257   6.896 -11.634  1.00 81.91           C  
ANISOU   23  CA  GLU A1004    11331  15754   4037  -2401   -503   1502       C  
ATOM     24  C   GLU A1004      10.668   6.866 -12.181  1.00 85.20           C  
ANISOU   24  C   GLU A1004    11747  16137   4489  -2638   -407   1538       C  
ATOM     25  O   GLU A1004      11.259   5.794 -12.246  1.00 84.65           O  
ANISOU   25  O   GLU A1004    11559  16099   4504  -2815   -272   1075       O  
ATOM     26  CB  GLU A1004       8.252   6.657 -12.774  1.00 86.88           C  
ANISOU   26  CB  GLU A1004    11584  17268   4159  -2434   -525   1481       C  
ATOM     27  CG  GLU A1004       8.161   7.705 -13.878  1.00 98.55           C  
ANISOU   27  CG  GLU A1004    12962  19218   5265  -2322   -662   2070       C  
ATOM     28  CD  GLU A1004       7.415   8.997 -13.606  1.00112.59           C  
ANISOU   28  CD  GLU A1004    14874  20750   7157  -1841   -918   2627       C  
ATOM     29  OE1 GLU A1004       6.978   9.222 -12.454  1.00106.18           O  
ANISOU   29  OE1 GLU A1004    14225  19412   6707  -1532   -949   2475       O  
ATOM     30  OE2 GLU A1004       7.239   9.776 -14.568  1.00103.67           O  
ANISOU   30  OE2 GLU A1004    13668  19996   5727  -1746  -1105   3211       O  
ATOM     31  N   ASP A1005      11.199   8.034 -12.592  1.00 82.53           N  
ANISOU   31  N   ASP A1005    11511  15741   4106  -2647   -488   2092       N  
ATOM     32  CA  ASP A1005      12.550   8.161 -13.123  1.00 83.57           C  
ANISOU   32  CA  ASP A1005    11544  16005   4204  -2957   -374   2221       C  
ATOM     33  C   ASP A1005      13.555   7.881 -12.049  1.00 83.99           C  
ANISOU   33  C   ASP A1005    11737  15427   4749  -3008   -359   1975       C  
ATOM     34  O   ASP A1005      14.450   7.080 -12.279  1.00 83.74           O  
ANISOU   34  O   ASP A1005    11444  15630   4746  -3145   -196   1618       O  
ATOM     35  CB  ASP A1005      12.785   9.545 -13.722  1.00 90.33           C  
ANISOU   35  CB  ASP A1005    12523  16876   4922  -3077   -518   3019       C  
ATOM     36  CG  ASP A1005      12.121   9.775 -15.076  1.00108.70           C  
ANISOU   36  CG  ASP A1005    14606  20080   6613  -3126   -548   3405       C  
ATOM     37  OD1 ASP A1005      11.803   8.771 -15.766  1.00110.16           O  
ANISOU   37  OD1 ASP A1005    14427  21068   6362  -3192   -378   2922       O  
ATOM     38  OD2 ASP A1005      12.022  10.950 -15.495  1.00119.21           O  
ANISOU   38  OD2 ASP A1005    16118  21306   7871  -3151   -769   4204       O  
ATOM     39  N   ASN A1006      13.401   8.509 -10.860  1.00 78.51           N  
ANISOU   39  N   ASN A1006    11418  13989   4423  -2851   -545   2103       N  
ATOM     40  CA  ASN A1006      14.264   8.269  -9.696  1.00 74.70           C  
ANISOU   40  CA  ASN A1006    11075  12969   4338  -2904   -604   1891       C  
ATOM     41  C   ASN A1006      14.084   6.851  -9.195  1.00 74.37           C  
ANISOU   41  C   ASN A1006    10931  12940   4386  -2818   -532   1391       C  
ATOM     42  O   ASN A1006      15.033   6.230  -8.729  1.00 72.51           O  
ANISOU   42  O   ASN A1006    10618  12525   4405  -2875   -550   1197       O  
ATOM     43  CB  ASN A1006      13.961   9.255  -8.590  1.00 71.42           C  
ANISOU   43  CB  ASN A1006    11083  11893   4161  -2757   -823   2035       C  
ATOM     44  CG  ASN A1006      14.158  10.707  -8.951  1.00 90.60           C  
ANISOU   44  CG  ASN A1006    13746  14004   6674  -2845   -988   2535       C  
ATOM     45  OD1 ASN A1006      15.084  11.097  -9.672  1.00 91.08           O  
ANISOU   45  OD1 ASN A1006    13685  14212   6710  -3220   -972   2879       O  
ATOM     46  ND2 ASN A1006      13.213  11.533  -8.527  1.00 77.73           N  
ANISOU   46  ND2 ASN A1006    12433  11963   5139  -2493  -1153   2604       N  
ATOM     47  N   TRP A1007      12.871   6.328  -9.318  1.00 71.52           N  
ANISOU   47  N   TRP A1007    10546  12790   3840  -2703   -487   1225       N  
ATOM     48  CA  TRP A1007      12.578   4.972  -8.909  1.00 71.28           C  
ANISOU   48  CA  TRP A1007    10473  12689   3922  -2738   -457    832       C  
ATOM     49  C   TRP A1007      13.318   3.970  -9.815  1.00 77.72           C  
ANISOU   49  C   TRP A1007    11006  13742   4781  -2826   -334    450       C  
ATOM     50  O   TRP A1007      13.744   2.911  -9.340  1.00 78.38           O  
ANISOU   50  O   TRP A1007    11115  13465   5200  -2810   -385    155       O  
ATOM     51  CB  TRP A1007      11.072   4.743  -8.948  1.00 71.00           C  
ANISOU   51  CB  TRP A1007    10397  12942   3637  -2716   -436    770       C  
ATOM     52  CG  TRP A1007      10.654   3.466  -8.288  1.00 72.39           C  
ANISOU   52  CG  TRP A1007    10617  12926   3963  -2888   -453    505       C  
ATOM     53  CD1 TRP A1007      10.467   2.255  -8.888  1.00 77.63           C  
ANISOU   53  CD1 TRP A1007    11147  13678   4669  -3095   -416    131       C  
ATOM     54  CD2 TRP A1007      10.380   3.264  -6.898  1.00 71.57           C  
ANISOU   54  CD2 TRP A1007    10731  12488   3974  -2936   -539    620       C  
ATOM     55  NE1 TRP A1007      10.086   1.316  -7.962  1.00 77.98           N  
ANISOU   55  NE1 TRP A1007    11356  13343   4930  -3306   -505     97       N  
ATOM     56  CE2 TRP A1007      10.020   1.907  -6.731  1.00 77.83           C  
ANISOU   56  CE2 TRP A1007    11527  13148   4898  -3230   -566    443       C  
ATOM     57  CE3 TRP A1007      10.387   4.102  -5.772  1.00 72.12           C  
ANISOU   57  CE3 TRP A1007    11002  12391   4009  -2796   -605    833       C  
ATOM     58  CZ2 TRP A1007       9.709   1.358  -5.483  1.00 78.31           C  
ANISOU   58  CZ2 TRP A1007    11775  12959   5020  -3439   -657    627       C  
ATOM     59  CZ3 TRP A1007      10.078   3.552  -4.532  1.00 74.15           C  
ANISOU   59  CZ3 TRP A1007    11399  12533   4242  -2959   -660    896       C  
ATOM     60  CH2 TRP A1007       9.748   2.196  -4.398  1.00 76.62           C  
ANISOU   60  CH2 TRP A1007    11699  12766   4648  -3302   -685    870       C  
ATOM     61  N   GLU A1008      13.488   4.319 -11.108  1.00 75.36           N  
ANISOU   61  N   GLU A1008    10437  14066   4132  -2891   -190    454       N  
ATOM     62  CA  GLU A1008      14.199   3.481 -12.048  1.00 78.21           C  
ANISOU   62  CA  GLU A1008    10459  14835   4423  -2931    -19    -33       C  
ATOM     63  C   GLU A1008      15.685   3.547 -11.771  1.00 83.23           C  
ANISOU   63  C   GLU A1008    10944  15319   5361  -2880      7    -39       C  
ATOM     64  O   GLU A1008      16.357   2.525 -11.840  1.00 85.49           O  
ANISOU   64  O   GLU A1008    11031  15534   5919  -2727     57   -563       O  
ATOM     65  CB  GLU A1008      13.889   3.906 -13.458  1.00 83.46           C  
ANISOU   65  CB  GLU A1008    10841  16410   4459  -3070    132     22       C  
ATOM     66  CG  GLU A1008      14.324   2.880 -14.475  1.00 99.93           C  
ANISOU   66  CG  GLU A1008    12554  19074   6341  -3096    341   -709       C  
ATOM     67  CD  GLU A1008      13.704   3.071 -15.836  1.00127.66           C  
ANISOU   67  CD  GLU A1008    15795  23626   9085  -3284    453   -758       C  
ATOM     68  OE1 GLU A1008      13.487   4.233 -16.255  1.00120.21           O  
ANISOU   68  OE1 GLU A1008    14840  23113   7721  -3406    413    -34       O  
ATOM     69  OE2 GLU A1008      13.420   2.041 -16.485  1.00134.40           O  
ANISOU   69  OE2 GLU A1008    16467  24839   9759  -3319    538  -1525       O  
ATOM     70  N   THR A1009      16.197   4.741 -11.413  1.00 79.25           N  
ANISOU   70  N   THR A1009    10525  14719   4867  -2995    -65    516       N  
ATOM     71  CA  THR A1009      17.598   4.952 -11.040  1.00 80.41           C  
ANISOU   71  CA  THR A1009    10475  14790   5287  -3047    -88    586       C  
ATOM     72  C   THR A1009      17.952   4.047  -9.887  1.00 82.19           C  
ANISOU   72  C   THR A1009    10811  14386   6031  -2806   -281    319       C  
ATOM     73  O   THR A1009      19.000   3.410  -9.912  1.00 84.96           O  
ANISOU   73  O   THR A1009    10810  14830   6642  -2651   -263     16       O  
ATOM     74  CB  THR A1009      17.857   6.429 -10.678  1.00 88.83           C  
ANISOU   74  CB  THR A1009    11752  15662   6338  -3316   -225   1234       C  
ATOM     75  OG1 THR A1009      17.448   7.266 -11.759  1.00 89.42           O  
ANISOU   75  OG1 THR A1009    11791  16222   5962  -3534   -119   1635       O  
ATOM     76  CG2 THR A1009      19.336   6.710 -10.317  1.00 92.11           C  
ANISOU   76  CG2 THR A1009    11885  16114   7000  -3511   -275   1322       C  
ATOM     77  N   LEU A1010      17.073   3.980  -8.879  1.00 75.11           N  
ANISOU   77  N   LEU A1010    10357  12924   5256  -2756   -475    456       N  
ATOM     78  CA  LEU A1010      17.306   3.155  -7.707  1.00 74.60           C  
ANISOU   78  CA  LEU A1010    10457  12295   5592  -2607   -710    377       C  
ATOM     79  C   LEU A1010      17.379   1.677  -8.089  1.00 81.81           C  
ANISOU   79  C   LEU A1010    11225  13077   6783  -2393   -688   -117       C  
ATOM     80  O   LEU A1010      18.297   0.988  -7.648  1.00 84.43           O  
ANISOU   80  O   LEU A1010    11425  13117   7538  -2161   -855   -245       O  
ATOM     81  CB  LEU A1010      16.219   3.380  -6.652  1.00 71.53           C  
ANISOU   81  CB  LEU A1010    10516  11553   5111  -2676   -854    628       C  
ATOM     82  CG  LEU A1010      16.199   4.761  -6.010  1.00 74.48           C  
ANISOU   82  CG  LEU A1010    11107  11857   5333  -2780   -947    962       C  
ATOM     83  CD1 LEU A1010      15.056   4.880  -5.069  1.00 72.92           C  
ANISOU   83  CD1 LEU A1010    11240  11499   4966  -2765  -1011   1040       C  
ATOM     84  CD2 LEU A1010      17.488   5.043  -5.275  1.00 77.22           C  
ANISOU   84  CD2 LEU A1010    11390  12041   5909  -2840  -1161   1067       C  
ATOM     85  N   ASN A1011      16.458   1.201  -8.937  1.00 79.35           N  
ANISOU   85  N   ASN A1011    10919  12966   6266  -2451   -523   -428       N  
ATOM     86  CA  ASN A1011      16.453  -0.201  -9.354  1.00 83.97           C  
ANISOU   86  CA  ASN A1011    11438  13304   7161  -2292   -531  -1018       C  
ATOM     87  C   ASN A1011      17.673  -0.570 -10.185  1.00 95.33           C  
ANISOU   87  C   ASN A1011    12390  15086   8747  -1989   -383  -1546       C  
ATOM     88  O   ASN A1011      18.310  -1.576  -9.874  1.00 99.52           O  
ANISOU   88  O   ASN A1011    12873  15097   9842  -1643   -551  -1883       O  
ATOM     89  CB  ASN A1011      15.216  -0.547 -10.145  1.00 85.11           C  
ANISOU   89  CB  ASN A1011    11645  13706   6986  -2514   -403  -1313       C  
ATOM     90  CG  ASN A1011      14.014  -0.968  -9.351  1.00100.41           C  
ANISOU   90  CG  ASN A1011    13964  15197   8991  -2770   -573  -1088       C  
ATOM     91  OD1 ASN A1011      13.713  -0.469  -8.268  1.00 79.30           O  
ANISOU   91  OD1 ASN A1011    11523  12313   6293  -2856   -695   -554       O  
ATOM     92  ND2 ASN A1011      13.157  -1.680 -10.025  1.00102.71           N  
ANISOU   92  ND2 ASN A1011    14247  15594   9183  -2980   -528  -1505       N  
ATOM     93  N   ASP A1012      18.002   0.214 -11.230  1.00 94.13           N  
ANISOU   93  N   ASP A1012    11846  15831   8087  -2098    -83  -1600       N  
ATOM     94  CA  ASP A1012      19.148  -0.101 -12.078  1.00101.00           C  
ANISOU   94  CA  ASP A1012    12124  17297   8955  -1848    141  -2150       C  
ATOM     95  C   ASP A1012      20.441  -0.074 -11.285  1.00106.56           C  
ANISOU   95  C   ASP A1012    12573  17781  10134  -1581    -22  -1994       C  
ATOM     96  O   ASP A1012      21.291  -0.933 -11.494  1.00113.08           O  
ANISOU   96  O   ASP A1012    13004  18624  11338  -1121     -6  -2592       O  
ATOM     97  CB  ASP A1012      19.251   0.862 -13.264  1.00105.40           C  
ANISOU   97  CB  ASP A1012    12299  19000   8747  -2164    489  -2025       C  
ATOM     98  CG  ASP A1012      18.140   0.727 -14.303  1.00123.47           C  
ANISOU   98  CG  ASP A1012    14654  21800  10460  -2368    648  -2297       C  
ATOM     99  OD1 ASP A1012      17.547  -0.380 -14.411  1.00127.02           O  
ANISOU   99  OD1 ASP A1012    15266  21871  11125  -2220    581  -2942       O  
ATOM    100  OD2 ASP A1012      17.911   1.703 -15.056  1.00129.98           O  
ANISOU  100  OD2 ASP A1012    15345  23427  10615  -2703    808  -1865       O  
ATOM    101  N   ASN A1013      20.589   0.870 -10.354  1.00 97.99           N  
ANISOU  101  N   ASN A1013    11688  16487   9056  -1823   -214  -1264       N  
ATOM    102  CA  ASN A1013      21.835   0.957  -9.601  1.00 99.59           C  
ANISOU  102  CA  ASN A1013    11583  16620   9636  -1649   -416  -1103       C  
ATOM    103  C   ASN A1013      21.923  -0.161  -8.562  1.00105.08           C  
ANISOU  103  C   ASN A1013    12526  16414  10987  -1219   -816  -1187       C  
ATOM    104  O   ASN A1013      23.035  -0.556  -8.220  1.00109.04           O  
ANISOU  104  O   ASN A1013    12613  16919  11899   -840   -994  -1304       O  
ATOM    105  CB  ASN A1013      22.002   2.309  -8.956  1.00 94.54           C  
ANISOU  105  CB  ASN A1013    11092  16042   8788  -2104   -535   -399       C  
ATOM    106  CG  ASN A1013      22.373   3.380  -9.957  1.00111.39           C  
ANISOU  106  CG  ASN A1013    12860  19038  10426  -2529   -220   -208       C  
ATOM    107  OD1 ASN A1013      21.823   4.468  -9.922  1.00102.51           O  
ANISOU  107  OD1 ASN A1013    12090  17844   9014  -2945   -236    301       O  
ATOM    108  ND2 ASN A1013      23.179   3.047 -10.966  1.00105.33           N  
ANISOU  108  ND2 ASN A1013    11394  19116   9510  -2421     90   -631       N  
ATOM    109  N   LEU A1014      20.785  -0.731  -8.128  1.00100.33           N  
ANISOU  109  N   LEU A1014    12528  15106  10486  -1276   -970  -1113       N  
ATOM    110  CA  LEU A1014      20.836  -1.915  -7.270  1.00104.26           C  
ANISOU  110  CA  LEU A1014    13294  14708  11611   -936  -1368  -1117       C  
ATOM    111  C   LEU A1014      21.465  -3.038  -8.039  1.00116.81           C  
ANISOU  111  C   LEU A1014    14515  16178  13687   -363  -1326  -1900       C  
ATOM    112  O   LEU A1014      22.282  -3.787  -7.504  1.00122.21           O  
ANISOU  112  O   LEU A1014    15058  16377  14998    155  -1663  -1952       O  
ATOM    113  CB  LEU A1014      19.450  -2.319  -6.755  1.00101.64           C  
ANISOU  113  CB  LEU A1014    13628  13759  11232  -1257  -1495   -857       C  
ATOM    114  CG  LEU A1014      18.888  -1.554  -5.567  1.00101.47           C  
ANISOU  114  CG  LEU A1014    13999  13663  10893  -1646  -1661   -125       C  
ATOM    115  CD1 LEU A1014      17.433  -1.904  -5.344  1.00 99.66           C  
ANISOU  115  CD1 LEU A1014    14236  13150  10481  -2008  -1643     16       C  
ATOM    116  CD2 LEU A1014      19.699  -1.823  -4.310  1.00106.82           C  
ANISOU  116  CD2 LEU A1014    14727  13956  11901  -1463  -2111    316       C  
ATOM    117  N   LYS A1015      21.120  -3.111  -9.334  1.00115.26           N  
ANISOU  117  N   LYS A1015    14117  16508  13169   -412   -922  -2550       N  
ATOM    118  CA  LYS A1015      21.644  -4.112 -10.253  1.00123.89           C  
ANISOU  118  CA  LYS A1015    14822  17650  14603    137   -789  -3537       C  
ATOM    119  C   LYS A1015      23.132  -3.911 -10.444  1.00132.38           C  
ANISOU  119  C   LYS A1015    15086  19415  15798    609   -689  -3773       C  
ATOM    120  O   LYS A1015      23.879  -4.881 -10.427  1.00139.56           O  
ANISOU  120  O   LYS A1015    15709  19942  17374   1332   -861  -4338       O  
ATOM    121  CB  LYS A1015      20.913  -4.062 -11.609  1.00127.73           C  
ANISOU  121  CB  LYS A1015    15223  18825  14483   -138   -356  -4171       C  
ATOM    122  CG  LYS A1015      19.381  -4.232 -11.540  1.00144.41           C  
ANISOU  122  CG  LYS A1015    17997  20465  16405   -657   -440  -3989       C  
ATOM    123  CD  LYS A1015      18.929  -5.536 -10.864  1.00162.39           C  
ANISOU  123  CD  LYS A1015    20829  21395  19479   -516   -860  -4129       C  
ATOM    124  CE  LYS A1015      17.432  -5.584 -10.697  1.00171.48           C  
ANISOU  124  CE  LYS A1015    22517  22270  20368  -1167   -925  -3823       C  
ATOM    125  NZ  LYS A1015      16.993  -6.818  -9.999  1.00185.35           N  
ANISOU  125  NZ  LYS A1015    24827  22718  22878  -1207  -1349  -3804       N  
ATOM    126  N   VAL A1016      23.565  -2.650 -10.587  1.00125.86           N  
ANISOU  126  N   VAL A1016    13875  19566  14378    198   -449  -3315       N  
ATOM    127  CA  VAL A1016      24.979  -2.297 -10.729  1.00131.28           C  
ANISOU  127  CA  VAL A1016    13695  21105  15080    448   -335  -3414       C  
ATOM    128  C   VAL A1016      25.747  -2.827  -9.529  1.00138.00           C  
ANISOU  128  C   VAL A1016    14490  21250  16694    964   -871  -3156       C  
ATOM    129  O   VAL A1016      26.786  -3.468  -9.695  1.00146.43           O  
ANISOU  129  O   VAL A1016    14879  22543  18215   1672   -915  -3697       O  
ATOM    130  CB  VAL A1016      25.179  -0.768 -10.889  1.00131.13           C  
ANISOU  130  CB  VAL A1016    13458  22015  14352   -305    -99  -2740       C  
ATOM    131  CG1 VAL A1016      26.664  -0.397 -10.882  1.00137.14           C  
ANISOU  131  CG1 VAL A1016    13286  23663  15158   -198    -38  -2737       C  
ATOM    132  CG2 VAL A1016      24.503  -0.256 -12.156  1.00129.96           C  
ANISOU  132  CG2 VAL A1016    13300  22660  13421   -766    382  -2894       C  
ATOM    133  N   ILE A1017      25.223  -2.566  -8.322  1.00127.69           N  
ANISOU  133  N   ILE A1017    13854  19173  15488    646  -1289  -2342       N  
ATOM    134  CA  ILE A1017      25.833  -2.997  -7.066  1.00129.65           C  
ANISOU  134  CA  ILE A1017    14139  18804  16317   1018  -1876  -1908       C  
ATOM    135  C   ILE A1017      25.906  -4.519  -7.003  1.00141.51           C  
ANISOU  135  C   ILE A1017    15764  19348  18655   1832  -2192  -2375       C  
ATOM    136  O   ILE A1017      26.965  -5.066  -6.690  1.00149.67           O  
ANISOU  136  O   ILE A1017    16279  20322  20268   2544  -2509  -2507       O  
ATOM    137  CB  ILE A1017      25.044  -2.441  -5.873  1.00124.72           C  
ANISOU  137  CB  ILE A1017    14276  17660  15451    432  -2191  -1025       C  
ATOM    138  CG1 ILE A1017      25.160  -0.902  -5.831  1.00119.24           C  
ANISOU  138  CG1 ILE A1017    13452  17756  14098   -265  -1982   -623       C  
ATOM    139  CG2 ILE A1017      25.559  -3.067  -4.573  1.00129.55           C  
ANISOU  139  CG2 ILE A1017    14995  17640  16587    805  -2851   -539       C  
ATOM    140  CD1 ILE A1017      24.182  -0.226  -4.941  1.00117.05           C  
ANISOU  140  CD1 ILE A1017    13919  17094  13462   -826  -2131    -19       C  
ATOM    141  N   GLU A1018      24.787  -5.193  -7.294  1.00136.41           N  
ANISOU  141  N   GLU A1018    15789  17928  18112   1723  -2150  -2615       N  
ATOM    142  CA  GLU A1018      24.697  -6.650  -7.286  1.00144.58           C  
ANISOU  142  CA  GLU A1018    17112  17814  20007   2367  -2483  -3069       C  
ATOM    143  C   GLU A1018      25.755  -7.294  -8.187  1.00158.77           C  
ANISOU  143  C   GLU A1018    18110  19942  22275   3295  -2326  -4145       C  
ATOM    144  O   GLU A1018      26.344  -8.307  -7.805  1.00167.93           O  
ANISOU  144  O   GLU A1018    19213  20249  24343   4130  -2791  -4333       O  
ATOM    145  CB  GLU A1018      23.303  -7.101  -7.744  1.00143.60           C  
ANISOU  145  CB  GLU A1018    17709  17084  19767   1899  -2336  -3322       C  
ATOM    146  CG  GLU A1018      22.173  -6.806  -6.764  1.00148.02           C  
ANISOU  146  CG  GLU A1018    19053  17156  20033   1125  -2554  -2348       C  
ATOM    147  CD  GLU A1018      20.768  -7.152  -7.228  1.00168.06           C  
ANISOU  147  CD  GLU A1018    22157  19326  22371    563  -2386  -2562       C  
ATOM    148  OE1 GLU A1018      19.813  -6.799  -6.500  1.00156.50           O  
ANISOU  148  OE1 GLU A1018    21185  17733  20545    -90  -2469  -1820       O  
ATOM    149  OE2 GLU A1018      20.616  -7.725  -8.333  1.00167.25           O  
ANISOU  149  OE2 GLU A1018    21939  19210  22399    751  -2152  -3522       O  
ATOM    150  N   LYS A1019      26.007  -6.705  -9.369  1.00154.64           N  
ANISOU  150  N   LYS A1019    16941  20696  21119   3179  -1687  -4829       N  
ATOM    151  CA  LYS A1019      26.950  -7.280 -10.323  1.00165.42           C  
ANISOU  151  CA  LYS A1019    17450  22641  22761   4029  -1419  -5997       C  
ATOM    152  C   LYS A1019      28.371  -6.634 -10.234  1.00172.78           C  
ANISOU  152  C   LYS A1019    17271  24822  23557   4330  -1315  -5886       C  
ATOM    153  O   LYS A1019      29.274  -7.062 -10.966  1.00182.47           O  
ANISOU  153  O   LYS A1019    17598  26755  24975   5094  -1063  -6857       O  
ATOM    154  CB  LYS A1019      26.415  -7.147 -11.760  1.00168.09           C  
ANISOU  154  CB  LYS A1019    17638  23842  22385   3718   -755  -6912       C  
ATOM    155  CG  LYS A1019      26.194  -5.738 -12.299  1.00173.56           C  
ANISOU  155  CG  LYS A1019    18077  25956  21913   2785   -234  -6436       C  
ATOM    156  CD  LYS A1019      25.645  -5.787 -13.734  1.00184.05           C  
ANISOU  156  CD  LYS A1019    19269  28129  22533   2553    331  -7338       C  
ATOM    157  CE  LYS A1019      25.339  -4.428 -14.325  1.00183.20           C  
ANISOU  157  CE  LYS A1019    18990  29332  21284   1626    776  -6743       C  
ATOM    158  NZ  LYS A1019      24.233  -3.736 -13.612  1.00175.82           N  
ANISOU  158  NZ  LYS A1019    18927  27723  20154    877    524  -5659       N  
ATOM    159  N   ALA A1020      28.581  -5.670  -9.315  1.00162.30           N  
ANISOU  159  N   ALA A1020    15963  23769  21932   3755  -1532  -4791       N  
ATOM    160  CA  ALA A1020      29.879  -4.998  -9.171  1.00165.70           C  
ANISOU  160  CA  ALA A1020    15351  25398  22210   3843  -1486  -4612       C  
ATOM    161  C   ALA A1020      30.983  -5.972  -8.749  1.00181.08           C  
ANISOU  161  C   ALA A1020    16642  27064  25094   5040  -1941  -4979       C  
ATOM    162  O   ALA A1020      30.723  -6.963  -8.062  1.00184.19           O  
ANISOU  162  O   ALA A1020    17640  26040  26305   5632  -2528  -4852       O  
ATOM    163  CB  ALA A1020      29.785  -3.870  -8.158  1.00157.50           C  
ANISOU  163  CB  ALA A1020    14627  24453  20764   2970  -1746  -3438       C  
ATOM    164  N   ASP A1021      32.219  -5.675  -9.172  1.00184.91           N  
ANISOU  164  N   ASP A1021    15850  28948  25459   5378  -1685  -5384       N  
ATOM    165  CA  ASP A1021      33.392  -6.483  -8.852  1.00197.40           C  
ANISOU  165  CA  ASP A1021    16551  30566  27886   6603  -2084  -5784       C  
ATOM    166  C   ASP A1021      34.349  -5.712  -7.948  1.00200.14           C  
ANISOU  166  C   ASP A1021    16207  31726  28113   6323  -2447  -4926       C  
ATOM    167  O   ASP A1021      35.269  -6.308  -7.386  1.00206.46           O  
ANISOU  167  O   ASP A1021    16631  32122  29694   6968  -2763  -4447       O  
ATOM    168  CB  ASP A1021      34.102  -6.911 -10.141  1.00203.38           C  
ANISOU  168  CB  ASP A1021    16927  31600  28749   6728  -1026  -5922       C  
ATOM    169  CG  ASP A1021      33.220  -7.725 -11.064  1.00209.73           C  
ANISOU  169  CG  ASP A1021    18884  31212  29593   6610   -360  -6020       C  
ATOM    170  OD1 ASP A1021      32.707  -8.778 -10.621  1.00211.96           O  
ANISOU  170  OD1 ASP A1021    20009  30005  30520   7100   -672  -5952       O  
ATOM    171  OD2 ASP A1021      33.077  -7.336 -12.238  1.00212.49           O  
ANISOU  171  OD2 ASP A1021    19361  32073  29302   5994    479  -6042       O  
ATOM    172  N   ASN A1022      34.132  -4.393  -7.795  1.00185.87           N  
ANISOU  172  N   ASN A1022    14549  30631  25441   5029  -2224  -4178       N  
ATOM    173  CA  ASN A1022      35.001  -3.568  -6.959  1.00185.89           C  
ANISOU  173  CA  ASN A1022    13942  31423  25265   4570  -2571  -3427       C  
ATOM    174  C   ASN A1022      34.206  -2.491  -6.205  1.00175.26           C  
ANISOU  174  C   ASN A1022    13597  29654  23339   3300  -2732  -2419       C  
ATOM    175  O   ASN A1022      33.084  -2.146  -6.583  1.00165.60           O  
ANISOU  175  O   ASN A1022    13286  27942  21692   2676  -2391  -2337       O  
ATOM    176  CB  ASN A1022      36.089  -2.914  -7.805  1.00194.85           C  
ANISOU  176  CB  ASN A1022    13627  34481  25925   4330  -2010  -3854       C  
ATOM    177  CG  ASN A1022      35.556  -2.043  -8.905  1.00211.18           C  
ANISOU  177  CG  ASN A1022    16399  36331  27507   3055  -1119  -3426       C  
ATOM    178  OD1 ASN A1022      34.968  -0.985  -8.662  1.00202.77           O  
ANISOU  178  OD1 ASN A1022    15464  36113  25466   2143  -1172  -3210       O  
ATOM    179  ND2 ASN A1022      35.797  -2.448 -10.143  1.00207.04           N  
ANISOU  179  ND2 ASN A1022    15576  36029  27061   3332   -406  -3949       N  
ATOM    180  N   ALA A1023      34.829  -1.937  -5.158  1.00171.31           N  
ANISOU  180  N   ALA A1023    12839  29449  22803   2948  -3259  -1727       N  
ATOM    181  CA  ALA A1023      34.232  -0.936  -4.279  1.00161.07           C  
ANISOU  181  CA  ALA A1023    12400  27783  21015   1864  -3507   -889       C  
ATOM    182  C   ALA A1023      33.888   0.362  -5.020  1.00157.64           C  
ANISOU  182  C   ALA A1023    12084  27992  19822    692  -2886   -817       C  
ATOM    183  O   ALA A1023      32.872   0.981  -4.695  1.00147.81           O  
ANISOU  183  O   ALA A1023    11884  26051  18225     -4  -2882   -396       O  
ATOM    184  CB  ALA A1023      35.176  -0.624  -3.132  1.00166.90           C  
ANISOU  184  CB  ALA A1023    12608  28978  21830   1752  -4188   -356       C  
ATOM    185  N   ALA A1024      34.712   0.775  -6.005  1.00159.56           N  
ANISOU  185  N   ALA A1024    11248  29573  19804    479  -2378  -1189       N  
ATOM    186  CA  ALA A1024      34.478   2.013  -6.761  1.00154.95           C  
ANISOU  186  CA  ALA A1024    10733  29629  18513   -683  -1837   -979       C  
ATOM    187  C   ALA A1024      33.152   1.957  -7.510  1.00148.47           C  
ANISOU  187  C   ALA A1024    10884  28119  17408   -791  -1400  -1117       C  
ATOM    188  O   ALA A1024      32.415   2.945  -7.515  1.00140.36           O  
ANISOU  188  O   ALA A1024    10607  26773  15951  -1679  -1301   -627       O  
ATOM    189  CB  ALA A1024      35.616   2.261  -7.737  1.00165.96           C  
ANISOU  189  CB  ALA A1024    10702  32705  19649   -836  -1346  -1341       C  
ATOM    190  N   GLN A1025      32.839   0.798  -8.117  1.00146.04           N  
ANISOU  190  N   GLN A1025    10566  27541  17381    138  -1191  -1814       N  
ATOM    191  CA  GLN A1025      31.584   0.590  -8.841  1.00138.88           C  
ANISOU  191  CA  GLN A1025    10499  26050  16221     89   -829  -2043       C  
ATOM    192  C   GLN A1025      30.401   0.687  -7.880  1.00131.32           C  
ANISOU  192  C   GLN A1025    10836  23703  15359   -155  -1237  -1477       C  
ATOM    193  O   GLN A1025      29.390   1.326  -8.198  1.00123.34           O  
ANISOU  193  O   GLN A1025    10535  22433  13896   -764  -1008  -1217       O  
ATOM    194  CB  GLN A1025      31.594  -0.773  -9.553  1.00146.27           C  
ANISOU  194  CB  GLN A1025    11135  26894  17545   1163   -632  -3027       C  
ATOM    195  CG  GLN A1025      32.683  -0.905 -10.607  1.00157.86           C  
ANISOU  195  CG  GLN A1025    11256  29914  18811   1483   -119  -3770       C  
ATOM    196  CD  GLN A1025      32.722  -2.273 -11.246  1.00171.89           C  
ANISOU  196  CD  GLN A1025    12754  31510  21045   2657     33  -4920       C  
ATOM    197  OE1 GLN A1025      32.744  -3.313 -10.577  1.00168.55           O  
ANISOU  197  OE1 GLN A1025    12592  29963  21485   3588   -478  -5151       O  
ATOM    198  NE2 GLN A1025      32.835  -2.294 -12.561  1.00164.71           N  
ANISOU  198  NE2 GLN A1025    11237  31781  19566   2647    719  -5685       N  
ATOM    199  N   VAL A1026      30.543   0.069  -6.697  1.00127.35           N  
ANISOU  199  N   VAL A1026    10574  22411  15402    326  -1855  -1252       N  
ATOM    200  CA  VAL A1026      29.517   0.094  -5.668  1.00119.00           C  
ANISOU  200  CA  VAL A1026    10620  20226  14369     95  -2249   -706       C  
ATOM    201  C   VAL A1026      29.309   1.534  -5.199  1.00117.91           C  
ANISOU  201  C   VAL A1026    10824  20278  13699   -903  -2276   -108       C  
ATOM    202  O   VAL A1026      28.166   1.986  -5.089  1.00109.60           O  
ANISOU  202  O   VAL A1026    10625  18672  12345  -1324  -2186    132       O  
ATOM    203  CB  VAL A1026      29.867  -0.836  -4.488  1.00126.41           C  
ANISOU  203  CB  VAL A1026    11639  20482  15909    751  -2940   -473       C  
ATOM    204  CG1 VAL A1026      28.864  -0.673  -3.352  1.00119.31           C  
ANISOU  204  CG1 VAL A1026    11789  18702  14840    344  -3311    173       C  
ATOM    205  CG2 VAL A1026      29.935  -2.291  -4.934  1.00132.66           C  
ANISOU  205  CG2 VAL A1026    12286  20746  17373   1780  -2985  -1065       C  
ATOM    206  N   LYS A1027      30.413   2.248  -4.928  1.00120.23           N  
ANISOU  206  N   LYS A1027    10422  21348  13914  -1268  -2421     83       N  
ATOM    207  CA  LYS A1027      30.370   3.633  -4.473  1.00117.41           C  
ANISOU  207  CA  LYS A1027    10360  21096  13156  -2243  -2514    561       C  
ATOM    208  C   LYS A1027      29.643   4.533  -5.443  1.00118.54           C  
ANISOU  208  C   LYS A1027    10878  21308  12854  -2878  -2000    631       C  
ATOM    209  O   LYS A1027      28.790   5.322  -5.031  1.00112.29           O  
ANISOU  209  O   LYS A1027    10915  19909  11840  -3362  -2082    950       O  
ATOM    210  CB  LYS A1027      31.776   4.183  -4.267  1.00127.36           C  
ANISOU  210  CB  LYS A1027    10648  23316  14428  -2612  -2704    661       C  
ATOM    211  CG  LYS A1027      32.330   3.968  -2.883  1.00145.85           C  
ANISOU  211  CG  LYS A1027    12903  25522  16990  -2449  -3416    901       C  
ATOM    212  CD  LYS A1027      33.690   4.651  -2.715  1.00165.72           C  
ANISOU  212  CD  LYS A1027    14406  29105  19456  -2987  -3616    995       C  
ATOM    213  CE  LYS A1027      33.671   6.133  -3.063  1.00173.81           C  
ANISOU  213  CE  LYS A1027    15602  30363  20076  -4216  -3382   1226       C  
ATOM    214  NZ  LYS A1027      32.677   6.897  -2.261  1.00174.49           N  
ANISOU  214  NZ  LYS A1027    16904  29446  19949  -4734  -3621   1481       N  
ATOM    215  N   ASP A1028      29.986   4.434  -6.728  1.00120.30           N  
ANISOU  215  N   ASP A1028    10460  22333  12915  -2848  -1487    332       N  
ATOM    216  CA  ASP A1028      29.387   5.281  -7.742  1.00118.34           C  
ANISOU  216  CA  ASP A1028    10477  22308  12177  -3469  -1034    513       C  
ATOM    217  C   ASP A1028      27.882   5.022  -7.837  1.00114.07           C  
ANISOU  217  C   ASP A1028    10915  20882  11543  -3243   -958    487       C  
ATOM    218  O   ASP A1028      27.115   5.982  -7.912  1.00109.66           O  
ANISOU  218  O   ASP A1028    10983  19978  10704  -3782   -919    886       O  
ATOM    219  CB  ASP A1028      30.065   5.044  -9.092  1.00127.83           C  
ANISOU  219  CB  ASP A1028    10717  24743  13109  -3422   -490    151       C  
ATOM    220  CG  ASP A1028      29.881   6.153 -10.116  1.00143.86           C  
ANISOU  220  CG  ASP A1028    12757  27371  14534  -4315    -88    576       C  
ATOM    221  OD1 ASP A1028      30.371   5.992 -11.258  1.00151.38           O  
ANISOU  221  OD1 ASP A1028    12921  29498  15100  -4364    402    320       O  
ATOM    222  OD2 ASP A1028      29.312   7.217  -9.754  1.00146.71           O  
ANISOU  222  OD2 ASP A1028    13876  27070  14799  -4976   -286   1183       O  
ATOM    223  N   ALA A1029      27.458   3.734  -7.791  1.00109.09           N  
ANISOU  223  N   ALA A1029    10410  19839  11200  -2454   -985     29       N  
ATOM    224  CA  ALA A1029      26.041   3.359  -7.861  1.00102.14           C  
ANISOU  224  CA  ALA A1029    10355  18208  10247  -2288   -929    -29       C  
ATOM    225  C   ALA A1029      25.291   3.894  -6.651  1.00 99.15           C  
ANISOU  225  C   ALA A1029    10790  17003   9877  -2551  -1302    443       C  
ATOM    226  O   ALA A1029      24.223   4.486  -6.813  1.00 94.23           O  
ANISOU  226  O   ALA A1029    10753  16088   8963  -2836  -1185    641       O  
ATOM    227  CB  ALA A1029      25.892   1.847  -7.954  1.00104.99           C  
ANISOU  227  CB  ALA A1029    10665  18209  11017  -1496   -966   -600       C  
ATOM    228  N   LEU A1030      25.863   3.722  -5.446  1.00 95.77           N  
ANISOU  228  N   LEU A1030    10342  16312   9733  -2439  -1758    605       N  
ATOM    229  CA  LEU A1030      25.254   4.219  -4.217  1.00 90.91           C  
ANISOU  229  CA  LEU A1030    10421  15100   9021  -2695  -2106    963       C  
ATOM    230  C   LEU A1030      25.108   5.736  -4.260  1.00 92.61           C  
ANISOU  230  C   LEU A1030    10890  15380   8917  -3387  -2042   1226       C  
ATOM    231  O   LEU A1030      24.113   6.271  -3.767  1.00 87.82           O  
ANISOU  231  O   LEU A1030    10968  14274   8124  -3544  -2098   1356       O  
ATOM    232  CB  LEU A1030      26.086   3.801  -3.011  1.00 94.56           C  
ANISOU  232  CB  LEU A1030    10679  15516   9734  -2505  -2631   1101       C  
ATOM    233  CG  LEU A1030      25.986   2.355  -2.579  1.00100.55           C  
ANISOU  233  CG  LEU A1030    11490  15845  10867  -1832  -2883   1046       C  
ATOM    234  CD1 LEU A1030      27.036   2.031  -1.530  1.00106.67           C  
ANISOU  234  CD1 LEU A1030    11891  16764  11875  -1624  -3452   1276       C  
ATOM    235  CD2 LEU A1030      24.607   2.058  -2.044  1.00 96.68           C  
ANISOU  235  CD2 LEU A1030    11840  14681  10211  -1874  -2914   1221       C  
ATOM    236  N   THR A1031      26.087   6.428  -4.868  1.00 93.80           N  
ANISOU  236  N   THR A1031    10473  16140   9026  -3804  -1925   1299       N  
ATOM    237  CA  THR A1031      26.027   7.881  -5.013  1.00 94.79           C  
ANISOU  237  CA  THR A1031    10869  16195   8952  -4536  -1908   1615       C  
ATOM    238  C   THR A1031      24.785   8.276  -5.812  1.00 95.38           C  
ANISOU  238  C   THR A1031    11487  15966   8787  -4554  -1599   1724       C  
ATOM    239  O   THR A1031      24.059   9.185  -5.411  1.00 93.55           O  
ANISOU  239  O   THR A1031    11906  15149   8492  -4787  -1730   1907       O  
ATOM    240  CB  THR A1031      27.298   8.427  -5.684  1.00115.37           C  
ANISOU  240  CB  THR A1031    12689  19613  11535  -5082  -1794   1758       C  
ATOM    241  OG1 THR A1031      28.448   8.078  -4.916  1.00119.73           O  
ANISOU  241  OG1 THR A1031    12635  20548  12310  -5038  -2126   1651       O  
ATOM    242  CG2 THR A1031      27.257   9.942  -5.849  1.00119.02           C  
ANISOU  242  CG2 THR A1031    13511  19832  11878  -5947  -1842   2185       C  
ATOM    243  N   LYS A1032      24.542   7.586  -6.938  1.00 91.54           N  
ANISOU  243  N   LYS A1032    10701  15917   8162  -4263  -1216   1555       N  
ATOM    244  CA  LYS A1032      23.392   7.837  -7.806  1.00 88.70           C  
ANISOU  244  CA  LYS A1032    10726  15468   7508  -4252   -949   1660       C  
ATOM    245  C   LYS A1032      22.093   7.501  -7.075  1.00 88.00           C  
ANISOU  245  C   LYS A1032    11311  14667   7458  -3875  -1085   1548       C  
ATOM    246  O   LYS A1032      21.096   8.204  -7.248  1.00 86.16           O  
ANISOU  246  O   LYS A1032    11550  14136   7051  -3953  -1056   1754       O  
ATOM    247  CB  LYS A1032      23.523   7.023  -9.103  1.00 93.38           C  
ANISOU  247  CB  LYS A1032    10764  16841   7876  -4028   -539   1358       C  
ATOM    248  CG  LYS A1032      24.689   7.548  -9.957  1.00112.21           C  
ANISOU  248  CG  LYS A1032    12427  20163  10044  -4518   -312   1541       C  
ATOM    249  CD  LYS A1032      25.413   6.537 -10.854  1.00119.79           C  
ANISOU  249  CD  LYS A1032    12529  22109  10875  -4187     49    993       C  
ATOM    250  CE  LYS A1032      24.658   6.014 -12.041  1.00113.22           C  
ANISOU  250  CE  LYS A1032    11672  21736   9612  -3970    420    675       C  
ATOM    251  NZ  LYS A1032      25.500   5.061 -12.804  1.00114.00           N  
ANISOU  251  NZ  LYS A1032    10895  22805   9616  -3604    760    -28       N  
ATOM    252  N   MET A1033      22.112   6.462  -6.235  1.00 83.24           N  
ANISOU  252  N   MET A1033    10723  13825   7080  -3480  -1259   1281       N  
ATOM    253  CA  MET A1033      20.941   6.092  -5.457  1.00 78.94           C  
ANISOU  253  CA  MET A1033    10738  12744   6510  -3241  -1375   1238       C  
ATOM    254  C   MET A1033      20.634   7.158  -4.424  1.00 83.08           C  
ANISOU  254  C   MET A1033    11742  12868   6954  -3479  -1620   1431       C  
ATOM    255  O   MET A1033      19.468   7.475  -4.213  1.00 81.38           O  
ANISOU  255  O   MET A1033    11965  12388   6566  -3394  -1576   1439       O  
ATOM    256  CB  MET A1033      21.125   4.740  -4.776  1.00 81.54           C  
ANISOU  256  CB  MET A1033    10992  12886   7102  -2867  -1559   1054       C  
ATOM    257  CG  MET A1033      21.218   3.590  -5.738  1.00 86.90           C  
ANISOU  257  CG  MET A1033    11322  13752   7943  -2531  -1346    698       C  
ATOM    258  SD  MET A1033      21.338   2.002  -4.891  1.00 93.50           S  
ANISOU  258  SD  MET A1033    12227  14052   9246  -2072  -1671    577       S  
ATOM    259  CE  MET A1033      19.683   1.773  -4.380  1.00 85.83           C  
ANISOU  259  CE  MET A1033    11933  12629   8051  -2222  -1671    737       C  
ATOM    260  N   ARG A1034      21.667   7.724  -3.787  1.00 82.39           N  
ANISOU  260  N   ARG A1034    11530  12793   6981  -3768  -1883   1512       N  
ATOM    261  CA  ARG A1034      21.459   8.764  -2.776  1.00 82.69           C  
ANISOU  261  CA  ARG A1034    12040  12436   6944  -4019  -2148   1540       C  
ATOM    262  C   ARG A1034      20.800   9.986  -3.406  1.00 86.50           C  
ANISOU  262  C   ARG A1034    12883  12613   7370  -4205  -2022   1673       C  
ATOM    263  O   ARG A1034      19.818  10.495  -2.872  1.00 85.31           O  
ANISOU  263  O   ARG A1034    13230  12066   7119  -4049  -2073   1559       O  
ATOM    264  CB  ARG A1034      22.785   9.161  -2.100  1.00 86.81           C  
ANISOU  264  CB  ARG A1034    12294  13098   7592  -4403  -2489   1560       C  
ATOM    265  CG  ARG A1034      22.574   9.955  -0.817  1.00 94.45           C  
ANISOU  265  CG  ARG A1034    13759  13700   8429  -4606  -2825   1406       C  
ATOM    266  CD  ARG A1034      23.871  10.305  -0.129  1.00107.73           C  
ANISOU  266  CD  ARG A1034    15141  15605  10186  -5052  -3219   1384       C  
ATOM    267  NE  ARG A1034      23.653  10.629   1.280  1.00123.13           N  
ANISOU  267  NE  ARG A1034    17504  17400  11882  -5130  -3570   1123       N  
ATOM    268  CZ  ARG A1034      23.292  11.822   1.742  1.00145.66           C  
ANISOU  268  CZ  ARG A1034    20887  19792  14666  -5417  -3701    840       C  
ATOM    269  NH1 ARG A1034      23.061  12.827   0.903  1.00130.31           N  
ANISOU  269  NH1 ARG A1034    19192  17346  12974  -5641  -3553    900       N  
ATOM    270  NH2 ARG A1034      23.124  12.011   3.044  1.00143.54           N  
ANISOU  270  NH2 ARG A1034    20924  19552  14062  -5457  -3997    486       N  
ATOM    271  N   ALA A1035      21.328  10.434  -4.555  1.00 84.64           N  
ANISOU  271  N   ALA A1035    12361  12615   7182  -4510  -1862   1939       N  
ATOM    272  CA  ALA A1035      20.792  11.584  -5.262  1.00 85.76           C  
ANISOU  272  CA  ALA A1035    12842  12437   7307  -4714  -1811   2243       C  
ATOM    273  C   ALA A1035      19.354  11.327  -5.683  1.00 84.22           C  
ANISOU  273  C   ALA A1035    12903  12174   6924  -4219  -1617   2209       C  
ATOM    274  O   ALA A1035      18.518  12.219  -5.536  1.00 84.42           O  
ANISOU  274  O   ALA A1035    13402  11687   6989  -4096  -1722   2277       O  
ATOM    275  CB  ALA A1035      21.652  11.897  -6.474  1.00 90.90           C  
ANISOU  275  CB  ALA A1035    13042  13579   7918  -5196  -1645   2645       C  
ATOM    276  N   ALA A1036      19.057  10.093  -6.171  1.00 76.55           N  
ANISOU  276  N   ALA A1036    11598  11703   5785  -3913  -1368   2046       N  
ATOM    277  CA  ALA A1036      17.716   9.703  -6.605  1.00 73.17           C  
ANISOU  277  CA  ALA A1036    11298  11358   5145  -3534  -1197   1977       C  
ATOM    278  C   ALA A1036      16.752   9.717  -5.449  1.00 75.88           C  
ANISOU  278  C   ALA A1036    12032  11321   5478  -3236  -1320   1746       C  
ATOM    279  O   ALA A1036      15.645  10.218  -5.597  1.00 75.12           O  
ANISOU  279  O   ALA A1036    12160  11109   5273  -2994  -1290   1782       O  
ATOM    280  CB  ALA A1036      17.738   8.326  -7.238  1.00 72.07           C  
ANISOU  280  CB  ALA A1036    10746  11743   4893  -3372   -965   1735       C  
ATOM    281  N   ALA A1037      17.169   9.173  -4.283  1.00 73.68           N  
ANISOU  281  N   ALA A1037    11782  10947   5265  -3239  -1468   1526       N  
ATOM    282  CA  ALA A1037      16.337   9.134  -3.075  1.00 73.14           C  
ANISOU  282  CA  ALA A1037    12024  10716   5049  -3039  -1558   1307       C  
ATOM    283  C   ALA A1037      16.012  10.539  -2.607  1.00 82.06           C  
ANISOU  283  C   ALA A1037    13551  11424   6204  -3007  -1702   1214       C  
ATOM    284  O   ALA A1037      14.875  10.806  -2.241  1.00 81.11           O  
ANISOU  284  O   ALA A1037    13622  11278   5919  -2684  -1638   1024       O  
ATOM    285  CB  ALA A1037      17.039   8.360  -1.971  1.00 73.90           C  
ANISOU  285  CB  ALA A1037    12060  10873   5146  -3138  -1753   1223       C  
ATOM    286  N   LEU A1038      16.993  11.449  -2.670  1.00 84.96           N  
ANISOU  286  N   LEU A1038    14012  11458   6810  -3342  -1901   1319       N  
ATOM    287  CA  LEU A1038      16.806  12.838  -2.263  1.00 90.76           C  
ANISOU  287  CA  LEU A1038    15206  11575   7704  -3356  -2110   1182       C  
ATOM    288  C   LEU A1038      15.764  13.534  -3.147  1.00 96.74           C  
ANISOU  288  C   LEU A1038    16144  12073   8540  -3010  -2017   1374       C  
ATOM    289  O   LEU A1038      14.980  14.337  -2.641  1.00 99.73           O  
ANISOU  289  O   LEU A1038    16885  12019   8989  -2648  -2120   1085       O  
ATOM    290  CB  LEU A1038      18.136  13.603  -2.312  1.00 95.99           C  
ANISOU  290  CB  LEU A1038    15901  11912   8659  -3952  -2368   1342       C  
ATOM    291  CG  LEU A1038      19.231  13.161  -1.322  1.00102.53           C  
ANISOU  291  CG  LEU A1038    16531  12995   9430  -4294  -2580   1135       C  
ATOM    292  CD1 LEU A1038      20.539  13.893  -1.586  1.00108.56           C  
ANISOU  292  CD1 LEU A1038    17175  13594  10479  -4975  -2808   1352       C  
ATOM    293  CD2 LEU A1038      18.799  13.368   0.112  1.00106.71           C  
ANISOU  293  CD2 LEU A1038    17413  13390   9742  -4125  -2768    596       C  
ATOM    294  N   ASP A1039      15.743  13.218  -4.453  1.00 92.17           N  
ANISOU  294  N   ASP A1039    15278  11824   7918  -3070  -1840   1823       N  
ATOM    295  CA  ASP A1039      14.776  13.801  -5.379  1.00 94.48           C  
ANISOU  295  CA  ASP A1039    15670  12014   8213  -2749  -1807   2127       C  
ATOM    296  C   ASP A1039      13.401  13.208  -5.178  1.00 95.62           C  
ANISOU  296  C   ASP A1039    15693  12550   8088  -2183  -1634   1839       C  
ATOM    297  O   ASP A1039      12.414  13.942  -5.158  1.00 99.95           O  
ANISOU  297  O   ASP A1039    16430  12841   8704  -1705  -1715   1789       O  
ATOM    298  CB  ASP A1039      15.206  13.600  -6.827  1.00 97.30           C  
ANISOU  298  CB  ASP A1039    15703  12822   8446  -3065  -1675   2687       C  
ATOM    299  CG  ASP A1039      16.473  14.326  -7.235  1.00118.73           C  
ANISOU  299  CG  ASP A1039    18451  15293  11368  -3714  -1813   3120       C  
ATOM    300  OD1 ASP A1039      16.816  15.342  -6.584  1.00123.89           O  
ANISOU  300  OD1 ASP A1039    19534  15155  12385  -3901  -2108   3101       O  
ATOM    301  OD2 ASP A1039      17.085  13.923  -8.248  1.00128.07           O  
ANISOU  301  OD2 ASP A1039    19216  17115  12329  -4068  -1626   3459       O  
ATOM    302  N   ALA A1040      13.328  11.877  -5.045  1.00 85.46           N  
ANISOU  302  N   ALA A1040    14063  11875   6532  -2237  -1418   1659       N  
ATOM    303  CA  ALA A1040      12.069  11.151  -4.845  1.00 82.24           C  
ANISOU  303  CA  ALA A1040    13467  11941   5838  -1892  -1241   1426       C  
ATOM    304  C   ALA A1040      11.372  11.594  -3.578  1.00 85.37           C  
ANISOU  304  C   ALA A1040    14075  12191   6171  -1560  -1287   1007       C  
ATOM    305  O   ALA A1040      10.140  11.663  -3.541  1.00 86.45           O  
ANISOU  305  O   ALA A1040    14076  12639   6131  -1143  -1184    857       O  
ATOM    306  CB  ALA A1040      12.337   9.667  -4.784  1.00 78.99           C  
ANISOU  306  CB  ALA A1040    12769  11970   5274  -2146  -1084   1332       C  
ATOM    307  N   GLN A1041      12.165  11.922  -2.547  1.00 80.76           N  
ANISOU  307  N   GLN A1041    13759  11246   5680  -1745  -1444    774       N  
ATOM    308  CA  GLN A1041      11.675  12.381  -1.258  1.00 82.85           C  
ANISOU  308  CA  GLN A1041    14230  11460   5788  -1484  -1487    258       C  
ATOM    309  C   GLN A1041      10.869  13.680  -1.405  1.00 90.95           C  
ANISOU  309  C   GLN A1041    15484  12042   7030   -914  -1577     47       C  
ATOM    310  O   GLN A1041      10.017  13.949  -0.572  1.00 94.21           O  
ANISOU  310  O   GLN A1041    15900  12660   7235   -480  -1501   -473       O  
ATOM    311  CB  GLN A1041      12.860  12.590  -0.306  1.00 85.18           C  
ANISOU  311  CB  GLN A1041    14773  11455   6137  -1876  -1716     67       C  
ATOM    312  CG  GLN A1041      12.479  13.001   1.101  1.00 93.34           C  
ANISOU  312  CG  GLN A1041    16011  12585   6870  -1689  -1764   -561       C  
ATOM    313  CD  GLN A1041      13.658  13.002   2.044  1.00116.50           C  
ANISOU  313  CD  GLN A1041    19103  15437   9725  -2159  -2025   -718       C  
ATOM    314  OE1 GLN A1041      14.696  13.599   1.788  1.00112.21           O  
ANISOU  314  OE1 GLN A1041    18730  14350   9554  -2496  -2282   -614       O  
ATOM    315  NE2 GLN A1041      13.484  12.401   3.204  1.00115.94           N  
ANISOU  315  NE2 GLN A1041    18958  15983   9112  -2231  -1989   -964       N  
ATOM    316  N   LYS A1042      11.112  14.462  -2.462  1.00 88.02           N  
ANISOU  316  N   LYS A1042    15274  11111   7058   -888  -1745    466       N  
ATOM    317  CA  LYS A1042      10.429  15.741  -2.655  1.00 94.38           C  
ANISOU  317  CA  LYS A1042    16369  11280   8210   -298  -1939    375       C  
ATOM    318  C   LYS A1042       9.190  15.599  -3.551  1.00 98.18           C  
ANISOU  318  C   LYS A1042    16485  12247   8571    242  -1824    644       C  
ATOM    319  O   LYS A1042       8.425  16.556  -3.691  1.00103.54           O  
ANISOU  319  O   LYS A1042    17301  12511   9527    913  -1996    568       O  
ATOM    320  CB  LYS A1042      11.395  16.767  -3.264  1.00100.98           C  
ANISOU  320  CB  LYS A1042    17648  11141   9580   -649  -2277    823       C  
ATOM    321  CG  LYS A1042      12.621  16.987  -2.391  1.00121.80           C  
ANISOU  321  CG  LYS A1042    20582  13348  12347  -1240  -2445    529       C  
ATOM    322  CD  LYS A1042      13.573  18.044  -2.918  1.00138.86           C  
ANISOU  322  CD  LYS A1042    23163  14548  15050  -1734  -2794    968       C  
ATOM    323  CE  LYS A1042      14.860  18.098  -2.107  1.00153.28           C  
ANISOU  323  CE  LYS A1042    25124  16183  16932  -2453  -2960    696       C  
ATOM    324  NZ  LYS A1042      14.631  18.283  -0.643  1.00165.93           N  
ANISOU  324  NZ  LYS A1042    26957  17691  18397  -2196  -3038   -252       N  
ATOM    325  N   ALA A1043       8.978  14.408  -4.126  1.00 90.07           N  
ANISOU  325  N   ALA A1043    14984  12081   7156    -20  -1574    909       N  
ATOM    326  CA  ALA A1043       7.850  14.150  -5.015  1.00 91.15           C  
ANISOU  326  CA  ALA A1043    14695  12845   7094    352  -1489   1150       C  
ATOM    327  C   ALA A1043       6.603  13.751  -4.236  1.00 97.70           C  
ANISOU  327  C   ALA A1043    15138  14392   7592    798  -1270    618       C  
ATOM    328  O   ALA A1043       6.670  13.521  -3.029  1.00 97.22           O  
ANISOU  328  O   ALA A1043    15136  14440   7362    730  -1139    112       O  
ATOM    329  CB  ALA A1043       8.210  13.055  -6.001  1.00 86.27           C  
ANISOU  329  CB  ALA A1043    13753  12822   6202   -202  -1338   1550       C  
ATOM    330  N   THR A1044       5.460  13.688  -4.940  1.00 97.35           N  
ANISOU  330  N   THR A1044    14640  14959   7391   1218  -1243    765       N  
ATOM    331  CA  THR A1044       4.176  13.279  -4.392  1.00 99.50           C  
ANISOU  331  CA  THR A1044    14364  16144   7299   1587  -1015    338       C  
ATOM    332  C   THR A1044       3.730  12.005  -5.079  1.00 99.03           C  
ANISOU  332  C   THR A1044    13777  17018   6832   1092   -834    580       C  
ATOM    333  O   THR A1044       3.385  12.036  -6.271  1.00 99.51           O  
ANISOU  333  O   THR A1044    13600  17345   6865   1172   -968    985       O  
ATOM    334  CB  THR A1044       3.125  14.379  -4.532  1.00117.61           C  
ANISOU  334  CB  THR A1044    16476  18406   9803   2595  -1187    195       C  
ATOM    335  OG1 THR A1044       3.572  15.557  -3.861  1.00124.61           O  
ANISOU  335  OG1 THR A1044    17944  18247  11157   3044  -1390   -146       O  
ATOM    336  CG2 THR A1044       1.777  13.949  -3.979  1.00118.52           C  
ANISOU  336  CG2 THR A1044    15855  19690   9485   2972   -908   -278       C  
ATOM    337  N   PRO A1045       3.717  10.869  -4.350  1.00 91.29           N  
ANISOU  337  N   PRO A1045    12626  16540   5520    538   -568    354       N  
ATOM    338  CA  PRO A1045       3.269   9.618  -4.965  1.00 88.67           C  
ANISOU  338  CA  PRO A1045    11854  16952   4884     -1   -437    515       C  
ATOM    339  C   PRO A1045       1.806   9.721  -5.417  1.00 98.02           C  
ANISOU  339  C   PRO A1045    12352  19078   5812    402   -411    466       C  
ATOM    340  O   PRO A1045       1.048  10.547  -4.901  1.00103.81           O  
ANISOU  340  O   PRO A1045    12863  20038   6540   1111   -399    197       O  
ATOM    341  CB  PRO A1045       3.460   8.595  -3.842  1.00 88.07           C  
ANISOU  341  CB  PRO A1045    11814  17063   4584   -585   -223    321       C  
ATOM    342  CG  PRO A1045       3.359   9.384  -2.603  1.00 95.08           C  
ANISOU  342  CG  PRO A1045    12842  17876   5408   -164   -160    -51       C  
ATOM    343  CD  PRO A1045       4.068  10.662  -2.934  1.00 91.41           C  
ANISOU  343  CD  PRO A1045    12851  16482   5398    339   -419    -25       C  
ATOM    344  N   PRO A1046       1.408   8.889  -6.394  1.00 93.28           N  
ANISOU  344  N   PRO A1046    11371  19073   4999    -17   -421    659       N  
ATOM    345  CA  PRO A1046       0.045   8.952  -6.940  1.00 98.78           C  
ANISOU  345  CA  PRO A1046    11324  20791   5418    295   -458    652       C  
ATOM    346  C   PRO A1046      -1.078   8.819  -5.897  1.00104.53           C  
ANISOU  346  C   PRO A1046    11468  22396   5855    454   -208    268       C  
ATOM    347  O   PRO A1046      -2.098   9.506  -6.007  1.00110.34           O  
ANISOU  347  O   PRO A1046    11639  23775   6510   1183   -266    162       O  
ATOM    348  CB  PRO A1046       0.003   7.744  -7.880  1.00 99.03           C  
ANISOU  348  CB  PRO A1046    11129  21287   5211   -504   -464    763       C  
ATOM    349  CG  PRO A1046       1.124   6.870  -7.434  1.00 97.52           C  
ANISOU  349  CG  PRO A1046    11484  20388   5182  -1193   -340    702       C  
ATOM    350  CD  PRO A1046       2.182   7.843  -7.074  1.00 90.24           C  
ANISOU  350  CD  PRO A1046    11172  18503   4611   -775   -422    810       C  
ATOM    351  N   LYS A1047      -0.896   7.968  -4.895  1.00 97.52           N  
ANISOU  351  N   LYS A1047    10669  21597   4787   -192     55     96       N  
ATOM    352  CA  LYS A1047      -1.900   7.723  -3.856  1.00102.27           C  
ANISOU  352  CA  LYS A1047    10681  23203   4974   -244    355   -208       C  
ATOM    353  C   LYS A1047      -2.034   8.912  -2.891  1.00109.45           C  
ANISOU  353  C   LYS A1047    11633  24043   5910    672    447   -627       C  
ATOM    354  O   LYS A1047      -2.996   8.964  -2.128  1.00114.61           O  
ANISOU  354  O   LYS A1047    11649  25734   6165    875    717   -981       O  
ATOM    355  CB  LYS A1047      -1.491   6.464  -3.087  1.00101.24           C  
ANISOU  355  CB  LYS A1047    10778  23040   4649  -1296    543   -105       C  
ATOM    356  CG  LYS A1047      -2.391   5.972  -1.968  1.00115.11           C  
ANISOU  356  CG  LYS A1047    11977  25897   5862  -1691    881   -251       C  
ATOM    357  CD  LYS A1047      -1.887   4.636  -1.475  1.00121.55           C  
ANISOU  357  CD  LYS A1047    13144  26444   6597  -2830    928     85       C  
ATOM    358  CE  LYS A1047      -2.793   3.955  -0.483  1.00142.94           C  
ANISOU  358  CE  LYS A1047    15293  30310   8706  -3514   1240    148       C  
ATOM    359  NZ  LYS A1047      -2.303   2.591  -0.148  1.00151.72           N  
ANISOU  359  NZ  LYS A1047    16830  30960   9858  -4673   1174    633       N  
ATOM    360  N   LEU A1048      -1.115   9.877  -2.948  1.00104.99           N  
ANISOU  360  N   LEU A1048    11766  22328   5799   1209    226   -643       N  
ATOM    361  CA  LEU A1048      -1.163  10.988  -2.008  1.00110.97           C  
ANISOU  361  CA  LEU A1048    12672  22848   6646   2034    273  -1171       C  
ATOM    362  C   LEU A1048      -1.311  12.349  -2.719  1.00121.89           C  
ANISOU  362  C   LEU A1048    14177  23575   8561   3123    -73  -1183       C  
ATOM    363  O   LEU A1048      -1.187  13.388  -2.063  1.00126.55           O  
ANISOU  363  O   LEU A1048    15071  23602   9411   3863   -132  -1660       O  
ATOM    364  CB  LEU A1048       0.107  10.992  -1.129  1.00106.48           C  
ANISOU  364  CB  LEU A1048    12905  21387   6164   1637    275  -1272       C  
ATOM    365  CG  LEU A1048       0.328   9.720  -0.275  1.00107.84           C  
ANISOU  365  CG  LEU A1048    13048  22084   5841    635    536  -1170       C  
ATOM    366  CD1 LEU A1048       1.534   9.858   0.616  1.00104.78           C  
ANISOU  366  CD1 LEU A1048    13371  20932   5508    388    463  -1270       C  
ATOM    367  CD2 LEU A1048      -0.890   9.413   0.571  1.00117.65           C  
ANISOU  367  CD2 LEU A1048    13520  24750   6431    622    915  -1509       C  
ATOM    368  N   GLU A1049      -1.654  12.347  -4.021  1.00119.95           N  
ANISOU  368  N   GLU A1049    13672  23453   8449   3236   -325   -682       N  
ATOM    369  CA  GLU A1049      -1.843  13.579  -4.800  1.00126.01           C  
ANISOU  369  CA  GLU A1049    14548  23621   9709   4224   -735   -473       C  
ATOM    370  C   GLU A1049      -2.983  14.438  -4.253  1.00140.93           C  
ANISOU  370  C   GLU A1049    15865  26020  11662   5419   -713  -1053       C  
ATOM    371  O   GLU A1049      -2.899  15.666  -4.292  1.00146.67           O  
ANISOU  371  O   GLU A1049    16969  25798  12959   6378  -1029  -1157       O  
ATOM    372  CB  GLU A1049      -2.125  13.259  -6.262  1.00126.87           C  
ANISOU  372  CB  GLU A1049    14340  24129   9735   4027   -996    206       C  
ATOM    373  CG  GLU A1049      -0.995  12.556  -6.994  1.00132.75           C  
ANISOU  373  CG  GLU A1049    15612  24377  10451   3032  -1046    704       C  
ATOM    374  CD  GLU A1049      -1.303  12.313  -8.469  1.00161.90           C  
ANISOU  374  CD  GLU A1049    18965  28606  13944   2872  -1305   1279       C  
ATOM    375  OE1 GLU A1049      -1.956  13.172  -9.109  1.00160.67           O  
ANISOU  375  OE1 GLU A1049    18541  28593  13912   3678  -1648   1586       O  
ATOM    376  OE2 GLU A1049      -0.855  11.272  -8.997  1.00154.77           O  
ANISOU  376  OE2 GLU A1049    18085  27960  12759   1965  -1200   1412       O  
ATOM    377  N   ASP A1050      -4.042  13.793  -3.757  1.00141.42           N  
ANISOU  377  N   ASP A1050    15000  27567  11168   5355   -352  -1436       N  
ATOM    378  CA  ASP A1050      -5.203  14.476  -3.190  1.00153.11           C  
ANISOU  378  CA  ASP A1050    15713  29867  12595   6491   -238  -2099       C  
ATOM    379  C   ASP A1050      -4.934  14.914  -1.745  1.00157.49           C  
ANISOU  379  C   ASP A1050    16572  30181  13085   6790     70  -2971       C  
ATOM    380  O   ASP A1050      -5.676  15.730  -1.193  1.00167.90           O  
ANISOU  380  O   ASP A1050    17454  31855  14487   7931    141  -3710       O  
ATOM    381  CB  ASP A1050      -6.426  13.548  -3.238  1.00159.17           C  
ANISOU  381  CB  ASP A1050    15249  32536  12694   6133     67  -2141       C  
ATOM    382  CG  ASP A1050      -6.257  12.296  -2.397  1.00169.72           C  
ANISOU  382  CG  ASP A1050    16493  34613  13382   4831    559  -2240       C  
ATOM    383  OD1 ASP A1050      -5.288  11.538  -2.641  1.00161.37           O  
ANISOU  383  OD1 ASP A1050    16130  32837  12346   3780    510  -1769       O  
ATOM    384  OD2 ASP A1050      -7.102  12.061  -1.512  1.00180.80           O  
ANISOU  384  OD2 ASP A1050    17402  36698  14595   4642   1003  -2647       O  
ATOM    385  N   LYS A1051      -3.896  14.339  -1.130  1.00143.29           N  
ANISOU  385  N   LYS A1051    15460  27888  11093   5789    244  -2930       N  
ATOM    386  CA  LYS A1051      -3.539  14.630   0.246  1.00144.81           C  
ANISOU  386  CA  LYS A1051    15968  27982  11071   5864    512  -3705       C  
ATOM    387  C   LYS A1051      -2.761  15.928   0.358  1.00149.84           C  
ANISOU  387  C   LYS A1051    17521  26966  12445   6618    140  -4043       C  
ATOM    388  O   LYS A1051      -2.179  16.415  -0.619  1.00146.51           O  
ANISOU  388  O   LYS A1051    17682  25298  12687   6722   -319  -3445       O  
ATOM    389  CB  LYS A1051      -2.706  13.484   0.848  1.00137.88           C  
ANISOU  389  CB  LYS A1051    15456  27235   9697   4485    751  -3421       C  
ATOM    390  CG  LYS A1051      -3.426  12.145   0.963  1.00149.47           C  
ANISOU  390  CG  LYS A1051    16135  30213  10445   3575   1120  -3119       C  
ATOM    391  CD  LYS A1051      -4.542  12.178   1.990  1.00172.05           C  
ANISOU  391  CD  LYS A1051    18081  34679  12610   3913   1591  -3823       C  
ATOM    392  CE  LYS A1051      -5.189  10.833   2.176  1.00184.51           C  
ANISOU  392  CE  LYS A1051    19174  37223  13710   2697   1955  -3328       C  
ATOM    393  NZ  LYS A1051      -6.279  10.894   3.190  1.00192.84           N  
ANISOU  393  NZ  LYS A1051    20652  37237  15382   2444   2538  -3393       N  
ATOM    394  N   SER A1052      -2.762  16.487   1.569  1.00151.82           N  
ANISOU  394  N   SER A1052    17887  27266  12533   7079    338  -5024       N  
ATOM    395  CA  SER A1052      -2.024  17.691   1.894  1.00155.22           C  
ANISOU  395  CA  SER A1052    19216  26136  13623   7685      1  -5551       C  
ATOM    396  C   SER A1052      -0.537  17.392   1.904  1.00145.64           C  
ANISOU  396  C   SER A1052    18956  23837  12544   6578   -190  -5044       C  
ATOM    397  O   SER A1052      -0.139  16.313   2.350  1.00137.40           O  
ANISOU  397  O   SER A1052    17839  23503  10865   5524     87  -4786       O  
ATOM    398  CB  SER A1052      -2.478  18.243   3.245  1.00170.29           C  
ANISOU  398  CB  SER A1052    20896  28642  15164   8401    317  -6901       C  
ATOM    399  OG  SER A1052      -1.689  19.342   3.672  1.00183.97           O  
ANISOU  399  OG  SER A1052    23575  28821  17504   8830    -21  -7545       O  
ATOM    400  N   PRO A1053       0.306  18.338   1.449  1.00140.78           N  
ANISOU  400  N   PRO A1053    19217  21510  12765   6785   -686  -4874       N  
ATOM    401  CA  PRO A1053       1.756  18.105   1.484  1.00131.61           C  
ANISOU  401  CA  PRO A1053    18853  19430  11723   5732   -866  -4440       C  
ATOM    402  C   PRO A1053       2.278  17.918   2.912  1.00135.76           C  
ANISOU  402  C   PRO A1053    19589  20298  11695   5285   -638  -5221       C  
ATOM    403  O   PRO A1053       3.384  17.410   3.102  1.00127.26           O  
ANISOU  403  O   PRO A1053    18934  18930  10488   4314   -707  -4849       O  
ATOM    404  CB  PRO A1053       2.324  19.379   0.854  1.00138.21           C  
ANISOU  404  CB  PRO A1053    20480  18475  13561   6183  -1432  -4269       C  
ATOM    405  CG  PRO A1053       1.200  19.920   0.020  1.00149.91           C  
ANISOU  405  CG  PRO A1053    21531  19991  15438   7271  -1601  -4081       C  
ATOM    406  CD  PRO A1053      -0.009  19.645   0.839  1.00151.44           C  
ANISOU  406  CD  PRO A1053    20851  21668  15022   7937  -1147  -4966       C  
ATOM    407  N   ASP A1054       1.466  18.302   3.912  1.00142.87           N  
ANISOU  407  N   ASP A1054    20120  21960  12204   6014   -365  -6310       N  
ATOM    408  CA  ASP A1054       1.822  18.196   5.320  1.00146.04           C  
ANISOU  408  CA  ASP A1054    20644  22930  11916   5667   -136  -7151       C  
ATOM    409  C   ASP A1054       1.054  17.060   5.995  1.00150.28           C  
ANISOU  409  C   ASP A1054    20311  25456  11334   5252    441  -7170       C  
ATOM    410  O   ASP A1054       1.148  16.896   7.211  1.00154.51           O  
ANISOU  410  O   ASP A1054    20786  26837  11084   4979    697  -7827       O  
ATOM    411  CB  ASP A1054       1.546  19.525   6.033  1.00161.76           C  
ANISOU  411  CB  ASP A1054    22900  24354  14206   6751   -244  -8517       C  
ATOM    412  CG  ASP A1054       2.301  20.694   5.433  1.00174.08           C  
ANISOU  412  CG  ASP A1054    25406  23797  16940   7068   -870  -8478       C  
ATOM    413  OD1 ASP A1054       1.991  21.072   4.282  1.00174.40           O  
ANISOU  413  OD1 ASP A1054    25471  23049  17745   7567  -1154  -7809       O  
ATOM    414  OD2 ASP A1054       3.145  21.279   6.141  1.00184.63           O  
ANISOU  414  OD2 ASP A1054    27436  24308  18406   6821  -1101  -9141       O  
ATOM    415  N   SER A1055       0.326  16.258   5.207  1.00142.99           N  
ANISOU  415  N   SER A1055    18726  25310  10293   5094    619  -6405       N  
ATOM    416  CA  SER A1055      -0.422  15.128   5.734  1.00143.25           C  
ANISOU  416  CA  SER A1055    17935  27152   9341   4530   1127  -6258       C  
ATOM    417  C   SER A1055       0.486  14.111   6.437  1.00141.78           C  
ANISOU  417  C   SER A1055    18077  27246   8546   3256   1190  -5779       C  
ATOM    418  O   SER A1055       1.671  14.017   6.109  1.00132.95           O  
ANISOU  418  O   SER A1055    17685  24949   7881   2729    825  -5264       O  
ATOM    419  CB  SER A1055      -1.183  14.422   4.619  1.00142.69           C  
ANISOU  419  CB  SER A1055    17229  27598   9388   4395   1183  -5437       C  
ATOM    420  OG  SER A1055      -2.244  15.212   4.126  1.00161.52           O  
ANISOU  420  OG  SER A1055    19053  30203  12113   5587   1172  -5860       O  
ATOM    421  N   PRO A1056      -0.066  13.317   7.387  1.00144.03           N  
ANISOU  421  N   PRO A1056    17780  29155   7792   2733   1637  -5865       N  
ATOM    422  CA  PRO A1056       0.745  12.282   8.053  1.00139.48           C  
ANISOU  422  CA  PRO A1056    17503  28852   6639   1530   1629  -5242       C  
ATOM    423  C   PRO A1056       1.296  11.257   7.063  1.00135.23           C  
ANISOU  423  C   PRO A1056    17197  27596   6586    730   1384  -4043       C  
ATOM    424  O   PRO A1056       2.382  10.714   7.278  1.00130.18           O  
ANISOU  424  O   PRO A1056    17099  26389   5973     10   1135  -3527       O  
ATOM    425  CB  PRO A1056      -0.251  11.635   9.011  1.00148.99           C  
ANISOU  425  CB  PRO A1056    17886  32044   6678   1167   2172  -5394       C  
ATOM    426  CG  PRO A1056      -1.255  12.717   9.284  1.00164.60           C  
ANISOU  426  CG  PRO A1056    19300  34720   8522   2372   2464  -6603       C  
ATOM    427  CD  PRO A1056      -1.433  13.353   7.947  1.00156.32           C  
ANISOU  427  CD  PRO A1056    18343  32440   8612   3205   2156  -6509       C  
ATOM    428  N   GLU A1057       0.561  11.015   5.964  1.00130.45           N  
ANISOU  428  N   GLU A1057    16155  27042   6368    912   1426  -3668       N  
ATOM    429  CA  GLU A1057       0.989  10.095   4.918  1.00121.34           C  
ANISOU  429  CA  GLU A1057    15177  25253   5676    253   1210  -2718       C  
ATOM    430  C   GLU A1057       2.228  10.638   4.223  1.00121.29           C  
ANISOU  430  C   GLU A1057    15954  23640   6489    406    764  -2543       C  
ATOM    431  O   GLU A1057       3.198   9.901   4.063  1.00115.30           O  
ANISOU  431  O   GLU A1057    15598  22317   5896   -294    567  -1958       O  
ATOM    432  CB  GLU A1057      -0.130   9.842   3.899  1.00123.25           C  
ANISOU  432  CB  GLU A1057    14727  26040   6063    452   1330  -2502       C  
ATOM    433  CG  GLU A1057      -1.336   9.079   4.422  1.00139.57           C  
ANISOU  433  CG  GLU A1057    15911  29778   7339     27   1763  -2483       C  
ATOM    434  CD  GLU A1057      -2.190   9.810   5.444  1.00173.84           C  
ANISOU  434  CD  GLU A1057    19670  35345  11038    687   2144  -3363       C  
ATOM    435  OE1 GLU A1057      -2.330  11.050   5.330  1.00168.71           O  
ANISOU  435  OE1 GLU A1057    19061  34279  10761   1836   2059  -4098       O  
ATOM    436  OE2 GLU A1057      -2.757   9.136   6.334  1.00176.77           O  
ANISOU  436  OE2 GLU A1057    19512  37121  10531     58   2527  -3321       O  
ATOM    437  N   MET A1058       2.211  11.938   3.834  1.00121.55           N  
ANISOU  437  N   MET A1058    16191  22939   7055   1319    588  -3039       N  
ATOM    438  CA  MET A1058       3.358  12.577   3.179  1.00116.97           C  
ANISOU  438  CA  MET A1058    16329  20881   7234   1391    167  -2836       C  
ATOM    439  C   MET A1058       4.563  12.620   4.112  1.00117.81           C  
ANISOU  439  C   MET A1058    17010  20537   7214    914      4  -2988       C  
ATOM    440  O   MET A1058       5.697  12.485   3.650  1.00111.09           O  
ANISOU  440  O   MET A1058    16606  18815   6788    480   -283  -2521       O  
ATOM    441  CB  MET A1058       3.030  13.994   2.691  1.00125.62           C  
ANISOU  441  CB  MET A1058    17573  21224   8933   2417    -36  -3279       C  
ATOM    442  CG  MET A1058       2.181  14.025   1.428  1.00129.82           C  
ANISOU  442  CG  MET A1058    17666  21884   9775   2852    -75  -2858       C  
ATOM    443  SD  MET A1058       2.916  13.161   0.014  1.00124.26           S  
ANISOU  443  SD  MET A1058    17120  20719   9375   2062   -269  -1787       S  
ATOM    444  CE  MET A1058       4.401  14.136  -0.257  1.00119.42           C  
ANISOU  444  CE  MET A1058    17419  18499   9457   2002   -697  -1635       C  
ATOM    445  N   LYS A1059       4.325  12.801   5.416  1.00119.69           N  
ANISOU  445  N   LYS A1059    17169  21501   6808    981    187  -3657       N  
ATOM    446  CA  LYS A1059       5.408  12.812   6.392  1.00119.54           C  
ANISOU  446  CA  LYS A1059    17623  21276   6520    493      1  -3827       C  
ATOM    447  C   LYS A1059       5.996  11.400   6.533  1.00116.02           C  
ANISOU  447  C   LYS A1059    17148  21177   5757   -473    -25  -2950       C  
ATOM    448  O   LYS A1059       7.218  11.236   6.695  1.00111.57           O  
ANISOU  448  O   LYS A1059    17010  20015   5368   -931   -347  -2665       O  
ATOM    449  CB  LYS A1059       4.925  13.348   7.746  1.00132.58           C  
ANISOU  449  CB  LYS A1059    19142  23815   7417    811    219  -4829       C  
ATOM    450  CG  LYS A1059       4.627  14.865   7.774  1.00152.32           C  
ANISOU  450  CG  LYS A1059    21861  25647  10368   1828    124  -5895       C  
ATOM    451  CD  LYS A1059       4.318  15.436   9.186  1.00168.95           C  
ANISOU  451  CD  LYS A1059    23896  28602  11693   2149    321  -7114       C  
ATOM    452  CE  LYS A1059       3.070  14.969   9.916  1.00179.24           C  
ANISOU  452  CE  LYS A1059    24368  31762  11973   2316    897  -7497       C  
ATOM    453  NZ  LYS A1059       1.823  15.388   9.237  1.00188.42           N  
ANISOU  453  NZ  LYS A1059    24950  33154  13487   3284   1135  -7793       N  
ATOM    454  N   ASP A1060       5.119  10.382   6.449  1.00111.80           N  
ANISOU  454  N   ASP A1060    16091  21575   4814   -775    278  -2514       N  
ATOM    455  CA  ASP A1060       5.521   8.982   6.479  1.00106.94           C  
ANISOU  455  CA  ASP A1060    15468  21133   4033  -1641    221  -1643       C  
ATOM    456  C   ASP A1060       6.319   8.665   5.225  1.00101.23           C  
ANISOU  456  C   ASP A1060    15011  19295   4156  -1765    -59  -1088       C  
ATOM    457  O   ASP A1060       7.373   8.028   5.293  1.00 97.13           O  
ANISOU  457  O   ASP A1060    14786  18312   3809  -2242   -322   -617       O  
ATOM    458  CB  ASP A1060       4.294   8.065   6.601  1.00112.13           C  
ANISOU  458  CB  ASP A1060    15512  22955   4139  -1984    594  -1348       C  
ATOM    459  CG  ASP A1060       4.643   6.583   6.560  1.00122.26           C  
ANISOU  459  CG  ASP A1060    16864  24195   5396  -2894    476   -412       C  
ATOM    460  OD1 ASP A1060       5.497   6.150   7.360  1.00123.56           O  
ANISOU  460  OD1 ASP A1060    17365  24267   5315  -3348    251    -82       O  
ATOM    461  OD2 ASP A1060       4.047   5.854   5.741  1.00128.33           O  
ANISOU  461  OD2 ASP A1060    17350  25009   6401  -3142    568    -24       O  
ATOM    462  N   PHE A1061       5.812   9.127   4.071  1.00 94.83           N  
ANISOU  462  N   PHE A1061    14047  18148   3837  -1292    -11  -1157       N  
ATOM    463  CA  PHE A1061       6.467   8.956   2.784  1.00 87.63           C  
ANISOU  463  CA  PHE A1061    13313  16370   3612  -1362   -221   -718       C  
ATOM    464  C   PHE A1061       7.888   9.502   2.841  1.00 92.42           C  
ANISOU  464  C   PHE A1061    14437  16065   4615  -1422   -552   -722       C  
ATOM    465  O   PHE A1061       8.836   8.809   2.453  1.00 88.41           O  
ANISOU  465  O   PHE A1061    14061  15150   4382  -1837   -724   -270       O  
ATOM    466  CB  PHE A1061       5.655   9.661   1.680  1.00 88.96           C  
ANISOU  466  CB  PHE A1061    13245  16452   4105   -758   -161   -842       C  
ATOM    467  CG  PHE A1061       6.338   9.719   0.336  1.00 84.18           C  
ANISOU  467  CG  PHE A1061    12825  15072   4087   -796   -370   -435       C  
ATOM    468  CD1 PHE A1061       6.295   8.637  -0.530  1.00 82.50           C  
ANISOU  468  CD1 PHE A1061    12400  15013   3933  -1213   -329     -5       C  
ATOM    469  CD2 PHE A1061       7.000  10.871  -0.077  1.00 86.34           C  
ANISOU  469  CD2 PHE A1061    13477  14504   4826   -457   -608   -507       C  
ATOM    470  CE1 PHE A1061       6.924   8.697  -1.777  1.00 80.08           C  
ANISOU  470  CE1 PHE A1061    12201  14189   4036  -1247   -476    288       C  
ATOM    471  CE2 PHE A1061       7.640  10.928  -1.315  1.00 85.57           C  
ANISOU  471  CE2 PHE A1061    13490  13879   5144   -583   -764    -65       C  
ATOM    472  CZ  PHE A1061       7.581   9.851  -2.169  1.00 79.72           C  
ANISOU  472  CZ  PHE A1061    12474  13466   4351   -943   -672    300       C  
ATOM    473  N   ARG A1062       8.035  10.735   3.350  1.00 94.24           N  
ANISOU  473  N   ARG A1062    14925  15996   4887  -1013   -651  -1290       N  
ATOM    474  CA  ARG A1062       9.329  11.388   3.435  1.00 94.40           C  
ANISOU  474  CA  ARG A1062    15406  15177   5283  -1149   -990  -1352       C  
ATOM    475  C   ARG A1062      10.240  10.700   4.477  1.00102.39           C  
ANISOU  475  C   ARG A1062    16530  16452   5923  -1723  -1149  -1222       C  
ATOM    476  O   ARG A1062      11.447  10.610   4.249  1.00 99.76           O  
ANISOU  476  O   ARG A1062    16377  15592   5934  -2046  -1429   -936       O  
ATOM    477  CB  ARG A1062       9.174  12.880   3.761  1.00 99.76           C  
ANISOU  477  CB  ARG A1062    16385  15374   6147   -606  -1102  -2070       C  
ATOM    478  CG  ARG A1062       8.606  13.666   2.588  1.00105.01           C  
ANISOU  478  CG  ARG A1062    17052  15470   7377    -41  -1122  -1994       C  
ATOM    479  CD  ARG A1062       8.756  15.172   2.713  1.00123.61           C  
ANISOU  479  CD  ARG A1062    19872  16894  10201    432  -1384  -2543       C  
ATOM    480  NE  ARG A1062       7.805  15.784   3.635  1.00143.97           N  
ANISOU  480  NE  ARG A1062    22378  19846  12478   1098  -1239  -3453       N  
ATOM    481  CZ  ARG A1062       6.576  16.156   3.289  1.00163.03           C  
ANISOU  481  CZ  ARG A1062    24475  22507  14960   1897  -1076  -3685       C  
ATOM    482  NH1 ARG A1062       6.126  15.930   2.062  1.00147.94           N  
ANISOU  482  NH1 ARG A1062    22304  20562  13344   2053  -1065  -3012       N  
ATOM    483  NH2 ARG A1062       5.774  16.720   4.180  1.00156.74           N  
ANISOU  483  NH2 ARG A1062    23545  22134  13875   2563   -919  -4632       N  
ATOM    484  N   HIS A1063       9.680  10.184   5.578  1.00105.30           N  
ANISOU  484  N   HIS A1063    16730  17721   5560  -1870   -986  -1358       N  
ATOM    485  CA  HIS A1063      10.510   9.521   6.580  1.00107.36           C  
ANISOU  485  CA  HIS A1063    17093  18294   5403  -2408  -1204  -1107       C  
ATOM    486  C   HIS A1063      11.109   8.220   6.016  1.00104.94           C  
ANISOU  486  C   HIS A1063    16706  17757   5411  -2829  -1338   -260       C  
ATOM    487  O   HIS A1063      12.240   7.862   6.367  1.00106.46           O  
ANISOU  487  O   HIS A1063    17029  17740   5681  -3137  -1676     35       O  
ATOM    488  CB  HIS A1063       9.719   9.234   7.862  1.00115.39           C  
ANISOU  488  CB  HIS A1063    17925  20468   5451  -2541   -987  -1331       C  
ATOM    489  CG  HIS A1063      10.570   8.679   8.953  1.00122.50           C  
ANISOU  489  CG  HIS A1063    18957  21759   5829  -3080  -1282  -1030       C  
ATOM    490  ND1 HIS A1063      11.438   9.489   9.657  1.00128.98           N  
ANISOU  490  ND1 HIS A1063    20055  22449   6502  -3105  -1593  -1533       N  
ATOM    491  CD2 HIS A1063      10.666   7.414   9.425  1.00125.50           C  
ANISOU  491  CD2 HIS A1063    19235  22622   5826  -3616  -1364   -242       C  
ATOM    492  CE1 HIS A1063      12.058   8.694  10.510  1.00131.23           C  
ANISOU  492  CE1 HIS A1063    20345  23240   6277  -3620  -1863  -1019       C  
ATOM    493  NE2 HIS A1063      11.611   7.437  10.421  1.00129.93           N  
ANISOU  493  NE2 HIS A1063    19979  23420   5967  -3918  -1744   -194       N  
ATOM    494  N   GLY A1064      10.367   7.537   5.153  1.00 94.47           N  
ANISOU  494  N   GLY A1064    15142  16470   4281  -2808  -1107     61       N  
ATOM    495  CA  GLY A1064      10.871   6.311   4.557  1.00 89.79           C  
ANISOU  495  CA  GLY A1064    14504  15553   4059  -3134  -1233    700       C  
ATOM    496  C   GLY A1064      12.149   6.578   3.799  1.00 91.70           C  
ANISOU  496  C   GLY A1064    14873  15023   4945  -3061  -1492    765       C  
ATOM    497  O   GLY A1064      13.099   5.786   3.861  1.00 91.49           O  
ANISOU  497  O   GLY A1064    14861  14758   5142  -3283  -1749   1148       O  
ATOM    498  N   PHE A1065      12.194   7.741   3.115  1.00 87.23           N  
ANISOU  498  N   PHE A1065    14376  14090   4678  -2740  -1445    410       N  
ATOM    499  CA  PHE A1065      13.358   8.142   2.346  1.00 84.28           C  
ANISOU  499  CA  PHE A1065    14065  13111   4845  -2765  -1643    496       C  
ATOM    500  C   PHE A1065      14.493   8.573   3.282  1.00 90.12           C  
ANISOU  500  C   PHE A1065    14972  13748   5523  -2983  -1986    382       C  
ATOM    501  O   PHE A1065      15.651   8.348   2.952  1.00 89.00           O  
ANISOU  501  O   PHE A1065    14735  13358   5725  -3165  -2201    615       O  
ATOM    502  CB  PHE A1065      13.013   9.243   1.348  1.00 85.62           C  
ANISOU  502  CB  PHE A1065    14291  12919   5320  -2463  -1534    313       C  
ATOM    503  CG  PHE A1065      12.367   8.671   0.110  1.00 84.43           C  
ANISOU  503  CG  PHE A1065    13891  12875   5315  -2356  -1307    557       C  
ATOM    504  CD1 PHE A1065      13.121   7.978  -0.827  1.00 85.24           C  
ANISOU  504  CD1 PHE A1065    13827  12840   5720  -2539  -1327    848       C  
ATOM    505  CD2 PHE A1065      11.007   8.828  -0.127  1.00 87.47           C  
ANISOU  505  CD2 PHE A1065    14143  13595   5495  -2057  -1081    424       C  
ATOM    506  CE1 PHE A1065      12.523   7.421  -1.961  1.00 83.65           C  
ANISOU  506  CE1 PHE A1065    13395  12820   5567  -2480  -1132    960       C  
ATOM    507  CE2 PHE A1065      10.413   8.273  -1.268  1.00 87.60           C  
ANISOU  507  CE2 PHE A1065    13891  13812   5580  -2027   -922    622       C  
ATOM    508  CZ  PHE A1065      11.172   7.566  -2.170  1.00 82.41           C  
ANISOU  508  CZ  PHE A1065    13136  12997   5178  -2265   -952    866       C  
ATOM    509  N   ASP A1066      14.176   9.121   4.461  1.00 90.18           N  
ANISOU  509  N   ASP A1066    15154  14071   5038  -2979  -2040    -12       N  
ATOM    510  CA  ASP A1066      15.212   9.448   5.436  1.00 93.97           C  
ANISOU  510  CA  ASP A1066    15765  14601   5339  -3260  -2411   -161       C  
ATOM    511  C   ASP A1066      15.882   8.171   5.886  1.00 97.57           C  
ANISOU  511  C   ASP A1066    16041  15368   5665  -3539  -2639    413       C  
ATOM    512  O   ASP A1066      17.110   8.121   6.007  1.00 98.87           O  
ANISOU  512  O   ASP A1066    16124  15402   6041  -3739  -2995    571       O  
ATOM    513  CB  ASP A1066      14.629  10.225   6.627  1.00102.41           C  
ANISOU  513  CB  ASP A1066    17042  16086   5784  -3183  -2394   -817       C  
ATOM    514  CG  ASP A1066      14.202  11.640   6.275  1.00119.74           C  
ANISOU  514  CG  ASP A1066    19489  17738   8271  -2827  -2310  -1477       C  
ATOM    515  OD1 ASP A1066      14.968  12.335   5.560  1.00121.11           O  
ANISOU  515  OD1 ASP A1066    19806  17150   9059  -2917  -2505  -1449       O  
ATOM    516  OD2 ASP A1066      13.138  12.081   6.767  1.00129.75           O  
ANISOU  516  OD2 ASP A1066    20798  19350   9151  -2467  -2075  -2025       O  
ATOM    517  N   ILE A1067      15.079   7.114   6.086  1.00 93.07           N  
ANISOU  517  N   ILE A1067    15380  15179   4802  -3559  -2466    772       N  
ATOM    518  CA  ILE A1067      15.605   5.806   6.485  1.00 93.48           C  
ANISOU  518  CA  ILE A1067    15333  15358   4827  -3786  -2733   1427       C  
ATOM    519  C   ILE A1067      16.479   5.240   5.373  1.00 94.83           C  
ANISOU  519  C   ILE A1067    15319  14925   5786  -3667  -2843   1711       C  
ATOM    520  O   ILE A1067      17.579   4.735   5.639  1.00 96.48           O  
ANISOU  520  O   ILE A1067    15404  15058   6197  -3723  -3230   2024       O  
ATOM    521  CB  ILE A1067      14.476   4.820   6.848  1.00 96.97           C  
ANISOU  521  CB  ILE A1067    15764  16221   4858  -3942  -2524   1805       C  
ATOM    522  CG1 ILE A1067      13.646   5.338   8.047  1.00101.74           C  
ANISOU  522  CG1 ILE A1067    16433  17696   4527  -4080  -2369   1498       C  
ATOM    523  CG2 ILE A1067      15.074   3.435   7.146  1.00 99.56           C  
ANISOU  523  CG2 ILE A1067    16080  16400   5347  -4158  -2887   2587       C  
ATOM    524  CD1 ILE A1067      12.425   4.442   8.428  1.00109.42           C  
ANISOU  524  CD1 ILE A1067    17300  19295   4979  -4362  -2094   1898       C  
ATOM    525  N   LEU A1068      15.982   5.322   4.134  1.00 88.24           N  
ANISOU  525  N   LEU A1068    14411  13769   5348  -3472  -2511   1571       N  
ATOM    526  CA  LEU A1068      16.699   4.833   2.963  1.00 86.35           C  
ANISOU  526  CA  LEU A1068    13946  13111   5751  -3340  -2519   1698       C  
ATOM    527  C   LEU A1068      18.034   5.535   2.809  1.00 91.01           C  
ANISOU  527  C   LEU A1068    14380  13584   6615  -3370  -2752   1585       C  
ATOM    528  O   LEU A1068      19.062   4.866   2.665  1.00 92.80           O  
ANISOU  528  O   LEU A1068    14337  13738   7184  -3319  -2988   1799       O  
ATOM    529  CB  LEU A1068      15.867   5.019   1.692  1.00 83.10           C  
ANISOU  529  CB  LEU A1068    13478  12570   5526  -3182  -2123   1507       C  
ATOM    530  CG  LEU A1068      14.713   4.048   1.525  1.00 88.75           C  
ANISOU  530  CG  LEU A1068    14201  13390   6129  -3220  -1918   1646       C  
ATOM    531  CD1 LEU A1068      13.843   4.439   0.346  1.00 85.92           C  
ANISOU  531  CD1 LEU A1068    13740  13074   5830  -3075  -1577   1411       C  
ATOM    532  CD2 LEU A1068      15.232   2.621   1.366  1.00 95.00           C  
ANISOU  532  CD2 LEU A1068    14921  13867   7309  -3259  -2110   1958       C  
ATOM    533  N   VAL A1069      18.033   6.874   2.883  1.00 86.18           N  
ANISOU  533  N   VAL A1069    13915  12946   5883  -3460  -2719   1241       N  
ATOM    534  CA  VAL A1069      19.256   7.661   2.768  1.00 86.78           C  
ANISOU  534  CA  VAL A1069    13855  12915   6204  -3660  -2955   1144       C  
ATOM    535  C   VAL A1069      20.236   7.223   3.869  1.00 93.73           C  
ANISOU  535  C   VAL A1069    14588  14097   6926  -3827  -3416   1306       C  
ATOM    536  O   VAL A1069      21.439   7.091   3.609  1.00 95.21           O  
ANISOU  536  O   VAL A1069    14394  14342   7440  -3907  -3643   1436       O  
ATOM    537  CB  VAL A1069      18.952   9.174   2.823  1.00 91.82           C  
ANISOU  537  CB  VAL A1069    14814  13304   6770  -3780  -2914    743       C  
ATOM    538  CG1 VAL A1069      20.232   9.994   2.932  1.00 95.67           C  
ANISOU  538  CG1 VAL A1069    15204  13675   7471  -4177  -3237    656       C  
ATOM    539  CG2 VAL A1069      18.148   9.610   1.599  1.00 88.45           C  
ANISOU  539  CG2 VAL A1069    14461  12577   6569  -3572  -2554    735       C  
ATOM    540  N   GLY A1070      19.705   6.953   5.058  1.00 92.01           N  
ANISOU  540  N   GLY A1070    14601  14193   6166  -3874  -3549   1336       N  
ATOM    541  CA  GLY A1070      20.514   6.483   6.172  1.00 96.72           C  
ANISOU  541  CA  GLY A1070    15078  15186   6484  -4034  -4038   1594       C  
ATOM    542  C   GLY A1070      21.211   5.174   5.862  1.00100.47           C  
ANISOU  542  C   GLY A1070    15205  15577   7393  -3814  -4252   2140       C  
ATOM    543  O   GLY A1070      22.409   5.016   6.122  1.00103.37           O  
ANISOU  543  O   GLY A1070    15221  16124   7932  -3834  -4673   2306       O  
ATOM    544  N   GLN A1071      20.467   4.236   5.276  1.00 94.39           N  
ANISOU  544  N   GLN A1071    14501  14516   6846  -3578  -3987   2368       N  
ATOM    545  CA  GLN A1071      21.002   2.923   4.922  1.00 96.07           C  
ANISOU  545  CA  GLN A1071    14468  14451   7582  -3281  -4186   2785       C  
ATOM    546  C   GLN A1071      22.012   3.041   3.788  1.00 99.23           C  
ANISOU  546  C   GLN A1071    14389  14706   8608  -3047  -4120   2547       C  
ATOM    547  O   GLN A1071      23.008   2.310   3.758  1.00102.80           O  
ANISOU  547  O   GLN A1071    14452  15136   9473  -2762  -4447   2752       O  
ATOM    548  CB  GLN A1071      19.869   1.978   4.524  1.00 95.46           C  
ANISOU  548  CB  GLN A1071    14637  14027   7606  -3194  -3908   2964       C  
ATOM    549  CG  GLN A1071      18.820   1.768   5.603  1.00116.14           C  
ANISOU  549  CG  GLN A1071    17631  16943   9553  -3509  -3914   3270       C  
ATOM    550  CD  GLN A1071      17.704   0.882   5.123  1.00139.34           C  
ANISOU  550  CD  GLN A1071    20745  19573  12626  -3554  -3632   3438       C  
ATOM    551  OE1 GLN A1071      16.642   1.373   4.778  1.00132.19           O  
ANISOU  551  OE1 GLN A1071    19926  18848  11452  -3666  -3198   3122       O  
ATOM    552  NE2 GLN A1071      17.910  -0.430   5.074  1.00137.46           N  
ANISOU  552  NE2 GLN A1071    20549  18832  12847  -3466  -3908   3919       N  
ATOM    553  N   ILE A1072      21.749   3.956   2.850  1.00 92.18           N  
ANISOU  553  N   ILE A1072    13485  13774   7766  -3148  -3704   2144       N  
ATOM    554  CA  ILE A1072      22.641   4.204   1.720  1.00 92.30           C  
ANISOU  554  CA  ILE A1072    13014  13839   8216  -3061  -3560   1944       C  
ATOM    555  C   ILE A1072      23.964   4.712   2.254  1.00101.62           C  
ANISOU  555  C   ILE A1072    13795  15394   9420  -3258  -3957   1975       C  
ATOM    556  O   ILE A1072      25.010   4.224   1.837  1.00105.18           O  
ANISOU  556  O   ILE A1072    13653  16050  10262  -3029  -4082   2005       O  
ATOM    557  CB  ILE A1072      21.999   5.192   0.707  1.00 91.15           C  
ANISOU  557  CB  ILE A1072    13016  13616   8000  -3238  -3092   1669       C  
ATOM    558  CG1 ILE A1072      20.844   4.499  -0.061  1.00 87.54           C  
ANISOU  558  CG1 ILE A1072    12748  12934   7578  -3000  -2724   1619       C  
ATOM    559  CG2 ILE A1072      23.041   5.720  -0.283  1.00 93.00           C  
ANISOU  559  CG2 ILE A1072    12737  14096   8503  -3366  -2979   1565       C  
ATOM    560  CD1 ILE A1072      20.058   5.403  -1.021  1.00 88.80           C  
ANISOU  560  CD1 ILE A1072    13057  13079   7604  -3109  -2328   1447       C  
ATOM    561  N   ASP A1073      23.920   5.645   3.212  1.00 99.72           N  
ANISOU  561  N   ASP A1073    13832  15305   8753  -3663  -4175   1905       N  
ATOM    562  CA  ASP A1073      25.127   6.215   3.807  1.00104.96           C  
ANISOU  562  CA  ASP A1073    14135  16375   9370  -3988  -4608   1882       C  
ATOM    563  C   ASP A1073      25.929   5.136   4.548  1.00113.33           C  
ANISOU  563  C   ASP A1073    14804  17751  10506  -3688  -5127   2259       C  
ATOM    564  O   ASP A1073      27.162   5.143   4.490  1.00117.03           O  
ANISOU  564  O   ASP A1073    14620  18626  11218  -3702  -5420   2295       O  
ATOM    565  CB  ASP A1073      24.763   7.373   4.751  1.00108.43           C  
ANISOU  565  CB  ASP A1073    15057  16847   9297  -4471  -4758   1599       C  
ATOM    566  CG  ASP A1073      24.314   8.627   4.012  1.00117.64           C  
ANISOU  566  CG  ASP A1073    16524  17614  10559  -4761  -4402   1247       C  
ATOM    567  OD1 ASP A1073      24.616   8.741   2.801  1.00118.66           O  
ANISOU  567  OD1 ASP A1073    16359  17636  11091  -4764  -4122   1316       O  
ATOM    568  OD2 ASP A1073      23.726   9.527   4.662  1.00121.12           O  
ANISOU  568  OD2 ASP A1073    17475  17879  10666  -4987  -4442    899       O  
ATOM    569  N   ASP A1074      25.232   4.188   5.192  1.00110.51           N  
ANISOU  569  N   ASP A1074    14797  17223   9966  -3418  -5254   2598       N  
ATOM    570  CA  ASP A1074      25.871   3.071   5.885  1.00116.90           C  
ANISOU  570  CA  ASP A1074    15340  18175  10900  -3073  -5807   3113       C  
ATOM    571  C   ASP A1074      26.600   2.177   4.895  1.00120.22           C  
ANISOU  571  C   ASP A1074    15186  18382  12109  -2476  -5777   3138       C  
ATOM    572  O   ASP A1074      27.713   1.720   5.175  1.00126.31           O  
ANISOU  572  O   ASP A1074    15373  19457  13161  -2169  -6259   3353       O  
ATOM    573  CB  ASP A1074      24.832   2.261   6.671  1.00120.34           C  
ANISOU  573  CB  ASP A1074    16357  18386  10980  -3027  -5896   3570       C  
ATOM    574  CG  ASP A1074      24.247   3.000   7.861  1.00142.44           C  
ANISOU  574  CG  ASP A1074    19591  21657  12872  -3547  -5996   3537       C  
ATOM    575  OD1 ASP A1074      24.999   3.767   8.518  1.00148.90           O  
ANISOU  575  OD1 ASP A1074    20211  23020  13344  -3856  -6347   3362       O  
ATOM    576  OD2 ASP A1074      23.076   2.733   8.205  1.00149.40           O  
ANISOU  576  OD2 ASP A1074    20959  22455  13350  -3658  -5765   3681       O  
ATOM    577  N   ALA A1075      25.978   1.941   3.731  1.00110.34           N  
ANISOU  577  N   ALA A1075    14047  16689  11188  -2275  -5222   2856       N  
ATOM    578  CA  ALA A1075      26.575   1.140   2.671  1.00111.65           C  
ANISOU  578  CA  ALA A1075    13677  16702  12042  -1692  -5090   2668       C  
ATOM    579  C   ALA A1075      27.756   1.879   2.052  1.00116.97           C  
ANISOU  579  C   ALA A1075    13557  18034  12852  -1796  -5002   2343       C  
ATOM    580  O   ALA A1075      28.751   1.249   1.691  1.00122.78           O  
ANISOU  580  O   ALA A1075    13570  19012  14069  -1276  -5158   2262       O  
ATOM    581  CB  ALA A1075      25.536   0.813   1.619  1.00106.85           C  
ANISOU  581  CB  ALA A1075    13415  15602  11580  -1585  -4521   2375       C  
ATOM    582  N   LEU A1076      27.655   3.217   1.946  1.00109.21           N  
ANISOU  582  N   LEU A1076    12685  17340  11470  -2474  -4772   2163       N  
ATOM    583  CA  LEU A1076      28.731   4.046   1.415  1.00111.94           C  
ANISOU  583  CA  LEU A1076    12324  18325  11881  -2815  -4700   1960       C  
ATOM    584  C   LEU A1076      29.967   3.969   2.288  1.00124.43           C  
ANISOU  584  C   LEU A1076    13267  20501  13509  -2812  -5324   2146       C  
ATOM    585  O   LEU A1076      31.086   3.902   1.768  1.00129.60           O  
ANISOU  585  O   LEU A1076    13000  21783  14460  -2683  -5341   2024       O  
ATOM    586  CB  LEU A1076      28.301   5.512   1.278  1.00108.15           C  
ANISOU  586  CB  LEU A1076    12259  17805  11027  -3611  -4451   1830       C  
ATOM    587  CG  LEU A1076      27.705   5.998  -0.042  1.00107.72           C  
ANISOU  587  CG  LEU A1076    12355  17581  10993  -3764  -3825   1653       C  
ATOM    588  CD1 LEU A1076      28.675   5.802  -1.229  1.00111.32           C  
ANISOU  588  CD1 LEU A1076    11908  18672  11718  -3668  -3537   1520       C  
ATOM    589  CD2 LEU A1076      26.386   5.502  -0.292  1.00104.47           C  
ANISOU  589  CD2 LEU A1076    12573  16608  10512  -3434  -3536   1621       C  
ATOM    590  N   LYS A1077      29.770   3.981   3.619  1.00122.95           N  
ANISOU  590  N   LYS A1077    13495  20261  12959  -2967  -5839   2435       N  
ATOM    591  CA  LYS A1077      30.875   3.884   4.563  1.00131.37           C  
ANISOU  591  CA  LYS A1077    13982  21971  13963  -2981  -6533   2671       C  
ATOM    592  C   LYS A1077      31.629   2.584   4.336  1.00142.23           C  
ANISOU  592  C   LYS A1077    14652  23451  15939  -2061  -6800   2870       C  
ATOM    593  O   LYS A1077      32.855   2.579   4.293  1.00149.16           O  
ANISOU  593  O   LYS A1077    14568  25063  17045  -1928  -7095   2839       O  
ATOM    594  CB  LYS A1077      30.367   3.977   6.004  1.00134.94           C  
ANISOU  594  CB  LYS A1077    15077  22396  13798  -3257  -7012   2966       C  
ATOM    595  CG  LYS A1077      31.506   4.024   7.014  1.00160.88           C  
ANISOU  595  CG  LYS A1077    17759  26495  16874  -3396  -7787   3202       C  
ATOM    596  CD  LYS A1077      31.021   4.108   8.453  1.00174.74           C  
ANISOU  596  CD  LYS A1077    20119  28417  17859  -3712  -8265   3479       C  
ATOM    597  CE  LYS A1077      32.165   4.245   9.450  1.00193.48           C  
ANISOU  597  CE  LYS A1077    21861  31742  19910  -3938  -9084   3683       C  
ATOM    598  NZ  LYS A1077      33.091   3.075   9.462  1.00206.62           N  
ANISOU  598  NZ  LYS A1077    22755  33633  22121  -3056  -9568   4165       N  
ATOM    599  N   LEU A1078      30.884   1.490   4.155  1.00137.45           N  
ANISOU  599  N   LEU A1078    14501  22089  15633  -1422  -6700   3032       N  
ATOM    600  CA  LEU A1078      31.453   0.171   3.905  1.00144.22           C  
ANISOU  600  CA  LEU A1078    14857  22742  17197   -432  -6969   3156       C  
ATOM    601  C   LEU A1078      32.248   0.156   2.605  1.00151.59           C  
ANISOU  601  C   LEU A1078    14869  24112  18616    -67  -6532   2569       C  
ATOM    602  O   LEU A1078      33.391  -0.302   2.592  1.00160.19           O  
ANISOU  602  O   LEU A1078    15008  25733  20125    519  -6877   2539       O  
ATOM    603  CB  LEU A1078      30.337  -0.881   3.858  1.00141.27           C  
ANISOU  603  CB  LEU A1078    15310  21299  17067    -18  -6879   3369       C  
ATOM    604  CG  LEU A1078      29.606  -1.125   5.173  1.00146.06           C  
ANISOU  604  CG  LEU A1078    16712  21588  17196   -305  -7342   4072       C  
ATOM    605  CD1 LEU A1078      28.340  -1.906   4.949  1.00141.90           C  
ANISOU  605  CD1 LEU A1078    17011  20097  16809   -209  -7072   4212       C  
ATOM    606  CD2 LEU A1078      30.509  -1.829   6.182  1.00160.44           C  
ANISOU  606  CD2 LEU A1078    18148  23633  19179    156  -8241   4732       C  
ATOM    607  N   ALA A1079      31.658   0.681   1.522  1.00142.31           N  
ANISOU  607  N   ALA A1079    13906  22842  17324   -412  -5782   2114       N  
ATOM    608  CA  ALA A1079      32.311   0.746   0.215  1.00145.25           C  
ANISOU  608  CA  ALA A1079    13427  23800  17962   -203  -5266   1554       C  
ATOM    609  C   ALA A1079      33.575   1.598   0.278  1.00157.19           C  
ANISOU  609  C   ALA A1079    13931  26474  19319   -663  -5401   1526       C  
ATOM    610  O   ALA A1079      34.583   1.252  -0.342  1.00164.38           O  
ANISOU  610  O   ALA A1079    13753  28136  20569   -184  -5310   1206       O  
ATOM    611  CB  ALA A1079      31.351   1.308  -0.816  1.00137.55           C  
ANISOU  611  CB  ALA A1079    12970  22596  16696   -673  -4521   1246       C  
ATOM    612  N   ASN A1080      33.538   2.690   1.058  1.00153.29           N  
ANISOU  612  N   ASN A1080    13755  26168  18320  -1593  -5638   1806       N  
ATOM    613  CA  ASN A1080      34.690   3.573   1.207  1.00160.48           C  
ANISOU  613  CA  ASN A1080    13785  28123  19066  -2239  -5834   1801       C  
ATOM    614  C   ASN A1080      35.819   2.910   1.997  1.00176.17           C  
ANISOU  614  C   ASN A1080    14868  30749  21319  -1665  -6563   1998       C  
ATOM    615  O   ASN A1080      36.963   3.366   1.923  1.00183.54           O  
ANISOU  615  O   ASN A1080    14726  32764  22249  -1990  -6705   1916       O  
ATOM    616  CB  ASN A1080      34.298   4.868   1.879  1.00159.10           C  
ANISOU  616  CB  ASN A1080    14300  27803  18348  -3359  -5964   1946       C  
ATOM    617  CG  ASN A1080      34.282   6.023   0.916  1.00180.28           C  
ANISOU  617  CG  ASN A1080    16943  30687  20866  -4241  -5400   1760       C  
ATOM    618  OD1 ASN A1080      33.228   6.430   0.412  1.00163.90           O  
ANISOU  618  OD1 ASN A1080    15711  27918  18644  -4467  -4948   1710       O  
ATOM    619  ND2 ASN A1080      35.468   6.539   0.593  1.00180.96           N  
ANISOU  619  ND2 ASN A1080    15981  31790  20987  -4753  -5429   1713       N  
ATOM    620  N   GLU A1081      35.506   1.836   2.732  1.00174.66           N  
ANISOU  620  N   GLU A1081    15069  29931  21363   -845  -7050   2316       N  
ATOM    621  CA  GLU A1081      36.493   1.080   3.496  1.00185.41           C  
ANISOU  621  CA  GLU A1081    15644  31770  23033   -132  -7837   2627       C  
ATOM    622  C   GLU A1081      37.006  -0.109   2.671  1.00196.71           C  
ANISOU  622  C   GLU A1081    16301  33168  25270   1153  -7716   2316       C  
ATOM    623  O   GLU A1081      37.867  -0.859   3.137  1.00206.86           O  
ANISOU  623  O   GLU A1081    16823  34788  26987   1998  -8358   2524       O  
ATOM    624  CB  GLU A1081      35.896   0.604   4.826  1.00186.44           C  
ANISOU  624  CB  GLU A1081    16661  31253  22927    -14  -8523   3283       C  
ATOM    625  CG  GLU A1081      35.499   1.737   5.758  1.00192.55           C  
ANISOU  625  CG  GLU A1081    18075  32231  22854  -1174  -8706   3448       C  
ATOM    626  CD  GLU A1081      34.918   1.292   7.086  1.00214.08           C  
ANISOU  626  CD  GLU A1081    21596  34584  25161  -1132  -9334   4083       C  
ATOM    627  OE1 GLU A1081      34.007   0.430   7.087  1.00205.98           O  
ANISOU  627  OE1 GLU A1081    21331  32614  24318   -644  -9233   4364       O  
ATOM    628  OE2 GLU A1081      35.333   1.853   8.125  1.00210.72           O  
ANISOU  628  OE2 GLU A1081    21148  34727  24190  -1569  -9828   4105       O  
ATOM    629  N   GLY A1082      36.478  -0.254   1.453  1.00188.70           N  
ANISOU  629  N   GLY A1082    15471  31786  24439   1319  -6924   1779       N  
ATOM    630  CA  GLY A1082      36.853  -1.319   0.529  1.00195.16           C  
ANISOU  630  CA  GLY A1082    15634  32548  25969   2501  -6681   1243       C  
ATOM    631  C   GLY A1082      36.105  -2.618   0.748  1.00199.85           C  
ANISOU  631  C   GLY A1082    17072  31726  27137   3446  -6958   1386       C  
ATOM    632  O   GLY A1082      36.434  -3.635   0.130  1.00206.75           O  
ANISOU  632  O   GLY A1082    17484  32334  28736   4571  -6911    906       O  
ATOM    633  N   LYS A1083      35.080  -2.591   1.610  1.00189.96           N  
ANISOU  633  N   LYS A1083    17054  29557  25566   2967  -7233   2005       N  
ATOM    634  CA  LYS A1083      34.291  -3.773   1.951  1.00190.78           C  
ANISOU  634  CA  LYS A1083    18060  28285  26145   3610  -7554   2332       C  
ATOM    635  C   LYS A1083      33.175  -3.987   0.930  1.00187.29           C  
ANISOU  635  C   LYS A1083    18352  27049  25761   3508  -6809   1801       C  
ATOM    636  O   LYS A1083      32.001  -3.773   1.239  1.00178.26           O  
ANISOU  636  O   LYS A1083    18263  25272  24196   2848  -6670   2120       O  
ATOM    637  CB  LYS A1083      33.712  -3.628   3.362  1.00190.91           C  
ANISOU  637  CB  LYS A1083    18953  27935  25649   3030  -8158   3276       C  
ATOM    638  CG  LYS A1083      34.773  -3.390   4.423  1.00214.83           C  
ANISOU  638  CG  LYS A1083    21283  31855  28486   3041  -8959   3814       C  
ATOM    639  CD  LYS A1083      34.163  -3.227   5.804  1.00223.92           C  
ANISOU  639  CD  LYS A1083    23304  32816  28960   2408  -9512   4686       C  
ATOM    640  CE  LYS A1083      35.205  -2.963   6.871  1.00235.46           C  
ANISOU  640  CE  LYS A1083    24638  35214  29613   3006  -9577   3941       C  
ATOM    641  NZ  LYS A1083      36.190  -4.068   6.996  1.00246.20           N  
ANISOU  641  NZ  LYS A1083    25945  36447  31152   4320  -9081   3255       N  
ATOM    642  N   VAL A1084      33.546  -4.437  -0.279  1.00188.41           N  
ANISOU  642  N   VAL A1084    17868  27332  26389   4186  -6342    948       N  
ATOM    643  CA  VAL A1084      32.615  -4.679  -1.389  1.00182.93           C  
ANISOU  643  CA  VAL A1084    17696  26085  25723   4140  -5641    301       C  
ATOM    644  C   VAL A1084      31.471  -5.612  -0.965  1.00185.91           C  
ANISOU  644  C   VAL A1084    19274  24933  26429   4268  -5923    664       C  
ATOM    645  O   VAL A1084      30.307  -5.241  -1.092  1.00176.04           O  
ANISOU  645  O   VAL A1084    18864  23328  24695   3506  -5553    754       O  
ATOM    646  CB  VAL A1084      33.331  -5.270  -2.623  1.00195.24           C  
ANISOU  646  CB  VAL A1084    18312  28059  27811   5065  -5237   -742       C  
ATOM    647  CG1 VAL A1084      32.346  -5.495  -3.765  1.00189.88           C  
ANISOU  647  CG1 VAL A1084    18181  26930  27035   4931  -4544  -1450       C  
ATOM    648  CG2 VAL A1084      34.472  -4.377  -3.073  1.00198.34           C  
ANISOU  648  CG2 VAL A1084    17408  30126  27825   4844  -4914  -1050       C  
ATOM    649  N   LYS A1085      31.803  -6.822  -0.500  1.00193.32           N  
ANISOU  649  N   LYS A1085    20256  24978  28218   5222  -6587    885       N  
ATOM    650  CA  LYS A1085      30.816  -7.823  -0.109  1.00194.34           C  
ANISOU  650  CA  LYS A1085    21487  23575  28777   5318  -6928   1304       C  
ATOM    651  C   LYS A1085      29.848  -7.276   0.949  1.00190.75           C  
ANISOU  651  C   LYS A1085    21956  22980  27541   4231  -7092   2288       C  
ATOM    652  O   LYS A1085      28.641  -7.483   0.814  1.00184.32           O  
ANISOU  652  O   LYS A1085    22018  21440  26575   3723  -6836   2349       O  
ATOM    653  CB  LYS A1085      31.515  -9.088   0.424  1.00211.17           C  
ANISOU  653  CB  LYS A1085    23475  24790  31968   6494  -7796   1633       C  
ATOM    654  CG  LYS A1085      30.585 -10.159   1.016  1.00221.11           C  
ANISOU  654  CG  LYS A1085    25938  24937  33136   6364  -7486   2518       C  
ATOM    655  CD  LYS A1085      29.552 -10.702   0.024  1.00225.13           C  
ANISOU  655  CD  LYS A1085    27124  24719  33695   6122  -6570   1898       C  
ATOM    656  CE  LYS A1085      28.602 -11.694   0.658  1.00231.84           C  
ANISOU  656  CE  LYS A1085    29091  24876  34121   5826  -5789   2769       C  
ATOM    657  NZ  LYS A1085      27.769 -11.084   1.735  1.00232.79           N  
ANISOU  657  NZ  LYS A1085    29792  25180  33478   4889  -6087   3563       N  
ATOM    658  N   GLU A1086      30.365  -6.602   1.994  1.00188.93           N  
ANISOU  658  N   GLU A1086    21479  23519  26786   3876  -7516   2989       N  
ATOM    659  CA  GLU A1086      29.507  -6.053   3.043  1.00182.90           C  
ANISOU  659  CA  GLU A1086    21506  22799  25190   2898  -7655   3797       C  
ATOM    660  C   GLU A1086      28.603  -4.967   2.505  1.00176.14           C  
ANISOU  660  C   GLU A1086    20978  22377  23570   1979  -6851   3361       C  
ATOM    661  O   GLU A1086      27.439  -4.909   2.897  1.00170.60           O  
ANISOU  661  O   GLU A1086    21107  21282  22433   1361  -6729   3711       O  
ATOM    662  CB  GLU A1086      30.305  -5.496   4.217  1.00187.99           C  
ANISOU  662  CB  GLU A1086    21756  24319  25351   2694  -8265   4458       C  
ATOM    663  CG  GLU A1086      30.931  -6.552   5.101  1.00211.24           C  
ANISOU  663  CG  GLU A1086    24613  26796  28852   3442  -9237   5275       C  
ATOM    664  CD  GLU A1086      31.450  -5.984   6.407  1.00228.35           C  
ANISOU  664  CD  GLU A1086    26702  30383  29678   3398  -8982   5484       C  
ATOM    665  OE1 GLU A1086      30.641  -5.401   7.166  1.00222.32           O  
ANISOU  665  OE1 GLU A1086    26557  29621  28295   2363  -9272   6065       O  
ATOM    666  OE2 GLU A1086      32.647  -6.190   6.706  1.00227.45           O  
ANISOU  666  OE2 GLU A1086    25813  30881  29727   4110  -9428   5541       O  
ATOM    667  N   ALA A1087      29.129  -4.105   1.615  1.00170.17           N  
ANISOU  667  N   ALA A1087    19541  22471  22643   1880  -6320   2650       N  
ATOM    668  CA  ALA A1087      28.346  -3.026   1.019  1.00159.81           C  
ANISOU  668  CA  ALA A1087    18507  21534  20678   1079  -5612   2291       C  
ATOM    669  C   ALA A1087      27.249  -3.601   0.138  1.00160.70           C  
ANISOU  669  C   ALA A1087    19171  20906  20982   1122  -5146   1903       C  
ATOM    670  O   ALA A1087      26.122  -3.112   0.173  1.00152.69           O  
ANISOU  670  O   ALA A1087    18788  19780  19448    475  -4831   2002       O  
ATOM    671  CB  ALA A1087      29.243  -2.101   0.220  1.00160.14           C  
ANISOU  671  CB  ALA A1087    17677  22598  20571    957  -5224   1755       C  
ATOM    672  N   GLN A1088      27.560  -4.671  -0.616  1.00164.20           N  
ANISOU  672  N   GLN A1088    19360  20846  22184   1913  -5142   1416       N  
ATOM    673  CA  GLN A1088      26.579  -5.329  -1.473  1.00162.42           C  
ANISOU  673  CA  GLN A1088    19630  19896  22187   1952  -4771    943       C  
ATOM    674  C   GLN A1088      25.472  -5.936  -0.633  1.00166.76           C  
ANISOU  674  C   GLN A1088    21139  19487  22738   1591  -5096   1624       C  
ATOM    675  O   GLN A1088      24.301  -5.820  -0.993  1.00160.50           O  
ANISOU  675  O   GLN A1088    20871  18497  21613   1049  -4710   1506       O  
ATOM    676  CB  GLN A1088      27.234  -6.399  -2.341  1.00172.99           C  
ANISOU  676  CB  GLN A1088    20502  20839  24389   2935  -4786    177       C  
ATOM    677  CG  GLN A1088      28.202  -5.846  -3.374  1.00184.04           C  
ANISOU  677  CG  GLN A1088    20870  23386  25670   3228  -4303   -622       C  
ATOM    678  CD  GLN A1088      28.830  -6.946  -4.190  1.00210.25           C  
ANISOU  678  CD  GLN A1088    23683  26390  29813   4301  -4297  -1522       C  
ATOM    679  OE1 GLN A1088      29.476  -7.861  -3.660  1.00216.20           O  
ANISOU  679  OE1 GLN A1088    24283  26485  31379   5161  -4905  -1394       O  
ATOM    680  NE2 GLN A1088      28.703  -6.849  -5.508  1.00199.23           N  
ANISOU  680  NE2 GLN A1088    21963  25532  28203   4321  -3625  -2480       N  
ATOM    681  N   ALA A1089      25.839  -6.561   0.499  1.00171.10           N  
ANISOU  681  N   ALA A1089    21862  19549  23597   1842  -5820   2401       N  
ATOM    682  CA  ALA A1089      24.876  -7.155   1.420  1.00172.52           C  
ANISOU  682  CA  ALA A1089    22907  18944  23701   1401  -6180   3234       C  
ATOM    683  C   ALA A1089      23.977  -6.085   2.003  1.00168.13           C  
ANISOU  683  C   ALA A1089    22710  19082  22089    430  -5878   3596       C  
ATOM    684  O   ALA A1089      22.767  -6.280   2.085  1.00164.28           O  
ANISOU  684  O   ALA A1089    22832  18246  21343   -123  -5686   3788       O  
ATOM    685  CB  ALA A1089      25.600  -7.901   2.527  1.00183.78           C  
ANISOU  685  CB  ALA A1089    24350  19925  25552   1852  -7059   4109       C  
ATOM    686  N   ALA A1090      24.569  -4.931   2.368  1.00162.64           N  
ANISOU  686  N   ALA A1090    21594  19395  20808    224  -5826   3604       N  
ATOM    687  CA  ALA A1090      23.839  -3.790   2.914  1.00155.56           C  
ANISOU  687  CA  ALA A1090    20985  19163  18957   -577  -5552   3771       C  
ATOM    688  C   ALA A1090      22.831  -3.270   1.913  1.00151.83           C  
ANISOU  688  C   ALA A1090    20698  18753  18237   -922  -4834   3180       C  
ATOM    689  O   ALA A1090      21.706  -2.983   2.302  1.00147.48           O  
ANISOU  689  O   ALA A1090    20628  18261  17147  -1467  -4640   3388       O  
ATOM    690  CB  ALA A1090      24.802  -2.677   3.309  1.00155.67           C  
ANISOU  690  CB  ALA A1090    20484  20095  18569   -688  -5661   3707       C  
ATOM    691  N   ALA A1091      23.209  -3.190   0.621  1.00147.42           N  
ANISOU  691  N   ALA A1091    19710  18274  18031   -590  -4448   2457       N  
ATOM    692  CA  ALA A1091      22.327  -2.692  -0.436  1.00140.78           C  
ANISOU  692  CA  ALA A1091    18974  17596  16920   -882  -3814   1932       C  
ATOM    693  C   ALA A1091      21.103  -3.590  -0.630  1.00145.54           C  
ANISOU  693  C   ALA A1091    20121  17521  17656  -1045  -3725   1955       C  
ATOM    694  O   ALA A1091      20.045  -3.091  -0.996  1.00139.01           O  
ANISOU  694  O   ALA A1091    19521  16918  16380  -1476  -3324   1809       O  
ATOM    695  CB  ALA A1091      23.086  -2.583  -1.742  1.00142.38           C  
ANISOU  695  CB  ALA A1091    18555  18134  17410   -496  -3479   1223       C  
ATOM    696  N   GLU A1092      21.234  -4.897  -0.353  1.00150.85           N  
ANISOU  696  N   GLU A1092    21000  17348  18969   -726  -4145   2177       N  
ATOM    697  CA  GLU A1092      20.139  -5.862  -0.484  1.00153.55           C  
ANISOU  697  CA  GLU A1092    21882  16919  19540   -989  -4150   2250       C  
ATOM    698  C   GLU A1092      19.020  -5.560   0.526  1.00154.73           C  
ANISOU  698  C   GLU A1092    22510  17277  19002  -1749  -4156   2951       C  
ATOM    699  O   GLU A1092      17.888  -5.983   0.301  1.00153.96           O  
ANISOU  699  O   GLU A1092    22750  16912  18835  -2194  -3979   2947       O  
ATOM    700  CB  GLU A1092      20.686  -7.298  -0.281  1.00166.04           C  
ANISOU  700  CB  GLU A1092    23626  17384  22076   -460  -4726   2437       C  
ATOM    701  CG  GLU A1092      19.728  -8.477  -0.479  1.00184.98           C  
ANISOU  701  CG  GLU A1092    26616  18718  24950   -733  -4844   2477       C  
ATOM    702  CD  GLU A1092      18.745  -8.820   0.631  1.00212.40           C  
ANISOU  702  CD  GLU A1092    30706  21899  28099  -1517  -5109   3487       C  
ATOM    703  OE1 GLU A1092      19.027  -8.501   1.810  1.00207.04           O  
ANISOU  703  OE1 GLU A1092    30074  21587  27004  -1663  -5428   4326       O  
ATOM    704  OE2 GLU A1092      17.739  -9.502   0.330  1.00211.26           O  
ANISOU  704  OE2 GLU A1092    30973  21167  28128  -2011  -5039   3447       O  
ATOM    705  N   GLN A1093      19.321  -4.815   1.606  1.00150.23           N  
ANISOU  705  N   GLN A1093    21907  17297  17877  -1926  -4337   3469       N  
ATOM    706  CA  GLN A1093      18.361  -4.514   2.672  1.00149.22           C  
ANISOU  706  CA  GLN A1093    22147  17553  16995  -2586  -4335   4069       C  
ATOM    707  C   GLN A1093      17.557  -3.224   2.367  1.00144.44           C  
ANISOU  707  C   GLN A1093    21453  17761  15667  -2915  -3754   3623       C  
ATOM    708  O   GLN A1093      16.602  -2.934   3.089  1.00143.32           O  
ANISOU  708  O   GLN A1093    21533  18044  14877  -3405  -3630   3918       O  
ATOM    709  CB  GLN A1093      19.101  -4.373   4.021  1.00155.27           C  
ANISOU  709  CB  GLN A1093    22916  18632  17448  -2591  -4857   4763       C  
ATOM    710  CG  GLN A1093      18.240  -4.305   5.301  1.00177.58           C  
ANISOU  710  CG  GLN A1093    26106  21926  19438  -3261  -4951   5480       C  
ATOM    711  CD  GLN A1093      17.493  -5.578   5.661  1.00209.23           C  
ANISOU  711  CD  GLN A1093    30563  25286  23648  -3653  -5191   6211       C  
ATOM    712  OE1 GLN A1093      17.700  -6.665   5.094  1.00210.64           O  
ANISOU  712  OE1 GLN A1093    30883  24422  24727  -3380  -5436   6264       O  
ATOM    713  NE2 GLN A1093      16.651  -5.477   6.675  1.00205.67           N  
ANISOU  713  NE2 GLN A1093    30342  25452  22351  -4330  -5157   6803       N  
ATOM    714  N   LEU A1094      17.906  -2.482   1.304  1.00135.86           N  
ANISOU  714  N   LEU A1094    20028  16908  14683  -2640  -3409   2950       N  
ATOM    715  CA  LEU A1094      17.180  -1.262   0.934  1.00129.42           C  
ANISOU  715  CA  LEU A1094    19161  16702  13308  -2862  -2941   2594       C  
ATOM    716  C   LEU A1094      15.760  -1.570   0.492  1.00133.80           C  
ANISOU  716  C   LEU A1094    19893  17258  13687  -3178  -2620   2495       C  
ATOM    717  O   LEU A1094      14.834  -0.847   0.845  1.00131.49           O  
ANISOU  717  O   LEU A1094    19670  17478  12813  -3449  -2383   2510       O  
ATOM    718  CB  LEU A1094      17.904  -0.523  -0.188  1.00125.99           C  
ANISOU  718  CB  LEU A1094    18344  16466  13061  -2566  -2701   2056       C  
ATOM    719  CG  LEU A1094      19.298  -0.022   0.122  1.00131.92           C  
ANISOU  719  CG  LEU A1094    18783  17405  13934  -2357  -2954   2086       C  
ATOM    720  CD1 LEU A1094      19.928   0.575  -1.102  1.00130.33           C  
ANISOU  720  CD1 LEU A1094    18159  17468  13893  -2192  -2664   1622       C  
ATOM    721  CD2 LEU A1094      19.266   0.999   1.217  1.00132.58           C  
ANISOU  721  CD2 LEU A1094    19020  17889  13464  -2651  -3079   2298       C  
ATOM    722  N   LYS A1095      15.595  -2.654  -0.273  1.00133.45           N  
ANISOU  722  N   LYS A1095    19883  16661  14160  -3125  -2634   2330       N  
ATOM    723  CA  LYS A1095      14.315  -3.122  -0.803  1.00133.53           C  
ANISOU  723  CA  LYS A1095    20007  16641  14088  -3494  -2394   2187       C  
ATOM    724  C   LYS A1095      13.309  -3.330   0.337  1.00140.14           C  
ANISOU  724  C   LYS A1095    21098  17696  14453  -4064  -2451   2784       C  
ATOM    725  O   LYS A1095      12.121  -3.066   0.163  1.00139.37           O  
ANISOU  725  O   LYS A1095    20935  18087  13933  -4413  -2141   2683       O  
ATOM    726  CB  LYS A1095      14.525  -4.435  -1.590  1.00141.20           C  
ANISOU  726  CB  LYS A1095    21055  16793  15803  -3368  -2550   1903       C  
ATOM    727  CG  LYS A1095      15.674  -4.384  -2.614  1.00153.97           C  
ANISOU  727  CG  LYS A1095    22337  18303  17861  -2747  -2501   1279       C  
ATOM    728  CD  LYS A1095      15.863  -5.694  -3.371  1.00170.42           C  
ANISOU  728  CD  LYS A1095    24496  19569  20688  -2531  -2648    811       C  
ATOM    729  CE  LYS A1095      16.993  -5.596  -4.368  1.00178.74           C  
ANISOU  729  CE  LYS A1095    25098  20765  22049  -1884  -2522    104       C  
ATOM    730  NZ  LYS A1095      17.146  -6.844  -5.157  1.00194.31           N  
ANISOU  730  NZ  LYS A1095    27125  21976  24729  -1588  -2632   -567       N  
ATOM    731  N   THR A1096      13.793  -3.779   1.505  1.00139.83           N  
ANISOU  731  N   THR A1096    21279  17428  14420  -4160  -2850   3428       N  
ATOM    732  CA  THR A1096      12.954  -4.026   2.669  1.00143.27           C  
ANISOU  732  CA  THR A1096    21925  18213  14299  -4767  -2916   4093       C  
ATOM    733  C   THR A1096      12.305  -2.722   3.129  1.00141.03           C  
ANISOU  733  C   THR A1096    21448  19002  13137  -4865  -2538   3898       C  
ATOM    734  O   THR A1096      11.109  -2.706   3.409  1.00141.26           O  
ANISOU  734  O   THR A1096    21424  19595  12653  -5327  -2275   4004       O  
ATOM    735  CB  THR A1096      13.785  -4.657   3.783  1.00163.11           C  
ANISOU  735  CB  THR A1096    24683  20364  16930  -4779  -3476   4866       C  
ATOM    736  OG1 THR A1096      14.411  -5.840   3.289  1.00169.51           O  
ANISOU  736  OG1 THR A1096    25667  20043  18695  -4522  -3861   4962       O  
ATOM    737  CG2 THR A1096      12.964  -5.014   4.986  1.00169.67           C  
ANISOU  737  CG2 THR A1096    25728  21638  17102  -5501  -3563   5673       C  
ATOM    738  N   THR A1097      13.087  -1.633   3.199  1.00133.49           N  
ANISOU  738  N   THR A1097    20358  18320  12040  -4434  -2521   3574       N  
ATOM    739  CA  THR A1097      12.573  -0.331   3.628  1.00130.67           C  
ANISOU  739  CA  THR A1097    19882  18788  10979  -4418  -2223   3268       C  
ATOM    740  C   THR A1097      11.608   0.242   2.606  1.00129.05           C  
ANISOU  740  C   THR A1097    19467  18836  10730  -4315  -1779   2743       C  
ATOM    741  O   THR A1097      10.550   0.760   2.983  1.00129.50           O  
ANISOU  741  O   THR A1097    19407  19583  10215  -4454  -1498   2629       O  
ATOM    742  CB  THR A1097      13.710   0.649   3.866  1.00140.31           C  
ANISOU  742  CB  THR A1097    21068  20045  12198  -4059  -2387   3029       C  
ATOM    743  OG1 THR A1097      14.575   0.111   4.868  1.00144.81           O  
ANISOU  743  OG1 THR A1097    21763  20526  12733  -4154  -2856   3552       O  
ATOM    744  CG2 THR A1097      13.208   2.039   4.292  1.00139.10           C  
ANISOU  744  CG2 THR A1097    20875  20543  11434  -3995  -2129   2592       C  
ATOM    745  N   ARG A1098      11.972   0.157   1.320  1.00120.82           N  
ANISOU  745  N   ARG A1098    18323  17344  10241  -4042  -1724   2417       N  
ATOM    746  CA  ARG A1098      11.153   0.686   0.242  1.00116.56           C  
ANISOU  746  CA  ARG A1098    17564  17078   9646  -3925  -1380   1993       C  
ATOM    747  C   ARG A1098       9.780   0.042   0.232  1.00121.84           C  
ANISOU  747  C   ARG A1098    18132  18096  10066  -4351  -1204   2090       C  
ATOM    748  O   ARG A1098       8.792   0.760   0.155  1.00120.95           O  
ANISOU  748  O   ARG A1098    17790  18631   9533  -4307   -931   1889       O  
ATOM    749  CB  ARG A1098      11.817   0.491  -1.118  1.00114.40           C  
ANISOU  749  CB  ARG A1098    17180  16388   9900  -3665  -1373   1683       C  
ATOM    750  CG  ARG A1098      13.197   1.119  -1.219  1.00125.05           C  
ANISOU  750  CG  ARG A1098    18502  17525  11486  -3327  -1512   1599       C  
ATOM    751  CD  ARG A1098      13.665   1.296  -2.653  1.00136.49           C  
ANISOU  751  CD  ARG A1098    19719  18932  13211  -3097  -1366   1244       C  
ATOM    752  NE  ARG A1098      13.622   0.056  -3.421  1.00142.59           N  
ANISOU  752  NE  ARG A1098    20430  19405  14342  -3131  -1372   1045       N  
ATOM    753  CZ  ARG A1098      13.947  -0.026  -4.703  1.00148.68           C  
ANISOU  753  CZ  ARG A1098    20963  20262  15265  -2968  -1220    644       C  
ATOM    754  NH1 ARG A1098      14.357   1.052  -5.360  1.00130.84           N  
ANISOU  754  NH1 ARG A1098    18501  18397  12815  -2821  -1058    555       N  
ATOM    755  NH2 ARG A1098      13.869  -1.186  -5.339  1.00137.03           N  
ANISOU  755  NH2 ARG A1098    19465  18486  14113  -2989  -1242    320       N  
ATOM    756  N   ASN A1099       9.718  -1.300   0.347  1.00121.57           N  
ANISOU  756  N   ASN A1099    18251  17619  10319  -4770  -1392   2414       N  
ATOM    757  CA  ASN A1099       8.480  -2.088   0.336  1.00125.19           C  
ANISOU  757  CA  ASN A1099    18624  18328  10616  -5373  -1282   2577       C  
ATOM    758  C   ASN A1099       7.558  -1.696   1.513  1.00131.18           C  
ANISOU  758  C   ASN A1099    19238  20009  10595  -5716  -1099   2883       C  
ATOM    759  O   ASN A1099       6.357  -1.513   1.300  1.00132.51           O  
ANISOU  759  O   ASN A1099    19050  20909  10388  -5939   -807   2725       O  
ATOM    760  CB  ASN A1099       8.834  -3.585   0.396  1.00132.17           C  
ANISOU  760  CB  ASN A1099    19838  18295  12084  -5770  -1635   2946       C  
ATOM    761  CG  ASN A1099       7.724  -4.600   0.487  1.00168.50           C  
ANISOU  761  CG  ASN A1099    24459  22912  16651  -6588  -1638   3245       C  
ATOM    762  OD1 ASN A1099       6.565  -4.353   0.136  1.00166.55           O  
ANISOU  762  OD1 ASN A1099    23855  23420  16007  -6893  -1334   3031       O  
ATOM    763  ND2 ASN A1099       8.093  -5.814   0.868  1.00166.90           N  
ANISOU  763  ND2 ASN A1099    24664  21796  16955  -6960  -2031   3746       N  
ATOM    764  N   ALA A1100       8.114  -1.542   2.729  1.00127.74           N  
ANISOU  764  N   ALA A1100    19003  19676   9856  -5737  -1262   3265       N  
ATOM    765  CA  ALA A1100       7.317  -1.248   3.918  1.00131.23           C  
ANISOU  765  CA  ALA A1100    19290  21125   9447  -6092  -1073   3515       C  
ATOM    766  C   ALA A1100       6.890   0.231   4.014  1.00130.22           C  
ANISOU  766  C   ALA A1100    18856  21814   8809  -5556   -730   2885       C  
ATOM    767  O   ALA A1100       5.788   0.510   4.507  1.00133.56           O  
ANISOU  767  O   ALA A1100    18923  23249   8576  -5746   -410   2797       O  
ATOM    768  CB  ALA A1100       8.105  -1.611   5.156  1.00136.49           C  
ANISOU  768  CB  ALA A1100    20279  21693   9886  -6310  -1414   4129       C  
ATOM    769  N   TYR A1101       7.746   1.169   3.587  1.00120.22           N  
ANISOU  769  N   TYR A1101    17706  20123   7848  -4905   -807   2452       N  
ATOM    770  CA  TYR A1101       7.414   2.580   3.764  1.00119.00           C  
ANISOU  770  CA  TYR A1101    17382  20507   7324  -4387   -575   1879       C  
ATOM    771  C   TYR A1101       6.820   3.245   2.501  1.00119.84           C  
ANISOU  771  C   TYR A1101    17226  20594   7714  -3935   -371   1434       C  
ATOM    772  O   TYR A1101       5.818   3.970   2.610  1.00122.46           O  
ANISOU  772  O   TYR A1101    17229  21636   7665  -3663   -103   1085       O  
ATOM    773  CB  TYR A1101       8.661   3.356   4.173  1.00118.14           C  
ANISOU  773  CB  TYR A1101    17584  19969   7335  -4043   -827   1708       C  
ATOM    774  N   ILE A1102       7.438   3.038   1.326  1.00111.14           N  
ANISOU  774  N   ILE A1102    16226  18773   7228  -3806   -508   1434       N  
ATOM    775  CA  ILE A1102       7.038   3.773   0.127  1.00107.74           C  
ANISOU  775  CA  ILE A1102    15587  18359   6991  -3377   -384   1109       C  
ATOM    776  C   ILE A1102       6.123   2.962  -0.790  1.00111.76           C  
ANISOU  776  C   ILE A1102    15775  19147   7543  -3668   -273   1148       C  
ATOM    777  O   ILE A1102       5.229   3.562  -1.376  1.00112.45           O  
ANISOU  777  O   ILE A1102    15515  19736   7474  -3383   -122    931       O  
ATOM    778  CB  ILE A1102       8.269   4.242  -0.694  1.00106.31           C  
ANISOU  778  CB  ILE A1102    15638  17442   7313  -3082   -566   1049       C  
ATOM    779  CG1 ILE A1102       9.221   5.117   0.120  1.00106.05           C  
ANISOU  779  CG1 ILE A1102    15894  17116   7283  -2878   -723    971       C  
ATOM    780  CG2 ILE A1102       7.855   4.988  -1.931  1.00106.01           C  
ANISOU  780  CG2 ILE A1102    15408  17485   7387  -2717   -475    871       C  
ATOM    781  CD1 ILE A1102      10.093   4.391   1.017  1.00107.82           C  
ANISOU  781  CD1 ILE A1102    16324  17126   7517  -3192   -943   1234       C  
ATOM    782  N   GLN A1103       6.350   1.654  -0.963  1.00108.19           N  
ANISOU  782  N   GLN A1103    15436  18333   7341  -4193   -396   1389       N  
ATOM    783  CA  GLN A1103       5.593   0.833  -1.919  1.00108.79           C  
ANISOU  783  CA  GLN A1103    15261  18552   7520  -4551   -349   1319       C  
ATOM    784  C   GLN A1103       4.068   0.965  -1.753  1.00112.65           C  
ANISOU  784  C   GLN A1103    15237  20065   7500  -4757   -112   1274       C  
ATOM    785  O   GLN A1103       3.374   1.030  -2.759  1.00111.81           O  
ANISOU  785  O   GLN A1103    14774  20341   7369  -4715    -53   1053       O  
ATOM    786  CB  GLN A1103       5.969  -0.639  -1.792  1.00113.42           C  
ANISOU  786  CB  GLN A1103    16126  18493   8474  -5148   -557   1577       C  
ATOM    787  CG  GLN A1103       5.412  -1.536  -2.893  1.00137.33           C  
ANISOU  787  CG  GLN A1103    18999  21444  11735  -5540   -579   1351       C  
ATOM    788  CD  GLN A1103       5.934  -1.134  -4.250  1.00158.08           C  
ANISOU  788  CD  GLN A1103    21561  23917  14586  -5068   -577    898       C  
ATOM    789  OE1 GLN A1103       7.142  -1.156  -4.538  1.00148.24           O  
ANISOU  789  OE1 GLN A1103    20568  22037  13718  -4744   -696    797       O  
ATOM    790  NE2 GLN A1103       5.020  -0.778  -5.122  1.00158.12           N  
ANISOU  790  NE2 GLN A1103    21154  24622  14302  -5050   -447    644       N  
ATOM    791  N   LYS A1104       3.556   1.039  -0.516  1.00110.85           N  
ANISOU  791  N   LYS A1104    14896  20418   6805  -4964     24   1461       N  
ATOM    792  CA  LYS A1104       2.119   1.155  -0.267  1.00114.90           C  
ANISOU  792  CA  LYS A1104    14788  22093   6775  -5158    296   1391       C  
ATOM    793  C   LYS A1104       1.522   2.438  -0.891  1.00114.09           C  
ANISOU  793  C   LYS A1104    14260  22541   6548  -4329    433    944       C  
ATOM    794  O   LYS A1104       0.306   2.495  -1.069  1.00117.88           O  
ANISOU  794  O   LYS A1104    14095  23999   6693  -4383    610    823       O  
ATOM    795  CB  LYS A1104       1.819   1.134   1.249  1.00123.28           C  
ANISOU  795  CB  LYS A1104    15779  23822   7241  -5458    464   1623       C  
ATOM    796  CG  LYS A1104       2.416   2.272   2.084  1.00140.16           C  
ANISOU  796  CG  LYS A1104    18133  25969   9154  -4782    502   1370       C  
ATOM    797  CD  LYS A1104       2.095   2.080   3.570  1.00159.86           C  
ANISOU  797  CD  LYS A1104    20523  29306  10909  -5213    674   1587       C  
ATOM    798  CE  LYS A1104       2.593   3.192   4.471  1.00173.81           C  
ANISOU  798  CE  LYS A1104    22471  31226  12344  -4601    714   1186       C  
ATOM    799  NZ  LYS A1104       4.074   3.331   4.465  1.00178.76           N  
ANISOU  799  NZ  LYS A1104    23768  30698  13454  -4410    343   1284       N  
ATOM    800  N   TYR A1105       2.374   3.431  -1.255  1.00103.45           N  
ANISOU  800  N   TYR A1105    13248  20555   5503  -3601    309    757       N  
ATOM    801  CA  TYR A1105       1.922   4.702  -1.820  1.00102.79           C  
ANISOU  801  CA  TYR A1105    12897  20746   5412  -2776    342    453       C  
ATOM    802  C   TYR A1105       2.057   4.787  -3.342  1.00102.87           C  
ANISOU  802  C   TYR A1105    12873  20474   5741  -2609    172    482       C  
ATOM    803  O   TYR A1105       1.814   5.855  -3.894  1.00103.78           O  
ANISOU  803  O   TYR A1105    12855  20668   5908  -1926    111    384       O  
ATOM    804  CB  TYR A1105       2.692   5.875  -1.226  1.00102.73           C  
ANISOU  804  CB  TYR A1105    13303  20208   5523  -2142    279    264       C  
ATOM    805  CG  TYR A1105       2.523   6.026   0.267  1.00109.44           C  
ANISOU  805  CG  TYR A1105    14148  21507   5926  -2180    449     94       C  
ATOM    806  CD1 TYR A1105       1.263   6.201   0.831  1.00118.51           C  
ANISOU  806  CD1 TYR A1105    14683  23796   6549  -2042    735   -163       C  
ATOM    807  CD2 TYR A1105       3.627   6.127   1.103  1.00108.27           C  
ANISOU  807  CD2 TYR A1105    14540  20780   5819  -2282    322    125       C  
ATOM    808  CE1 TYR A1105       1.101   6.376   2.202  1.00124.78           C  
ANISOU  808  CE1 TYR A1105    15418  25195   6796  -2076    938   -392       C  
ATOM    809  CE2 TYR A1105       3.480   6.317   2.475  1.00113.66           C  
ANISOU  809  CE2 TYR A1105    15208  22016   5962  -2326    463    -75       C  
ATOM    810  CZ  TYR A1105       2.213   6.450   3.021  1.00129.36           C  
ANISOU  810  CZ  TYR A1105    16601  25185   7365  -2221    793   -355       C  
ATOM    811  OH  TYR A1105       2.051   6.663   4.374  1.00136.60           O  
ANISOU  811  OH  TYR A1105    17446  26837   7618  -2265    981   -628       O  
ATOM    812  N   LEU A1106       2.382   3.692  -4.021  1.00 96.42           N  
ANISOU  812  N   LEU A1106    12157  19373   5104  -3204     79    601       N  
ATOM    813  CA  LEU A1106       2.477   3.698  -5.476  1.00 94.05           C  
ANISOU  813  CA  LEU A1106    11766  19020   4947  -3117    -52    553       C  
ATOM    814  C   LEU A1106       1.371   2.814  -6.044  1.00102.78           C  
ANISOU  814  C   LEU A1106    12349  20885   5819  -3656    -29    463       C  
ATOM    815  O   LEU A1106       0.684   3.225  -6.964  1.00105.47           O  
ANISOU  815  O   LEU A1106    12255  21850   5969  -3407    -89    394       O  
ATOM    816  CB  LEU A1106       3.867   3.255  -5.952  1.00 89.07           C  
ANISOU  816  CB  LEU A1106    11642  17492   4708  -3273   -180    579       C  
ATOM    817  CG  LEU A1106       5.027   4.158  -5.539  1.00 88.64           C  
ANISOU  817  CG  LEU A1106    12026  16764   4888  -2836   -241    678       C  
ATOM    818  CD1 LEU A1106       5.690   3.644  -4.368  1.00 87.82           C  
ANISOU  818  CD1 LEU A1106    12257  16198   4911  -3096   -259    760       C  
ATOM    819  CD2 LEU A1106       6.121   4.073  -6.540  1.00 86.58           C  
ANISOU  819  CD2 LEU A1106    11963  16047   4888  -2834   -337    677       C  
ATOM    820  N   MET A 123       1.102   1.692  -5.365  1.00116.00           N  
ANISOU  820  N   MET A 123    13373  25901   4799  -4340   2147  -2525       N  
ATOM    821  CA  MET A 123       0.047   0.762  -5.717  1.00117.33           C  
ANISOU  821  CA  MET A 123    13299  26408   4874  -4510   2224  -2521       C  
ATOM    822  C   MET A 123      -1.287   1.209  -5.091  1.00124.91           C  
ANISOU  822  C   MET A 123    13961  27985   5512  -4462   2377  -2866       C  
ATOM    823  O   MET A 123      -1.616   0.810  -3.966  1.00127.91           O  
ANISOU  823  O   MET A 123    14254  28740   5606  -4807   2453  -2875       O  
ATOM    824  CB  MET A 123       0.415  -0.666  -5.268  1.00120.00           C  
ANISOU  824  CB  MET A 123    13719  26720   5154  -5010   2169  -2193       C  
ATOM    825  CG  MET A 123       1.731  -1.166  -5.829  1.00121.74           C  
ANISOU  825  CG  MET A 123    14202  26384   5668  -5031   1995  -1894       C  
ATOM    826  SD  MET A 123       1.810  -1.235  -7.642  1.00124.62           S  
ANISOU  826  SD  MET A 123    14549  26416   6386  -4719   1941  -1851       S  
ATOM    827  CE  MET A 123       0.610  -2.514  -7.984  1.00122.61           C  
ANISOU  827  CE  MET A 123    14085  26500   6002  -4998   2000  -1787       C  
ATOM    828  N   ASP A 124      -2.033   2.073  -5.803  1.00120.72           N  
ANISOU  828  N   ASP A 124    13285  27570   5014  -4023   2409  -3171       N  
ATOM    829  CA  ASP A 124      -3.361   2.495  -5.366  1.00123.40           C  
ANISOU  829  CA  ASP A 124    13293  28538   5057  -3906   2536  -3558       C  
ATOM    830  C   ASP A 124      -4.385   2.017  -6.415  1.00126.72           C  
ANISOU  830  C   ASP A 124    13446  29193   5509  -3816   2583  -3658       C  
ATOM    831  O   ASP A 124      -3.988   1.454  -7.441  1.00123.36           O  
ANISOU  831  O   ASP A 124    13133  28390   5346  -3825   2511  -3417       O  
ATOM    832  CB  ASP A 124      -3.459   4.021  -5.101  1.00126.44           C  
ANISOU  832  CB  ASP A 124    13731  28931   5381  -3418   2504  -3913       C  
ATOM    833  CG  ASP A 124      -3.214   4.970  -6.261  1.00133.71           C  
ANISOU  833  CG  ASP A 124    14848  29402   6553  -2893   2377  -4013       C  
ATOM    834  OD1 ASP A 124      -2.394   4.639  -7.132  1.00132.74           O  
ANISOU  834  OD1 ASP A 124    14944  28775   6717  -2925   2294  -3726       O  
ATOM    835  OD2 ASP A 124      -3.739   6.106  -6.217  1.00138.73           O  
ANISOU  835  OD2 ASP A 124    15468  30163   7082  -2454   2343  -4380       O  
ATOM    836  N   GLY A 125      -5.676   2.188  -6.113  1.00126.63           N  
ANISOU  836  N   GLY A 125    13064  29833   5216  -3755   2704  -4018       N  
ATOM    837  CA  GLY A 125      -6.787   1.774  -6.965  1.00127.53           C  
ANISOU  837  CA  GLY A 125    12860  30295   5300  -3681   2764  -4180       C  
ATOM    838  C   GLY A 125      -6.539   1.909  -8.455  1.00128.52           C  
ANISOU  838  C   GLY A 125    13127  29933   5774  -3322   2646  -4093       C  
ATOM    839  O   GLY A 125      -6.732   0.948  -9.202  1.00126.78           O  
ANISOU  839  O   GLY A 125    12835  29678   5657  -3522   2656  -3906       O  
ATOM    840  N   GLU A 126      -6.061   3.089  -8.891  1.00123.65           N  
ANISOU  840  N   GLU A 126    12750  28906   5327  -2819   2524  -4213       N  
ATOM    841  CA  GLU A 126      -5.815   3.390 -10.302  1.00120.83           C  
ANISOU  841  CA  GLU A 126    12568  28072   5269  -2455   2403  -4161       C  
ATOM    842  C   GLU A 126      -4.480   2.799 -10.785  1.00121.54           C  
ANISOU  842  C   GLU A 126    12990  27529   5660  -2691   2324  -3700       C  
ATOM    843  O   GLU A 126      -4.430   2.283 -11.906  1.00119.53           O  
ANISOU  843  O   GLU A 126    12758  27042   5616  -2662   2283  -3548       O  
ATOM    844  CB  GLU A 126      -5.820   4.922 -10.530  1.00122.87           C  
ANISOU  844  CB  GLU A 126    13016  28127   5541  -1859   2282  -4476       C  
ATOM    845  CG  GLU A 126      -5.723   5.360 -11.991  1.00127.41           C  
ANISOU  845  CG  GLU A 126    13792  28252   6367  -1457   2148  -4479       C  
ATOM    846  CD  GLU A 126      -5.695   6.855 -12.277  1.00141.92           C  
ANISOU  846  CD  GLU A 126    15913  29812   8197   -890   1988  -4765       C  
ATOM    847  OE1 GLU A 126      -5.673   7.219 -13.475  1.00131.27           O  
ANISOU  847  OE1 GLU A 126    14756  28100   7019   -577   1868  -4775       O  
ATOM    848  OE2 GLU A 126      -5.688   7.661 -11.318  1.00137.50           O  
ANISOU  848  OE2 GLU A 126    15416  29377   7450   -764   1968  -4976       O  
ATOM    849  N   GLU A 127      -3.399   2.899  -9.966  1.00117.13           N  
ANISOU  849  N   GLU A 127    12678  26707   5117  -2898   2293  -3504       N  
ATOM    850  CA  GLU A 127      -2.052   2.479 -10.378  1.00113.49           C  
ANISOU  850  CA  GLU A 127    12520  25673   4927  -3065   2198  -3128       C  
ATOM    851  C   GLU A 127      -1.901   0.935 -10.389  1.00117.81           C  
ANISOU  851  C   GLU A 127    12993  26257   5511  -3533   2216  -2805       C  
ATOM    852  O   GLU A 127      -1.066   0.420 -11.139  1.00115.01           O  
ANISOU  852  O   GLU A 127    12810  25482   5408  -3592   2125  -2541       O  
ATOM    853  CB  GLU A 127      -0.981   3.098  -9.466  1.00114.00           C  
ANISOU  853  CB  GLU A 127    12847  25494   4974  -3124   2150  -3061       C  
ATOM    854  CG  GLU A 127       0.460   2.833  -9.891  1.00119.48           C  
ANISOU  854  CG  GLU A 127    13830  25634   5932  -3247   2043  -2740       C  
ATOM    855  CD  GLU A 127       0.898   3.315 -11.263  1.00141.01           C  
ANISOU  855  CD  GLU A 127    16737  27925   8916  -2957   1959  -2716       C  
ATOM    856  OE1 GLU A 127       1.866   2.736 -11.806  1.00138.59           O  
ANISOU  856  OE1 GLU A 127    16558  27279   8820  -3108   1892  -2453       O  
ATOM    857  OE2 GLU A 127       0.242   4.221 -11.826  1.00134.53           O  
ANISOU  857  OE2 GLU A 127    15928  27117   8072  -2579   1948  -2969       O  
ATOM    858  N   ILE A 128      -2.721   0.207  -9.622  1.00117.33           N  
ANISOU  858  N   ILE A 128    12694  26696   5190  -3861   2320  -2841       N  
ATOM    859  CA  ILE A 128      -2.650  -1.255  -9.597  1.00116.94           C  
ANISOU  859  CA  ILE A 128    12634  26669   5130  -4327   2311  -2542       C  
ATOM    860  C   ILE A 128      -3.292  -1.825 -10.918  1.00118.56           C  
ANISOU  860  C   ILE A 128    12695  26874   5479  -4235   2309  -2528       C  
ATOM    861  O   ILE A 128      -2.979  -2.954 -11.308  1.00115.41           O  
ANISOU  861  O   ILE A 128    12379  26291   5181  -4510   2244  -2245       O  
ATOM    862  CB  ILE A 128      -3.328  -1.808  -8.302  1.00123.79           C  
ANISOU  862  CB  ILE A 128    13337  28077   5620  -4768   2422  -2586       C  
ATOM    863  CG1 ILE A 128      -2.915  -3.270  -8.008  1.00124.30           C  
ANISOU  863  CG1 ILE A 128    13556  28028   5645  -5305   2353  -2217       C  
ATOM    864  CG2 ILE A 128      -4.861  -1.586  -8.282  1.00128.22           C  
ANISOU  864  CG2 ILE A 128    13496  29298   5924  -4701   2580  -2948       C  
ATOM    865  CD1 ILE A 128      -3.303  -3.811  -6.608  1.00139.09           C  
ANISOU  865  CD1 ILE A 128    15392  30329   7128  -5813   2431  -2197       C  
ATOM    866  N   GLU A 129      -4.130  -1.007 -11.618  1.00116.78           N  
ANISOU  866  N   GLU A 129    12285  26819   5266  -3815   2354  -2839       N  
ATOM    867  CA  GLU A 129      -4.822  -1.358 -12.878  1.00116.42           C  
ANISOU  867  CA  GLU A 129    12086  26804   5345  -3657   2353  -2884       C  
ATOM    868  C   GLU A 129      -3.898  -1.176 -14.095  1.00115.83           C  
ANISOU  868  C   GLU A 129    12274  26106   5631  -3395   2223  -2706       C  
ATOM    869  O   GLU A 129      -3.885  -2.032 -14.985  1.00112.78           O  
ANISOU  869  O   GLU A 129    11882  25569   5401  -3489   2184  -2525       O  
ATOM    870  CB  GLU A 129      -6.093  -0.508 -13.063  1.00120.79           C  
ANISOU  870  CB  GLU A 129    12342  27816   5738  -3281   2429  -3328       C  
ATOM    871  CG  GLU A 129      -7.119  -0.706 -11.957  1.00141.00           C  
ANISOU  871  CG  GLU A 129    14568  31092   7914  -3542   2577  -3559       C  
ATOM    872  CD  GLU A 129      -8.377   0.144 -12.019  1.00177.15           C  
ANISOU  872  CD  GLU A 129    18805  36206  12297  -3148   2640  -4058       C  
ATOM    873  OE1 GLU A 129      -8.713   0.648 -13.116  1.00174.19           O  
ANISOU  873  OE1 GLU A 129    18411  35693  12080  -2694   2566  -4220       O  
ATOM    874  OE2 GLU A 129      -9.064   0.251 -10.976  1.00179.49           O  
ANISOU  874  OE2 GLU A 129    19079  36617  12503  -3160   2731  -4165       O  
ATOM    875  N   VAL A 130      -3.122  -0.057 -14.113  1.00111.45           N  
ANISOU  875  N   VAL A 130    11959  25203   5185  -3092   2156  -2765       N  
ATOM    876  CA  VAL A 130      -2.121   0.312 -15.134  1.00107.87           C  
ANISOU  876  CA  VAL A 130    11786  24172   5026  -2878   2043  -2623       C  
ATOM    877  C   VAL A 130      -1.125  -0.849 -15.290  1.00108.85           C  
ANISOU  877  C   VAL A 130    12033  24004   5320  -3223   1977  -2249       C  
ATOM    878  O   VAL A 130      -0.807  -1.236 -16.415  1.00106.03           O  
ANISOU  878  O   VAL A 130    11738  23364   5184  -3153   1914  -2116       O  
ATOM    879  CB  VAL A 130      -1.406   1.651 -14.758  1.00111.41           C  
ANISOU  879  CB  VAL A 130    12493  24363   5475  -2636   1992  -2738       C  
ATOM    880  CG1 VAL A 130      -0.304   2.007 -15.754  1.00108.27           C  
ANISOU  880  CG1 VAL A 130    12395  23403   5341  -2505   1888  -2585       C  
ATOM    881  CG2 VAL A 130      -2.408   2.800 -14.631  1.00113.94           C  
ANISOU  881  CG2 VAL A 130    12730  24946   5616  -2241   2012  -3133       C  
ATOM    882  N   GLN A 131      -0.696  -1.434 -14.147  1.00106.38           N  
ANISOU  882  N   GLN A 131    11754  23784   4881  -3585   1978  -2099       N  
ATOM    883  CA  GLN A 131       0.198  -2.593 -14.038  1.00104.84           C  
ANISOU  883  CA  GLN A 131    11691  23359   4784  -3918   1879  -1774       C  
ATOM    884  C   GLN A 131      -0.211  -3.731 -14.980  1.00109.10           C  
ANISOU  884  C   GLN A 131    12143  23883   5426  -4025   1845  -1632       C  
ATOM    885  O   GLN A 131       0.658  -4.366 -15.571  1.00106.88           O  
ANISOU  885  O   GLN A 131    12008  23253   5349  -4072   1723  -1415       O  
ATOM    886  CB  GLN A 131       0.199  -3.120 -12.590  1.00107.79           C  
ANISOU  886  CB  GLN A 131    12070  23980   4907  -4302   1896  -1698       C  
ATOM    887  CG  GLN A 131       0.851  -2.213 -11.549  1.00114.39           C  
ANISOU  887  CG  GLN A 131    13033  24777   5654  -4266   1900  -1773       C  
ATOM    888  CD  GLN A 131       2.359  -2.293 -11.515  1.00127.24           C  
ANISOU  888  CD  GLN A 131    14916  25964   7465  -4302   1759  -1570       C  
ATOM    889  OE1 GLN A 131       2.947  -2.679 -10.501  1.00119.08           O  
ANISOU  889  OE1 GLN A 131    13995  24923   6327  -4557   1700  -1446       O  
ATOM    890  NE2 GLN A 131       3.023  -2.002 -12.626  1.00121.05           N  
ANISOU  890  NE2 GLN A 131    14223  24827   6942  -4070   1695  -1535       N  
ATOM    891  N   LYS A 132      -1.531  -3.984 -15.110  1.00108.13           N  
ANISOU  891  N   LYS A 132    11771  24162   5150  -4061   1947  -1774       N  
ATOM    892  CA  LYS A 132      -2.090  -5.041 -15.955  1.00108.03           C  
ANISOU  892  CA  LYS A 132    11656  24194   5195  -4186   1928  -1667       C  
ATOM    893  C   LYS A 132      -2.212  -4.575 -17.418  1.00111.47           C  
ANISOU  893  C   LYS A 132    12062  24419   5874  -3786   1911  -1754       C  
ATOM    894  O   LYS A 132      -2.049  -5.389 -18.332  1.00109.28           O  
ANISOU  894  O   LYS A 132    11817  23938   5764  -3828   1836  -1587       O  
ATOM    895  CB  LYS A 132      -3.465  -5.485 -15.423  1.00113.42           C  
ANISOU  895  CB  LYS A 132    12066  25456   5575  -4439   2056  -1806       C  
ATOM    896  CG  LYS A 132      -3.407  -6.088 -14.009  1.00133.70           C  
ANISOU  896  CG  LYS A 132    14690  28246   7865  -4913   2071  -1695       C  
ATOM    897  CD  LYS A 132      -4.767  -6.602 -13.480  1.00147.66           C  
ANISOU  897  CD  LYS A 132    16182  30634   9287  -5254   2212  -1832       C  
ATOM    898  CE  LYS A 132      -5.806  -5.542 -13.165  1.00161.66           C  
ANISOU  898  CE  LYS A 132    17629  32930  10865  -5014   2381  -2240       C  
ATOM    899  NZ  LYS A 132      -5.393  -4.673 -12.032  1.00172.77           N  
ANISOU  899  NZ  LYS A 132    19103  34397  12144  -4958   2413  -2350       N  
ATOM    900  N   GLU A 133      -2.498  -3.266 -17.632  1.00109.22           N  
ANISOU  900  N   GLU A 133    11743  24166   5589  -3395   1962  -2020       N  
ATOM    901  CA  GLU A 133      -2.670  -2.665 -18.968  1.00107.62           C  
ANISOU  901  CA  GLU A 133    11558  23758   5574  -2995   1933  -2132       C  
ATOM    902  C   GLU A 133      -1.340  -2.669 -19.717  1.00105.61           C  
ANISOU  902  C   GLU A 133    11573  22961   5592  -2938   1822  -1917       C  
ATOM    903  O   GLU A 133      -1.292  -3.015 -20.898  1.00103.74           O  
ANISOU  903  O   GLU A 133    11351  22526   5539  -2833   1775  -1841       O  
ATOM    904  CB  GLU A 133      -3.233  -1.222 -18.881  1.00111.10           C  
ANISOU  904  CB  GLU A 133    11977  24327   5908  -2592   1970  -2475       C  
ATOM    905  CG  GLU A 133      -4.368  -0.995 -17.880  1.00130.86           C  
ANISOU  905  CG  GLU A 133    14208  27409   8103  -2621   2077  -2748       C  
ATOM    906  CD  GLU A 133      -5.655  -1.798 -17.972  1.00169.78           C  
ANISOU  906  CD  GLU A 133    18783  32849  12879  -2771   2166  -2856       C  
ATOM    907  OE1 GLU A 133      -6.036  -2.212 -19.092  1.00178.16           O  
ANISOU  907  OE1 GLU A 133    19771  33846  14074  -2669   2139  -2832       O  
ATOM    908  OE2 GLU A 133      -6.343  -1.909 -16.930  1.00167.39           O  
ANISOU  908  OE2 GLU A 133    18259  33045  12295  -2974   2268  -3005       O  
ATOM    909  N   VAL A 134      -0.261  -2.282 -19.013  1.00 99.17           N  
ANISOU  909  N   VAL A 134    10954  21939   4787  -3017   1783  -1835       N  
ATOM    910  CA  VAL A 134       1.115  -2.292 -19.505  1.00 95.49           C  
ANISOU  910  CA  VAL A 134    10713  21035   4535  -3021   1685  -1655       C  
ATOM    911  C   VAL A 134       1.530  -3.760 -19.766  1.00 99.18           C  
ANISOU  911  C   VAL A 134    11159  21412   5112  -3285   1599  -1395       C  
ATOM    912  O   VAL A 134       2.148  -4.045 -20.783  1.00 96.62           O  
ANISOU  912  O   VAL A 134    10907  20810   4994  -3210   1525  -1292       O  
ATOM    913  CB  VAL A 134       2.054  -1.576 -18.491  1.00 97.93           C  
ANISOU  913  CB  VAL A 134    11193  21240   4777  -3083   1670  -1661       C  
ATOM    914  CG1 VAL A 134       3.519  -1.782 -18.823  1.00 95.43           C  
ANISOU  914  CG1 VAL A 134    11051  20561   4645  -3164   1569  -1481       C  
ATOM    915  CG2 VAL A 134       1.731  -0.096 -18.387  1.00 98.66           C  
ANISOU  915  CG2 VAL A 134    11371  21341   4774  -2792   1717  -1914       C  
ATOM    916  N   ALA A 135       1.117  -4.689 -18.872  1.00 98.14           N  
ANISOU  916  N   ALA A 135    10942  21529   4818  -3594   1600  -1305       N  
ATOM    917  CA  ALA A 135       1.430  -6.123 -18.937  1.00 97.53           C  
ANISOU  917  CA  ALA A 135    10905  21364   4787  -3868   1482  -1064       C  
ATOM    918  C   ALA A 135       0.846  -6.788 -20.177  1.00100.27           C  
ANISOU  918  C   ALA A 135    11156  21682   5261  -3798   1464  -1025       C  
ATOM    919  O   ALA A 135       1.526  -7.615 -20.790  1.00 98.15           O  
ANISOU  919  O   ALA A 135    10985  21154   5156  -3841   1330   -851       O  
ATOM    920  CB  ALA A 135       0.898  -6.830 -17.700  1.00100.51           C  
ANISOU  920  CB  ALA A 135    11250  22041   4900  -4233   1496  -1005       C  
ATOM    921  N   LYS A 136      -0.416  -6.454 -20.537  1.00 97.89           N  
ANISOU  921  N   LYS A 136    10656  21664   4873  -3679   1586  -1205       N  
ATOM    922  CA  LYS A 136      -1.085  -7.075 -21.682  1.00 97.03           C  
ANISOU  922  CA  LYS A 136    10435  21568   4863  -3620   1577  -1187       C  
ATOM    923  C   LYS A 136      -0.570  -6.452 -23.003  1.00 97.52           C  
ANISOU  923  C   LYS A 136    10574  21298   5182  -3263   1544  -1223       C  
ATOM    924  O   LYS A 136      -0.854  -6.979 -24.076  1.00 95.50           O  
ANISOU  924  O   LYS A 136    10268  20963   5054  -3192   1511  -1178       O  
ATOM    925  CB  LYS A 136      -2.625  -6.961 -21.573  1.00102.21           C  
ANISOU  925  CB  LYS A 136    10823  22696   5316  -3626   1713  -1395       C  
ATOM    926  CG  LYS A 136      -3.216  -5.561 -21.738  1.00123.29           C  
ANISOU  926  CG  LYS A 136    13386  25515   7943  -3241   1811  -1705       C  
ATOM    927  CD  LYS A 136      -4.744  -5.611 -21.657  1.00139.38           C  
ANISOU  927  CD  LYS A 136    15110  28078   9770  -3244   1924  -1939       C  
ATOM    928  CE  LYS A 136      -5.437  -4.340 -22.103  1.00155.18           C  
ANISOU  928  CE  LYS A 136    17006  30206  11749  -2778   1970  -2275       C  
ATOM    929  NZ  LYS A 136      -5.053  -3.156 -21.296  1.00165.00           N  
ANISOU  929  NZ  LYS A 136    18367  31419  12906  -2601   1983  -2424       N  
ATOM    930  N   MET A 137       0.204  -5.360 -22.909  1.00 93.43           N  
ANISOU  930  N   MET A 137    10196  20585   4718  -3075   1549  -1297       N  
ATOM    931  CA  MET A 137       0.803  -4.684 -24.051  1.00 91.68           C  
ANISOU  931  CA  MET A 137    10098  20043   4691  -2802   1519  -1327       C  
ATOM    932  C   MET A 137       2.116  -5.363 -24.447  1.00 95.15           C  
ANISOU  932  C   MET A 137    10664  20174   5314  -2913   1401  -1122       C  
ATOM    933  O   MET A 137       2.368  -5.531 -25.638  1.00 93.29           O  
ANISOU  933  O   MET A 137    10452  19745   5249  -2789   1360  -1085       O  
ATOM    934  CB  MET A 137       1.027  -3.214 -23.731  1.00 94.30           C  
ANISOU  934  CB  MET A 137    10562  20313   4957  -2600   1567  -1504       C  
ATOM    935  CG  MET A 137       1.866  -2.516 -24.734  1.00 96.51           C  
ANISOU  935  CG  MET A 137    11040  20237   5394  -2421   1526  -1504       C  
ATOM    936  SD  MET A 137       1.969  -0.756 -24.447  1.00102.27           S  
ANISOU  936  SD  MET A 137    11993  20861   6005  -2190   1555  -1720       S  
ATOM    937  CE  MET A 137       0.248  -0.253 -24.893  1.00100.76           C  
ANISOU  937  CE  MET A 137    11674  20912   5700  -1851   1593  -1981       C  
ATOM    938  N   TYR A 138       2.946  -5.752 -23.465  1.00 93.23           N  
ANISOU  938  N   TYR A 138    10495  19903   5026  -3131   1335  -1009       N  
ATOM    939  CA  TYR A 138       4.193  -6.459 -23.740  1.00 92.54           C  
ANISOU  939  CA  TYR A 138    10500  19571   5088  -3213   1193   -853       C  
ATOM    940  C   TYR A 138       3.913  -7.880 -24.233  1.00 97.34           C  
ANISOU  940  C   TYR A 138    11056  20166   5762  -3321   1083   -705       C  
ATOM    941  O   TYR A 138       4.644  -8.359 -25.099  1.00 96.35           O  
ANISOU  941  O   TYR A 138    10965  19834   5810  -3253    979   -636       O  
ATOM    942  CB  TYR A 138       5.097  -6.495 -22.516  1.00 95.08           C  
ANISOU  942  CB  TYR A 138    10918  19883   5327  -3387   1127   -798       C  
ATOM    943  CG  TYR A 138       5.748  -5.165 -22.207  1.00 98.79           C  
ANISOU  943  CG  TYR A 138    11479  20283   5775  -3290   1197   -922       C  
ATOM    944  CD1 TYR A 138       5.133  -4.246 -21.368  1.00102.70           C  
ANISOU  944  CD1 TYR A 138    11978  20947   6096  -3269   1310  -1051       C  
ATOM    945  CD2 TYR A 138       7.007  -4.852 -22.704  1.00 99.19           C  
ANISOU  945  CD2 TYR A 138    11613  20118   5955  -3241   1141   -921       C  
ATOM    946  CE1 TYR A 138       5.739  -3.029 -21.062  1.00104.80           C  
ANISOU  946  CE1 TYR A 138    12370  21121   6327  -3191   1353  -1161       C  
ATOM    947  CE2 TYR A 138       7.627  -3.643 -22.397  1.00100.81           C  
ANISOU  947  CE2 TYR A 138    11930  20259   6114  -3206   1200  -1029       C  
ATOM    948  CZ  TYR A 138       6.992  -2.735 -21.569  1.00111.34           C  
ANISOU  948  CZ  TYR A 138    13307  21716   7280  -3179   1298  -1139       C  
ATOM    949  OH  TYR A 138       7.601  -1.545 -21.240  1.00114.77           O  
ANISOU  949  OH  TYR A 138    13890  22063   7655  -3154   1338  -1242       O  
ATOM    950  N   SER A 139       2.841  -8.535 -23.731  1.00 95.79           N  
ANISOU  950  N   SER A 139    10779  20203   5412  -3496   1107   -671       N  
ATOM    951  CA  SER A 139       2.462  -9.868 -24.201  1.00 96.48           C  
ANISOU  951  CA  SER A 139    10853  20274   5530  -3630    998   -531       C  
ATOM    952  C   SER A 139       1.811  -9.781 -25.591  1.00102.63           C  
ANISOU  952  C   SER A 139    11517  21033   6445  -3418   1056   -596       C  
ATOM    953  O   SER A 139       1.822 -10.772 -26.326  1.00103.14           O  
ANISOU  953  O   SER A 139    11595  20982   6610  -3449    945   -485       O  
ATOM    954  CB  SER A 139       1.525 -10.555 -23.220  1.00102.81           C  
ANISOU  954  CB  SER A 139    11626  21351   6086  -3948   1014   -477       C  
ATOM    955  OG  SER A 139       0.289  -9.866 -23.155  1.00116.54           O  
ANISOU  955  OG  SER A 139    13171  23416   7693  -3898   1206   -656       O  
ATOM    956  N   SER A 140       1.223  -8.603 -25.949  1.00 99.35           N  
ANISOU  956  N   SER A 140    11010  20718   6019  -3189   1210   -786       N  
ATOM    957  CA  SER A 140       0.652  -8.388 -27.287  1.00 97.84           C  
ANISOU  957  CA  SER A 140    10739  20484   5951  -2951   1251   -866       C  
ATOM    958  C   SER A 140       1.789  -8.167 -28.268  1.00 99.68           C  
ANISOU  958  C   SER A 140    11093  20383   6399  -2787   1182   -825       C  
ATOM    959  O   SER A 140       1.774  -8.760 -29.341  1.00 98.38           O  
ANISOU  959  O   SER A 140    10906  20101   6374  -2717   1125   -768       O  
ATOM    960  CB  SER A 140      -0.342  -7.230 -27.310  1.00102.05           C  
ANISOU  960  CB  SER A 140    11175  21221   6378  -2737   1393  -1099       C  
ATOM    961  OG  SER A 140      -1.496  -7.502 -26.531  1.00111.92           O  
ANISOU  961  OG  SER A 140    12250  22857   7417  -2889   1468  -1176       O  
ATOM    962  N   PHE A 141       2.830  -7.398 -27.860  1.00 96.37           N  
ANISOU  962  N   PHE A 141    10796  19829   5990  -2762   1183   -851       N  
ATOM    963  CA  PHE A 141       4.031  -7.196 -28.674  1.00 95.09           C  
ANISOU  963  CA  PHE A 141    10733  19406   5992  -2672   1125   -828       C  
ATOM    964  C   PHE A 141       4.754  -8.520 -28.881  1.00 98.39           C  
ANISOU  964  C   PHE A 141    11141  19723   6519  -2786    961   -676       C  
ATOM    965  O   PHE A 141       5.402  -8.702 -29.905  1.00 95.43           O  
ANISOU  965  O   PHE A 141    10774  19190   6294  -2689    907   -667       O  
ATOM    966  CB  PHE A 141       4.989  -6.165 -28.056  1.00 97.29           C  
ANISOU  966  CB  PHE A 141    11135  19610   6222  -2685   1158   -894       C  
ATOM    967  CG  PHE A 141       4.498  -4.741 -27.881  1.00 99.54           C  
ANISOU  967  CG  PHE A 141    11504  19924   6394  -2547   1279  -1057       C  
ATOM    968  CD1 PHE A 141       3.473  -4.235 -28.678  1.00102.45           C  
ANISOU  968  CD1 PHE A 141    11862  20311   6755  -2334   1340  -1167       C  
ATOM    969  CD2 PHE A 141       5.175  -3.854 -27.045  1.00101.73           C  
ANISOU  969  CD2 PHE A 141    11903  20171   6579  -2600   1306  -1115       C  
ATOM    970  CE1 PHE A 141       3.064  -2.904 -28.561  1.00104.15           C  
ANISOU  970  CE1 PHE A 141    12202  20514   6855  -2161   1405  -1338       C  
ATOM    971  CE2 PHE A 141       4.783  -2.514 -26.947  1.00105.11           C  
ANISOU  971  CE2 PHE A 141    12462  20578   6896  -2451   1384  -1273       C  
ATOM    972  CZ  PHE A 141       3.729  -2.048 -27.705  1.00103.57           C  
ANISOU  972  CZ  PHE A 141    12275  20392   6683  -2220   1422  -1387       C  
ATOM    973  N   GLN A 142       4.615  -9.450 -27.905  1.00 97.91           N  
ANISOU  973  N   GLN A 142    11082  19757   6363  -2991    869   -568       N  
ATOM    974  CA  GLN A 142       5.169 -10.809 -27.910  1.00 98.77           C  
ANISOU  974  CA  GLN A 142    11239  19760   6529  -3100    662   -425       C  
ATOM    975  C   GLN A 142       4.553 -11.644 -29.033  1.00102.91           C  
ANISOU  975  C   GLN A 142    11710  20237   7155  -3040    611   -371       C  
ATOM    976  O   GLN A 142       5.258 -12.449 -29.626  1.00102.71           O  
ANISOU  976  O   GLN A 142    11721  20050   7252  -2993    446   -310       O  
ATOM    977  CB  GLN A 142       4.935 -11.496 -26.553  1.00102.39           C  
ANISOU  977  CB  GLN A 142    11773  20325   6804  -3360    578   -323       C  
ATOM    978  CG  GLN A 142       5.397 -12.957 -26.463  1.00128.53           C  
ANISOU  978  CG  GLN A 142    15211  23494  10129  -3478    317   -169       C  
ATOM    979  CD  GLN A 142       4.882 -13.652 -25.219  1.00159.67           C  
ANISOU  979  CD  GLN A 142    19276  27544  13846  -3783    242    -55       C  
ATOM    980  OE1 GLN A 142       4.676 -13.045 -24.154  1.00155.82           O  
ANISOU  980  OE1 GLN A 142    18789  27218  13198  -3910    351    -90       O  
ATOM    981  NE2 GLN A 142       4.681 -14.958 -25.325  1.00157.79           N  
ANISOU  981  NE2 GLN A 142    19172  27208  13572  -3924     43     86       N  
ATOM    982  N   VAL A 143       3.255 -11.489 -29.315  1.00 99.81           N  
ANISOU  982  N   VAL A 143    11221  20001   6703  -3031    737   -411       N  
ATOM    983  CA  VAL A 143       2.692 -12.255 -30.422  1.00 99.52           C  
ANISOU  983  CA  VAL A 143    11130  19919   6765  -2974    688   -366       C  
ATOM    984  C   VAL A 143       2.832 -11.420 -31.693  1.00102.81           C  
ANISOU  984  C   VAL A 143    11497  20231   7334  -2699    779   -478       C  
ATOM    985  O   VAL A 143       3.004 -11.982 -32.770  1.00101.41           O  
ANISOU  985  O   VAL A 143    11309  19923   7300  -2603    702   -442       O  
ATOM    986  CB  VAL A 143       1.237 -12.741 -30.215  1.00104.97           C  
ANISOU  986  CB  VAL A 143    11728  20846   7312  -3130    747   -352       C  
ATOM    987  CG1 VAL A 143       1.143 -13.686 -29.021  1.00106.72           C  
ANISOU  987  CG1 VAL A 143    12050  21146   7351  -3466    637   -218       C  
ATOM    988  CG2 VAL A 143       0.250 -11.581 -30.084  1.00105.43           C  
ANISOU  988  CG2 VAL A 143    11644  21148   7267  -3023    959   -532       C  
ATOM    989  N   MET A 144       2.845 -10.078 -31.546  1.00100.49           N  
ANISOU  989  N   MET A 144    11211  19973   6999  -2582    924   -611       N  
ATOM    990  CA  MET A 144       2.926  -9.115 -32.647  1.00100.19           C  
ANISOU  990  CA  MET A 144    11197  19820   7052  -2349   1007   -722       C  
ATOM    991  C   MET A 144       4.204  -9.339 -33.470  1.00100.24           C  
ANISOU  991  C   MET A 144    11260  19614   7214  -2306    920   -685       C  
ATOM    992  O   MET A 144       4.175  -9.098 -34.672  1.00 98.35           O  
ANISOU  992  O   MET A 144    11027  19272   7070  -2159    946   -727       O  
ATOM    993  CB  MET A 144       2.873  -7.681 -32.100  1.00103.89           C  
ANISOU  993  CB  MET A 144    11741  20327   7405  -2273   1129   -860       C  
ATOM    994  CG  MET A 144       2.191  -6.688 -33.029  1.00108.52           C  
ANISOU  994  CG  MET A 144    12370  20869   7992  -2028   1213  -1000       C  
ATOM    995  SD  MET A 144       1.819  -5.072 -32.250  1.00114.93           S  
ANISOU  995  SD  MET A 144    13305  21742   8620  -1906   1312  -1188       S  
ATOM    996  CE  MET A 144       3.476  -4.364 -32.127  1.00111.37           C  
ANISOU  996  CE  MET A 144    13068  21050   8197  -2004   1298  -1159       C  
ATOM    997  N   TYR A 145       5.292  -9.859 -32.846  1.00 96.16           N  
ANISOU  997  N   TYR A 145    10772  19055   6711  -2430    806   -622       N  
ATOM    998  CA  TYR A 145       6.524 -10.182 -33.574  1.00 94.83           C  
ANISOU  998  CA  TYR A 145    10604  18755   6672  -2385    707   -625       C  
ATOM    999  C   TYR A 145       6.539 -11.690 -33.902  1.00 96.33           C  
ANISOU  999  C   TYR A 145    10754  18901   6948  -2396    516   -521       C  
ATOM   1000  O   TYR A 145       7.190 -12.093 -34.867  1.00 95.30           O  
ANISOU 1000  O   TYR A 145    10587  18683   6941  -2296    435   -543       O  
ATOM   1001  CB  TYR A 145       7.805  -9.762 -32.808  1.00 97.03           C  
ANISOU 1001  CB  TYR A 145    10923  19033   6910  -2470    677   -671       C  
ATOM   1002  CG  TYR A 145       8.341 -10.747 -31.785  1.00100.45           C  
ANISOU 1002  CG  TYR A 145    11364  19493   7311  -2584    494   -593       C  
ATOM   1003  CD1 TYR A 145       7.873 -10.747 -30.476  1.00103.89           C  
ANISOU 1003  CD1 TYR A 145    11853  20015   7604  -2724    500   -537       C  
ATOM   1004  CD2 TYR A 145       9.425 -11.570 -32.082  1.00101.69           C  
ANISOU 1004  CD2 TYR A 145    11488  19594   7556  -2542    305   -602       C  
ATOM   1005  CE1 TYR A 145       8.395 -11.618 -29.515  1.00106.97           C  
ANISOU 1005  CE1 TYR A 145    12302  20401   7939  -2838    312   -461       C  
ATOM   1006  CE2 TYR A 145       9.957 -12.448 -31.134  1.00104.12           C  
ANISOU 1006  CE2 TYR A 145    11846  19896   7817  -2611     95   -547       C  
ATOM   1007  CZ  TYR A 145       9.441 -12.467 -29.846  1.00113.82           C  
ANISOU 1007  CZ  TYR A 145    13169  21177   8901  -2769     96   -464       C  
ATOM   1008  OH  TYR A 145       9.973 -13.314 -28.891  1.00114.78           O  
ANISOU 1008  OH  TYR A 145    13390  21267   8954  -2847   -131   -404       O  
ATOM   1009  N   THR A 146       5.823 -12.518 -33.102  1.00 91.61           N  
ANISOU 1009  N   THR A 146    10178  18366   6263  -2530    436   -414       N  
ATOM   1010  CA  THR A 146       5.719 -13.960 -33.348  1.00 90.60           C  
ANISOU 1010  CA  THR A 146    10081  18164   6179  -2568    230   -302       C  
ATOM   1011  C   THR A 146       4.916 -14.162 -34.633  1.00 90.96           C  
ANISOU 1011  C   THR A 146    10053  18185   6321  -2451    280   -307       C  
ATOM   1012  O   THR A 146       5.286 -15.005 -35.450  1.00 90.16           O  
ANISOU 1012  O   THR A 146     9956  17965   6334  -2366    131   -278       O  
ATOM   1013  CB  THR A 146       5.101 -14.686 -32.136  1.00 98.55           C  
ANISOU 1013  CB  THR A 146    11180  19245   7019  -2806    146   -183       C  
ATOM   1014  OG1 THR A 146       5.923 -14.450 -31.001  1.00 98.08           O  
ANISOU 1014  OG1 THR A 146    11197  19193   6876  -2892     92   -187       O  
ATOM   1015  CG2 THR A 146       4.978 -16.199 -32.343  1.00 97.82           C  
ANISOU 1015  CG2 THR A 146    11196  19034   6936  -2881   -100    -54       C  
ATOM   1016  N   VAL A 147       3.844 -13.362 -34.822  1.00 85.37           N  
ANISOU 1016  N   VAL A 147     9280  17594   5564  -2419    476   -363       N  
ATOM   1017  CA  VAL A 147       3.007 -13.390 -36.022  1.00 84.00           C  
ANISOU 1017  CA  VAL A 147     9032  17417   5468  -2287    536   -392       C  
ATOM   1018  C   VAL A 147       3.880 -12.946 -37.227  1.00 87.50           C  
ANISOU 1018  C   VAL A 147     9476  17708   6061  -2093    547   -465       C  
ATOM   1019  O   VAL A 147       3.983 -13.681 -38.217  1.00 86.45           O  
ANISOU 1019  O   VAL A 147     9319  17484   6045  -2011    452   -437       O  
ATOM   1020  CB  VAL A 147       1.723 -12.522 -35.850  1.00 87.36           C  
ANISOU 1020  CB  VAL A 147     9383  18028   5781  -2257    722   -483       C  
ATOM   1021  CG1 VAL A 147       1.055 -12.218 -37.185  1.00 86.38           C  
ANISOU 1021  CG1 VAL A 147     9200  17876   5744  -2050    788   -557       C  
ATOM   1022  CG2 VAL A 147       0.737 -13.184 -34.891  1.00 88.34           C  
ANISOU 1022  CG2 VAL A 147     9460  18361   5745  -2483    713   -423       C  
ATOM   1023  N   GLY A 148       4.546 -11.798 -37.081  1.00 83.85           N  
ANISOU 1023  N   GLY A 148     9056  17230   5574  -2054    652   -558       N  
ATOM   1024  CA  GLY A 148       5.433 -11.228 -38.088  1.00 82.57           C  
ANISOU 1024  CA  GLY A 148     8916  16960   5498  -1946    686   -639       C  
ATOM   1025  C   GLY A 148       6.413 -12.225 -38.648  1.00 86.30           C  
ANISOU 1025  C   GLY A 148     9337  17367   6086  -1925    524   -618       C  
ATOM   1026  O   GLY A 148       6.467 -12.406 -39.861  1.00 84.67           O  
ANISOU 1026  O   GLY A 148     9096  17098   5975  -1814    516   -646       O  
ATOM   1027  N   TYR A 149       7.149 -12.922 -37.756  1.00 84.85           N  
ANISOU 1027  N   TYR A 149     9152  17202   5883  -2013    372   -581       N  
ATOM   1028  CA  TYR A 149       8.121 -13.955 -38.122  1.00 85.05           C  
ANISOU 1028  CA  TYR A 149     9134  17182   6000  -1954    163   -593       C  
ATOM   1029  C   TYR A 149       7.469 -15.213 -38.692  1.00 84.76           C  
ANISOU 1029  C   TYR A 149     9102  17066   6035  -1894      7   -501       C  
ATOM   1030  O   TYR A 149       8.078 -15.821 -39.558  1.00 84.55           O  
ANISOU 1030  O   TYR A 149     9026  16990   6110  -1770   -118   -551       O  
ATOM   1031  CB  TYR A 149       8.998 -14.381 -36.935  1.00 88.97           C  
ANISOU 1031  CB  TYR A 149     9663  17706   6437  -2033      1   -589       C  
ATOM   1032  CG  TYR A 149      10.200 -13.502 -36.675  1.00 93.32           C  
ANISOU 1032  CG  TYR A 149    10165  18338   6956  -2056     69   -724       C  
ATOM   1033  CD1 TYR A 149      11.273 -13.481 -37.562  1.00 95.81           C  
ANISOU 1033  CD1 TYR A 149    10365  18698   7339  -1967     37   -866       C  
ATOM   1034  CD2 TYR A 149      10.374 -12.880 -35.442  1.00 95.60           C  
ANISOU 1034  CD2 TYR A 149    10510  18685   7130  -2186    125   -720       C  
ATOM   1035  CE1 TYR A 149      12.430 -12.757 -37.287  1.00 98.61           C  
ANISOU 1035  CE1 TYR A 149    10656  19172   7641  -2031     89  -1006       C  
ATOM   1036  CE2 TYR A 149      11.527 -12.149 -35.154  1.00 97.53           C  
ANISOU 1036  CE2 TYR A 149    10709  19014   7335  -2231    168   -847       C  
ATOM   1037  CZ  TYR A 149      12.552 -12.089 -36.081  1.00107.86           C  
ANISOU 1037  CZ  TYR A 149    11896  20384   8703  -2165    152   -992       C  
ATOM   1038  OH  TYR A 149      13.685 -11.357 -35.816  1.00114.00           O  
ANISOU 1038  OH  TYR A 149    12611  21288   9416  -2251    207  -1135       O  
ATOM   1039  N   SER A 150       6.290 -15.648 -38.183  1.00 78.34           N  
ANISOU 1039  N   SER A 150     8348  16262   5154  -1999      1   -381       N  
ATOM   1040  CA  SER A 150       5.627 -16.860 -38.688  1.00 76.86           C  
ANISOU 1040  CA  SER A 150     8194  15999   5009  -1991   -152   -286       C  
ATOM   1041  C   SER A 150       5.185 -16.651 -40.135  1.00 78.51           C  
ANISOU 1041  C   SER A 150     8316  16183   5331  -1836    -54   -336       C  
ATOM   1042  O   SER A 150       5.404 -17.536 -40.964  1.00 77.97           O  
ANISOU 1042  O   SER A 150     8245  16020   5361  -1735   -208   -327       O  
ATOM   1043  CB  SER A 150       4.441 -17.250 -37.813  1.00 79.77           C  
ANISOU 1043  CB  SER A 150     8632  16437   5240  -2200   -145   -166       C  
ATOM   1044  OG  SER A 150       4.863 -17.636 -36.515  1.00 85.64           O  
ANISOU 1044  OG  SER A 150     9497  17177   5866  -2362   -275   -101       O  
ATOM   1045  N   LEU A 151       4.623 -15.455 -40.449  1.00 73.72           N  
ANISOU 1045  N   LEU A 151     7660  15647   4703  -1798    183   -401       N  
ATOM   1046  CA  LEU A 151       4.225 -15.048 -41.810  1.00 72.38           C  
ANISOU 1046  CA  LEU A 151     7441  15441   4618  -1642    285   -460       C  
ATOM   1047  C   LEU A 151       5.476 -14.844 -42.698  1.00 74.99           C  
ANISOU 1047  C   LEU A 151     7746  15708   5040  -1534    265   -556       C  
ATOM   1048  O   LEU A 151       5.486 -15.243 -43.861  1.00 72.47           O  
ANISOU 1048  O   LEU A 151     7388  15331   4817  -1418    225   -577       O  
ATOM   1049  CB  LEU A 151       3.363 -13.756 -41.785  1.00 72.14           C  
ANISOU 1049  CB  LEU A 151     7419  15483   4508  -1610    502   -525       C  
ATOM   1050  CG  LEU A 151       1.829 -13.882 -41.588  1.00 76.66           C  
ANISOU 1050  CG  LEU A 151     7942  16174   5010  -1632    556   -500       C  
ATOM   1051  CD1 LEU A 151       1.454 -14.579 -40.277  1.00 78.16           C  
ANISOU 1051  CD1 LEU A 151     8128  16483   5088  -1849    490   -410       C  
ATOM   1052  CD2 LEU A 151       1.173 -12.520 -41.655  1.00 77.51           C  
ANISOU 1052  CD2 LEU A 151     8066  16345   5038  -1521    731   -618       C  
ATOM   1053  N   SER A 152       6.527 -14.244 -42.119  1.00 73.67           N  
ANISOU 1053  N   SER A 152     7587  15579   4826  -1592    294   -624       N  
ATOM   1054  CA  SER A 152       7.827 -14.000 -42.736  1.00 73.90           C  
ANISOU 1054  CA  SER A 152     7562  15624   4893  -1551    287   -744       C  
ATOM   1055  C   SER A 152       8.483 -15.360 -43.120  1.00 79.51           C  
ANISOU 1055  C   SER A 152     8193  16318   5700  -1454     45   -760       C  
ATOM   1056  O   SER A 152       9.009 -15.501 -44.225  1.00 79.71           O  
ANISOU 1056  O   SER A 152     8138  16355   5793  -1354     29   -853       O  
ATOM   1057  CB  SER A 152       8.691 -13.196 -41.771  1.00 77.40           C  
ANISOU 1057  CB  SER A 152     8024  16145   5240  -1672    349   -808       C  
ATOM   1058  OG  SER A 152       9.933 -12.803 -42.314  1.00 89.04           O  
ANISOU 1058  OG  SER A 152     9428  17690   6712  -1685    375   -949       O  
ATOM   1059  N   LEU A 153       8.370 -16.370 -42.217  1.00 75.99           N  
ANISOU 1059  N   LEU A 153     7797  15835   5241  -1484   -157   -670       N  
ATOM   1060  CA  LEU A 153       8.801 -17.768 -42.377  1.00 75.86           C  
ANISOU 1060  CA  LEU A 153     7787  15751   5287  -1377   -449   -665       C  
ATOM   1061  C   LEU A 153       8.046 -18.440 -43.512  1.00 81.26           C  
ANISOU 1061  C   LEU A 153     8470  16343   6062  -1275   -495   -618       C  
ATOM   1062  O   LEU A 153       8.665 -18.926 -44.458  1.00 80.79           O  
ANISOU 1062  O   LEU A 153     8333  16276   6087  -1118   -603   -717       O  
ATOM   1063  CB  LEU A 153       8.545 -18.531 -41.054  1.00 76.29           C  
ANISOU 1063  CB  LEU A 153     7990  15742   5257  -1490   -635   -540       C  
ATOM   1064  CG  LEU A 153       8.680 -20.044 -41.063  1.00 81.02           C  
ANISOU 1064  CG  LEU A 153     8705  16200   5878  -1409   -979   -490       C  
ATOM   1065  CD1 LEU A 153      10.118 -20.460 -41.143  1.00 82.24           C  
ANISOU 1065  CD1 LEU A 153     8798  16381   6068  -1225  -1200   -659       C  
ATOM   1066  CD2 LEU A 153       8.074 -20.629 -39.830  1.00 82.95           C  
ANISOU 1066  CD2 LEU A 153     9156  16365   5995  -1602  -1107   -325       C  
ATOM   1067  N   GLY A 154       6.712 -18.467 -43.382  1.00 78.97           N  
ANISOU 1067  N   GLY A 154     8251  16013   5741  -1369   -414   -484       N  
ATOM   1068  CA  GLY A 154       5.787 -19.051 -44.344  1.00 79.14           C  
ANISOU 1068  CA  GLY A 154     8277  15965   5830  -1308   -438   -426       C  
ATOM   1069  C   GLY A 154       5.933 -18.478 -45.736  1.00 84.14           C  
ANISOU 1069  C   GLY A 154     8805  16611   6552  -1160   -303   -531       C  
ATOM   1070  O   GLY A 154       5.867 -19.224 -46.717  1.00 83.67           O  
ANISOU 1070  O   GLY A 154     8725  16484   6582  -1038   -414   -540       O  
ATOM   1071  N   ALA A 155       6.159 -17.141 -45.830  1.00 81.72           N  
ANISOU 1071  N   ALA A 155     8464  16380   6207  -1181    -73   -611       N  
ATOM   1072  CA  ALA A 155       6.373 -16.449 -47.107  1.00 81.40           C  
ANISOU 1072  CA  ALA A 155     8377  16344   6208  -1087     63   -710       C  
ATOM   1073  C   ALA A 155       7.556 -17.071 -47.837  1.00 86.75           C  
ANISOU 1073  C   ALA A 155     8956  17050   6954   -984    -72   -825       C  
ATOM   1074  O   ALA A 155       7.381 -17.580 -48.946  1.00 87.12           O  
ANISOU 1074  O   ALA A 155     8966  17054   7081   -865   -123   -845       O  
ATOM   1075  CB  ALA A 155       6.599 -14.950 -46.884  1.00 81.97           C  
ANISOU 1075  CB  ALA A 155     8498  16464   6183  -1170    284   -774       C  
ATOM   1076  N   LEU A 156       8.724 -17.135 -47.155  1.00 82.80           N  
ANISOU 1076  N   LEU A 156     8401  16640   6418  -1016   -156   -913       N  
ATOM   1077  CA  LEU A 156       9.972 -17.699 -47.665  1.00 82.62           C  
ANISOU 1077  CA  LEU A 156     8243  16716   6434   -904   -303  -1078       C  
ATOM   1078  C   LEU A 156       9.843 -19.191 -47.964  1.00 86.55           C  
ANISOU 1078  C   LEU A 156     8748  17115   7021   -732   -592  -1052       C  
ATOM   1079  O   LEU A 156      10.403 -19.638 -48.955  1.00 86.59           O  
ANISOU 1079  O   LEU A 156     8644  17174   7083   -584   -676  -1184       O  
ATOM   1080  CB  LEU A 156      11.099 -17.477 -46.660  1.00 83.47           C  
ANISOU 1080  CB  LEU A 156     8291  16956   6467   -968   -354  -1181       C  
ATOM   1081  CG  LEU A 156      11.431 -16.026 -46.343  1.00 87.36           C  
ANISOU 1081  CG  LEU A 156     8788  17551   6853  -1154    -95  -1229       C  
ATOM   1082  CD1 LEU A 156      12.325 -15.941 -45.165  1.00 88.45           C  
ANISOU 1082  CD1 LEU A 156     8887  17798   6921  -1223   -169  -1296       C  
ATOM   1083  CD2 LEU A 156      12.024 -15.308 -47.534  1.00 89.27           C  
ANISOU 1083  CD2 LEU A 156     8941  17914   7064  -1192     70  -1377       C  
ATOM   1084  N   LEU A 157       9.092 -19.956 -47.139  1.00 83.12           N  
ANISOU 1084  N   LEU A 157     8462  16539   6581   -768   -748   -890       N  
ATOM   1085  CA  LEU A 157       8.872 -21.394 -47.384  1.00 83.57           C  
ANISOU 1085  CA  LEU A 157     8605  16454   6695   -639  -1048   -842       C  
ATOM   1086  C   LEU A 157       8.093 -21.597 -48.680  1.00 85.71           C  
ANISOU 1086  C   LEU A 157     8854  16660   7050   -561   -988   -811       C  
ATOM   1087  O   LEU A 157       8.384 -22.527 -49.427  1.00 85.46           O  
ANISOU 1087  O   LEU A 157     8809  16574   7087   -386  -1194   -877       O  
ATOM   1088  CB  LEU A 157       8.136 -22.075 -46.212  1.00 84.37           C  
ANISOU 1088  CB  LEU A 157     8916  16414   6725   -778  -1202   -654       C  
ATOM   1089  CG  LEU A 157       8.894 -22.193 -44.885  1.00 90.12           C  
ANISOU 1089  CG  LEU A 157     9720  17158   7364   -833  -1350   -668       C  
ATOM   1090  CD1 LEU A 157       7.977 -22.640 -43.777  1.00 90.65           C  
ANISOU 1090  CD1 LEU A 157    10008  17108   7326  -1045  -1426   -463       C  
ATOM   1091  CD2 LEU A 157      10.092 -23.125 -45.004  1.00 94.19           C  
ANISOU 1091  CD2 LEU A 157    10231  17652   7906   -600  -1688   -827       C  
ATOM   1092  N   LEU A 158       7.141 -20.696 -48.960  1.00 80.84           N  
ANISOU 1092  N   LEU A 158     8236  16058   6422   -666   -719   -734       N  
ATOM   1093  CA  LEU A 158       6.345 -20.709 -50.175  1.00 79.88           C  
ANISOU 1093  CA  LEU A 158     8094  15888   6368   -595   -636   -713       C  
ATOM   1094  C   LEU A 158       7.157 -20.166 -51.368  1.00 84.31           C  
ANISOU 1094  C   LEU A 158     8525  16543   6967   -483   -529   -881       C  
ATOM   1095  O   LEU A 158       7.082 -20.730 -52.464  1.00 85.26           O  
ANISOU 1095  O   LEU A 158     8606  16626   7162   -348   -603   -922       O  
ATOM   1096  CB  LEU A 158       5.071 -19.874 -49.967  1.00 79.19           C  
ANISOU 1096  CB  LEU A 158     8054  15804   6231   -718   -410   -606       C  
ATOM   1097  CG  LEU A 158       4.054 -19.877 -51.111  1.00 84.03           C  
ANISOU 1097  CG  LEU A 158     8658  16370   6900   -641   -335   -579       C  
ATOM   1098  CD1 LEU A 158       3.451 -21.266 -51.307  1.00 85.18           C  
ANISOU 1098  CD1 LEU A 158     8855  16414   7096   -620   -557   -487       C  
ATOM   1099  CD2 LEU A 158       2.943 -18.887 -50.844  1.00 87.00           C  
ANISOU 1099  CD2 LEU A 158     9058  16794   7206   -717   -121   -536       C  
ATOM   1100  N   ALA A 159       7.914 -19.061 -51.156  1.00 79.11           N  
ANISOU 1100  N   ALA A 159     7809  16012   6235   -569   -351   -980       N  
ATOM   1101  CA  ALA A 159       8.717 -18.405 -52.188  1.00 78.39           C  
ANISOU 1101  CA  ALA A 159     7615  16044   6126   -550   -218  -1142       C  
ATOM   1102  C   ALA A 159       9.766 -19.351 -52.755  1.00 83.66           C  
ANISOU 1102  C   ALA A 159     8129  16816   6842   -392   -420  -1311       C  
ATOM   1103  O   ALA A 159      10.025 -19.333 -53.959  1.00 83.49           O  
ANISOU 1103  O   ALA A 159     8022  16861   6839   -323   -374  -1418       O  
ATOM   1104  CB  ALA A 159       9.389 -17.169 -51.620  1.00 79.35           C  
ANISOU 1104  CB  ALA A 159     7736  16285   6129   -723    -30  -1210       C  
ATOM   1105  N   LEU A 160      10.349 -20.193 -51.889  1.00 81.21           N  
ANISOU 1105  N   LEU A 160     7795  16521   6540   -319   -662  -1347       N  
ATOM   1106  CA  LEU A 160      11.366 -21.171 -52.266  1.00 82.11           C  
ANISOU 1106  CA  LEU A 160     7771  16738   6689   -111   -916  -1541       C  
ATOM   1107  C   LEU A 160      10.740 -22.382 -52.908  1.00 85.49           C  
ANISOU 1107  C   LEU A 160     8277  16988   7215     74  -1142  -1478       C  
ATOM   1108  O   LEU A 160      11.315 -22.934 -53.839  1.00 85.26           O  
ANISOU 1108  O   LEU A 160     8122  17047   7225    260  -1262  -1649       O  
ATOM   1109  CB  LEU A 160      12.182 -21.602 -51.038  1.00 83.36           C  
ANISOU 1109  CB  LEU A 160     7923  16948   6802    -73  -1131  -1609       C  
ATOM   1110  CG  LEU A 160      13.029 -20.521 -50.399  1.00 87.96           C  
ANISOU 1110  CG  LEU A 160     8395  17744   7282   -238   -948  -1717       C  
ATOM   1111  CD1 LEU A 160      13.587 -20.981 -49.095  1.00 89.55           C  
ANISOU 1111  CD1 LEU A 160     8634  17947   7443   -201  -1171  -1740       C  
ATOM   1112  CD2 LEU A 160      14.109 -20.086 -51.312  1.00 91.54           C  
ANISOU 1112  CD2 LEU A 160     8600  18493   7687   -224   -843  -1984       C  
ATOM   1113  N   ALA A 161       9.567 -22.801 -52.414  1.00 81.91           N  
ANISOU 1113  N   ALA A 161     8027  16308   6788      9  -1202  -1246       N  
ATOM   1114  CA  ALA A 161       8.852 -23.966 -52.930  1.00 82.35           C  
ANISOU 1114  CA  ALA A 161     8201  16172   6917    130  -1420  -1158       C  
ATOM   1115  C   ALA A 161       8.437 -23.783 -54.380  1.00 85.22           C  
ANISOU 1115  C   ALA A 161     8483  16551   7346    201  -1283  -1191       C  
ATOM   1116  O   ALA A 161       8.288 -24.779 -55.092  1.00 85.23           O  
ANISOU 1116  O   ALA A 161     8515  16455   7414    366  -1488  -1211       O  
ATOM   1117  CB  ALA A 161       7.617 -24.240 -52.089  1.00 82.96           C  
ANISOU 1117  CB  ALA A 161     8491  16064   6966    -43  -1443   -909       C  
ATOM   1118  N   ILE A 162       8.230 -22.526 -54.818  1.00 81.10           N  
ANISOU 1118  N   ILE A 162     7892  16128   6795     78   -956  -1195       N  
ATOM   1119  CA  ILE A 162       7.788 -22.278 -56.184  1.00 80.55           C  
ANISOU 1119  CA  ILE A 162     7783  16055   6767    132   -825  -1216       C  
ATOM   1120  C   ILE A 162       9.077 -22.139 -57.076  1.00 84.94           C  
ANISOU 1120  C   ILE A 162     8143  16828   7301    229   -807  -1469       C  
ATOM   1121  O   ILE A 162       9.120 -22.754 -58.141  1.00 83.48           O  
ANISOU 1121  O   ILE A 162     7900  16645   7173    385   -900  -1549       O  
ATOM   1122  CB  ILE A 162       6.784 -21.057 -56.297  1.00 82.22           C  
ANISOU 1122  CB  ILE A 162     8077  16225   6936    -24   -527  -1094       C  
ATOM   1123  CG1 ILE A 162       7.373 -19.654 -55.974  1.00 82.29           C  
ANISOU 1123  CG1 ILE A 162     8069  16362   6833   -182   -283  -1161       C  
ATOM   1124  CG2 ILE A 162       5.500 -21.315 -55.496  1.00 82.20           C  
ANISOU 1124  CG2 ILE A 162     8207  16084   6941   -103   -557   -896       C  
ATOM   1125  CD1 ILE A 162       7.992 -18.915 -57.142  1.00 86.30           C  
ANISOU 1125  CD1 ILE A 162     8518  16986   7287   -204   -120  -1304       C  
ATOM   1126  N   LEU A 163      10.140 -21.460 -56.592  1.00 83.65           N  
ANISOU 1126  N   LEU A 163     7868  16869   7047    135   -716  -1609       N  
ATOM   1127  CA  LEU A 163      11.388 -21.309 -57.359  1.00 85.53           C  
ANISOU 1127  CA  LEU A 163     7885  17386   7227    178   -685  -1878       C  
ATOM   1128  C   LEU A 163      12.152 -22.644 -57.466  1.00 93.45           C  
ANISOU 1128  C   LEU A 163     8754  18468   8284    457  -1024  -2063       C  
ATOM   1129  O   LEU A 163      12.700 -22.959 -58.524  1.00 94.64           O  
ANISOU 1129  O   LEU A 163     8740  18785   8433    588  -1062  -2262       O  
ATOM   1130  CB  LEU A 163      12.302 -20.242 -56.743  1.00 86.16           C  
ANISOU 1130  CB  LEU A 163     7877  17688   7173    -31   -502  -1988       C  
ATOM   1131  CG  LEU A 163      11.783 -18.805 -56.781  1.00 89.80           C  
ANISOU 1131  CG  LEU A 163     8486  18093   7542   -297   -180  -1865       C  
ATOM   1132  CD1 LEU A 163      12.692 -17.891 -56.027  1.00 91.25           C  
ANISOU 1132  CD1 LEU A 163     8613  18469   7590   -508    -47  -1963       C  
ATOM   1133  CD2 LEU A 163      11.631 -18.300 -58.200  1.00 92.28           C  
ANISOU 1133  CD2 LEU A 163     8813  18439   7810   -352     -9  -1909       C  
ATOM   1134  N   GLY A 164      12.163 -23.409 -56.385  1.00 91.96           N  
ANISOU 1134  N   GLY A 164     8660  18155   8126    550  -1282  -2005       N  
ATOM   1135  CA  GLY A 164      12.795 -24.719 -56.353  1.00 94.21           C  
ANISOU 1135  CA  GLY A 164     8902  18444   8449    847  -1668  -2167       C  
ATOM   1136  C   GLY A 164      11.944 -25.743 -57.070  1.00 98.91           C  
ANISOU 1136  C   GLY A 164     9646  18791   9145   1011  -1859  -2061       C  
ATOM   1137  O   GLY A 164      10.762 -25.910 -56.747  1.00 96.53           O  
ANISOU 1137  O   GLY A 164     9575  18217   8884    902  -1853  -1790       O  
ATOM   1138  N   GLY A 165      12.541 -26.403 -58.057  1.00 98.87           N  
ANISOU 1138  N   GLY A 165     9493  18909   9164   1261  -2020  -2290       N  
ATOM   1139  CA  GLY A 165      11.847 -27.385 -58.877  1.00 99.54           C  
ANISOU 1139  CA  GLY A 165     9704  18779   9338   1436  -2212  -2226       C  
ATOM   1140  C   GLY A 165      10.890 -26.694 -59.825  1.00102.77           C  
ANISOU 1140  C   GLY A 165    10127  19139   9782   1269  -1897  -2074       C  
ATOM   1141  O   GLY A 165       9.690 -26.578 -59.531  1.00100.63           O  
ANISOU 1141  O   GLY A 165    10059  18629   9547   1114  -1815  -1801       O  
ATOM   1142  N   LEU A 166      11.443 -26.170 -60.945  1.00100.12           N  
ANISOU 1142  N   LEU A 166     9568  19060   9413   1284  -1711  -2270       N  
ATOM   1143  CA  LEU A 166      10.698 -25.431 -61.971  1.00 98.36           C  
ANISOU 1143  CA  LEU A 166     9363  18813   9196   1141  -1419  -2168       C  
ATOM   1144  C   LEU A 166      11.560 -25.307 -63.274  1.00104.89           C  
ANISOU 1144  C   LEU A 166     9944  19941   9967   1225  -1341  -2449       C  
ATOM   1145  O   LEU A 166      12.475 -26.115 -63.513  1.00105.09           O  
ANISOU 1145  O   LEU A 166     9795  20147   9987   1467  -1577  -2711       O  
ATOM   1146  CB  LEU A 166      10.330 -24.020 -61.387  1.00 96.39           C  
ANISOU 1146  CB  LEU A 166     9185  18566   8873    825  -1081  -2012       C  
ATOM   1147  CG  LEU A 166       8.945 -23.434 -61.727  1.00 97.99           C  
ANISOU 1147  CG  LEU A 166     9576  18550   9106    691   -884  -1766       C  
ATOM   1148  CD1 LEU A 166       7.824 -24.165 -60.972  1.00 96.66           C  
ANISOU 1148  CD1 LEU A 166     9598  18105   9022    715  -1052  -1535       C  
ATOM   1149  CD2 LEU A 166       8.865 -21.995 -61.322  1.00 99.04           C  
ANISOU 1149  CD2 LEU A 166     9764  18733   9135    436   -582  -1700       C  
ATOM   1150  N   SER A 167      11.226 -24.315 -64.118  1.00102.32           N  
ANISOU 1150  N   SER A 167     9624  19668   9585   1031  -1029  -2403       N  
ATOM   1151  CA  SER A 167      12.007 -23.896 -65.273  1.00103.86           C  
ANISOU 1151  CA  SER A 167     9618  20174   9672    988   -873  -2641       C  
ATOM   1152  C   SER A 167      12.862 -22.700 -64.825  1.00110.16           C  
ANISOU 1152  C   SER A 167    10314  21241  10300    698   -621  -2743       C  
ATOM   1153  O   SER A 167      13.764 -22.265 -65.539  1.00110.58           O  
ANISOU 1153  O   SER A 167    10170  21637  10209    586   -480  -2981       O  
ATOM   1154  CB  SER A 167      11.113 -23.588 -66.475  1.00106.34           C  
ANISOU 1154  CB  SER A 167    10057  20347  10002    937   -718  -2520       C  
ATOM   1155  OG  SER A 167      10.206 -22.528 -66.227  1.00113.04           O  
ANISOU 1155  OG  SER A 167    11134  20993  10821    705   -485  -2274       O  
ATOM   1156  N   LYS A 168      12.563 -22.197 -63.593  1.00108.48           N  
ANISOU 1156  N   LYS A 168    10243  20882  10091    560   -572  -2566       N  
ATOM   1157  CA  LYS A 168      13.289 -21.155 -62.854  1.00109.82           C  
ANISOU 1157  CA  LYS A 168    10363  21246  10117    296   -382  -2627       C  
ATOM   1158  C   LYS A 168      14.564 -21.749 -62.256  1.00117.98           C  
ANISOU 1158  C   LYS A 168    11124  22585  11118    429   -575  -2904       C  
ATOM   1159  O   LYS A 168      15.558 -21.047 -62.077  1.00118.66           O  
ANISOU 1159  O   LYS A 168    11040  22997  11049    234   -428  -3093       O  
ATOM   1160  CB  LYS A 168      12.401 -20.534 -61.750  1.00110.02           C  
ANISOU 1160  CB  LYS A 168    10645  20984  10175    153   -298  -2340       C  
ATOM   1161  CG  LYS A 168      11.202 -19.686 -62.217  1.00120.36           C  
ANISOU 1161  CG  LYS A 168    12216  22038  11476     12    -89  -2107       C  
ATOM   1162  CD  LYS A 168      11.462 -18.210 -62.669  1.00133.36           C  
ANISOU 1162  CD  LYS A 168    13964  23777  12928   -301    219  -2131       C  
ATOM   1163  CE  LYS A 168      12.220 -17.924 -63.961  1.00149.47           C  
ANISOU 1163  CE  LYS A 168    15893  26072  14828   -417    342  -2334       C  
ATOM   1164  NZ  LYS A 168      13.681 -18.183 -63.866  1.00161.95           N  
ANISOU 1164  NZ  LYS A 168    17154  28071  16311   -459    309  -2632       N  
ATOM   1165  N   LEU A 169      14.515 -23.068 -61.965  1.00116.94           N  
ANISOU 1165  N   LEU A 169    10973  22341  11118    766   -925  -2937       N  
ATOM   1166  CA  LEU A 169      15.597 -23.922 -61.470  1.00119.98           C  
ANISOU 1166  CA  LEU A 169    11142  22951  11494   1017  -1218  -3215       C  
ATOM   1167  C   LEU A 169      16.839 -23.789 -62.384  1.00128.90           C  
ANISOU 1167  C   LEU A 169    11902  24590  12484   1031  -1149  -3616       C  
ATOM   1168  O   LEU A 169      17.975 -23.853 -61.904  1.00131.05           O  
ANISOU 1168  O   LEU A 169    11921  25208  12664   1088  -1237  -3902       O  
ATOM   1169  CB  LEU A 169      15.062 -25.383 -61.425  1.00120.02           C  
ANISOU 1169  CB  LEU A 169    11292  22657  11653   1379  -1615  -3149       C  
ATOM   1170  CG  LEU A 169      15.999 -26.547 -61.049  1.00127.36           C  
ANISOU 1170  CG  LEU A 169    12089  23713  12590   1752  -2034  -3432       C  
ATOM   1171  CD1 LEU A 169      15.229 -27.682 -60.416  1.00127.34           C  
ANISOU 1171  CD1 LEU A 169    12410  23267  12706   1960  -2398  -3222       C  
ATOM   1172  CD2 LEU A 169      16.808 -27.048 -62.251  1.00131.60           C  
ANISOU 1172  CD2 LEU A 169    12329  24590  13084   1996  -2131  -3803       C  
ATOM   1173  N   HIS A 170      16.607 -23.546 -63.686  1.00126.76           N  
ANISOU 1173  N   HIS A 170    11597  24389  12176    955   -975  -3643       N  
ATOM   1174  CA  HIS A 170      17.649 -23.379 -64.699  1.00129.88           C  
ANISOU 1174  CA  HIS A 170    11654  25282  12411    911   -868  -4009       C  
ATOM   1175  C   HIS A 170      18.267 -21.957 -64.650  1.00131.24           C  
ANISOU 1175  C   HIS A 170    11741  25762  12360    444   -494  -4074       C  
ATOM   1176  O   HIS A 170      19.129 -21.646 -65.486  1.00133.84           O  
ANISOU 1176  O   HIS A 170    11801  26546  12506    298   -347  -4370       O  
ATOM   1177  CB  HIS A 170      17.065 -23.654 -66.099  1.00131.34           C  
ANISOU 1177  CB  HIS A 170    11889  25384  12632    978   -824  -3978       C  
ATOM   1178  CG  HIS A 170      16.476 -25.023 -66.239  1.00135.45           C  
ANISOU 1178  CG  HIS A 170    12508  25608  13347   1402  -1186  -3923       C  
ATOM   1179  ND1 HIS A 170      15.155 -25.279 -65.901  1.00135.32           N  
ANISOU 1179  ND1 HIS A 170    12845  25075  13496   1437  -1257  -3544       N  
ATOM   1180  CD2 HIS A 170      17.050 -26.174 -66.661  1.00140.06           C  
ANISOU 1180  CD2 HIS A 170    12893  26360  13964   1788  -1502  -4215       C  
ATOM   1181  CE1 HIS A 170      14.968 -26.568 -66.136  1.00135.67           C  
ANISOU 1181  CE1 HIS A 170    12919  24970  13661   1803  -1603  -3596       C  
ATOM   1182  NE2 HIS A 170      16.079 -27.149 -66.595  1.00138.76           N  
ANISOU 1182  NE2 HIS A 170    13001  25738  13983   2046  -1775  -3993       N  
ATOM   1183  N   CYS A 171      17.840 -21.108 -63.675  1.00122.04           N  
ANISOU 1183  N   CYS A 171    10813  24366  11191    195   -347  -3813       N  
ATOM   1184  CA  CYS A 171      18.361 -19.747 -63.508  1.00120.85           C  
ANISOU 1184  CA  CYS A 171    10657  24437  10822   -259    -21  -3843       C  
ATOM   1185  C   CYS A 171      19.405 -19.733 -62.378  1.00123.57           C  
ANISOU 1185  C   CYS A 171    10774  25078  11100   -267   -106  -4050       C  
ATOM   1186  O   CYS A 171      19.267 -20.486 -61.412  1.00121.94           O  
ANISOU 1186  O   CYS A 171    10598  24689  11045     19   -376  -3994       O  
ATOM   1187  CB  CYS A 171      17.223 -18.763 -63.236  1.00118.12           C  
ANISOU 1187  CB  CYS A 171    10732  23653  10495   -508    184  -3450       C  
ATOM   1188  SG  CYS A 171      17.727 -17.020 -63.183  1.00122.89           S  
ANISOU 1188  SG  CYS A 171    11452  24435  10806  -1086    567  -3453       S  
ATOM   1189  N   THR A 172      20.468 -18.902 -62.523  1.00121.32           N  
ANISOU 1189  N   THR A 172    10265  25263  10568   -608    115  -4303       N  
ATOM   1190  CA  THR A 172      21.537 -18.770 -61.517  1.00122.77           C  
ANISOU 1190  CA  THR A 172    10198  25793  10654   -659     65  -4536       C  
ATOM   1191  C   THR A 172      21.180 -17.630 -60.537  1.00123.01           C  
ANISOU 1191  C   THR A 172    10524  25579  10633  -1007    266  -4259       C  
ATOM   1192  O   THR A 172      21.567 -17.695 -59.368  1.00123.13           O  
ANISOU 1192  O   THR A 172    10479  25630  10673   -948    152  -4292       O  
ATOM   1193  CB  THR A 172      22.920 -18.548 -62.160  1.00136.81           C  
ANISOU 1193  CB  THR A 172    11530  28278  12173   -849    184  -5001       C  
ATOM   1194  OG1 THR A 172      22.910 -17.344 -62.927  1.00138.66           O  
ANISOU 1194  OG1 THR A 172    11896  28613  12177  -1379    559  -4939       O  
ATOM   1195  CG2 THR A 172      23.358 -19.721 -63.026  1.00137.74           C  
ANISOU 1195  CG2 THR A 172    11312  28690  12333   -451    -48  -5332       C  
ATOM   1196  N   ARG A 173      20.429 -16.600 -61.011  1.00115.71           N  
ANISOU 1196  N   ARG A 173     9940  24391   9633  -1344    540  -3994       N  
ATOM   1197  CA  ARG A 173      19.929 -15.502 -60.172  1.00112.74           C  
ANISOU 1197  CA  ARG A 173     9905  23720   9211  -1634    710  -3717       C  
ATOM   1198  C   ARG A 173      18.992 -16.071 -59.115  1.00112.57           C  
ANISOU 1198  C   ARG A 173    10078  23254   9440  -1322    500  -3445       C  
ATOM   1199  O   ARG A 173      19.123 -15.763 -57.939  1.00111.51           O  
ANISOU 1199  O   ARG A 173     9994  23070   9306  -1382    482  -3382       O  
ATOM   1200  CB  ARG A 173      19.220 -14.446 -61.039  1.00110.20           C  
ANISOU 1200  CB  ARG A 173     9944  23162   8763  -1960    973  -3509       C  
ATOM   1201  CG  ARG A 173      18.628 -13.279 -60.259  1.00112.72           C  
ANISOU 1201  CG  ARG A 173    10660  23147   9023  -2220   1123  -3237       C  
ATOM   1202  CD  ARG A 173      17.794 -12.351 -61.128  1.00119.71           C  
ANISOU 1202  CD  ARG A 173    11959  23726   9800  -2444   1308  -3030       C  
ATOM   1203  NE  ARG A 173      16.630 -13.031 -61.704  1.00128.02           N  
ANISOU 1203  NE  ARG A 173    13138  24437  11067  -2104   1187  -2848       N  
ATOM   1204  CZ  ARG A 173      15.722 -12.451 -62.485  1.00137.05           C  
ANISOU 1204  CZ  ARG A 173    14632  25271  12168  -2174   1283  -2664       C  
ATOM   1205  NH1 ARG A 173      15.819 -11.160 -62.783  1.00120.56           N  
ANISOU 1205  NH1 ARG A 173    12858  23125   9824  -2571   1486  -2621       N  
ATOM   1206  NH2 ARG A 173      14.704 -13.152 -62.963  1.00120.27           N  
ANISOU 1206  NH2 ARG A 173    12573  22881  10244  -1852   1160  -2526       N  
ATOM   1207  N   ASN A 174      18.110 -16.989 -59.543  1.00107.09           N  
ANISOU 1207  N   ASN A 174     9467  22275   8946   -992    325  -3309       N  
ATOM   1208  CA  ASN A 174      17.127 -17.688 -58.717  1.00104.24           C  
ANISOU 1208  CA  ASN A 174     9293  21507   8805   -714    114  -3055       C  
ATOM   1209  C   ASN A 174      17.816 -18.853 -57.936  1.00107.00           C  
ANISOU 1209  C   ASN A 174     9412  21998   9246   -393   -216  -3237       C  
ATOM   1210  O   ASN A 174      17.304 -19.975 -57.854  1.00105.33           O  
ANISOU 1210  O   ASN A 174     9253  21566   9200    -66   -489  -3163       O  
ATOM   1211  CB  ASN A 174      15.986 -18.191 -59.624  1.00103.29           C  
ANISOU 1211  CB  ASN A 174     9345  21078   8824   -537     67  -2873       C  
ATOM   1212  CG  ASN A 174      15.241 -17.087 -60.373  1.00123.83           C  
ANISOU 1212  CG  ASN A 174    12212  23502  11336   -798    343  -2698       C  
ATOM   1213  OD1 ASN A 174      14.864 -17.251 -61.537  1.00119.95           O  
ANISOU 1213  OD1 ASN A 174    11753  22966  10855   -748    375  -2695       O  
ATOM   1214  ND2 ASN A 174      15.056 -15.915 -59.751  1.00112.94           N  
ANISOU 1214  ND2 ASN A 174    11046  22018   9848  -1075    533  -2567       N  
ATOM   1215  N   ALA A 175      18.991 -18.544 -57.368  1.00104.70           N  
ANISOU 1215  N   ALA A 175     8886  22074   8821   -503   -200  -3483       N  
ATOM   1216  CA  ALA A 175      19.838 -19.411 -56.540  1.00106.03           C  
ANISOU 1216  CA  ALA A 175     8830  22434   9021   -231   -501  -3707       C  
ATOM   1217  C   ALA A 175      20.570 -18.559 -55.500  1.00109.55           C  
ANISOU 1217  C   ALA A 175     9208  23085   9332   -488   -380  -3779       C  
ATOM   1218  O   ALA A 175      20.655 -18.945 -54.329  1.00108.47           O  
ANISOU 1218  O   ALA A 175     9114  22843   9256   -343   -581  -3739       O  
ATOM   1219  CB  ALA A 175      20.822 -20.192 -57.403  1.00109.39           C  
ANISOU 1219  CB  ALA A 175     8880  23283   9400      5   -661  -4110       C  
ATOM   1220  N   ILE A 176      21.025 -17.347 -55.924  1.00106.08           N  
ANISOU 1220  N   ILE A 176     8714  22901   8692   -905    -46  -3858       N  
ATOM   1221  CA  ILE A 176      21.670 -16.354 -55.055  1.00105.84           C  
ANISOU 1221  CA  ILE A 176     8657  23056   8501  -1231    119  -3909       C  
ATOM   1222  C   ILE A 176      20.549 -15.673 -54.212  1.00103.13           C  
ANISOU 1222  C   ILE A 176     8739  22218   8229  -1367    222  -3502       C  
ATOM   1223  O   ILE A 176      20.853 -14.909 -53.299  1.00103.19           O  
ANISOU 1223  O   ILE A 176     8804  22264   8141  -1592    323  -3475       O  
ATOM   1224  CB  ILE A 176      22.559 -15.328 -55.847  1.00111.38           C  
ANISOU 1224  CB  ILE A 176     9185  24207   8926  -1673    426  -4143       C  
ATOM   1225  CG1 ILE A 176      21.737 -14.331 -56.705  1.00110.60           C  
ANISOU 1225  CG1 ILE A 176     9435  23844   8743  -2007    718  -3894       C  
ATOM   1226  CG2 ILE A 176      23.645 -16.048 -56.672  1.00114.05           C  
ANISOU 1226  CG2 ILE A 176     9054  25100   9181  -1525    323  -4584       C  
ATOM   1227  CD1 ILE A 176      22.575 -13.228 -57.445  1.00120.12           C  
ANISOU 1227  CD1 ILE A 176    10567  25445   9626  -2531   1025  -4088       C  
ATOM   1228  N   HIS A 177      19.259 -15.974 -54.552  1.00 94.50           N  
ANISOU 1228  N   HIS A 177     7921  20691   7293  -1221    191  -3211       N  
ATOM   1229  CA  HIS A 177      18.017 -15.619 -53.851  1.00 90.48           C  
ANISOU 1229  CA  HIS A 177     7774  19724   6879  -1245    231  -2851       C  
ATOM   1230  C   HIS A 177      17.579 -16.733 -52.946  1.00 90.39           C  
ANISOU 1230  C   HIS A 177     7800  19499   7044   -925    -68  -2742       C  
ATOM   1231  O   HIS A 177      17.179 -16.495 -51.814  1.00 88.24           O  
ANISOU 1231  O   HIS A 177     7691  19043   6791   -973    -82  -2571       O  
ATOM   1232  CB  HIS A 177      16.859 -15.307 -54.827  1.00 89.58           C  
ANISOU 1232  CB  HIS A 177     7912  19317   6808  -1277    367  -2637       C  
ATOM   1233  CG  HIS A 177      17.049 -14.153 -55.746  1.00 93.31           C  
ANISOU 1233  CG  HIS A 177     8476  19888   7091  -1610    649  -2679       C  
ATOM   1234  ND1 HIS A 177      17.100 -12.860 -55.266  1.00 95.30           N  
ANISOU 1234  ND1 HIS A 177     8935  20094   7181  -1942    856  -2606       N  
ATOM   1235  CD2 HIS A 177      16.928 -14.109 -57.091  1.00 94.62           C  
ANISOU 1235  CD2 HIS A 177     8649  20091   7211  -1649    737  -2726       C  
ATOM   1236  CE1 HIS A 177      17.166 -12.086 -56.335  1.00 95.04           C  
ANISOU 1236  CE1 HIS A 177     9024  20103   6985  -2194   1051  -2637       C  
ATOM   1237  NE2 HIS A 177      17.053 -12.794 -57.455  1.00 95.17           N  
ANISOU 1237  NE2 HIS A 177     8922  20173   7064  -2032    994  -2706       N  
ATOM   1238  N   ALA A 178      17.589 -17.970 -53.498  1.00 87.24           N  
ANISOU 1238  N   ALA A 178     7284  19104   6761   -605   -317  -2832       N  
ATOM   1239  CA  ALA A 178      17.189 -19.224 -52.858  1.00 87.25           C  
ANISOU 1239  CA  ALA A 178     7362  18880   6910   -289   -656  -2743       C  
ATOM   1240  C   ALA A 178      17.989 -19.487 -51.595  1.00 94.58           C  
ANISOU 1240  C   ALA A 178     8210  19926   7801   -222   -846  -2858       C  
ATOM   1241  O   ALA A 178      17.562 -20.270 -50.744  1.00 93.92           O  
ANISOU 1241  O   ALA A 178     8292  19595   7799    -57  -1097  -2719       O  
ATOM   1242  CB  ALA A 178      17.369 -20.378 -53.825  1.00 88.92           C  
ANISOU 1242  CB  ALA A 178     7437  19147   7200     22   -889  -2903       C  
ATOM   1243  N   ASN A 179      19.162 -18.841 -51.487  1.00 94.45           N  
ANISOU 1243  N   ASN A 179     7947  20298   7642   -369   -733  -3119       N  
ATOM   1244  CA  ASN A 179      20.042 -18.909 -50.327  1.00 96.15           C  
ANISOU 1244  CA  ASN A 179     8049  20688   7796   -334   -880  -3267       C  
ATOM   1245  C   ASN A 179      19.820 -17.674 -49.449  1.00 98.18           C  
ANISOU 1245  C   ASN A 179     8464  20872   7968   -685   -616  -3090       C  
ATOM   1246  O   ASN A 179      19.807 -17.811 -48.228  1.00 97.46           O  
ANISOU 1246  O   ASN A 179     8474  20667   7888   -651   -747  -3005       O  
ATOM   1247  CB  ASN A 179      21.501 -19.049 -50.737  1.00101.23           C  
ANISOU 1247  CB  ASN A 179     8281  21858   8324   -256   -947  -3710       C  
ATOM   1248  CG  ASN A 179      21.923 -20.401 -51.305  1.00129.74           C  
ANISOU 1248  CG  ASN A 179    11711  25578  12005    181  -1305  -3957       C  
ATOM   1249  OD1 ASN A 179      23.036 -20.880 -51.041  1.00129.97           O  
ANISOU 1249  OD1 ASN A 179    11460  25952  11970    395  -1531  -4308       O  
ATOM   1250  ND2 ASN A 179      21.036 -21.092 -52.019  1.00119.38           N  
ANISOU 1250  ND2 ASN A 179    10570  23967  10823    356  -1400  -3793       N  
ATOM   1251  N   LEU A 180      19.593 -16.479 -50.068  1.00 93.59           N  
ANISOU 1251  N   LEU A 180     7946  20323   7291  -1016   -264  -3023       N  
ATOM   1252  CA  LEU A 180      19.220 -15.255 -49.347  1.00 92.22           C  
ANISOU 1252  CA  LEU A 180     7991  20017   7033  -1333    -21  -2836       C  
ATOM   1253  C   LEU A 180      17.950 -15.518 -48.564  1.00 96.40           C  
ANISOU 1253  C   LEU A 180     8819  20120   7689  -1234   -100  -2508       C  
ATOM   1254  O   LEU A 180      17.859 -15.135 -47.404  1.00 95.89           O  
ANISOU 1254  O   LEU A 180     8868  19974   7593  -1328    -89  -2408       O  
ATOM   1255  CB  LEU A 180      19.046 -14.056 -50.304  1.00 91.44           C  
ANISOU 1255  CB  LEU A 180     7994  19943   6805  -1658    310  -2805       C  
ATOM   1256  CG  LEU A 180      18.497 -12.739 -49.710  1.00 94.19           C  
ANISOU 1256  CG  LEU A 180     8647  20084   7058  -1956    542  -2600       C  
ATOM   1257  CD1 LEU A 180      19.495 -12.074 -48.793  1.00 95.60           C  
ANISOU 1257  CD1 LEU A 180     8731  20506   7087  -2183    604  -2741       C  
ATOM   1258  CD2 LEU A 180      18.157 -11.771 -50.794  1.00 96.05           C  
ANISOU 1258  CD2 LEU A 180     9065  20253   7176  -2200    790  -2549       C  
ATOM   1259  N   PHE A 181      17.000 -16.254 -49.173  1.00 94.08           N  
ANISOU 1259  N   PHE A 181     8634  19584   7528  -1043   -195  -2361       N  
ATOM   1260  CA  PHE A 181      15.762 -16.635 -48.502  1.00 93.66           C  
ANISOU 1260  CA  PHE A 181     8833  19178   7577   -966   -279  -2075       C  
ATOM   1261  C   PHE A 181      16.048 -17.728 -47.461  1.00 99.29           C  
ANISOU 1261  C   PHE A 181     9538  19850   8340   -769   -606  -2087       C  
ATOM   1262  O   PHE A 181      15.359 -17.790 -46.442  1.00 97.70           O  
ANISOU 1262  O   PHE A 181     9530  19442   8149   -812   -650  -1885       O  
ATOM   1263  CB  PHE A 181      14.677 -17.104 -49.499  1.00 94.55           C  
ANISOU 1263  CB  PHE A 181     9052  19074   7797   -847   -284  -1932       C  
ATOM   1264  CG  PHE A 181      14.243 -16.146 -50.599  1.00 95.99           C  
ANISOU 1264  CG  PHE A 181     9300  19238   7935   -998     -9  -1901       C  
ATOM   1265  CD1 PHE A 181      14.324 -14.766 -50.420  1.00 99.67           C  
ANISOU 1265  CD1 PHE A 181     9869  19736   8267  -1266    250  -1884       C  
ATOM   1266  CD2 PHE A 181      13.587 -16.617 -51.732  1.00 97.62           C  
ANISOU 1266  CD2 PHE A 181     9531  19334   8226   -869    -28  -1854       C  
ATOM   1267  CE1 PHE A 181      13.902 -13.886 -51.423  1.00100.23           C  
ANISOU 1267  CE1 PHE A 181    10071  19741   8270  -1399    465  -1849       C  
ATOM   1268  CE2 PHE A 181      13.142 -15.736 -52.722  1.00 99.81           C  
ANISOU 1268  CE2 PHE A 181     9910  19563   8448   -996    202  -1818       C  
ATOM   1269  CZ  PHE A 181      13.306 -14.377 -52.563  1.00 98.24           C  
ANISOU 1269  CZ  PHE A 181     9831  19395   8101  -1258    438  -1815       C  
ATOM   1270  N   ALA A 182      17.091 -18.556 -47.699  1.00 98.38           N  
ANISOU 1270  N   ALA A 182     9207  19943   8230   -555   -845  -2343       N  
ATOM   1271  CA  ALA A 182      17.478 -19.616 -46.775  1.00 99.93           C  
ANISOU 1271  CA  ALA A 182     9429  20089   8450   -331  -1208  -2391       C  
ATOM   1272  C   ALA A 182      18.153 -19.039 -45.516  1.00106.46           C  
ANISOU 1272  C   ALA A 182    10229  21045   9176   -465  -1188  -2445       C  
ATOM   1273  O   ALA A 182      18.128 -19.692 -44.468  1.00106.92           O  
ANISOU 1273  O   ALA A 182    10427  20961   9237   -359  -1443  -2377       O  
ATOM   1274  CB  ALA A 182      18.403 -20.606 -47.458  1.00102.63           C  
ANISOU 1274  CB  ALA A 182     9549  20631   8814    -18  -1488  -2691       C  
ATOM   1275  N   SER A 183      18.735 -17.816 -45.604  1.00104.24           N  
ANISOU 1275  N   SER A 183     9801  21016   8788   -718   -894  -2559       N  
ATOM   1276  CA  SER A 183      19.389 -17.175 -44.453  1.00105.48           C  
ANISOU 1276  CA  SER A 183     9926  21311   8840   -871   -851  -2618       C  
ATOM   1277  C   SER A 183      18.354 -16.546 -43.521  1.00107.81           C  
ANISOU 1277  C   SER A 183    10515  21318   9129  -1069   -703  -2305       C  
ATOM   1278  O   SER A 183      18.554 -16.534 -42.300  1.00108.80           O  
ANISOU 1278  O   SER A 183    10710  21419   9211  -1098   -798  -2269       O  
ATOM   1279  CB  SER A 183      20.391 -16.118 -44.901  1.00111.01           C  
ANISOU 1279  CB  SER A 183    10383  22392   9402  -1107   -600  -2860       C  
ATOM   1280  OG  SER A 183      19.724 -15.034 -45.523  1.00121.27           O  
ANISOU 1280  OG  SER A 183    11825  23592  10662  -1384   -262  -2706       O  
ATOM   1281  N   PHE A 184      17.260 -16.007 -44.096  1.00101.12           N  
ANISOU 1281  N   PHE A 184     9831  20276   8315  -1193   -478  -2100       N  
ATOM   1282  CA  PHE A 184      16.177 -15.407 -43.322  1.00 98.67           C  
ANISOU 1282  CA  PHE A 184     9773  19725   7991  -1347   -337  -1836       C  
ATOM   1283  C   PHE A 184      15.247 -16.478 -42.719  1.00101.03           C  
ANISOU 1283  C   PHE A 184    10250  19767   8370  -1207   -562  -1633       C  
ATOM   1284  O   PHE A 184      14.661 -16.225 -41.663  1.00 99.79           O  
ANISOU 1284  O   PHE A 184    10255  19491   8171  -1320   -530  -1470       O  
ATOM   1285  CB  PHE A 184      15.360 -14.442 -44.178  1.00 98.65           C  
ANISOU 1285  CB  PHE A 184     9879  19627   7975  -1492    -47  -1732       C  
ATOM   1286  CG  PHE A 184      15.996 -13.100 -44.413  1.00100.38           C  
ANISOU 1286  CG  PHE A 184    10073  20009   8058  -1740    208  -1848       C  
ATOM   1287  CD1 PHE A 184      15.663 -12.010 -43.626  1.00102.88           C  
ANISOU 1287  CD1 PHE A 184    10567  20243   8279  -1936    378  -1747       C  
ATOM   1288  CD2 PHE A 184      16.922 -12.922 -45.427  1.00103.79           C  
ANISOU 1288  CD2 PHE A 184    10319  20684   8434  -1797    273  -2064       C  
ATOM   1289  CE1 PHE A 184      16.240 -10.763 -43.855  1.00104.69           C  
ANISOU 1289  CE1 PHE A 184    10832  20587   8358  -2192    593  -1845       C  
ATOM   1290  CE2 PHE A 184      17.487 -11.670 -45.664  1.00107.52           C  
ANISOU 1290  CE2 PHE A 184    10812  21300   8742  -2091    510  -2159       C  
ATOM   1291  CZ  PHE A 184      17.153 -10.602 -44.868  1.00105.22           C  
ANISOU 1291  CZ  PHE A 184    10739  20883   8356  -2289    659  -2043       C  
ATOM   1292  N   VAL A 185      15.110 -17.664 -43.376  1.00 97.67           N  
ANISOU 1292  N   VAL A 185     9809  19263   8039   -986   -791  -1646       N  
ATOM   1293  CA  VAL A 185      14.236 -18.748 -42.891  1.00 97.24           C  
ANISOU 1293  CA  VAL A 185     9961  18953   8032   -896  -1023  -1452       C  
ATOM   1294  C   VAL A 185      14.933 -19.442 -41.701  1.00101.24           C  
ANISOU 1294  C   VAL A 185    10528  19454   8483   -818  -1323  -1499       C  
ATOM   1295  O   VAL A 185      14.245 -19.852 -40.761  1.00101.27           O  
ANISOU 1295  O   VAL A 185    10759  19270   8450   -893  -1431  -1304       O  
ATOM   1296  CB  VAL A 185      13.826 -19.772 -44.002  1.00101.77           C  
ANISOU 1296  CB  VAL A 185    10546  19413   8710   -701  -1183  -1443       C  
ATOM   1297  CG1 VAL A 185      15.010 -20.601 -44.488  1.00103.66           C  
ANISOU 1297  CG1 VAL A 185    10619  19792   8975   -437  -1458  -1703       C  
ATOM   1298  CG2 VAL A 185      12.703 -20.690 -43.530  1.00101.41           C  
ANISOU 1298  CG2 VAL A 185    10759  19094   8680   -711  -1357  -1203       C  
ATOM   1299  N   LEU A 186      16.289 -19.525 -41.726  1.00 97.42           N  
ANISOU 1299  N   LEU A 186     9842  19201   7974   -682  -1453  -1771       N  
ATOM   1300  CA  LEU A 186      17.084 -20.123 -40.653  1.00 98.28           C  
ANISOU 1300  CA  LEU A 186     9991  19331   8021   -565  -1761  -1865       C  
ATOM   1301  C   LEU A 186      17.000 -19.266 -39.380  1.00100.01           C  
ANISOU 1301  C   LEU A 186    10299  19557   8144   -808  -1605  -1756       C  
ATOM   1302  O   LEU A 186      16.888 -19.812 -38.285  1.00 99.65           O  
ANISOU 1302  O   LEU A 186    10455  19363   8042   -802  -1824  -1653       O  
ATOM   1303  CB  LEU A 186      18.534 -20.274 -41.108  1.00100.31           C  
ANISOU 1303  CB  LEU A 186     9945  19906   8263   -356  -1899  -2232       C  
ATOM   1304  CG  LEU A 186      19.436 -21.137 -40.230  1.00107.85           C  
ANISOU 1304  CG  LEU A 186    10926  20888   9163   -117  -2312  -2396       C  
ATOM   1305  CD1 LEU A 186      19.008 -22.611 -40.283  1.00109.09           C  
ANISOU 1305  CD1 LEU A 186    11350  20737   9364    145  -2730  -2311       C  
ATOM   1306  CD2 LEU A 186      20.880 -21.027 -40.680  1.00112.40           C  
ANISOU 1306  CD2 LEU A 186    11121  21882   9702     58  -2378  -2809       C  
ATOM   1307  N   LYS A 187      17.019 -17.921 -39.548  1.00 95.34           N  
ANISOU 1307  N   LYS A 187     9589  19118   7518  -1031  -1235  -1773       N  
ATOM   1308  CA  LYS A 187      16.891 -16.918 -38.485  1.00 94.69           C  
ANISOU 1308  CA  LYS A 187     9585  19052   7343  -1271  -1040  -1681       C  
ATOM   1309  C   LYS A 187      15.492 -16.953 -37.838  1.00 98.51           C  
ANISOU 1309  C   LYS A 187    10336  19278   7816  -1401   -979  -1381       C  
ATOM   1310  O   LYS A 187      15.391 -17.128 -36.622  1.00 99.16           O  
ANISOU 1310  O   LYS A 187    10564  19289   7824  -1470  -1086  -1287       O  
ATOM   1311  CB  LYS A 187      17.163 -15.505 -39.049  1.00 95.63           C  
ANISOU 1311  CB  LYS A 187     9566  19354   7417  -1469   -680  -1773       C  
ATOM   1312  CG  LYS A 187      16.883 -14.376 -38.052  1.00 99.00           C  
ANISOU 1312  CG  LYS A 187    10112  19758   7744  -1714   -465  -1668       C  
ATOM   1313  CD  LYS A 187      16.797 -13.032 -38.748  1.00 99.17           C  
ANISOU 1313  CD  LYS A 187    10120  19848   7715  -1911   -130  -1697       C  
ATOM   1314  CE  LYS A 187      16.338 -11.934 -37.823  1.00 94.51           C  
ANISOU 1314  CE  LYS A 187     9697  19185   7026  -2116     61  -1583       C  
ATOM   1315  NZ  LYS A 187      16.139 -10.655 -38.555  1.00 93.80           N  
ANISOU 1315  NZ  LYS A 187     9677  19092   6871  -2287    344  -1597       N  
ATOM   1316  N   ALA A 188      14.427 -16.732 -38.647  1.00 94.13           N  
ANISOU 1316  N   ALA A 188     9830  18617   7317  -1446   -796  -1252       N  
ATOM   1317  CA  ALA A 188      13.025 -16.671 -38.208  1.00 93.38           C  
ANISOU 1317  CA  ALA A 188     9927  18353   7200  -1574   -698  -1012       C  
ATOM   1318  C   ALA A 188      12.620 -17.923 -37.421  1.00 99.09           C  
ANISOU 1318  C   ALA A 188    10842  18914   7895  -1552   -993   -873       C  
ATOM   1319  O   ALA A 188      11.924 -17.805 -36.413  1.00 98.45           O  
ANISOU 1319  O   ALA A 188    10908  18777   7720  -1721   -952   -722       O  
ATOM   1320  CB  ALA A 188      12.107 -16.505 -39.410  1.00 92.62           C  
ANISOU 1320  CB  ALA A 188     9816  18195   7182  -1549   -536   -953       C  
ATOM   1321  N   SER A 189      13.069 -19.112 -37.877  1.00 97.05           N  
ANISOU 1321  N   SER A 189    10600  18581   7693  -1352  -1300   -933       N  
ATOM   1322  CA  SER A 189      12.798 -20.392 -37.215  1.00 98.04           C  
ANISOU 1322  CA  SER A 189    10975  18508   7766  -1326  -1641   -810       C  
ATOM   1323  C   SER A 189      13.574 -20.499 -35.894  1.00101.16           C  
ANISOU 1323  C   SER A 189    11468  18918   8051  -1349  -1829   -847       C  
ATOM   1324  O   SER A 189      13.065 -21.080 -34.937  1.00100.87           O  
ANISOU 1324  O   SER A 189    11695  18725   7906  -1477  -1988   -679       O  
ATOM   1325  CB  SER A 189      13.156 -21.553 -38.135  1.00103.26           C  
ANISOU 1325  CB  SER A 189    11649  19073   8512  -1066  -1942   -899       C  
ATOM   1326  OG  SER A 189      14.506 -21.462 -38.560  1.00115.35           O  
ANISOU 1326  OG  SER A 189    12953  20788  10088   -841  -2034  -1177       O  
ATOM   1327  N   SER A 190      14.795 -19.931 -35.840  1.00 97.41           N  
ANISOU 1327  N   SER A 190    10784  18644   7583  -1249  -1808  -1072       N  
ATOM   1328  CA  SER A 190      15.599 -19.933 -34.623  1.00 98.58           C  
ANISOU 1328  CA  SER A 190    10991  18838   7628  -1254  -1975  -1137       C  
ATOM   1329  C   SER A 190      14.931 -19.074 -33.554  1.00102.57           C  
ANISOU 1329  C   SER A 190    11598  19343   8031  -1548  -1731   -967       C  
ATOM   1330  O   SER A 190      14.814 -19.524 -32.416  1.00104.09           O  
ANISOU 1330  O   SER A 190    12016  19425   8110  -1633  -1912   -857       O  
ATOM   1331  CB  SER A 190      17.017 -19.448 -34.897  1.00101.22           C  
ANISOU 1331  CB  SER A 190    11030  19445   7983  -1105  -1973  -1443       C  
ATOM   1332  OG  SER A 190      17.703 -20.336 -35.762  1.00108.46           O  
ANISOU 1332  OG  SER A 190    11840  20400   8970   -803  -2244  -1640       O  
ATOM   1333  N   VAL A 191      14.412 -17.884 -33.938  1.00 96.70           N  
ANISOU 1333  N   VAL A 191    10723  18706   7313  -1698  -1341   -941       N  
ATOM   1334  CA  VAL A 191      13.721 -16.961 -33.029  1.00 95.47           C  
ANISOU 1334  CA  VAL A 191    10642  18573   7060  -1943  -1093   -813       C  
ATOM   1335  C   VAL A 191      12.445 -17.637 -32.463  1.00 99.00           C  
ANISOU 1335  C   VAL A 191    11328  18859   7430  -2090  -1155   -575       C  
ATOM   1336  O   VAL A 191      12.144 -17.434 -31.297  1.00 99.10           O  
ANISOU 1336  O   VAL A 191    11465  18876   7313  -2267  -1131   -481       O  
ATOM   1337  CB  VAL A 191      13.379 -15.611 -33.718  1.00 97.88           C  
ANISOU 1337  CB  VAL A 191    10801  18988   7401  -2023   -713   -854       C  
ATOM   1338  CG1 VAL A 191      12.638 -14.668 -32.768  1.00 97.07           C  
ANISOU 1338  CG1 VAL A 191    10787  18908   7188  -2229   -489   -750       C  
ATOM   1339  CG2 VAL A 191      14.635 -14.933 -34.262  1.00 97.97           C  
ANISOU 1339  CG2 VAL A 191    10605  19176   7444  -1959   -641  -1083       C  
ATOM   1340  N   LEU A 192      11.735 -18.465 -33.259  1.00 96.03           N  
ANISOU 1340  N   LEU A 192    11014  18359   7112  -2038  -1243   -488       N  
ATOM   1341  CA  LEU A 192      10.514 -19.146 -32.787  1.00 96.74           C  
ANISOU 1341  CA  LEU A 192    11322  18331   7103  -2228  -1297   -275       C  
ATOM   1342  C   LEU A 192      10.836 -20.348 -31.884  1.00103.06           C  
ANISOU 1342  C   LEU A 192    12409  18963   7786  -2262  -1683   -192       C  
ATOM   1343  O   LEU A 192       9.917 -20.914 -31.299  1.00103.51           O  
ANISOU 1343  O   LEU A 192    12689  18932   7708  -2489  -1742    -10       O  
ATOM   1344  CB  LEU A 192       9.611 -19.631 -33.946  1.00 96.13           C  
ANISOU 1344  CB  LEU A 192    11228  18184   7113  -2189  -1263   -211       C  
ATOM   1345  CG  LEU A 192       8.969 -18.577 -34.871  1.00 98.84           C  
ANISOU 1345  CG  LEU A 192    11359  18650   7544  -2171   -910   -256       C  
ATOM   1346  CD1 LEU A 192       8.099 -19.253 -35.897  1.00 98.54           C  
ANISOU 1346  CD1 LEU A 192    11334  18530   7577  -2132   -937   -186       C  
ATOM   1347  CD2 LEU A 192       8.113 -17.559 -34.092  1.00100.55           C  
ANISOU 1347  CD2 LEU A 192    11558  19000   7648  -2373   -629   -202       C  
ATOM   1348  N   VAL A 193      12.112 -20.746 -31.781  1.00101.77           N  
ANISOU 1348  N   VAL A 193    12254  18764   7651  -2046  -1956   -337       N  
ATOM   1349  CA  VAL A 193      12.531 -21.835 -30.889  1.00104.85           C  
ANISOU 1349  CA  VAL A 193    12957  18967   7913  -2032  -2370   -284       C  
ATOM   1350  C   VAL A 193      13.005 -21.179 -29.558  1.00111.20           C  
ANISOU 1350  C   VAL A 193    13786  19870   8594  -2159  -2322   -299       C  
ATOM   1351  O   VAL A 193      12.774 -21.736 -28.483  1.00112.05           O  
ANISOU 1351  O   VAL A 193    14200  19848   8528  -2329  -2515   -160       O  
ATOM   1352  CB  VAL A 193      13.599 -22.764 -31.541  1.00110.06           C  
ANISOU 1352  CB  VAL A 193    13631  19527   8660  -1671  -2757   -462       C  
ATOM   1353  CG1 VAL A 193      14.062 -23.853 -30.577  1.00112.71           C  
ANISOU 1353  CG1 VAL A 193    14344  19638   8843  -1620  -3232   -425       C  
ATOM   1354  CG2 VAL A 193      13.053 -23.400 -32.816  1.00109.27           C  
ANISOU 1354  CG2 VAL A 193    13523  19325   8672  -1564  -2796   -435       C  
ATOM   1355  N   ILE A 194      13.595 -19.955 -29.644  1.00108.29           N  
ANISOU 1355  N   ILE A 194    13118  19730   8298  -2113  -2047   -457       N  
ATOM   1356  CA  ILE A 194      14.010 -19.155 -28.478  1.00109.09           C  
ANISOU 1356  CA  ILE A 194    13206  19949   8294  -2240  -1947   -484       C  
ATOM   1357  C   ILE A 194      12.735 -18.729 -27.742  1.00114.49           C  
ANISOU 1357  C   ILE A 194    14007  20645   8849  -2564  -1707   -279       C  
ATOM   1358  O   ILE A 194      12.559 -19.101 -26.588  1.00115.91           O  
ANISOU 1358  O   ILE A 194    14425  20756   8858  -2737  -1843   -163       O  
ATOM   1359  CB  ILE A 194      14.920 -17.934 -28.863  1.00110.76           C  
ANISOU 1359  CB  ILE A 194    13086  20399   8600  -2144  -1707   -706       C  
ATOM   1360  CG1 ILE A 194      16.098 -18.312 -29.821  1.00111.63           C  
ANISOU 1360  CG1 ILE A 194    13000  20584   8832  -1840  -1893   -950       C  
ATOM   1361  CG2 ILE A 194      15.380 -17.129 -27.640  1.00111.18           C  
ANISOU 1361  CG2 ILE A 194    13139  20564   8538  -2278  -1623   -739       C  
ATOM   1362  CD1 ILE A 194      17.067 -19.450 -29.378  1.00120.26           C  
ANISOU 1362  CD1 ILE A 194    14222  21593   9880  -1607  -2370  -1062       C  
ATOM   1363  N   ASP A 195      11.812 -18.038 -28.456  1.00110.63           N  
ANISOU 1363  N   ASP A 195    13361  20246   8425  -2637  -1376   -246       N  
ATOM   1364  CA  ASP A 195      10.487 -17.605 -27.988  1.00111.15           C  
ANISOU 1364  CA  ASP A 195    13470  20384   8378  -2899  -1128   -104       C  
ATOM   1365  C   ASP A 195       9.693 -18.774 -27.363  1.00117.60           C  
ANISOU 1365  C   ASP A 195    14580  21073   9029  -3117  -1336     92       C  
ATOM   1366  O   ASP A 195       9.082 -18.608 -26.299  1.00118.18           O  
ANISOU 1366  O   ASP A 195    14763  21222   8917  -3382  -1255    192       O  
ATOM   1367  CB  ASP A 195       9.698 -17.012 -29.179  1.00111.80           C  
ANISOU 1367  CB  ASP A 195    13355  20542   8581  -2842   -850   -133       C  
ATOM   1368  CG  ASP A 195       8.235 -16.670 -28.933  1.00128.40           C  
ANISOU 1368  CG  ASP A 195    15456  22753  10577  -3052   -618    -32       C  
ATOM   1369  OD1 ASP A 195       7.897 -16.256 -27.790  1.00131.94           O  
ANISOU 1369  OD1 ASP A 195    15960  23308  10863  -3245   -527      7       O  
ATOM   1370  OD2 ASP A 195       7.441 -16.734 -29.902  1.00132.57           O  
ANISOU 1370  OD2 ASP A 195    15899  23291  11180  -3008   -514    -20       O  
ATOM   1371  N   GLY A 196       9.712 -19.923 -28.046  1.00114.92           N  
ANISOU 1371  N   GLY A 196    14374  20549   8740  -3021  -1600    138       N  
ATOM   1372  CA  GLY A 196       9.019 -21.137 -27.634  1.00116.89           C  
ANISOU 1372  CA  GLY A 196    14956  20634   8825  -3239  -1839    326       C  
ATOM   1373  C   GLY A 196       9.541 -21.730 -26.345  1.00124.36           C  
ANISOU 1373  C   GLY A 196    16226  21449   9576  -3362  -2138    399       C  
ATOM   1374  O   GLY A 196       8.764 -21.939 -25.412  1.00125.70           O  
ANISOU 1374  O   GLY A 196    16601  21639   9521  -3709  -2115    555       O  
ATOM   1375  N   LEU A 197      10.868 -21.983 -26.275  1.00122.16           N  
ANISOU 1375  N   LEU A 197    15989  21061   9366  -3080  -2420    269       N  
ATOM   1376  CA  LEU A 197      11.526 -22.571 -25.099  1.00124.70           C  
ANISOU 1376  CA  LEU A 197    16638  21232   9512  -3123  -2763    306       C  
ATOM   1377  C   LEU A 197      11.547 -21.613 -23.895  1.00129.18           C  
ANISOU 1377  C   LEU A 197    17146  21982   9953  -3324  -2544    314       C  
ATOM   1378  O   LEU A 197      11.554 -22.097 -22.759  1.00130.79           O  
ANISOU 1378  O   LEU A 197    17679  22077   9938  -3520  -2752    427       O  
ATOM   1379  CB  LEU A 197      12.977 -23.003 -25.411  1.00125.61           C  
ANISOU 1379  CB  LEU A 197    16745  21241   9742  -2708  -3119    104       C  
ATOM   1380  CG  LEU A 197      13.219 -24.430 -25.966  1.00132.34           C  
ANISOU 1380  CG  LEU A 197    17897  21793  10593  -2505  -3590    112       C  
ATOM   1381  CD1 LEU A 197      12.846 -25.496 -24.944  1.00135.85           C  
ANISOU 1381  CD1 LEU A 197    18906  21948  10762  -2752  -3952    322       C  
ATOM   1382  CD2 LEU A 197      12.512 -24.681 -27.286  1.00133.38           C  
ANISOU 1382  CD2 LEU A 197    17904  21907  10867  -2464  -3468    141       C  
ATOM   1383  N   LEU A 198      11.533 -20.274 -24.126  1.00123.94           N  
ANISOU 1383  N   LEU A 198    16107  21576   9408  -3288  -2144    199       N  
ATOM   1384  CA  LEU A 198      11.553 -19.293 -23.030  1.00123.79           C  
ANISOU 1384  CA  LEU A 198    16026  21731   9276  -3456  -1930    188       C  
ATOM   1385  C   LEU A 198      10.181 -19.231 -22.301  1.00128.61           C  
ANISOU 1385  C   LEU A 198    16756  22437   9673  -3854  -1736    368       C  
ATOM   1386  O   LEU A 198      10.079 -18.561 -21.269  1.00128.02           O  
ANISOU 1386  O   LEU A 198    16677  22503   9462  -4027  -1589    374       O  
ATOM   1387  CB  LEU A 198      11.954 -17.878 -23.508  1.00121.37           C  
ANISOU 1387  CB  LEU A 198    15338  21642   9135  -3306  -1590      7       C  
ATOM   1388  CG  LEU A 198      13.422 -17.659 -23.961  1.00125.39           C  
ANISOU 1388  CG  LEU A 198    15676  22168   9799  -2993  -1716   -210       C  
ATOM   1389  CD1 LEU A 198      13.636 -16.233 -24.404  1.00123.37           C  
ANISOU 1389  CD1 LEU A 198    15107  22117   9652  -2949  -1355   -354       C  
ATOM   1390  CD2 LEU A 198      14.424 -17.977 -22.850  1.00129.88           C  
ANISOU 1390  CD2 LEU A 198    16407  22686  10253  -2957  -2006   -258       C  
ATOM   1391  N   ARG A 199       9.158 -19.962 -22.800  1.00126.48           N  
ANISOU 1391  N   ARG A 199    16589  22111   9355  -4010  -1749    497       N  
ATOM   1392  CA  ARG A 199       7.856 -20.041 -22.139  1.00127.78           C  
ANISOU 1392  CA  ARG A 199    16854  22413   9283  -4418  -1588    643       C  
ATOM   1393  C   ARG A 199       7.360 -21.509 -22.186  1.00133.78           C  
ANISOU 1393  C   ARG A 199    17990  22952   9888  -4634  -1895    826       C  
ATOM   1394  O   ARG A 199       6.496 -21.866 -22.994  1.00133.00           O  
ANISOU 1394  O   ARG A 199    17840  22877   9817  -4710  -1817    876       O  
ATOM   1395  CB  ARG A 199       6.827 -19.057 -22.755  1.00126.68           C  
ANISOU 1395  CB  ARG A 199    16359  22556   9220  -4439  -1161    572       C  
ATOM   1396  CG  ARG A 199       5.471 -18.930 -21.999  1.00139.84           C  
ANISOU 1396  CG  ARG A 199    18029  24479  10623  -4845   -944    652       C  
ATOM   1397  CD  ARG A 199       5.508 -18.296 -20.588  1.00152.38           C  
ANISOU 1397  CD  ARG A 199    19651  26240  12005  -5047   -837    643       C  
ATOM   1398  NE  ARG A 199       6.220 -19.102 -19.583  1.00160.39           N  
ANISOU 1398  NE  ARG A 199    21044  27046  12852  -5195  -1167    762       N  
ATOM   1399  CZ  ARG A 199       6.350 -18.772 -18.298  1.00167.70           C  
ANISOU 1399  CZ  ARG A 199    22073  28070  13574  -5392  -1144    781       C  
ATOM   1400  NH1 ARG A 199       5.801 -17.655 -17.834  1.00152.11           N  
ANISOU 1400  NH1 ARG A 199    19843  26415  11537  -5468   -802    681       N  
ATOM   1401  NH2 ARG A 199       7.018 -19.562 -17.467  1.00149.52           N  
ANISOU 1401  NH2 ARG A 199    20149  25543  11119  -5502  -1482    890       N  
ATOM   1402  N   THR A 200       7.961 -22.354 -21.321  1.00132.48           N  
ANISOU 1402  N   THR A 200    18232  22554   9550  -4723  -2269    920       N  
ATOM   1403  CA  THR A 200       7.643 -23.778 -21.130  1.00159.27           C  
ANISOU 1403  CA  THR A 200    22112  25671  12734  -4961  -2637   1108       C  
ATOM   1404  C   THR A 200       7.706 -24.141 -19.634  1.00192.52           C  
ANISOU 1404  C   THR A 200    26726  29809  16614  -5301  -2824   1240       C  
ATOM   1405  O   THR A 200       8.201 -23.365 -18.811  1.00149.93           O  
ANISOU 1405  O   THR A 200    21225  24546  11196  -5269  -2718   1167       O  
ATOM   1406  CB  THR A 200       8.578 -24.698 -21.947  1.00166.69           C  
ANISOU 1406  CB  THR A 200    23233  26266  13836  -4579  -3061   1058       C  
ATOM   1407  OG1 THR A 200       9.936 -24.308 -21.731  1.00165.29           O  
ANISOU 1407  OG1 THR A 200    22963  26048  13793  -4204  -3205    886       O  
ATOM   1408  CG2 THR A 200       8.274 -24.683 -23.438  1.00163.29           C  
ANISOU 1408  CG2 THR A 200    22519  25867  13658  -4353  -2929    984       C  
ATOM   1409  N   LEU A 216      16.851 -33.562 -16.195  1.00191.21           N  
ANISOU 1409  N   LEU A 216    31470  25820  15364  -2723  -8872    882       N  
ATOM   1410  CA  LEU A 216      15.448 -33.716 -16.571  1.00190.22           C  
ANISOU 1410  CA  LEU A 216    31433  25689  15152  -3300  -8534   1183       C  
ATOM   1411  C   LEU A 216      15.000 -32.542 -17.460  1.00190.73           C  
ANISOU 1411  C   LEU A 216    30619  26281  15567  -3325  -7799   1099       C  
ATOM   1412  O   LEU A 216      14.737 -32.741 -18.650  1.00188.45           O  
ANISOU 1412  O   LEU A 216    30111  26010  15480  -3164  -7718   1047       O  
ATOM   1413  CB  LEU A 216      14.546 -33.820 -15.314  1.00192.24           C  
ANISOU 1413  CB  LEU A 216    32195  25853  14995  -4043  -8452   1528       C  
ATOM   1414  CG  LEU A 216      14.779 -35.006 -14.355  1.00197.87           C  
ANISOU 1414  CG  LEU A 216    33125  26410  15647  -3664  -8602   1475       C  
ATOM   1415  CD1 LEU A 216      13.988 -34.834 -13.075  1.00197.37           C  
ANISOU 1415  CD1 LEU A 216    33082  26512  15399  -4096  -8194   1658       C  
ATOM   1416  CD2 LEU A 216      14.437 -36.342 -15.007  1.00199.69           C  
ANISOU 1416  CD2 LEU A 216    33310  26537  16027  -3308  -8599   1440       C  
ATOM   1417  N   SER A 217      14.933 -31.320 -16.880  1.00186.33           N  
ANISOU 1417  N   SER A 217    29591  26134  15070  -3510  -7290   1080       N  
ATOM   1418  CA  SER A 217      14.532 -30.084 -17.565  1.00182.15           C  
ANISOU 1418  CA  SER A 217    28281  26092  14836  -3544  -6605    997       C  
ATOM   1419  C   SER A 217      15.618 -29.611 -18.535  1.00184.03           C  
ANISOU 1419  C   SER A 217    27956  26522  15443  -2907  -6584    646       C  
ATOM   1420  O   SER A 217      15.295 -29.083 -19.602  1.00179.95           O  
ANISOU 1420  O   SER A 217    26946  26246  15182  -2833  -6202    575       O  
ATOM   1421  CB  SER A 217      14.234 -28.985 -16.546  1.00184.86           C  
ANISOU 1421  CB  SER A 217    28385  26762  15091  -3899  -6160   1063       C  
ATOM   1422  OG  SER A 217      13.845 -27.766 -17.162  1.00189.80           O  
ANISOU 1422  OG  SER A 217    28315  27824  15976  -3918  -5536    977       O  
ATOM   1423  N   ASP A 218      16.905 -29.833 -18.169  1.00182.98           N  
ANISOU 1423  N   ASP A 218    27913  26295  15317  -2455  -7013    414       N  
ATOM   1424  CA  ASP A 218      18.102 -29.461 -18.937  1.00181.67           C  
ANISOU 1424  CA  ASP A 218    27237  26347  15442  -1851  -7062     33       C  
ATOM   1425  C   ASP A 218      18.091 -30.146 -20.330  1.00184.95           C  
ANISOU 1425  C   ASP A 218    27588  26651  16033  -1535  -7226    -71       C  
ATOM   1426  O   ASP A 218      18.804 -29.705 -21.234  1.00183.18           O  
ANISOU 1426  O   ASP A 218    26829  26698  16074  -1132  -7109   -365       O  
ATOM   1427  CB  ASP A 218      19.376 -29.843 -18.142  1.00187.05           C  
ANISOU 1427  CB  ASP A 218    28160  26898  16012  -1459  -7605   -183       C  
ATOM   1428  CG  ASP A 218      20.700 -29.286 -18.656  1.00195.60           C  
ANISOU 1428  CG  ASP A 218    28657  28319  17344   -899  -7614   -615       C  
ATOM   1429  OD1 ASP A 218      20.674 -28.360 -19.498  1.00191.52           O  
ANISOU 1429  OD1 ASP A 218    27503  28183  17083   -879  -7113   -732       O  
ATOM   1430  OD2 ASP A 218      21.756 -29.690 -18.125  1.00205.34           O  
ANISOU 1430  OD2 ASP A 218    30063  29467  18491   -519  -8100   -837       O  
ATOM   1431  N   GLY A 219      17.231 -31.161 -20.498  1.00182.40           N  
ANISOU 1431  N   GLY A 219    27796  25961  15548  -1768  -7457    177       N  
ATOM   1432  CA  GLY A 219      17.021 -31.855 -21.766  1.00181.73           C  
ANISOU 1432  CA  GLY A 219    27715  25736  15597  -1550  -7598    131       C  
ATOM   1433  C   GLY A 219      16.269 -30.998 -22.771  1.00180.59           C  
ANISOU 1433  C   GLY A 219    26976  25939  15700  -1719  -6956    162       C  
ATOM   1434  O   GLY A 219      16.069 -31.406 -23.919  1.00179.15           O  
ANISOU 1434  O   GLY A 219    26698  25706  15664  -1545  -6984    113       O  
ATOM   1435  N   ALA A 220      15.853 -29.790 -22.331  1.00174.17           N  
ANISOU 1435  N   ALA A 220    25778  25473  14925  -2045  -6390    235       N  
ATOM   1436  CA  ALA A 220      15.150 -28.780 -23.120  1.00169.66           C  
ANISOU 1436  CA  ALA A 220    24646  25252  14564  -2210  -5762    253       C  
ATOM   1437  C   ALA A 220      15.776 -27.377 -22.914  1.00170.39           C  
ANISOU 1437  C   ALA A 220    24169  25756  14813  -2114  -5356     61       C  
ATOM   1438  O   ALA A 220      15.807 -26.590 -23.861  1.00167.06           O  
ANISOU 1438  O   ALA A 220    23234  25611  14631  -1990  -4985    -74       O  
ATOM   1439  CB  ALA A 220      13.675 -28.760 -22.748  1.00169.95           C  
ANISOU 1439  CB  ALA A 220    24880  25270  14421  -2811  -5471    581       C  
ATOM   1440  N   VAL A 221      16.287 -27.080 -21.683  1.00167.61           N  
ANISOU 1440  N   VAL A 221    23943  25429  14312  -2180  -5445     49       N  
ATOM   1441  CA  VAL A 221      16.913 -25.792 -21.309  1.00165.08           C  
ANISOU 1441  CA  VAL A 221    23160  25468  14095  -2128  -5107   -121       C  
ATOM   1442  C   VAL A 221      18.185 -25.563 -22.174  1.00167.62           C  
ANISOU 1442  C   VAL A 221    23056  25981  14649  -1608  -5197   -490       C  
ATOM   1443  O   VAL A 221      18.410 -24.446 -22.650  1.00164.08           O  
ANISOU 1443  O   VAL A 221    22095  25873  14376  -1582  -4776   -631       O  
ATOM   1444  CB  VAL A 221      17.241 -25.728 -19.784  1.00170.97           C  
ANISOU 1444  CB  VAL A 221    24203  26151  14605  -2287  -5274    -59       C  
ATOM   1445  CG1 VAL A 221      17.959 -24.430 -19.421  1.00169.11           C  
ANISOU 1445  CG1 VAL A 221    23503  26277  14474  -2216  -4956   -252       C  
ATOM   1446  CG2 VAL A 221      15.979 -25.882 -18.939  1.00171.30           C  
ANISOU 1446  CG2 VAL A 221    24619  26075  14392  -2846  -5140    283       C  
ATOM   1447  N   ALA A 222      18.981 -26.626 -22.394  1.00167.00           N  
ANISOU 1447  N   ALA A 222    23208  25694  14551  -1208  -5751   -653       N  
ATOM   1448  CA  ALA A 222      20.181 -26.581 -23.233  1.00167.02           C  
ANISOU 1448  CA  ALA A 222    22816  25905  14738   -700  -5893  -1038       C  
ATOM   1449  C   ALA A 222      19.815 -26.749 -24.721  1.00168.67           C  
ANISOU 1449  C   ALA A 222    22786  26159  15143   -577  -5747  -1082       C  
ATOM   1450  O   ALA A 222      20.666 -26.559 -25.594  1.00167.71           O  
ANISOU 1450  O   ALA A 222    22252  26284  15185   -222  -5747  -1397       O  
ATOM   1451  CB  ALA A 222      21.162 -27.664 -22.802  1.00171.99           C  
ANISOU 1451  CB  ALA A 222    23799  26307  15243   -283  -6582  -1227       C  
ATOM   1452  N   GLY A 223      18.552 -27.084 -24.982  1.00164.39           N  
ANISOU 1452  N   GLY A 223    22489  25408  14565   -894  -5613   -778       N  
ATOM   1453  CA  GLY A 223      18.017 -27.281 -26.324  1.00162.89           C  
ANISOU 1453  CA  GLY A 223    22132  25221  14538   -835  -5468   -768       C  
ATOM   1454  C   GLY A 223      17.904 -26.015 -27.154  1.00164.23           C  
ANISOU 1454  C   GLY A 223    21706  25775  14919   -899  -4886   -860       C  
ATOM   1455  O   GLY A 223      17.977 -26.081 -28.385  1.00162.80           O  
ANISOU 1455  O   GLY A 223    21271  25681  14904   -699  -4817   -987       O  
ATOM   1456  N   CYS A 224      17.698 -24.851 -26.496  1.00159.57           N  
ANISOU 1456  N   CYS A 224    20919  25402  14307  -1186  -4473   -792       N  
ATOM   1457  CA  CYS A 224      17.588 -23.567 -27.198  1.00156.40           C  
ANISOU 1457  CA  CYS A 224    20022  25331  14071  -1268  -3939   -871       C  
ATOM   1458  C   CYS A 224      18.965 -22.892 -27.253  1.00157.60           C  
ANISOU 1458  C   CYS A 224    19792  25791  14297  -1017  -3919  -1206       C  
ATOM   1459  O   CYS A 224      19.154 -21.953 -28.030  1.00155.22           O  
ANISOU 1459  O   CYS A 224    19087  25763  14128  -1021  -3559  -1337       O  
ATOM   1460  CB  CYS A 224      16.551 -22.660 -26.543  1.00155.78           C  
ANISOU 1460  CB  CYS A 224    19954  25316  13919  -1700  -3513   -635       C  
ATOM   1461  SG  CYS A 224      17.014 -22.064 -24.896  1.00161.38           S  
ANISOU 1461  SG  CYS A 224    20762  26101  14453  -1868  -3512   -623       S  
ATOM   1462  N   ARG A 225      19.911 -23.349 -26.400  1.00154.50           N  
ANISOU 1462  N   ARG A 225    19544  25362  13796   -824  -4309  -1348       N  
ATOM   1463  CA  ARG A 225      21.283 -22.838 -26.360  1.00154.07           C  
ANISOU 1463  CA  ARG A 225    19131  25629  13779   -577  -4350  -1700       C  
ATOM   1464  C   ARG A 225      21.972 -23.135 -27.686  1.00155.32           C  
ANISOU 1464  C   ARG A 225    18966  25967  14082   -224  -4443  -1998       C  
ATOM   1465  O   ARG A 225      22.647 -22.261 -28.231  1.00153.88           O  
ANISOU 1465  O   ARG A 225    18329  26156  13983   -193  -4174  -2236       O  
ATOM   1466  CB  ARG A 225      22.062 -23.445 -25.181  1.00157.71           C  
ANISOU 1466  CB  ARG A 225    19864  25980  14079   -405  -4818  -1791       C  
ATOM   1467  N   VAL A 226      21.725 -24.348 -28.243  1.00151.11           N  
ANISOU 1467  N   VAL A 226    18683  25169  13562      4  -4805  -1972       N  
ATOM   1468  CA  VAL A 226      22.264 -24.791 -29.536  1.00150.38           C  
ANISOU 1468  CA  VAL A 226    18328  25213  13595    359  -4934  -2245       C  
ATOM   1469  C   VAL A 226      21.457 -24.122 -30.675  1.00147.58           C  
ANISOU 1469  C   VAL A 226    17725  24961  13388    139  -4441  -2125       C  
ATOM   1470  O   VAL A 226      21.946 -24.031 -31.801  1.00146.27           O  
ANISOU 1470  O   VAL A 226    17212  25031  13333    337  -4371  -2367       O  
ATOM   1471  CB  VAL A 226      22.292 -26.345 -29.694  1.00157.27           C  
ANISOU 1471  CB  VAL A 226    19605  25735  14416    704  -5537  -2268       C  
ATOM   1472  CG1 VAL A 226      23.168 -26.994 -28.622  1.00160.73           C  
ANISOU 1472  CG1 VAL A 226    20309  26066  14696    975  -6071  -2424       C  
ATOM   1473  CG2 VAL A 226      20.888 -26.954 -29.692  1.00156.10           C  
ANISOU 1473  CG2 VAL A 226    19923  25160  14227    429  -5541  -1858       C  
ATOM   1474  N   ALA A 227      20.231 -23.656 -30.368  1.00140.22           N  
ANISOU 1474  N   ALA A 227    16970  23870  12439   -261  -4113  -1773       N  
ATOM   1475  CA  ALA A 227      19.369 -22.971 -31.324  1.00136.46           C  
ANISOU 1475  CA  ALA A 227    16303  23465  12081   -471  -3660  -1646       C  
ATOM   1476  C   ALA A 227      19.764 -21.499 -31.455  1.00137.54           C  
ANISOU 1476  C   ALA A 227    16042  23956  12261   -634  -3204  -1769       C  
ATOM   1477  O   ALA A 227      19.640 -20.940 -32.546  1.00136.20           O  
ANISOU 1477  O   ALA A 227    15609  23942  12197   -661  -2913  -1832       O  
ATOM   1478  CB  ALA A 227      17.913 -23.091 -30.906  1.00135.89           C  
ANISOU 1478  CB  ALA A 227    16566  23118  11950   -806  -3526  -1265       C  
ATOM   1479  N   ALA A 228      20.267 -20.877 -30.358  1.00133.00           N  
ANISOU 1479  N   ALA A 228    15449  23496  11588   -748  -3160  -1808       N  
ATOM   1480  CA  ALA A 228      20.718 -19.478 -30.344  1.00130.96           C  
ANISOU 1480  CA  ALA A 228    14869  23553  11337   -926  -2766  -1927       C  
ATOM   1481  C   ALA A 228      21.949 -19.286 -31.251  1.00135.12           C  
ANISOU 1481  C   ALA A 228    14985  24434  11920   -710  -2777  -2306       C  
ATOM   1482  O   ALA A 228      22.238 -18.164 -31.684  1.00133.80           O  
ANISOU 1482  O   ALA A 228    14542  24531  11766   -884  -2418  -2409       O  
ATOM   1483  CB  ALA A 228      21.039 -19.051 -28.923  1.00132.52           C  
ANISOU 1483  CB  ALA A 228    15172  23775  11405  -1063  -2792  -1898       C  
ATOM   1484  N   VAL A 229      22.651 -20.404 -31.550  1.00132.96           N  
ANISOU 1484  N   VAL A 229    14692  24168  11657   -337  -3204  -2521       N  
ATOM   1485  CA  VAL A 229      23.827 -20.476 -32.421  1.00133.70           C  
ANISOU 1485  CA  VAL A 229    14385  24629  11784    -74  -3291  -2926       C  
ATOM   1486  C   VAL A 229      23.410 -20.107 -33.836  1.00135.12           C  
ANISOU 1486  C   VAL A 229    14366  24902  12072   -156  -2978  -2921       C  
ATOM   1487  O   VAL A 229      23.965 -19.172 -34.410  1.00134.25           O  
ANISOU 1487  O   VAL A 229    13913  25141  11956   -292  -2675  -3109       O  
ATOM   1488  CB  VAL A 229      24.488 -21.886 -32.370  1.00140.46           C  
ANISOU 1488  CB  VAL A 229    15339  25410  12618    395  -3879  -3143       C  
ATOM   1489  CG1 VAL A 229      25.713 -21.958 -33.276  1.00142.23           C  
ANISOU 1489  CG1 VAL A 229    15096  26085  12861    688  -3969  -3613       C  
ATOM   1490  CG2 VAL A 229      24.858 -22.277 -30.944  1.00142.49           C  
ANISOU 1490  CG2 VAL A 229    15860  25530  12751    479  -4224  -3131       C  
ATOM   1491  N   PHE A 230      22.392 -20.822 -34.370  1.00130.52           N  
ANISOU 1491  N   PHE A 230    14027  23996  11567   -109  -3047  -2692       N  
ATOM   1492  CA  PHE A 230      21.849 -20.641 -35.716  1.00128.45           C  
ANISOU 1492  CA  PHE A 230    13640  23755  11411   -156  -2800  -2653       C  
ATOM   1493  C   PHE A 230      21.279 -19.244 -35.922  1.00129.20           C  
ANISOU 1493  C   PHE A 230    13652  23926  11511   -541  -2278  -2501       C  
ATOM   1494  O   PHE A 230      21.300 -18.746 -37.045  1.00128.29           O  
ANISOU 1494  O   PHE A 230    13327  23974  11445   -599  -2031  -2586       O  
ATOM   1495  CB  PHE A 230      20.741 -21.668 -36.017  1.00129.65           C  
ANISOU 1495  CB  PHE A 230    14127  23507  11626    -76  -2985  -2394       C  
ATOM   1496  CG  PHE A 230      21.071 -23.120 -35.775  1.00134.09           C  
ANISOU 1496  CG  PHE A 230    14912  23872  12163    282  -3541  -2477       C  
ATOM   1497  CD1 PHE A 230      22.062 -23.757 -36.515  1.00139.56           C  
ANISOU 1497  CD1 PHE A 230    15379  24766  12883    668  -3823  -2835       C  
ATOM   1498  CD2 PHE A 230      20.284 -23.894 -34.931  1.00136.91           C  
ANISOU 1498  CD2 PHE A 230    15734  23827  12456    226  -3789  -2193       C  
ATOM   1499  CE1 PHE A 230      22.343 -25.111 -36.318  1.00143.36           C  
ANISOU 1499  CE1 PHE A 230    16113  25028  13329   1040  -4380  -2925       C  
ATOM   1500  CE2 PHE A 230      20.553 -25.253 -34.746  1.00142.63           C  
ANISOU 1500  CE2 PHE A 230    16747  24313  13134    545  -4337  -2255       C  
ATOM   1501  CZ  PHE A 230      21.578 -25.854 -35.444  1.00143.00           C  
ANISOU 1501  CZ  PHE A 230    16586  24534  13213    974  -4644  -2622       C  
ATOM   1502  N   MET A 231      20.747 -18.626 -34.854  1.00123.85           N  
ANISOU 1502  N   MET A 231    13168  23119  10770   -795  -2126  -2280       N  
ATOM   1503  CA  MET A 231      20.132 -17.305 -34.927  1.00121.01           C  
ANISOU 1503  CA  MET A 231    12793  22786  10398  -1128  -1676  -2133       C  
ATOM   1504  C   MET A 231      21.189 -16.220 -35.169  1.00122.01           C  
ANISOU 1504  C   MET A 231    12614  23282  10464  -1255  -1450  -2391       C  
ATOM   1505  O   MET A 231      20.957 -15.328 -35.981  1.00119.59           O  
ANISOU 1505  O   MET A 231    12221  23053  10163  -1439  -1127  -2382       O  
ATOM   1506  CB  MET A 231      19.347 -17.007 -33.647  1.00123.02           C  
ANISOU 1506  CB  MET A 231    13326  22836  10582  -1330  -1617  -1869       C  
ATOM   1507  CG  MET A 231      18.497 -15.759 -33.744  1.00124.97           C  
ANISOU 1507  CG  MET A 231    13609  23057  10815  -1616  -1199  -1708       C  
ATOM   1508  SD  MET A 231      17.593 -15.423 -32.230  1.00129.13           S  
ANISOU 1508  SD  MET A 231    14418  23406  11239  -1833  -1134  -1447       S  
ATOM   1509  CE  MET A 231      18.959 -15.146 -31.078  1.00127.92           C  
ANISOU 1509  CE  MET A 231    14178  23449  10978  -1837  -1270  -1641       C  
ATOM   1510  N   GLN A 232      22.336 -16.297 -34.475  1.00118.76           N  
ANISOU 1510  N   GLN A 232    12056  23095   9973  -1173  -1630  -2623       N  
ATOM   1511  CA  GLN A 232      23.421 -15.324 -34.650  1.00118.57           C  
ANISOU 1511  CA  GLN A 232    11723  23468   9860  -1327  -1433  -2897       C  
ATOM   1512  C   GLN A 232      24.160 -15.611 -35.966  1.00121.78           C  
ANISOU 1512  C   GLN A 232    11803  24177  10291  -1183  -1456  -3195       C  
ATOM   1513  O   GLN A 232      24.618 -14.682 -36.637  1.00120.56           O  
ANISOU 1513  O   GLN A 232    11436  24301  10069  -1413  -1168  -3341       O  
ATOM   1514  CB  GLN A 232      24.378 -15.352 -33.447  1.00121.58           C  
ANISOU 1514  CB  GLN A 232    12037  24016  10141  -1278  -1630  -3064       C  
ATOM   1515  CG  GLN A 232      23.686 -15.053 -32.103  1.00127.49           C  
ANISOU 1515  CG  GLN A 232    13105  24490  10847  -1436  -1604  -2780       C  
ATOM   1516  CD  GLN A 232      23.023 -13.686 -32.018  1.00138.51           C  
ANISOU 1516  CD  GLN A 232    14598  25827  12202  -1806  -1178  -2593       C  
ATOM   1517  OE1 GLN A 232      23.459 -12.695 -32.625  1.00129.93           O  
ANISOU 1517  OE1 GLN A 232    13335  24966  11065  -2011   -904  -2725       O  
ATOM   1518  NE2 GLN A 232      22.002 -13.587 -31.181  1.00130.36           N  
ANISOU 1518  NE2 GLN A 232    13866  24502  11162  -1908  -1135  -2300       N  
ATOM   1519  N   TYR A 233      24.221 -16.913 -36.336  1.00118.93           N  
ANISOU 1519  N   TYR A 233    11435  23743  10009   -816  -1808  -3277       N  
ATOM   1520  CA  TYR A 233      24.780 -17.475 -37.572  1.00120.07           C  
ANISOU 1520  CA  TYR A 233    11302  24128  10190   -593  -1908  -3553       C  
ATOM   1521  C   TYR A 233      24.010 -16.891 -38.776  1.00121.16           C  
ANISOU 1521  C   TYR A 233    11453  24199  10382   -803  -1557  -3404       C  
ATOM   1522  O   TYR A 233      24.599 -16.193 -39.609  1.00121.43           O  
ANISOU 1522  O   TYR A 233    11217  24570  10349   -971  -1319  -3609       O  
ATOM   1523  CB  TYR A 233      24.673 -19.027 -37.486  1.00122.85           C  
ANISOU 1523  CB  TYR A 233    11805  24256  10618   -153  -2397  -3569       C  
ATOM   1524  CG  TYR A 233      25.144 -19.850 -38.672  1.00126.97           C  
ANISOU 1524  CG  TYR A 233    12095  24959  11188    168  -2591  -3847       C  
ATOM   1525  CD1 TYR A 233      24.294 -20.109 -39.746  1.00127.44           C  
ANISOU 1525  CD1 TYR A 233    12243  24827  11351    173  -2489  -3687       C  
ATOM   1526  CD2 TYR A 233      26.349 -20.550 -38.623  1.00131.13           C  
ANISOU 1526  CD2 TYR A 233    12363  25801  11659    530  -2952  -4263       C  
ATOM   1527  CE1 TYR A 233      24.686 -20.933 -40.802  1.00129.77           C  
ANISOU 1527  CE1 TYR A 233    12350  25267  11689    489  -2693  -3937       C  
ATOM   1528  CE2 TYR A 233      26.746 -21.388 -39.666  1.00133.61           C  
ANISOU 1528  CE2 TYR A 233    12479  26277  12011    874  -3173  -4536       C  
ATOM   1529  CZ  TYR A 233      25.912 -21.574 -40.756  1.00139.20           C  
ANISOU 1529  CZ  TYR A 233    13271  26796  12821    843  -3036  -4365       C  
ATOM   1530  OH  TYR A 233      26.299 -22.389 -41.795  1.00140.79           O  
ANISOU 1530  OH  TYR A 233    13277  27161  13056   1183  -3251  -4640       O  
ATOM   1531  N   GLY A 234      22.689 -17.111 -38.781  1.00114.11           N  
ANISOU 1531  N   GLY A 234    10890  22883   9585   -830  -1519  -3047       N  
ATOM   1532  CA  GLY A 234      21.764 -16.646 -39.807  1.00110.94           C  
ANISOU 1532  CA  GLY A 234    10567  22343   9243   -987  -1231  -2866       C  
ATOM   1533  C   GLY A 234      21.328 -15.198 -39.671  1.00112.66           C  
ANISOU 1533  C   GLY A 234    10880  22536   9390  -1370   -828  -2713       C  
ATOM   1534  O   GLY A 234      20.416 -14.769 -40.386  1.00110.19           O  
ANISOU 1534  O   GLY A 234    10698  22052   9118  -1486   -611  -2534       O  
ATOM   1535  N   ILE A 235      21.952 -14.433 -38.737  1.00109.77           N  
ANISOU 1535  N   ILE A 235    10474  22323   8909  -1554   -746  -2785       N  
ATOM   1536  CA  ILE A 235      21.678 -12.996 -38.543  1.00108.16           C  
ANISOU 1536  CA  ILE A 235    10385  22103   8610  -1917   -393  -2675       C  
ATOM   1537  C   ILE A 235      22.736 -12.197 -39.300  1.00112.33           C  
ANISOU 1537  C   ILE A 235    10654  23017   9009  -2132   -198  -2951       C  
ATOM   1538  O   ILE A 235      22.484 -11.079 -39.762  1.00110.84           O  
ANISOU 1538  O   ILE A 235    10573  22806   8735  -2429    100  -2885       O  
ATOM   1539  CB  ILE A 235      21.622 -12.594 -37.046  1.00111.06           C  
ANISOU 1539  CB  ILE A 235    10906  22377   8913  -2023   -409  -2564       C  
ATOM   1540  N   VAL A 236      23.928 -12.785 -39.417  1.00110.70           N  
ANISOU 1540  N   VAL A 236    10118  23175   8767  -1984   -385  -3279       N  
ATOM   1541  CA  VAL A 236      25.042 -12.188 -40.135  1.00112.46           C  
ANISOU 1541  CA  VAL A 236    10029  23858   8841  -2194   -226  -3598       C  
ATOM   1542  C   VAL A 236      24.963 -12.690 -41.566  1.00115.89           C  
ANISOU 1542  C   VAL A 236    10326  24378   9328  -2075   -221  -3693       C  
ATOM   1543  O   VAL A 236      25.179 -11.914 -42.494  1.00116.14           O  
ANISOU 1543  O   VAL A 236    10291  24591   9246  -2363     43  -3774       O  
ATOM   1544  CB  VAL A 236      26.414 -12.494 -39.454  1.00119.48           C  
ANISOU 1544  CB  VAL A 236    10584  25176   9638  -2100   -426  -3954       C  
ATOM   1545  CG1 VAL A 236      27.543 -11.707 -40.110  1.00121.54           C  
ANISOU 1545  CG1 VAL A 236    10514  25968   9699  -2416   -209  -4289       C  
ATOM   1546  CG2 VAL A 236      26.371 -12.178 -37.965  1.00119.18           C  
ANISOU 1546  CG2 VAL A 236    10720  24990   9572  -2158   -482  -3825       C  
ATOM   1547  N   ALA A 237      24.586 -13.986 -41.743  1.00111.38           N  
ANISOU 1547  N   ALA A 237     9761  23640   8918  -1668   -517  -3662       N  
ATOM   1548  CA  ALA A 237      24.449 -14.640 -43.050  1.00110.73           C  
ANISOU 1548  CA  ALA A 237     9561  23603   8906  -1490   -564  -3747       C  
ATOM   1549  C   ALA A 237      23.507 -13.865 -43.956  1.00112.10           C  
ANISOU 1549  C   ALA A 237     9951  23556   9085  -1743   -248  -3510       C  
ATOM   1550  O   ALA A 237      23.814 -13.713 -45.133  1.00112.54           O  
ANISOU 1550  O   ALA A 237     9844  23833   9085  -1828   -120  -3664       O  
ATOM   1551  CB  ALA A 237      23.953 -16.063 -42.886  1.00110.99           C  
ANISOU 1551  CB  ALA A 237     9699  23363   9107  -1050   -938  -3662       C  
ATOM   1552  N   ASN A 238      22.420 -13.289 -43.401  1.00106.41           N  
ANISOU 1552  N   ASN A 238     9588  22438   8403  -1879   -115  -3164       N  
ATOM   1553  CA  ASN A 238      21.470 -12.498 -44.184  1.00104.66           C  
ANISOU 1553  CA  ASN A 238     9606  21983   8176  -2083    156  -2949       C  
ATOM   1554  C   ASN A 238      22.080 -11.088 -44.508  1.00110.56           C  
ANISOU 1554  C   ASN A 238    10347  22953   8708  -2518    467  -3057       C  
ATOM   1555  O   ASN A 238      21.342 -10.154 -44.828  1.00108.91           O  
ANISOU 1555  O   ASN A 238    10425  22510   8446  -2735    687  -2867       O  
ATOM   1556  CB  ASN A 238      20.107 -12.378 -43.456  1.00103.04           C  
ANISOU 1556  CB  ASN A 238     9758  21328   8066  -2049    169  -2592       C  
ATOM   1557  CG  ASN A 238      20.101 -11.681 -42.110  1.00137.39           C  
ANISOU 1557  CG  ASN A 238    14250  25609  12341  -2209    222  -2498       C  
ATOM   1558  OD1 ASN A 238      20.529 -10.529 -41.962  1.00136.96           O  
ANISOU 1558  OD1 ASN A 238    14234  25668  12136  -2509    431  -2553       O  
ATOM   1559  ND2 ASN A 238      19.413 -12.283 -41.150  1.00128.61           N  
ANISOU 1559  ND2 ASN A 238    13283  24260  11322  -2045     56  -2315       N  
ATOM   1560  N   TYR A 239      23.424 -10.971 -44.488  1.00110.49           N  
ANISOU 1560  N   TYR A 239    10020  23404   8557  -2643    466  -3382       N  
ATOM   1561  CA  TYR A 239      24.118  -9.734 -44.832  1.00112.29           C  
ANISOU 1561  CA  TYR A 239    10227  23893   8545  -3103    743  -3516       C  
ATOM   1562  C   TYR A 239      25.248 -10.011 -45.845  1.00117.64           C  
ANISOU 1562  C   TYR A 239    10498  25099   9100  -3173    761  -3890       C  
ATOM   1563  O   TYR A 239      25.684  -9.068 -46.513  1.00117.77           O  
ANISOU 1563  O   TYR A 239    10523  25325   8898  -3593   1013  -3988       O  
ATOM   1564  CB  TYR A 239      24.659  -9.010 -43.592  1.00115.11           C  
ANISOU 1564  CB  TYR A 239    10614  24340   8782  -3320    786  -3548       C  
ATOM   1565  CG  TYR A 239      23.768  -7.859 -43.180  1.00115.91           C  
ANISOU 1565  CG  TYR A 239    11164  24046   8830  -3567    982  -3248       C  
ATOM   1566  CD1 TYR A 239      22.741  -8.040 -42.256  1.00115.81           C  
ANISOU 1566  CD1 TYR A 239    11405  23632   8967  -3358    886  -2972       C  
ATOM   1567  CD2 TYR A 239      23.893  -6.607 -43.779  1.00117.77           C  
ANISOU 1567  CD2 TYR A 239    11597  24301   8848  -4004   1248  -3247       C  
ATOM   1568  CE1 TYR A 239      21.884  -6.992 -41.914  1.00115.68           C  
ANISOU 1568  CE1 TYR A 239    11782  23276   8894  -3537   1049  -2733       C  
ATOM   1569  CE2 TYR A 239      23.046  -5.554 -43.443  1.00117.42           C  
ANISOU 1569  CE2 TYR A 239    12004  23866   8746  -4180   1387  -2991       C  
ATOM   1570  CZ  TYR A 239      22.044  -5.749 -42.510  1.00123.46           C  
ANISOU 1570  CZ  TYR A 239    12971  24265   9672  -3923   1286  -2749       C  
ATOM   1571  OH  TYR A 239      21.219  -4.703 -42.190  1.00124.81           O  
ANISOU 1571  OH  TYR A 239    13561  24088   9773  -4061   1408  -2540       O  
ATOM   1572  N   CYS A 240      25.682 -11.291 -46.003  1.00115.57           N  
ANISOU 1572  N   CYS A 240     9907  25047   8956  -2772    488  -4104       N  
ATOM   1573  CA  CYS A 240      26.644 -11.657 -47.061  1.00118.13           C  
ANISOU 1573  CA  CYS A 240     9822  25889   9174  -2775    488  -4481       C  
ATOM   1574  C   CYS A 240      25.854 -11.963 -48.328  1.00119.30           C  
ANISOU 1574  C   CYS A 240    10092  25828   9410  -2685    541  -4350       C  
ATOM   1575  O   CYS A 240      26.333 -11.736 -49.442  1.00121.07           O  
ANISOU 1575  O   CYS A 240    10136  26377   9487  -2886    693  -4550       O  
ATOM   1576  CB  CYS A 240      27.546 -12.823 -46.663  1.00121.14           C  
ANISOU 1576  CB  CYS A 240     9794  26621   9614  -2362    148  -4823       C  
ATOM   1577  SG  CYS A 240      26.786 -14.458 -46.862  1.00123.25           S  
ANISOU 1577  SG  CYS A 240    10124  26538  10168  -1720   -242  -4718       S  
ATOM   1578  N   TRP A 241      24.637 -12.518 -48.141  1.00110.36           N  
ANISOU 1578  N   TRP A 241     9257  24171   8505  -2389    408  -4023       N  
ATOM   1579  CA  TRP A 241      23.702 -12.771 -49.214  1.00107.17           C  
ANISOU 1579  CA  TRP A 241     9024  23494   8203  -2295    452  -3846       C  
ATOM   1580  C   TRP A 241      23.131 -11.443 -49.661  1.00108.54           C  
ANISOU 1580  C   TRP A 241     9531  23466   8244  -2716    780  -3636       C  
ATOM   1581  O   TRP A 241      22.746 -11.312 -50.816  1.00108.38           O  
ANISOU 1581  O   TRP A 241     9594  23387   8200  -2788    897  -3594       O  
ATOM   1582  CB  TRP A 241      22.610 -13.770 -48.803  1.00103.34           C  
ANISOU 1582  CB  TRP A 241     8740  22551   7973  -1885    205  -3582       C  
ATOM   1583  CG  TRP A 241      23.123 -15.171 -48.699  1.00105.42           C  
ANISOU 1583  CG  TRP A 241     8739  22968   8347  -1450   -153  -3797       C  
ATOM   1584  CD1 TRP A 241      23.394 -15.868 -47.556  1.00108.72           C  
ANISOU 1584  CD1 TRP A 241     9126  23350   8832  -1196   -441  -3833       C  
ATOM   1585  CD2 TRP A 241      23.600 -15.975 -49.783  1.00106.91           C  
ANISOU 1585  CD2 TRP A 241     8647  23423   8549  -1229   -276  -4061       C  
ATOM   1586  NE1 TRP A 241      23.948 -17.087 -47.866  1.00109.74           N  
ANISOU 1586  NE1 TRP A 241     9015  23660   9023   -801   -763  -4091       N  
ATOM   1587  CE2 TRP A 241      24.110 -17.170 -49.227  1.00112.19           C  
ANISOU 1587  CE2 TRP A 241     9144  24179   9302   -806   -665  -4251       C  
ATOM   1588  CE3 TRP A 241      23.629 -15.809 -51.186  1.00108.45           C  
ANISOU 1588  CE3 TRP A 241     8740  23784   8683  -1338   -109  -4161       C  
ATOM   1589  CZ2 TRP A 241      24.655 -18.191 -50.023  1.00113.59           C  
ANISOU 1589  CZ2 TRP A 241     9041  24610   9507   -465   -900  -4554       C  
ATOM   1590  CZ3 TRP A 241      24.161 -16.820 -51.972  1.00111.58           C  
ANISOU 1590  CZ3 TRP A 241     8833  24453   9110  -1025   -314  -4453       C  
ATOM   1591  CH2 TRP A 241      24.666 -17.994 -51.395  1.00113.73           C  
ANISOU 1591  CH2 TRP A 241     8929  24813   9471   -580   -710  -4655       C  
ATOM   1592  N   LEU A 242      23.157 -10.430 -48.773  1.00103.31           N  
ANISOU 1592  N   LEU A 242     9068  22714   7471  -3002    916  -3530       N  
ATOM   1593  CA  LEU A 242      22.752  -9.070 -49.113  1.00102.07           C  
ANISOU 1593  CA  LEU A 242     9269  22371   7142  -3416   1196  -3367       C  
ATOM   1594  C   LEU A 242      23.948  -8.353 -49.773  1.00106.52           C  
ANISOU 1594  C   LEU A 242     9649  23414   7411  -3866   1394  -3655       C  
ATOM   1595  O   LEU A 242      23.775  -7.332 -50.430  1.00105.65           O  
ANISOU 1595  O   LEU A 242     9823  23209   7109  -4245   1615  -3576       O  
ATOM   1596  CB  LEU A 242      22.235  -8.313 -47.871  1.00101.13           C  
ANISOU 1596  CB  LEU A 242     9465  21938   7021  -3509   1234  -3140       C  
ATOM   1597  CG  LEU A 242      21.549  -6.953 -48.121  1.00105.50           C  
ANISOU 1597  CG  LEU A 242    10490  22171   7426  -3835   1458  -2930       C  
ATOM   1598  CD1 LEU A 242      20.165  -7.123 -48.771  1.00102.93           C  
ANISOU 1598  CD1 LEU A 242    10445  21415   7247  -3607   1442  -2677       C  
ATOM   1599  CD2 LEU A 242      21.396  -6.187 -46.840  1.00108.79           C  
ANISOU 1599  CD2 LEU A 242    11130  22413   7793  -3953   1487  -2808       C  
ATOM   1600  N   LEU A 243      25.159  -8.909 -49.610  1.00105.54           N  
ANISOU 1600  N   LEU A 243     9054  23816   7229  -3824   1299  -4007       N  
ATOM   1601  CA  LEU A 243      26.374  -8.403 -50.256  1.00109.44           C  
ANISOU 1601  CA  LEU A 243     9272  24881   7429  -4242   1473  -4345       C  
ATOM   1602  C   LEU A 243      26.436  -8.938 -51.682  1.00114.34           C  
ANISOU 1602  C   LEU A 243     9710  25700   8033  -4178   1494  -4489       C  
ATOM   1603  O   LEU A 243      26.710  -8.180 -52.614  1.00115.79           O  
ANISOU 1603  O   LEU A 243     9971  26058   7968  -4620   1729  -4557       O  
ATOM   1604  CB  LEU A 243      27.641  -8.793 -49.458  1.00112.43           C  
ANISOU 1604  CB  LEU A 243     9178  25796   7746  -4190   1347  -4706       C  
ATOM   1605  CG  LEU A 243      28.985  -8.278 -49.988  1.00121.56           C  
ANISOU 1605  CG  LEU A 243     9975  27644   8569  -4649   1529  -5110       C  
ATOM   1606  CD1 LEU A 243      29.115  -6.785 -49.775  1.00122.71           C  
ANISOU 1606  CD1 LEU A 243    10456  27733   8436  -5287   1812  -4996       C  
ATOM   1607  CD2 LEU A 243      30.131  -8.958 -49.287  1.00126.80           C  
ANISOU 1607  CD2 LEU A 243    10103  28851   9223  -4435   1332  -5507       C  
ATOM   1608  N   VAL A 244      26.150 -10.254 -51.840  1.00109.29           N  
ANISOU 1608  N   VAL A 244     8867  25011   7649  -3634   1235  -4526       N  
ATOM   1609  CA  VAL A 244      26.072 -10.977 -53.110  1.00108.94           C  
ANISOU 1609  CA  VAL A 244     8651  25092   7648  -3452   1194  -4644       C  
ATOM   1610  C   VAL A 244      25.060 -10.241 -54.039  1.00112.04           C  
ANISOU 1610  C   VAL A 244     9499  25074   7998  -3691   1407  -4338       C  
ATOM   1611  O   VAL A 244      25.452  -9.859 -55.135  1.00113.56           O  
ANISOU 1611  O   VAL A 244     9631  25535   7980  -4003   1586  -4483       O  
ATOM   1612  CB  VAL A 244      25.694 -12.475 -52.863  1.00110.75           C  
ANISOU 1612  CB  VAL A 244     8732  25163   8187  -2799    836  -4643       C  
ATOM   1613  CG1 VAL A 244      25.149 -13.159 -54.111  1.00109.59           C  
ANISOU 1613  CG1 VAL A 244     8581  24914   8143  -2576    788  -4618       C  
ATOM   1614  CG2 VAL A 244      26.874 -13.255 -52.283  1.00113.05           C  
ANISOU 1614  CG2 VAL A 244     8539  25950   8465  -2546    599  -5043       C  
ATOM   1615  N   GLU A 245      23.819  -9.955 -53.560  1.00106.51           N  
ANISOU 1615  N   GLU A 245     9251  23760   7457  -3583   1392  -3940       N  
ATOM   1616  CA  GLU A 245      22.758  -9.265 -54.326  1.00105.30           C  
ANISOU 1616  CA  GLU A 245     9557  23174   7277  -3733   1546  -3651       C  
ATOM   1617  C   GLU A 245      23.183  -7.879 -54.833  1.00113.01           C  
ANISOU 1617  C   GLU A 245    10774  24258   7906  -4344   1828  -3680       C  
ATOM   1618  O   GLU A 245      22.738  -7.467 -55.908  1.00112.78           O  
ANISOU 1618  O   GLU A 245    11001  24076   7774  -4511   1949  -3588       O  
ATOM   1619  CB  GLU A 245      21.481  -9.095 -53.494  1.00103.48           C  
ANISOU 1619  CB  GLU A 245     9721  22358   7239  -3526   1476  -3283       C  
ATOM   1620  CG  GLU A 245      20.733 -10.399 -53.275  1.00114.42           C  
ANISOU 1620  CG  GLU A 245    11007  23528   8941  -2989   1221  -3176       C  
ATOM   1621  CD  GLU A 245      20.211 -11.088 -54.526  1.00145.46           C  
ANISOU 1621  CD  GLU A 245    14910  27384  12974  -2780   1174  -3160       C  
ATOM   1622  OE1 GLU A 245      19.812 -10.382 -55.482  1.00144.35           O  
ANISOU 1622  OE1 GLU A 245    15017  27116  12713  -3001   1348  -3074       O  
ATOM   1623  OE2 GLU A 245      20.121 -12.337 -54.512  1.00143.37           O  
ANISOU 1623  OE2 GLU A 245    14425  27139  12909  -2383    943  -3212       O  
ATOM   1624  N   GLY A 246      24.018  -7.186 -54.067  1.00112.38           N  
ANISOU 1624  N   GLY A 246    10642  24422   7636  -4678   1918  -3803       N  
ATOM   1625  CA  GLY A 246      24.531  -5.873 -54.437  1.00115.63           C  
ANISOU 1625  CA  GLY A 246    11299  24958   7679  -5314   2170  -3846       C  
ATOM   1626  C   GLY A 246      25.666  -5.936 -55.444  1.00125.78           C  
ANISOU 1626  C   GLY A 246    12223  26867   8700  -5654   2300  -4202       C  
ATOM   1627  O   GLY A 246      25.752  -5.090 -56.343  1.00127.54           O  
ANISOU 1627  O   GLY A 246    12720  27105   8633  -6133   2499  -4188       O  
ATOM   1628  N   LEU A 247      26.540  -6.956 -55.310  1.00124.98           N  
ANISOU 1628  N   LEU A 247    11514  27295   8679  -5402   2172  -4539       N  
ATOM   1629  CA  LEU A 247      27.698  -7.138 -56.186  1.00129.13           C  
ANISOU 1629  CA  LEU A 247    11584  28524   8954  -5670   2275  -4952       C  
ATOM   1630  C   LEU A 247      27.318  -7.808 -57.511  1.00134.09           C  
ANISOU 1630  C   LEU A 247    12139  29158   9649  -5470   2254  -4980       C  
ATOM   1631  O   LEU A 247      27.818  -7.388 -58.547  1.00136.05           O  
ANISOU 1631  O   LEU A 247    12342  29748   9602  -5904   2449  -5148       O  
ATOM   1632  CB  LEU A 247      28.795  -7.974 -55.496  1.00131.14           C  
ANISOU 1632  CB  LEU A 247    11199  29369   9260  -5418   2110  -5350       C  
ATOM   1633  CG  LEU A 247      29.452  -7.370 -54.244  1.00137.23           C  
ANISOU 1633  CG  LEU A 247    11921  30301   9919  -5652   2136  -5423       C  
ATOM   1634  CD1 LEU A 247      30.393  -8.359 -53.593  1.00139.05           C  
ANISOU 1634  CD1 LEU A 247    11536  31051  10245  -5272   1907  -5809       C  
ATOM   1635  CD2 LEU A 247      30.177  -6.078 -54.557  1.00142.88           C  
ANISOU 1635  CD2 LEU A 247    12755  31336  10196  -6444   2444  -5535       C  
ATOM   1636  N   TYR A 248      26.440  -8.834 -57.489  1.00129.10           N  
ANISOU 1636  N   TYR A 248    11512  28159   9383  -4851   2022  -4817       N  
ATOM   1637  CA  TYR A 248      26.052  -9.576 -58.699  1.00128.88           C  
ANISOU 1637  CA  TYR A 248    11399  28121   9446  -4606   1971  -4846       C  
ATOM   1638  C   TYR A 248      24.876  -8.857 -59.432  1.00129.93           C  
ANISOU 1638  C   TYR A 248    12137  27673   9560  -4774   2103  -4465       C  
ATOM   1639  O   TYR A 248      24.109  -9.475 -60.176  1.00127.15           O  
ANISOU 1639  O   TYR A 248    11857  27071   9384  -4457   2015  -4347       O  
ATOM   1640  CB  TYR A 248      25.700 -11.032 -58.362  1.00128.75           C  
ANISOU 1640  CB  TYR A 248    11125  27992   9801  -3890   1642  -4866       C  
ATOM   1641  CG  TYR A 248      26.916 -11.849 -57.960  1.00134.07           C  
ANISOU 1641  CG  TYR A 248    11192  29287  10462  -3673   1472  -5312       C  
ATOM   1642  CD1 TYR A 248      27.633 -12.580 -58.903  1.00138.62           C  
ANISOU 1642  CD1 TYR A 248    11310  30396  10962  -3546   1420  -5698       C  
ATOM   1643  CD2 TYR A 248      27.378 -11.856 -56.643  1.00135.38           C  
ANISOU 1643  CD2 TYR A 248    11237  29531  10670  -3592   1357  -5376       C  
ATOM   1644  CE1 TYR A 248      28.758 -13.323 -58.543  1.00142.47           C  
ANISOU 1644  CE1 TYR A 248    11230  31479  11422  -3301   1235  -6153       C  
ATOM   1645  CE2 TYR A 248      28.500 -12.597 -56.270  1.00139.04           C  
ANISOU 1645  CE2 TYR A 248    11152  30568  11110  -3357   1171  -5811       C  
ATOM   1646  CZ  TYR A 248      29.186 -13.333 -57.225  1.00149.91           C  
ANISOU 1646  CZ  TYR A 248    12073  32473  12413  -3197   1102  -6209       C  
ATOM   1647  OH  TYR A 248      30.286 -14.077 -56.872  1.00154.52           O  
ANISOU 1647  OH  TYR A 248    12106  33640  12964  -2912    886  -6679       O  
ATOM   1648  N   LEU A 249      24.796  -7.536 -59.228  1.00127.51           N  
ANISOU 1648  N   LEU A 249    12263  27172   9012  -5277   2299  -4300       N  
ATOM   1649  CA  LEU A 249      23.995  -6.565 -59.959  1.00127.12           C  
ANISOU 1649  CA  LEU A 249    12814  26676   8809  -5581   2446  -4022       C  
ATOM   1650  C   LEU A 249      24.961  -5.663 -60.689  1.00139.06           C  
ANISOU 1650  C   LEU A 249    14361  28612   9863  -6288   2696  -4227       C  
ATOM   1651  O   LEU A 249      24.661  -5.155 -61.763  1.00139.17           O  
ANISOU 1651  O   LEU A 249    14712  28488   9679  -6577   2818  -4140       O  
ATOM   1652  CB  LEU A 249      23.023  -5.767 -59.073  1.00124.14           C  
ANISOU 1652  CB  LEU A 249    12987  25666   8515  -5550   2420  -3659       C  
ATOM   1653  CG  LEU A 249      22.130  -4.787 -59.854  1.00127.03           C  
ANISOU 1653  CG  LEU A 249    14010  25534   8722  -5786   2519  -3390       C  
ATOM   1654  CD1 LEU A 249      20.861  -5.454 -60.313  1.00123.59           C  
ANISOU 1654  CD1 LEU A 249    13706  24664   8589  -5268   2374  -3174       C  
ATOM   1655  CD2 LEU A 249      21.774  -3.612 -59.036  1.00127.67           C  
ANISOU 1655  CD2 LEU A 249    14603  25225   8682  -6017   2560  -3182       C  
ATOM   1656  N   HIS A 250      26.146  -5.473 -60.069  1.00141.48           N  
ANISOU 1656  N   HIS A 250    14316  29454   9985  -6585   2767  -4511       N  
ATOM   1657  CA  HIS A 250      27.284  -4.685 -60.540  1.00146.96           C  
ANISOU 1657  CA  HIS A 250    14926  30698  10213  -7310   3007  -4777       C  
ATOM   1658  C   HIS A 250      28.209  -5.566 -61.383  1.00155.93           C  
ANISOU 1658  C   HIS A 250    15404  32576  11266  -7280   3028  -5208       C  
ATOM   1659  O   HIS A 250      28.270  -5.413 -62.605  1.00156.58           O  
ANISOU 1659  O   HIS A 250    15558  32807  11126  -7573   3164  -5271       O  
ATOM   1660  CB  HIS A 250      28.027  -4.099 -59.317  1.00148.76           C  
ANISOU 1660  CB  HIS A 250    15074  31133  10315  -7587   3049  -4874       C  
ATOM   1661  CG  HIS A 250      29.196  -3.231 -59.648  1.00157.02           C  
ANISOU 1661  CG  HIS A 250    16048  32752  10862  -8385   3298  -5144       C  
ATOM   1662  ND1 HIS A 250      29.064  -1.861 -59.759  1.00159.46           N  
ANISOU 1662  ND1 HIS A 250    17042  32652  10894  -8943   3449  -4894       N  
ATOM   1663  CD2 HIS A 250      30.494  -3.564 -59.837  1.00159.11           C  
ANISOU 1663  CD2 HIS A 250    15913  33285  11256  -8220   3281  -5362       C  
ATOM   1664  CE1 HIS A 250      30.277  -1.406 -60.028  1.00159.25           C  
ANISOU 1664  CE1 HIS A 250    17026  32572  10911  -9006   3505  -4914       C  
ATOM   1665  NE2 HIS A 250      31.169  -2.396 -60.092  1.00159.19           N  
ANISOU 1665  NE2 HIS A 250    16378  32956  11152  -8588   3415  -5186       N  
ATOM   1666  N   ASN A 251      28.891  -6.527 -60.719  1.00155.17           N  
ANISOU 1666  N   ASN A 251    14676  32930  11353  -6881   2867  -5512       N  
ATOM   1667  CA  ASN A 251      29.830  -7.481 -61.313  1.00158.64           C  
ANISOU 1667  CA  ASN A 251    14413  34118  11745  -6725   2823  -5986       C  
ATOM   1668  C   ASN A 251      29.166  -8.302 -62.427  1.00163.39           C  
ANISOU 1668  C   ASN A 251    15031  34496  12554  -6312   2726  -5908       C  
ATOM   1669  O   ASN A 251      29.842  -8.702 -63.378  1.00163.14           O  
ANISOU 1669  O   ASN A 251    14843  34534  12608  -6163   2723  -6032       O  
ATOM   1670  CB  ASN A 251      30.392  -8.424 -60.233  1.00158.00           C  
ANISOU 1670  CB  ASN A 251    13792  34335  11907  -6198   2570  -6241       C  
ATOM   1671  CG  ASN A 251      31.217  -7.750 -59.145  1.00168.24           C  
ANISOU 1671  CG  ASN A 251    15588  34671  13663  -5942   2480  -5828       C  
ATOM   1672  OD1 ASN A 251      31.613  -6.578 -59.235  1.00163.17           O  
ANISOU 1672  OD1 ASN A 251    15101  34284  12611  -6657   2745  -5873       O  
ATOM   1673  ND2 ASN A 251      31.557  -8.511 -58.120  1.00162.16           N  
ANISOU 1673  ND2 ASN A 251    14134  34709  12771  -5804   2327  -6279       N  
ATOM   1674  N   LEU A 252      27.846  -8.514 -62.328  1.00158.41           N  
ANISOU 1674  N   LEU A 252    14814  33154  12219  -5928   2595  -5509       N  
ATOM   1675  CA  LEU A 252      27.118  -9.282 -63.320  1.00157.75           C  
ANISOU 1675  CA  LEU A 252    14760  32853  12323  -5550   2497  -5425       C  
ATOM   1676  C   LEU A 252      26.415  -8.320 -64.323  1.00163.71           C  
ANISOU 1676  C   LEU A 252    16116  33221  12867  -5990   2703  -5140       C  
ATOM   1677  O   LEU A 252      26.978  -8.064 -65.391  1.00166.66           O  
ANISOU 1677  O   LEU A 252    16395  34007  12922  -6409   2883  -5348       O  
ATOM   1678  CB  LEU A 252      26.108 -10.226 -62.624  1.00153.68           C  
ANISOU 1678  CB  LEU A 252    14320  31785  12287  -4814   2196  -5171       C  
ATOM   1679  CG  LEU A 252      25.458 -11.341 -63.468  1.00156.84           C  
ANISOU 1679  CG  LEU A 252    14627  32025  12939  -4299   2021  -5145       C  
ATOM   1680  CD1 LEU A 252      26.489 -12.390 -63.884  1.00159.74           C  
ANISOU 1680  CD1 LEU A 252    14328  33082  13285  -4052   1898  -5633       C  
ATOM   1681  CD2 LEU A 252      24.375 -12.048 -62.676  1.00155.87           C  
ANISOU 1681  CD2 LEU A 252    14694  31300  13231  -3715   1758  -4835       C  
ATOM   1682  N   LEU A 253      25.220  -7.771 -63.970  1.00157.98           N  
ANISOU 1682  N   LEU A 253    16005  31731  12290  -5903   2669  -4692       N  
ATOM   1683  CA  LEU A 253      24.407  -6.915 -64.855  1.00157.76           C  
ANISOU 1683  CA  LEU A 253    16605  31239  12098  -6202   2795  -4404       C  
ATOM   1684  C   LEU A 253      25.004  -5.506 -65.057  1.00166.52           C  
ANISOU 1684  C   LEU A 253    18077  32475  12719  -7018   3050  -4421       C  
ATOM   1685  O   LEU A 253      24.842  -4.945 -66.141  1.00167.60           O  
ANISOU 1685  O   LEU A 253    18566  32527  12587  -7395   3182  -4358       O  
ATOM   1686  CB  LEU A 253      22.959  -6.748 -64.331  1.00153.63           C  
ANISOU 1686  CB  LEU A 253    16600  29902  11870  -5820   2654  -3967       C  
ATOM   1687  CG  LEU A 253      21.903  -7.880 -64.573  1.00154.69           C  
ANISOU 1687  CG  LEU A 253    16659  29695  12420  -5131   2435  -3818       C  
ATOM   1688  CD1 LEU A 253      21.544  -8.027 -66.047  1.00155.33           C  
ANISOU 1688  CD1 LEU A 253    16863  29738  12418  -5168   2485  -3809       C  
ATOM   1689  CD2 LEU A 253      22.289  -9.208 -63.938  1.00156.09           C  
ANISOU 1689  CD2 LEU A 253    16243  30167  12896  -4621   2231  -4019       C  
ATOM   1690  N   GLY A 254      25.631  -4.938 -64.032  1.00165.75           N  
ANISOU 1690  N   GLY A 254    17942  32535  12500  -7290   3104  -4486       N  
ATOM   1691  CA  GLY A 254      26.215  -3.604 -64.124  1.00170.06           C  
ANISOU 1691  CA  GLY A 254    18861  33179  12574  -8084   3327  -4495       C  
ATOM   1692  C   GLY A 254      27.228  -3.526 -65.239  1.00174.77           C  
ANISOU 1692  C   GLY A 254    19589  33348  13469  -7746   3317  -4367       C  
ATOM   1693  O   GLY A 254      27.087  -2.702 -66.147  1.00174.78           O  
ANISOU 1693  O   GLY A 254    20113  33022  13274  -8041   3414  -4182       O  
ATOM   1694  N   LEU A 255      28.214  -4.449 -65.211  1.00174.15           N  
ANISOU 1694  N   LEU A 255    18894  33663  13612  -7409   3253  -4634       N  
ATOM   1695  CA  LEU A 255      29.276  -4.569 -66.217  1.00175.06           C  
ANISOU 1695  CA  LEU A 255    18925  33735  13855  -7269   3284  -4675       C  
ATOM   1696  C   LEU A 255      28.706  -5.099 -67.529  1.00179.20           C  
ANISOU 1696  C   LEU A 255    19601  33933  14554  -6933   3232  -4539       C  
ATOM   1697  O   LEU A 255      28.898  -4.466 -68.567  1.00179.18           O  
ANISOU 1697  O   LEU A 255    19949  33724  14407  -7157   3341  -4413       O  
ATOM   1698  CB  LEU A 255      30.417  -5.488 -65.715  1.00174.94           C  
ANISOU 1698  CB  LEU A 255    18294  34046  14129  -6857   3163  -4941       C  
ATOM   1699  CG  LEU A 255      31.243  -4.991 -64.511  1.00178.41           C  
ANISOU 1699  CG  LEU A 255    18832  34135  14820  -6691   3090  -4801       C  
ATOM   1700  CD1 LEU A 255      32.087  -6.099 -63.930  1.00178.40           C  
ANISOU 1700  CD1 LEU A 255    18243  34433  15108  -6235   2915  -5064       C  
ATOM   1701  CD2 LEU A 255      32.116  -3.789 -64.879  1.00180.65           C  
ANISOU 1701  CD2 LEU A 255    19575  33956  15108  -6871   3195  -4551       C  
ATOM   1702  N   ALA A 256      27.984  -6.254 -67.470  1.00177.79           N  
ANISOU 1702  N   ALA A 256    18980  34154  14420  -6694   3129  -4752       N  
ATOM   1703  CA  ALA A 256      27.335  -6.957 -68.593  1.00178.40           C  
ANISOU 1703  CA  ALA A 256    18995  34273  14518  -6516   3098  -4784       C  
ATOM   1704  C   ALA A 256      28.304  -7.112 -69.801  1.00182.66           C  
ANISOU 1704  C   ALA A 256    19641  34425  15335  -6196   3088  -4679       C  
ATOM   1705  O   ALA A 256      27.868  -7.088 -70.958  1.00182.68           O  
ANISOU 1705  O   ALA A 256    19838  34352  15219  -6286   3149  -4621       O  
ATOM   1706  CB  ALA A 256      26.068  -6.218 -69.022  1.00179.04           C  
ANISOU 1706  CB  ALA A 256    19651  34027  14351  -6845   3177  -4529       C  
ATOM   1707  N   THR A 257      29.613  -7.294 -69.513  1.00181.42           N  
ANISOU 1707  N   THR A 257    19161  34478  15293  -6103   3076  -4850       N  
ATOM   1708  CA  THR A 257      30.664  -7.446 -70.527  1.00182.08           C  
ANISOU 1708  CA  THR A 257    19185  34518  15479  -5989   3111  -4888       C  
ATOM   1709  C   THR A 257      31.533  -8.708 -70.259  1.00185.35           C  
ANISOU 1709  C   THR A 257    19168  34884  16374  -5325   2887  -5015       C  
ATOM   1710  O   THR A 257      32.041  -9.300 -71.218  1.00185.23           O  
ANISOU 1710  O   THR A 257    18986  34953  16442  -5150   2872  -5121       O  
ATOM   1711  CB  THR A 257      31.562  -6.185 -70.583  1.00187.83           C  
ANISOU 1711  CB  THR A 257    20498  34482  16388  -5978   3164  -4482       C  
ATOM   1712  OG1 THR A 257      32.006  -5.856 -69.263  1.00187.38           O  
ANISOU 1712  OG1 THR A 257    20350  34465  16380  -6022   3131  -4505       O  
ATOM   1713  CG2 THR A 257      30.851  -4.974 -71.193  1.00186.90           C  
ANISOU 1713  CG2 THR A 257    20959  34137  15919  -6448   3317  -4256       C  
ATOM   1714  N   LEU A 258      31.685  -9.117 -68.970  1.00183.04           N  
ANISOU 1714  N   LEU A 258    18491  34934  16121  -5231   2776  -5224       N  
ATOM   1715  CA  LEU A 258      32.513 -10.262 -68.548  1.00182.70           C  
ANISOU 1715  CA  LEU A 258    17946  35119  16353  -4773   2568  -5479       C  
ATOM   1716  C   LEU A 258      31.826 -11.621 -68.845  1.00184.63           C  
ANISOU 1716  C   LEU A 258    17972  35339  16842  -4248   2343  -5557       C  
ATOM   1717  O   LEU A 258      30.616 -11.760 -68.629  1.00183.87           O  
ANISOU 1717  O   LEU A 258    17876  35355  16632  -4272   2318  -5555       O  
ATOM   1718  CB  LEU A 258      32.858 -10.183 -67.042  1.00182.63           C  
ANISOU 1718  CB  LEU A 258    17799  35154  16438  -4701   2464  -5521       C  
ATOM   1719  CG  LEU A 258      33.954  -9.177 -66.580  1.00186.08           C  
ANISOU 1719  CG  LEU A 258    18569  35121  17011  -4809   2533  -5271       C  
ATOM   1720  CD1 LEU A 258      35.331  -9.539 -67.141  1.00186.33           C  
ANISOU 1720  CD1 LEU A 258    18419  35166  17212  -4629   2499  -5368       C  
ATOM   1721  CD2 LEU A 258      33.592  -7.722 -66.874  1.00188.14           C  
ANISOU 1721  CD2 LEU A 258    19438  34948  17098  -5215   2741  -4923       C  
ATOM   1722  N   PRO A 259      32.609 -12.640 -69.307  1.00182.21           N  
ANISOU 1722  N   PRO A 259    17224  35375  16633  -3955   2217  -5860       N  
ATOM   1723  CA  PRO A 259      32.005 -13.941 -69.663  1.00181.84           C  
ANISOU 1723  CA  PRO A 259    16885  35488  16718  -3512   2002  -6035       C  
ATOM   1724  C   PRO A 259      31.571 -14.766 -68.443  1.00183.96           C  
ANISOU 1724  C   PRO A 259    17016  35631  17249  -3053   1705  -6042       C  
ATOM   1725  O   PRO A 259      30.526 -15.419 -68.513  1.00183.23           O  
ANISOU 1725  O   PRO A 259    16796  35684  17141  -2841   1582  -6116       O  
ATOM   1726  CB  PRO A 259      33.134 -14.668 -70.414  1.00183.13           C  
ANISOU 1726  CB  PRO A 259    16926  35532  17124  -3201   1901  -6109       C  
ATOM   1727  CG  PRO A 259      34.143 -13.609 -70.748  1.00186.34           C  
ANISOU 1727  CG  PRO A 259    17726  35503  17573  -3477   2101  -5829       C  
ATOM   1728  CD  PRO A 259      34.048 -12.622 -69.635  1.00183.37           C  
ANISOU 1728  CD  PRO A 259    17354  35375  16943  -3877   2223  -5858       C  
ATOM   1729  N   GLU A 260      32.368 -14.756 -67.346  1.00181.63           N  
ANISOU 1729  N   GLU A 260    16467  35585  16958  -3025   1619  -6217       N  
ATOM   1730  CA  GLU A 260      32.073 -15.508 -66.118  1.00181.18           C  
ANISOU 1730  CA  GLU A 260    16166  35646  17029  -2652   1338  -6345       C  
ATOM   1731  C   GLU A 260      30.748 -15.040 -65.500  1.00182.68           C  
ANISOU 1731  C   GLU A 260    16581  35707  17122  -2796   1391  -6140       C  
ATOM   1732  O   GLU A 260      30.545 -13.835 -65.328  1.00182.40           O  
ANISOU 1732  O   GLU A 260    16808  35632  16863  -3295   1649  -5979       O  
ATOM   1733  CB  GLU A 260      33.217 -15.359 -65.102  1.00182.33           C  
ANISOU 1733  CB  GLU A 260    16293  35645  17338  -2587   1250  -6335       C  
ATOM   1734  N   ARG A 261      29.831 -16.001 -65.217  1.00179.34           N  
ANISOU 1734  N   ARG A 261    15788  35726  16628  -2462   1169  -6392       N  
ATOM   1735  CA  ARG A 261      28.499 -15.745 -64.646  1.00178.53           C  
ANISOU 1735  CA  ARG A 261    15723  35768  16342  -2575   1196  -6316       C  
ATOM   1736  C   ARG A 261      27.993 -16.946 -63.817  1.00179.39           C  
ANISOU 1736  C   ARG A 261    15633  35861  16666  -1954    808  -6397       C  
ATOM   1737  O   ARG A 261      27.528 -16.757 -62.695  1.00178.39           O  
ANISOU 1737  O   ARG A 261    15453  35886  16442  -1977    758  -6390       O  
ATOM   1738  CB  ARG A 261      27.485 -15.426 -65.757  1.00178.59           C  
ANISOU 1738  CB  ARG A 261    15914  35770  16170  -2819   1382  -6192       C  
ATOM   1739  N   SER A 262      28.080 -18.171 -64.383  1.00176.69           N  
ANISOU 1739  N   SER A 262    14940  35801  16392  -1466    545  -6700       N  
ATOM   1740  CA  SER A 262      27.596 -19.422 -63.784  1.00176.24           C  
ANISOU 1740  CA  SER A 262    14688  35789  16485   -824    127  -6839       C  
ATOM   1741  C   SER A 262      28.664 -20.111 -62.898  1.00178.05           C  
ANISOU 1741  C   SER A 262    14910  35729  17013   -435   -187  -6888       C  
ATOM   1742  O   SER A 262      28.302 -20.833 -61.966  1.00177.58           O  
ANISOU 1742  O   SER A 262    14770  35684  17017    -18   -514  -6962       O  
ATOM   1743  CB  SER A 262      27.164 -20.388 -64.887  1.00178.50           C  
ANISOU 1743  CB  SER A 262    15056  35791  16977   -436    -42  -6794       C  
ATOM   1744  OG  SER A 262      26.661 -21.609 -64.371  1.00183.51           O  
ANISOU 1744  OG  SER A 262    15921  35813  17992    180   -468  -6599       O  
ATOM   1745  N   PHE A 263      29.963 -19.896 -63.196  1.00175.28           N  
ANISOU 1745  N   PHE A 263    14364  35622  16614   -586    -96  -7104       N  
ATOM   1746  CA  PHE A 263      31.079 -20.513 -62.473  1.00175.09           C  
ANISOU 1746  CA  PHE A 263    14225  35520  16781   -258   -378  -7246       C  
ATOM   1747  C   PHE A 263      31.438 -19.734 -61.179  1.00176.50           C  
ANISOU 1747  C   PHE A 263    14527  35587  16950   -506   -302  -7110       C  
ATOM   1748  O   PHE A 263      32.466 -20.032 -60.559  1.00176.12           O  
ANISOU 1748  O   PHE A 263    14388  35509  17021   -333   -481  -7221       O  
ATOM   1749  CB  PHE A 263      32.312 -20.597 -63.384  1.00176.46           C  
ANISOU 1749  CB  PHE A 263    14444  35488  17115   -314   -304  -7233       C  
ATOM   1750  N   PHE A 264      30.576 -18.780 -60.747  1.00173.84           N  
ANISOU 1750  N   PHE A 264    14136  35636  16279   -917    -49  -7107       N  
ATOM   1751  CA  PHE A 264      30.795 -18.008 -59.518  1.00173.51           C  
ANISOU 1751  CA  PHE A 264    14128  35659  16137  -1182     37  -7055       C  
ATOM   1752  C   PHE A 264      30.393 -18.792 -58.246  1.00174.28           C  
ANISOU 1752  C   PHE A 264    14197  35668  16352   -707   -341  -7075       C  
ATOM   1753  O   PHE A 264      30.394 -18.198 -57.166  1.00173.46           O  
ANISOU 1753  O   PHE A 264    14089  35692  16125   -907   -282  -7054       O  
ATOM   1754  CB  PHE A 264      30.029 -16.671 -59.526  1.00174.51           C  
ANISOU 1754  CB  PHE A 264    14528  35741  16037  -1808    436  -6780       C  
ATOM   1755  CG  PHE A 264      30.582 -15.551 -60.370  1.00175.44           C  
ANISOU 1755  CG  PHE A 264    14892  35700  16066  -2366    814  -6622       C  
ATOM   1756  CD1 PHE A 264      31.715 -14.854 -59.967  1.00177.53           C  
ANISOU 1756  CD1 PHE A 264    15342  35675  16436  -2577    916  -6501       C  
ATOM   1757  CD2 PHE A 264      29.858 -15.049 -61.442  1.00176.57           C  
ANISOU 1757  CD2 PHE A 264    15280  35712  16096  -2668   1057  -6436       C  
ATOM   1758  CE1 PHE A 264      32.189 -13.769 -60.707  1.00178.25           C  
ANISOU 1758  CE1 PHE A 264    15701  35602  16423  -3067   1240  -6340       C  
ATOM   1759  CE2 PHE A 264      30.317 -13.946 -62.165  1.00178.48           C  
ANISOU 1759  CE2 PHE A 264    15887  35649  16280  -3150   1372  -6212       C  
ATOM   1760  CZ  PHE A 264      31.485 -13.321 -61.801  1.00177.52           C  
ANISOU 1760  CZ  PHE A 264    15764  35553  16130  -3381   1470  -6255       C  
ATOM   1761  N   SER A 265      30.090 -20.117 -58.359  1.00171.06           N  
ANISOU 1761  N   SER A 265    13507  35523  15964    -84   -742  -7379       N  
ATOM   1762  CA  SER A 265      29.749 -20.987 -57.217  1.00169.50           C  
ANISOU 1762  CA  SER A 265    13419  35056  15929    428  -1166  -7334       C  
ATOM   1763  C   SER A 265      30.920 -21.055 -56.217  1.00172.20           C  
ANISOU 1763  C   SER A 265    13694  35384  16351    528  -1341  -7460       C  
ATOM   1764  O   SER A 265      30.737 -21.445 -55.061  1.00172.17           O  
ANISOU 1764  O   SER A 265    13725  35330  16361    811  -1624  -7481       O  
ATOM   1765  CB  SER A 265      29.379 -22.387 -57.696  1.00172.90           C  
ANISOU 1765  CB  SER A 265    13896  35248  16551   1057  -1578  -7396       C  
ATOM   1766  OG  SER A 265      29.068 -23.235 -56.603  1.00178.65           O  
ANISOU 1766  OG  SER A 265    15018  35303  17559   1474  -1991  -7128       O  
ATOM   1767  N   LEU A 266      32.114 -20.637 -56.684  1.00169.15           N  
ANISOU 1767  N   LEU A 266    13068  35307  15894    289  -1167  -7680       N  
ATOM   1768  CA  LEU A 266      33.369 -20.540 -55.943  1.00168.92           C  
ANISOU 1768  CA  LEU A 266    12990  35240  15951    291  -1258  -7763       C  
ATOM   1769  C   LEU A 266      33.317 -19.309 -54.997  1.00170.87           C  
ANISOU 1769  C   LEU A 266    13415  35404  16105   -209   -973  -7531       C  
ATOM   1770  O   LEU A 266      34.141 -19.194 -54.090  1.00171.52           O  
ANISOU 1770  O   LEU A 266    13523  35380  16268   -191  -1075  -7536       O  
ATOM   1771  CB  LEU A 266      34.534 -20.443 -56.971  1.00168.71           C  
ANISOU 1771  CB  LEU A 266    12891  35199  16012    141  -1111  -7825       C  
ATOM   1772  CG  LEU A 266      35.990 -20.613 -56.490  1.00171.96           C  
ANISOU 1772  CG  LEU A 266    13451  35183  16704    223  -1254  -7713       C  
ATOM   1773  CD1 LEU A 266      36.252 -22.035 -55.992  1.00172.43           C  
ANISOU 1773  CD1 LEU A 266    13532  35002  16981    867  -1790  -7802       C  
ATOM   1774  CD2 LEU A 266      36.962 -20.325 -57.623  1.00173.30           C  
ANISOU 1774  CD2 LEU A 266    13658  35217  16969    -13  -1024  -7637       C  
ATOM   1775  N   TYR A 267      32.330 -18.403 -55.212  1.00166.56           N  
ANISOU 1775  N   TYR A 267    12685  35449  15152   -668   -623  -7615       N  
ATOM   1776  CA  TYR A 267      32.086 -17.204 -54.399  1.00165.66           C  
ANISOU 1776  CA  TYR A 267    12625  35519  14799  -1203   -329  -7507       C  
ATOM   1777  C   TYR A 267      30.563 -17.039 -54.127  1.00162.38           C  
ANISOU 1777  C   TYR A 267    12809  34307  14581  -1224   -282  -6906       C  
ATOM   1778  O   TYR A 267      30.156 -16.081 -53.463  1.00161.10           O  
ANISOU 1778  O   TYR A 267    12970  33846  14393  -1604    -65  -6581       O  
ATOM   1779  CB  TYR A 267      32.664 -15.940 -55.073  1.00166.46           C  
ANISOU 1779  CB  TYR A 267    12906  35524  14819  -1863    117  -7344       C  
ATOM   1780  CG  TYR A 267      34.166 -15.973 -55.267  1.00168.71           C  
ANISOU 1780  CG  TYR A 267    13258  35486  15358  -1798     73  -7332       C  
ATOM   1781  CD1 TYR A 267      35.030 -15.539 -54.264  1.00170.30           C  
ANISOU 1781  CD1 TYR A 267    13561  35491  15656  -1878     45  -7258       C  
ATOM   1782  CD2 TYR A 267      34.726 -16.400 -56.468  1.00169.69           C  
ANISOU 1782  CD2 TYR A 267    13380  35461  15632  -1675     70  -7353       C  
ATOM   1783  CE1 TYR A 267      36.416 -15.564 -54.438  1.00171.45           C  
ANISOU 1783  CE1 TYR A 267    13708  35450  15986  -1832      6  -7279       C  
ATOM   1784  CE2 TYR A 267      36.110 -16.426 -56.658  1.00170.79           C  
ANISOU 1784  CE2 TYR A 267    13523  35420  15950  -1641     41  -7369       C  
ATOM   1785  CZ  TYR A 267      36.951 -16.007 -55.639  1.00175.48           C  
ANISOU 1785  CZ  TYR A 267    14405  35494  16777  -1673     -8  -7112       C  
ATOM   1786  OH  TYR A 267      38.313 -16.031 -55.826  1.00176.20           O  
ANISOU 1786  OH  TYR A 267    14472  35457  17019  -1645    -37  -7133       O  
ATOM   1787  N   LEU A 268      29.738 -17.991 -54.615  1.00154.12           N  
ANISOU 1787  N   LEU A 268    11952  32843  13762   -796   -503  -6735       N  
ATOM   1788  CA  LEU A 268      28.288 -17.999 -54.396  1.00148.31           C  
ANISOU 1788  CA  LEU A 268    11788  31305  13258   -754   -499  -6163       C  
ATOM   1789  C   LEU A 268      27.994 -18.502 -52.974  1.00148.40           C  
ANISOU 1789  C   LEU A 268    12020  30923  13443   -442   -804  -5980       C  
ATOM   1790  O   LEU A 268      27.942 -17.700 -52.035  1.00146.23           O  
ANISOU 1790  O   LEU A 268    11909  30528  13122   -728   -661  -5802       O  
ATOM   1791  CB  LEU A 268      27.574 -18.874 -55.464  1.00146.96           C  
ANISOU 1791  CB  LEU A 268    11709  30887  13242   -433   -630  -6083       C  
ATOM   1792  CG  LEU A 268      26.519 -18.216 -56.375  1.00147.90           C  
ANISOU 1792  CG  LEU A 268    12172  30644  13379   -758   -315  -5713       C  
ATOM   1793  CD1 LEU A 268      27.158 -17.278 -57.388  1.00149.78           C  
ANISOU 1793  CD1 LEU A 268    12192  31383  13335  -1257     54  -5930       C  
ATOM   1794  CD2 LEU A 268      25.734 -19.267 -57.139  1.00147.09           C  
ANISOU 1794  CD2 LEU A 268    12192  30219  13477   -351   -529  -5605       C  
ATOM   1795  N   GLY A 269      27.898 -19.827 -52.823  1.00144.57           N  
ANISOU 1795  N   GLY A 269    11531  30275  13125    132  -1237  -6060       N  
ATOM   1796  CA  GLY A 269      27.682 -20.486 -51.541  1.00143.91           C  
ANISOU 1796  CA  GLY A 269    11671  29831  13179    461  -1589  -5923       C  
ATOM   1797  C   GLY A 269      28.947 -20.527 -50.708  1.00152.06           C  
ANISOU 1797  C   GLY A 269    12355  31343  14078    574  -1764  -6328       C  
ATOM   1798  O   GLY A 269      29.072 -21.354 -49.802  1.00152.36           O  
ANISOU 1798  O   GLY A 269    12485  31206  14198    976  -2167  -6368       O  
ATOM   1799  N   ILE A 270      29.908 -19.638 -51.039  1.00151.84           N  
ANISOU 1799  N   ILE A 270    11932  31940  13821    204  -1469  -6647       N  
ATOM   1800  CA  ILE A 270      31.205 -19.472 -50.380  1.00155.60           C  
ANISOU 1800  CA  ILE A 270    11994  33004  14122    212  -1554  -7087       C  
ATOM   1801  C   ILE A 270      31.236 -18.125 -49.662  1.00158.14           C  
ANISOU 1801  C   ILE A 270    12437  33328  14321   -367  -1189  -6886       C  
ATOM   1802  O   ILE A 270      31.933 -17.983 -48.654  1.00158.43           O  
ANISOU 1802  O   ILE A 270    12333  33579  14283   -350  -1298  -7057       O  
ATOM   1803  CB  ILE A 270      32.348 -19.597 -51.401  1.00163.01           C  
ANISOU 1803  CB  ILE A 270    12327  34750  14858    239  -1518  -7678       C  
ATOM   1804  N   GLY A 271      30.454 -17.163 -50.178  1.00152.93           N  
ANISOU 1804  N   GLY A 271    12067  32400  13639   -851   -787  -6525       N  
ATOM   1805  CA  GLY A 271      30.236 -15.862 -49.552  1.00151.63           C  
ANISOU 1805  CA  GLY A 271    12148  32090  13375  -1390   -453  -6254       C  
ATOM   1806  C   GLY A 271      29.550 -16.106 -48.222  1.00153.29           C  
ANISOU 1806  C   GLY A 271    12734  31741  13769  -1181   -657  -5911       C  
ATOM   1807  O   GLY A 271      29.770 -15.375 -47.256  1.00153.31           O  
ANISOU 1807  O   GLY A 271    12810  31746  13692  -1434   -554  -5843       O  
ATOM   1808  N   TRP A 272      28.763 -17.217 -48.176  1.00147.27           N  
ANISOU 1808  N   TRP A 272    12196  30523  13237   -711   -971  -5722       N  
ATOM   1809  CA  TRP A 272      28.093 -17.875 -47.048  1.00144.78           C  
ANISOU 1809  CA  TRP A 272    12225  29684  13100   -404  -1271  -5440       C  
ATOM   1810  C   TRP A 272      29.087 -18.159 -45.898  1.00151.05           C  
ANISOU 1810  C   TRP A 272    12818  30747  13826   -207  -1545  -5721       C  
ATOM   1811  O   TRP A 272      28.670 -18.274 -44.742  1.00149.87           O  
ANISOU 1811  O   TRP A 272    12966  30226  13752   -137  -1690  -5475       O  
ATOM   1812  CB  TRP A 272      27.491 -19.200 -47.584  1.00142.82           C  
ANISOU 1812  CB  TRP A 272    12102  29129  13034     77  -1602  -5380       C  
ATOM   1813  CG  TRP A 272      26.814 -20.105 -46.594  1.00142.61           C  
ANISOU 1813  CG  TRP A 272    12446  28576  13165    409  -1967  -5121       C  
ATOM   1814  CD1 TRP A 272      27.429 -20.897 -45.667  1.00147.92           C  
ANISOU 1814  CD1 TRP A 272    13083  29288  13834    772  -2382  -5312       C  
ATOM   1815  CD2 TRP A 272      25.448 -20.551 -46.650  1.00139.54           C  
ANISOU 1815  CD2 TRP A 272    12493  27582  12943    473  -2017  -4688       C  
ATOM   1816  NE1 TRP A 272      26.499 -21.678 -45.021  1.00146.05           N  
ANISOU 1816  NE1 TRP A 272    13293  28468  13732    978  -2654  -4975       N  
ATOM   1817  CE2 TRP A 272      25.276 -21.505 -45.622  1.00144.19           C  
ANISOU 1817  CE2 TRP A 272    13331  27852  13602    793  -2431  -4598       C  
ATOM   1818  CE3 TRP A 272      24.338 -20.201 -47.438  1.00137.55           C  
ANISOU 1818  CE3 TRP A 272    12459  27033  12770    268  -1750  -4370       C  
ATOM   1819  CZ2 TRP A 272      24.034 -22.096 -45.347  1.00141.07           C  
ANISOU 1819  CZ2 TRP A 272    13383  26879  13336    860  -2560  -4196       C  
ATOM   1820  CZ3 TRP A 272      23.111 -20.779 -47.161  1.00136.75           C  
ANISOU 1820  CZ3 TRP A 272    12762  26382  12813    371  -1879  -3992       C  
ATOM   1821  CH2 TRP A 272      22.968 -21.720 -46.132  1.00138.04           C  
ANISOU 1821  CH2 TRP A 272    13156  26264  13030    642  -2271  -3908       C  
ATOM   1822  N   GLY A 273      30.380 -18.279 -46.247  1.00150.52           N  
ANISOU 1822  N   GLY A 273    12241  31347  13605   -120  -1615  -6248       N  
ATOM   1823  CA  GLY A 273      31.483 -18.593 -45.340  1.00153.02           C  
ANISOU 1823  CA  GLY A 273    12272  32039  13830    114  -1898  -6624       C  
ATOM   1824  C   GLY A 273      31.959 -17.493 -44.406  1.00156.20           C  
ANISOU 1824  C   GLY A 273    12630  32632  14089   -305  -1667  -6620       C  
ATOM   1825  O   GLY A 273      32.381 -17.800 -43.287  1.00157.20           O  
ANISOU 1825  O   GLY A 273    12756  32759  14214    -86  -1939  -6712       O  
ATOM   1826  N   ALA A 274      31.935 -16.207 -44.860  1.00151.20           N  
ANISOU 1826  N   ALA A 274    11976  32161  13312   -910  -1183  -6529       N  
ATOM   1827  CA  ALA A 274      32.366 -15.041 -44.055  1.00151.28           C  
ANISOU 1827  CA  ALA A 274    11978  32341  13159  -1377   -929  -6512       C  
ATOM   1828  C   ALA A 274      31.488 -14.878 -42.769  1.00152.87           C  
ANISOU 1828  C   ALA A 274    12675  31908  13499  -1366   -992  -6054       C  
ATOM   1829  O   ALA A 274      32.070 -14.742 -41.686  1.00153.67           O  
ANISOU 1829  O   ALA A 274    12704  32144  13538  -1352  -1108  -6168       O  
ATOM   1830  CB  ALA A 274      32.322 -13.764 -44.886  1.00151.45           C  
ANISOU 1830  CB  ALA A 274    12013  32531  12999  -2020   -435  -6441       C  
ATOM   1831  N   PRO A 275      30.123 -14.997 -42.820  1.00145.96           N  
ANISOU 1831  N   PRO A 275    12276  30375  12807  -1328   -957  -5571       N  
ATOM   1832  CA  PRO A 275      29.326 -14.886 -41.581  1.00143.72           C  
ANISOU 1832  CA  PRO A 275    12415  29566  12627  -1320  -1021  -5182       C  
ATOM   1833  C   PRO A 275      29.348 -16.160 -40.714  1.00148.52           C  
ANISOU 1833  C   PRO A 275    13100  29975  13357   -794  -1510  -5209       C  
ATOM   1834  O   PRO A 275      28.510 -16.308 -39.812  1.00146.19           O  
ANISOU 1834  O   PRO A 275    13197  29190  13160   -748  -1601  -4856       O  
ATOM   1835  CB  PRO A 275      27.908 -14.646 -42.107  1.00141.66           C  
ANISOU 1835  CB  PRO A 275    12562  28772  12491  -1447   -822  -4732       C  
ATOM   1836  CG  PRO A 275      28.057 -14.357 -43.548  1.00145.96           C  
ANISOU 1836  CG  PRO A 275    12920  29571  12967  -1617   -597  -4872       C  
ATOM   1837  CD  PRO A 275      29.225 -15.134 -43.979  1.00144.82           C  
ANISOU 1837  CD  PRO A 275    12300  29966  12760  -1338   -826  -5360       C  
ATOM   1838  N   MET A 276      30.288 -17.082 -41.004  1.00147.61           N  
ANISOU 1838  N   MET A 276    12632  30239  13216   -398  -1836  -5638       N  
ATOM   1839  CA  MET A 276      30.499 -18.333 -40.284  1.00148.56           C  
ANISOU 1839  CA  MET A 276    12820  30216  13411    141  -2362  -5746       C  
ATOM   1840  C   MET A 276      31.919 -18.318 -39.711  1.00156.02           C  
ANISOU 1840  C   MET A 276    13349  31732  14199    266  -2541  -6235       C  
ATOM   1841  O   MET A 276      32.101 -18.568 -38.520  1.00156.59           O  
ANISOU 1841  O   MET A 276    13567  31666  14266    425  -2798  -6212       O  
ATOM   1842  CB  MET A 276      30.247 -19.529 -41.226  1.00151.35           C  
ANISOU 1842  CB  MET A 276    13172  30458  13876    575  -2647  -5831       C  
ATOM   1843  CG  MET A 276      30.262 -20.903 -40.557  1.00156.59           C  
ANISOU 1843  CG  MET A 276    14047  30835  14614   1138  -3233  -5875       C  
ATOM   1844  SD  MET A 276      31.860 -21.502 -39.948  1.00166.24           S  
ANISOU 1844  SD  MET A 276    14867  32599  15698   1594  -3695  -6495       S  
ATOM   1845  CE  MET A 276      31.413 -23.164 -39.477  1.00164.07           C  
ANISOU 1845  CE  MET A 276    15058  31751  15532   2225  -4373  -6395       C  
ATOM   1846  N   LEU A 277      32.916 -17.971 -40.550  1.00154.68           N  
ANISOU 1846  N   LEU A 277    12658  32230  13882    159  -2388  -6681       N  
ATOM   1847  CA  LEU A 277      34.324 -17.907 -40.156  1.00158.51           C  
ANISOU 1847  CA  LEU A 277    12658  33379  14190    250  -2525  -7216       C  
ATOM   1848  C   LEU A 277      34.565 -16.792 -39.118  1.00161.50           C  
ANISOU 1848  C   LEU A 277    13084  33821  14455   -192  -2280  -7110       C  
ATOM   1849  O   LEU A 277      35.077 -17.082 -38.041  1.00162.47           O  
ANISOU 1849  O   LEU A 277    13189  33992  14550     36  -2570  -7246       O  
ATOM   1850  CB  LEU A 277      35.220 -17.684 -41.385  1.00161.37           C  
ANISOU 1850  CB  LEU A 277    12446  34475  14392    131  -2342  -7697       C  
ATOM   1851  N   PHE A 278      34.166 -15.540 -39.419  1.00155.96           N  
ANISOU 1851  N   PHE A 278    12490  33082  13686   -804  -1776  -6857       N  
ATOM   1852  CA  PHE A 278      34.385 -14.404 -38.521  1.00155.71           C  
ANISOU 1852  CA  PHE A 278    12525  33108  13530  -1256  -1524  -6759       C  
ATOM   1853  C   PHE A 278      33.189 -14.212 -37.540  1.00156.65           C  
ANISOU 1853  C   PHE A 278    13242  32482  13797  -1312  -1510  -6192       C  
ATOM   1854  O   PHE A 278      32.947 -13.092 -37.075  1.00154.34           O  
ANISOU 1854  O   PHE A 278    13133  32079  13429  -1767  -1197  -5971       O  
ATOM   1855  CB  PHE A 278      34.617 -13.126 -39.341  1.00157.62           C  
ANISOU 1855  CB  PHE A 278    12617  33689  13581  -1900  -1018  -6803       C  
ATOM   1856  N   VAL A 279      32.478 -15.314 -37.193  1.00153.29           N  
ANISOU 1856  N   VAL A 279    13116  31569  13557   -855  -1865  -5980       N  
ATOM   1857  CA  VAL A 279      31.349 -15.282 -36.250  1.00150.79           C  
ANISOU 1857  CA  VAL A 279    13335  30600  13360   -887  -1884  -5480       C  
ATOM   1858  C   VAL A 279      31.397 -16.515 -35.324  1.00155.86           C  
ANISOU 1858  C   VAL A 279    14140  31003  14078   -375  -2411  -5499       C  
ATOM   1859  O   VAL A 279      31.479 -16.340 -34.106  1.00155.65           O  
ANISOU 1859  O   VAL A 279    14274  30855  14012   -408  -2506  -5410       O  
ATOM   1860  CB  VAL A 279      29.944 -15.190 -36.945  1.00151.57           C  
ANISOU 1860  CB  VAL A 279    13800  30193  13598  -1015  -1670  -5037       C  
ATOM   1861  CG1 VAL A 279      28.805 -15.255 -35.921  1.00148.63           C  
ANISOU 1861  CG1 VAL A 279    13929  29220  13324  -1026  -1718  -4574       C  
ATOM   1862  CG2 VAL A 279      29.809 -13.938 -37.807  1.00150.50           C  
ANISOU 1862  CG2 VAL A 279    13605  30208  13372  -1518  -1180  -4981       C  
ATOM   1863  N   VAL A 280      31.288 -17.750 -35.908  1.00152.87           N  
ANISOU 1863  N   VAL A 280    13771  30516  13796     83  -2759  -5594       N  
ATOM   1864  CA  VAL A 280      31.177 -19.038 -35.203  1.00153.69           C  
ANISOU 1864  CA  VAL A 280    14143  30290  13964    579  -3300  -5571       C  
ATOM   1865  C   VAL A 280      32.192 -19.130 -34.040  1.00160.45           C  
ANISOU 1865  C   VAL A 280    14874  31389  14701    754  -3590  -5852       C  
ATOM   1866  O   VAL A 280      31.719 -19.260 -32.917  1.00159.56           O  
ANISOU 1866  O   VAL A 280    15152  30873  14599    748  -3731  -5569       O  
ATOM   1867  CB  VAL A 280      31.331 -20.267 -36.121  1.00159.24           C  
ANISOU 1867  CB  VAL A 280    14754  31020  14732   1068  -3661  -5801       C  
ATOM   1868  N   PRO A 281      33.540 -19.026 -34.217  1.00160.02           N  
ANISOU 1868  N   PRO A 281    14292  31991  14518    883  -3672  -6397       N  
ATOM   1869  CA  PRO A 281      34.427 -19.141 -33.041  1.00162.47           C  
ANISOU 1869  CA  PRO A 281    14516  32497  14718   1072  -3975  -6650       C  
ATOM   1870  C   PRO A 281      34.250 -17.975 -32.061  1.00163.66           C  
ANISOU 1870  C   PRO A 281    14801  32574  14807    579  -3637  -6392       C  
ATOM   1871  O   PRO A 281      34.267 -18.195 -30.849  1.00163.36           O  
ANISOU 1871  O   PRO A 281    15019  32306  14744    695  -3887  -6295       O  
ATOM   1872  CB  PRO A 281      35.834 -19.135 -33.650  1.00168.42           C  
ANISOU 1872  CB  PRO A 281    14602  34053  15335   1243  -4043  -7308       C  
ATOM   1873  CG  PRO A 281      35.681 -18.475 -34.969  1.00171.55           C  
ANISOU 1873  CG  PRO A 281    14736  34718  15729    878  -3578  -7322       C  
ATOM   1874  CD  PRO A 281      34.322 -18.862 -35.461  1.00163.42           C  
ANISOU 1874  CD  PRO A 281    14175  33037  14880    877  -3522  -6831       C  
ATOM   1875  N   TRP A 282      34.001 -16.754 -32.592  1.00157.59           N  
ANISOU 1875  N   TRP A 282    13922  31948  14009     28  -3084  -6256       N  
ATOM   1876  CA  TRP A 282      33.832 -15.514 -31.829  1.00155.53           C  
ANISOU 1876  CA  TRP A 282    13780  31639  13674   -475  -2721  -6031       C  
ATOM   1877  C   TRP A 282      32.542 -15.526 -30.971  1.00155.06           C  
ANISOU 1877  C   TRP A 282    14318  30877  13720   -560  -2710  -5470       C  
ATOM   1878  O   TRP A 282      32.280 -14.559 -30.252  1.00152.93           O  
ANISOU 1878  O   TRP A 282    14203  30504  13397   -933  -2443  -5257       O  
ATOM   1879  CB  TRP A 282      33.803 -14.321 -32.789  1.00153.05           C  
ANISOU 1879  CB  TRP A 282    13274  31587  13289  -1004  -2185  -6022       C  
ATOM   1880  N   ALA A 283      31.770 -16.626 -31.016  1.00150.16           N  
ANISOU 1880  N   ALA A 283    14027  29801  13227   -223  -3010  -5256       N  
ATOM   1881  CA  ALA A 283      30.554 -16.771 -30.226  1.00147.01           C  
ANISOU 1881  CA  ALA A 283    14169  28789  12900   -302  -3027  -4760       C  
ATOM   1882  C   ALA A 283      30.458 -18.170 -29.593  1.00152.26           C  
ANISOU 1882  C   ALA A 283    15134  29126  13591    162  -3590  -4733       C  
ATOM   1883  O   ALA A 283      29.944 -18.259 -28.486  1.00151.31           O  
ANISOU 1883  O   ALA A 283    15392  28653  13446     99  -3692  -4456       O  
ATOM   1884  CB  ALA A 283      29.327 -16.504 -31.082  1.00144.18           C  
ANISOU 1884  CB  ALA A 283    14011  28117  12653   -526  -2706  -4405       C  
ATOM   1885  N   VAL A 284      30.939 -19.255 -30.273  1.00150.82           N  
ANISOU 1885  N   VAL A 284    14817  29049  13439    618  -3969  -5021       N  
ATOM   1886  CA  VAL A 284      30.848 -20.623 -29.714  1.00152.28           C  
ANISOU 1886  CA  VAL A 284    15363  28872  13624   1073  -4556  -4998       C  
ATOM   1887  C   VAL A 284      31.948 -20.808 -28.662  1.00158.56           C  
ANISOU 1887  C   VAL A 284    16064  29893  14289   1321  -4916  -5316       C  
ATOM   1888  O   VAL A 284      31.706 -21.456 -27.641  1.00159.30           O  
ANISOU 1888  O   VAL A 284    16592  29599  14335   1478  -5281  -5149       O  
ATOM   1889  CB  VAL A 284      30.884 -21.800 -30.748  1.00157.91           C  
ANISOU 1889  CB  VAL A 284    16059  29532  14408   1518  -4899  -5173       C  
ATOM   1890  CG1 VAL A 284      29.718 -21.726 -31.732  1.00154.14           C  
ANISOU 1890  CG1 VAL A 284    15726  28779  14061   1295  -4586  -4834       C  
ATOM   1891  CG2 VAL A 284      32.223 -21.909 -31.481  1.00161.23           C  
ANISOU 1891  CG2 VAL A 284    15893  30590  14777   1831  -5030  -5778       C  
ATOM   1892  N   VAL A 285      33.148 -20.256 -28.913  1.00156.45           N  
ANISOU 1892  N   VAL A 285    15239  30260  13944   1343  -4825  -5781       N  
ATOM   1893  CA  VAL A 285      34.259 -20.369 -27.975  1.00159.57           C  
ANISOU 1893  CA  VAL A 285    15474  30947  14207   1584  -5153  -6137       C  
ATOM   1894  C   VAL A 285      34.087 -19.337 -26.850  1.00160.27           C  
ANISOU 1894  C   VAL A 285    15695  30968  14232   1143  -4860  -5891       C  
ATOM   1895  O   VAL A 285      34.358 -19.654 -25.695  1.00160.96           O  
ANISOU 1895  O   VAL A 285    16004  30915  14239   1306  -5187  -5898       O  
ATOM   1896  CB  VAL A 285      35.619 -20.211 -28.680  1.00167.00           C  
ANISOU 1896  CB  VAL A 285    15729  32657  15068   1771  -5174  -6771       C  
ATOM   1897  N   LYS A 286      33.596 -18.122 -27.183  1.00153.13           N  
ANISOU 1897  N   LYS A 286    14699  30129  13356    597  -4268  -5663       N  
ATOM   1898  CA  LYS A 286      33.355 -17.054 -26.210  1.00150.85           C  
ANISOU 1898  CA  LYS A 286    14545  29764  13006    160  -3956  -5422       C  
ATOM   1899  C   LYS A 286      32.139 -17.377 -25.316  1.00151.54           C  
ANISOU 1899  C   LYS A 286    15251  29191  13135     87  -4035  -4904       C  
ATOM   1900  O   LYS A 286      32.018 -16.791 -24.240  1.00149.74           O  
ANISOU 1900  O   LYS A 286    15194  28864  12836   -146  -3935  -4738       O  
ATOM   1901  CB  LYS A 286      33.142 -15.712 -26.923  1.00151.03           C  
ANISOU 1901  CB  LYS A 286    14347  30006  13031   -368  -3345  -5340       C  
ATOM   1902  N   CYS A 287      31.251 -18.310 -25.754  1.00147.46           N  
ANISOU 1902  N   CYS A 287    15063  28250  12715    268  -4213  -4663       N  
ATOM   1903  CA  CYS A 287      30.067 -18.725 -24.987  1.00145.63           C  
ANISOU 1903  CA  CYS A 287    15410  27429  12494    173  -4299  -4191       C  
ATOM   1904  C   CYS A 287      30.488 -19.670 -23.858  1.00153.34           C  
ANISOU 1904  C   CYS A 287    16689  28212  13363    504  -4862  -4257       C  
ATOM   1905  O   CYS A 287      30.191 -19.381 -22.706  1.00152.08           O  
ANISOU 1905  O   CYS A 287    16808  27857  13119    305  -4845  -4036       O  
ATOM   1906  CB  CYS A 287      29.014 -19.374 -25.884  1.00143.72           C  
ANISOU 1906  CB  CYS A 287    15396  26842  12368    212  -4288  -3935       C  
ATOM   1907  N   LEU A 288      31.213 -20.775 -24.179  1.00154.03           N  
ANISOU 1907  N   LEU A 288    16726  28363  13435   1020  -5376  -4582       N  
ATOM   1908  CA  LEU A 288      31.687 -21.773 -23.202  1.00157.57           C  
ANISOU 1908  CA  LEU A 288    17501  28607  13764   1409  -5995  -4690       C  
ATOM   1909  C   LEU A 288      32.606 -21.134 -22.124  1.00163.54           C  
ANISOU 1909  C   LEU A 288    18078  29664  14397   1369  -6021  -4904       C  
ATOM   1910  O   LEU A 288      32.829 -21.728 -21.068  1.00165.07           O  
ANISOU 1910  O   LEU A 288    18619  29630  14470   1574  -6458  -4898       O  
ATOM   1911  CB  LEU A 288      32.438 -22.897 -23.927  1.00161.10           C  
ANISOU 1911  CB  LEU A 288    17822  29170  14217   2006  -6510  -5097       C  
ATOM   1912  N   PHE A 289      33.101 -19.912 -22.404  1.00159.96           N  
ANISOU 1912  N   PHE A 289    17116  29703  13959   1075  -5552  -5078       N  
ATOM   1913  CA  PHE A 289      33.956 -19.084 -21.554  1.00161.45           C  
ANISOU 1913  CA  PHE A 289    17052  30252  14038    942  -5460  -5287       C  
ATOM   1914  C   PHE A 289      33.106 -18.339 -20.513  1.00163.46           C  
ANISOU 1914  C   PHE A 289    17667  30183  14256    483  -5163  -4835       C  
ATOM   1915  O   PHE A 289      33.393 -18.430 -19.324  1.00164.50           O  
ANISOU 1915  O   PHE A 289    18006  30223  14273    534  -5402  -4828       O  
ATOM   1916  CB  PHE A 289      34.739 -18.098 -22.448  1.00163.31           C  
ANISOU 1916  CB  PHE A 289    16628  31134  14288    753  -5055  -5639       C  
ATOM   1917  CG  PHE A 289      35.650 -17.102 -21.775  1.00166.27           C  
ANISOU 1917  CG  PHE A 289    16671  31961  14545    535  -4880  -5883       C  
ATOM   1918  CD1 PHE A 289      36.977 -17.417 -21.513  1.00174.27           C  
ANISOU 1918  CD1 PHE A 289    17323  33443  15449    893  -5238  -6412       C  
ATOM   1919  CD2 PHE A 289      35.216 -15.808 -21.509  1.00165.65           C  
ANISOU 1919  CD2 PHE A 289    16601  31883  14454    -27  -4348  -5625       C  
ATOM   1920  CE1 PHE A 289      37.836 -16.478 -20.930  1.00176.91           C  
ANISOU 1920  CE1 PHE A 289    17322  34234  15663    662  -5062  -6656       C  
ATOM   1921  CE2 PHE A 289      36.074 -14.868 -20.929  1.00170.30           C  
ANISOU 1921  CE2 PHE A 289    16892  32891  14921   -255  -4184  -5856       C  
ATOM   1922  CZ  PHE A 289      37.379 -15.210 -20.643  1.00172.94           C  
ANISOU 1922  CZ  PHE A 289    16868  33693  15148     73  -4532  -6365       C  
ATOM   1923  N   GLU A 290      32.051 -17.625 -20.960  1.00157.62           N  
ANISOU 1923  N   GLU A 290    17009  29276  13605     58  -4664  -4474       N  
ATOM   1924  CA  GLU A 290      31.162 -16.864 -20.081  1.00155.71           C  
ANISOU 1924  CA  GLU A 290    17074  28761  13326   -370  -4351  -4068       C  
ATOM   1925  C   GLU A 290      29.678 -17.083 -20.483  1.00158.57           C  
ANISOU 1925  C   GLU A 290    17795  28678  13776   -558  -4164  -3620       C  
ATOM   1926  O   GLU A 290      28.994 -16.146 -20.915  1.00154.82           O  
ANISOU 1926  O   GLU A 290    17248  28215  13361   -913  -3681  -3430       O  
ATOM   1927  CB  GLU A 290      31.528 -15.372 -20.122  1.00155.89           C  
ANISOU 1927  CB  GLU A 290    16740  29162  13328   -761  -3853  -4162       C  
ATOM   1928  N   ASN A 291      29.190 -18.336 -20.323  1.00157.98           N  
ANISOU 1928  N   ASN A 291    18126  28210  13689   -316  -4572  -3464       N  
ATOM   1929  CA  ASN A 291      27.808 -18.730 -20.628  1.00156.08           C  
ANISOU 1929  CA  ASN A 291    18247  27555  13501   -478  -4467  -3061       C  
ATOM   1930  C   ASN A 291      26.891 -18.440 -19.448  1.00160.97           C  
ANISOU 1930  C   ASN A 291    19266  27883  14013   -820  -4342  -2684       C  
ATOM   1931  O   ASN A 291      27.285 -18.631 -18.291  1.00162.69           O  
ANISOU 1931  O   ASN A 291    19689  28035  14093   -778  -4602  -2698       O  
ATOM   1932  CB  ASN A 291      27.728 -20.217 -20.998  1.00157.73           C  
ANISOU 1932  CB  ASN A 291    18736  27479  13714   -101  -4976  -3076       C  
ATOM   1933  N   VAL A 292      25.663 -17.987 -19.743  1.00156.00           N  
ANISOU 1933  N   VAL A 292    18741  27099  13435  -1147  -3954  -2365       N  
ATOM   1934  CA  VAL A 292      24.673 -17.669 -18.723  1.00155.50           C  
ANISOU 1934  CA  VAL A 292    19010  26813  13261  -1492  -3788  -2023       C  
ATOM   1935  C   VAL A 292      23.314 -18.237 -19.150  1.00159.53           C  
ANISOU 1935  C   VAL A 292    19806  27015  13793  -1631  -3724  -1702       C  
ATOM   1936  O   VAL A 292      23.085 -19.441 -19.011  1.00160.55           O  
ANISOU 1936  O   VAL A 292    20289  26858  13855  -1497  -4117  -1603       O  
ATOM   1937  CB  VAL A 292      24.608 -16.143 -18.464  1.00157.52           C  
ANISOU 1937  CB  VAL A 292    19021  27307  13520  -1808  -3291  -2016       C  
ATOM   1938  N   GLN A 293      22.430 -17.373 -19.683  1.00155.03           N  
ANISOU 1938  N   GLN A 293    19096  26504  13302  -1895  -3250  -1556       N  
ATOM   1939  CA  GLN A 293      21.085 -17.732 -20.121  1.00154.37           C  
ANISOU 1939  CA  GLN A 293    19212  26201  13239  -2058  -3121  -1276       C  
ATOM   1940  C   GLN A 293      21.099 -18.267 -21.558  1.00160.22           C  
ANISOU 1940  C   GLN A 293    19801  26932  14142  -1835  -3175  -1368       C  
ATOM   1941  O   GLN A 293      22.166 -18.361 -22.173  1.00160.93           O  
ANISOU 1941  O   GLN A 293    19627  27203  14316  -1556  -3313  -1658       O  
ATOM   1942  CB  GLN A 293      20.157 -16.509 -20.015  1.00153.22           C  
ANISOU 1942  CB  GLN A 293    18972  26150  13095  -2395  -2610  -1122       C  
ATOM   1943  N   CYS A 294      19.906 -18.634 -22.080  1.00157.19           N  
ANISOU 1943  N   CYS A 294    19573  26364  13787  -1963  -3068  -1136       N  
ATOM   1944  CA  CYS A 294      19.709 -19.142 -23.437  1.00157.07           C  
ANISOU 1944  CA  CYS A 294    19450  26309  13919  -1791  -3092  -1178       C  
ATOM   1945  C   CYS A 294      20.102 -18.050 -24.447  1.00161.01           C  
ANISOU 1945  C   CYS A 294    19503  27103  14569  -1766  -2724  -1369       C  
ATOM   1946  O   CYS A 294      21.105 -18.203 -25.148  1.00161.11           O  
ANISOU 1946  O   CYS A 294    19269  27283  14663  -1508  -2853  -1640       O  
ATOM   1947  CB  CYS A 294      18.265 -19.602 -23.626  1.00156.34           C  
ANISOU 1947  CB  CYS A 294    19614  25990  13800  -2003  -3005   -878       C  
ATOM   1948  SG  CYS A 294      17.905 -20.273 -25.270  1.00159.40           S  
ANISOU 1948  SG  CYS A 294    19905  26299  14360  -1810  -3040   -902       S  
ATOM   1949  N   TRP A 295      19.352 -16.927 -24.464  1.00157.32           N  
ANISOU 1949  N   TRP A 295    18949  26713  14111  -2040  -2283  -1249       N  
ATOM   1950  CA  TRP A 295      19.651 -15.772 -25.307  1.00156.37           C  
ANISOU 1950  CA  TRP A 295    18495  26831  14089  -2080  -1929  -1398       C  
ATOM   1951  C   TRP A 295      20.747 -14.953 -24.623  1.00163.62           C  
ANISOU 1951  C   TRP A 295    19248  27980  14940  -2117  -1884  -1596       C  
ATOM   1952  O   TRP A 295      20.455 -14.137 -23.740  1.00162.90           O  
ANISOU 1952  O   TRP A 295    19234  27904  14758  -2337  -1692  -1502       O  
ATOM   1953  CB  TRP A 295      18.381 -14.943 -25.576  1.00152.69           C  
ANISOU 1953  CB  TRP A 295    18062  26316  13637  -2320  -1534  -1201       C  
ATOM   1954  N   THR A 296      22.019 -15.243 -24.977  1.00163.42           N  
ANISOU 1954  N   THR A 296    18997  28151  14943  -1890  -2090  -1887       N  
ATOM   1955  CA  THR A 296      23.216 -14.636 -24.391  1.00165.65           C  
ANISOU 1955  CA  THR A 296    19085  28702  15154  -1895  -2105  -2129       C  
ATOM   1956  C   THR A 296      23.146 -13.101 -24.458  1.00170.06           C  
ANISOU 1956  C   THR A 296    19502  29423  15689  -2195  -1659  -2134       C  
ATOM   1957  O   THR A 296      22.852 -12.530 -25.512  1.00168.00           O  
ANISOU 1957  O   THR A 296    19117  29218  15499  -2282  -1389  -2140       O  
ATOM   1958  CB  THR A 296      24.468 -15.147 -25.097  1.00176.07           C  
ANISOU 1958  CB  THR A 296    20106  30277  16516  -1605  -2343  -2481       C  
ATOM   1959  N   SER A 297      23.382 -12.452 -23.300  1.00168.83           N  
ANISOU 1959  N   SER A 297    19412  29315  15420  -2354  -1604  -2121       N  
ATOM   1960  CA  SER A 297      23.335 -10.998 -23.120  1.00168.29           C  
ANISOU 1960  CA  SER A 297    19288  29360  15295  -2641  -1232  -2119       C  
ATOM   1961  C   SER A 297      24.658 -10.326 -23.545  1.00174.86           C  
ANISOU 1961  C   SER A 297    19794  30548  16097  -2685  -1157  -2441       C  
ATOM   1962  O   SER A 297      25.632 -11.012 -23.869  1.00176.03           O  
ANISOU 1962  O   SER A 297    19724  30895  16265  -2472  -1401  -2688       O  
ATOM   1963  CB  SER A 297      23.031 -10.661 -21.662  1.00172.06           C  
ANISOU 1963  CB  SER A 297    19985  29739  15651  -2786  -1230  -1977       C  
ATOM   1964  N   ASN A 298      24.676  -8.974 -23.528  1.00172.02           N  
ANISOU 1964  N   ASN A 298    19413  30278  15669  -2973   -826  -2451       N  
ATOM   1965  CA  ASN A 298      25.803  -8.124 -23.914  1.00173.74           C  
ANISOU 1965  CA  ASN A 298    19366  30832  15813  -3134   -686  -2726       C  
ATOM   1966  C   ASN A 298      27.073  -8.453 -23.108  1.00181.59           C  
ANISOU 1966  C   ASN A 298    20170  32097  16729  -3037   -940  -2984       C  
ATOM   1967  O   ASN A 298      27.117  -8.240 -21.893  1.00181.60           O  
ANISOU 1967  O   ASN A 298    20308  32044  16650  -3095   -999  -2924       O  
ATOM   1968  CB  ASN A 298      25.437  -6.651 -23.718  1.00173.88           C  
ANISOU 1968  CB  ASN A 298    19530  30799  15736  -3474   -340  -2633       C  
ATOM   1969  N   ASP A 299      28.099  -8.982 -23.802  1.00181.21           N  
ANISOU 1969  N   ASP A 299    19793  32362  16695  -2874  -1099  -3292       N  
ATOM   1970  CA  ASP A 299      29.401  -9.330 -23.222  1.00184.51           C  
ANISOU 1970  CA  ASP A 299    19959  33113  17034  -2733  -1362  -3614       C  
ATOM   1971  C   ASP A 299      30.474  -8.300 -23.637  1.00191.23           C  
ANISOU 1971  C   ASP A 299    20478  34418  17763  -3018  -1134  -3921       C  
ATOM   1972  O   ASP A 299      31.609  -8.367 -23.150  1.00193.69           O  
ANISOU 1972  O   ASP A 299    20533  35079  17980  -2965  -1297  -4225       O  
ATOM   1973  CB  ASP A 299      29.818 -10.746 -23.655  1.00187.87           C  
ANISOU 1973  CB  ASP A 299    20239  33606  17539  -2300  -1756  -3793       C  
ATOM   1974  N   ASN A 300      30.088  -7.337 -24.529  1.00186.84           N  
ANISOU 1974  N   ASN A 300    19951  33851  17188  -3338   -764  -3840       N  
ATOM   1975  CA  ASN A 300      30.892  -6.243 -25.112  1.00188.00           C  
ANISOU 1975  CA  ASN A 300    19877  34365  17189  -3715   -489  -4068       C  
ATOM   1976  C   ASN A 300      32.028  -6.833 -25.962  1.00193.64           C  
ANISOU 1976  C   ASN A 300    20124  35575  17876  -3581   -622  -4476       C  
ATOM   1977  O   ASN A 300      31.953  -6.784 -27.190  1.00192.44           O  
ANISOU 1977  O   ASN A 300    19861  35516  17740  -3657   -475  -4527       O  
ATOM   1978  CB  ASN A 300      31.449  -5.282 -24.030  1.00190.90           C  
ANISOU 1978  CB  ASN A 300    20278  34860  17395  -3999   -399  -4131       C  
ATOM   1979  CG  ASN A 300      32.247  -4.098 -24.553  1.00209.84           C  
ANISOU 1979  CG  ASN A 300    23209  36170  20350  -3867   -241  -3852       C  
ATOM   1980  OD1 ASN A 300      32.170  -3.712 -25.729  1.00206.18           O  
ANISOU 1980  OD1 ASN A 300    22583  36024  19733  -4147    -15  -3958       O  
ATOM   1981  ND2 ASN A 300      32.978  -3.448 -23.661  1.00204.34           N  
ANISOU 1981  ND2 ASN A 300    22301  35996  19342  -4200   -196  -4093       N  
ATOM   1982  N   MET A 301      33.061  -7.397 -25.302  1.00192.75           N  
ANISOU 1982  N   MET A 301    19735  35788  17712  -3366   -910  -4779       N  
ATOM   1983  CA  MET A 301      34.222  -8.027 -25.932  1.00194.22           C  
ANISOU 1983  CA  MET A 301    19572  36246  17978  -3107  -1111  -5132       C  
ATOM   1984  C   MET A 301      33.784  -9.288 -26.712  1.00196.42           C  
ANISOU 1984  C   MET A 301    19844  36364  18424  -2678  -1349  -5106       C  
ATOM   1985  O   MET A 301      34.326  -9.568 -27.782  1.00196.12           O  
ANISOU 1985  O   MET A 301    19662  36324  18532  -2552  -1363  -5238       O  
ATOM   1986  CB  MET A 301      35.273  -8.374 -24.851  1.00196.90           C  
ANISOU 1986  CB  MET A 301    20015  36290  18507  -2790  -1449  -5190       C  
ATOM   1987  CG  MET A 301      36.613  -8.886 -25.396  1.00199.87           C  
ANISOU 1987  CG  MET A 301    20401  36286  19255  -2442  -1686  -5281       C  
ATOM   1988  SD  MET A 301      37.570  -7.700 -26.394  1.00201.80           S  
ANISOU 1988  SD  MET A 301    20740  36200  19735  -2730  -1348  -5189       S  
ATOM   1989  CE  MET A 301      37.906  -6.418 -25.173  1.00199.59           C  
ANISOU 1989  CE  MET A 301    20497  36096  19240  -3125  -1165  -5213       C  
ATOM   1990  N   GLY A 302      32.790 -10.001 -26.182  1.00190.76           N  
ANISOU 1990  N   GLY A 302    19366  35387  17726  -2466  -1528  -4874       N  
ATOM   1991  CA  GLY A 302      32.270 -11.222 -26.780  1.00189.29           C  
ANISOU 1991  CA  GLY A 302    19257  34973  17691  -2067  -1782  -4804       C  
ATOM   1992  C   GLY A 302      31.509 -11.038 -28.079  1.00189.79           C  
ANISOU 1992  C   GLY A 302    19370  34903  17839  -2198  -1516  -4642       C  
ATOM   1993  O   GLY A 302      31.909 -11.589 -29.110  1.00190.42           O  
ANISOU 1993  O   GLY A 302    19179  35225  17949  -2019  -1597  -4878       O  
ATOM   1994  N   PHE A 303      30.395 -10.275 -28.040  1.00182.34           N  
ANISOU 1994  N   PHE A 303    18773  33580  16928  -2488  -1212  -4256       N  
ATOM   1995  CA  PHE A 303      29.516 -10.099 -29.198  1.00179.13           C  
ANISOU 1995  CA  PHE A 303    18478  32977  16605  -2590   -978  -4063       C  
ATOM   1996  C   PHE A 303      30.020  -9.057 -30.220  1.00180.92           C  
ANISOU 1996  C   PHE A 303    18488  33538  16715  -2967   -631  -4238       C  
ATOM   1997  O   PHE A 303      29.583  -9.138 -31.372  1.00179.82           O  
ANISOU 1997  O   PHE A 303    18347  33343  16634  -2978   -510  -4187       O  
ATOM   1998  CB  PHE A 303      28.096  -9.695 -28.789  1.00178.08           C  
ANISOU 1998  CB  PHE A 303    18793  32331  16537  -2721   -811  -3617       C  
ATOM   1999  CG  PHE A 303      27.193 -10.848 -28.410  1.00178.72           C  
ANISOU 1999  CG  PHE A 303    19129  32026  16751  -2399  -1082  -3376       C  
ATOM   2000  CD1 PHE A 303      26.632 -11.663 -29.390  1.00180.76           C  
ANISOU 2000  CD1 PHE A 303    19407  32139  17134  -2192  -1164  -3308       C  
ATOM   2001  CD2 PHE A 303      26.802 -11.043 -27.091  1.00180.97           C  
ANISOU 2001  CD2 PHE A 303    19672  32071  17016  -2360  -1225  -3190       C  
ATOM   2002  CE1 PHE A 303      25.764 -12.701 -29.050  1.00180.78           C  
ANISOU 2002  CE1 PHE A 303    19679  31778  17231  -1955  -1406  -3074       C  
ATOM   2003  CE2 PHE A 303      25.925 -12.079 -26.753  1.00182.97           C  
ANISOU 2003  CE2 PHE A 303    20198  31969  17352  -2139  -1459  -2954       C  
ATOM   2004  CZ  PHE A 303      25.408 -12.896 -27.737  1.00180.14           C  
ANISOU 2004  CZ  PHE A 303    19859  31477  17110  -1949  -1547  -2895       C  
ATOM   2005  N   TRP A 304      30.906  -8.100 -29.851  1.00176.94           N  
ANISOU 2005  N   TRP A 304    17826  33373  16032  -3297   -473  -4438       N  
ATOM   2006  CA  TRP A 304      31.361  -7.136 -30.866  1.00176.63           C  
ANISOU 2006  CA  TRP A 304    17631  33639  15844  -3711   -149  -4592       C  
ATOM   2007  C   TRP A 304      32.217  -7.863 -31.912  1.00178.81           C  
ANISOU 2007  C   TRP A 304    17454  34382  16104  -3543   -262  -4969       C  
ATOM   2008  O   TRP A 304      32.154  -7.545 -33.100  1.00177.87           O  
ANISOU 2008  O   TRP A 304    17271  34372  15940  -3743    -51  -5007       O  
ATOM   2009  CB  TRP A 304      32.126  -5.963 -30.257  1.00177.54           C  
ANISOU 2009  CB  TRP A 304    17697  34018  15742  -4146     39  -4726       C  
ATOM   2010  CG  TRP A 304      32.043  -4.731 -31.105  1.00178.83           C  
ANISOU 2010  CG  TRP A 304    17986  34216  15746  -4662    415  -4681       C  
ATOM   2011  CD1 TRP A 304      32.699  -4.491 -32.277  1.00183.72           C  
ANISOU 2011  CD1 TRP A 304    18340  35237  16227  -4913    570  -4934       C  
ATOM   2012  CD2 TRP A 304      31.268  -3.555 -30.830  1.00176.99           C  
ANISOU 2012  CD2 TRP A 304    18209  33594  15445  -4998    662  -4374       C  
ATOM   2013  NE1 TRP A 304      32.345  -3.257 -32.774  1.00182.89           N  
ANISOU 2013  NE1 TRP A 304    18546  34974  15971  -5401    893  -4773       N  
ATOM   2014  CE2 TRP A 304      31.484  -2.651 -31.894  1.00182.18           C  
ANISOU 2014  CE2 TRP A 304    18905  34394  15922  -5443    942  -4440       C  
ATOM   2015  CE3 TRP A 304      30.411  -3.173 -29.780  1.00176.16           C  
ANISOU 2015  CE3 TRP A 304    18495  33041  15397  -4963    662  -4065       C  
ATOM   2016  CZ2 TRP A 304      30.877  -1.388 -31.941  1.00180.60           C  
ANISOU 2016  CZ2 TRP A 304    19160  33863  15597  -5826   1189  -4204       C  
ATOM   2017  CZ3 TRP A 304      29.811  -1.922 -29.827  1.00176.65           C  
ANISOU 2017  CZ3 TRP A 304    18957  32815  15346  -5318    918  -3855       C  
ATOM   2018  CH2 TRP A 304      30.045  -1.044 -30.896  1.00178.48           C  
ANISOU 2018  CH2 TRP A 304    19258  33155  15400  -5731   1163  -3923       C  
ATOM   2019  N   TRP A 305      32.974  -8.874 -31.459  1.00175.16           N  
ANISOU 2019  N   TRP A 305    16701  34179  15674  -3146   -620  -5251       N  
ATOM   2020  CA  TRP A 305      33.769  -9.763 -32.298  1.00176.53           C  
ANISOU 2020  CA  TRP A 305    16436  34790  15846  -2857   -818  -5645       C  
ATOM   2021  C   TRP A 305      32.886 -10.812 -32.964  1.00177.05           C  
ANISOU 2021  C   TRP A 305    16665  34488  16118  -2467   -993  -5457       C  
ATOM   2022  O   TRP A 305      33.192 -11.253 -34.073  1.00177.89           O  
ANISOU 2022  O   TRP A 305    16502  34862  16228  -2353  -1011  -5681       O  
ATOM   2023  CB  TRP A 305      34.863 -10.453 -31.465  1.00178.37           C  
ANISOU 2023  CB  TRP A 305    16345  35397  16029  -2520  -1189  -6026       C  
ATOM   2024  CG  TRP A 305      36.048  -9.596 -31.128  1.00180.82           C  
ANISOU 2024  CG  TRP A 305    16508  35925  16270  -2803  -1065  -6217       C  
ATOM   2025  CD1 TRP A 305      36.069  -8.522 -30.288  1.00182.54           C  
ANISOU 2025  CD1 TRP A 305    16991  35912  16454  -3162   -865  -6009       C  
ATOM   2026  CD2 TRP A 305      37.418  -9.891 -31.432  1.00181.10           C  
ANISOU 2026  CD2 TRP A 305    16424  35860  16523  -2575  -1238  -6402       C  
ATOM   2027  NE1 TRP A 305      37.356  -8.054 -30.150  1.00182.45           N  
ANISOU 2027  NE1 TRP A 305    16943  35827  16553  -3226   -864  -6120       N  
ATOM   2028  CE2 TRP A 305      38.208  -8.889 -30.825  1.00183.77           C  
ANISOU 2028  CE2 TRP A 305    17002  35841  16980  -2832  -1104  -6244       C  
ATOM   2029  CE3 TRP A 305      38.056 -10.887 -32.192  1.00182.32           C  
ANISOU 2029  CE3 TRP A 305    16495  35850  16927  -2142  -1505  -6515       C  
ATOM   2030  CZ2 TRP A 305      39.602  -8.849 -30.958  1.00183.72           C  
ANISOU 2030  CZ2 TRP A 305    16898  35771  17136  -2753  -1197  -6383       C  
ATOM   2031  CZ3 TRP A 305      39.436 -10.847 -32.323  1.00183.64           C  
ANISOU 2031  CZ3 TRP A 305    16662  35794  17321  -2061  -1597  -6570       C  
ATOM   2032  CH2 TRP A 305      40.195  -9.838 -31.711  1.00184.08           C  
ANISOU 2032  CH2 TRP A 305    16803  35763  17376  -2369  -1441  -6516       C  
ATOM   2033  N   ILE A 306      31.798 -11.224 -32.284  1.00169.71           N  
ANISOU 2033  N   ILE A 306    16169  32969  15344  -2278  -1121  -5059       N  
ATOM   2034  CA  ILE A 306      30.894 -12.258 -32.778  1.00167.08           C  
ANISOU 2034  CA  ILE A 306    16036  32251  15195  -1930  -1308  -4854       C  
ATOM   2035  C   ILE A 306      30.155 -11.770 -34.036  1.00166.07           C  
ANISOU 2035  C   ILE A 306    15996  31999  15106  -2166   -980  -4679       C  
ATOM   2036  O   ILE A 306      30.568 -12.138 -35.135  1.00166.45           O  
ANISOU 2036  O   ILE A 306    15766  32330  15150  -2072   -991  -4917       O  
ATOM   2037  CB  ILE A 306      29.887 -12.716 -31.696  1.00168.31           C  
ANISOU 2037  CB  ILE A 306    16645  31844  15463  -1768  -1488  -4467       C  
ATOM   2038  N   LEU A 307      29.091 -10.944 -33.892  1.00158.20           N  
ANISOU 2038  N   LEU A 307    15374  30601  14132  -2454   -702  -4292       N  
ATOM   2039  CA  LEU A 307      28.294 -10.556 -35.048  1.00155.52           C  
ANISOU 2039  CA  LEU A 307    15169  30088  13835  -2620   -441  -4112       C  
ATOM   2040  C   LEU A 307      28.616  -9.128 -35.545  1.00157.54           C  
ANISOU 2040  C   LEU A 307    15403  30549  13907  -3136    -50  -4167       C  
ATOM   2041  O   LEU A 307      28.612  -8.937 -36.759  1.00158.11           O  
ANISOU 2041  O   LEU A 307    15393  30738  13944  -3265    113  -4232       O  
ATOM   2042  CB  LEU A 307      26.760 -10.656 -34.782  1.00152.48           C  
ANISOU 2042  CB  LEU A 307    15230  29112  13593  -2555   -411  -3661       C  
ATOM   2043  CG  LEU A 307      26.033  -9.685 -33.821  1.00155.89           C  
ANISOU 2043  CG  LEU A 307    16004  29245  13981  -2809   -224  -3373       C  
ATOM   2044  CD1 LEU A 307      24.524  -9.751 -34.020  1.00153.11           C  
ANISOU 2044  CD1 LEU A 307    15997  28427  13749  -2759   -146  -3009       C  
ATOM   2045  CD2 LEU A 307      26.394  -9.927 -32.373  1.00159.48           C  
ANISOU 2045  CD2 LEU A 307    16488  29699  14408  -2715   -429  -3388       C  
ATOM   2046  N   ARG A 308      28.874  -8.141 -34.655  1.00151.50           N  
ANISOU 2046  N   ARG A 308    14744  29810  13008  -3442     90  -4137       N  
ATOM   2047  CA  ARG A 308      29.100  -6.745 -35.077  1.00150.81           C  
ANISOU 2047  CA  ARG A 308    14736  29842  12721  -3965    441  -4155       C  
ATOM   2048  C   ARG A 308      30.269  -6.593 -36.081  1.00155.78           C  
ANISOU 2048  C   ARG A 308    14961  31052  13177  -4188    541  -4545       C  
ATOM   2049  O   ARG A 308      30.281  -5.605 -36.818  1.00155.64           O  
ANISOU 2049  O   ARG A 308    15058  31082  12995  -4619    828  -4528       O  
ATOM   2050  CB  ARG A 308      29.371  -5.813 -33.883  1.00151.33           C  
ANISOU 2050  CB  ARG A 308    14946  29896  12656  -4235    524  -4117       C  
ATOM   2051  CG  ARG A 308      28.126  -5.281 -33.151  1.00155.16           C  
ANISOU 2051  CG  ARG A 308    15915  29830  13211  -4255    602  -3717       C  
ATOM   2052  CD  ARG A 308      27.339  -6.301 -32.342  1.00154.47           C  
ANISOU 2052  CD  ARG A 308    15946  29420  13325  -3830    346  -3513       C  
ATOM   2053  NE  ARG A 308      26.166  -5.694 -31.708  1.00151.21           N  
ANISOU 2053  NE  ARG A 308    15950  28563  12940  -3896    458  -3175       N  
ATOM   2054  CZ  ARG A 308      26.167  -5.139 -30.499  1.00158.34           C  
ANISOU 2054  CZ  ARG A 308    17004  29386  13771  -4005    470  -3104       C  
ATOM   2055  NH1 ARG A 308      27.282  -5.108 -29.775  1.00144.94           N  
ANISOU 2055  NH1 ARG A 308    15088  28006  11976  -4071    376  -3332       N  
ATOM   2056  NH2 ARG A 308      25.057  -4.609 -30.005  1.00137.12           N  
ANISOU 2056  NH2 ARG A 308    14672  26327  11102  -4040    570  -2826       N  
ATOM   2057  N   PHE A 309      31.213  -7.562 -36.135  1.00153.36           N  
ANISOU 2057  N   PHE A 309    14203  31181  12887  -3898    297  -4901       N  
ATOM   2058  CA  PHE A 309      32.367  -7.515 -37.043  1.00155.70           C  
ANISOU 2058  CA  PHE A 309    14040  32117  13003  -4079    374  -5330       C  
ATOM   2059  C   PHE A 309      31.915  -7.705 -38.530  1.00156.16           C  
ANISOU 2059  C   PHE A 309    14105  32136  13094  -4093    497  -5292       C  
ATOM   2060  O   PHE A 309      32.038  -6.740 -39.290  1.00155.91           O  
ANISOU 2060  O   PHE A 309    14138  32232  12870  -4579    804  -5304       O  
ATOM   2061  CB  PHE A 309      33.430  -8.575 -36.653  1.00160.43           C  
ANISOU 2061  CB  PHE A 309    14151  33187  13618  -3673     30  -5750       C  
ATOM   2062  CG  PHE A 309      34.666  -8.666 -37.530  1.00165.86           C  
ANISOU 2062  CG  PHE A 309    14280  34625  14115  -3789     68  -6265       C  
ATOM   2063  CD1 PHE A 309      34.708  -9.538 -38.615  1.00169.28           C  
ANISOU 2063  CD1 PHE A 309    14474  35227  14619  -3497    -43  -6441       C  
ATOM   2064  CD2 PHE A 309      35.812  -7.938 -37.226  1.00170.17           C  
ANISOU 2064  CD2 PHE A 309    14659  35469  14527  -4096    175  -6481       C  
ATOM   2065  CE1 PHE A 309      35.855  -9.640 -39.408  1.00171.11           C  
ANISOU 2065  CE1 PHE A 309    14503  35569  14943  -3447    -51  -6661       C  
ATOM   2066  CE2 PHE A 309      36.963  -8.048 -38.015  1.00172.11           C  
ANISOU 2066  CE2 PHE A 309    14898  35455  15040  -3939    134  -6527       C  
ATOM   2067  CZ  PHE A 309      36.977  -8.898 -39.100  1.00170.72           C  
ANISOU 2067  CZ  PHE A 309    14479  35470  14916  -3678     41  -6702       C  
ATOM   2068  N   PRO A 310      31.395  -8.879 -38.987  1.00150.31           N  
ANISOU 2068  N   PRO A 310    13333  31209  12569  -3609    269  -5241       N  
ATOM   2069  CA  PRO A 310      31.104  -9.018 -40.421  1.00149.56           C  
ANISOU 2069  CA  PRO A 310    13200  31148  12479  -3648    393  -5251       C  
ATOM   2070  C   PRO A 310      29.820  -8.293 -40.882  1.00149.33           C  
ANISOU 2070  C   PRO A 310    13680  30562  12498  -3871    637  -4813       C  
ATOM   2071  O   PRO A 310      29.700  -8.078 -42.089  1.00149.87           O  
ANISOU 2071  O   PRO A 310    13745  30699  12500  -4046    807  -4834       O  
ATOM   2072  CB  PRO A 310      30.941 -10.530 -40.607  1.00150.97           C  
ANISOU 2072  CB  PRO A 310    13220  31266  12876  -3032     31  -5329       C  
ATOM   2073  CG  PRO A 310      31.514 -11.144 -39.376  1.00156.68           C  
ANISOU 2073  CG  PRO A 310    13799  32092  13639  -2715   -289  -5484       C  
ATOM   2074  CD  PRO A 310      31.211 -10.172 -38.300  1.00151.00           C  
ANISOU 2074  CD  PRO A 310    13389  31116  12866  -3023   -133  -5229       C  
ATOM   2075  N   VAL A 311      28.883  -7.900 -39.977  1.00141.51           N  
ANISOU 2075  N   VAL A 311    13112  29052  11601  -3866    652  -4445       N  
ATOM   2076  CA  VAL A 311      27.673  -7.177 -40.429  1.00137.92           C  
ANISOU 2076  CA  VAL A 311    13122  28107  11174  -4043    864  -4078       C  
ATOM   2077  C   VAL A 311      28.058  -5.728 -40.805  1.00141.63           C  
ANISOU 2077  C   VAL A 311    13741  28708  11364  -4639   1184  -4115       C  
ATOM   2078  O   VAL A 311      27.433  -5.150 -41.693  1.00140.28           O  
ANISOU 2078  O   VAL A 311    13851  28310  11140  -4836   1366  -3953       O  
ATOM   2079  CB  VAL A 311      26.467  -7.177 -39.441  1.00138.98           C  
ANISOU 2079  CB  VAL A 311    13653  27681  11474  -3853    793  -3698       C  
ATOM   2080  CG1 VAL A 311      25.901  -8.576 -39.244  1.00137.22           C  
ANISOU 2080  CG1 VAL A 311    13381  27260  11496  -3338    497  -3608       C  
ATOM   2081  CG2 VAL A 311      26.805  -6.517 -38.105  1.00139.62           C  
ANISOU 2081  CG2 VAL A 311    13822  27768  11460  -4022    807  -3684       C  
ATOM   2082  N   PHE A 312      29.081  -5.159 -40.133  1.00139.47           N  
ANISOU 2082  N   PHE A 312    13305  28789  10900  -4928   1235  -4329       N  
ATOM   2083  CA  PHE A 312      29.575  -3.810 -40.395  1.00140.76           C  
ANISOU 2083  CA  PHE A 312    13617  29108  10759  -5542   1515  -4390       C  
ATOM   2084  C   PHE A 312      30.428  -3.799 -41.660  1.00145.46           C  
ANISOU 2084  C   PHE A 312    13896  30215  11155  -5823   1645  -4700       C  
ATOM   2085  O   PHE A 312      30.367  -2.845 -42.440  1.00145.47           O  
ANISOU 2085  O   PHE A 312    14158  30177  10937  -6293   1885  -4644       O  
ATOM   2086  CB  PHE A 312      30.376  -3.285 -39.198  1.00144.55           C  
ANISOU 2086  CB  PHE A 312    14010  29810  11102  -5751   1510  -4523       C  
ATOM   2087  N   LEU A 313      31.214  -4.876 -41.861  1.00142.65           N  
ANISOU 2087  N   LEU A 313    12997  30340  10862  -5526   1468  -5037       N  
ATOM   2088  CA  LEU A 313      32.089  -5.089 -43.019  1.00145.07           C  
ANISOU 2088  CA  LEU A 313    12891  31232  10995  -5704   1551  -5401       C  
ATOM   2089  C   LEU A 313      31.268  -5.200 -44.316  1.00147.60           C  
ANISOU 2089  C   LEU A 313    13428  31281  11373  -5681   1646  -5220       C  
ATOM   2090  O   LEU A 313      31.723  -4.755 -45.370  1.00149.30           O  
ANISOU 2090  O   LEU A 313    13559  31817  11350  -6086   1849  -5383       O  
ATOM   2091  CB  LEU A 313      32.917  -6.379 -42.789  1.00146.52           C  
ANISOU 2091  CB  LEU A 313    12480  31898  11291  -5219   1256  -5786       C  
ATOM   2092  CG  LEU A 313      33.896  -6.839 -43.884  1.00154.02           C  
ANISOU 2092  CG  LEU A 313    12888  33548  12085  -5269   1276  -6247       C  
ATOM   2093  CD1 LEU A 313      34.965  -5.790 -44.166  1.00157.90           C  
ANISOU 2093  CD1 LEU A 313    13180  34636  12179  -5968   1562  -6542       C  
ATOM   2094  CD2 LEU A 313      34.553  -8.141 -43.495  1.00157.32           C  
ANISOU 2094  CD2 LEU A 313    12802  34327  12645  -4674    914  -6599       C  
ATOM   2095  N   ALA A 314      30.060  -5.785 -44.221  1.00140.58           N  
ANISOU 2095  N   ALA A 314    12818  29814  10781  -5231   1501  -4887       N  
ATOM   2096  CA  ALA A 314      29.157  -5.991 -45.341  1.00138.66           C  
ANISOU 2096  CA  ALA A 314    12790  29260  10634  -5128   1553  -4692       C  
ATOM   2097  C   ALA A 314      28.381  -4.704 -45.693  1.00142.41           C  
ANISOU 2097  C   ALA A 314    13843  29301  10967  -5552   1804  -4380       C  
ATOM   2098  O   ALA A 314      28.334  -4.359 -46.873  1.00144.26           O  
ANISOU 2098  O   ALA A 314    14171  29585  11056  -5814   1963  -4396       O  
ATOM   2099  CB  ALA A 314      28.181  -7.114 -45.024  1.00136.13           C  
ANISOU 2099  CB  ALA A 314    12540  28519  10664  -4507   1290  -4474       C  
ATOM   2100  N   ILE A 315      27.784  -3.995 -44.690  1.00136.23           N  
ANISOU 2100  N   ILE A 315    13458  28095  10208  -5610   1822  -4112       N  
ATOM   2101  CA  ILE A 315      26.965  -2.781 -44.917  1.00134.77           C  
ANISOU 2101  CA  ILE A 315    13872  27440   9894  -5928   2002  -3821       C  
ATOM   2102  C   ILE A 315      27.856  -1.609 -45.437  1.00140.98           C  
ANISOU 2102  C   ILE A 315    14762  28525  10279  -6624   2244  -3986       C  
ATOM   2103  O   ILE A 315      27.357  -0.764 -46.190  1.00140.74           O  
ANISOU 2103  O   ILE A 315    15184  28204  10085  -6923   2388  -3823       O  
ATOM   2104  CB  ILE A 315      26.155  -2.335 -43.638  1.00135.79           C  
ANISOU 2104  CB  ILE A 315    14367  27092  10134  -5787   1941  -3541       C  
ATOM   2105  CG1 ILE A 315      25.241  -1.107 -43.908  1.00135.84           C  
ANISOU 2105  CG1 ILE A 315    15011  26593  10008  -6035   2082  -3268       C  
ATOM   2106  CG2 ILE A 315      27.048  -2.062 -42.424  1.00138.08           C  
ANISOU 2106  CG2 ILE A 315    14483  27651  10329  -5940   1915  -3694       C  
ATOM   2107  CD1 ILE A 315      24.221  -1.254 -45.027  1.00144.90           C  
ANISOU 2107  CD1 ILE A 315    16403  27409  11245  -5867   2096  -3091       C  
ATOM   2108  N   LEU A 316      29.148  -1.578 -45.062  1.00139.66           N  
ANISOU 2108  N   LEU A 316    14191  28936   9936  -6883   2274  -4313       N  
ATOM   2109  CA  LEU A 316      30.069  -0.520 -45.483  1.00142.93           C  
ANISOU 2109  CA  LEU A 316    14666  29702   9939  -7596   2503  -4497       C  
ATOM   2110  C   LEU A 316      30.314  -0.569 -47.015  1.00147.75           C  
ANISOU 2110  C   LEU A 316    15192  30576  10370  -7860   2642  -4633       C  
ATOM   2111  O   LEU A 316      29.977   0.386 -47.718  1.00148.05           O  
ANISOU 2111  O   LEU A 316    15723  30353  10175  -8292   2806  -4476       O  
ATOM   2112  CB  LEU A 316      31.412  -0.648 -44.719  1.00145.80           C  
ANISOU 2112  CB  LEU A 316    14515  30709  10174  -7757   2484  -4864       C  
ATOM   2113  CG  LEU A 316      32.512   0.393 -45.015  1.00154.45           C  
ANISOU 2113  CG  LEU A 316    15589  32281  10813  -8545   2721  -5108       C  
ATOM   2114  CD1 LEU A 316      32.100   1.797 -44.556  1.00154.68           C  
ANISOU 2114  CD1 LEU A 316    16304  31828  10638  -8999   2845  -4828       C  
ATOM   2115  CD2 LEU A 316      33.810   0.006 -44.340  1.00157.76           C  
ANISOU 2115  CD2 LEU A 316    15446  33244  11252  -8468   2637  -5455       C  
ATOM   2116  N   ILE A 317      30.856  -1.699 -47.514  1.00144.30           N  
ANISOU 2116  N   ILE A 317    14162  30625  10040  -7571   2552  -4923       N  
ATOM   2117  CA  ILE A 317      31.240  -1.912 -48.913  1.00146.01           C  
ANISOU 2117  CA  ILE A 317    14170  31216  10090  -7780   2669  -5126       C  
ATOM   2118  C   ILE A 317      29.973  -2.038 -49.827  1.00146.39           C  
ANISOU 2118  C   ILE A 317    14639  30683  10298  -7550   2660  -4797       C  
ATOM   2119  O   ILE A 317      30.089  -1.820 -51.034  1.00147.15           O  
ANISOU 2119  O   ILE A 317    14792  30925  10191  -7862   2806  -4863       O  
ATOM   2120  CB  ILE A 317      32.166  -3.159 -49.044  1.00150.89           C  
ANISOU 2120  CB  ILE A 317    14007  32522  10801  -7435   2526  -5562       C  
ATOM   2121  CG1 ILE A 317      31.507  -4.455 -48.497  1.00147.88           C  
ANISOU 2121  CG1 ILE A 317    13469  31848  10871  -6605   2210  -5456       C  
ATOM   2122  CG2 ILE A 317      33.506  -2.889 -48.342  1.00155.45           C  
ANISOU 2122  CG2 ILE A 317    14165  33750  11150  -7749   2565  -5938       C  
ATOM   2123  CD1 ILE A 317      32.404  -5.775 -48.544  1.00155.78           C  
ANISOU 2123  CD1 ILE A 317    13741  33471  11976  -6162   1989  -5901       C  
ATOM   2124  N   ASN A 318      28.783  -2.318 -49.253  1.00139.13           N  
ANISOU 2124  N   ASN A 318    14026  29131   9707  -7055   2503  -4454       N  
ATOM   2125  CA  ASN A 318      27.526  -2.378 -50.011  1.00136.39           C  
ANISOU 2125  CA  ASN A 318    14084  28229   9508  -6828   2486  -4146       C  
ATOM   2126  C   ASN A 318      27.005  -0.970 -50.366  1.00140.83           C  
ANISOU 2126  C   ASN A 318    15342  28360   9808  -7309   2656  -3902       C  
ATOM   2127  O   ASN A 318      26.135  -0.856 -51.233  1.00139.15           O  
ANISOU 2127  O   ASN A 318    15475  27771   9624  -7237   2671  -3705       O  
ATOM   2128  CB  ASN A 318      26.438  -3.140 -49.251  1.00133.73           C  
ANISOU 2128  CB  ASN A 318    13817  27419   9575  -6175   2264  -3892       C  
ATOM   2129  CG  ASN A 318      26.359  -4.621 -49.553  1.00150.76           C  
ANISOU 2129  CG  ASN A 318    15532  29732  12017  -5625   2069  -4001       C  
ATOM   2130  OD1 ASN A 318      26.463  -5.055 -50.708  1.00136.03           O  
ANISOU 2130  OD1 ASN A 318    13506  28054  10127  -5610   2098  -4118       O  
ATOM   2131  ND2 ASN A 318      25.913  -5.390 -48.569  1.00144.72           N  
ANISOU 2131  ND2 ASN A 318    14680  28767  11541  -5143   1854  -3897       N  
ATOM   2132  N   PHE A 319      27.509   0.087 -49.688  1.00138.92           N  
ANISOU 2132  N   PHE A 319    15329  28146   9307  -7775   2758  -3916       N  
ATOM   2133  CA  PHE A 319      27.111   1.477 -49.953  1.00139.33           C  
ANISOU 2133  CA  PHE A 319    16095  27777   9067  -8254   2885  -3707       C  
ATOM   2134  C   PHE A 319      27.855   2.050 -51.158  1.00144.15           C  
ANISOU 2134  C   PHE A 319    16787  28721   9264  -8914   3084  -3874       C  
ATOM   2135  O   PHE A 319      27.254   2.732 -51.994  1.00143.70           O  
ANISOU 2135  O   PHE A 319    17291  28271   9036  -9135   3142  -3687       O  
ATOM   2136  CB  PHE A 319      27.358   2.381 -48.720  1.00142.14           C  
ANISOU 2136  CB  PHE A 319    16700  28012   9295  -8501   2897  -3656       C  
ATOM   2137  CG  PHE A 319      27.381   3.871 -49.023  1.00146.49           C  
ANISOU 2137  CG  PHE A 319    17938  28288   9432  -9147   3031  -3545       C  
ATOM   2138  CD1 PHE A 319      26.202   4.571 -49.258  1.00148.25           C  
ANISOU 2138  CD1 PHE A 319    18869  27810   9650  -9048   2976  -3233       C  
ATOM   2139  CD2 PHE A 319      28.580   4.576 -49.044  1.00152.87           C  
ANISOU 2139  CD2 PHE A 319    18704  29542   9837  -9854   3193  -3767       C  
ATOM   2140  CE1 PHE A 319      26.226   5.945 -49.536  1.00151.94           C  
ANISOU 2140  CE1 PHE A 319    20038  27978   9714  -9625   3055  -3135       C  
ATOM   2141  CE2 PHE A 319      28.602   5.948 -49.323  1.00158.49           C  
ANISOU 2141  CE2 PHE A 319    20117  29966  10137 -10486   3295  -3654       C  
ATOM   2142  CZ  PHE A 319      27.425   6.623 -49.564  1.00155.13           C  
ANISOU 2142  CZ  PHE A 319    20437  28793   9711 -10356   3212  -3333       C  
ATOM   2143  N   PHE A 320      29.170   1.833 -51.206  1.00142.14           N  
ANISOU 2143  N   PHE A 320    15996  29197   8816  -9253   3185  -4237       N  
ATOM   2144  CA  PHE A 320      30.011   2.388 -52.249  1.00145.59           C  
ANISOU 2144  CA  PHE A 320    16447  30062   8807  -9964   3398  -4442       C  
ATOM   2145  C   PHE A 320      29.717   1.700 -53.572  1.00146.78           C  
ANISOU 2145  C   PHE A 320    16456  30293   9020  -9792   3410  -4478       C  
ATOM   2146  O   PHE A 320      29.925   2.312 -54.614  1.00149.06           O  
ANISOU 2146  O   PHE A 320    17023  30658   8953 -10343   3571  -4503       O  
ATOM   2147  CB  PHE A 320      31.492   2.268 -51.874  1.00151.06           C  
ANISOU 2147  CB  PHE A 320    16533  31548   9315 -10292   3485  -4849       C  
ATOM   2148  CG  PHE A 320      31.790   2.939 -50.552  1.00152.46           C  
ANISOU 2148  CG  PHE A 320    16895  31483   9548 -10305   3433  -4747       C  
ATOM   2149  CD1 PHE A 320      31.924   4.321 -50.468  1.00154.99           C  
ANISOU 2149  CD1 PHE A 320    17943  31105   9840 -10483   3453  -4428       C  
ATOM   2150  CD2 PHE A 320      31.918   2.192 -49.387  1.00154.01           C  
ANISOU 2150  CD2 PHE A 320    16616  31923   9978  -9898   3291  -4880       C  
ATOM   2151  CE1 PHE A 320      32.168   4.943 -49.238  1.00155.92           C  
ANISOU 2151  CE1 PHE A 320    18223  31030   9988 -10506   3403  -4352       C  
ATOM   2152  CE2 PHE A 320      32.159   2.816 -48.157  1.00156.06           C  
ANISOU 2152  CE2 PHE A 320    17080  31894  10323  -9861   3231  -4758       C  
ATOM   2153  CZ  PHE A 320      32.287   4.186 -48.091  1.00155.15           C  
ANISOU 2153  CZ  PHE A 320    17593  31368   9990 -10310   3326  -4559       C  
ATOM   2154  N   ILE A 321      29.152   0.478 -53.543  1.00138.62           N  
ANISOU 2154  N   ILE A 321    15068  29179   8422  -9047   3231  -4451       N  
ATOM   2155  CA  ILE A 321      28.779  -0.204 -54.781  1.00137.21           C  
ANISOU 2155  CA  ILE A 321    14781  29023   8329  -8835   3224  -4465       C  
ATOM   2156  C   ILE A 321      27.402   0.363 -55.210  1.00136.64           C  
ANISOU 2156  C   ILE A 321    15460  28137   8318  -8724   3187  -4047       C  
ATOM   2157  O   ILE A 321      27.229   0.682 -56.383  1.00136.66           O  
ANISOU 2157  O   ILE A 321    15741  28070   8115  -9005   3285  -4008       O  
ATOM   2158  CB  ILE A 321      28.814  -1.775 -54.675  1.00138.33           C  
ANISOU 2158  CB  ILE A 321    14244  29444   8871  -8118   3032  -4640       C  
ATOM   2159  CG1 ILE A 321      27.814  -2.399 -53.671  1.00134.45           C  
ANISOU 2159  CG1 ILE A 321    13824  28429   8833  -7411   2794  -4378       C  
ATOM   2160  CG2 ILE A 321      30.222  -2.266 -54.386  1.00142.49           C  
ANISOU 2160  CG2 ILE A 321    14051  30808   9282  -8234   3050  -5103       C  
ATOM   2161  CD1 ILE A 321      26.367  -2.588 -54.139  1.00139.68           C  
ANISOU 2161  CD1 ILE A 321    14908  28422   9741  -7014   2703  -4023       C  
ATOM   2162  N   PHE A 322      26.492   0.598 -54.228  1.00129.64           N  
ANISOU 2162  N   PHE A 322    14920  26672   7667  -8371   3053  -3762       N  
ATOM   2163  CA  PHE A 322      25.130   1.125 -54.389  1.00126.61           C  
ANISOU 2163  CA  PHE A 322    15209  25526   7372  -8166   2978  -3396       C  
ATOM   2164  C   PHE A 322      25.132   2.494 -55.082  1.00132.61           C  
ANISOU 2164  C   PHE A 322    16670  26031   7687  -8813   3110  -3294       C  
ATOM   2165  O   PHE A 322      24.299   2.727 -55.961  1.00131.13           O  
ANISOU 2165  O   PHE A 322    16924  25429   7471  -8748   3082  -3112       O  
ATOM   2166  CB  PHE A 322      24.441   1.237 -53.006  1.00125.50           C  
ANISOU 2166  CB  PHE A 322    15225  24976   7483  -7776   2835  -3198       C  
ATOM   2167  CG  PHE A 322      23.151   2.026 -52.960  1.00125.48           C  
ANISOU 2167  CG  PHE A 322    15936  24240   7500  -7630   2760  -2873       C  
ATOM   2168  CD1 PHE A 322      23.155   3.380 -52.641  1.00130.86           C  
ANISOU 2168  CD1 PHE A 322    17228  24619   7872  -8057   2806  -2772       C  
ATOM   2169  CD2 PHE A 322      21.937   1.423 -53.251  1.00124.43           C  
ANISOU 2169  CD2 PHE A 322    15871  23733   7676  -7063   2628  -2690       C  
ATOM   2170  CE1 PHE A 322      21.965   4.115 -52.619  1.00130.75           C  
ANISOU 2170  CE1 PHE A 322    17880  23937   7861  -7872   2702  -2510       C  
ATOM   2171  CE2 PHE A 322      20.743   2.153 -53.202  1.00126.18           C  
ANISOU 2171  CE2 PHE A 322    16714  23326   7904  -6893   2544  -2435       C  
ATOM   2172  CZ  PHE A 322      20.766   3.496 -52.900  1.00126.47           C  
ANISOU 2172  CZ  PHE A 322    17352  23068   7633  -7279   2573  -2356       C  
ATOM   2173  N   VAL A 323      26.035   3.402 -54.668  1.00132.29           N  
ANISOU 2173  N   VAL A 323    16767  26209   7288  -9434   3233  -3405       N  
ATOM   2174  CA  VAL A 323      26.106   4.747 -55.246  1.00135.38           C  
ANISOU 2174  CA  VAL A 323    17892  26339   7208 -10114   3337  -3306       C  
ATOM   2175  C   VAL A 323      26.667   4.660 -56.695  1.00143.05           C  
ANISOU 2175  C   VAL A 323    18782  27692   7879 -10573   3493  -3469       C  
ATOM   2176  O   VAL A 323      26.340   5.528 -57.507  1.00145.34           O  
ANISOU 2176  O   VAL A 323    19752  27620   7851 -10968   3528  -3320       O  
ATOM   2177  CB  VAL A 323      26.910   5.759 -54.390  1.00141.80           C  
ANISOU 2177  CB  VAL A 323    18914  27268   7696 -10694   3420  -3374       C  
ATOM   2178  CG1 VAL A 323      26.157   6.104 -53.112  1.00139.04           C  
ANISOU 2178  CG1 VAL A 323    18858  26396   7576 -10292   3261  -3159       C  
ATOM   2179  CG2 VAL A 323      28.321   5.261 -54.081  1.00143.89           C  
ANISOU 2179  CG2 VAL A 323    18411  28392   7870 -10985   3553  -3748       C  
ATOM   2180  N   ARG A 324      27.456   3.611 -57.037  1.00138.97           N  
ANISOU 2180  N   ARG A 324    17469  27878   7455 -10493   3564  -3775       N  
ATOM   2181  CA  ARG A 324      27.920   3.490 -58.416  1.00140.92           C  
ANISOU 2181  CA  ARG A 324    17617  28500   7425 -10890   3710  -3939       C  
ATOM   2182  C   ARG A 324      26.816   2.820 -59.233  1.00142.37           C  
ANISOU 2182  C   ARG A 324    17901  28286   7907 -10317   3589  -3755       C  
ATOM   2183  O   ARG A 324      26.680   3.110 -60.421  1.00143.68           O  
ANISOU 2183  O   ARG A 324    18386  28380   7826 -10625   3666  -3718       O  
ATOM   2184  CB  ARG A 324      29.256   2.744 -58.544  1.00142.14           C  
ANISOU 2184  CB  ARG A 324    16901  29614   7491 -11083   3838  -4387       C  
ATOM   2185  CG  ARG A 324      29.887   3.001 -59.913  1.00150.81           C  
ANISOU 2185  CG  ARG A 324    18157  30469   8674 -10982   3871  -4287       C  
ATOM   2186  CD  ARG A 324      31.175   2.260 -60.189  1.00155.39           C  
ANISOU 2186  CD  ARG A 324    18111  31174   9757 -10311   3797  -4400       C  
ATOM   2187  NE  ARG A 324      31.708   2.631 -61.504  1.00157.68           N  
ANISOU 2187  NE  ARG A 324    18639  31149  10122 -10219   3827  -4252       N  
ATOM   2188  CZ  ARG A 324      31.397   2.021 -62.648  1.00165.77           C  
ANISOU 2188  CZ  ARG A 324    19713  31678  11593  -9493   3704  -4043       C  
ATOM   2189  NH1 ARG A 324      30.563   0.988 -62.654  1.00156.33           N  
ANISOU 2189  NH1 ARG A 324    18016  31458   9925 -10032   3829  -4481       N  
ATOM   2190  NH2 ARG A 324      31.923   2.437 -63.792  1.00157.45           N  
ANISOU 2190  NH2 ARG A 324    18702  31103  10018 -10233   3920  -4230       N  
ATOM   2191  N   ILE A 325      25.999   1.958 -58.578  1.00134.79           N  
ANISOU 2191  N   ILE A 325    16706  27051   7459  -9511   3396  -3630       N  
ATOM   2192  CA  ILE A 325      24.845   1.286 -59.187  1.00131.22           C  
ANISOU 2192  CA  ILE A 325    16340  26188   7329  -8915   3259  -3440       C  
ATOM   2193  C   ILE A 325      23.897   2.338 -59.759  1.00134.45           C  
ANISOU 2193  C   ILE A 325    17636  25906   7544  -9088   3233  -3139       C  
ATOM   2194  O   ILE A 325      23.525   2.247 -60.927  1.00133.80           O  
ANISOU 2194  O   ILE A 325    17741  25712   7385  -9112   3247  -3092       O  
ATOM   2195  CB  ILE A 325      24.112   0.355 -58.164  1.00130.17           C  
ANISOU 2195  CB  ILE A 325    15896  25839   7724  -8114   3055  -3334       C  
ATOM   2196  CG1 ILE A 325      24.974  -0.863 -57.746  1.00130.63           C  
ANISOU 2196  CG1 ILE A 325    15100  26539   7994  -7844   3021  -3638       C  
ATOM   2197  CG2 ILE A 325      22.742  -0.103 -58.685  1.00127.97           C  
ANISOU 2197  CG2 ILE A 325    15851  25032   7740  -7555   2911  -3088       C  
ATOM   2198  CD1 ILE A 325      25.388  -1.835 -58.869  1.00140.58           C  
ANISOU 2198  CD1 ILE A 325    15871  28264   9280  -7748   3048  -3875       C  
ATOM   2199  N   VAL A 326      23.530   3.343 -58.944  1.00131.11           N  
ANISOU 2199  N   VAL A 326    17769  25024   7024  -9199   3178  -2953       N  
ATOM   2200  CA  VAL A 326      22.628   4.410 -59.377  1.00131.48           C  
ANISOU 2200  CA  VAL A 326    18712  24377   6868  -9319   3103  -2688       C  
ATOM   2201  C   VAL A 326      23.382   5.320 -60.389  1.00140.61           C  
ANISOU 2201  C   VAL A 326    20302  25674   7451 -10175   3266  -2762       C  
ATOM   2202  O   VAL A 326      22.776   5.720 -61.387  1.00140.69           O  
ANISOU 2202  O   VAL A 326    20862  25296   7296 -10254   3223  -2619       O  
ATOM   2203  CB  VAL A 326      22.003   5.236 -58.204  1.00134.05           C  
ANISOU 2203  CB  VAL A 326    19526  24166   7239  -9158   2970  -2494       C  
ATOM   2204  CG1 VAL A 326      20.986   4.411 -57.421  1.00128.99           C  
ANISOU 2204  CG1 VAL A 326    18595  23292   7122  -8322   2799  -2378       C  
ATOM   2205  CG2 VAL A 326      23.059   5.825 -57.274  1.00136.33           C  
ANISOU 2205  CG2 VAL A 326    19742  24759   7296  -9656   3074  -2624       C  
ATOM   2206  N   GLN A 327      24.708   5.569 -60.170  1.00141.47           N  
ANISOU 2206  N   GLN A 327    20126  26374   7252 -10812   3450  -3002       N  
ATOM   2207  CA  GLN A 327      25.555   6.392 -61.054  1.00146.96           C  
ANISOU 2207  CA  GLN A 327    21165  27314   7359 -11721   3632  -3107       C  
ATOM   2208  C   GLN A 327      25.567   5.811 -62.482  1.00151.52           C  
ANISOU 2208  C   GLN A 327    21571  28131   7868 -11775   3710  -3192       C  
ATOM   2209  O   GLN A 327      25.507   6.575 -63.445  1.00151.69           O  
ANISOU 2209  O   GLN A 327    22195  27759   7682 -11980   3694  -3027       O  
ATOM   2210  CB  GLN A 327      26.998   6.499 -60.502  1.00149.96           C  
ANISOU 2210  CB  GLN A 327    21043  28256   7679 -12016   3764  -3333       C  
ATOM   2211  CG  GLN A 327      27.952   7.442 -61.279  1.00161.97           C  
ANISOU 2211  CG  GLN A 327    22785  28889   9866 -11028   3561  -2926       C  
ATOM   2212  CD  GLN A 327      27.666   8.936 -61.164  1.00173.54           C  
ANISOU 2212  CD  GLN A 327    24971  29143  11824 -10140   3245  -2403       C  
ATOM   2213  OE1 GLN A 327      28.008   9.724 -62.056  1.00169.68           O  
ANISOU 2213  OE1 GLN A 327    24870  28572  11030 -10543   3289  -2351       O  
ATOM   2214  NE2 GLN A 327      27.066   9.371 -60.060  1.00167.66           N  
ANISOU 2214  NE2 GLN A 327    24616  28425  10663 -10726   3266  -2459       N  
ATOM   2215  N   LEU A 328      25.621   4.471 -62.616  1.00146.07           N  
ANISOU 2215  N   LEU A 328    20070  27862   7569 -11235   3704  -3357       N  
ATOM   2216  CA  LEU A 328      25.604   3.855 -63.933  1.00146.80           C  
ANISOU 2216  CA  LEU A 328    19967  28186   7627 -11226   3764  -3449       C  
ATOM   2217  C   LEU A 328      24.156   3.698 -64.406  1.00148.48           C  
ANISOU 2217  C   LEU A 328    20626  27672   8119 -10626   3569  -3145       C  
ATOM   2218  O   LEU A 328      23.924   3.710 -65.609  1.00149.20           O  
ANISOU 2218  O   LEU A 328    20957  27690   8044 -10773   3599  -3113       O  
ATOM   2219  CB  LEU A 328      26.355   2.501 -63.964  1.00146.10           C  
ANISOU 2219  CB  LEU A 328    18839  28885   7788 -10931   3825  -3794       C  
ATOM   2220  CG  LEU A 328      25.867   1.308 -63.125  1.00145.97           C  
ANISOU 2220  CG  LEU A 328    18251  28834   8379 -10025   3639  -3790       C  
ATOM   2221  CD1 LEU A 328      24.700   0.577 -63.804  1.00142.28           C  
ANISOU 2221  CD1 LEU A 328    17859  27945   8258  -9383   3488  -3602       C  
ATOM   2222  CD2 LEU A 328      26.970   0.288 -62.994  1.00150.32           C  
ANISOU 2222  CD2 LEU A 328    17868  30236   9013  -9947   3702  -4195       C  
ATOM   2223  N   LEU A 329      23.187   3.580 -63.468  1.00141.95           N  
ANISOU 2223  N   LEU A 329    19914  26332   7689  -9977   3373  -2935       N  
ATOM   2224  CA  LEU A 329      21.763   3.411 -63.788  1.00138.81           C  
ANISOU 2224  CA  LEU A 329    19884  25283   7575  -9364   3177  -2673       C  
ATOM   2225  C   LEU A 329      21.207   4.647 -64.519  1.00147.04           C  
ANISOU 2225  C   LEU A 329    21917  25723   8227  -9730   3124  -2461       C  
ATOM   2226  O   LEU A 329      20.473   4.490 -65.499  1.00146.32           O  
ANISOU 2226  O   LEU A 329    22082  25347   8166  -9522   3049  -2356       O  
ATOM   2227  CB  LEU A 329      20.945   3.148 -62.505  1.00134.72           C  
ANISOU 2227  CB  LEU A 329    19279  24418   7492  -8696   2999  -2528       C  
ATOM   2228  CG  LEU A 329      19.451   2.805 -62.658  1.00135.69           C  
ANISOU 2228  CG  LEU A 329    19624  23970   7963  -7987   2795  -2302       C  
ATOM   2229  CD1 LEU A 329      19.255   1.433 -63.305  1.00133.49           C  
ANISOU 2229  CD1 LEU A 329    18737  23970   8013  -7541   2780  -2387       C  
ATOM   2230  CD2 LEU A 329      18.760   2.803 -61.306  1.00135.71           C  
ANISOU 2230  CD2 LEU A 329    19617  23670   8275  -7498   2651  -2179       C  
ATOM   2231  N   VAL A 330      21.577   5.864 -64.058  1.00147.42           N  
ANISOU 2231  N   VAL A 330    22541  25576   7895 -10277   3147  -2408       N  
ATOM   2232  CA  VAL A 330      21.119   7.131 -64.649  1.00150.23           C  
ANISOU 2232  CA  VAL A 330    23934  25317   7830 -10660   3057  -2213       C  
ATOM   2233  C   VAL A 330      21.822   7.379 -66.014  1.00158.37           C  
ANISOU 2233  C   VAL A 330    25162  26631   8380 -11389   3224  -2311       C  
ATOM   2234  O   VAL A 330      21.309   8.160 -66.817  1.00159.74           O  
ANISOU 2234  O   VAL A 330    26090  26218   8386 -11387   3085  -2106       O  
ATOM   2235  CB  VAL A 330      21.316   8.347 -63.706  1.00156.02           C  
ANISOU 2235  CB  VAL A 330    25259  25734   8286 -11027   3006  -2132       C  
ATOM   2236  CG1 VAL A 330      20.407   8.246 -62.486  1.00152.16           C  
ANISOU 2236  CG1 VAL A 330    24733  24852   8227 -10290   2812  -2005       C  
ATOM   2237  CG2 VAL A 330      22.777   8.523 -63.293  1.00158.06           C  
ANISOU 2237  CG2 VAL A 330    25111  26597   8349 -11604   3215  -2330       C  
ATOM   2238  N   ALA A 331      22.978   6.721 -66.273  1.00155.52           N  
ANISOU 2238  N   ALA A 331    24053  27084   7953 -11734   3458  -2589       N  
ATOM   2239  CA  ALA A 331      23.689   6.840 -67.555  1.00155.45           C  
ANISOU 2239  CA  ALA A 331    23973  27149   7944 -11726   3510  -2575       C  
ATOM   2240  C   ALA A 331      22.911   6.124 -68.653  1.00158.16           C  
ANISOU 2240  C   ALA A 331    24299  27411   8383 -11439   3467  -2546       C  
ATOM   2241  O   ALA A 331      22.929   6.547 -69.812  1.00158.56           O  
ANISOU 2241  O   ALA A 331    24708  27184   8354 -11419   3425  -2416       O  
ATOM   2242  CB  ALA A 331      25.096   6.274 -67.437  1.00155.29           C  
ANISOU 2242  CB  ALA A 331    23063  27801   8141 -11648   3666  -2808       C  
ATOM   2243  N   LYS A 332      22.186   5.060 -68.256  1.00152.53           N  
ANISOU 2243  N   LYS A 332    23156  26883   7917 -11093   3443  -2637       N  
ATOM   2244  CA  LYS A 332      21.323   4.248 -69.103  1.00149.53           C  
ANISOU 2244  CA  LYS A 332    22652  26330   7832 -10522   3341  -2568       C  
ATOM   2245  C   LYS A 332      19.952   4.925 -69.326  1.00154.96           C  
ANISOU 2245  C   LYS A 332    24211  26119   8547 -10181   3095  -2251       C  
ATOM   2246  O   LYS A 332      19.108   4.343 -70.006  1.00153.51           O  
ANISOU 2246  O   LYS A 332    24002  25720   8604  -9686   2986  -2172       O  
ATOM   2247  CB  LYS A 332      21.125   2.850 -68.483  1.00145.78           C  
ANISOU 2247  CB  LYS A 332    21277  26150   7963  -9743   3288  -2671       C  
ATOM   2248  CG  LYS A 332      22.228   1.813 -68.738  1.00139.47           C  
ANISOU 2248  CG  LYS A 332    19560  26222   7211  -9848   3464  -3013       C  
ATOM   2249  CD  LYS A 332      23.624   2.152 -68.257  1.00145.94           C  
ANISOU 2249  CD  LYS A 332    20063  27677   7708 -10500   3665  -3275       C  
ATOM   2250  CE  LYS A 332      24.591   1.015 -68.469  1.00151.01           C  
ANISOU 2250  CE  LYS A 332    19745  29178   8453 -10440   3785  -3648       C  
ATOM   2251  NZ  LYS A 332      24.754   0.673 -69.906  1.00162.20           N  
ANISOU 2251  NZ  LYS A 332    21122  30534   9971 -10207   3789  -3624       N  
ATOM   2252  N   LEU A 333      19.730   6.143 -68.769  1.00153.49           N  
ANISOU 2252  N   LEU A 333    24793  25421   8105 -10427   2992  -2091       N  
ATOM   2253  CA  LEU A 333      18.476   6.889 -68.956  1.00153.18           C  
ANISOU 2253  CA  LEU A 333    25628  24536   8038 -10105   2726  -1831       C  
ATOM   2254  C   LEU A 333      18.483   7.530 -70.359  1.00161.48           C  
ANISOU 2254  C   LEU A 333    27398  25360   8599 -10629   2724  -1767       C  
ATOM   2255  O   LEU A 333      17.639   7.179 -71.191  1.00158.79           O  
ANISOU 2255  O   LEU A 333    27195  24744   8395 -10223   2601  -1681       O  
ATOM   2256  CB  LEU A 333      18.287   7.949 -67.835  1.00154.15           C  
ANISOU 2256  CB  LEU A 333    26312  24209   8047 -10160   2594  -1715       C  
ATOM   2257  CG  LEU A 333      16.936   8.715 -67.710  1.00158.37           C  
ANISOU 2257  CG  LEU A 333    27685  23877   8612  -9679   2270  -1490       C  
ATOM   2258  CD1 LEU A 333      16.856   9.466 -66.384  1.00158.53           C  
ANISOU 2258  CD1 LEU A 333    27980  23623   8631  -9621   2166  -1439       C  
ATOM   2259  CD2 LEU A 333      16.699   9.691 -68.864  1.00165.13           C  
ANISOU 2259  CD2 LEU A 333    29547  24237   8958 -10101   2150  -1372       C  
ATOM   2260  N   ARG A 334      19.441   8.457 -70.620  1.00161.66           N  
ANISOU 2260  N   ARG A 334    27665  25399   8360 -11054   2776  -1738       N  
ATOM   2261  CA  ARG A 334      19.576   9.130 -71.917  1.00162.33           C  
ANISOU 2261  CA  ARG A 334    28116  25170   8391 -10939   2673  -1583       C  
ATOM   2262  C   ARG A 334      19.980   8.105 -72.996  1.00165.46           C  
ANISOU 2262  C   ARG A 334    27794  26034   9040 -10690   2808  -1687       C  
ATOM   2263  O   ARG A 334      19.410   8.118 -74.094  1.00165.74           O  
ANISOU 2263  O   ARG A 334    28179  25811   8984 -10605   2719  -1600       O  
ATOM   2264  CB  ARG A 334      20.593  10.291 -71.836  1.00161.76           C  
ANISOU 2264  CB  ARG A 334    28150  25006   8307 -11008   2648  -1487       C  
ATOM   2265  CG  ARG A 334      20.904  11.001 -73.172  1.00167.26           C  
ANISOU 2265  CG  ARG A 334    28871  25412   9270 -10450   2500  -1287       C  
ATOM   2266  CD  ARG A 334      19.706  11.658 -73.853  1.00171.80           C  
ANISOU 2266  CD  ARG A 334    30030  25280   9965  -9860   2169  -1059       C  
ATOM   2267  NE  ARG A 334      20.073  12.236 -75.151  1.00173.52           N  
ANISOU 2267  NE  ARG A 334    30290  25398  10240  -9666   2106   -942       N  
ATOM   2268  CZ  ARG A 334      20.003  11.588 -76.313  1.00181.36           C  
ANISOU 2268  CZ  ARG A 334    30727  26494  11688  -8955   2083   -900       C  
ATOM   2269  NH1 ARG A 334      19.563  10.336 -76.358  1.00172.11           N  
ANISOU 2269  NH1 ARG A 334    29761  25675   9959  -9843   2313  -1128       N  
ATOM   2270  NH2 ARG A 334      20.361  12.191 -77.437  1.00172.41           N  
ANISOU 2270  NH2 ARG A 334    30202  25354   9952  -9741   2153   -888       N  
ATOM   2271  N   ALA A 335      20.915   7.185 -72.655  1.00162.70           N  
ANISOU 2271  N   ALA A 335    26630  26484   8706 -11004   3079  -1962       N  
ATOM   2272  CA  ALA A 335      21.370   6.111 -73.550  1.00162.28           C  
ANISOU 2272  CA  ALA A 335    25917  27018   8723 -11019   3252  -2158       C  
ATOM   2273  C   ALA A 335      20.249   5.088 -73.803  1.00164.16           C  
ANISOU 2273  C   ALA A 335    26050  27278   9045 -10811   3214  -2212       C  
ATOM   2274  O   ALA A 335      20.331   4.319 -74.754  1.00163.39           O  
ANISOU 2274  O   ALA A 335    25614  27532   8934 -10840   3310  -2340       O  
ATOM   2275  CB  ALA A 335      22.587   5.415 -72.957  1.00162.13           C  
ANISOU 2275  CB  ALA A 335    24959  27717   8928 -10998   3442  -2406       C  
ATOM   2276  N   ARG A 336      19.209   5.095 -72.940  1.00159.85           N  
ANISOU 2276  N   ARG A 336    25798  26368   8570 -10618   3076  -2125       N  
ATOM   2277  CA  ARG A 336      18.023   4.244 -72.989  1.00155.19           C  
ANISOU 2277  CA  ARG A 336    24974  25478   8514  -9704   2887  -2022       C  
ATOM   2278  C   ARG A 336      18.417   2.761 -73.176  1.00157.18           C  
ANISOU 2278  C   ARG A 336    24187  26395   9140  -9369   3012  -2240       C  
ATOM   2279  O   ARG A 336      17.863   2.057 -74.024  1.00155.22           O  
ANISOU 2279  O   ARG A 336    23791  26110   9077  -9003   2956  -2227       O  
ATOM   2280  CB  ARG A 336      17.084   4.703 -74.096  1.00155.85           C  
ANISOU 2280  CB  ARG A 336    25823  24967   8424  -9621   2716  -1837       C  
ATOM   2281  N   GLN A 337      19.380   2.307 -72.361  1.00153.83           N  
ANISOU 2281  N   GLN A 337    23070  26566   8814  -9484   3159  -2449       N  
ATOM   2282  CA  GLN A 337      19.862   0.927 -72.305  1.00151.43           C  
ANISOU 2282  CA  GLN A 337    21777  26901   8858  -9141   3239  -2689       C  
ATOM   2283  C   GLN A 337      18.941   0.133 -71.356  1.00149.90           C  
ANISOU 2283  C   GLN A 337    21252  26438   9266  -8264   3042  -2579       C  
ATOM   2284  O   GLN A 337      18.162  -0.710 -71.818  1.00146.84           O  
ANISOU 2284  O   GLN A 337    20670  25915   9205  -7704   2927  -2526       O  
ATOM   2285  CB  GLN A 337      21.341   0.912 -71.851  1.00155.50           C  
ANISOU 2285  CB  GLN A 337    21765  28170   9146  -9691   3460  -2987       C  
ATOM   2286  CG  GLN A 337      22.000  -0.467 -71.719  1.00161.68           C  
ANISOU 2286  CG  GLN A 337    21523  29668  10240  -9352   3518  -3292       C  
ATOM   2287  CD  GLN A 337      22.545  -1.010 -73.008  1.00176.08           C  
ANISOU 2287  CD  GLN A 337    23090  31486  12328  -8919   3507  -3299       C  
ATOM   2288  OE1 GLN A 337      23.063  -0.269 -73.854  1.00172.70           O  
ANISOU 2288  OE1 GLN A 337    23016  31006  11597  -9324   3602  -3260       O  
ATOM   2289  NE2 GLN A 337      22.632  -2.328 -73.088  1.00170.41           N  
ANISOU 2289  NE2 GLN A 337    21554  31669  11523  -9042   3600  -3712       N  
ATOM   2290  N   MET A 338      18.985   0.465 -70.035  1.00144.89           N  
ANISOU 2290  N   MET A 338    20608  25697   8747  -8179   2999  -2531       N  
ATOM   2291  CA  MET A 338      18.150  -0.145 -68.994  1.00139.92           C  
ANISOU 2291  CA  MET A 338    19724  24814   8625  -7444   2824  -2420       C  
ATOM   2292  C   MET A 338      16.774   0.535 -69.006  1.00142.06           C  
ANISOU 2292  C   MET A 338    20718  24310   8947  -7124   2627  -2135       C  
ATOM   2293  O   MET A 338      16.491   1.412 -68.182  1.00141.59           O  
ANISOU 2293  O   MET A 338    21097  23891   8811  -7167   2555  -2012       O  
ATOM   2294  CB  MET A 338      18.825  -0.058 -67.610  1.00141.85           C  
ANISOU 2294  CB  MET A 338    19656  25306   8934  -7522   2867  -2508       C  
ATOM   2295  N   HIS A 339      15.939   0.137 -69.995  1.00136.77           N  
ANISOU 2295  N   HIS A 339    20172  23405   8389  -6802   2533  -2053       N  
ATOM   2296  CA  HIS A 339      14.588   0.645 -70.265  1.00134.65           C  
ANISOU 2296  CA  HIS A 339    20536  22458   8167  -6441   2328  -1829       C  
ATOM   2297  C   HIS A 339      13.638   0.349 -69.064  1.00134.85           C  
ANISOU 2297  C   HIS A 339    20408  22216   8612  -5793   2163  -1723       C  
ATOM   2298  O   HIS A 339      13.895  -0.565 -68.274  1.00131.13           O  
ANISOU 2298  O   HIS A 339    19279  22082   8464  -5535   2193  -1807       O  
ATOM   2299  CB  HIS A 339      14.055   0.009 -71.573  1.00133.83           C  
ANISOU 2299  CB  HIS A 339    20396  22315   8138  -6216   2286  -1819       C  
ATOM   2300  CG  HIS A 339      12.747   0.559 -72.061  1.00136.04           C  
ANISOU 2300  CG  HIS A 339    21341  21943   8404  -5893   2074  -1626       C  
ATOM   2301  ND1 HIS A 339      11.567  -0.152 -71.922  1.00133.84           N  
ANISOU 2301  ND1 HIS A 339    20862  21447   8543  -5180   1906  -1548       N  
ATOM   2302  CD2 HIS A 339      12.475   1.744 -72.657  1.00140.29           C  
ANISOU 2302  CD2 HIS A 339    22737  22025   8542  -6194   1992  -1517       C  
ATOM   2303  CE1 HIS A 339      10.624   0.610 -72.454  1.00133.92           C  
ANISOU 2303  CE1 HIS A 339    21566  20913   8405  -5045   1732  -1417       C  
ATOM   2304  NE2 HIS A 339      11.120   1.764 -72.900  1.00138.18           N  
ANISOU 2304  NE2 HIS A 339    22781  21263   8456  -5620   1761  -1389       N  
ATOM   2305  N   HIS A 340      12.552   1.153 -68.940  1.00132.32           N  
ANISOU 2305  N   HIS A 340    20724  21297   8255  -5547   1977  -1555       N  
ATOM   2306  CA  HIS A 340      11.525   1.113 -67.883  1.00129.97           C  
ANISOU 2306  CA  HIS A 340    20411  20703   8269  -4976   1810  -1461       C  
ATOM   2307  C   HIS A 340      10.968  -0.295 -67.659  1.00128.75           C  
ANISOU 2307  C   HIS A 340    19559  20758   8603  -4396   1770  -1482       C  
ATOM   2308  O   HIS A 340      10.375  -0.565 -66.606  1.00125.95           O  
ANISOU 2308  O   HIS A 340    18997  20335   8525  -3999   1685  -1442       O  
ATOM   2309  CB  HIS A 340      10.356   2.050 -68.245  1.00132.39           C  
ANISOU 2309  CB  HIS A 340    21491  20376   8435  -4744   1592  -1329       C  
ATOM   2310  CG  HIS A 340      10.773   3.459 -68.541  1.00140.59           C  
ANISOU 2310  CG  HIS A 340    23347  21106   8966  -5287   1573  -1288       C  
ATOM   2311  ND1 HIS A 340      10.924   3.911 -69.847  1.00145.49           N  
ANISOU 2311  ND1 HIS A 340    24472  21572   9236  -5641   1570  -1265       N  
ATOM   2312  CD2 HIS A 340      11.096   4.464 -67.691  1.00144.69           C  
ANISOU 2312  CD2 HIS A 340    24265  21450   9260  -5555   1552  -1267       C  
ATOM   2313  CE1 HIS A 340      11.308   5.175 -69.748  1.00148.75           C  
ANISOU 2313  CE1 HIS A 340    25603  21700   9213  -6120   1536  -1222       C  
ATOM   2314  NE2 HIS A 340      11.431   5.552 -68.470  1.00148.73           N  
ANISOU 2314  NE2 HIS A 340    25563  21675   9273  -6083   1523  -1224       N  
ATOM   2315  N   THR A 341      11.152  -1.182 -68.654  1.00123.77           N  
ANISOU 2315  N   THR A 341    18591  20380   8056  -4367   1825  -1547       N  
ATOM   2316  CA  THR A 341      10.661  -2.556 -68.633  1.00119.90           C  
ANISOU 2316  CA  THR A 341    17498  20071   7989  -3862   1772  -1569       C  
ATOM   2317  C   THR A 341      11.818  -3.576 -68.817  1.00121.39           C  
ANISOU 2317  C   THR A 341    17029  20843   8251  -4039   1915  -1745       C  
ATOM   2318  O   THR A 341      11.572  -4.697 -69.264  1.00119.64           O  
ANISOU 2318  O   THR A 341    16397  20777   8285  -3721   1872  -1785       O  
ATOM   2319  CB  THR A 341       9.594  -2.747 -69.735  1.00130.19           C  
ANISOU 2319  CB  THR A 341    19033  21080   9352  -3543   1647  -1492       C  
ATOM   2320  OG1 THR A 341      10.176  -2.468 -71.014  1.00134.27           O  
ANISOU 2320  OG1 THR A 341    19785  21670   9560  -3947   1737  -1541       O  
ATOM   2321  CG2 THR A 341       8.351  -1.876 -69.514  1.00129.69           C  
ANISOU 2321  CG2 THR A 341    19545  20476   9255  -3247   1463  -1361       C  
ATOM   2322  N   ASP A 342      13.058  -3.210 -68.451  1.00117.75           N  
ANISOU 2322  N   ASP A 342    16459  20714   7565  -4521   2066  -1869       N  
ATOM   2323  CA  ASP A 342      14.183  -4.144 -68.573  1.00116.93           C  
ANISOU 2323  CA  ASP A 342    15709  21207   7513  -4655   2180  -2086       C  
ATOM   2324  C   ASP A 342      14.200  -5.066 -67.361  1.00116.90           C  
ANISOU 2324  C   ASP A 342    15164  21377   7875  -4269   2105  -2122       C  
ATOM   2325  O   ASP A 342      13.894  -4.608 -66.263  1.00115.47           O  
ANISOU 2325  O   ASP A 342    15128  20992   7753  -4191   2058  -2024       O  
ATOM   2326  CB  ASP A 342      15.517  -3.380 -68.720  1.00122.07           C  
ANISOU 2326  CB  ASP A 342    16436  22203   7744  -5350   2375  -2240       C  
ATOM   2327  CG  ASP A 342      16.754  -4.225 -68.988  1.00128.92           C  
ANISOU 2327  CG  ASP A 342    16642  23752   8589  -5530   2499  -2524       C  
ATOM   2328  OD1 ASP A 342      16.607  -5.444 -69.226  1.00125.65           O  
ANISOU 2328  OD1 ASP A 342    15743  23524   8476  -5108   2420  -2604       O  
ATOM   2329  OD2 ASP A 342      17.863  -3.658 -69.011  1.00139.05           O  
ANISOU 2329  OD2 ASP A 342    17907  25392   9532  -6100   2665  -2682       O  
ATOM   2330  N   TYR A 343      14.562  -6.363 -67.553  1.00112.03           N  
ANISOU 2330  N   TYR A 343    13952  21128   7487  -4026   2075  -2268       N  
ATOM   2331  CA  TYR A 343      14.618  -7.337 -66.451  1.00109.69           C  
ANISOU 2331  CA  TYR A 343    13173  20987   7519  -3660   1970  -2308       C  
ATOM   2332  C   TYR A 343      15.736  -6.934 -65.493  1.00114.61           C  
ANISOU 2332  C   TYR A 343    13627  21924   7997  -3986   2064  -2443       C  
ATOM   2333  O   TYR A 343      15.636  -7.163 -64.284  1.00113.37           O  
ANISOU 2333  O   TYR A 343    13320  21730   8025  -3784   1985  -2401       O  
ATOM   2334  CB  TYR A 343      14.808  -8.784 -66.963  1.00110.19           C  
ANISOU 2334  CB  TYR A 343    12708  21344   7814  -3338   1882  -2451       C  
ATOM   2335  CG  TYR A 343      16.243  -9.242 -67.113  1.00114.53           C  
ANISOU 2335  CG  TYR A 343    12777  22495   8242  -3558   1961  -2759       C  
ATOM   2336  CD1 TYR A 343      16.993  -8.893 -68.229  1.00119.59           C  
ANISOU 2336  CD1 TYR A 343    13424  23441   8576  -3961   2117  -2928       C  
ATOM   2337  CD2 TYR A 343      16.827 -10.083 -66.173  1.00114.87           C  
ANISOU 2337  CD2 TYR A 343    12349  22825   8471  -3343   1862  -2901       C  
ATOM   2338  CE1 TYR A 343      18.308  -9.334 -68.387  1.00123.55           C  
ANISOU 2338  CE1 TYR A 343    13429  24567   8949  -4151   2190  -3258       C  
ATOM   2339  CE2 TYR A 343      18.144 -10.523 -66.312  1.00118.35           C  
ANISOU 2339  CE2 TYR A 343    12319  23852   8794  -3493   1907  -3229       C  
ATOM   2340  CZ  TYR A 343      18.881 -10.148 -67.424  1.00129.15           C  
ANISOU 2340  CZ  TYR A 343    13653  25566   9853  -3893   2078  -3420       C  
ATOM   2341  OH  TYR A 343      20.173 -10.595 -67.581  1.00131.85           O  
ANISOU 2341  OH  TYR A 343    13481  26553  10062  -4030   2124  -3787       O  
ATOM   2342  N   LYS A 344      16.791  -6.312 -66.050  1.00112.84           N  
ANISOU 2342  N   LYS A 344    13437  22018   7417  -4520   2237  -2608       N  
ATOM   2343  CA  LYS A 344      17.908  -5.763 -65.306  1.00114.36           C  
ANISOU 2343  CA  LYS A 344    13515  22540   7397  -4930   2355  -2756       C  
ATOM   2344  C   LYS A 344      17.430  -4.565 -64.485  1.00117.57           C  
ANISOU 2344  C   LYS A 344    14462  22518   7692  -5088   2361  -2550       C  
ATOM   2345  O   LYS A 344      17.796  -4.440 -63.319  1.00117.11           O  
ANISOU 2345  O   LYS A 344    14270  22545   7681  -5104   2354  -2575       O  
ATOM   2346  CB  LYS A 344      19.045  -5.370 -66.262  1.00120.57           C  
ANISOU 2346  CB  LYS A 344    14237  23784   7790  -5509   2548  -2987       C  
ATOM   2347  N   PHE A 345      16.556  -3.722 -65.073  1.00113.65           N  
ANISOU 2347  N   PHE A 345    14586  21538   7058  -5151   2346  -2352       N  
ATOM   2348  CA  PHE A 345      16.023  -2.544 -64.397  1.00113.67           C  
ANISOU 2348  CA  PHE A 345    15165  21091   6933  -5256   2316  -2172       C  
ATOM   2349  C   PHE A 345      14.994  -2.931 -63.327  1.00114.40           C  
ANISOU 2349  C   PHE A 345    15190  20887   7390  -4696   2153  -2023       C  
ATOM   2350  O   PHE A 345      14.868  -2.193 -62.349  1.00114.99           O  
ANISOU 2350  O   PHE A 345    15511  20768   7411  -4753   2135  -1947       O  
ATOM   2351  CB  PHE A 345      15.394  -1.577 -65.400  1.00117.05           C  
ANISOU 2351  CB  PHE A 345    16296  21088   7091  -5443   2304  -2034       C  
ATOM   2352  CG  PHE A 345      14.811  -0.318 -64.796  1.00119.16           C  
ANISOU 2352  CG  PHE A 345    17226  20853   7195  -5516   2230  -1869       C  
ATOM   2353  CD1 PHE A 345      15.636   0.726 -64.390  1.00124.71           C  
ANISOU 2353  CD1 PHE A 345    18237  21600   7546  -6072   2330  -1907       C  
ATOM   2354  CD2 PHE A 345      13.434  -0.138 -64.719  1.00119.14           C  
ANISOU 2354  CD2 PHE A 345    17569  20342   7357  -5044   2052  -1695       C  
ATOM   2355  CE1 PHE A 345      15.095   1.908 -63.876  1.00126.36           C  
ANISOU 2355  CE1 PHE A 345    19110  21315   7585  -6126   2234  -1764       C  
ATOM   2356  CE2 PHE A 345      12.893   1.047 -64.209  1.00122.81           C  
ANISOU 2356  CE2 PHE A 345    18663  20348   7650  -5074   1957  -1578       C  
ATOM   2357  CZ  PHE A 345      13.727   2.060 -63.789  1.00123.63           C  
ANISOU 2357  CZ  PHE A 345    19094  20465   7415  -5606   2040  -1608       C  
ATOM   2358  N   ARG A 346      14.260  -4.064 -63.494  1.00107.46           N  
ANISOU 2358  N   ARG A 346    13992  19981   6857  -4183   2036  -1985       N  
ATOM   2359  CA  ARG A 346      13.293  -4.510 -62.473  1.00104.22           C  
ANISOU 2359  CA  ARG A 346    13483  19347   6768  -3699   1892  -1858       C  
ATOM   2360  C   ARG A 346      14.008  -4.914 -61.180  1.00106.42           C  
ANISOU 2360  C   ARG A 346    13361  19910   7162  -3698   1896  -1941       C  
ATOM   2361  O   ARG A 346      13.609  -4.494 -60.083  1.00104.16           O  
ANISOU 2361  O   ARG A 346    13213  19437   6928  -3606   1852  -1847       O  
ATOM   2362  CB  ARG A 346      12.426  -5.684 -62.954  1.00102.84           C  
ANISOU 2362  CB  ARG A 346    13051  19117   6906  -3219   1769  -1810       C  
ATOM   2363  CG  ARG A 346      11.523  -5.420 -64.136  1.00117.41           C  
ANISOU 2363  CG  ARG A 346    15258  20656   8697  -3113   1729  -1717       C  
ATOM   2364  CD  ARG A 346      10.499  -6.536 -64.260  1.00128.70           C  
ANISOU 2364  CD  ARG A 346    16437  21998  10464  -2605   1588  -1648       C  
ATOM   2365  NE  ARG A 346      11.098  -7.869 -64.378  1.00135.63           N  
ANISOU 2365  NE  ARG A 346    16761  23237  11535  -2485   1565  -1768       N  
ATOM   2366  CZ  ARG A 346      11.340  -8.483 -65.530  1.00144.38           C  
ANISOU 2366  CZ  ARG A 346    17712  24500  12646  -2475   1573  -1855       C  
ATOM   2367  NH1 ARG A 346      11.029  -7.898 -66.680  1.00131.85           N  
ANISOU 2367  NH1 ARG A 346    16477  22741  10878  -2599   1616  -1821       N  
ATOM   2368  NH2 ARG A 346      11.881  -9.693 -65.543  1.00125.92           N  
ANISOU 2368  NH2 ARG A 346    14886  22477  10481  -2323   1517  -1983       N  
ATOM   2369  N   LEU A 347      15.069  -5.747 -61.327  1.00103.00           N  
ANISOU 2369  N   LEU A 347    12428  19947   6761  -3780   1935  -2139       N  
ATOM   2370  CA  LEU A 347      15.911  -6.239 -60.238  1.00102.09           C  
ANISOU 2370  CA  LEU A 347    11891  20162   6735  -3774   1918  -2267       C  
ATOM   2371  C   LEU A 347      16.576  -5.066 -59.526  1.00106.52           C  
ANISOU 2371  C   LEU A 347    12683  20759   7030  -4204   2035  -2293       C  
ATOM   2372  O   LEU A 347      16.687  -5.075 -58.301  1.00104.39           O  
ANISOU 2372  O   LEU A 347    12306  20504   6853  -4126   1991  -2277       O  
ATOM   2373  CB  LEU A 347      16.965  -7.216 -60.802  1.00103.02           C  
ANISOU 2373  CB  LEU A 347    11482  20793   6868  -3796   1926  -2524       C  
ATOM   2374  CG  LEU A 347      17.927  -7.877 -59.807  1.00107.82           C  
ANISOU 2374  CG  LEU A 347    11609  21793   7565  -3734   1867  -2712       C  
ATOM   2375  CD1 LEU A 347      17.184  -8.717 -58.772  1.00105.14           C  
ANISOU 2375  CD1 LEU A 347    11150  21239   7557  -3260   1670  -2576       C  
ATOM   2376  CD2 LEU A 347      18.925  -8.741 -60.532  1.00111.72           C  
ANISOU 2376  CD2 LEU A 347    11620  22796   8032  -3734   1860  -3005       C  
ATOM   2377  N   ALA A 348      16.961  -4.034 -60.315  1.00105.33           N  
ANISOU 2377  N   ALA A 348    12897  20593   6533  -4673   2175  -2320       N  
ATOM   2378  CA  ALA A 348      17.589  -2.798 -59.867  1.00107.26           C  
ANISOU 2378  CA  ALA A 348    13463  20837   6454  -5170   2291  -2339       C  
ATOM   2379  C   ALA A 348      16.672  -2.024 -58.930  1.00109.43           C  
ANISOU 2379  C   ALA A 348    14178  20629   6772  -5016   2210  -2130       C  
ATOM   2380  O   ALA A 348      17.097  -1.735 -57.825  1.00109.43           O  
ANISOU 2380  O   ALA A 348    14111  20711   6756  -5113   2222  -2157       O  
ATOM   2381  CB  ALA A 348      17.962  -1.935 -61.059  1.00110.98           C  
ANISOU 2381  CB  ALA A 348    14324  21307   6538  -5680   2424  -2373       C  
ATOM   2382  N   LYS A 349      15.399  -1.768 -59.310  1.00104.55           N  
ANISOU 2382  N   LYS A 349    13959  19539   6227  -4729   2111  -1946       N  
ATOM   2383  CA  LYS A 349      14.474  -1.025 -58.433  1.00103.67           C  
ANISOU 2383  CA  LYS A 349    14247  18998   6144  -4538   2017  -1786       C  
ATOM   2384  C   LYS A 349      13.951  -1.924 -57.248  1.00103.90           C  
ANISOU 2384  C   LYS A 349    13869  19069   6539  -4070   1912  -1744       C  
ATOM   2385  O   LYS A 349      13.137  -1.459 -56.439  1.00101.92           O  
ANISOU 2385  O   LYS A 349    13857  18528   6342  -3864   1834  -1635       O  
ATOM   2386  CB  LYS A 349      13.277  -0.439 -59.226  1.00105.92           C  
ANISOU 2386  CB  LYS A 349    15080  18797   6366  -4355   1922  -1645       C  
ATOM   2387  CG  LYS A 349      12.305  -1.437 -59.864  1.00106.01           C  
ANISOU 2387  CG  LYS A 349    14876  18738   6663  -3877   1824  -1592       C  
ATOM   2388  CD  LYS A 349      11.149  -0.673 -60.506  1.00111.42           C  
ANISOU 2388  CD  LYS A 349    16146  18942   7247  -3702   1714  -1477       C  
ATOM   2389  CE  LYS A 349      10.089  -1.552 -61.119  1.00117.36           C  
ANISOU 2389  CE  LYS A 349    16723  19606   8263  -3233   1611  -1426       C  
ATOM   2390  NZ  LYS A 349       8.986  -0.743 -61.709  1.00123.35           N  
ANISOU 2390  NZ  LYS A 349    18055  19912   8902  -3045   1485  -1345       N  
ATOM   2391  N   SER A 350      14.452  -3.180 -57.145  1.00 99.27           N  
ANISOU 2391  N   SER A 350    12696  18850   6171  -3922   1901  -1845       N  
ATOM   2392  CA  SER A 350      14.087  -4.130 -56.096  1.00 96.87           C  
ANISOU 2392  CA  SER A 350    12024  18606   6175  -3540   1791  -1810       C  
ATOM   2393  C   SER A 350      15.291  -4.459 -55.189  1.00103.35           C  
ANISOU 2393  C   SER A 350    12462  19812   6993  -3705   1821  -1957       C  
ATOM   2394  O   SER A 350      15.087  -4.750 -54.012  1.00101.74           O  
ANISOU 2394  O   SER A 350    12126  19590   6940  -3518   1745  -1910       O  
ATOM   2395  CB  SER A 350      13.531  -5.412 -56.704  1.00 97.69           C  
ANISOU 2395  CB  SER A 350    11825  18749   6544  -3165   1690  -1794       C  
ATOM   2396  OG  SER A 350      13.127  -6.347 -55.716  1.00 99.89           O  
ANISOU 2396  OG  SER A 350    11809  19054   7089  -2832   1567  -1745       O  
ATOM   2397  N   THR A 351      16.535  -4.414 -55.714  1.00103.09           N  
ANISOU 2397  N   THR A 351    12243  20150   6775  -4057   1926  -2150       N  
ATOM   2398  CA  THR A 351      17.706  -4.716 -54.875  1.00103.91           C  
ANISOU 2398  CA  THR A 351    11959  20661   6863  -4196   1940  -2329       C  
ATOM   2399  C   THR A 351      18.212  -3.407 -54.189  1.00108.17           C  
ANISOU 2399  C   THR A 351    12804  21166   7129  -4620   2053  -2333       C  
ATOM   2400  O   THR A 351      18.628  -3.481 -53.034  1.00107.11           O  
ANISOU 2400  O   THR A 351    12492  21160   7046  -4605   2021  -2375       O  
ATOM   2401  CB  THR A 351      18.831  -5.420 -55.668  1.00114.59           C  
ANISOU 2401  CB  THR A 351    12868  22517   8156  -4323   1979  -2591       C  
ATOM   2402  OG1 THR A 351      19.870  -5.818 -54.769  1.00116.52           O  
ANISOU 2402  OG1 THR A 351    12705  23154   8413  -4360   1947  -2784       O  
ATOM   2403  CG2 THR A 351      19.391  -4.590 -56.795  1.00116.04           C  
ANISOU 2403  CG2 THR A 351    13257  22830   8002  -4809   2157  -2686       C  
ATOM   2404  N   LEU A 352      18.120  -2.218 -54.868  1.00105.75           N  
ANISOU 2404  N   LEU A 352    13001  20648   6529  -4985   2163  -2277       N  
ATOM   2405  CA  LEU A 352      18.524  -0.925 -54.281  1.00107.16           C  
ANISOU 2405  CA  LEU A 352    13562  20732   6424  -5404   2248  -2264       C  
ATOM   2406  C   LEU A 352      17.422  -0.414 -53.320  1.00109.09           C  
ANISOU 2406  C   LEU A 352    14163  20509   6777  -5121   2145  -2061       C  
ATOM   2407  O   LEU A 352      17.515   0.704 -52.803  1.00109.76           O  
ANISOU 2407  O   LEU A 352    14650  20409   6644  -5386   2178  -2020       O  
ATOM   2408  CB  LEU A 352      18.863   0.161 -55.353  1.00110.03           C  
ANISOU 2408  CB  LEU A 352    14398  21017   6390  -5935   2376  -2280       C  
ATOM   2409  CG  LEU A 352      17.844   0.598 -56.447  1.00114.20           C  
ANISOU 2409  CG  LEU A 352    15445  21099   6846  -5853   2334  -2121       C  
ATOM   2410  CD1 LEU A 352      16.543   1.171 -55.878  1.00112.67           C  
ANISOU 2410  CD1 LEU A 352    15717  20346   6748  -5507   2196  -1913       C  
ATOM   2411  CD2 LEU A 352      18.465   1.620 -57.381  1.00119.08           C  
ANISOU 2411  CD2 LEU A 352    16505  21719   7022  -6475   2460  -2168       C  
ATOM   2412  N   THR A 353      16.382  -1.236 -53.111  1.00103.15           N  
ANISOU 2412  N   THR A 353    13263  19588   6341  -4597   2017  -1949       N  
ATOM   2413  CA  THR A 353      15.245  -0.964 -52.233  1.00101.47           C  
ANISOU 2413  CA  THR A 353    13281  19015   6259  -4270   1915  -1789       C  
ATOM   2414  C   THR A 353      15.408  -1.852 -50.975  1.00104.37           C  
ANISOU 2414  C   THR A 353    13196  19593   6866  -4037   1848  -1810       C  
ATOM   2415  O   THR A 353      14.663  -1.708 -50.011  1.00102.38           O  
ANISOU 2415  O   THR A 353    13042  19147   6711  -3815   1780  -1709       O  
ATOM   2416  CB  THR A 353      13.924  -1.223 -53.025  1.00105.60           C  
ANISOU 2416  CB  THR A 353    13977  19227   6917  -3900   1827  -1666       C  
ATOM   2417  OG1 THR A 353      13.972  -0.551 -54.287  1.00108.53           O  
ANISOU 2417  OG1 THR A 353    14724  19456   7056  -4140   1879  -1670       O  
ATOM   2418  CG2 THR A 353      12.676  -0.792 -52.274  1.00101.36           C  
ANISOU 2418  CG2 THR A 353    13711  18343   6459  -3579   1727  -1540       C  
ATOM   2419  N   LEU A 354      16.415  -2.741 -50.984  1.00101.86           N  
ANISOU 2419  N   LEU A 354    12399  19685   6618  -4096   1858  -1960       N  
ATOM   2420  CA  LEU A 354      16.667  -3.701 -49.911  1.00100.39           C  
ANISOU 2420  CA  LEU A 354    11797  19701   6643  -3870   1759  -1997       C  
ATOM   2421  C   LEU A 354      18.066  -3.553 -49.323  1.00106.16           C  
ANISOU 2421  C   LEU A 354    12289  20809   7237  -4177   1814  -2185       C  
ATOM   2422  O   LEU A 354      18.368  -4.155 -48.299  1.00104.22           O  
ANISOU 2422  O   LEU A 354    11765  20713   7119  -4029   1723  -2224       O  
ATOM   2423  CB  LEU A 354      16.508  -5.113 -50.495  1.00 99.13           C  
ANISOU 2423  CB  LEU A 354    11268  19677   6721  -3549   1650  -2028       C  
ATOM   2424  CG  LEU A 354      16.314  -6.247 -49.516  1.00101.81           C  
ANISOU 2424  CG  LEU A 354    11299  20076   7307  -3214   1485  -2000       C  
ATOM   2425  CD1 LEU A 354      14.913  -6.223 -48.974  1.00 99.55           C  
ANISOU 2425  CD1 LEU A 354    11234  19439   7152  -2953   1423  -1786       C  
ATOM   2426  CD2 LEU A 354      16.517  -7.566 -50.196  1.00104.66           C  
ANISOU 2426  CD2 LEU A 354    11313  20620   7833  -2982   1369  -2087       C  
ATOM   2427  N   ILE A 355      18.940  -2.811 -49.998  1.00106.88           N  
ANISOU 2427  N   ILE A 355    12474  21080   7054  -4615   1955  -2316       N  
ATOM   2428  CA  ILE A 355      20.302  -2.628 -49.527  1.00109.57           C  
ANISOU 2428  CA  ILE A 355    12562  21839   7230  -4950   2022  -2529       C  
ATOM   2429  C   ILE A 355      20.317  -1.446 -48.522  1.00115.23           C  
ANISOU 2429  C   ILE A 355    13636  22367   7779  -5198   2076  -2452       C  
ATOM   2430  O   ILE A 355      21.025  -1.567 -47.520  1.00114.99           O  
ANISOU 2430  O   ILE A 355    13362  22575   7753  -5250   2054  -2556       O  
ATOM   2431  CB  ILE A 355      21.315  -2.440 -50.702  1.00115.65           C  
ANISOU 2431  CB  ILE A 355    13211  22979   7752  -5359   2161  -2742       C  
ATOM   2432  CG1 ILE A 355      22.762  -2.775 -50.319  1.00118.89           C  
ANISOU 2432  CG1 ILE A 355    13128  23979   8067  -5566   2188  -3043       C  
ATOM   2433  CG2 ILE A 355      21.183  -1.140 -51.469  1.00117.79           C  
ANISOU 2433  CG2 ILE A 355    14027  23022   7704  -5803   2307  -2666       C  
ATOM   2434  CD1 ILE A 355      22.984  -4.211 -50.027  1.00127.29           C  
ANISOU 2434  CD1 ILE A 355    13656  25300   9407  -5114   2012  -3169       C  
ATOM   2435  N   PRO A 356      19.507  -0.353 -48.684  1.00113.23           N  
ANISOU 2435  N   PRO A 356    13960  21675   7389  -5300   2115  -2279       N  
ATOM   2436  CA  PRO A 356      19.538   0.720 -47.679  1.00114.44           C  
ANISOU 2436  CA  PRO A 356    14449  21648   7384  -5499   2138  -2224       C  
ATOM   2437  C   PRO A 356      18.479   0.504 -46.578  1.00116.40           C  
ANISOU 2437  C   PRO A 356    14749  21611   7867  -5058   2013  -2064       C  
ATOM   2438  O   PRO A 356      18.831   0.547 -45.402  1.00116.14           O  
ANISOU 2438  O   PRO A 356    14594  21679   7856  -5069   1990  -2091       O  
ATOM   2439  CB  PRO A 356      19.250   1.986 -48.503  1.00118.06           C  
ANISOU 2439  CB  PRO A 356    15535  21780   7544  -5825   2209  -2149       C  
ATOM   2440  CG  PRO A 356      18.684   1.496 -49.826  1.00121.54           C  
ANISOU 2440  CG  PRO A 356    15991  22130   8058  -5656   2196  -2107       C  
ATOM   2441  CD  PRO A 356      18.587   0.002 -49.783  1.00114.57           C  
ANISOU 2441  CD  PRO A 356    14522  21494   7514  -5238   2120  -2149       C  
ATOM   2442  N   LEU A 357      17.196   0.258 -46.959  1.00111.32           N  
ANISOU 2442  N   LEU A 357    14266  20647   7383  -4685   1935  -1913       N  
ATOM   2443  CA  LEU A 357      16.072   0.010 -46.047  1.00109.33           C  
ANISOU 2443  CA  LEU A 357    14042  20167   7332  -4277   1827  -1778       C  
ATOM   2444  C   LEU A 357      16.458  -1.022 -44.984  1.00112.70           C  
ANISOU 2444  C   LEU A 357    13996  20865   7960  -4109   1759  -1817       C  
ATOM   2445  O   LEU A 357      16.453  -0.690 -43.800  1.00112.37           O  
ANISOU 2445  O   LEU A 357    13999  20794   7904  -4110   1739  -1795       O  
ATOM   2446  CB  LEU A 357      14.841  -0.478 -46.847  1.00107.78           C  
ANISOU 2446  CB  LEU A 357    13906  19746   7298  -3914   1759  -1670       C  
ATOM   2447  CG  LEU A 357      13.514  -0.676 -46.086  1.00110.87           C  
ANISOU 2447  CG  LEU A 357    14344  19921   7860  -3511   1660  -1548       C  
ATOM   2448  CD1 LEU A 357      12.940   0.664 -45.628  1.00112.59           C  
ANISOU 2448  CD1 LEU A 357    15057  19829   7892  -3541   1656  -1509       C  
ATOM   2449  CD2 LEU A 357      12.469  -1.362 -46.972  1.00111.05           C  
ANISOU 2449  CD2 LEU A 357    14319  19827   8050  -3187   1598  -1477       C  
ATOM   2450  N   LEU A 358      16.872  -2.236 -45.418  1.00108.83           N  
ANISOU 2450  N   LEU A 358    13079  20639   7632  -3983   1710  -1892       N  
ATOM   2451  CA  LEU A 358      17.276  -3.339 -44.541  1.00108.12           C  
ANISOU 2451  CA  LEU A 358    12570  20787   7722  -3798   1597  -1942       C  
ATOM   2452  C   LEU A 358      18.630  -3.027 -43.884  1.00114.78           C  
ANISOU 2452  C   LEU A 358    13248  21943   8419  -4098   1638  -2113       C  
ATOM   2453  O   LEU A 358      18.818  -3.339 -42.708  1.00114.23           O  
ANISOU 2453  O   LEU A 358    13033  21948   8419  -4005   1557  -2116       O  
ATOM   2454  CB  LEU A 358      17.338  -4.657 -45.356  1.00107.23           C  
ANISOU 2454  CB  LEU A 358    12119  20834   7792  -3568   1503  -1993       C  
ATOM   2455  CG  LEU A 358      17.483  -6.019 -44.622  1.00110.67           C  
ANISOU 2455  CG  LEU A 358    12192  21420   8438  -3278   1318  -2016       C  
ATOM   2456  CD1 LEU A 358      16.903  -7.152 -45.444  1.00109.08           C  
ANISOU 2456  CD1 LEU A 358    11850  21170   8426  -2981   1207  -1972       C  
ATOM   2457  CD2 LEU A 358      18.916  -6.317 -44.200  1.00114.35           C  
ANISOU 2457  CD2 LEU A 358    12332  22275   8841  -3409   1276  -2240       C  
ATOM   2458  N   GLY A 359      19.530  -2.394 -44.633  1.00114.22           N  
ANISOU 2458  N   GLY A 359    13211  22059   8128  -4473   1765  -2257       N  
ATOM   2459  CA  GLY A 359      20.868  -2.041 -44.170  1.00116.87           C  
ANISOU 2459  CA  GLY A 359    13369  22752   8286  -4815   1825  -2456       C  
ATOM   2460  C   GLY A 359      20.954  -1.002 -43.066  1.00122.78           C  
ANISOU 2460  C   GLY A 359    14389  23374   8889  -5024   1870  -2408       C  
ATOM   2461  O   GLY A 359      21.581  -1.255 -42.035  1.00122.31           O  
ANISOU 2461  O   GLY A 359    14091  23526   8856  -5019   1815  -2496       O  
ATOM   2462  N   VAL A 360      20.337   0.176 -43.277  1.00121.28           N  
ANISOU 2462  N   VAL A 360    14717  22831   8534  -5195   1952  -2279       N  
ATOM   2463  CA  VAL A 360      20.358   1.312 -42.348  1.00123.17           C  
ANISOU 2463  CA  VAL A 360    15303  22898   8600  -5408   1989  -2235       C  
ATOM   2464  C   VAL A 360      19.578   0.991 -41.049  1.00130.50           C  
ANISOU 2464  C   VAL A 360    16202  23657   9725  -5039   1876  -2111       C  
ATOM   2465  O   VAL A 360      20.103   1.266 -39.968  1.00130.28           O  
ANISOU 2465  O   VAL A 360    16124  23737   9640  -5154   1870  -2160       O  
ATOM   2466  CB  VAL A 360      19.784   2.596 -43.009  1.00127.35           C  
ANISOU 2466  CB  VAL A 360    16454  23036   8897  -5619   2055  -2133       C  
ATOM   2467  CG1 VAL A 360      19.663   3.744 -42.009  1.00127.98           C  
ANISOU 2467  CG1 VAL A 360    16938  22880   8809  -5767   2054  -2081       C  
ATOM   2468  CG2 VAL A 360      20.626   3.020 -44.205  1.00129.55           C  
ANISOU 2468  CG2 VAL A 360    16818  23487   8919  -6080   2178  -2251       C  
ATOM   2469  N   HIS A 361      18.334   0.437 -41.145  1.00129.91           N  
ANISOU 2469  N   HIS A 361    16160  23341   9859  -4628   1792  -1961       N  
ATOM   2470  CA  HIS A 361      17.502   0.208 -39.949  1.00130.55           C  
ANISOU 2470  CA  HIS A 361    16244  23278  10083  -4328   1702  -1847       C  
ATOM   2471  C   HIS A 361      18.095  -0.919 -39.061  1.00136.08           C  
ANISOU 2471  C   HIS A 361    16490  24271  10943  -4202   1605  -1905       C  
ATOM   2472  O   HIS A 361      17.787  -0.951 -37.867  1.00136.18           O  
ANISOU 2472  O   HIS A 361    16507  24236  11001  -4089   1549  -1846       O  
ATOM   2473  CB  HIS A 361      16.021  -0.117 -40.292  1.00130.33           C  
ANISOU 2473  CB  HIS A 361    16336  22976  10208  -3956   1644  -1699       C  
ATOM   2474  CG  HIS A 361      15.670  -1.575 -40.449  1.00132.65           C  
ANISOU 2474  CG  HIS A 361    16259  23388  10755  -3654   1546  -1660       C  
ATOM   2475  ND1 HIS A 361      15.309  -2.350 -39.354  1.00133.70           N  
ANISOU 2475  ND1 HIS A 361    16196  23570  11033  -3443   1446  -1600       N  
ATOM   2476  CD2 HIS A 361      15.502  -2.312 -41.572  1.00133.90           C  
ANISOU 2476  CD2 HIS A 361    16278  23575  11021  -3535   1524  -1660       C  
ATOM   2477  CE1 HIS A 361      15.007  -3.542 -39.842  1.00131.98           C  
ANISOU 2477  CE1 HIS A 361    15740  23410  10997  -3226   1358  -1566       C  
ATOM   2478  NE2 HIS A 361      15.105  -3.567 -41.171  1.00132.27           N  
ANISOU 2478  NE2 HIS A 361    15790  23438  11028  -3258   1401  -1604       N  
ATOM   2479  N   GLU A 362      18.932  -1.820 -39.618  1.00133.28           N  
ANISOU 2479  N   GLU A 362    15769  24215  10657  -4211   1568  -2033       N  
ATOM   2480  CA  GLU A 362      19.525  -2.869 -38.791  1.00133.03           C  
ANISOU 2480  CA  GLU A 362    15357  24434  10753  -4062   1431  -2108       C  
ATOM   2481  C   GLU A 362      20.989  -2.476 -38.471  1.00138.56           C  
ANISOU 2481  C   GLU A 362    15883  25479  11283  -4383   1476  -2325       C  
ATOM   2482  O   GLU A 362      21.752  -3.266 -37.907  1.00137.50           O  
ANISOU 2482  O   GLU A 362    15411  25617  11213  -4291   1352  -2455       O  
ATOM   2483  CB  GLU A 362      19.412  -4.236 -39.475  1.00133.55           C  
ANISOU 2483  CB  GLU A 362    15131  24596  11017  -3778   1303  -2126       C  
ATOM   2484  CG  GLU A 362      19.116  -5.392 -38.522  1.00144.00           C  
ANISOU 2484  CG  GLU A 362    16278  25913  12522  -3470   1102  -2060       C  
ATOM   2485  CD  GLU A 362      17.760  -5.437 -37.821  1.00161.37           C  
ANISOU 2485  CD  GLU A 362    18695  27810  14807  -3286   1072  -1833       C  
ATOM   2486  OE1 GLU A 362      17.279  -6.564 -37.566  1.00156.47           O  
ANISOU 2486  OE1 GLU A 362    17962  27150  14340  -3038    913  -1753       O  
ATOM   2487  OE2 GLU A 362      17.156  -4.368 -37.569  1.00151.23           O  
ANISOU 2487  OE2 GLU A 362    17701  26337  13423  -3391   1195  -1749       O  
ATOM   2488  N   VAL A 363      21.336  -1.210 -38.798  1.00137.98           N  
ANISOU 2488  N   VAL A 363    16078  25378  10972  -4765   1639  -2367       N  
ATOM   2489  CA  VAL A 363      22.596  -0.537 -38.480  1.00141.14           C  
ANISOU 2489  CA  VAL A 363    16406  26071  11150  -5164   1720  -2557       C  
ATOM   2490  C   VAL A 363      22.332   0.447 -37.336  1.00147.01           C  
ANISOU 2490  C   VAL A 363    17473  26596  11787  -5281   1749  -2460       C  
ATOM   2491  O   VAL A 363      23.227   0.719 -36.536  1.00148.57           O  
ANISOU 2491  O   VAL A 363    17552  27019  11877  -5483   1754  -2585       O  
ATOM   2492  CB  VAL A 363      23.236   0.158 -39.699  1.00147.29           C  
ANISOU 2492  CB  VAL A 363    17276  26994  11692  -5580   1880  -2682       C  
ATOM   2493  N   VAL A 364      21.082   0.962 -37.252  1.00142.91           N  
ANISOU 2493  N   VAL A 364    17350  25653  11297  -5128   1757  -2254       N  
ATOM   2494  CA  VAL A 364      20.585   1.820 -36.165  1.00143.15           C  
ANISOU 2494  CA  VAL A 364    17702  25437  11251  -5139   1758  -2155       C  
ATOM   2495  C   VAL A 364      20.465   0.939 -34.904  1.00147.79           C  
ANISOU 2495  C   VAL A 364    18010  26121  12022  -4856   1630  -2124       C  
ATOM   2496  O   VAL A 364      20.651   1.409 -33.781  1.00147.39           O  
ANISOU 2496  O   VAL A 364    18039  26065  11899  -4933   1621  -2127       O  
ATOM   2497  CB  VAL A 364      19.240   2.505 -36.575  1.00145.80           C  
ANISOU 2497  CB  VAL A 364    18495  25336  11567  -4989   1774  -1991       C  
ATOM   2498  CG1 VAL A 364      18.516   3.136 -35.388  1.00145.16           C  
ANISOU 2498  CG1 VAL A 364    18674  25025  11458  -4864   1737  -1903       C  
ATOM   2499  CG2 VAL A 364      19.458   3.531 -37.683  1.00147.44           C  
ANISOU 2499  CG2 VAL A 364    19078  25407  11535  -5320   1874  -2022       C  
ATOM   2500  N   PHE A 365      20.232  -0.367 -35.142  1.00145.42           N  
ANISOU 2500  N   PHE A 365    17396  25916  11941  -4555   1521  -2102       N  
ATOM   2501  CA  PHE A 365      20.083  -1.470 -34.200  1.00145.39           C  
ANISOU 2501  CA  PHE A 365    17138  25989  12115  -4272   1363  -2062       C  
ATOM   2502  C   PHE A 365      21.219  -1.529 -33.167  1.00151.90           C  
ANISOU 2502  C   PHE A 365    17760  27083  12872  -4404   1303  -2204       C  
ATOM   2503  O   PHE A 365      20.935  -1.568 -31.970  1.00151.01           O  
ANISOU 2503  O   PHE A 365    17697  26901  12780  -4314   1237  -2129       O  
ATOM   2504  CB  PHE A 365      20.054  -2.791 -34.997  1.00146.87           C  
ANISOU 2504  CB  PHE A 365    17036  26283  12484  -4031   1251  -2081       C  
ATOM   2505  CG  PHE A 365      20.022  -4.073 -34.199  1.00148.49           C  
ANISOU 2505  CG  PHE A 365    17006  26561  12851  -3755   1045  -2054       C  
ATOM   2506  CD1 PHE A 365      18.813  -4.653 -33.830  1.00150.57           C  
ANISOU 2506  CD1 PHE A 365    17368  26599  13243  -3508    968  -1861       C  
ATOM   2507  CD2 PHE A 365      21.201  -4.740 -33.878  1.00152.52           C  
ANISOU 2507  CD2 PHE A 365    17206  27377  13367  -3745    911  -2238       C  
ATOM   2508  CE1 PHE A 365      18.783  -5.853 -33.108  1.00151.48           C  
ANISOU 2508  CE1 PHE A 365    17329  26753  13471  -3299    760  -1822       C  
ATOM   2509  CE2 PHE A 365      21.172  -5.936 -33.152  1.00155.39           C  
ANISOU 2509  CE2 PHE A 365    17422  27762  13857  -3479    678  -2211       C  
ATOM   2510  CZ  PHE A 365      19.962  -6.487 -32.775  1.00151.99           C  
ANISOU 2510  CZ  PHE A 365    17145  27067  13538  -3277    603  -1989       C  
ATOM   2511  N   ALA A 366      22.485  -1.585 -33.625  1.00151.75           N  
ANISOU 2511  N   ALA A 366    17492  27400  12768  -4606   1319  -2422       N  
ATOM   2512  CA  ALA A 366      23.655  -1.742 -32.754  1.00154.21           C  
ANISOU 2512  CA  ALA A 366    17546  28032  13015  -4705   1241  -2605       C  
ATOM   2513  C   ALA A 366      24.048  -0.412 -32.025  1.00161.10           C  
ANISOU 2513  C   ALA A 366    18653  28889  13669  -5058   1368  -2634       C  
ATOM   2514  O   ALA A 366      24.174  -0.420 -30.792  1.00160.52           O  
ANISOU 2514  O   ALA A 366    18568  28826  13596  -5011   1290  -2620       O  
ATOM   2515  CB  ALA A 366      24.838  -2.250 -33.564  1.00156.75           C  
ANISOU 2515  CB  ALA A 366    17484  28773  13301  -4789   1216  -2873       C  
ATOM   2516  N   PHE A 367      24.271   0.704 -32.775  1.00159.87           N  
ANISOU 2516  N   PHE A 367    18729  28703  13310  -5426   1548  -2674       N  
ATOM   2517  CA  PHE A 367      24.675   1.983 -32.173  1.00161.43           C  
ANISOU 2517  CA  PHE A 367    19195  28867  13274  -5794   1654  -2706       C  
ATOM   2518  C   PHE A 367      24.255   3.201 -33.050  1.00165.77           C  
ANISOU 2518  C   PHE A 367    20218  29139  13629  -6086   1811  -2628       C  
ATOM   2519  O   PHE A 367      24.876   3.501 -34.077  1.00167.10           O  
ANISOU 2519  O   PHE A 367    20375  29473  13644  -6400   1912  -2746       O  
ATOM   2520  CB  PHE A 367      26.198   2.017 -31.936  1.00165.86           C  
ANISOU 2520  CB  PHE A 367    19425  29907  13687  -6097   1665  -2980       C  
ATOM   2521  N   VAL A 368      23.194   3.893 -32.601  1.00160.48           N  
ANISOU 2521  N   VAL A 368    19975  28053  12947  -5973   1812  -2443       N  
ATOM   2522  CA  VAL A 368      22.613   5.135 -33.140  1.00160.45           C  
ANISOU 2522  CA  VAL A 368    20527  27685  12752  -6161   1896  -2353       C  
ATOM   2523  C   VAL A 368      22.059   5.897 -31.953  1.00162.71           C  
ANISOU 2523  C   VAL A 368    21132  27709  12980  -6090   1859  -2266       C  
ATOM   2524  O   VAL A 368      22.219   7.113 -31.825  1.00163.72           O  
ANISOU 2524  O   VAL A 368    21681  27660  12864  -6388   1905  -2278       O  
ATOM   2525  CB  VAL A 368      21.563   4.878 -34.239  1.00162.68           C  
ANISOU 2525  CB  VAL A 368    20958  27712  13142  -5912   1890  -2230       C  
ATOM   2526  N   THR A 369      21.432   5.125 -31.060  1.00156.76           N  
ANISOU 2526  N   THR A 369    20173  26946  12441  -5702   1763  -2187       N  
ATOM   2527  CA  THR A 369      20.951   5.480 -29.735  1.00156.13           C  
ANISOU 2527  CA  THR A 369    20233  26732  12357  -5567   1713  -2125       C  
ATOM   2528  C   THR A 369      21.698   4.471 -28.834  1.00159.70           C  
ANISOU 2528  C   THR A 369    20215  27527  12936  -5501   1638  -2195       C  
ATOM   2529  O   THR A 369      21.116   3.501 -28.335  1.00157.44           O  
ANISOU 2529  O   THR A 369    19720  27255  12845  -5169   1543  -2113       O  
ATOM   2530  CB  THR A 369      19.406   5.486 -29.704  1.00159.18           C  
ANISOU 2530  CB  THR A 369    20836  26800  12847  -5184   1670  -1977       C  
ATOM   2531  OG1 THR A 369      18.922   6.330 -30.755  1.00156.74           O  
ANISOU 2531  OG1 THR A 369    20935  26209  12411  -5249   1712  -1953       O  
ATOM   2532  CG2 THR A 369      18.846   5.950 -28.358  1.00157.13           C  
ANISOU 2532  CG2 THR A 369    20734  26421  12548  -5052   1628  -1939       C  
ATOM   2533  N   ASP A 370      23.044   4.655 -28.761  1.00157.97           N  
ANISOU 2533  N   ASP A 370    19828  27607  12588  -5840   1671  -2364       N  
ATOM   2534  CA  ASP A 370      24.035   3.786 -28.107  1.00157.51           C  
ANISOU 2534  CA  ASP A 370    19315  27928  12602  -5823   1584  -2498       C  
ATOM   2535  C   ASP A 370      24.132   4.017 -26.558  1.00160.74           C  
ANISOU 2535  C   ASP A 370    19759  28337  12979  -5799   1520  -2486       C  
ATOM   2536  O   ASP A 370      24.759   3.192 -25.879  1.00161.03           O  
ANISOU 2536  O   ASP A 370    19453  28634  13098  -5697   1406  -2571       O  
ATOM   2537  CB  ASP A 370      25.432   4.010 -28.745  1.00161.20           C  
ANISOU 2537  CB  ASP A 370    19578  28764  12905  -6220   1657  -2729       C  
ATOM   2538  CG  ASP A 370      25.908   5.455 -28.785  1.00166.71           C  
ANISOU 2538  CG  ASP A 370    20635  29403  13303  -6705   1791  -2786       C  
ATOM   2539  OD1 ASP A 370      26.496   5.914 -27.784  1.00168.29           O  
ANISOU 2539  OD1 ASP A 370    20842  29710  13389  -6880   1781  -2861       O  
ATOM   2540  OD2 ASP A 370      25.745   6.106 -29.845  1.00168.00           O  
ANISOU 2540  OD2 ASP A 370    21083  29419  13329  -6932   1895  -2763       O  
ATOM   2541  N   GLU A 371      23.498   5.084 -25.999  1.00155.80           N  
ANISOU 2541  N   GLU A 371    19549  27416  12231  -5860   1572  -2392       N  
ATOM   2542  CA  GLU A 371      23.532   5.349 -24.546  1.00154.91           C  
ANISOU 2542  CA  GLU A 371    19487  27296  12076  -5837   1519  -2381       C  
ATOM   2543  C   GLU A 371      22.610   4.361 -23.803  1.00154.98           C  
ANISOU 2543  C   GLU A 371    19360  27240  12287  -5426   1407  -2245       C  
ATOM   2544  O   GLU A 371      21.492   4.112 -24.254  1.00152.46           O  
ANISOU 2544  O   GLU A 371    19141  26718  12069  -5186   1411  -2117       O  
ATOM   2545  CB  GLU A 371      23.129   6.811 -24.237  1.00157.23           C  
ANISOU 2545  CB  GLU A 371    20287  27294  12161  -6014   1593  -2344       C  
ATOM   2546  CG  GLU A 371      23.293   7.199 -22.769  1.00166.17           C  
ANISOU 2546  CG  GLU A 371    21479  28441  13218  -6039   1551  -2358       C  
ATOM   2547  CD  GLU A 371      22.886   8.597 -22.333  1.00183.07           C  
ANISOU 2547  CD  GLU A 371    24124  30285  15151  -6168   1590  -2337       C  
ATOM   2548  OE1 GLU A 371      22.320   9.352 -23.156  1.00178.80           O  
ANISOU 2548  OE1 GLU A 371    23960  29462  14513  -6203   1632  -2298       O  
ATOM   2549  OE2 GLU A 371      23.109   8.924 -21.146  1.00173.62           O  
ANISOU 2549  OE2 GLU A 371    22963  29123  13882  -6209   1557  -2365       O  
ATOM   2550  N   HIS A 372      23.090   3.802 -22.669  1.00151.53           N  
ANISOU 2550  N   HIS A 372    18705  26986  11885  -5368   1300  -2280       N  
ATOM   2551  CA  HIS A 372      22.335   2.859 -21.816  1.00149.70           C  
ANISOU 2551  CA  HIS A 372    18372  26712  11793  -5053   1181  -2154       C  
ATOM   2552  C   HIS A 372      21.053   3.530 -21.255  1.00151.37           C  
ANISOU 2552  C   HIS A 372    18907  26651  11956  -4939   1240  -2021       C  
ATOM   2553  O   HIS A 372      20.010   2.878 -21.159  1.00149.93           O  
ANISOU 2553  O   HIS A 372    18704  26381  11883  -4688   1202  -1897       O  
ATOM   2554  CB  HIS A 372      23.216   2.343 -20.656  1.00151.29           C  
ANISOU 2554  CB  HIS A 372    18356  27143  11985  -5069   1046  -2235       C  
ATOM   2555  CG  HIS A 372      23.598   3.414 -19.687  1.00155.98           C  
ANISOU 2555  CG  HIS A 372    19133  27731  12400  -5286   1099  -2291       C  
ATOM   2556  ND1 HIS A 372      22.874   3.627 -18.527  1.00157.41           N  
ANISOU 2556  ND1 HIS A 372    19484  27778  12545  -5185   1080  -2188       N  
ATOM   2557  CD2 HIS A 372      24.534   4.382 -19.800  1.00159.64           C  
ANISOU 2557  CD2 HIS A 372    19665  28294  12697  -5615   1183  -2437       C  
ATOM   2558  CE1 HIS A 372      23.432   4.674 -17.942  1.00158.47           C  
ANISOU 2558  CE1 HIS A 372    19776  27926  12509  -5424   1136  -2275       C  
ATOM   2559  NE2 HIS A 372      24.431   5.167 -18.674  1.00160.22           N  
ANISOU 2559  NE2 HIS A 372    19955  28278  12643  -5700   1198  -2421       N  
ATOM   2560  N   ALA A 373      21.159   4.843 -20.897  1.00146.94           N  
ANISOU 2560  N   ALA A 373    18644  25976  11210  -5134   1324  -2070       N  
ATOM   2561  CA  ALA A 373      20.120   5.726 -20.355  1.00145.65           C  
ANISOU 2561  CA  ALA A 373    18817  25573  10950  -5041   1368  -2009       C  
ATOM   2562  C   ALA A 373      19.357   5.058 -19.193  1.00146.34           C  
ANISOU 2562  C   ALA A 373    18797  25704  11103  -4809   1299  -1920       C  
ATOM   2563  O   ALA A 373      19.710   5.273 -18.033  1.00147.02           O  
ANISOU 2563  O   ALA A 373    18893  25864  11104  -4884   1266  -1950       O  
ATOM   2564  CB  ALA A 373      19.145   6.140 -21.451  1.00145.79           C  
ANISOU 2564  CB  ALA A 373    19066  25353  10977  -4917   1429  -1960       C  
ATOM   2565  N   GLN A 374      18.315   4.260 -19.511  1.00139.47           N  
ANISOU 2565  N   GLN A 374    17834  24797  10362  -4559   1280  -1816       N  
ATOM   2566  CA  GLN A 374      17.451   3.577 -18.544  1.00137.74           C  
ANISOU 2566  CA  GLN A 374    17527  24631  10176  -4379   1228  -1725       C  
ATOM   2567  C   GLN A 374      16.705   2.426 -19.231  1.00138.01           C  
ANISOU 2567  C   GLN A 374    17387  24679  10370  -4191   1191  -1622       C  
ATOM   2568  O   GLN A 374      16.674   2.365 -20.457  1.00137.35           O  
ANISOU 2568  O   GLN A 374    17293  24527  10367  -4158   1222  -1625       O  
ATOM   2569  CB  GLN A 374      16.463   4.580 -17.897  1.00139.74           C  
ANISOU 2569  CB  GLN A 374    18037  24769  10287  -4295   1295  -1745       C  
ATOM   2570  CG  GLN A 374      15.633   5.418 -18.888  1.00152.55           C  
ANISOU 2570  CG  GLN A 374    19902  26185  11875  -4174   1367  -1778       C  
ATOM   2571  CD  GLN A 374      14.871   6.566 -18.245  1.00173.67           C  
ANISOU 2571  CD  GLN A 374    22863  28745  14380  -4076   1396  -1855       C  
ATOM   2572  OE1 GLN A 374      14.491   7.529 -18.917  1.00169.67           O  
ANISOU 2572  OE1 GLN A 374    22648  28029  13791  -4010   1417  -1920       O  
ATOM   2573  NE2 GLN A 374      14.718   6.557 -16.922  1.00166.11           N  
ANISOU 2573  NE2 GLN A 374    21862  27909  13342  -4070   1381  -1865       N  
ATOM   2574  N   GLY A 375      16.135   1.527 -18.433  1.00132.49           N  
ANISOU 2574  N   GLY A 375    16572  24070   9699  -4098   1121  -1531       N  
ATOM   2575  CA  GLY A 375      15.390   0.369 -18.914  1.00130.80           C  
ANISOU 2575  CA  GLY A 375    16216  23875   9609  -3955   1070  -1423       C  
ATOM   2576  C   GLY A 375      14.126   0.689 -19.695  1.00133.89           C  
ANISOU 2576  C   GLY A 375    16686  24170  10017  -3800   1171  -1407       C  
ATOM   2577  O   GLY A 375      13.847   0.028 -20.699  1.00133.27           O  
ANISOU 2577  O   GLY A 375    16513  24061  10063  -3711   1153  -1358       O  
ATOM   2578  N   THR A 376      13.347   1.705 -19.243  1.00130.10           N  
ANISOU 2578  N   THR A 376    16379  23650   9403  -3743   1261  -1467       N  
ATOM   2579  CA  THR A 376      12.082   2.145 -19.862  1.00129.39           C  
ANISOU 2579  CA  THR A 376    16376  23491   9296  -3551   1336  -1499       C  
ATOM   2580  C   THR A 376      12.332   2.580 -21.336  1.00132.16           C  
ANISOU 2580  C   THR A 376    16833  23661   9719  -3515   1364  -1532       C  
ATOM   2581  O   THR A 376      11.570   2.182 -22.223  1.00130.72           O  
ANISOU 2581  O   THR A 376    16595  23449   9623  -3367   1374  -1501       O  
ATOM   2582  CB  THR A 376      11.454   3.292 -19.023  1.00137.79           C  
ANISOU 2582  CB  THR A 376    17628  24549  10176  -3481   1392  -1610       C  
ATOM   2583  OG1 THR A 376      11.126   2.780 -17.732  1.00137.12           O  
ANISOU 2583  OG1 THR A 376    17420  24664  10017  -3526   1377  -1576       O  
ATOM   2584  CG2 THR A 376      10.182   3.869 -19.645  1.00137.60           C  
ANISOU 2584  CG2 THR A 376    17706  24465  10110  -3233   1439  -1696       C  
ATOM   2585  N   LEU A 377      13.402   3.366 -21.585  1.00128.96           N  
ANISOU 2585  N   LEU A 377    16582  23154   9264  -3678   1375  -1595       N  
ATOM   2586  CA  LEU A 377      13.761   3.852 -22.921  1.00128.29           C  
ANISOU 2586  CA  LEU A 377    16636  22909   9200  -3718   1405  -1629       C  
ATOM   2587  C   LEU A 377      14.565   2.801 -23.703  1.00129.70           C  
ANISOU 2587  C   LEU A 377    16565  23181   9535  -3802   1368  -1579       C  
ATOM   2588  O   LEU A 377      14.559   2.850 -24.935  1.00129.15           O  
ANISOU 2588  O   LEU A 377    16538  23018   9516  -3786   1394  -1584       O  
ATOM   2589  CB  LEU A 377      14.560   5.171 -22.848  1.00130.06           C  
ANISOU 2589  CB  LEU A 377    17160  22999   9256  -3918   1435  -1726       C  
ATOM   2590  CG  LEU A 377      13.769   6.500 -22.718  1.00136.45           C  
ANISOU 2590  CG  LEU A 377    18356  23596   9894  -3800   1448  -1808       C  
ATOM   2591  CD1 LEU A 377      12.850   6.535 -21.488  1.00136.99           C  
ANISOU 2591  CD1 LEU A 377    18383  23761   9904  -3613   1436  -1833       C  
ATOM   2592  CD2 LEU A 377      14.711   7.691 -22.690  1.00141.01           C  
ANISOU 2592  CD2 LEU A 377    19260  24023  10294  -4061   1457  -1886       C  
ATOM   2593  N   ARG A 378      15.234   1.848 -23.007  1.00124.56           N  
ANISOU 2593  N   ARG A 378    15669  22710   8950  -3872   1290  -1544       N  
ATOM   2594  CA  ARG A 378      16.009   0.784 -23.663  1.00123.33           C  
ANISOU 2594  CA  ARG A 378    15267  22660   8933  -3900   1214  -1529       C  
ATOM   2595  C   ARG A 378      15.071  -0.234 -24.339  1.00124.38           C  
ANISOU 2595  C   ARG A 378    15277  22771   9209  -3699   1177  -1429       C  
ATOM   2596  O   ARG A 378      15.304  -0.613 -25.491  1.00122.98           O  
ANISOU 2596  O   ARG A 378    15019  22577   9130  -3673   1171  -1437       O  
ATOM   2597  CB  ARG A 378      16.938   0.065 -22.663  1.00124.41           C  
ANISOU 2597  CB  ARG A 378    15217  22973   9078  -3981   1094  -1541       C  
ATOM   2598  CG  ARG A 378      17.844  -0.986 -23.317  1.00136.24           C  
ANISOU 2598  CG  ARG A 378    16466  24598  10702  -3972    978  -1577       C  
ATOM   2599  CD  ARG A 378      18.575  -1.859 -22.318  1.00146.76           C  
ANISOU 2599  CD  ARG A 378    17638  26079  12045  -3970    804  -1589       C  
ATOM   2600  NE  ARG A 378      19.484  -1.102 -21.460  1.00156.13           N  
ANISOU 2600  NE  ARG A 378    18857  27362  13104  -4148    818  -1696       N  
ATOM   2601  CZ  ARG A 378      20.247  -1.652 -20.521  1.00170.61           C  
ANISOU 2601  CZ  ARG A 378    20575  29332  14917  -4160    663  -1739       C  
ATOM   2602  NH1 ARG A 378      20.218  -2.964 -20.316  1.00157.73           N  
ANISOU 2602  NH1 ARG A 378    18826  27730  13376  -4002    465  -1679       N  
ATOM   2603  NH2 ARG A 378      21.051  -0.896 -19.785  1.00157.67           N  
ANISOU 2603  NH2 ARG A 378    18964  27787  13156  -4330    687  -1845       N  
ATOM   2604  N   SER A 379      14.024  -0.680 -23.610  1.00119.80           N  
ANISOU 2604  N   SER A 379    14680  22214   8624  -3582   1156  -1344       N  
ATOM   2605  CA  SER A 379      13.036  -1.652 -24.085  1.00118.29           C  
ANISOU 2605  CA  SER A 379    14382  22026   8538  -3430   1122  -1248       C  
ATOM   2606  C   SER A 379      12.305  -1.142 -25.337  1.00121.00           C  
ANISOU 2606  C   SER A 379    14818  22242   8915  -3305   1212  -1272       C  
ATOM   2607  O   SER A 379      12.094  -1.925 -26.260  1.00120.10           O  
ANISOU 2607  O   SER A 379    14593  22113   8926  -3223   1176  -1223       O  
ATOM   2608  CB  SER A 379      12.027  -1.965 -22.987  1.00122.14           C  
ANISOU 2608  CB  SER A 379    14861  22600   8946  -3396   1115  -1183       C  
ATOM   2609  OG  SER A 379      11.374  -0.789 -22.538  1.00131.99           O  
ANISOU 2609  OG  SER A 379    16266  23828  10057  -3358   1226  -1262       O  
ATOM   2610  N   ALA A 380      11.976   0.179 -25.390  1.00117.12           N  
ANISOU 2610  N   ALA A 380    14556  21641   8303  -3284   1307  -1357       N  
ATOM   2611  CA  ALA A 380      11.303   0.834 -26.528  1.00116.10           C  
ANISOU 2611  CA  ALA A 380    14589  21354   8171  -3151   1366  -1399       C  
ATOM   2612  C   ALA A 380      12.115   0.673 -27.828  1.00117.48           C  
ANISOU 2612  C   ALA A 380    14749  21456   8432  -3231   1364  -1401       C  
ATOM   2613  O   ALA A 380      11.529   0.536 -28.906  1.00115.83           O  
ANISOU 2613  O   ALA A 380    14559  21162   8290  -3103   1377  -1386       O  
ATOM   2614  CB  ALA A 380      11.088   2.310 -26.230  1.00118.18           C  
ANISOU 2614  CB  ALA A 380    15163  21481   8258  -3136   1416  -1504       C  
ATOM   2615  N   LYS A 381      13.462   0.678 -27.712  1.00113.18           N  
ANISOU 2615  N   LYS A 381    14152  20978   7875  -3445   1349  -1437       N  
ATOM   2616  CA  LYS A 381      14.365   0.469 -28.833  1.00112.21           C  
ANISOU 2616  CA  LYS A 381    13958  20868   7808  -3557   1352  -1473       C  
ATOM   2617  C   LYS A 381      14.273  -0.990 -29.243  1.00115.23           C  
ANISOU 2617  C   LYS A 381    14053  21356   8372  -3431   1262  -1405       C  
ATOM   2618  O   LYS A 381      13.903  -1.267 -30.380  1.00114.59           O  
ANISOU 2618  O   LYS A 381    13956  21210   8372  -3338   1275  -1385       O  
ATOM   2619  CB  LYS A 381      15.810   0.889 -28.475  1.00115.08           C  
ANISOU 2619  CB  LYS A 381    14303  21343   8078  -3828   1360  -1570       C  
ATOM   2620  CG  LYS A 381      16.809   0.744 -29.631  1.00119.51           C  
ANISOU 2620  CG  LYS A 381    14761  21989   8656  -3983   1380  -1650       C  
ATOM   2621  CD  LYS A 381      18.238   1.119 -29.238  1.00123.93           C  
ANISOU 2621  CD  LYS A 381    15250  22734   9104  -4271   1392  -1780       C  
ATOM   2622  CE  LYS A 381      19.215   0.934 -30.380  1.00122.87           C  
ANISOU 2622  CE  LYS A 381    14963  22759   8962  -4440   1421  -1894       C  
ATOM   2623  NZ  LYS A 381      20.608   1.274 -29.984  1.00128.20           N  
ANISOU 2623  NZ  LYS A 381    15520  23682   9508  -4734   1436  -2055       N  
ATOM   2624  N   LEU A 382      14.525  -1.916 -28.286  1.00111.93           N  
ANISOU 2624  N   LEU A 382    13447  21075   8005  -3417   1155  -1364       N  
ATOM   2625  CA  LEU A 382      14.480  -3.374 -28.458  1.00111.60           C  
ANISOU 2625  CA  LEU A 382    13185  21108   8109  -3302   1020  -1295       C  
ATOM   2626  C   LEU A 382      13.182  -3.838 -29.132  1.00114.49           C  
ANISOU 2626  C   LEU A 382    13559  21382   8558  -3127   1033  -1200       C  
ATOM   2627  O   LEU A 382      13.251  -4.567 -30.122  1.00114.49           O  
ANISOU 2627  O   LEU A 382    13451  21376   8676  -3050    982  -1187       O  
ATOM   2628  CB  LEU A 382      14.617  -4.070 -27.088  1.00112.62           C  
ANISOU 2628  CB  LEU A 382    13241  21331   8218  -3317    894  -1243       C  
ATOM   2629  CG  LEU A 382      14.396  -5.601 -27.030  1.00117.90           C  
ANISOU 2629  CG  LEU A 382    13777  22027   8994  -3207    713  -1147       C  
ATOM   2630  CD1 LEU A 382      15.429  -6.362 -27.863  1.00118.35           C  
ANISOU 2630  CD1 LEU A 382    13664  22145   9157  -3157    584  -1227       C  
ATOM   2631  CD2 LEU A 382      14.426  -6.095 -25.593  1.00122.39           C  
ANISOU 2631  CD2 LEU A 382    14364  22650   9488  -3259    594  -1085       C  
ATOM   2632  N   PHE A 383      12.013  -3.440 -28.587  1.00109.87           N  
ANISOU 2632  N   PHE A 383    13084  20758   7905  -3061   1097  -1155       N  
ATOM   2633  CA  PHE A 383      10.708  -3.821 -29.126  1.00108.46           C  
ANISOU 2633  CA  PHE A 383    12890  20541   7778  -2903   1116  -1093       C  
ATOM   2634  C   PHE A 383      10.486  -3.221 -30.512  1.00110.66           C  
ANISOU 2634  C   PHE A 383    13265  20689   8089  -2816   1192  -1143       C  
ATOM   2635  O   PHE A 383       9.873  -3.890 -31.346  1.00109.86           O  
ANISOU 2635  O   PHE A 383    13085  20568   8091  -2698   1168  -1096       O  
ATOM   2636  CB  PHE A 383       9.564  -3.404 -28.187  1.00110.97           C  
ANISOU 2636  CB  PHE A 383    13272  20912   7979  -2856   1175  -1089       C  
ATOM   2637  CG  PHE A 383       9.371  -4.347 -27.019  1.00113.06           C  
ANISOU 2637  CG  PHE A 383    13428  21315   8214  -2937   1092  -1000       C  
ATOM   2638  CD1 PHE A 383      10.107  -4.196 -25.850  1.00117.22           C  
ANISOU 2638  CD1 PHE A 383    13982  21900   8656  -3073   1055  -1007       C  
ATOM   2639  CD2 PHE A 383       8.456  -5.390 -27.092  1.00114.78           C  
ANISOU 2639  CD2 PHE A 383    13542  21601   8469  -2904   1042   -909       C  
ATOM   2640  CE1 PHE A 383       9.944  -5.082 -24.783  1.00118.58           C  
ANISOU 2640  CE1 PHE A 383    14099  22178   8778  -3165    961   -917       C  
ATOM   2641  CE2 PHE A 383       8.286  -6.269 -26.021  1.00118.23           C  
ANISOU 2641  CE2 PHE A 383    13936  22148   8841  -3030    954   -816       C  
ATOM   2642  CZ  PHE A 383       9.043  -6.119 -24.881  1.00117.26           C  
ANISOU 2642  CZ  PHE A 383    13861  22062   8631  -3156    908   -817       C  
ATOM   2643  N   PHE A 384      11.018  -2.002 -30.785  1.00106.61           N  
ANISOU 2643  N   PHE A 384    12948  20080   7479  -2896   1271  -1234       N  
ATOM   2644  CA  PHE A 384      10.867  -1.371 -32.103  1.00105.55           C  
ANISOU 2644  CA  PHE A 384    12971  19792   7339  -2848   1327  -1277       C  
ATOM   2645  C   PHE A 384      11.734  -2.099 -33.146  1.00104.47           C  
ANISOU 2645  C   PHE A 384    12682  19695   7316  -2915   1294  -1275       C  
ATOM   2646  O   PHE A 384      11.297  -2.255 -34.284  1.00102.53           O  
ANISOU 2646  O   PHE A 384    12454  19368   7133  -2813   1305  -1263       O  
ATOM   2647  CB  PHE A 384      11.215   0.123 -32.063  1.00109.09           C  
ANISOU 2647  CB  PHE A 384    13736  20101   7612  -2958   1396  -1366       C  
ATOM   2648  CG  PHE A 384      10.752   0.880 -33.286  1.00111.43           C  
ANISOU 2648  CG  PHE A 384    14290  20190   7856  -2880   1429  -1403       C  
ATOM   2649  CD1 PHE A 384      11.610   1.098 -34.358  1.00115.11           C  
ANISOU 2649  CD1 PHE A 384    14839  20595   8301  -3050   1458  -1429       C  
ATOM   2650  CD2 PHE A 384       9.449   1.359 -33.375  1.00114.08           C  
ANISOU 2650  CD2 PHE A 384    14785  20413   8148  -2632   1420  -1428       C  
ATOM   2651  CE1 PHE A 384      11.180   1.806 -35.488  1.00116.50           C  
ANISOU 2651  CE1 PHE A 384    15304  20555   8405  -2997   1474  -1452       C  
ATOM   2652  CE2 PHE A 384       9.017   2.055 -34.511  1.00117.39           C  
ANISOU 2652  CE2 PHE A 384    15479  20616   8507  -2532   1416  -1468       C  
ATOM   2653  CZ  PHE A 384       9.886   2.274 -35.559  1.00115.71           C  
ANISOU 2653  CZ  PHE A 384    15394  20302   8269  -2724   1441  -1467       C  
ATOM   2654  N   ASP A 385      12.940  -2.566 -32.749  1.00 99.49           N  
ANISOU 2654  N   ASP A 385    11888  19209   6705  -3063   1242  -1306       N  
ATOM   2655  CA  ASP A 385      13.825  -3.323 -33.632  1.00 98.55           C  
ANISOU 2655  CA  ASP A 385    11575  19187   6680  -3101   1190  -1348       C  
ATOM   2656  C   ASP A 385      13.272  -4.716 -33.862  1.00100.18           C  
ANISOU 2656  C   ASP A 385    11591  19423   7051  -2911   1071  -1260       C  
ATOM   2657  O   ASP A 385      13.320  -5.172 -34.994  1.00 99.62           O  
ANISOU 2657  O   ASP A 385    11444  19342   7067  -2847   1055  -1272       O  
ATOM   2658  CB  ASP A 385      15.270  -3.407 -33.106  1.00101.33           C  
ANISOU 2658  CB  ASP A 385    11785  19727   6989  -3280   1146  -1452       C  
ATOM   2659  CG  ASP A 385      16.200  -2.314 -33.637  1.00111.60           C  
ANISOU 2659  CG  ASP A 385    13201  21058   8143  -3533   1262  -1578       C  
ATOM   2660  OD1 ASP A 385      16.098  -1.970 -34.845  1.00110.39           O  
ANISOU 2660  OD1 ASP A 385    13145  20827   7970  -3569   1336  -1599       O  
ATOM   2661  OD2 ASP A 385      17.139  -1.947 -32.921  1.00120.74           O  
ANISOU 2661  OD2 ASP A 385    14323  22348   9205  -3715   1265  -1666       O  
ATOM   2662  N   LEU A 386      12.706  -5.367 -32.830  1.00 95.83           N  
ANISOU 2662  N   LEU A 386    10989  18898   6523  -2842    987  -1171       N  
ATOM   2663  CA  LEU A 386      12.088  -6.695 -32.958  1.00 95.06           C  
ANISOU 2663  CA  LEU A 386    10768  18804   6545  -2706    860  -1071       C  
ATOM   2664  C   LEU A 386      10.894  -6.697 -33.949  1.00 98.34           C  
ANISOU 2664  C   LEU A 386    11231  19117   7017  -2570    925  -1020       C  
ATOM   2665  O   LEU A 386      10.685  -7.707 -34.633  1.00 97.05           O  
ANISOU 2665  O   LEU A 386    10962  18944   6968  -2474    834   -973       O  
ATOM   2666  CB  LEU A 386      11.601  -7.209 -31.589  1.00 95.42           C  
ANISOU 2666  CB  LEU A 386    10817  18894   6545  -2727    781   -979       C  
ATOM   2667  CG  LEU A 386      12.659  -7.732 -30.617  1.00101.01           C  
ANISOU 2667  CG  LEU A 386    11459  19692   7230  -2807    634  -1000       C  
ATOM   2668  CD1 LEU A 386      12.110  -7.820 -29.216  1.00101.87           C  
ANISOU 2668  CD1 LEU A 386    11641  19829   7237  -2877    609   -915       C  
ATOM   2669  CD2 LEU A 386      13.232  -9.073 -31.076  1.00103.47           C  
ANISOU 2669  CD2 LEU A 386    11641  20019   7655  -2713    422   -998       C  
ATOM   2670  N   PHE A 387      10.121  -5.574 -34.018  1.00 94.76           N  
ANISOU 2670  N   PHE A 387    10947  18585   6473  -2544   1061  -1044       N  
ATOM   2671  CA  PHE A 387       8.947  -5.431 -34.892  1.00 93.68           C  
ANISOU 2671  CA  PHE A 387    10868  18362   6365  -2387   1113  -1027       C  
ATOM   2672  C   PHE A 387       9.352  -5.437 -36.376  1.00 94.89           C  
ANISOU 2672  C   PHE A 387    11030  18432   6591  -2354   1126  -1062       C  
ATOM   2673  O   PHE A 387       8.725  -6.123 -37.180  1.00 93.47           O  
ANISOU 2673  O   PHE A 387    10775  18228   6512  -2228   1090  -1018       O  
ATOM   2674  CB  PHE A 387       8.169  -4.136 -34.571  1.00 96.65           C  
ANISOU 2674  CB  PHE A 387    11449  18673   6602  -2331   1217  -1089       C  
ATOM   2675  CG  PHE A 387       6.890  -3.989 -35.372  1.00 98.90           C  
ANISOU 2675  CG  PHE A 387    11780  18897   6901  -2128   1244  -1104       C  
ATOM   2676  CD1 PHE A 387       5.700  -4.556 -34.926  1.00102.71           C  
ANISOU 2676  CD1 PHE A 387    12134  19503   7389  -2027   1229  -1074       C  
ATOM   2677  CD2 PHE A 387       6.881  -3.309 -36.587  1.00101.01           C  
ANISOU 2677  CD2 PHE A 387    12220  19000   7160  -2053   1277  -1156       C  
ATOM   2678  CE1 PHE A 387       4.525  -4.443 -35.678  1.00103.52           C  
ANISOU 2678  CE1 PHE A 387    12244  19591   7499  -1829   1246  -1117       C  
ATOM   2679  CE2 PHE A 387       5.705  -3.202 -37.339  1.00103.48           C  
ANISOU 2679  CE2 PHE A 387    12576  19258   7485  -1837   1279  -1184       C  
ATOM   2680  CZ  PHE A 387       4.535  -3.765 -36.877  1.00101.69           C  
ANISOU 2680  CZ  PHE A 387    12184  19179   7274  -1713   1263  -1174       C  
ATOM   2681  N   LEU A 388      10.355  -4.631 -36.734  1.00 90.89           N  
ANISOU 2681  N   LEU A 388    10626  17894   6013  -2490   1184  -1146       N  
ATOM   2682  CA  LEU A 388      10.849  -4.512 -38.100  1.00 90.10           C  
ANISOU 2682  CA  LEU A 388    10553  17745   5937  -2519   1215  -1195       C  
ATOM   2683  C   LEU A 388      11.650  -5.751 -38.471  1.00 95.95           C  
ANISOU 2683  C   LEU A 388    11026  18625   6806  -2520   1112  -1205       C  
ATOM   2684  O   LEU A 388      11.480  -6.283 -39.560  1.00 94.57           O  
ANISOU 2684  O   LEU A 388    10784  18426   6720  -2428   1088  -1199       O  
ATOM   2685  CB  LEU A 388      11.704  -3.242 -38.238  1.00 90.74           C  
ANISOU 2685  CB  LEU A 388    10846  17780   5852  -2734   1311  -1289       C  
ATOM   2686  CG  LEU A 388      11.091  -1.918 -37.739  1.00 95.14           C  
ANISOU 2686  CG  LEU A 388    11725  18174   6249  -2736   1376  -1303       C  
ATOM   2687  CD1 LEU A 388      12.090  -0.799 -37.839  1.00 96.49           C  
ANISOU 2687  CD1 LEU A 388    12122  18298   6240  -3005   1447  -1386       C  
ATOM   2688  CD2 LEU A 388       9.799  -1.555 -38.476  1.00 96.44           C  
ANISOU 2688  CD2 LEU A 388    12076  18158   6410  -2513   1381  -1283       C  
ATOM   2689  N   SER A 389      12.473  -6.247 -37.526  1.00 95.74           N  
ANISOU 2689  N   SER A 389    10851  18739   6784  -2594   1028  -1228       N  
ATOM   2690  CA  SER A 389      13.312  -7.444 -37.655  1.00 96.80           C  
ANISOU 2690  CA  SER A 389    10743  19014   7020  -2554    877  -1271       C  
ATOM   2691  C   SER A 389      12.451  -8.718 -37.817  1.00101.22           C  
ANISOU 2691  C   SER A 389    11224  19517   7719  -2361    739  -1157       C  
ATOM   2692  O   SER A 389      12.958  -9.711 -38.337  1.00101.18           O  
ANISOU 2692  O   SER A 389    11065  19572   7808  -2274    602  -1196       O  
ATOM   2693  CB  SER A 389      14.230  -7.583 -36.437  1.00102.34           C  
ANISOU 2693  CB  SER A 389    11360  19854   7672  -2647    793  -1324       C  
ATOM   2694  OG  SER A 389      15.095  -8.706 -36.482  1.00113.78           O  
ANISOU 2694  OG  SER A 389    12592  21440   9199  -2568    606  -1399       O  
ATOM   2695  N   SER A 390      11.161  -8.690 -37.393  1.00 97.92           N  
ANISOU 2695  N   SER A 390    10909  19000   7295  -2301    769  -1036       N  
ATOM   2696  CA  SER A 390      10.280  -9.847 -37.552  1.00 97.51           C  
ANISOU 2696  CA  SER A 390    10801  18908   7342  -2176    653   -927       C  
ATOM   2697  C   SER A 390       9.798  -9.950 -38.998  1.00103.19           C  
ANISOU 2697  C   SER A 390    11510  19552   8144  -2060    693   -931       C  
ATOM   2698  O   SER A 390      10.109 -10.941 -39.663  1.00103.48           O  
ANISOU 2698  O   SER A 390    11437  19596   8285  -1978    567   -936       O  
ATOM   2699  CB  SER A 390       9.095  -9.787 -36.595  1.00100.29           C  
ANISOU 2699  CB  SER A 390    11227  19250   7628  -2192    684   -826       C  
ATOM   2700  OG  SER A 390       8.304  -8.634 -36.813  1.00108.77           O  
ANISOU 2700  OG  SER A 390    12415  20282   8630  -2164    853   -858       O  
ATOM   2701  N   PHE A 391       9.113  -8.899 -39.510  1.00100.29           N  
ANISOU 2701  N   PHE A 391    11277  19107   7722  -2040    850   -948       N  
ATOM   2702  CA  PHE A 391       8.572  -8.842 -40.881  1.00 99.97           C  
ANISOU 2702  CA  PHE A 391    11268  18978   7738  -1926    893   -955       C  
ATOM   2703  C   PHE A 391       9.683  -8.628 -41.950  1.00103.61           C  
ANISOU 2703  C   PHE A 391    11708  19453   8206  -1983    920  -1056       C  
ATOM   2704  O   PHE A 391       9.379  -8.198 -43.074  1.00103.09           O  
ANISOU 2704  O   PHE A 391    11735  19300   8136  -1938    991  -1079       O  
ATOM   2705  CB  PHE A 391       7.536  -7.701 -40.994  1.00102.22           C  
ANISOU 2705  CB  PHE A 391    11744  19166   7930  -1866   1019   -967       C  
ATOM   2706  CG  PHE A 391       6.237  -7.905 -40.249  1.00104.23           C  
ANISOU 2706  CG  PHE A 391    11976  19462   8166  -1781   1012   -910       C  
ATOM   2707  CD1 PHE A 391       6.091  -7.463 -38.940  1.00108.71           C  
ANISOU 2707  CD1 PHE A 391    12578  20099   8628  -1854   1041   -914       C  
ATOM   2708  CD2 PHE A 391       5.146  -8.500 -40.872  1.00106.16           C  
ANISOU 2708  CD2 PHE A 391    12154  19704   8479  -1643    984   -872       C  
ATOM   2709  CE1 PHE A 391       4.883  -7.636 -38.256  1.00110.09           C  
ANISOU 2709  CE1 PHE A 391    12704  20371   8756  -1801   1049   -890       C  
ATOM   2710  CE2 PHE A 391       3.938  -8.672 -40.191  1.00109.80           C  
ANISOU 2710  CE2 PHE A 391    12561  20267   8892  -1600    991   -850       C  
ATOM   2711  CZ  PHE A 391       3.812  -8.235 -38.888  1.00108.98           C  
ANISOU 2711  CZ  PHE A 391    12477  20259   8671  -1684   1028   -865       C  
ATOM   2712  N   GLN A 392      10.947  -8.966 -41.612  1.00 99.63           N  
ANISOU 2712  N   GLN A 392    11072  19083   7701  -2081    855  -1131       N  
ATOM   2713  CA  GLN A 392      12.125  -8.766 -42.461  1.00 99.46           C  
ANISOU 2713  CA  GLN A 392    10976  19166   7650  -2178    888  -1268       C  
ATOM   2714  C   GLN A 392      12.056  -9.680 -43.716  1.00100.56           C  
ANISOU 2714  C   GLN A 392    10988  19310   7908  -2037    813  -1284       C  
ATOM   2715  O   GLN A 392      12.041  -9.177 -44.843  1.00 98.98           O  
ANISOU 2715  O   GLN A 392    10862  19073   7674  -2070    914  -1327       O  
ATOM   2716  CB  GLN A 392      13.401  -9.053 -41.633  1.00101.98           C  
ANISOU 2716  CB  GLN A 392    11131  19679   7938  -2276    805  -1372       C  
ATOM   2717  CG  GLN A 392      14.666  -8.259 -42.022  1.00112.85           C  
ANISOU 2717  CG  GLN A 392    12467  21224   9185  -2494    911  -1545       C  
ATOM   2718  CD  GLN A 392      14.711  -6.809 -41.553  1.00122.45           C  
ANISOU 2718  CD  GLN A 392    13920  22376  10228  -2717   1076  -1546       C  
ATOM   2719  OE1 GLN A 392      13.743  -6.032 -41.651  1.00117.27           O  
ANISOU 2719  OE1 GLN A 392    13523  21510   9524  -2704   1167  -1451       O  
ATOM   2720  NE2 GLN A 392      15.892  -6.383 -41.125  1.00107.84           N  
ANISOU 2720  NE2 GLN A 392    11992  20717   8263  -2926   1108  -1682       N  
ATOM   2721  N   GLY A 393      11.944 -10.994 -43.488  1.00 96.40           N  
ANISOU 2721  N   GLY A 393    10315  18805   7505  -1885    626  -1242       N  
ATOM   2722  CA  GLY A 393      11.869 -12.020 -44.530  1.00 95.28           C  
ANISOU 2722  CA  GLY A 393    10057  18660   7484  -1725    512  -1257       C  
ATOM   2723  C   GLY A 393      10.591 -12.045 -45.358  1.00 96.89           C  
ANISOU 2723  C   GLY A 393    10367  18701   7748  -1620    564  -1148       C  
ATOM   2724  O   GLY A 393      10.542 -12.725 -46.387  1.00 96.84           O  
ANISOU 2724  O   GLY A 393    10283  18685   7828  -1504    498  -1169       O  
ATOM   2725  N   LEU A 394       9.529 -11.340 -44.905  1.00 91.18           N  
ANISOU 2725  N   LEU A 394     9807  17865   6973  -1640    669  -1048       N  
ATOM   2726  CA  LEU A 394       8.292 -11.207 -45.678  1.00 89.30           C  
ANISOU 2726  CA  LEU A 394     9662  17501   6768  -1527    724   -981       C  
ATOM   2727  C   LEU A 394       8.533 -10.338 -46.908  1.00 91.78           C  
ANISOU 2727  C   LEU A 394    10084  17763   7026  -1553    848  -1059       C  
ATOM   2728  O   LEU A 394       8.281 -10.762 -48.037  1.00 91.36           O  
ANISOU 2728  O   LEU A 394    10000  17669   7043  -1452    824  -1063       O  
ATOM   2729  CB  LEU A 394       7.151 -10.606 -44.824  1.00 89.18           C  
ANISOU 2729  CB  LEU A 394     9768  17432   6684  -1520    793   -909       C  
ATOM   2730  CG  LEU A 394       5.893 -10.159 -45.618  1.00 93.03           C  
ANISOU 2730  CG  LEU A 394    10362  17818   7168  -1384    862   -893       C  
ATOM   2731  CD1 LEU A 394       5.133 -11.349 -46.191  1.00 92.22           C  
ANISOU 2731  CD1 LEU A 394    10136  17713   7189  -1261    759   -827       C  
ATOM   2732  CD2 LEU A 394       4.981  -9.298 -44.776  1.00 95.35           C  
ANISOU 2732  CD2 LEU A 394    10769  18106   7353  -1364    937   -894       C  
ATOM   2733  N   LEU A 395       9.036  -9.117 -46.660  1.00 87.10           N  
ANISOU 2733  N   LEU A 395     9644  17163   6288  -1711    971  -1119       N  
ATOM   2734  CA  LEU A 395       9.295  -8.062 -47.629  1.00 86.26           C  
ANISOU 2734  CA  LEU A 395     9735  16979   6060  -1811   1091  -1184       C  
ATOM   2735  C   LEU A 395      10.351  -8.514 -48.677  1.00 90.22           C  
ANISOU 2735  C   LEU A 395    10089  17613   6576  -1891   1086  -1285       C  
ATOM   2736  O   LEU A 395      10.195  -8.146 -49.843  1.00 89.99           O  
ANISOU 2736  O   LEU A 395    10187  17505   6502  -1902   1146  -1306       O  
ATOM   2737  CB  LEU A 395       9.760  -6.811 -46.853  1.00 86.56           C  
ANISOU 2737  CB  LEU A 395     9971  16997   5922  -2008   1189  -1223       C  
ATOM   2738  CG  LEU A 395      10.001  -5.480 -47.568  1.00 90.44           C  
ANISOU 2738  CG  LEU A 395    10784  17359   6220  -2175   1303  -1277       C  
ATOM   2739  CD1 LEU A 395      11.418  -5.302 -47.972  1.00 91.13           C  
ANISOU 2739  CD1 LEU A 395    10807  17614   6204  -2454   1365  -1388       C  
ATOM   2740  CD2 LEU A 395       8.917  -5.126 -48.576  1.00 91.01           C  
ANISOU 2740  CD2 LEU A 395    11082  17215   6282  -2008   1304  -1237       C  
ATOM   2741  N   VAL A 396      11.367  -9.348 -48.296  1.00 86.00           N  
ANISOU 2741  N   VAL A 396     9289  17290   6098  -1922    999  -1363       N  
ATOM   2742  CA  VAL A 396      12.356  -9.843 -49.282  1.00 85.76           C  
ANISOU 2742  CA  VAL A 396     9068  17443   6074  -1961    979  -1504       C  
ATOM   2743  C   VAL A 396      11.652 -10.856 -50.223  1.00 86.55           C  
ANISOU 2743  C   VAL A 396     9088  17468   6329  -1725    878  -1454       C  
ATOM   2744  O   VAL A 396      11.819 -10.774 -51.449  1.00 86.13           O  
ANISOU 2744  O   VAL A 396     9040  17438   6248  -1747    931  -1518       O  
ATOM   2745  CB  VAL A 396      13.656 -10.453 -48.678  1.00 90.66           C  
ANISOU 2745  CB  VAL A 396     9410  18338   6698  -2008    883  -1653       C  
ATOM   2746  CG1 VAL A 396      14.373  -9.454 -47.789  1.00 91.74           C  
ANISOU 2746  CG1 VAL A 396     9615  18568   6676  -2258    986  -1711       C  
ATOM   2747  CG2 VAL A 396      13.389 -11.746 -47.917  1.00 89.95           C  
ANISOU 2747  CG2 VAL A 396     9173  18234   6770  -1776    662  -1592       C  
ATOM   2748  N   ALA A 397      10.827 -11.770 -49.638  1.00 79.90           N  
ANISOU 2748  N   ALA A 397     8196  16533   5629  -1530    736  -1335       N  
ATOM   2749  CA  ALA A 397      10.061 -12.776 -50.370  1.00 77.66           C  
ANISOU 2749  CA  ALA A 397     7858  16163   5487  -1323    624  -1271       C  
ATOM   2750  C   ALA A 397       9.120 -12.104 -51.358  1.00 79.19           C  
ANISOU 2750  C   ALA A 397     8237  16198   5654  -1292    743  -1216       C  
ATOM   2751  O   ALA A 397       8.950 -12.596 -52.469  1.00 77.94           O  
ANISOU 2751  O   ALA A 397     8033  16020   5560  -1190    709  -1234       O  
ATOM   2752  CB  ALA A 397       9.283 -13.652 -49.400  1.00 77.60           C  
ANISOU 2752  CB  ALA A 397     7830  16080   5575  -1211    477  -1140       C  
ATOM   2753  N   VAL A 398       8.577 -10.931 -50.980  1.00 75.15           N  
ANISOU 2753  N   VAL A 398     7949  15573   5031  -1370    868  -1170       N  
ATOM   2754  CA  VAL A 398       7.667 -10.148 -51.816  1.00 74.66           C  
ANISOU 2754  CA  VAL A 398     8117  15338   4914  -1314    952  -1137       C  
ATOM   2755  C   VAL A 398       8.475  -9.420 -52.944  1.00 78.77           C  
ANISOU 2755  C   VAL A 398     8762  15865   5303  -1475   1055  -1234       C  
ATOM   2756  O   VAL A 398       8.185  -9.646 -54.116  1.00 76.31           O  
ANISOU 2756  O   VAL A 398     8474  15499   5020  -1394   1049  -1241       O  
ATOM   2757  CB  VAL A 398       6.840  -9.146 -50.959  1.00 78.47           C  
ANISOU 2757  CB  VAL A 398     8812  15700   5301  -1306   1012  -1088       C  
ATOM   2758  CG1 VAL A 398       6.016  -8.204 -51.831  1.00 78.68           C  
ANISOU 2758  CG1 VAL A 398     9123  15536   5237  -1222   1067  -1092       C  
ATOM   2759  CG2 VAL A 398       5.938  -9.881 -49.979  1.00 77.62           C  
ANISOU 2759  CG2 VAL A 398     8572  15626   5294  -1179    928  -1004       C  
ATOM   2760  N   LEU A 399       9.479  -8.580 -52.585  1.00 78.03           N  
ANISOU 2760  N   LEU A 399     8749  15852   5049  -1728   1149  -1312       N  
ATOM   2761  CA  LEU A 399      10.270  -7.784 -53.537  1.00 79.74           C  
ANISOU 2761  CA  LEU A 399     9118  16096   5082  -1969   1262  -1405       C  
ATOM   2762  C   LEU A 399      10.956  -8.641 -54.641  1.00 86.56           C  
ANISOU 2762  C   LEU A 399     9739  17151   5998  -1973   1241  -1506       C  
ATOM   2763  O   LEU A 399      10.848  -8.294 -55.827  1.00 86.54           O  
ANISOU 2763  O   LEU A 399     9893  17078   5909  -2030   1298  -1524       O  
ATOM   2764  CB  LEU A 399      11.371  -6.958 -52.826  1.00 80.83           C  
ANISOU 2764  CB  LEU A 399     9309  16362   5041  -2281   1354  -1488       C  
ATOM   2765  CG  LEU A 399      10.984  -5.732 -51.977  1.00 84.80           C  
ANISOU 2765  CG  LEU A 399    10145  16672   5402  -2372   1407  -1429       C  
ATOM   2766  CD1 LEU A 399      12.214  -5.104 -51.403  1.00 85.84           C  
ANISOU 2766  CD1 LEU A 399    10280  16972   5363  -2706   1491  -1527       C  
ATOM   2767  CD2 LEU A 399      10.279  -4.662 -52.804  1.00 87.82           C  
ANISOU 2767  CD2 LEU A 399    10972  16766   5628  -2391   1448  -1387       C  
ATOM   2768  N   TYR A 400      11.692  -9.708 -54.260  1.00 84.49           N  
ANISOU 2768  N   TYR A 400     9120  17130   5852  -1912   1146  -1589       N  
ATOM   2769  CA  TYR A 400      12.418 -10.496 -55.255  1.00 85.22           C  
ANISOU 2769  CA  TYR A 400     8965  17438   5976  -1892   1110  -1729       C  
ATOM   2770  C   TYR A 400      11.588 -11.617 -55.882  1.00 89.19           C  
ANISOU 2770  C   TYR A 400     9370  17839   6678  -1584    973  -1661       C  
ATOM   2771  O   TYR A 400      11.784 -11.883 -57.064  1.00 89.51           O  
ANISOU 2771  O   TYR A 400     9354  17949   6708  -1571    985  -1738       O  
ATOM   2772  CB  TYR A 400      13.691 -11.146 -54.686  1.00 87.16           C  
ANISOU 2772  CB  TYR A 400     8867  18016   6232  -1930   1035  -1905       C  
ATOM   2773  CG  TYR A 400      14.856 -10.211 -54.431  1.00 90.77           C  
ANISOU 2773  CG  TYR A 400     9318  18706   6466  -2281   1179  -2054       C  
ATOM   2774  CD1 TYR A 400      15.295  -9.331 -55.421  1.00 94.33           C  
ANISOU 2774  CD1 TYR A 400     9911  19232   6699  -2582   1350  -2136       C  
ATOM   2775  CD2 TYR A 400      15.678 -10.385 -53.320  1.00 92.16           C  
ANISOU 2775  CD2 TYR A 400     9296  19085   6635  -2323   1122  -2151       C  
ATOM   2776  CE1 TYR A 400      16.424  -8.533 -55.234  1.00 97.67           C  
ANISOU 2776  CE1 TYR A 400    10312  19910   6887  -2959   1483  -2290       C  
ATOM   2777  CE2 TYR A 400      16.821  -9.609 -53.133  1.00 94.98           C  
ANISOU 2777  CE2 TYR A 400     9598  19710   6779  -2660   1249  -2318       C  
ATOM   2778  CZ  TYR A 400      17.191  -8.683 -54.093  1.00103.84           C  
ANISOU 2778  CZ  TYR A 400    10876  20906   7674  -2994   1436  -2388       C  
ATOM   2779  OH  TYR A 400      18.320  -7.923 -53.913  1.00105.75           O  
ANISOU 2779  OH  TYR A 400    11068  21436   7676  -3380   1568  -2558       O  
ATOM   2780  N   CYS A 401      10.730 -12.310 -55.121  1.00 85.55           N  
ANISOU 2780  N   CYS A 401     8882  17243   6382  -1365    841  -1530       N  
ATOM   2781  CA  CYS A 401      10.026 -13.474 -55.653  1.00 85.04           C  
ANISOU 2781  CA  CYS A 401     8718  17102   6493  -1108    693  -1474       C  
ATOM   2782  C   CYS A 401       8.615 -13.106 -56.181  1.00 89.74           C  
ANISOU 2782  C   CYS A 401     9537  17447   7114  -1007    739  -1332       C  
ATOM   2783  O   CYS A 401       8.382 -13.193 -57.389  1.00 89.25           O  
ANISOU 2783  O   CYS A 401     9509  17341   7059   -948    755  -1352       O  
ATOM   2784  CB  CYS A 401       9.932 -14.561 -54.588  1.00 85.03           C  
ANISOU 2784  CB  CYS A 401     8571  17112   6626   -964    501  -1423       C  
ATOM   2785  SG  CYS A 401       8.921 -15.981 -55.060  1.00 87.96           S  
ANISOU 2785  SG  CYS A 401     8891  17342   7185   -696    300  -1321       S  
ATOM   2786  N   PHE A 402       7.676 -12.773 -55.289  1.00 86.95           N  
ANISOU 2786  N   PHE A 402     9308  16957   6772   -967    744  -1211       N  
ATOM   2787  CA  PHE A 402       6.282 -12.551 -55.663  1.00 86.82           C  
ANISOU 2787  CA  PHE A 402     9446  16756   6784   -825    754  -1113       C  
ATOM   2788  C   PHE A 402       6.062 -11.241 -56.495  1.00 92.19           C  
ANISOU 2788  C   PHE A 402    10417  17302   7309   -889    886  -1139       C  
ATOM   2789  O   PHE A 402       4.967 -11.077 -57.038  1.00 91.46           O  
ANISOU 2789  O   PHE A 402    10451  17066   7234   -733    873  -1093       O  
ATOM   2790  CB  PHE A 402       5.392 -12.494 -54.401  1.00 88.63           C  
ANISOU 2790  CB  PHE A 402     9700  16943   7033   -780    730  -1019       C  
ATOM   2791  CG  PHE A 402       5.512 -13.694 -53.481  1.00 90.19           C  
ANISOU 2791  CG  PHE A 402     9697  17231   7341   -759    588   -971       C  
ATOM   2792  CD1 PHE A 402       4.937 -14.913 -53.819  1.00 93.06           C  
ANISOU 2792  CD1 PHE A 402     9951  17574   7833   -628    448   -914       C  
ATOM   2793  CD2 PHE A 402       6.113 -13.578 -52.236  1.00 92.52           C  
ANISOU 2793  CD2 PHE A 402     9956  17606   7590   -877    581   -972       C  
ATOM   2794  CE1 PHE A 402       5.052 -16.019 -52.970  1.00 93.85           C  
ANISOU 2794  CE1 PHE A 402     9941  17716   8001   -630    286   -861       C  
ATOM   2795  CE2 PHE A 402       6.227 -14.683 -51.388  1.00 95.18           C  
ANISOU 2795  CE2 PHE A 402    10165  17996   8004   -861    423   -923       C  
ATOM   2796  CZ  PHE A 402       5.690 -15.894 -51.757  1.00 92.92           C  
ANISOU 2796  CZ  PHE A 402     9807  17668   7830   -743    270   -864       C  
ATOM   2797  N   LEU A 403       7.074 -10.347 -56.627  1.00 90.53           N  
ANISOU 2797  N   LEU A 403    10329  17137   6932  -1121    995  -1219       N  
ATOM   2798  CA  LEU A 403       6.894  -9.086 -57.370  1.00 91.33           C  
ANISOU 2798  CA  LEU A 403    10787  17069   6846  -1219   1092  -1231       C  
ATOM   2799  C   LEU A 403       7.582  -9.108 -58.742  1.00 96.10           C  
ANISOU 2799  C   LEU A 403    11414  17729   7370  -1344   1141  -1309       C  
ATOM   2800  O   LEU A 403       7.364  -8.188 -59.538  1.00 96.84           O  
ANISOU 2800  O   LEU A 403    11839  17655   7300  -1424   1197  -1308       O  
ATOM   2801  CB  LEU A 403       7.433  -7.897 -56.562  1.00 92.67           C  
ANISOU 2801  CB  LEU A 403    11173  17210   6826  -1448   1183  -1254       C  
ATOM   2802  CG  LEU A 403       6.413  -6.809 -56.182  1.00 97.59           C  
ANISOU 2802  CG  LEU A 403    12148  17584   7347  -1352   1181  -1203       C  
ATOM   2803  CD1 LEU A 403       5.180  -7.395 -55.490  1.00 96.33           C  
ANISOU 2803  CD1 LEU A 403    11839  17408   7354  -1059   1092  -1140       C  
ATOM   2804  CD2 LEU A 403       7.056  -5.743 -55.306  1.00100.76           C  
ANISOU 2804  CD2 LEU A 403    12751  17966   7568  -1587   1252  -1231       C  
ATOM   2805  N   ASN A 404       8.363 -10.160 -59.042  1.00 92.99           N  
ANISOU 2805  N   ASN A 404    10689  17566   7076  -1347   1103  -1387       N  
ATOM   2806  CA  ASN A 404       9.038 -10.277 -60.338  1.00 93.98           C  
ANISOU 2806  CA  ASN A 404    10779  17806   7121  -1461   1151  -1490       C  
ATOM   2807  C   ASN A 404       8.021 -10.736 -61.387  1.00 96.48           C  
ANISOU 2807  C   ASN A 404    11155  17960   7541  -1223   1083  -1427       C  
ATOM   2808  O   ASN A 404       7.280 -11.690 -61.154  1.00 94.75           O  
ANISOU 2808  O   ASN A 404    10769  17706   7527   -963    961  -1362       O  
ATOM   2809  CB  ASN A 404      10.235 -11.224 -60.247  1.00 96.42           C  
ANISOU 2809  CB  ASN A 404    10695  18451   7489  -1505   1112  -1638       C  
ATOM   2810  CG  ASN A 404      11.165 -11.208 -61.437  1.00125.75           C  
ANISOU 2810  CG  ASN A 404    14329  22384  11066  -1688   1192  -1799       C  
ATOM   2811  OD1 ASN A 404      10.990 -10.452 -62.401  1.00119.63           O  
ANISOU 2811  OD1 ASN A 404    13826  21500  10129  -1837   1291  -1786       O  
ATOM   2812  ND2 ASN A 404      12.233 -11.988 -61.348  1.00123.07           N  
ANISOU 2812  ND2 ASN A 404    13625  22379  10758  -1698   1146  -1975       N  
ATOM   2813  N   LYS A 405       7.970 -10.029 -62.524  1.00 93.69           N  
ANISOU 2813  N   LYS A 405    11069  17504   7026  -1335   1157  -1444       N  
ATOM   2814  CA  LYS A 405       6.976 -10.246 -63.573  1.00 92.61           C  
ANISOU 2814  CA  LYS A 405    11053  17184   6949  -1123   1099  -1387       C  
ATOM   2815  C   LYS A 405       7.191 -11.590 -64.329  1.00 92.53           C  
ANISOU 2815  C   LYS A 405    10707  17345   7105   -978   1022  -1447       C  
ATOM   2816  O   LYS A 405       6.195 -12.189 -64.742  1.00 90.67           O  
ANISOU 2816  O   LYS A 405    10449  16983   7018   -718    924  -1378       O  
ATOM   2817  CB  LYS A 405       6.969  -9.080 -64.584  1.00 97.77           C  
ANISOU 2817  CB  LYS A 405    12135  17664   7347  -1310   1182  -1394       C  
ATOM   2818  CG  LYS A 405       6.552  -7.735 -63.930  1.00119.15           C  
ANISOU 2818  CG  LYS A 405    15262  20125   9884  -1387   1205  -1333       C  
ATOM   2819  CD  LYS A 405       6.168  -6.585 -64.904  1.00131.55           C  
ANISOU 2819  CD  LYS A 405    17373  21406  11206  -1475   1212  -1311       C  
ATOM   2820  CE  LYS A 405       7.268  -6.057 -65.803  1.00142.64           C  
ANISOU 2820  CE  LYS A 405    18964  22894  12338  -1892   1330  -1381       C  
ATOM   2821  NZ  LYS A 405       6.791  -4.929 -66.646  1.00150.20           N  
ANISOU 2821  NZ  LYS A 405    20525  23508  13035  -1972   1299  -1338       N  
ATOM   2822  N   GLU A 406       8.433 -12.080 -64.484  1.00 88.14           N  
ANISOU 2822  N   GLU A 406     9884  17084   6521  -1122   1049  -1590       N  
ATOM   2823  CA  GLU A 406       8.617 -13.359 -65.181  1.00 87.11           C  
ANISOU 2823  CA  GLU A 406     9451  17104   6542   -940    945  -1668       C  
ATOM   2824  C   GLU A 406       8.387 -14.527 -64.195  1.00 88.80           C  
ANISOU 2824  C   GLU A 406     9400  17348   6992   -697    772  -1630       C  
ATOM   2825  O   GLU A 406       8.140 -15.652 -64.623  1.00 86.68           O  
ANISOU 2825  O   GLU A 406     8959  17094   6881   -477    632  -1642       O  
ATOM   2826  CB  GLU A 406       9.995 -13.476 -65.876  1.00 90.43           C  
ANISOU 2826  CB  GLU A 406     9673  17864   6821  -1150   1020  -1881       C  
ATOM   2827  CG  GLU A 406      11.234 -13.272 -65.015  1.00105.99           C  
ANISOU 2827  CG  GLU A 406    11455  20125   8691  -1367   1076  -2021       C  
ATOM   2828  CD  GLU A 406      12.563 -13.397 -65.750  1.00138.54           C  
ANISOU 2828  CD  GLU A 406    15333  24656  12651  -1575   1155  -2276       C  
ATOM   2829  OE1 GLU A 406      12.652 -14.195 -66.712  1.00141.00           O  
ANISOU 2829  OE1 GLU A 406    15466  25088  13020  -1428   1091  -2378       O  
ATOM   2830  OE2 GLU A 406      13.538 -12.745 -65.312  1.00138.41           O  
ANISOU 2830  OE2 GLU A 406    15272  24873  12447  -1881   1273  -2395       O  
ATOM   2831  N   VAL A 407       8.396 -14.244 -62.895  1.00 87.28           N  
ANISOU 2831  N   VAL A 407     9219  17136   6809   -745    772  -1574       N  
ATOM   2832  CA  VAL A 407       8.131 -15.254 -61.863  1.00 87.44           C  
ANISOU 2832  CA  VAL A 407     9058  17153   7011   -564    606  -1517       C  
ATOM   2833  C   VAL A 407       6.574 -15.456 -61.778  1.00 91.99           C  
ANISOU 2833  C   VAL A 407     9769  17478   7706   -375    542  -1341       C  
ATOM   2834  O   VAL A 407       6.101 -16.598 -61.813  1.00 91.77           O  
ANISOU 2834  O   VAL A 407     9615  17420   7835   -191    384  -1299       O  
ATOM   2835  CB  VAL A 407       8.782 -14.859 -60.495  1.00 91.42           C  
ANISOU 2835  CB  VAL A 407     9522  17756   7459   -709    634  -1534       C  
ATOM   2836  CG1 VAL A 407       8.436 -15.861 -59.396  1.00 90.10           C  
ANISOU 2836  CG1 VAL A 407     9229  17554   7451   -548    454  -1455       C  
ATOM   2837  CG2 VAL A 407      10.298 -14.737 -60.636  1.00 92.74           C  
ANISOU 2837  CG2 VAL A 407     9510  18225   7503   -889    689  -1740       C  
ATOM   2838  N   GLN A 408       5.805 -14.340 -61.736  1.00 88.00           N  
ANISOU 2838  N   GLN A 408     9526  16805   7104   -423    653  -1263       N  
ATOM   2839  CA  GLN A 408       4.332 -14.311 -61.715  1.00 86.48           C  
ANISOU 2839  CA  GLN A 408     9451  16430   6979   -250    613  -1148       C  
ATOM   2840  C   GLN A 408       3.710 -15.074 -62.911  1.00 87.55           C  
ANISOU 2840  C   GLN A 408     9541  16507   7216    -70    530  -1139       C  
ATOM   2841  O   GLN A 408       2.715 -15.775 -62.742  1.00 85.18           O  
ANISOU 2841  O   GLN A 408     9174  16154   7038     85    430  -1065       O  
ATOM   2842  CB  GLN A 408       3.840 -12.844 -61.751  1.00 88.76           C  
ANISOU 2842  CB  GLN A 408    10061  16564   7102   -307    729  -1131       C  
ATOM   2843  CG  GLN A 408       4.309 -11.955 -60.585  1.00111.05           C  
ANISOU 2843  CG  GLN A 408    12979  19407   9807   -477    809  -1134       C  
ATOM   2844  CD  GLN A 408       3.917 -10.488 -60.737  1.00135.77           C  
ANISOU 2844  CD  GLN A 408    16486  22353  12747   -525    890  -1136       C  
ATOM   2845  OE1 GLN A 408       3.066 -10.111 -61.554  1.00133.82           O  
ANISOU 2845  OE1 GLN A 408    16441  21942  12463   -382    866  -1126       O  
ATOM   2846  NE2 GLN A 408       4.511  -9.625 -59.925  1.00127.67           N  
ANISOU 2846  NE2 GLN A 408    15588  21334  11586   -713    965  -1154       N  
ATOM   2847  N   SER A 409       4.307 -14.914 -64.114  1.00 84.69           N  
ANISOU 2847  N   SER A 409     9221  16173   6783   -120    580  -1223       N  
ATOM   2848  CA  SER A 409       3.843 -15.483 -65.382  1.00 84.13           C  
ANISOU 2848  CA  SER A 409     9136  16049   6778     29    520  -1231       C  
ATOM   2849  C   SER A 409       4.032 -17.004 -65.451  1.00 86.06           C  
ANISOU 2849  C   SER A 409     9106  16393   7201    165    357  -1252       C  
ATOM   2850  O   SER A 409       3.073 -17.707 -65.757  1.00 84.93           O  
ANISOU 2850  O   SER A 409     8937  16156   7177    336    251  -1184       O  
ATOM   2851  CB  SER A 409       4.576 -14.843 -66.560  1.00 89.82           C  
ANISOU 2851  CB  SER A 409     9986  16805   7337   -114    629  -1327       C  
ATOM   2852  OG  SER A 409       5.958 -15.164 -66.576  1.00101.71           O  
ANISOU 2852  OG  SER A 409    11290  18558   8798   -264    656  -1460       O  
ATOM   2853  N   GLU A 410       5.267 -17.511 -65.223  1.00 82.40           N  
ANISOU 2853  N   GLU A 410     8449  16121   6738     99    319  -1363       N  
ATOM   2854  CA  GLU A 410       5.554 -18.951 -65.304  1.00 81.79           C  
ANISOU 2854  CA  GLU A 410     8152  16120   6806    259    120  -1411       C  
ATOM   2855  C   GLU A 410       4.683 -19.713 -64.291  1.00 81.27           C  
ANISOU 2855  C   GLU A 410     8077  15933   6870    356    -31  -1271       C  
ATOM   2856  O   GLU A 410       4.251 -20.843 -64.542  1.00 79.09           O  
ANISOU 2856  O   GLU A 410     7742  15595   6713    505   -209  -1238       O  
ATOM   2857  CB  GLU A 410       7.053 -19.224 -65.071  1.00 84.94           C  
ANISOU 2857  CB  GLU A 410     8349  16770   7156    195     90  -1592       C  
ATOM   2858  CG  GLU A 410       7.460 -20.691 -65.214  1.00 99.92           C  
ANISOU 2858  CG  GLU A 410    10046  18740   9179    407   -158  -1686       C  
ATOM   2859  CD  GLU A 410       7.177 -21.370 -66.546  1.00129.69           C  
ANISOU 2859  CD  GLU A 410    13783  22482  13011    572   -237  -1734       C  
ATOM   2860  OE1 GLU A 410       7.290 -20.708 -67.606  1.00119.40           O  
ANISOU 2860  OE1 GLU A 410    12523  21237  11609    490    -78  -1795       O  
ATOM   2861  OE2 GLU A 410       6.898 -22.591 -66.526  1.00131.48           O  
ANISOU 2861  OE2 GLU A 410    13959  22628  13371    772   -472  -1717       O  
ATOM   2862  N   LEU A 411       4.383 -19.049 -63.182  1.00 77.49           N  
ANISOU 2862  N   LEU A 411     7680  15420   6344    246     45  -1188       N  
ATOM   2863  CA  LEU A 411       3.516 -19.558 -62.139  1.00 76.36           C  
ANISOU 2863  CA  LEU A 411     7546  15197   6271    268    -54  -1056       C  
ATOM   2864  C   LEU A 411       2.081 -19.744 -62.704  1.00 78.90           C  
ANISOU 2864  C   LEU A 411     7935  15395   6648    373    -71   -964       C  
ATOM   2865  O   LEU A 411       1.550 -20.850 -62.624  1.00 78.19           O  
ANISOU 2865  O   LEU A 411     7794  15263   6652    439   -234   -903       O  
ATOM   2866  CB  LEU A 411       3.553 -18.576 -60.951  1.00 75.96           C  
ANISOU 2866  CB  LEU A 411     7567  15168   6124    119     71  -1018       C  
ATOM   2867  CG  LEU A 411       2.917 -19.011 -59.651  1.00 79.83           C  
ANISOU 2867  CG  LEU A 411     8049  15637   6645     81    -10   -907       C  
ATOM   2868  CD1 LEU A 411       3.701 -20.147 -59.012  1.00 80.34           C  
ANISOU 2868  CD1 LEU A 411     8013  15745   6767     84   -208   -919       C  
ATOM   2869  CD2 LEU A 411       2.881 -17.863 -58.691  1.00 82.92           C  
ANISOU 2869  CD2 LEU A 411     8524  16054   6928    -46    140   -890       C  
ATOM   2870  N   ARG A 412       1.506 -18.703 -63.365  1.00 74.91           N  
ANISOU 2870  N   ARG A 412     7560  14831   6070    390     76   -971       N  
ATOM   2871  CA  ARG A 412       0.161 -18.814 -63.945  1.00 74.76           C  
ANISOU 2871  CA  ARG A 412     7588  14727   6092    516     54   -919       C  
ATOM   2872  C   ARG A 412       0.190 -19.752 -65.169  1.00 80.57           C  
ANISOU 2872  C   ARG A 412     8261  15432   6920    638    -57   -948       C  
ATOM   2873  O   ARG A 412      -0.833 -20.368 -65.454  1.00 80.11           O  
ANISOU 2873  O   ARG A 412     8178  15327   6933    729   -142   -895       O  
ATOM   2874  CB  ARG A 412      -0.459 -17.441 -64.324  1.00 74.88           C  
ANISOU 2874  CB  ARG A 412     7794  14669   5990    550    195   -942       C  
ATOM   2875  CG  ARG A 412       0.259 -16.649 -65.415  1.00 89.59           C  
ANISOU 2875  CG  ARG A 412     9810  16479   7751    524    289  -1019       C  
ATOM   2876  CD  ARG A 412      -0.341 -15.281 -65.719  1.00109.54           C  
ANISOU 2876  CD  ARG A 412    12609  18879  10133    559    383  -1036       C  
ATOM   2877  NE  ARG A 412      -0.224 -14.334 -64.605  1.00131.86           N  
ANISOU 2877  NE  ARG A 412    15542  21704  12853    458    460  -1032       N  
ATOM   2878  CZ  ARG A 412      -1.202 -14.052 -63.748  1.00158.11           C  
ANISOU 2878  CZ  ARG A 412    18869  25032  16174    542    447  -1011       C  
ATOM   2879  NH1 ARG A 412      -1.001 -13.184 -62.764  1.00149.36           N  
ANISOU 2879  NH1 ARG A 412    17864  23925  14962    452    514  -1020       N  
ATOM   2880  NH2 ARG A 412      -2.392 -14.631 -63.872  1.00151.67           N  
ANISOU 2880  NH2 ARG A 412    17941  24243  15444    707    367   -998       N  
ATOM   2881  N   ARG A 413       1.354 -19.903 -65.854  1.00 78.65           N  
ANISOU 2881  N   ARG A 413     7974  15244   6666    631    -60  -1046       N  
ATOM   2882  CA  ARG A 413       1.453 -20.810 -67.002  1.00 79.11           C  
ANISOU 2882  CA  ARG A 413     7962  15292   6805    761   -172  -1095       C  
ATOM   2883  C   ARG A 413       1.221 -22.245 -66.597  1.00 84.58           C  
ANISOU 2883  C   ARG A 413     8553  15959   7625    836   -396  -1045       C  
ATOM   2884  O   ARG A 413       0.319 -22.882 -67.127  1.00 83.94           O  
ANISOU 2884  O   ARG A 413     8483  15794   7616    931   -488   -992       O  
ATOM   2885  CB  ARG A 413       2.804 -20.723 -67.715  1.00 81.23           C  
ANISOU 2885  CB  ARG A 413     8163  15689   7014    730   -134  -1246       C  
ATOM   2886  CG  ARG A 413       3.036 -19.482 -68.556  1.00 97.88           C  
ANISOU 2886  CG  ARG A 413    10417  17804   8969    631     62  -1302       C  
ATOM   2887  CD  ARG A 413       4.339 -19.573 -69.355  1.00117.71           C  
ANISOU 2887  CD  ARG A 413    12819  20503  11403    568     97  -1473       C  
ATOM   2888  NE  ARG A 413       4.326 -20.623 -70.390  1.00132.46           N  
ANISOU 2888  NE  ARG A 413    14571  22394  13364    742    -36  -1540       N  
ATOM   2889  CZ  ARG A 413       4.852 -21.843 -70.257  1.00145.94           C  
ANISOU 2889  CZ  ARG A 413    16078  24194  15178    876   -226  -1622       C  
ATOM   2890  NH1 ARG A 413       5.465 -22.192 -69.131  1.00122.14           N  
ANISOU 2890  NH1 ARG A 413    12956  21262  12189    857   -313  -1650       N  
ATOM   2891  NH2 ARG A 413       4.794 -22.709 -71.259  1.00138.81           N  
ANISOU 2891  NH2 ARG A 413    15103  23295  14345   1044   -349  -1690       N  
ATOM   2892  N   ARG A 414       1.998 -22.740 -65.626  1.00 83.77           N  
ANISOU 2892  N   ARG A 414     8381  15914   7532    785   -497  -1059       N  
ATOM   2893  CA  ARG A 414       1.927 -24.125 -65.171  1.00 84.77           C  
ANISOU 2893  CA  ARG A 414     8480  15981   7747    843   -752  -1015       C  
ATOM   2894  C   ARG A 414       0.631 -24.372 -64.365  1.00 87.78           C  
ANISOU 2894  C   ARG A 414     8938  16275   8140    749   -786   -850       C  
ATOM   2895  O   ARG A 414       0.271 -25.531 -64.172  1.00 88.17           O  
ANISOU 2895  O   ARG A 414     9022  16240   8240    760   -998   -785       O  
ATOM   2896  CB  ARG A 414       3.167 -24.470 -64.330  1.00 87.65           C  
ANISOU 2896  CB  ARG A 414     8781  16429   8093    827   -865  -1097       C  
ATOM   2897  CG  ARG A 414       3.415 -25.971 -64.187  1.00105.78           C  
ANISOU 2897  CG  ARG A 414    11088  18642  10460    953  -1189  -1110       C  
ATOM   2898  CD  ARG A 414       4.778 -26.279 -63.592  1.00126.82           C  
ANISOU 2898  CD  ARG A 414    13675  21414  13098   1011  -1326  -1254       C  
ATOM   2899  NE  ARG A 414       5.873 -25.772 -64.428  1.00141.43           N  
ANISOU 2899  NE  ARG A 414    15354  23475  14906   1083  -1216  -1471       N  
ATOM   2900  CZ  ARG A 414       7.163 -25.974 -64.174  1.00160.81           C  
ANISOU 2900  CZ  ARG A 414    17672  26106  17322   1162  -1316  -1668       C  
ATOM   2901  NH1 ARG A 414       7.535 -26.708 -63.132  1.00152.76           N  
ANISOU 2901  NH1 ARG A 414    16697  25034  16312   1220  -1560  -1669       N  
ATOM   2902  NH2 ARG A 414       8.090 -25.473 -64.980  1.00147.11           N  
ANISOU 2902  NH2 ARG A 414    15759  24616  15521   1179  -1187  -1880       N  
ATOM   2903  N   TRP A 415      -0.095 -23.303 -63.953  1.00 83.00           N  
ANISOU 2903  N   TRP A 415     8368  15702   7468    656   -590   -797       N  
ATOM   2904  CA  TRP A 415      -1.344 -23.467 -63.209  1.00 82.92           C  
ANISOU 2904  CA  TRP A 415     8381  15685   7439    558   -598   -683       C  
ATOM   2905  C   TRP A 415      -2.436 -23.953 -64.146  1.00 84.81           C  
ANISOU 2905  C   TRP A 415     8616  15879   7728    640   -649   -659       C  
ATOM   2906  O   TRP A 415      -3.162 -24.882 -63.794  1.00 84.31           O  
ANISOU 2906  O   TRP A 415     8558  15798   7679    558   -783   -576       O  
ATOM   2907  CB  TRP A 415      -1.766 -22.164 -62.502  1.00 82.26           C  
ANISOU 2907  CB  TRP A 415     8317  15678   7258    478   -392   -678       C  
ATOM   2908  CG  TRP A 415      -2.987 -22.318 -61.634  1.00 84.48           C  
ANISOU 2908  CG  TRP A 415     8577  16027   7495    365   -391   -599       C  
ATOM   2909  CD1 TRP A 415      -3.054 -22.944 -60.424  1.00 88.29           C  
ANISOU 2909  CD1 TRP A 415     9058  16546   7943    189   -480   -516       C  
ATOM   2910  CD2 TRP A 415      -4.285 -21.738 -61.859  1.00 84.86           C  
ANISOU 2910  CD2 TRP A 415     8596  16150   7498    410   -290   -622       C  
ATOM   2911  NE1 TRP A 415      -4.332 -22.853 -59.911  1.00 88.58           N  
ANISOU 2911  NE1 TRP A 415     9047  16700   7908     86   -426   -483       N  
ATOM   2912  CE2 TRP A 415      -5.103 -22.103 -60.762  1.00 89.86           C  
ANISOU 2912  CE2 TRP A 415     9171  16905   8067    237   -310   -562       C  
ATOM   2913  CE3 TRP A 415      -4.846 -20.961 -62.891  1.00 86.10           C  
ANISOU 2913  CE3 TRP A 415     8777  16291   7645    584   -199   -701       C  
ATOM   2914  CZ2 TRP A 415      -6.448 -21.714 -60.665  1.00 89.83           C  
ANISOU 2914  CZ2 TRP A 415     9082  17058   7991    242   -232   -607       C  
ATOM   2915  CZ3 TRP A 415      -6.180 -20.579 -62.794  1.00 88.13           C  
ANISOU 2915  CZ3 TRP A 415     8977  16666   7843    626   -148   -742       C  
ATOM   2916  CH2 TRP A 415      -6.965 -20.954 -61.693  1.00 89.75           C  
ANISOU 2916  CH2 TRP A 415     9075  17039   7986    461   -159   -708       C  
ATOM   2917  N   HIS A 416      -2.511 -23.358 -65.359  1.00 80.34           N  
ANISOU 2917  N   HIS A 416     8058  15295   7173    781   -552   -733       N  
ATOM   2918  CA  HIS A 416      -3.495 -23.693 -66.393  1.00 79.13           C  
ANISOU 2918  CA  HIS A 416     7898  15102   7064    889   -590   -732       C  
ATOM   2919  C   HIS A 416      -3.147 -24.999 -67.069  1.00 78.17           C  
ANISOU 2919  C   HIS A 416     7765  14899   7036    958   -795   -732       C  
ATOM   2920  O   HIS A 416      -4.056 -25.708 -67.495  1.00 77.33           O  
ANISOU 2920  O   HIS A 416     7655  14758   6970    977   -893   -691       O  
ATOM   2921  CB  HIS A 416      -3.586 -22.581 -67.432  1.00 80.27           C  
ANISOU 2921  CB  HIS A 416     8102  15229   7167   1018   -438   -813       C  
ATOM   2922  CG  HIS A 416      -4.052 -21.284 -66.856  1.00 84.83           C  
ANISOU 2922  CG  HIS A 416     8740  15852   7640    992   -276   -828       C  
ATOM   2923  ND1 HIS A 416      -3.154 -20.331 -66.402  1.00 87.26           N  
ANISOU 2923  ND1 HIS A 416     9125  16166   7866    923   -158   -860       N  
ATOM   2924  CD2 HIS A 416      -5.311 -20.839 -66.635  1.00 87.74           C  
ANISOU 2924  CD2 HIS A 416     9098  16278   7961   1034   -234   -835       C  
ATOM   2925  CE1 HIS A 416      -3.890 -19.334 -65.936  1.00 87.36           C  
ANISOU 2925  CE1 HIS A 416     9203  16200   7788    937    -59   -874       C  
ATOM   2926  NE2 HIS A 416      -5.195 -19.590 -66.062  1.00 87.97           N  
ANISOU 2926  NE2 HIS A 416     9219  16323   7883   1023   -103   -874       N  
ATOM   2927  N   ARG A 417      -1.838 -25.328 -67.148  1.00 72.50           N  
ANISOU 2927  N   ARG A 417     7037  14167   6341   1001   -872   -796       N  
ATOM   2928  CA  ARG A 417      -1.331 -26.569 -67.750  1.00 72.04           C  
ANISOU 2928  CA  ARG A 417     6975  14037   6362   1114  -1101   -836       C  
ATOM   2929  C   ARG A 417      -1.674 -27.756 -66.840  1.00 75.17           C  
ANISOU 2929  C   ARG A 417     7442  14345   6773   1015  -1334   -730       C  
ATOM   2930  O   ARG A 417      -2.082 -28.811 -67.334  1.00 74.43           O  
ANISOU 2930  O   ARG A 417     7405  14146   6728   1063  -1529   -701       O  
ATOM   2931  CB  ARG A 417       0.186 -26.484 -68.015  1.00 72.00           C  
ANISOU 2931  CB  ARG A 417     6905  14104   6348   1202  -1114   -984       C  
ATOM   2932  CG  ARG A 417       0.582 -25.308 -68.919  1.00 82.40           C  
ANISOU 2932  CG  ARG A 417     8189  15515   7606   1228   -881  -1085       C  
ATOM   2933  CD  ARG A 417       2.064 -25.272 -69.248  1.00 91.37           C  
ANISOU 2933  CD  ARG A 417     9223  16790   8704   1274   -882  -1260       C  
ATOM   2934  NE  ARG A 417       2.410 -26.187 -70.337  1.00 88.98           N  
ANISOU 2934  NE  ARG A 417     8858  16494   8458   1454  -1040  -1373       N  
ATOM   2935  CZ  ARG A 417       2.656 -25.804 -71.586  1.00 88.76           C  
ANISOU 2935  CZ  ARG A 417     8795  16539   8389   1506   -932  -1478       C  
ATOM   2936  NH1 ARG A 417       2.933 -26.704 -72.520  1.00 77.97           N  
ANISOU 2936  NH1 ARG A 417     7362  15187   7074   1680  -1089  -1588       N  
ATOM   2937  NH2 ARG A 417       2.625 -24.517 -71.911  1.00 60.96           N  
ANISOU 2937  NH2 ARG A 417     5333  13067   4760   1378   -679  -1477       N  
ATOM   2938  N   TRP A 418      -1.557 -27.549 -65.508  1.00 71.96           N  
ANISOU 2938  N   TRP A 418     7063  13973   6305    853  -1314   -665       N  
ATOM   2939  CA  TRP A 418      -1.928 -28.517 -64.477  1.00 73.05           C  
ANISOU 2939  CA  TRP A 418     7315  14031   6410    691  -1513   -546       C  
ATOM   2940  C   TRP A 418      -3.417 -28.742 -64.512  1.00 73.56           C  
ANISOU 2940  C   TRP A 418     7398  14105   6446    548  -1487   -442       C  
ATOM   2941  O   TRP A 418      -3.870 -29.887 -64.501  1.00 74.06           O  
ANISOU 2941  O   TRP A 418     7577  14060   6505    465  -1704   -366       O  
ATOM   2942  CB  TRP A 418      -1.484 -28.027 -63.091  1.00 73.32           C  
ANISOU 2942  CB  TRP A 418     7362  14130   6367    542  -1450   -511       C  
ATOM   2943  CG  TRP A 418      -1.774 -28.989 -61.975  1.00 77.01           C  
ANISOU 2943  CG  TRP A 418     7985  14507   6768    345  -1660   -385       C  
ATOM   2944  CD1 TRP A 418      -2.860 -28.990 -61.148  1.00 80.48           C  
ANISOU 2944  CD1 TRP A 418     8463  15002   7115     85  -1604   -262       C  
ATOM   2945  CD2 TRP A 418      -0.963 -30.108 -61.579  1.00 78.81           C  
ANISOU 2945  CD2 TRP A 418     8376  14577   6993    385  -1980   -383       C  
ATOM   2946  NE1 TRP A 418      -2.768 -30.028 -60.247  1.00 81.98           N  
ANISOU 2946  NE1 TRP A 418     8853  15068   7230    -86  -1854   -160       N  
ATOM   2947  CE2 TRP A 418      -1.620 -30.738 -60.499  1.00 84.40           C  
ANISOU 2947  CE2 TRP A 418     9261  15214   7592    112  -2107   -228       C  
ATOM   2948  CE3 TRP A 418       0.277 -30.623 -62.014  1.00 81.05           C  
ANISOU 2948  CE3 TRP A 418     8673  14789   7333    633  -2184   -519       C  
ATOM   2949  CZ2 TRP A 418      -1.095 -31.874 -59.867  1.00 85.76           C  
ANISOU 2949  CZ2 TRP A 418     9684  15189   7710     79  -2453   -182       C  
ATOM   2950  CZ3 TRP A 418       0.800 -31.739 -61.379  1.00 84.44           C  
ANISOU 2950  CZ3 TRP A 418     9314  15046   7722    650  -2535   -501       C  
ATOM   2951  CH2 TRP A 418       0.118 -32.356 -60.323  1.00 86.48           C  
ANISOU 2951  CH2 TRP A 418     9807  15181   7872    376  -2677   -323       C  
ATOM   2952  N   ARG A 419      -4.182 -27.632 -64.565  1.00 66.79           N  
ANISOU 2952  N   ARG A 419     6435  13388   5553    520  -1233   -455       N  
ATOM   2953  CA  ARG A 419      -5.632 -27.637 -64.669  1.00 65.78           C  
ANISOU 2953  CA  ARG A 419     6259  13349   5384    419  -1172   -413       C  
ATOM   2954  C   ARG A 419      -6.063 -28.386 -65.927  1.00 67.11           C  
ANISOU 2954  C   ARG A 419     6440  13431   5628    536  -1293   -429       C  
ATOM   2955  O   ARG A 419      -6.972 -29.216 -65.850  1.00 67.90           O  
ANISOU 2955  O   ARG A 419     6571  13533   5694    384  -1405   -361       O  
ATOM   2956  CB  ARG A 419      -6.183 -26.209 -64.671  1.00 66.24           C  
ANISOU 2956  CB  ARG A 419     6208  13565   5395    473   -909   -482       C  
ATOM   2957  CG  ARG A 419      -6.099 -25.476 -63.335  1.00 75.73           C  
ANISOU 2957  CG  ARG A 419     7391  14881   6501    327   -786   -465       C  
ATOM   2958  CD  ARG A 419      -6.805 -24.128 -63.410  1.00 90.71           C  
ANISOU 2958  CD  ARG A 419     9209  16920   8338    417   -570   -554       C  
ATOM   2959  NE  ARG A 419      -8.206 -24.265 -63.831  1.00106.39           N  
ANISOU 2959  NE  ARG A 419    11096  19033  10293    426   -560   -589       N  
ATOM   2960  CZ  ARG A 419      -9.223 -24.485 -63.004  1.00129.96           C  
ANISOU 2960  CZ  ARG A 419    13982  22220  13177    231   -544   -578       C  
ATOM   2961  NH1 ARG A 419      -9.019 -24.567 -61.695  1.00125.22           N  
ANISOU 2961  NH1 ARG A 419    13392  21693  12494      9   -532   -516       N  
ATOM   2962  NH2 ARG A 419     -10.454 -24.616 -63.479  1.00119.07           N  
ANISOU 2962  NH2 ARG A 419    12481  20996  11763    247   -537   -643       N  
ATOM   2963  N   LEU A 420      -5.365 -28.135 -67.072  1.00 60.46           N  
ANISOU 2963  N   LEU A 420     5583  12521   4870    779  -1276   -523       N  
ATOM   2964  CA  LEU A 420      -5.583 -28.837 -68.338  1.00 58.81           C  
ANISOU 2964  CA  LEU A 420     5390  12219   4737    921  -1397   -554       C  
ATOM   2965  C   LEU A 420      -5.203 -30.288 -68.172  1.00 64.98           C  
ANISOU 2965  C   LEU A 420     6302  12844   5545    878  -1696   -501       C  
ATOM   2966  O   LEU A 420      -5.970 -31.153 -68.595  1.00 65.72           O  
ANISOU 2966  O   LEU A 420     6453  12871   5648    829  -1838   -453       O  
ATOM   2967  CB  LEU A 420      -4.793 -28.182 -69.481  1.00 56.99           C  
ANISOU 2967  CB  LEU A 420     5121  11977   4558   1156  -1300   -675       C  
ATOM   2968  CG  LEU A 420      -4.771 -28.870 -70.856  1.00 59.68           C  
ANISOU 2968  CG  LEU A 420     5473  12227   4975   1332  -1424   -730       C  
ATOM   2969  CD1 LEU A 420      -6.156 -29.087 -71.418  1.00 58.69           C  
ANISOU 2969  CD1 LEU A 420     5333  12109   4858   1319  -1428   -692       C  
ATOM   2970  CD2 LEU A 420      -3.943 -28.079 -71.814  1.00 60.25           C  
ANISOU 2970  CD2 LEU A 420     5508  12331   5052   1499  -1292   -853       C  
ATOM   2971  N   GLY A 421      -4.064 -30.539 -67.505  1.00 61.96           N  
ANISOU 2971  N   GLY A 421     5984  12403   5157    891  -1807   -515       N  
ATOM   2972  CA  GLY A 421      -3.596 -31.881 -67.177  1.00 63.61           C  
ANISOU 2972  CA  GLY A 421     6370  12434   5365    877  -2138   -479       C  
ATOM   2973  C   GLY A 421      -4.683 -32.697 -66.500  1.00 70.71           C  
ANISOU 2973  C   GLY A 421     7419  13267   6180    592  -2271   -324       C  
ATOM   2974  O   GLY A 421      -5.070 -33.756 -67.012  1.00 70.98           O  
ANISOU 2974  O   GLY A 421     7592  13156   6223    582  -2494   -287       O  
ATOM   2975  N   LYS A 422      -5.259 -32.150 -65.388  1.00 69.18           N  
ANISOU 2975  N   LYS A 422     7192  13207   5887    335  -2115   -240       N  
ATOM   2976  CA  LYS A 422      -6.357 -32.777 -64.639  1.00 71.14           C  
ANISOU 2976  CA  LYS A 422     7549  13473   6009    -12  -2187   -104       C  
ATOM   2977  C   LYS A 422      -7.536 -33.103 -65.545  1.00 77.98           C  
ANISOU 2977  C   LYS A 422     8360  14387   6880    -59  -2173    -99       C  
ATOM   2978  O   LYS A 422      -8.046 -34.216 -65.456  1.00 79.73           O  
ANISOU 2978  O   LYS A 422     8767  14496   7030   -266  -2391     -7       O  
ATOM   2979  CB  LYS A 422      -6.854 -31.900 -63.474  1.00 73.10           C  
ANISOU 2979  CB  LYS A 422     7687  13942   6145   -245  -1955    -65       C  
ATOM   2980  CG  LYS A 422      -5.950 -31.844 -62.252  1.00 80.26           C  
ANISOU 2980  CG  LYS A 422     8704  14797   6993   -327  -2013    -23       C  
ATOM   2981  CD  LYS A 422      -6.627 -31.058 -61.117  1.00 94.81           C  
ANISOU 2981  CD  LYS A 422    10439  16876   8707   -586  -1789     16       C  
ATOM   2982  CE  LYS A 422      -5.836 -31.101 -59.824  1.00123.84           C  
ANISOU 2982  CE  LYS A 422    14249  20498  12306   -712  -1863     76       C  
ATOM   2983  NZ  LYS A 422      -6.507 -30.373 -58.706  1.00140.05           N  
ANISOU 2983  NZ  LYS A 422    16198  22794  14222   -971  -1649    107       N  
ATOM   2984  N   VAL A 423      -7.951 -32.149 -66.429  1.00 74.47           N  
ANISOU 2984  N   VAL A 423     7690  14097   6508    129  -1937   -201       N  
ATOM   2985  CA  VAL A 423      -9.093 -32.291 -67.352  1.00 75.13           C  
ANISOU 2985  CA  VAL A 423     7682  14262   6601    129  -1900   -227       C  
ATOM   2986  C   VAL A 423      -8.883 -33.509 -68.271  1.00 82.84           C  
ANISOU 2986  C   VAL A 423     8825  15006   7645    220  -2175   -210       C  
ATOM   2987  O   VAL A 423      -9.775 -34.354 -68.375  1.00 83.17           O  
ANISOU 2987  O   VAL A 423     8946  15033   7622     12  -2301   -146       O  
ATOM   2988  CB  VAL A 423      -9.327 -31.000 -68.189  1.00 77.08           C  
ANISOU 2988  CB  VAL A 423     7717  14658   6914    388  -1642   -355       C  
ATOM   2989  CG1 VAL A 423     -10.344 -31.227 -69.305  1.00 76.99           C  
ANISOU 2989  CG1 VAL A 423     7628  14696   6929    457  -1649   -402       C  
ATOM   2990  CG2 VAL A 423      -9.765 -29.841 -67.301  1.00 76.65           C  
ANISOU 2990  CG2 VAL A 423     7519  14834   6769    302  -1402   -386       C  
ATOM   2991  N   LEU A 424      -7.704 -33.599 -68.910  1.00 82.28           N  
ANISOU 2991  N   LEU A 424     8804  14773   7685    514  -2271   -282       N  
ATOM   2992  CA  LEU A 424      -7.344 -34.681 -69.835  1.00 84.06           C  
ANISOU 2992  CA  LEU A 424     9176  14782   7980    673  -2541   -306       C  
ATOM   2993  C   LEU A 424      -7.203 -36.013 -69.077  1.00 94.95           C  
ANISOU 2993  C   LEU A 424    10860  15942   9273    474  -2881   -195       C  
ATOM   2994  O   LEU A 424      -7.576 -37.059 -69.616  1.00 95.94           O  
ANISOU 2994  O   LEU A 424    11157  15904   9391    441  -3117   -161       O  
ATOM   2995  CB  LEU A 424      -6.040 -34.334 -70.584  1.00 82.39           C  
ANISOU 2995  CB  LEU A 424     8900  14526   7877   1031  -2535   -449       C  
ATOM   2996  CG  LEU A 424      -6.075 -33.071 -71.457  1.00 83.72           C  
ANISOU 2996  CG  LEU A 424     8847  14860   8102   1212  -2234   -554       C  
ATOM   2997  CD1 LEU A 424      -4.704 -32.617 -71.807  1.00 82.75           C  
ANISOU 2997  CD1 LEU A 424     8663  14752   8025   1443  -2194   -685       C  
ATOM   2998  CD2 LEU A 424      -6.920 -33.265 -72.691  1.00 85.30           C  
ANISOU 2998  CD2 LEU A 424     9008  15055   8348   1302  -2231   -580       C  
ATOM   2999  N   TRP A 425      -6.708 -35.964 -67.816  1.00 95.69           N  
ANISOU 2999  N   TRP A 425    11053  16019   9287    326  -2918   -135       N  
ATOM   3000  CA  TRP A 425      -6.591 -37.137 -66.953  1.00100.11           C  
ANISOU 3000  CA  TRP A 425    11956  16354   9727    105  -3250    -18       C  
ATOM   3001  C   TRP A 425      -7.975 -37.756 -66.680  1.00108.49           C  
ANISOU 3001  C   TRP A 425    13139  17440  10644   -315  -3291    122       C  
ATOM   3002  O   TRP A 425      -8.088 -38.985 -66.651  1.00110.84           O  
ANISOU 3002  O   TRP A 425    13770  17487  10858   -457  -3622    205       O  
ATOM   3003  CB  TRP A 425      -5.895 -36.778 -65.634  1.00100.04           C  
ANISOU 3003  CB  TRP A 425    12000  16364   9648     13  -3233     16       C  
ATOM   3004  CG  TRP A 425      -6.085 -37.800 -64.551  1.00104.79           C  
ANISOU 3004  CG  TRP A 425    12969  16773  10072   -323  -3518    171       C  
ATOM   3005  CD1 TRP A 425      -6.955 -37.721 -63.503  1.00108.79           C  
ANISOU 3005  CD1 TRP A 425    13525  17405  10407   -765  -3416    307       C  
ATOM   3006  CD2 TRP A 425      -5.552 -39.132 -64.529  1.00107.41           C  
ANISOU 3006  CD2 TRP A 425    13707  16751  10353   -274  -3974    202       C  
ATOM   3007  NE1 TRP A 425      -6.924 -38.886 -62.772  1.00111.38           N  
ANISOU 3007  NE1 TRP A 425    14284  17468  10568  -1028  -3769    439       N  
ATOM   3008  CE2 TRP A 425      -6.069 -39.770 -63.377  1.00113.87           C  
ANISOU 3008  CE2 TRP A 425    14848  17462  10955   -720  -4132    380       C  
ATOM   3009  CE3 TRP A 425      -4.656 -39.841 -65.349  1.00109.56           C  
ANISOU 3009  CE3 TRP A 425    14116  16790  10724    114  -4280     80       C  
ATOM   3010  CZ2 TRP A 425      -5.705 -41.072 -63.015  1.00116.37           C  
ANISOU 3010  CZ2 TRP A 425    15668  17399  11147   -788  -4604    457       C  
ATOM   3011  CZ3 TRP A 425      -4.303 -41.134 -64.991  1.00114.27           C  
ANISOU 3011  CZ3 TRP A 425    15180  17027  11209     89  -4754    132       C  
ATOM   3012  CH2 TRP A 425      -4.822 -41.736 -63.838  1.00117.20           C  
ANISOU 3012  CH2 TRP A 425    15917  17252  11362   -358  -4923    327       C  
ATOM   3013  N   GLU A 426      -9.021 -36.907 -66.481  1.00105.55           N  
ANISOU 3013  N   GLU A 426    12503  17380  10222   -515  -2968    130       N  
ATOM   3014  CA  GLU A 426     -10.403 -37.360 -66.232  1.00107.53           C  
ANISOU 3014  CA  GLU A 426    12780  17764  10312   -937  -2953    220       C  
ATOM   3015  C   GLU A 426     -10.998 -37.984 -67.509  1.00112.04           C  
ANISOU 3015  C   GLU A 426    13362  18266  10941   -858  -3059    188       C  
ATOM   3016  O   GLU A 426     -11.835 -38.887 -67.429  1.00112.86           O  
ANISOU 3016  O   GLU A 426    13638  18338  10905  -1204  -3209    277       O  
ATOM   3017  CB  GLU A 426     -11.310 -36.203 -65.733  1.00108.36           C  
ANISOU 3017  CB  GLU A 426    12544  18279  10350  -1096  -2582    174       C  
ATOM   3018  CG  GLU A 426     -10.770 -35.343 -64.591  1.00119.53           C  
ANISOU 3018  CG  GLU A 426    13884  19804  11726  -1122  -2420    177       C  
ATOM   3019  CD  GLU A 426     -10.400 -35.973 -63.258  1.00146.24           C  
ANISOU 3019  CD  GLU A 426    17555  23062  14949  -1444  -2596    314       C  
ATOM   3020  OE1 GLU A 426     -10.908 -37.073 -62.939  1.00152.66           O  
ANISOU 3020  OE1 GLU A 426    18636  23766  15600  -1807  -2816    434       O  
ATOM   3021  OE2 GLU A 426      -9.659 -35.313 -62.492  1.00135.04           O  
ANISOU 3021  OE2 GLU A 426    16099  21666  13543  -1364  -2505    304       O  
ATOM   3022  N   GLU A 427     -10.556 -37.485 -68.683  1.00108.10           N  
ANISOU 3022  N   GLU A 427    12688  17752  10633   -426  -2978     59       N  
ATOM   3023  CA  GLU A 427     -10.970 -37.953 -70.004  1.00108.70           C  
ANISOU 3023  CA  GLU A 427    12752  17759  10790   -273  -3063      7       C  
ATOM   3024  C   GLU A 427     -10.363 -39.336 -70.288  1.00116.72           C  
ANISOU 3024  C   GLU A 427    14143  18398  11806   -226  -3476     56       C  
ATOM   3025  O   GLU A 427     -11.039 -40.184 -70.883  1.00117.54           O  
ANISOU 3025  O   GLU A 427    14380  18409  11873   -346  -3641     91       O  
ATOM   3026  CB  GLU A 427     -10.550 -36.932 -71.083  1.00107.42           C  
ANISOU 3026  CB  GLU A 427    12322  17688  10805    164  -2851   -146       C  
ATOM   3027  CG  GLU A 427     -11.020 -37.257 -72.496  1.00116.25           C  
ANISOU 3027  CG  GLU A 427    13394  18768  12008    340  -2901   -212       C  
ATOM   3028  CD  GLU A 427     -10.694 -36.237 -73.575  1.00133.84           C  
ANISOU 3028  CD  GLU A 427    15395  21086  14372    723  -2692   -352       C  
ATOM   3029  OE1 GLU A 427      -9.746 -35.440 -73.389  1.00110.57           O  
ANISOU 3029  OE1 GLU A 427    12379  18159  11475    908  -2568   -409       O  
ATOM   3030  OE2 GLU A 427     -11.350 -36.280 -74.641  1.00137.62           O  
ANISOU 3030  OE2 GLU A 427    15793  21602  14895    826  -2671   -406       O  
ATOM   3031  N   ARG A 428      -9.088 -39.556 -69.856  1.00115.26           N  
ANISOU 3031  N   ARG A 428    14134  18007  11654    -37  -3658     42       N  
ATOM   3032  CA  ARG A 428      -8.341 -40.817 -70.012  1.00117.74           C  
ANISOU 3032  CA  ARG A 428    14826  17951  11957     85  -4094     50       C  
ATOM   3033  C   ARG A 428      -9.133 -42.019 -69.442  1.00125.64           C  
ANISOU 3033  C   ARG A 428    16223  18756  12756   -365  -4379    221       C  
ATOM   3034  O   ARG A 428      -9.221 -43.071 -70.085  1.00127.17           O  
ANISOU 3034  O   ARG A 428    16690  18693  12935   -330  -4689    232       O  
ATOM   3035  CB  ARG A 428      -6.964 -40.724 -69.311  1.00119.09           C  
ANISOU 3035  CB  ARG A 428    15090  18008  12149    301  -4219     -5       C  
ATOM   3036  CG  ARG A 428      -6.206 -42.055 -69.304  1.00135.74           C  
ANISOU 3036  CG  ARG A 428    17629  19731  14215    444  -4723    -18       C  
ATOM   3037  CD  ARG A 428      -4.941 -42.070 -68.467  1.00147.43           C  
ANISOU 3037  CD  ARG A 428    19229  21109  15680    629  -4894    -80       C  
ATOM   3038  NE  ARG A 428      -4.390 -43.428 -68.407  1.00158.32           N  
ANISOU 3038  NE  ARG A 428    21079  22093  16982    753  -5431    -94       N  
ATOM   3039  CZ  ARG A 428      -3.263 -43.763 -67.787  1.00174.50           C  
ANISOU 3039  CZ  ARG A 428    23323  23981  18999    976  -5717   -178       C  
ATOM   3040  NH1 ARG A 428      -2.529 -42.837 -67.182  1.00164.03           N  
ANISOU 3040  NH1 ARG A 428    21737  22871  17717   1081  -5497   -254       N  
ATOM   3041  NH2 ARG A 428      -2.848 -45.023 -67.789  1.00162.08           N  
ANISOU 3041  NH2 ARG A 428    22217  22026  17341   1116  -6243   -204       N  
ATOM   3042  N   ASN A 429      -9.687 -41.854 -68.234  1.00123.21           N  
ANISOU 3042  N   ASN A 429    15963  18574  12276   -802  -4277    350       N  
ATOM   3043  CA  ASN A 429     -10.434 -42.894 -67.540  1.00155.32           C  
ANISOU 3043  CA  ASN A 429    20418  22498  16100  -1322  -4513    522       C  
ATOM   3044  C   ASN A 429     -11.941 -42.651 -67.674  1.00183.05           C  
ANISOU 3044  C   ASN A 429    23696  26346  19507  -1723  -4251    558       C  
ATOM   3045  O   ASN A 429     -12.448 -42.483 -68.784  1.00141.94           O  
ANISOU 3045  O   ASN A 429    18261  21255  14414  -1558  -4139    469       O  
ATOM   3046  CB  ASN A 429     -10.015 -42.926 -66.061  1.00157.05           C  
ANISOU 3046  CB  ASN A 429    20863  22653  16158  -1577  -4589    630       C  
ATOM   3047  CG  ASN A 429      -8.532 -43.159 -65.821  1.00173.80           C  
ANISOU 3047  CG  ASN A 429    23201  24476  18359  -1182  -4864    571       C  
ATOM   3048  OD1 ASN A 429      -7.799 -43.695 -66.665  1.00168.28           O  
ANISOU 3048  OD1 ASN A 429    22627  23532  17781   -777  -5127    466       O  
ATOM   3049  ND2 ASN A 429      -8.071 -42.804 -64.634  1.00162.78           N  
ANISOU 3049  ND2 ASN A 429    21858  23111  16880  -1297  -4828    620       N  
TER    3050      ASN A 429                                                      
HETATM 3051  C1  PEG A1200       9.491  -3.620 -57.167  1.00 74.79           C  
HETATM 3052  O1  PEG A1200       8.868  -2.350 -57.061  1.00 74.85           O  
HETATM 3053  C2  PEG A1200       9.077  -4.348 -58.417  1.00 73.96           C  
HETATM 3054  O2  PEG A1200       9.735  -5.610 -58.495  1.00 73.87           O  
HETATM 3055  C3  PEG A1200      10.501  -5.768 -59.685  1.00 72.77           C  
HETATM 3056  C4  PEG A1200      11.009  -7.180 -59.816  1.00 70.17           C  
HETATM 3057  O4  PEG A1200      11.860  -7.550 -58.747  1.00 67.41           O  
CONECT 1461 1948                                                                
CONECT 1948 1461                                                                
CONECT 3051 3052 3053                                                           
CONECT 3052 3051                                                                
CONECT 3053 3051 3054                                                           
CONECT 3054 3053 3055                                                           
CONECT 3055 3054 3056                                                           
CONECT 3056 3055 3057                                                           
CONECT 3057 3056                                                                
MASTER      376    0    1   24    0    0    1    6 3056    1    9   33          
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.