CNRS Nantes University UFIP UFIP
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***  TRANSFERASE 17-SEP-15 5DT0  ***

elNémo ID: 22013104163646826

Job options:

ID        	=	 22013104163646826
JOBID     	=	 TRANSFERASE 17-SEP-15 5DT0
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    TRANSFERASE                             17-SEP-15   5DT0              
TITLE     AURORA A KINASE IN COMPLEX WITH JNJ-7706621 IN SPACE GROUP P6122      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: AURORA KINASE A;                                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 126-390;                                      
COMPND   5 SYNONYM: AURORA 2,AURORA/IPL1-RELATED KINASE 1,HARK1,BREAST TUMOR-   
COMPND   6 AMPLIFIED KINASE,SERINE/THREONINE-PROTEIN KINASE 15,SERINE/THREONINE-
COMPND   7 PROTEIN KINASE 6,SERINE/THREONINE-PROTEIN KINASE AURORA-A;           
COMPND   8 EC: 2.7.11.1;                                                        
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: AURKA, AIK, AIRK1, ARK1, AURA, AYK1, BTAK, IAK1, STK15, STK6;  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: PUBS520;                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PBAT4                                     
KEYWDS    AURORA A KINASE, MITOTIC KINASE, PPI, TRANSFERASE                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.JANECEK,M.ROSSMANN,P.SHARMA,A.EMERY,G.J.MCKENZIE,D.J.HUGGINS,       
AUTHOR   2 S.STOCKWELL,J.A.STOKES,E.G.ALMEIDA,B.HARDWICK,A.J.NARVAEZ,M.HYVONEN, 
AUTHOR   3 D.R.SPRING,A.R.VENKITARAMAN                                          
REVDAT   1   20-JUL-16 5DT0    0                                                
JRNL        AUTH   M.JANECEK,M.ROSSMANN,P.SHARMA,A.EMERY,D.J.HUGGINS,           
JRNL        AUTH 2 S.R.STOCKWELL,J.E.STOKES,Y.S.TAN,E.G.ALMEIDA,B.HARDWICK,     
JRNL        AUTH 3 A.J.NARVAEZ,M.HYVONEN,D.R.SPRING,G.J.MCKENZIE,               
JRNL        AUTH 4 A.R.VENKITARAMAN                                             
JRNL        TITL   ALLOSTERIC MODULATION OF AURKA KINASE ACTIVITY BY A          
JRNL        TITL 2 SMALL-MOLECULE INHIBITOR OF ITS PROTEIN-PROTEIN INTERACTION  
JRNL        TITL 3 WITH TPX2.                                                   
JRNL        REF    SCI REP                       V.   6 28528 2016              
JRNL        REFN                   ESSN 2045-2322                               
JRNL        PMID   27339427                                                     
JRNL        DOI    10.1038/SREP28528                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.1                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 70.79                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 18428                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : FREE R-VALUE                   
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.211                          
REMARK   3   R VALUE            (WORKING SET)  : 0.210                          
REMARK   3   FREE R VALUE                      : 0.225                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.010                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 924                            
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               : 9                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.15                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.28                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 100.0                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2894                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2151                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2749                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2142                   
REMARK   3   BIN FREE R VALUE                        : 0.2327                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.01                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 145                      
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            : 2120                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 27                                      
REMARK   3   SOLVENT ATOMS            : 102                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 60.11                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 66.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.40620                                              
REMARK   3    B22 (A**2) : 2.40620                                              
REMARK   3    B33 (A**2) : -4.81250                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : NULL                
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.235               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.172               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.221               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.169               
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      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.944                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 2215   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 2999   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 777    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 49     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 320    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 2215   ; 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   : 268    ; 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   : 2525   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.16                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.04                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 19.81                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -17.1134  -32.3436    7.9763           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0668 T22:   -0.1310                                    
REMARK   3     T33:   -0.1743 T12:    0.0379                                    
REMARK   3     T13:    0.0111 T23:    0.0030                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.9452 L22:    3.5163                                    
REMARK   3     L33:    1.4606 L12:    0.7119                                    
REMARK   3     L13:    0.9971 L23:    1.5539                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0554 S12:   -0.2618 S13:    0.0259                     
REMARK   3     S21:   -0.1810 S22:    0.0367 S23:    0.2648                     
REMARK   3     S31:   -0.1180 S32:   -0.0940 S33:    0.0186                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5DT0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-SEP-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000213511.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-MAY-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9184                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS (VERSION MARCH 1, AUTOPROC     
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS (VERSION 0.3.11)           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18585                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.146                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 70.790                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 18.40                              
REMARK 200  R MERGE                    (I) : 0.07900                            
REMARK 200  R SYM                      (I) : 0.07900                            
REMARK 200   FOR THE DATA SET  : 18.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 19.60                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.14700                            
REMARK 200  R SYM FOR SHELL            (I) : 1.14700                            
REMARK 200   FOR SHELL         : 2.000                              
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: 3FDN                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.46                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES PH 7.4, 200 MM MAGNESIUM    
REMARK 280  SULFATE, 2-20% PEG3350, VAPOR DIFFUSION, SITTING DROP,              
REMARK 280  TEMPERATURE 292K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       54.87067            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      109.74133            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       82.30600            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      137.17667            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       27.43533            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       54.87067            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      109.74133            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      137.17667            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       82.30600            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       27.43533            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 12700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
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     MET A   124                                                      
REMARK 465     GLY A   125                                                      
REMARK 465     ARG A   126                                                      
REMARK 465     ARG A   285                                                      
REMARK 465     ARG A   286                                                      
REMARK 465     ALA A   287                                                      
REMARK 465     THR A   288                                                      
REMARK 465     LEU A   289                                                      
REMARK 465     HIS A   391                                                      
REMARK 465     HIS A   392                                                      
REMARK 465     HIS A   393                                                      
REMARK 465     HIS A   394                                                      
REMARK 465     HIS A   395                                                      
REMARK 465     HIS A   396                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH1  ARG A   179     O    HOH A   501              0.39            
REMARK 500   NH1  ARG A   180     OE1  GLU A   183              1.00            
REMARK 500   CZ   ARG A   179     O    HOH A   501              1.06            
REMARK 500   OE1  GLU A   302     NH2  ARG A   304              1.57            
REMARK 500   CZ   ARG A   180     OE1  GLU A   183              1.75            
REMARK 500   NH2  ARG A   179     O    HOH A   501              1.91            
REMARK 500   NH1  ARG A   180     CD   GLU A   183              2.04            
REMARK 500   NE   ARG A   179     O    HOH A   501              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CE   MET A   305     CE   MET A   305    12555     1.52            
REMARK 500   CE   LYS A   143     OE1  GLN A   154     5554     1.63            
REMARK 500   OE1  GLU A   175     NH2  ARG A   179    12555     1.98            
REMARK 500   NZ   LYS A   143     OE1  GLN A   154     5554     2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 226      -52.37     73.86                                   
REMARK 500    ARG A 251       10.75     56.93                                   
REMARK 500    ASP A 256       28.86   -143.89                                   
REMARK 500    ASP A 294      -37.40    -37.39                                   
REMARK 500    ASP A 307     -142.74   -138.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 602        DISTANCE = 12.38 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SKE A 401                 
DBREF  5DT0 A  126   390  UNP    O14965   AURKA_HUMAN    126    390             
SEQADV 5DT0 MET A  124  UNP  O14965              INITIATING METHIONINE          
SEQADV 5DT0 GLY A  125  UNP  O14965              EXPRESSION TAG                 
SEQADV 5DT0 ALA A  287  UNP  O14965    THR   287 CONFLICT                       
SEQADV 5DT0 HIS A  391  UNP  O14965              EXPRESSION TAG                 
SEQADV 5DT0 HIS A  392  UNP  O14965              EXPRESSION TAG                 
SEQADV 5DT0 HIS A  393  UNP  O14965              EXPRESSION TAG                 
SEQADV 5DT0 HIS A  394  UNP  O14965              EXPRESSION TAG                 
SEQADV 5DT0 HIS A  395  UNP  O14965              EXPRESSION TAG                 
SEQADV 5DT0 HIS A  396  UNP  O14965              EXPRESSION TAG                 
SEQRES   1 A  273  MET GLY ARG GLN TRP ALA LEU GLU ASP PHE GLU ILE GLY          
SEQRES   2 A  273  ARG PRO LEU GLY LYS GLY LYS PHE GLY ASN VAL TYR LEU          
SEQRES   3 A  273  ALA ARG GLU LYS GLN SER LYS PHE ILE LEU ALA LEU LYS          
SEQRES   4 A  273  VAL LEU PHE LYS ALA GLN LEU GLU LYS ALA GLY VAL GLU          
SEQRES   5 A  273  HIS GLN LEU ARG ARG GLU VAL GLU ILE GLN SER HIS LEU          
SEQRES   6 A  273  ARG HIS PRO ASN ILE LEU ARG LEU TYR GLY TYR PHE HIS          
SEQRES   7 A  273  ASP ALA THR ARG VAL TYR LEU ILE LEU GLU TYR ALA PRO          
SEQRES   8 A  273  LEU GLY THR VAL TYR ARG GLU LEU GLN LYS LEU SER LYS          
SEQRES   9 A  273  PHE ASP GLU GLN ARG THR ALA THR TYR ILE THR GLU LEU          
SEQRES  10 A  273  ALA ASN ALA LEU SER TYR CYS HIS SER LYS ARG VAL ILE          
SEQRES  11 A  273  HIS ARG ASP ILE LYS PRO GLU ASN LEU LEU LEU GLY SER          
SEQRES  12 A  273  ALA GLY GLU LEU LYS ILE ALA ASP PHE GLY TRP SER VAL          
SEQRES  13 A  273  HIS ALA PRO SER SER ARG ARG ALA THR LEU CYS GLY THR          
SEQRES  14 A  273  LEU ASP TYR LEU PRO PRO GLU MET ILE GLU GLY ARG MET          
SEQRES  15 A  273  HIS ASP GLU LYS VAL ASP LEU TRP SER LEU GLY VAL LEU          
SEQRES  16 A  273  CYS TYR GLU PHE LEU VAL GLY LYS PRO PRO PHE GLU ALA          
SEQRES  17 A  273  ASN THR TYR GLN GLU THR TYR LYS ARG ILE SER ARG VAL          
SEQRES  18 A  273  GLU PHE THR PHE PRO ASP PHE VAL THR GLU GLY ALA ARG          
SEQRES  19 A  273  ASP LEU ILE SER ARG LEU LEU LYS HIS ASN PRO SER GLN          
SEQRES  20 A  273  ARG PRO MET LEU ARG GLU VAL LEU GLU HIS PRO TRP ILE          
SEQRES  21 A  273  THR ALA ASN SER SER LYS PRO HIS HIS HIS HIS HIS HIS          
HET    SKE  A 401      27                                                       
HETNAM     SKE 4-({5-AMINO-1-[(2,6-DIFLUOROPHENYL)CARBONYL]-1H-1,2,4-           
HETNAM   2 SKE  TRIAZOL-3-YL}AMINO)BENZENESULFONAMIDE                           
FORMUL   2  SKE    C15 H12 F2 N6 O3 S                                           
FORMUL   3  HOH   *102(H2 O)                                                    
HELIX    1 AA1 ALA A  129  GLU A  131  5                                   3    
HELIX    2 AA2 LYS A  166  GLY A  173  1                                   8    
HELIX    3 AA3 VAL A  174  LEU A  188  1                                  15    
HELIX    4 AA4 THR A  217  SER A  226  1                                  10    
HELIX    5 AA5 ASP A  229  SER A  249  1                                  21    
HELIX    6 AA6 LYS A  258  GLU A  260  5                                   3    
HELIX    7 AA7 ASP A  274  SER A  278  5                                   5    
HELIX    8 AA8 PRO A  297  GLU A  302  1                                   6    
HELIX    9 AA9 GLU A  308  GLY A  325  1                                  18    
HELIX   10 AB1 THR A  333  ARG A  343  1                                  11    
HELIX   11 AB2 THR A  353  LEU A  364  1                                  12    
HELIX   12 AB3 ASN A  367  ARG A  371  5                                   5    
HELIX   13 AB4 MET A  373  GLU A  379  1                                   7    
HELIX   14 AB5 HIS A  380  SER A  387  1                                   8    
SHEET    1 AA1 5 PHE A 133  GLY A 140  0                                        
SHEET    2 AA1 5 GLY A 145  GLU A 152 -1  O  LEU A 149   N  GLY A 136           
SHEET    3 AA1 5 ILE A 158  PHE A 165 -1  O  VAL A 163   N  ASN A 146           
SHEET    4 AA1 5 ARG A 205  LEU A 210 -1  O  LEU A 210   N  ALA A 160           
SHEET    5 AA1 5 LEU A 196  HIS A 201 -1  N  PHE A 200   O  TYR A 207           
SHEET    1 AA2 2 VAL A 252  ILE A 253  0                                        
SHEET    2 AA2 2 VAL A 279  HIS A 280 -1  O  VAL A 279   N  ILE A 253           
SHEET    1 AA3 2 LEU A 262  LEU A 264  0                                        
SHEET    2 AA3 2 LEU A 270  ILE A 272 -1  O  LYS A 271   N  LEU A 263           
CISPEP   1 ALA A  281    PRO A  282          0         1.27                     
SITE     1 AC1 14 ARG A 137  LEU A 139  GLY A 140  VAL A 147                    
SITE     2 AC1 14 ALA A 160  LEU A 210  GLU A 211  ALA A 213                    
SITE     3 AC1 14 GLY A 216  ARG A 220  GLU A 260  LEU A 263                    
SITE     4 AC1 14 ALA A 273  HOH A 522                                          
CRYST1   81.741   81.741  164.612  90.00  90.00 120.00 P 61 2 2     12          
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      0.012234  0.007063  0.000000        0.00000                         
SCALE2      0.000000  0.014126  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006075        0.00000                         
ATOM      1  N   GLN A 127       1.760 -16.127  25.297  1.00 88.30           N  
ANISOU    1  N   GLN A 127    10453  11767  11329    922   -944  -3417       N  
ATOM      2  CA  GLN A 127       1.469 -17.555  25.204  1.00 87.04           C  
ANISOU    2  CA  GLN A 127    10402  11718  10951    938   -937  -3174       C  
ATOM      3  C   GLN A 127       1.934 -18.158  23.860  1.00 90.60           C  
ANISOU    3  C   GLN A 127    10825  12004  11592    841   -821  -3012       C  
ATOM      4  O   GLN A 127       2.685 -19.139  23.873  1.00 91.29           O  
ANISOU    4  O   GLN A 127    10884  12109  11692    859   -908  -2970       O  
ATOM      5  CB  GLN A 127      -0.029 -17.842  25.487  1.00 87.37           C  
ANISOU    5  CB  GLN A 127    10588  11911  10697    966   -847  -3024       C  
ATOM      6  CG  GLN A 127      -0.499 -19.292  25.250  1.00 99.60           C  
ANISOU    6  CG  GLN A 127    12257  13544  12043    959   -811  -2745       C  
ATOM      7  CD  GLN A 127       0.004 -20.291  26.271  1.00124.52           C  
ANISOU    7  CD  GLN A 127    15469  16857  14985   1026  -1000  -2717       C  
ATOM      8  OE1 GLN A 127      -0.629 -20.536  27.303  1.00124.01           O  
ANISOU    8  OE1 GLN A 127    15512  16994  14613   1068  -1048  -2701       O  
ATOM      9  NE2 GLN A 127       1.120 -20.941  25.975  1.00117.98           N  
ANISOU    9  NE2 GLN A 127    14579  15938  14311   1028  -1110  -2703       N  
ATOM     10  N   TRP A 128       1.470 -17.593  22.711  1.00 84.33           N  
ANISOU   10  N   TRP A 128    10050  11053  10941    740   -637  -2928       N  
ATOM     11  CA  TRP A 128       1.815 -18.093  21.374  1.00 80.98           C  
ANISOU   11  CA  TRP A 128     9622  10489  10658    629   -499  -2781       C  
ATOM     12  C   TRP A 128       2.243 -17.022  20.398  1.00 78.87           C  
ANISOU   12  C   TRP A 128     9298  10006  10665    493   -374  -2847       C  
ATOM     13  O   TRP A 128       1.566 -15.999  20.264  1.00 78.79           O  
ANISOU   13  O   TRP A 128     9333   9913  10690    470   -332  -2861       O  
ATOM     14  CB  TRP A 128       0.650 -18.900  20.769  1.00 78.77           C  
ANISOU   14  CB  TRP A 128     9490  10252  10187    619   -390  -2517       C  
ATOM     15  CG  TRP A 128       0.447 -20.265  21.361  1.00 79.26           C  
ANISOU   15  CG  TRP A 128     9611  10478  10026    701   -478  -2394       C  
ATOM     16  CD1 TRP A 128      -0.712 -20.774  21.878  1.00 81.59           C  
ANISOU   16  CD1 TRP A 128    10025  10919  10058    758   -480  -2259       C  
ATOM     17  CD2 TRP A 128       1.441 -21.290  21.512  1.00 79.27           C  
ANISOU   17  CD2 TRP A 128     9552  10499  10067    729   -586  -2400       C  
ATOM     18  NE1 TRP A 128      -0.503 -22.062  22.327  1.00 81.12           N  
ANISOU   18  NE1 TRP A 128    10006  10961   9856    805   -580  -2151       N  
ATOM     19  CE2 TRP A 128       0.814 -22.395  22.128  1.00 82.77           C  
ANISOU   19  CE2 TRP A 128    10107  11088  10254    800   -666  -2238       C  
ATOM     20  CE3 TRP A 128       2.805 -21.375  21.193  1.00 81.57           C  
ANISOU   20  CE3 TRP A 128     9694  10690  10609    696   -628  -2538       C  
ATOM     21  CZ2 TRP A 128       1.502 -23.568  22.425  1.00 82.73           C  
ANISOU   21  CZ2 TRP A 128    10087  11108  10237    850   -813  -2193       C  
ATOM     22  CZ3 TRP A 128       3.492 -22.532  21.507  1.00 83.69           C  
ANISOU   22  CZ3 TRP A 128     9921  10996  10882    759   -774  -2527       C  
ATOM     23  CH2 TRP A 128       2.842 -23.613  22.111  1.00 84.08           C  
ANISOU   23  CH2 TRP A 128    10100  11169  10675    840   -879  -2347       C  
ATOM     24  N   ALA A 129       3.350 -17.280  19.692  1.00 71.69           N  
ANISOU   24  N   ALA A 129     8289   8996   9954    395   -312  -2886       N  
ATOM     25  CA  ALA A 129       3.927 -16.406  18.661  1.00 71.34           C  
ANISOU   25  CA  ALA A 129     8196   8747  10165    221   -161  -2931       C  
ATOM     26  C   ALA A 129       4.427 -17.234  17.451  1.00 72.65           C  
ANISOU   26  C   ALA A 129     8356   8858  10388     93      5  -2821       C  
ATOM     27  O   ALA A 129       4.771 -18.402  17.613  1.00 71.75           O  
ANISOU   27  O   ALA A 129     8195   8846  10221    159    -47  -2808       O  
ATOM     28  CB  ALA A 129       5.074 -15.590  19.243  1.00 73.90           C  
ANISOU   28  CB  ALA A 129     8333   9005  10739    205   -246  -3210       C  
ATOM     29  N   LEU A 130       4.489 -16.617  16.255  1.00 67.97           N  
ANISOU   29  N   LEU A 130     7817   8102   9906    -93    196  -2752       N  
ATOM     30  CA  LEU A 130       4.959 -17.269  15.034  1.00 67.52           C  
ANISOU   30  CA  LEU A 130     7766   8001   9889   -243    386  -2673       C  
ATOM     31  C   LEU A 130       6.407 -17.785  15.143  1.00 70.64           C  
ANISOU   31  C   LEU A 130     7927   8414  10500   -272    394  -2891       C  
ATOM     32  O   LEU A 130       6.731 -18.828  14.578  1.00 69.06           O  
ANISOU   32  O   LEU A 130     7690   8259  10291   -297    472  -2864       O  
ATOM     33  CB  LEU A 130       4.765 -16.338  13.823  1.00 68.23           C  
ANISOU   33  CB  LEU A 130     7985   7910  10030   -458    577  -2561       C  
ATOM     34  CG  LEU A 130       4.870 -16.967  12.417  1.00 72.87           C  
ANISOU   34  CG  LEU A 130     8661   8469  10557   -627    795  -2425       C  
ATOM     35  CD1 LEU A 130       3.905 -18.116  12.235  1.00 71.06           C  
ANISOU   35  CD1 LEU A 130     8556   8361  10081   -514    760  -2239       C  
ATOM     36  CD2 LEU A 130       4.614 -15.941  11.364  1.00 76.97           C  
ANISOU   36  CD2 LEU A 130     9350   8807  11087   -839    943  -2296       C  
ATOM     37  N   GLU A 131       7.244 -17.095  15.931  1.00 67.20           N  
ANISOU   37  N   GLU A 131     7318   7946  10271   -249    289  -3128       N  
ATOM     38  CA  GLU A 131       8.638 -17.461  16.179  1.00 68.30           C  
ANISOU   38  CA  GLU A 131     7199   8088  10662   -256    253  -3381       C  
ATOM     39  C   GLU A 131       8.788 -18.784  16.969  1.00 68.66           C  
ANISOU   39  C   GLU A 131     7179   8285  10625    -53     42  -3409       C  
ATOM     40  O   GLU A 131       9.902 -19.247  17.176  1.00 68.18           O  
ANISOU   40  O   GLU A 131     6901   8223  10782    -31    -27  -3617       O  
ATOM     41  CB  GLU A 131       9.385 -16.308  16.881  1.00 72.09           C  
ANISOU   41  CB  GLU A 131     7519   8486  11386   -272    163  -3629       C  
ATOM     42  CG  GLU A 131       8.658 -15.698  18.070  1.00 85.63           C  
ANISOU   42  CG  GLU A 131     9314  10256  12964   -105    -57  -3641       C  
ATOM     43  CD  GLU A 131       9.493 -14.743  18.901  1.00118.22           C  
ANISOU   43  CD  GLU A 131    13257  14323  17339    -87   -193  -3930       C  
ATOM     44  OE1 GLU A 131       9.668 -15.016  20.111  1.00127.94           O  
ANISOU   44  OE1 GLU A 131    14420  15675  18515    100   -447  -4067       O  
ATOM     45  OE2 GLU A 131       9.987 -13.735  18.345  1.00109.57           O  
ANISOU   45  OE2 GLU A 131    12089  13055  16487   -268    -51  -4019       O  
ATOM     46  N   ASP A 132       7.671 -19.362  17.439  1.00 63.06           N  
ANISOU   46  N   ASP A 132     6652   7691   9617     91    -72  -3208       N  
ATOM     47  CA  ASP A 132       7.688 -20.619  18.194  1.00 62.13           C  
ANISOU   47  CA  ASP A 132     6520   7699   9386    268   -281  -3184       C  
ATOM     48  C   ASP A 132       7.615 -21.813  17.241  1.00 61.32           C  
ANISOU   48  C   ASP A 132     6444   7599   9256    227   -163  -3052       C  
ATOM     49  O   ASP A 132       7.843 -22.940  17.660  1.00 61.65           O  
ANISOU   49  O   ASP A 132     6442   7700   9281    348   -324  -3050       O  
ATOM     50  CB  ASP A 132       6.489 -20.666  19.176  1.00 62.15           C  
ANISOU   50  CB  ASP A 132     6711   7832   9070    414   -435  -3029       C  
ATOM     51  CG  ASP A 132       6.547 -19.642  20.306  1.00 71.44           C  
ANISOU   51  CG  ASP A 132     7858   9042  10244    488   -590  -3191       C  
ATOM     52  OD1 ASP A 132       7.576 -19.596  21.023  1.00 72.30           O  
ANISOU   52  OD1 ASP A 132     7804   9155  10513    549   -765  -3413       O  
ATOM     53  OD2 ASP A 132       5.531 -18.962  20.535  1.00 73.72           O  
ANISOU   53  OD2 ASP A 132     8281   9361  10367    500   -559  -3108       O  
ATOM     54  N   PHE A 133       7.258 -21.560  15.977  1.00 56.22           N  
ANISOU   54  N   PHE A 133     5885   6882   8595     59    100  -2940       N  
ATOM     55  CA  PHE A 133       7.049 -22.581  14.955  1.00 57.06           C  
ANISOU   55  CA  PHE A 133     6042   6993   8645      2    240  -2816       C  
ATOM     56  C   PHE A 133       7.983 -22.511  13.751  1.00 66.03           C  
ANISOU   56  C   PHE A 133     7050   8043   9997   -197    489  -2951       C  
ATOM     57  O   PHE A 133       8.302 -21.431  13.250  1.00 65.46           O  
ANISOU   57  O   PHE A 133     6965   7881  10025   -367    657  -3013       O  
ATOM     58  CB  PHE A 133       5.588 -22.545  14.466  1.00 56.73           C  
ANISOU   58  CB  PHE A 133     6261   6973   8322    -15    323  -2533       C  
ATOM     59  CG  PHE A 133       4.583 -22.609  15.592  1.00 57.76           C  
ANISOU   59  CG  PHE A 133     6510   7203   8234    155    125  -2411       C  
ATOM     60  CD1 PHE A 133       4.328 -23.808  16.254  1.00 59.91           C  
ANISOU   60  CD1 PHE A 133     6799   7575   8387    302    -43  -2335       C  
ATOM     61  CD2 PHE A 133       3.930 -21.456  16.032  1.00 59.42           C  
ANISOU   61  CD2 PHE A 133     6807   7403   8368    162    106  -2390       C  
ATOM     62  CE1 PHE A 133       3.426 -23.859  17.320  1.00 60.24           C  
ANISOU   62  CE1 PHE A 133     6956   7726   8205    429   -196  -2228       C  
ATOM     63  CE2 PHE A 133       3.028 -21.511  17.099  1.00 60.93           C  
ANISOU   63  CE2 PHE A 133     7089   7708   8355    307    -49  -2316       C  
ATOM     64  CZ  PHE A 133       2.779 -22.710  17.730  1.00 59.13           C  
ANISOU   64  CZ  PHE A 133     6889   7599   7980    428   -184  -2231       C  
ATOM     65  N   GLU A 134       8.376 -23.697  13.261  1.00 65.56           N  
ANISOU   65  N   GLU A 134     6901   8007  10001   -185    521  -2993       N  
ATOM     66  CA  GLU A 134       9.134 -23.893  12.026  1.00 66.34           C  
ANISOU   66  CA  GLU A 134     6888   8060  10259   -374    786  -3121       C  
ATOM     67  C   GLU A 134       8.070 -24.363  11.016  1.00 66.92           C  
ANISOU   67  C   GLU A 134     7198   8158  10071   -438    933  -2871       C  
ATOM     68  O   GLU A 134       7.459 -25.418  11.208  1.00 66.54           O  
ANISOU   68  O   GLU A 134     7217   8168   9898   -298    804  -2748       O  
ATOM     69  CB  GLU A 134      10.252 -24.920  12.227  1.00 69.36           C  
ANISOU   69  CB  GLU A 134     6993   8451  10911   -291    692  -3372       C  
ATOM     70  CG  GLU A 134      11.621 -24.279  12.378  1.00 82.13           C  
ANISOU   70  CG  GLU A 134     8325  10007  12874   -376    738  -3697       C  
ATOM     71  CD  GLU A 134      12.665 -25.102  13.108  1.00109.06           C  
ANISOU   71  CD  GLU A 134    11447  13412  16580   -213    499  -3962       C  
ATOM     72  OE1 GLU A 134      12.329 -25.722  14.143  1.00119.91           O  
ANISOU   72  OE1 GLU A 134    12870  14822  17867     14    173  -3876       O  
ATOM     73  OE2 GLU A 134      13.841 -25.061  12.686  1.00110.61           O  
ANISOU   73  OE2 GLU A 134    11363  13562  17103   -320    630  -4264       O  
ATOM     74  N   ILE A 135       7.764 -23.523  10.019  1.00 61.03           N  
ANISOU   74  N   ILE A 135     6602   7359   9229   -647   1174  -2775       N  
ATOM     75  CA  ILE A 135       6.725 -23.781   9.014  1.00 58.83           C  
ANISOU   75  CA  ILE A 135     6572   7090   8690   -722   1299  -2537       C  
ATOM     76  C   ILE A 135       7.280 -24.663   7.897  1.00 63.34           C  
ANISOU   76  C   ILE A 135     7068   7689   9309   -844   1505  -2644       C  
ATOM     77  O   ILE A 135       8.417 -24.472   7.463  1.00 65.29           O  
ANISOU   77  O   ILE A 135     7131   7914   9762   -995   1686  -2876       O  
ATOM     78  CB  ILE A 135       6.140 -22.454   8.429  1.00 61.88           C  
ANISOU   78  CB  ILE A 135     7181   7387   8944   -892   1427  -2376       C  
ATOM     79  CG1 ILE A 135       5.826 -21.369   9.507  1.00 62.67           C  
ANISOU   79  CG1 ILE A 135     7301   7438   9072   -797   1250  -2351       C  
ATOM     80  CG2 ILE A 135       4.927 -22.707   7.539  1.00 62.14           C  
ANISOU   80  CG2 ILE A 135     7488   7425   8699   -929   1481  -2116       C  
ATOM     81  CD1 ILE A 135       4.897 -21.695  10.594  1.00 67.51           C  
ANISOU   81  CD1 ILE A 135     7969   8123   9557   -558    997  -2244       C  
ATOM     82  N   GLY A 136       6.441 -25.548   7.384  1.00 58.70           N  
ANISOU   82  N   GLY A 136     6624   7148   8533   -796   1498  -2487       N  
ATOM     83  CA  GLY A 136       6.799 -26.463   6.300  1.00 59.10           C  
ANISOU   83  CA  GLY A 136     6624   7234   8596   -896   1681  -2586       C  
ATOM     84  C   GLY A 136       5.826 -26.436   5.152  1.00 62.13           C  
ANISOU   84  C   GLY A 136     7290   7625   8693  -1019   1821  -2371       C  
ATOM     85  O   GLY A 136       5.256 -25.389   4.859  1.00 62.32           O  
ANISOU   85  O   GLY A 136     7524   7595   8559  -1127   1872  -2198       O  
ATOM     86  N   ARG A 137       5.597 -27.603   4.534  1.00 59.63           N  
ANISOU   86  N   ARG A 137     6979   7361   8316   -990   1850  -2381       N  
ATOM     87  CA  ARG A 137       4.730 -27.815   3.372  1.00 59.29           C  
ANISOU   87  CA  ARG A 137     7183   7337   8006  -1095   1966  -2215       C  
ATOM     88  C   ARG A 137       3.290 -27.332   3.537  1.00 61.10           C  
ANISOU   88  C   ARG A 137     7688   7532   7996  -1024   1814  -1901       C  
ATOM     89  O   ARG A 137       2.662 -27.686   4.540  1.00 56.15           O  
ANISOU   89  O   ARG A 137     7040   6912   7383   -813   1579  -1806       O  
ATOM     90  CB  ARG A 137       4.693 -29.316   3.008  1.00 60.52           C  
ANISOU   90  CB  ARG A 137     7251   7551   8194  -1005   1941  -2305       C  
ATOM     91  CG  ARG A 137       3.916 -29.602   1.726  1.00 68.74           C  
ANISOU   91  CG  ARG A 137     8529   8621   8969  -1124   2069  -2182       C  
ATOM     92  CD  ARG A 137       3.945 -31.030   1.272  1.00 78.59           C  
ANISOU   92  CD  ARG A 137     9681   9918  10264  -1056   2066  -2306       C  
ATOM     93  NE  ARG A 137       3.391 -31.932   2.274  1.00 66.89           N  
ANISOU   93  NE  ARG A 137     8126   8413   8877   -797   1775  -2223       N  
ATOM     94  CZ  ARG A 137       2.188 -32.470   2.200  1.00 78.53           C  
ANISOU   94  CZ  ARG A 137     9763   9883  10192   -701   1638  -2016       C  
ATOM     95  NH1 ARG A 137       1.374 -32.155   1.203  1.00 70.48           N  
ANISOU   95  NH1 ARG A 137     8990   8875   8913   -819   1733  -1872       N  
ATOM     96  NH2 ARG A 137       1.781 -33.328   3.127  1.00 68.93           N  
ANISOU   96  NH2 ARG A 137     8470   8644   9075   -492   1396  -1949       N  
ATOM     97  N   PRO A 138       2.701 -26.658   2.507  1.00 60.84           N  
ANISOU   97  N   PRO A 138     7917   7463   7735  -1197   1939  -1741       N  
ATOM     98  CA  PRO A 138       1.269 -26.307   2.584  1.00 59.48           C  
ANISOU   98  CA  PRO A 138     7987   7247   7365  -1113   1770  -1466       C  
ATOM     99  C   PRO A 138       0.409 -27.585   2.490  1.00 61.38           C  
ANISOU   99  C   PRO A 138     8254   7545   7522   -964   1649  -1393       C  
ATOM    100  O   PRO A 138       0.725 -28.486   1.707  1.00 60.92           O  
ANISOU  100  O   PRO A 138     8162   7539   7447  -1022   1761  -1497       O  
ATOM    101  CB  PRO A 138       1.061 -25.403   1.364  1.00 62.80           C  
ANISOU  101  CB  PRO A 138     8671   7603   7587  -1353   1929  -1346       C  
ATOM    102  CG  PRO A 138       2.440 -24.977   0.946  1.00 69.59           C  
ANISOU  102  CG  PRO A 138     9417   8465   8557  -1572   2186  -1545       C  
ATOM    103  CD  PRO A 138       3.292 -26.168   1.246  1.00 64.70           C  
ANISOU  103  CD  PRO A 138     8505   7946   8132  -1484   2226  -1801       C  
ATOM    104  N   LEU A 139      -0.633 -27.675   3.335  1.00 55.59           N  
ANISOU  104  N   LEU A 139     7561   6803   6759   -776   1427  -1238       N  
ATOM    105  CA  LEU A 139      -1.563 -28.802   3.442  1.00 54.05           C  
ANISOU  105  CA  LEU A 139     7383   6645   6507   -629   1290  -1147       C  
ATOM    106  C   LEU A 139      -2.908 -28.503   2.765  1.00 61.42           C  
ANISOU  106  C   LEU A 139     8565   7538   7235   -649   1233   -938       C  
ATOM    107  O   LEU A 139      -3.618 -29.426   2.390  1.00 60.72           O  
ANISOU  107  O   LEU A 139     8519   7473   7080   -592   1175   -881       O  
ATOM    108  CB  LEU A 139      -1.771 -29.184   4.935  1.00 51.14           C  
ANISOU  108  CB  LEU A 139     6873   6307   6253   -421   1092  -1131       C  
ATOM    109  CG  LEU A 139      -0.498 -29.600   5.761  1.00 54.36           C  
ANISOU  109  CG  LEU A 139     7033   6743   6878   -361   1072  -1331       C  
ATOM    110  CD1 LEU A 139      -0.841 -29.835   7.228  1.00 51.04           C  
ANISOU  110  CD1 LEU A 139     6542   6352   6499   -174    858  -1271       C  
ATOM    111  CD2 LEU A 139       0.171 -30.902   5.199  1.00 58.40           C  
ANISOU  111  CD2 LEU A 139     7413   7276   7499   -365   1126  -1484       C  
ATOM    112  N   GLY A 140      -3.233 -27.216   2.616  1.00 61.38           N  
ANISOU  112  N   GLY A 140     8711   7456   7156   -725   1230   -835       N  
ATOM    113  CA  GLY A 140      -4.468 -26.741   1.990  1.00 62.15           C  
ANISOU  113  CA  GLY A 140     9043   7482   7087   -741   1140   -644       C  
ATOM    114  C   GLY A 140      -4.455 -25.245   1.760  1.00 69.27           C  
ANISOU  114  C   GLY A 140    10096   8268   7954   -857   1152   -567       C  
ATOM    115  O   GLY A 140      -3.765 -24.522   2.482  1.00 68.64           O  
ANISOU  115  O   GLY A 140     9910   8166   8005   -865   1179   -645       O  
ATOM    116  N   LYS A 141      -5.150 -24.789   0.743  1.00 70.28           N  
ANISOU  116  N   LYS A 141    10482   8308   7915   -950   1113   -415       N  
ATOM    117  CA  LYS A 141      -5.160 -23.388   0.414  1.00 73.41           C  
ANISOU  117  CA  LYS A 141    11065   8555   8274  -1073   1093   -308       C  
ATOM    118  C   LYS A 141      -6.592 -23.006   0.222  1.00 81.78           C  
ANISOU  118  C   LYS A 141    12278   9497   9297   -967    852   -139       C  
ATOM    119  O   LYS A 141      -7.401 -23.821  -0.146  1.00 80.41           O  
ANISOU  119  O   LYS A 141    12179   9344   9028   -894    747    -66       O  
ATOM    120  CB  LYS A 141      -4.381 -23.127  -0.862  1.00 78.20           C  
ANISOU  120  CB  LYS A 141    11875   9130   8709  -1344   1283   -283       C  
ATOM    121  CG  LYS A 141      -2.883 -23.375  -0.763  1.00 96.35           C  
ANISOU  121  CG  LYS A 141    14016  11493  11100  -1496   1539   -468       C  
ATOM    122  CD  LYS A 141      -2.154 -23.122  -2.074  1.00111.28           C  
ANISOU  122  CD  LYS A 141    16084  13411  12788  -1771   1774   -479       C  
ATOM    123  CE  LYS A 141      -0.646 -23.344  -1.985  1.00127.54           C  
ANISOU  123  CE  LYS A 141    17978  15639  14843  -1761   1923   -669       C  
ATOM    124  NZ  LYS A 141       0.050 -23.114  -3.284  1.00143.83           N  
ANISOU  124  NZ  LYS A 141    20158  17757  16734  -2048   2207   -747       N  
ATOM    125  N   GLY A 142      -6.923 -21.763   0.497  1.00 83.48           N  
ANISOU  125  N   GLY A 142    12525   9580   9614   -960    761    -98       N  
ATOM    126  CA  GLY A 142      -8.298 -21.375   0.390  1.00 85.15           C  
ANISOU  126  CA  GLY A 142    12852   9647   9853   -857    520     26       C  
ATOM    127  C   GLY A 142      -8.529 -19.896   0.431  1.00 93.88           C  
ANISOU  127  C   GLY A 142    14264  10554  10852  -1033    463    189       C  
ATOM    128  O   GLY A 142      -7.612 -19.103   0.494  1.00 98.11           O  
ANISOU  128  O   GLY A 142    14940  11092  11244  -1255    642    216       O  
ATOM    129  N   LYS A 143      -9.802 -19.568   0.360  1.00 89.27           N  
ANISOU  129  N   LYS A 143    13807   9789  10324   -952    211    303       N  
ATOM    130  CA  LYS A 143     -10.366 -18.257   0.573  1.00 87.44           C  
ANISOU  130  CA  LYS A 143    13435   9512  10276   -715    -11    265       C  
ATOM    131  C   LYS A 143      -9.679 -17.390   1.599  1.00 86.19           C  
ANISOU  131  C   LYS A 143    13136   9284  10328   -682    -11    162       C  
ATOM    132  O   LYS A 143      -9.114 -16.377   1.272  1.00 86.84           O  
ANISOU  132  O   LYS A 143    13374   9185  10438   -824    -27    234       O  
ATOM    133  CB  LYS A 143     -11.793 -18.475   1.039  1.00 88.85           C  
ANISOU  133  CB  LYS A 143    13405   9882  10470   -527    -22    179       C  
ATOM    134  CG  LYS A 143     -12.688 -19.080  -0.044  1.00107.07           C  
ANISOU  134  CG  LYS A 143    15838  12150  12692   -462   -198    281       C  
ATOM    135  CD  LYS A 143     -14.118 -19.322   0.433  1.00118.11           C  
ANISOU  135  CD  LYS A 143    17080  13748  14050   -369   -129    217       C  
ATOM    136  CE  LYS A 143     -15.000 -19.901  -0.662  1.00129.47           C  
ANISOU  136  CE  LYS A 143    18612  15284  15296   -519     48    231       C  
ATOM    137  NZ  LYS A 143     -16.389 -20.165  -0.207  1.00134.39           N  
ANISOU  137  NZ  LYS A 143    19092  16061  15907   -422     77    175       N  
ATOM    138  N   PHE A 144      -9.756 -17.794   2.850  1.00 79.42           N  
ANISOU  138  N   PHE A 144    12001   8569   9606   -515     12     -2       N  
ATOM    139  CA  PHE A 144      -9.358 -16.959   3.964  1.00 78.69           C  
ANISOU  139  CA  PHE A 144    11761   8433   9705   -472      8   -132       C  
ATOM    140  C   PHE A 144      -7.902 -17.025   4.299  1.00 78.55           C  
ANISOU  140  C   PHE A 144    11650   8501   9694   -601    228   -229       C  
ATOM    141  O   PHE A 144      -7.366 -16.165   4.950  1.00 79.10           O  
ANISOU  141  O   PHE A 144    11643   8496   9915   -621    232   -323       O  
ATOM    142  CB  PHE A 144     -10.175 -17.345   5.169  1.00 79.70           C  
ANISOU  142  CB  PHE A 144    11655   8669   9957   -240    -89   -272       C  
ATOM    143  CG  PHE A 144     -11.631 -17.159   4.963  1.00 81.81           C  
ANISOU  143  CG  PHE A 144    11962   8870  10252   -107   -288   -215       C  
ATOM    144  CD1 PHE A 144     -12.131 -15.918   4.678  1.00 86.45           C  
ANISOU  144  CD1 PHE A 144    12704   9204  10940   -111   -495   -137       C  
ATOM    145  CD2 PHE A 144     -12.487 -18.218   5.022  1.00 83.36           C  
ANISOU  145  CD2 PHE A 144    12034   9241  10397     17   -283   -246       C  
ATOM    146  CE1 PHE A 144     -13.465 -15.724   4.472  1.00 87.69           C  
ANISOU  146  CE1 PHE A 144    12874   9288  11157     22   -701   -110       C  
ATOM    147  CE2 PHE A 144     -13.825 -18.034   4.813  1.00 87.23           C  
ANISOU  147  CE2 PHE A 144    12533   9669  10944    133   -461   -218       C  
ATOM    148  CZ  PHE A 144     -14.315 -16.783   4.539  1.00 86.75           C  
ANISOU  148  CZ  PHE A 144    12609   9359  10994    141   -673   -161       C  
ATOM    149  N   GLY A 145      -7.288 -18.082   3.843  1.00 72.21           N  
ANISOU  149  N   GLY A 145    10848   7840   8750   -688    398   -224       N  
ATOM    150  CA  GLY A 145      -5.858 -18.347   3.974  1.00 71.38           C  
ANISOU  150  CA  GLY A 145    10627   7829   8667   -807    612   -343       C  
ATOM    151  C   GLY A 145      -5.516 -19.824   3.889  1.00 71.14           C  
ANISOU  151  C   GLY A 145    10492   7998   8541   -783    734   -400       C  
ATOM    152  O   GLY A 145      -6.388 -20.648   3.629  1.00 71.19           O  
ANISOU  152  O   GLY A 145    10539   8064   8445   -695    665   -327       O  
ATOM    153  N   ASN A 146      -4.253 -20.171   4.153  1.00 64.43           N  
ANISOU  153  N   ASN A 146     9485   7240   7755   -850    900   -546       N  
ATOM    154  CA  ASN A 146      -3.732 -21.533   4.026  1.00 61.92           C  
ANISOU  154  CA  ASN A 146     9052   7083   7392   -841   1015   -628       C  
ATOM    155  C   ASN A 146      -3.479 -22.296   5.328  1.00 59.66           C  
ANISOU  155  C   ASN A 146     8515   6936   7217   -657    960   -764       C  
ATOM    156  O   ASN A 146      -3.384 -21.702   6.396  1.00 58.34           O  
ANISOU  156  O   ASN A 146     8237   6767   7164   -564    877   -837       O  
ATOM    157  CB  ASN A 146      -2.436 -21.483   3.212  1.00 65.21           C  
ANISOU  157  CB  ASN A 146     9472   7495   7809  -1069   1247   -715       C  
ATOM    158  CG  ASN A 146      -2.521 -20.793   1.868  1.00 98.42           C  
ANISOU  158  CG  ASN A 146    13956  11578  11861  -1298   1335   -573       C  
ATOM    159  OD1 ASN A 146      -3.591 -20.438   1.375  1.00 91.35           O  
ANISOU  159  OD1 ASN A 146    13277  10587  10844  -1283   1197   -392       O  
ATOM    160  ND2 ASN A 146      -1.383 -20.625   1.220  1.00 98.22           N  
ANISOU  160  ND2 ASN A 146    13932  11554  11833  -1525   1567   -656       N  
ATOM    161  N   VAL A 147      -3.337 -23.625   5.214  1.00 52.92           N  
ANISOU  161  N   VAL A 147     7582   6199   6325   -611    999   -800       N  
ATOM    162  CA  VAL A 147      -2.975 -24.505   6.325  1.00 51.31           C  
ANISOU  162  CA  VAL A 147     7166   6114   6215   -460    940   -910       C  
ATOM    163  C   VAL A 147      -1.580 -25.014   5.972  1.00 53.71           C  
ANISOU  163  C   VAL A 147     7338   6453   6617   -561   1092  -1077       C  
ATOM    164  O   VAL A 147      -1.363 -25.476   4.862  1.00 53.51           O  
ANISOU  164  O   VAL A 147     7377   6428   6525   -683   1224  -1080       O  
ATOM    165  CB  VAL A 147      -3.967 -25.673   6.611  1.00 52.10           C  
ANISOU  165  CB  VAL A 147     7263   6295   6239   -312    829   -819       C  
ATOM    166  CG1 VAL A 147      -3.517 -26.511   7.821  1.00 51.44           C  
ANISOU  166  CG1 VAL A 147     6989   6313   6242   -174    751   -910       C  
ATOM    167  CG2 VAL A 147      -5.395 -25.164   6.812  1.00 49.99           C  
ANISOU  167  CG2 VAL A 147     7109   5991   5893   -231    704   -679       C  
ATOM    168  N   TYR A 148      -0.634 -24.901   6.890  1.00 49.71           N  
ANISOU  168  N   TYR A 148     6639   5975   6273   -514   1071  -1237       N  
ATOM    169  CA  TYR A 148       0.718 -25.366   6.643  1.00 51.40           C  
ANISOU  169  CA  TYR A 148     6683   6215   6632   -594   1197  -1435       C  
ATOM    170  C   TYR A 148       1.110 -26.420   7.642  1.00 54.49           C  
ANISOU  170  C   TYR A 148     6881   6686   7139   -420   1059  -1536       C  
ATOM    171  O   TYR A 148       0.632 -26.377   8.782  1.00 53.22           O  
ANISOU  171  O   TYR A 148     6702   6557   6960   -266    881  -1484       O  
ATOM    172  CB  TYR A 148       1.710 -24.196   6.750  1.00 55.23           C  
ANISOU  172  CB  TYR A 148     7092   6633   7260   -720   1293  -1569       C  
ATOM    173  CG  TYR A 148       1.454 -23.096   5.748  1.00 59.37           C  
ANISOU  173  CG  TYR A 148     7824   7050   7684   -921   1426  -1457       C  
ATOM    174  CD1 TYR A 148       1.832 -23.241   4.418  1.00 62.78           C  
ANISOU  174  CD1 TYR A 148     8347   7470   8036  -1132   1644  -1462       C  
ATOM    175  CD2 TYR A 148       0.826 -21.911   6.125  1.00 59.71           C  
ANISOU  175  CD2 TYR A 148     7982   6998   7706   -905   1326  -1349       C  
ATOM    176  CE1 TYR A 148       1.595 -22.235   3.485  1.00 65.30           C  
ANISOU  176  CE1 TYR A 148     8897   7682   8233  -1334   1750  -1329       C  
ATOM    177  CE2 TYR A 148       0.582 -20.898   5.198  1.00 62.87           C  
ANISOU  177  CE2 TYR A 148     8594   7267   8026  -1090   1412  -1225       C  
ATOM    178  CZ  TYR A 148       0.980 -21.064   3.880  1.00 71.51           C  
ANISOU  178  CZ  TYR A 148     9805   8347   9017  -1310   1620  -1201       C  
ATOM    179  OH  TYR A 148       0.742 -20.100   2.940  1.00 74.46           O  
ANISOU  179  OH  TYR A 148    10425   8586   9278  -1510   1693  -1050       O  
ATOM    180  N   LEU A 149       2.021 -27.339   7.262  1.00 49.52           N  
ANISOU  180  N   LEU A 149     6101   6081   6632   -447   1132  -1695       N  
ATOM    181  CA  LEU A 149       2.591 -28.266   8.242  1.00 47.03           C  
ANISOU  181  CA  LEU A 149     5590   5807   6475   -285    968  -1811       C  
ATOM    182  C   LEU A 149       3.585 -27.419   9.057  1.00 51.71           C  
ANISOU  182  C   LEU A 149     6026   6380   7242   -283    931  -1983       C  
ATOM    183  O   LEU A 149       4.238 -26.537   8.507  1.00 54.17           O  
ANISOU  183  O   LEU A 149     6306   6645   7630   -447   1104  -2090       O  
ATOM    184  CB  LEU A 149       3.332 -29.444   7.554  1.00 47.64           C  
ANISOU  184  CB  LEU A 149     5524   5890   6685   -310   1044  -1971       C  
ATOM    185  CG  LEU A 149       3.839 -30.515   8.492  1.00 50.60           C  
ANISOU  185  CG  LEU A 149     5716   6273   7236   -131    829  -2068       C  
ATOM    186  CD1 LEU A 149       2.688 -31.222   9.148  1.00 48.36           C  
ANISOU  186  CD1 LEU A 149     5561   6012   6800     20    631  -1838       C  
ATOM    187  CD2 LEU A 149       4.762 -31.467   7.780  1.00 50.62           C  
ANISOU  187  CD2 LEU A 149     5534   6258   7442   -166    914  -2293       C  
ATOM    188  N   ALA A 150       3.639 -27.611  10.366  1.00 46.89           N  
ANISOU  188  N   ALA A 150     5338   5802   6677   -113    705  -1996       N  
ATOM    189  CA  ALA A 150       4.554 -26.839  11.196  1.00 48.09           C  
ANISOU  189  CA  ALA A 150     5340   5938   6994    -95    637  -2172       C  
ATOM    190  C   ALA A 150       5.080 -27.674  12.327  1.00 52.68           C  
ANISOU  190  C   ALA A 150     5776   6553   7688     84    387  -2262       C  
ATOM    191  O   ALA A 150       4.491 -28.688  12.680  1.00 50.89           O  
ANISOU  191  O   ALA A 150     5612   6362   7363    203    245  -2130       O  
ATOM    192  CB  ALA A 150       3.861 -25.587  11.754  1.00 48.71           C  
ANISOU  192  CB  ALA A 150     5547   6012   6948    -91    599  -2071       C  
ATOM    193  N   ARG A 151       6.187 -27.241  12.910  1.00 53.46           N  
ANISOU  193  N   ARG A 151     5685   6628   7998    101    315  -2483       N  
ATOM    194  CA  ARG A 151       6.787 -27.907  14.054  1.00 54.23           C  
ANISOU  194  CA  ARG A 151     5650   6743   8213    274     33  -2584       C  
ATOM    195  C   ARG A 151       7.053 -26.867  15.141  1.00 59.50           C  
ANISOU  195  C   ARG A 151     6287   7429   8893    324   -100  -2667       C  
ATOM    196  O   ARG A 151       7.607 -25.815  14.851  1.00 60.39           O  
ANISOU  196  O   ARG A 151     6315   7495   9136    207     36  -2814       O  
ATOM    197  CB  ARG A 151       8.100 -28.613  13.661  1.00 51.57           C  
ANISOU  197  CB  ARG A 151     5049   6345   8201    266     35  -2848       C  
ATOM    198  CG  ARG A 151       8.627 -29.492  14.787  1.00 57.78           C  
ANISOU  198  CG  ARG A 151     5723   7122   9110    466   -311  -2920       C  
ATOM    199  CD  ARG A 151       9.918 -30.191  14.450  1.00 66.12           C  
ANISOU  199  CD  ARG A 151     6490   8100  10534    482   -347  -3210       C  
ATOM    200  NE  ARG A 151      10.997 -29.249  14.151  1.00 76.46           N  
ANISOU  200  NE  ARG A 151     7579   9375  12098    359   -191  -3499       N  
ATOM    201  CZ  ARG A 151      12.290 -29.565  14.093  1.00 79.91           C  
ANISOU  201  CZ  ARG A 151     7705   9745  12910    375   -240  -3823       C  
ATOM    202  NH1 ARG A 151      12.693 -30.801  14.354  1.00 68.20           N  
ANISOU  202  NH1 ARG A 151     6098   8210  11604    529   -477  -3903       N  
ATOM    203  NH2 ARG A 151      13.188 -28.647  13.782  1.00 69.98           N  
ANISOU  203  NH2 ARG A 151     6251   8460  11877    235    -61  -4077       N  
ATOM    204  N   GLU A 152       6.673 -27.171  16.390  1.00 57.26           N  
ANISOU  204  N   GLU A 152     6076   7212   8468    487   -364  -2580       N  
ATOM    205  CA  GLU A 152       6.928 -26.318  17.531  1.00 57.30           C  
ANISOU  205  CA  GLU A 152     6056   7255   8462    556   -527  -2679       C  
ATOM    206  C   GLU A 152       8.417 -26.472  17.864  1.00 62.00           C  
ANISOU  206  C   GLU A 152     6389   7789   9379    600   -675  -2967       C  
ATOM    207  O   GLU A 152       8.876 -27.590  18.094  1.00 61.35           O  
ANISOU  207  O   GLU A 152     6228   7686   9396    703   -859  -2997       O  
ATOM    208  CB  GLU A 152       6.044 -26.734  18.709  1.00 58.31           C  
ANISOU  208  CB  GLU A 152     6360   7493   8302    698   -748  -2493       C  
ATOM    209  CG  GLU A 152       5.797 -25.598  19.696  1.00 65.33           C  
ANISOU  209  CG  GLU A 152     7301   8453   9067    732   -823  -2546       C  
ATOM    210  CD  GLU A 152       6.916 -25.309  20.676  1.00 91.89           C  
ANISOU  210  CD  GLU A 152    10512  11816  12586    817  -1060  -2784       C  
ATOM    211  OE1 GLU A 152       7.207 -26.187  21.520  1.00 93.49           O  
ANISOU  211  OE1 GLU A 152    10724  12056  12740    945  -1329  -2768       O  
ATOM    212  OE2 GLU A 152       7.494 -24.200  20.608  1.00 96.28           O  
ANISOU  212  OE2 GLU A 152    10946  12322  13315    755   -993  -2984       O  
ATOM    213  N   LYS A 153       9.178 -25.355  17.839  1.00 62.02           N  
ANISOU  213  N   LYS A 153     6245   7744   9576    519   -600  -3186       N  
ATOM    214  CA  LYS A 153      10.634 -25.374  18.056  1.00 65.61           C  
ANISOU  214  CA  LYS A 153     6411   8129  10388    540   -713  -3502       C  
ATOM    215  C   LYS A 153      11.056 -25.990  19.375  1.00 72.17           C  
ANISOU  215  C   LYS A 153     7197   8992  11234    748  -1113  -3566       C  
ATOM    216  O   LYS A 153      11.896 -26.875  19.384  1.00 74.50           O  
ANISOU  216  O   LYS A 153     7316   9226  11763    822  -1267  -3707       O  
ATOM    217  CB  LYS A 153      11.246 -23.971  17.905  1.00 68.93           C  
ANISOU  217  CB  LYS A 153     6702   8491  10996    406   -568  -3708       C  
ATOM    218  CG  LYS A 153      11.131 -23.403  16.508  1.00 73.20           C  
ANISOU  218  CG  LYS A 153     7262   8970  11582    171   -181  -3677       C  
ATOM    219  CD  LYS A 153      11.636 -21.983  16.494  1.00 72.15           C  
ANISOU  219  CD  LYS A 153     7036   8762  11614     37    -68  -3841       C  
ATOM    220  CE  LYS A 153      11.504 -21.364  15.129  1.00 76.84           C  
ANISOU  220  CE  LYS A 153     7691   9283  12221   -218    303  -3777       C  
ATOM    221  NZ  LYS A 153      11.707 -19.890  15.187  1.00 79.96           N  
ANISOU  221  NZ  LYS A 153     8072   9588  12722   -349    391  -3858       N  
ATOM    222  N   GLN A 154      10.451 -25.557  20.468  1.00 69.22           N  
ANISOU  222  N   GLN A 154     6988   8709  10603    840  -1289  -3466       N  
ATOM    223  CA  GLN A 154      10.820 -26.000  21.822  1.00 71.48           C  
ANISOU  223  CA  GLN A 154     7279   9040  10841   1024  -1686  -3515       C  
ATOM    224  C   GLN A 154      10.605 -27.491  22.090  1.00 72.73           C  
ANISOU  224  C   GLN A 154     7534   9203  10898   1144  -1902  -3336       C  
ATOM    225  O   GLN A 154      11.463 -28.129  22.705  1.00 76.25           O  
ANISOU  225  O   GLN A 154     7868   9597  11507   1272  -2222  -3460       O  
ATOM    226  CB  GLN A 154      10.102 -25.155  22.900  1.00 73.08           C  
ANISOU  226  CB  GLN A 154     7665   9367  10734   1071  -1782  -3445       C  
ATOM    227  CG  GLN A 154      10.622 -23.720  23.034  1.00 99.25           C  
ANISOU  227  CG  GLN A 154    10842  12652  14216   1006  -1714  -3694       C  
ATOM    228  CD  GLN A 154      10.061 -22.991  24.239  1.00131.12           C  
ANISOU  228  CD  GLN A 154    15027  16814  17977   1083  -1866  -3686       C  
ATOM    229  OE1 GLN A 154       9.744 -23.587  25.281  1.00128.81           O  
ANISOU  229  OE1 GLN A 154    14885  16635  17420   1211  -2123  -3585       O  
ATOM    230  NE2 GLN A 154       9.969 -21.667  24.142  1.00125.84           N  
ANISOU  230  NE2 GLN A 154    14319  16124  17372    999  -1717  -3810       N  
ATOM    231  N   SER A 155       9.468 -28.037  21.648  1.00 62.43           N  
ANISOU  231  N   SER A 155     6436   7943   9341   1106  -1753  -3049       N  
ATOM    232  CA  SER A 155       9.102 -29.432  21.915  1.00 60.18           C  
ANISOU  232  CA  SER A 155     6275   7654   8936   1202  -1946  -2842       C  
ATOM    233  C   SER A 155       9.286 -30.406  20.740  1.00 61.16           C  
ANISOU  233  C   SER A 155     6295   7669   9275   1161  -1815  -2835       C  
ATOM    234  O   SER A 155       9.271 -31.618  20.964  1.00 62.62           O  
ANISOU  234  O   SER A 155     6524   7803   9467   1255  -2025  -2724       O  
ATOM    235  CB  SER A 155       7.653 -29.492  22.394  1.00 57.73           C  
ANISOU  235  CB  SER A 155     6269   7477   8188   1197  -1904  -2527       C  
ATOM    236  OG  SER A 155       6.810 -28.985  21.375  1.00 59.05           O  
ANISOU  236  OG  SER A 155     6494   7662   8282   1063  -1548  -2432       O  
ATOM    237  N   LYS A 156       9.392 -29.889  19.500  1.00 55.45           N  
ANISOU  237  N   LYS A 156     5459   6908   8700   1012  -1472  -2938       N  
ATOM    238  CA  LYS A 156       9.479 -30.664  18.249  1.00 55.43           C  
ANISOU  238  CA  LYS A 156     5370   6829   8861    941  -1282  -2952       C  
ATOM    239  C   LYS A 156       8.106 -31.313  17.919  1.00 59.27           C  
ANISOU  239  C   LYS A 156     6112   7364   9044    924  -1190  -2621       C  
ATOM    240  O   LYS A 156       8.025 -32.272  17.144  1.00 58.54           O  
ANISOU  240  O   LYS A 156     5993   7212   9038    912  -1131  -2586       O  
ATOM    241  CB  LYS A 156      10.666 -31.670  18.213  1.00 57.88           C  
ANISOU  241  CB  LYS A 156     5429   7018   9542   1038  -1491  -3176       C  
ATOM    242  CG  LYS A 156      12.067 -31.030  18.453  1.00 57.68           C  
ANISOU  242  CG  LYS A 156     5106   6936   9872   1047  -1568  -3545       C  
ATOM    243  CD  LYS A 156      13.237 -32.068  18.503  1.00 70.18           C  
ANISOU  243  CD  LYS A 156     6416   8386  11865   1171  -1825  -3794       C  
ATOM    244  CE  LYS A 156      13.010 -33.311  19.368  1.00 83.41           C  
ANISOU  244  CE  LYS A 156     8219  10007  13465   1364  -2238  -3611       C  
ATOM    245  NZ  LYS A 156      14.196 -34.242  19.368  1.00 78.35           N  
ANISOU  245  NZ  LYS A 156     7288   9205  13277   1492  -2511  -3885       N  
ATOM    246  N   PHE A 157       7.023 -30.753  18.493  1.00 55.87           N  
ANISOU  246  N   PHE A 157     5910   7042   8277    918  -1170  -2407       N  
ATOM    247  CA  PHE A 157       5.634 -31.196  18.272  1.00 52.68           C  
ANISOU  247  CA  PHE A 157     5737   6694   7585    893  -1073  -2109       C  
ATOM    248  C   PHE A 157       5.206 -30.817  16.848  1.00 53.13           C  
ANISOU  248  C   PHE A 157     5801   6730   7658    743   -732  -2097       C  
ATOM    249  O   PHE A 157       5.262 -29.641  16.494  1.00 52.52           O  
ANISOU  249  O   PHE A 157     5705   6663   7587    644   -551  -2182       O  
ATOM    250  CB  PHE A 157       4.684 -30.548  19.313  1.00 53.68           C  
ANISOU  250  CB  PHE A 157     6063   6952   7381    920  -1127  -1948       C  
ATOM    251  CG  PHE A 157       3.349 -31.241  19.437  1.00 54.81           C  
ANISOU  251  CG  PHE A 157     6420   7157   7248    923  -1109  -1655       C  
ATOM    252  CD1 PHE A 157       3.189 -32.337  20.285  1.00 59.19           C  
ANISOU  252  CD1 PHE A 157     7074   7721   7693   1012  -1356  -1500       C  
ATOM    253  CD2 PHE A 157       2.270 -30.852  18.653  1.00 56.21           C  
ANISOU  253  CD2 PHE A 157     6697   7365   7296    828   -855  -1532       C  
ATOM    254  CE1 PHE A 157       1.967 -33.035  20.335  1.00 60.83           C  
ANISOU  254  CE1 PHE A 157     7465   7974   7672    991  -1316  -1230       C  
ATOM    255  CE2 PHE A 157       1.054 -31.549  18.703  1.00 55.78           C  
ANISOU  255  CE2 PHE A 157     6807   7357   7030    824   -833  -1284       C  
ATOM    256  CZ  PHE A 157       0.904 -32.622  19.559  1.00 55.96           C  
ANISOU  256  CZ  PHE A 157     6916   7397   6950    899  -1049  -1136       C  
ATOM    257  N   ILE A 158       4.822 -31.793  16.034  1.00 47.26           N  
ANISOU  257  N   ILE A 158     5087   5944   6926    721   -659  -1998       N  
ATOM    258  CA  ILE A 158       4.347 -31.561  14.658  1.00 47.85           C  
ANISOU  258  CA  ILE A 158     5202   6004   6975    580   -360  -1969       C  
ATOM    259  C   ILE A 158       2.851 -31.293  14.722  1.00 50.43           C  
ANISOU  259  C   ILE A 158     5762   6403   6997    560   -292  -1706       C  
ATOM    260  O   ILE A 158       2.104 -31.974  15.428  1.00 48.90           O  
ANISOU  260  O   ILE A 158     5683   6249   6647    643   -438  -1522       O  
ATOM    261  CB  ILE A 158       4.776 -32.640  13.607  1.00 51.70           C  
ANISOU  261  CB  ILE A 158     5579   6414   7652    552   -289  -2057       C  
ATOM    262  CG1 ILE A 158       6.268 -32.485  13.262  1.00 55.37           C  
ANISOU  262  CG1 ILE A 158     5776   6817   8444    516   -246  -2385       C  
ATOM    263  CG2 ILE A 158       3.958 -32.585  12.307  1.00 54.05           C  
ANISOU  263  CG2 ILE A 158     5995   6720   7822    421    -25  -1955       C  
ATOM    264  CD1 ILE A 158       6.695 -31.478  12.129  1.00 66.90           C  
ANISOU  264  CD1 ILE A 158     7173   8279   9967    319     87  -2542       C  
ATOM    265  N   LEU A 159       2.440 -30.256  14.037  1.00 47.21           N  
ANISOU  265  N   LEU A 159     5418   6003   6516    445    -81  -1697       N  
ATOM    266  CA  LEU A 159       1.061 -29.786  14.068  1.00 46.55           C  
ANISOU  266  CA  LEU A 159     5524   5973   6188    428    -19  -1494       C  
ATOM    267  C   LEU A 159       0.777 -29.151  12.738  1.00 48.36           C  
ANISOU  267  C   LEU A 159     5811   6153   6409    285    214  -1487       C  
ATOM    268  O   LEU A 159       1.663 -29.118  11.876  1.00 46.10           O  
ANISOU  268  O   LEU A 159     5428   5811   6278    190    340  -1633       O  
ATOM    269  CB  LEU A 159       0.915 -28.735  15.219  1.00 48.02           C  
ANISOU  269  CB  LEU A 159     5737   6226   6282    477   -105  -1517       C  
ATOM    270  CG  LEU A 159       1.960 -27.620  15.250  1.00 54.75           C  
ANISOU  270  CG  LEU A 159     6465   7037   7301    426    -65  -1735       C  
ATOM    271  CD1 LEU A 159       1.443 -26.361  14.559  1.00 52.86           C  
ANISOU  271  CD1 LEU A 159     6308   6757   7019    310    117  -1713       C  
ATOM    272  CD2 LEU A 159       2.364 -27.343  16.648  1.00 62.56           C  
ANISOU  272  CD2 LEU A 159     7405   8089   8275    534   -268  -1821       C  
ATOM    273  N   ALA A 160      -0.442 -28.609  12.591  1.00 46.71           N  
ANISOU  273  N   ALA A 160     5761   5965   6023    264    268  -1328       N  
ATOM    274  CA  ALA A 160      -0.895 -27.907  11.389  1.00 45.46           C  
ANISOU  274  CA  ALA A 160     5706   5747   5818    135    444  -1281       C  
ATOM    275  C   ALA A 160      -1.314 -26.506  11.818  1.00 51.06           C  
ANISOU  275  C   ALA A 160     6476   6446   6478    124    443  -1275       C  
ATOM    276  O   ALA A 160      -2.075 -26.336  12.771  1.00 49.08           O  
ANISOU  276  O   ALA A 160     6262   6261   6127    222    337  -1211       O  
ATOM    277  CB  ALA A 160      -2.063 -28.635  10.747  1.00 43.31           C  
ANISOU  277  CB  ALA A 160     5563   5480   5414    138    464  -1103       C  
ATOM    278  N   LEU A 161      -0.785 -25.506  11.120  1.00 51.22           N  
ANISOU  278  N   LEU A 161     6502   6382   6577     -5    566  -1352       N  
ATOM    279  CA  LEU A 161      -1.057 -24.085  11.358  1.00 51.16           C  
ANISOU  279  CA  LEU A 161     6547   6320   6573    -35    567  -1364       C  
ATOM    280  C   LEU A 161      -1.961 -23.509  10.275  1.00 51.88           C  
ANISOU  280  C   LEU A 161     6820   6318   6573   -132    649  -1218       C  
ATOM    281  O   LEU A 161      -1.538 -23.379   9.120  1.00 49.43           O  
ANISOU  281  O   LEU A 161     6569   5933   6278   -285    788  -1211       O  
ATOM    282  CB  LEU A 161       0.260 -23.312  11.357  1.00 53.41           C  
ANISOU  282  CB  LEU A 161     6710   6542   7041   -129    631  -1552       C  
ATOM    283  CG  LEU A 161       0.679 -22.619  12.655  1.00 61.49           C  
ANISOU  283  CG  LEU A 161     7622   7593   8149    -38    502  -1692       C  
ATOM    284  CD1 LEU A 161       1.972 -21.876  12.460  1.00 63.50           C  
ANISOU  284  CD1 LEU A 161     7747   7764   8615   -156    583  -1882       C  
ATOM    285  CD2 LEU A 161      -0.350 -21.647  13.135  1.00 64.55           C  
ANISOU  285  CD2 LEU A 161     8109   7965   8453     13    435  -1628       C  
ATOM    286  N   LYS A 162      -3.202 -23.168  10.645  1.00 49.70           N  
ANISOU  286  N   LYS A 162     6633   6049   6201    -48    559  -1113       N  
ATOM    287  CA  LYS A 162      -4.163 -22.514   9.749  1.00 48.98           C  
ANISOU  287  CA  LYS A 162     6712   5850   6049   -110    576   -982       C  
ATOM    288  C   LYS A 162      -3.911 -21.021   9.915  1.00 55.49           C  
ANISOU  288  C   LYS A 162     7548   6557   6977   -162    563  -1050       C  
ATOM    289  O   LYS A 162      -3.984 -20.509  11.027  1.00 54.78           O  
ANISOU  289  O   LYS A 162     7368   6506   6940    -61    473  -1147       O  
ATOM    290  CB  LYS A 162      -5.592 -22.885  10.126  1.00 49.69           C  
ANISOU  290  CB  LYS A 162     6847   5996   6036     15    475   -874       C  
ATOM    291  CG  LYS A 162      -6.654 -22.464   9.119  1.00 51.55           C  
ANISOU  291  CG  LYS A 162     7248   6118   6219    -28    455   -739       C  
ATOM    292  CD  LYS A 162      -8.059 -22.641   9.718  1.00 55.51           C  
ANISOU  292  CD  LYS A 162     7739   6675   6677    108    349   -689       C  
ATOM    293  CE  LYS A 162      -8.548 -24.050   9.685  1.00 70.51           C  
ANISOU  293  CE  LYS A 162     9621   8681   8488    155    354   -611       C  
ATOM    294  NZ  LYS A 162      -9.928 -24.138  10.179  1.00 72.22           N  
ANISOU  294  NZ  LYS A 162     9820   8942   8678    257    278   -571       N  
ATOM    295  N   VAL A 163      -3.506 -20.354   8.836  1.00 55.39           N  
ANISOU  295  N   VAL A 163     7645   6405   6996   -332    658  -1012       N  
ATOM    296  CA  VAL A 163      -3.176 -18.915   8.804  1.00 57.19           C  
ANISOU  296  CA  VAL A 163     7907   6477   7345   -421    654  -1056       C  
ATOM    297  C   VAL A 163      -4.296 -18.196   8.045  1.00 65.68           C  
ANISOU  297  C   VAL A 163     9190   7399   8367   -452    579   -890       C  
ATOM    298  O   VAL A 163      -4.356 -18.273   6.815  1.00 64.69           O  
ANISOU  298  O   VAL A 163     9239   7193   8149   -594    649   -758       O  
ATOM    299  CB  VAL A 163      -1.803 -18.648   8.131  1.00 61.31           C  
ANISOU  299  CB  VAL A 163     8406   6935   7953   -626    827  -1130       C  
ATOM    300  CG1 VAL A 163      -1.455 -17.163   8.157  1.00 63.29           C  
ANISOU  300  CG1 VAL A 163     8689   7008   8351   -729    819  -1169       C  
ATOM    301  CG2 VAL A 163      -0.695 -19.478   8.766  1.00 60.54           C  
ANISOU  301  CG2 VAL A 163     8087   6977   7938   -585    880  -1310       C  
ATOM    302  N   LEU A 164      -5.186 -17.521   8.774  1.00 64.54           N  
ANISOU  302  N   LEU A 164     9027   7214   8279   -318    426   -910       N  
ATOM    303  CA  LEU A 164      -6.301 -16.809   8.158  1.00 65.88           C  
ANISOU  303  CA  LEU A 164     9366   7219   8445   -316    307   -779       C  
ATOM    304  C   LEU A 164      -5.982 -15.323   8.139  1.00 69.38           C  
ANISOU  304  C   LEU A 164     9856   7449   9056   -395    253   -815       C  
ATOM    305  O   LEU A 164      -5.352 -14.812   9.064  1.00 68.96           O  
ANISOU  305  O   LEU A 164     9650   7416   9138   -361    253   -985       O  
ATOM    306  CB  LEU A 164      -7.635 -17.065   8.898  1.00 65.79           C  
ANISOU  306  CB  LEU A 164     9289   7289   8420   -113    168   -795       C  
ATOM    307  CG  LEU A 164      -7.984 -18.504   9.262  1.00 69.64           C  
ANISOU  307  CG  LEU A 164     9694   7994   8774    -18    209   -782       C  
ATOM    308  CD1 LEU A 164      -7.790 -18.716  10.759  1.00 69.42           C  
ANISOU  308  CD1 LEU A 164     9469   8139   8767    111    200   -944       C  
ATOM    309  CD2 LEU A 164      -9.424 -18.821   8.895  1.00 73.25           C  
ANISOU  309  CD2 LEU A 164    10220   8434   9176     63    109   -677       C  
ATOM    310  N   PHE A 165      -6.476 -14.643   7.123  1.00 67.25           N  
ANISOU  310  N   PHE A 165     9804   6966   8780   -506    193   -655       N  
ATOM    311  CA  PHE A 165      -6.261 -13.216   6.958  1.00 71.12           C  
ANISOU  311  CA  PHE A 165    10376   7207   9440   -602    122   -652       C  
ATOM    312  C   PHE A 165      -7.387 -12.352   7.487  1.00 69.80           C  
ANISOU  312  C   PHE A 165    10191   6911   9420   -429   -116   -690       C  
ATOM    313  O   PHE A 165      -8.521 -12.481   7.078  1.00 65.54           O  
ANISOU  313  O   PHE A 165     9743   6339   8822   -343   -244   -587       O  
ATOM    314  CB  PHE A 165      -6.016 -12.883   5.500  1.00 76.43           C  
ANISOU  314  CB  PHE A 165    11323   7696  10021   -852    186   -444       C  
ATOM    315  CG  PHE A 165      -4.689 -13.332   5.015  1.00 81.60           C  
ANISOU  315  CG  PHE A 165    11960   8333  10713  -1077    401   -493       C  
ATOM    316  CD1 PHE A 165      -4.583 -14.408   4.170  1.00 85.23           C  
ANISOU  316  CD1 PHE A 165    12338   8993  11052  -1163    625   -546       C  
ATOM    317  CD2 PHE A 165      -3.553 -12.704   5.437  1.00 89.18           C  
ANISOU  317  CD2 PHE A 165    12978   9060  11849  -1215    378   -493       C  
ATOM    318  CE1 PHE A 165      -3.363 -14.840   3.742  1.00 88.77           C  
ANISOU  318  CE1 PHE A 165    12736   9427  11564  -1375    836   -625       C  
ATOM    319  CE2 PHE A 165      -2.328 -13.127   5.008  1.00 94.74           C  
ANISOU  319  CE2 PHE A 165    13647   9746  12606  -1444    596   -551       C  
ATOM    320  CZ  PHE A 165      -2.234 -14.196   4.159  1.00 91.95           C  
ANISOU  320  CZ  PHE A 165    13188   9611  12139  -1520    830   -628       C  
ATOM    321  N   LYS A 166      -7.062 -11.443   8.384  1.00 67.69           N  
ANISOU  321  N   LYS A 166     9781   6578   9359   -372   -176   -869       N  
ATOM    322  CA  LYS A 166      -8.075 -10.596   8.983  1.00 68.83           C  
ANISOU  322  CA  LYS A 166     9860   6601   9691   -203   -391   -975       C  
ATOM    323  C   LYS A 166      -8.910  -9.869   7.945  1.00 76.00           C  
ANISOU  323  C   LYS A 166    10993   7212  10670   -241   -585   -795       C  
ATOM    324  O   LYS A 166     -10.111  -9.825   8.046  1.00 75.50           O  
ANISOU  324  O   LYS A 166    10897   7114  10674    -73   -759   -827       O  
ATOM    325  CB  LYS A 166      -7.422  -9.634   9.955  1.00 70.15           C  
ANISOU  325  CB  LYS A 166     9864   6713  10076   -183   -410  -1198       C  
ATOM    326  CG  LYS A 166      -6.784 -10.350  11.120  1.00 70.95           C  
ANISOU  326  CG  LYS A 166     9724   7117  10118    -62   -313  -1415       C  
ATOM    327  CD  LYS A 166      -6.124  -9.414  12.101  1.00 76.13           C  
ANISOU  327  CD  LYS A 166    10227   7729  10968    -60   -328  -1643       C  
ATOM    328  CE  LYS A 166      -6.234  -9.943  13.512  1.00 78.84           C  
ANISOU  328  CE  LYS A 166    10359   8379  11218     76   -273  -1849       C  
ATOM    329  NZ  LYS A 166      -5.155  -9.420  14.376  1.00 80.68           N  
ANISOU  329  NZ  LYS A 166    10433   8583  11640    123   -336  -2110       N  
ATOM    330  N   ALA A 167      -8.254  -9.330   6.933  1.00 75.49           N  
ANISOU  330  N   ALA A 167    11164   6942  10578   -470   -552   -602       N  
ATOM    331  CA  ALA A 167      -8.895  -8.583   5.856  1.00 78.07           C  
ANISOU  331  CA  ALA A 167    11766   6958  10939   -549   -748   -385       C  
ATOM    332  C   ALA A 167     -10.058  -9.364   5.265  1.00 80.99           C  
ANISOU  332  C   ALA A 167    12238   7383  11150   -451   -855   -255       C  
ATOM    333  O   ALA A 167     -11.181  -8.861   5.285  1.00 81.04           O  
ANISOU  333  O   ALA A 167    12261   7229  11303   -306  -1111   -260       O  
ATOM    334  CB  ALA A 167      -7.877  -8.233   4.774  1.00 80.84           C  
ANISOU  334  CB  ALA A 167    12365   7156  11197   -856   -619   -186       C  
ATOM    335  N   GLN A 168      -9.825 -10.603   4.872  1.00 76.45           N  
ANISOU  335  N   GLN A 168    11704   7036  10309   -518   -670   -171       N  
ATOM    336  CA  GLN A 168     -10.852 -11.412   4.245  1.00 75.86           C  
ANISOU  336  CA  GLN A 168    11722   7032  10069   -444   -750    -53       C  
ATOM    337  C   GLN A 168     -11.921 -11.830   5.199  1.00 76.96           C  
ANISOU  337  C   GLN A 168    11619   7310  10311   -177   -853   -225       C  
ATOM    338  O   GLN A 168     -13.072 -11.878   4.844  1.00 76.14           O  
ANISOU  338  O   GLN A 168    11576   7122  10231    -74  -1050   -164       O  
ATOM    339  CB  GLN A 168     -10.247 -12.662   3.645  1.00 76.02           C  
ANISOU  339  CB  GLN A 168    11806   7272   9806   -577   -508     32       C  
ATOM    340  CG  GLN A 168      -9.707 -12.485   2.247  1.00104.04           C  
ANISOU  340  CG  GLN A 168    15666  10681  13184   -852   -431    246       C  
ATOM    341  CD  GLN A 168      -8.239 -12.808   2.181  1.00134.52           C  
ANISOU  341  CD  GLN A 168    19478  14553  17079  -1042   -199    182       C  
ATOM    342  OE1 GLN A 168      -7.400 -11.986   2.526  1.00132.18           O  
ANISOU  342  OE1 GLN A 168    19062  14480  16680  -1107     48     96       O  
ATOM    343  NE2 GLN A 168      -7.917 -14.009   1.715  1.00128.69           N  
ANISOU  343  NE2 GLN A 168    18822  13561  16513  -1136   -283    211       N  
ATOM    344  N   LEU A 169     -11.519 -12.171   6.407  1.00 71.50           N  
ANISOU  344  N   LEU A 169    10656   6835   9677    -77   -722   -443       N  
ATOM    345  CA  LEU A 169     -12.454 -12.566   7.471  1.00 70.48           C  
ANISOU  345  CA  LEU A 169    10287   6875   9618    146   -769   -624       C  
ATOM    346  C   LEU A 169     -13.458 -11.420   7.768  1.00 76.15           C  
ANISOU  346  C   LEU A 169    10954   7373  10605    285  -1022   -730       C  
ATOM    347  O   LEU A 169     -14.654 -11.684   7.944  1.00 74.57           O  
ANISOU  347  O   LEU A 169    10664   7206  10462    437  -1136   -789       O  
ATOM    348  CB  LEU A 169     -11.710 -12.948   8.761  1.00 69.09           C  
ANISOU  348  CB  LEU A 169     9876   6952   9425    196   -592   -824       C  
ATOM    349  CG  LEU A 169     -10.806 -14.170   8.726  1.00 70.47           C  
ANISOU  349  CG  LEU A 169    10033   7358   9384    111   -372   -776       C  
ATOM    350  CD1 LEU A 169      -9.766 -14.074   9.869  1.00 70.07           C  
ANISOU  350  CD1 LEU A 169     9800   7450   9374    123   -258   -965       C  
ATOM    351  CD2 LEU A 169     -11.623 -15.470   8.767  1.00 68.71           C  
ANISOU  351  CD2 LEU A 169     9762   7332   9014    202   -341   -733       C  
ATOM    352  N   GLU A 170     -12.966 -10.164   7.774  1.00 74.74           N  
ANISOU  352  N   GLU A 170    10829   6957  10611    226  -1113   -759       N  
ATOM    353  CA  GLU A 170     -13.763  -8.951   7.988  1.00 77.61           C  
ANISOU  353  CA  GLU A 170    11154   7059  11275    345  -1375   -867       C  
ATOM    354  C   GLU A 170     -14.782  -8.765   6.866  1.00 85.09           C  
ANISOU  354  C   GLU A 170    12306   7762  12260    360  -1628   -679       C  
ATOM    355  O   GLU A 170     -15.974  -8.656   7.149  1.00 86.25           O  
ANISOU  355  O   GLU A 170    12326   7871  12573    544  -1806   -803       O  
ATOM    356  CB  GLU A 170     -12.857  -7.717   8.083  1.00 81.24           C  
ANISOU  356  CB  GLU A 170    11662   7289  11916    240  -1412   -900       C  
ATOM    357  CG  GLU A 170     -12.259  -7.491   9.463  1.00 98.56           C  
ANISOU  357  CG  GLU A 170    13588   9654  14208    315  -1289  -1189       C  
ATOM    358  CD  GLU A 170     -11.391  -6.255   9.639  1.00139.15           C  
ANISOU  358  CD  GLU A 170    18743  14560  19568    222  -1338  -1257       C  
ATOM    359  OE1 GLU A 170     -10.570  -5.957   8.739  1.00138.81           O  
ANISOU  359  OE1 GLU A 170    18917  14343  19480      4  -1296  -1047       O  
ATOM    360  OE2 GLU A 170     -11.490  -5.620  10.714  1.00142.52           O  
ANISOU  360  OE2 GLU A 170    18954  14993  20203    356  -1398  -1536       O  
ATOM    361  N   LYS A 171     -14.315  -8.781   5.595  1.00 82.67           N  
ANISOU  361  N   LYS A 171    12315   7307  11790    161  -1639   -392       N  
ATOM    362  CA  LYS A 171     -15.119  -8.604   4.384  1.00 84.29           C  
ANISOU  362  CA  LYS A 171    12784   7267  11974    137  -1894   -170       C  
ATOM    363  C   LYS A 171     -16.293  -9.579   4.296  1.00 85.95           C  
ANISOU  363  C   LYS A 171    12907   7629  12122    294  -1962   -197       C  
ATOM    364  O   LYS A 171     -17.376  -9.185   3.858  1.00 88.51           O  
ANISOU  364  O   LYS A 171    13290   7739  12600    402  -2263   -168       O  
ATOM    365  CB  LYS A 171     -14.241  -8.717   3.122  1.00 88.49           C  
ANISOU  365  CB  LYS A 171    13666   7717  12239   -139  -1801    129       C  
ATOM    366  CG  LYS A 171     -13.239  -7.574   2.945  1.00113.90           C  
ANISOU  366  CG  LYS A 171    17031  10695  15551   -330  -1789    205       C  
ATOM    367  CD  LYS A 171     -12.577  -7.564   1.556  1.00130.52           C  
ANISOU  367  CD  LYS A 171    19524  12678  17389   -623  -1728    521       C  
ATOM    368  CE  LYS A 171     -11.380  -8.487   1.434  1.00144.04           C  
ANISOU  368  CE  LYS A 171    21219  14682  18828   -808  -1336    532       C  
ATOM    369  NZ  LYS A 171     -10.724  -8.368   0.106  1.00157.13           N  
ANISOU  369  NZ  LYS A 171    23249  16226  20229  -1112  -1256    809       N  
ATOM    370  N   ALA A 172     -16.077 -10.836   4.718  1.00 77.61           N  
ANISOU  370  N   ALA A 172    11702   6921  10864    306  -1700   -257       N  
ATOM    371  CA  ALA A 172     -17.085 -11.897   4.710  1.00 75.22           C  
ANISOU  371  CA  ALA A 172    11294   6792  10494    431  -1714   -289       C  
ATOM    372  C   ALA A 172     -17.977 -11.887   5.964  1.00 77.46           C  
ANISOU  372  C   ALA A 172    11234   7199  10998    652  -1737   -577       C  
ATOM    373  O   ALA A 172     -19.068 -12.462   5.942  1.00 76.57           O  
ANISOU  373  O   ALA A 172    11018   7149  10926    772  -1817   -627       O  
ATOM    374  CB  ALA A 172     -16.409 -13.255   4.550  1.00 73.41           C  
ANISOU  374  CB  ALA A 172    11079   6853   9959    326  -1431   -209       C  
ATOM    375  N   GLY A 173     -17.492 -11.267   7.039  1.00 75.33           N  
ANISOU  375  N   GLY A 173    10786   6976  10858    692  -1650   -774       N  
ATOM    376  CA  GLY A 173     -18.183 -11.174   8.325  1.00 75.03           C  
ANISOU  376  CA  GLY A 173    10427   7084  10998    874  -1629  -1076       C  
ATOM    377  C   GLY A 173     -18.294 -12.521   9.022  1.00 73.84           C  
ANISOU  377  C   GLY A 173    10106   7305  10646    903  -1381  -1142       C  
ATOM    378  O   GLY A 173     -19.348 -12.863   9.580  1.00 72.62           O  
ANISOU  378  O   GLY A 173     9748   7267  10579   1035  -1391  -1302       O  
ATOM    379  N   VAL A 174     -17.188 -13.291   8.988  1.00 67.55           N  
ANISOU  379  N   VAL A 174     9389   6686   9592    771  -1158  -1023       N  
ATOM    380  CA  VAL A 174     -17.091 -14.647   9.566  1.00 65.57           C  
ANISOU  380  CA  VAL A 174     9021   6763   9130    772   -932  -1037       C  
ATOM    381  C   VAL A 174     -16.375 -14.683  10.936  1.00 68.04           C  
ANISOU  381  C   VAL A 174     9157   7301   9395    792   -754  -1220       C  
ATOM    382  O   VAL A 174     -16.118 -15.766  11.483  1.00 65.11           O  
ANISOU  382  O   VAL A 174     8715   7187   8836    779   -578  -1215       O  
ATOM    383  CB  VAL A 174     -16.482 -15.669   8.579  1.00 68.65           C  
ANISOU  383  CB  VAL A 174     9602   7203   9279    634   -834   -797       C  
ATOM    384  CG1 VAL A 174     -17.535 -16.174   7.604  1.00 68.70           C  
ANISOU  384  CG1 VAL A 174     9698   7129   9276    659   -969   -674       C  
ATOM    385  CG2 VAL A 174     -15.282 -15.098   7.835  1.00 69.22           C  
ANISOU  385  CG2 VAL A 174     9883   7119   9297    472   -817   -662       C  
ATOM    386  N   GLU A 175     -16.133 -13.506  11.482  1.00 67.58           N  
ANISOU  386  N   GLU A 175     9030   7135   9513    832   -821  -1388       N  
ATOM    387  CA  GLU A 175     -15.509 -13.376  12.773  1.00 69.32           C  
ANISOU  387  CA  GLU A 175     9087   7548   9702    862   -692  -1593       C  
ATOM    388  C   GLU A 175     -16.217 -14.208  13.842  1.00 74.84           C  
ANISOU  388  C   GLU A 175     9590   8549  10296    957   -569  -1740       C  
ATOM    389  O   GLU A 175     -15.580 -14.830  14.652  1.00 71.34           O  
ANISOU  389  O   GLU A 175     9089   8347   9671    934   -415  -1783       O  
ATOM    390  CB  GLU A 175     -15.338 -11.899  13.155  1.00 73.29           C  
ANISOU  390  CB  GLU A 175     9530   7858  10459    910   -822  -1785       C  
ATOM    391  CG  GLU A 175     -16.549 -11.007  12.933  1.00 95.47           C  
ANISOU  391  CG  GLU A 175    12221  10832  13222    908   -707  -1971       C  
ATOM    392  CD  GLU A 175     -16.480 -10.114  11.705  1.00135.96           C  
ANISOU  392  CD  GLU A 175    17449  15848  18362    781   -682  -1914       C  
ATOM    393  OE1 GLU A 175     -17.261 -10.322  10.787  1.00143.76           O  
ANISOU  393  OE1 GLU A 175    18600  16550  19471    687   -785  -1767       O  
ATOM    394  OE2 GLU A 175     -15.689  -9.182  11.657  1.00131.43           O  
ANISOU  394  OE2 GLU A 175    16783  15465  17688    773   -569  -2032       O  
ATOM    395  N   HIS A 176     -17.534 -14.294  13.783  1.00 77.03           N  
ANISOU  395  N   HIS A 176     9778   8811  10681   1048   -641  -1800       N  
ATOM    396  CA  HIS A 176     -18.272 -15.075  14.768  1.00 79.46           C  
ANISOU  396  CA  HIS A 176     9904   9402  10886   1106   -498  -1931       C  
ATOM    397  C   HIS A 176     -18.001 -16.525  14.602  1.00 77.05           C  
ANISOU  397  C   HIS A 176     9667   9279  10329   1028   -356  -1729       C  
ATOM    398  O   HIS A 176     -17.839 -17.246  15.553  1.00 76.85           O  
ANISOU  398  O   HIS A 176     9560   9517  10124   1017   -195  -1782       O  
ATOM    399  CB  HIS A 176     -19.778 -14.876  14.648  1.00 85.32           C  
ANISOU  399  CB  HIS A 176    10473  10103  11842   1222   -581  -2115       C  
ATOM    400  CG  HIS A 176     -20.585 -16.043  15.142  1.00 92.72           C  
ANISOU  400  CG  HIS A 176    11185  11319  12725   1276   -419  -2386       C  
ATOM    401  ND1 HIS A 176     -20.871 -16.242  16.475  1.00 97.42           N  
ANISOU  401  ND1 HIS A 176    11663  11920  13431   1339   -436  -2659       N  
ATOM    402  CD2 HIS A 176     -21.179 -17.066  14.478  1.00 96.14           C  
ANISOU  402  CD2 HIS A 176    11522  12043  12965   1251   -224  -2407       C  
ATOM    403  CE1 HIS A 176     -21.593 -17.340  16.612  1.00 98.41           C  
ANISOU  403  CE1 HIS A 176    11626  12350  13416   1354   -250  -2849       C  
ATOM    404  NE2 HIS A 176     -21.790 -17.861  15.416  1.00 97.99           N  
ANISOU  404  NE2 HIS A 176    11586  12476  13171   1293   -113  -2695       N  
ATOM    405  N   GLN A 177     -17.939 -16.970  13.351  1.00 68.58           N  
ANISOU  405  N   GLN A 177     8764   8063   9229    963   -420  -1494       N  
ATOM    406  CA  GLN A 177     -17.736 -18.379  13.007  1.00 65.49           C  
ANISOU  406  CA  GLN A 177     8447   7807   8629    888   -308  -1301       C  
ATOM    407  C   GLN A 177     -16.370 -18.901  13.400  1.00 64.74           C  
ANISOU  407  C   GLN A 177     8415   7845   8340    805   -178  -1228       C  
ATOM    408  O   GLN A 177     -16.225 -20.020  13.814  1.00 62.48           O  
ANISOU  408  O   GLN A 177     8101   7754   7886    779    -58  -1169       O  
ATOM    409  CB  GLN A 177     -17.909 -18.600  11.510  1.00 66.86           C  
ANISOU  409  CB  GLN A 177     8779   7787   8836    849   -427  -1108       C  
ATOM    410  CG  GLN A 177     -19.317 -18.479  10.974  1.00 89.86           C  
ANISOU  410  CG  GLN A 177    11590  10641  11912    941   -539  -1178       C  
ATOM    411  CD  GLN A 177     -19.409 -18.888   9.514  1.00121.20           C  
ANISOU  411  CD  GLN A 177    15716  14487  15846    895   -635   -976       C  
ATOM    412  OE1 GLN A 177     -18.416 -19.252   8.897  1.00114.31           O  
ANISOU  412  OE1 GLN A 177    15053  13499  14879    802   -668   -809       O  
ATOM    413  NE2 GLN A 177     -20.609 -18.838   8.958  1.00120.84           N  
ANISOU  413  NE2 GLN A 177    15573  14478  15864    946   -667   -995       N  
ATOM    414  N   LEU A 178     -15.363 -18.077  13.232  1.00 59.93           N  
ANISOU  414  N   LEU A 178     7879   7118   7775    761   -212  -1242       N  
ATOM    415  CA  LEU A 178     -13.992 -18.409  13.617  1.00 58.70           C  
ANISOU  415  CA  LEU A 178     7749   7063   7491    693   -112  -1222       C  
ATOM    416  C   LEU A 178     -13.877 -18.529  15.157  1.00 61.61           C  
ANISOU  416  C   LEU A 178     7970   7667   7773    754    -36  -1397       C  
ATOM    417  O   LEU A 178     -13.266 -19.475  15.668  1.00 59.57           O  
ANISOU  417  O   LEU A 178     7708   7581   7346    726     50  -1348       O  
ATOM    418  CB  LEU A 178     -13.022 -17.322  13.091  1.00 59.74           C  
ANISOU  418  CB  LEU A 178     7971   6991   7738    625   -170  -1228       C  
ATOM    419  CG  LEU A 178     -11.549 -17.454  13.525  1.00 64.85           C  
ANISOU  419  CG  LEU A 178     8607   7717   8315    558    -82  -1261       C  
ATOM    420  CD1 LEU A 178     -10.891 -18.680  12.911  1.00 63.23           C  
ANISOU  420  CD1 LEU A 178     8478   7581   7967    472     11  -1098       C  
ATOM    421  CD2 LEU A 178     -10.775 -16.225  13.185  1.00 67.95           C  
ANISOU  421  CD2 LEU A 178     9047   7907   8863    494   -134  -1310       C  
ATOM    422  N   ARG A 179     -14.535 -17.627  15.869  1.00 59.33           N  
ANISOU  422  N   ARG A 179     7565   7378   7602    838    -81  -1607       N  
ATOM    423  CA  ARG A 179     -14.619 -17.680  17.314  1.00 60.82           C  
ANISOU  423  CA  ARG A 179     7622   7797   7689    892     -9  -1800       C  
ATOM    424  C   ARG A 179     -15.274 -18.953  17.767  1.00 63.69           C  
ANISOU  424  C   ARG A 179     7946   8382   7872    891    102  -1735       C  
ATOM    425  O   ARG A 179     -14.894 -19.519  18.760  1.00 61.40           O  
ANISOU  425  O   ARG A 179     7637   8309   7382    876    186  -1755       O  
ATOM    426  CB  ARG A 179     -15.445 -16.524  17.840  1.00 64.46           C  
ANISOU  426  CB  ARG A 179     7955   8200   8336    982    -77  -2065       C  
ATOM    427  CG  ARG A 179     -14.693 -15.248  18.138  1.00 80.95           C  
ANISOU  427  CG  ARG A 179    10078  10095  10585    970   -177  -2144       C  
ATOM    428  CD  ARG A 179     -15.648 -14.218  18.727  1.00107.00           C  
ANISOU  428  CD  ARG A 179    13244  13322  14088   1063   -260  -2432       C  
ATOM    429  NE  ARG A 179     -15.448 -12.901  18.144  1.00128.70           N  
ANISOU  429  NE  ARG A 179    15940  16170  16791   1067   -244  -2609       N  
ATOM    430  CZ  ARG A 179     -16.359 -12.249  17.439  1.00146.92           C  
ANISOU  430  CZ  ARG A 179    18289  18295  19239   1027   -324  -2635       C  
ATOM    431  NH1 ARG A 179     -17.549 -12.776  17.241  1.00133.63           N  
ANISOU  431  NH1 ARG A 179    16722  16317  17734    964   -414  -2476       N  
ATOM    432  NH2 ARG A 179     -16.076 -11.054  16.945  1.00137.13           N  
ANISOU  432  NH2 ARG A 179    16982  17166  17957   1040   -316  -2819       N  
ATOM    433  N   ARG A 180     -16.285 -19.391  17.040  1.00 59.70           N  
ANISOU  433  N   ARG A 180     7444   7803   7434    894     89  -1635       N  
ATOM    434  CA  ARG A 180     -16.998 -20.601  17.381  1.00 59.73           C  
ANISOU  434  CA  ARG A 180     7405   7977   7312    876    192  -1561       C  
ATOM    435  C   ARG A 180     -16.154 -21.824  17.087  1.00 65.34           C  
ANISOU  435  C   ARG A 180     8229   8762   7837    798    246  -1342       C  
ATOM    436  O   ARG A 180     -16.209 -22.795  17.801  1.00 67.12           O  
ANISOU  436  O   ARG A 180     8433   9188   7882    769    344  -1308       O  
ATOM    437  CB  ARG A 180     -18.318 -20.657  16.638  1.00 63.50           C  
ANISOU  437  CB  ARG A 180     7840   8328   7959    907    135  -1540       C  
ATOM    438  CG  ARG A 180     -19.185 -21.841  16.987  1.00 86.57           C  
ANISOU  438  CG  ARG A 180    10571  11414  10908    953    227  -1741       C  
ATOM    439  CD  ARG A 180     -20.148 -21.489  18.096  1.00107.30           C  
ANISOU  439  CD  ARG A 180    13099  13953  13716    989    185  -1764       C  
ATOM    440  NE  ARG A 180     -19.622 -20.385  18.887  1.00122.82           N  
ANISOU  440  NE  ARG A 180    15054  15647  15965   1072    -16  -1844       N  
ATOM    441  CZ  ARG A 180     -19.252 -20.474  20.160  1.00138.60           C  
ANISOU  441  CZ  ARG A 180    17167  17426  18069   1071   -168  -1679       C  
ATOM    442  NH1 ARG A 180     -18.773 -19.414  20.784  1.00128.16           N  
ANISOU  442  NH1 ARG A 180    15854  15847  16992   1144   -376  -1743       N  
ATOM    443  NH2 ARG A 180     -19.362 -21.619  20.806  1.00119.65           N  
ANISOU  443  NH2 ARG A 180    14883  15053  15526    995   -129  -1450       N  
ATOM    444  N   GLU A 181     -15.357 -21.768  16.035  1.00 58.60           N  
ANISOU  444  N   GLU A 181     7498   7741   7025    755    181  -1202       N  
ATOM    445  CA  GLU A 181     -14.493 -22.877  15.699  1.00 55.89           C  
ANISOU  445  CA  GLU A 181     7248   7428   6558    688    214  -1026       C  
ATOM    446  C   GLU A 181     -13.540 -23.070  16.844  1.00 58.38           C  
ANISOU  446  C   GLU A 181     7546   7907   6728    684    250  -1078       C  
ATOM    447  O   GLU A 181     -13.407 -24.151  17.360  1.00 57.96           O  
ANISOU  447  O   GLU A 181     7506   7993   6525    661    295   -985       O  
ATOM    448  CB  GLU A 181     -13.727 -22.631  14.388  1.00 55.11           C  
ANISOU  448  CB  GLU A 181     7269   7120   6551    635    153   -927       C  
ATOM    449  CG  GLU A 181     -12.679 -23.686  14.064  1.00 59.84           C  
ANISOU  449  CG  GLU A 181     7931   7742   7062    570    191   -824       C  
ATOM    450  CD  GLU A 181     -12.032 -23.553  12.691  1.00 76.81           C  
ANISOU  450  CD  GLU A 181    10194   9723   9267    490    179   -730       C  
ATOM    451  OE1 GLU A 181     -12.461 -22.732  11.878  1.00 72.93           O  
ANISOU  451  OE1 GLU A 181     9772   9068   8870    471    123   -722       O  
ATOM    452  OE2 GLU A 181     -11.078 -24.284  12.421  1.00 63.47           O  
ANISOU  452  OE2 GLU A 181     8528   8064   7522    441    222   -668       O  
ATOM    453  N   VAL A 182     -12.879 -21.989  17.216  1.00 52.98           N  
ANISOU  453  N   VAL A 182     6841   7184   6104    705    208  -1223       N  
ATOM    454  CA  VAL A 182     -11.868 -21.978  18.262  1.00 52.46           C  
ANISOU  454  CA  VAL A 182     6754   7245   5933    714    202  -1311       C  
ATOM    455  C   VAL A 182     -12.478 -22.485  19.585  1.00 59.14           C  
ANISOU  455  C   VAL A 182     7556   8335   6581    738    259  -1361       C  
ATOM    456  O   VAL A 182     -11.938 -23.395  20.217  1.00 60.30           O  
ANISOU  456  O   VAL A 182     7744   8610   6557    717    259  -1283       O  
ATOM    457  CB  VAL A 182     -11.250 -20.558  18.392  1.00 56.24           C  
ANISOU  457  CB  VAL A 182     7194   7621   6555    738    142  -1496       C  
ATOM    458  CG1 VAL A 182     -10.357 -20.452  19.629  1.00 56.65           C  
ANISOU  458  CG1 VAL A 182     7202   7823   6498    765    117  -1636       C  
ATOM    459  CG2 VAL A 182     -10.506 -20.150  17.116  1.00 55.52           C  
ANISOU  459  CG2 VAL A 182     7173   7300   6624    674    109  -1421       C  
ATOM    460  N   GLU A 183     -13.612 -21.891  19.959  1.00 57.63           N  
ANISOU  460  N   GLU A 183     7282   8196   6420    775    303  -1492       N  
ATOM    461  CA  GLU A 183     -14.389 -22.172  21.157  1.00 60.63           C  
ANISOU  461  CA  GLU A 183     7605   8813   6620    779    397  -1579       C  
ATOM    462  C   GLU A 183     -14.736 -23.657  21.232  1.00 64.64           C  
ANISOU  462  C   GLU A 183     8174   9428   6958    711    467  -1364       C  
ATOM    463  O   GLU A 183     -14.381 -24.317  22.206  1.00 63.97           O  
ANISOU  463  O   GLU A 183     8142   9520   6645    677    490  -1320       O  
ATOM    464  CB  GLU A 183     -15.657 -21.295  21.136  1.00 63.57           C  
ANISOU  464  CB  GLU A 183     7849   9162   7144    827    437  -1763       C  
ATOM    465  CG  GLU A 183     -15.471 -19.800  21.272  1.00 82.05           C  
ANISOU  465  CG  GLU A 183    10098  11740   9337    810    579  -1874       C  
ATOM    466  CD  GLU A 183     -16.797 -19.066  21.160  1.00116.77           C  
ANISOU  466  CD  GLU A 183    14364  16058  13945    843    614  -1966       C  
ATOM    467  OE1 GLU A 183     -17.811 -19.703  20.792  1.00108.11           O  
ANISOU  467  OE1 GLU A 183    13156  14873  13049    921    562  -2198       O  
ATOM    468  OE2 GLU A 183     -16.834 -17.866  21.515  1.00112.32           O  
ANISOU  468  OE2 GLU A 183    13806  15491  13380    795    667  -1809       O  
ATOM    469  N   ILE A 184     -15.338 -24.192  20.165  1.00 59.90           N  
ANISOU  469  N   ILE A 184     7584   8702   6474    689    475  -1219       N  
ATOM    470  CA  ILE A 184     -15.798 -25.569  20.094  1.00 58.90           C  
ANISOU  470  CA  ILE A 184     7500   8639   6241    624    535  -1021       C  
ATOM    471  C   ILE A 184     -14.643 -26.556  20.014  1.00 61.99           C  
ANISOU  471  C   ILE A 184     8006   9010   6538    591    468   -843       C  
ATOM    472  O   ILE A 184     -14.588 -27.464  20.829  1.00 62.97           O  
ANISOU  472  O   ILE A 184     8180   9271   6473    544    495   -742       O  
ATOM    473  CB  ILE A 184     -16.850 -25.742  18.951  1.00 61.36           C  
ANISOU  473  CB  ILE A 184     7768   8810   6734    622    544   -961       C  
ATOM    474  CG1 ILE A 184     -18.163 -25.009  19.340  1.00 63.02           C  
ANISOU  474  CG1 ILE A 184     7832   9088   7025    652    620  -1153       C  
ATOM    475  CG2 ILE A 184     -17.115 -27.218  18.600  1.00 60.05           C  
ANISOU  475  CG2 ILE A 184     7657   8645   6513    554    572   -739       C  
ATOM    476  CD1 ILE A 184     -19.210 -24.777  18.221  1.00 78.55           C  
ANISOU  476  CD1 ILE A 184     9731  10879   9234    687    570  -1166       C  
ATOM    477  N   GLN A 185     -13.713 -26.394  19.081  1.00 54.57           N  
ANISOU  477  N   GLN A 185     7106   7900   5728    607    381   -808       N  
ATOM    478  CA  GLN A 185     -12.669 -27.384  18.909  1.00 52.94           C  
ANISOU  478  CA  GLN A 185     6974   7661   5480    582    319   -669       C  
ATOM    479  C   GLN A 185     -11.605 -27.465  19.988  1.00 56.78           C  
ANISOU  479  C   GLN A 185     7488   8253   5832    597    250   -710       C  
ATOM    480  O   GLN A 185     -10.868 -28.468  20.059  1.00 54.26           O  
ANISOU  480  O   GLN A 185     7223   7923   5470    583    178   -590       O  
ATOM    481  CB  GLN A 185     -12.000 -27.212  17.561  1.00 52.14           C  
ANISOU  481  CB  GLN A 185     6894   7363   5555    577    274   -645       C  
ATOM    482  CG  GLN A 185     -12.640 -28.095  16.570  1.00 51.58           C  
ANISOU  482  CG  GLN A 185     6850   7210   5538    543    297   -502       C  
ATOM    483  CD  GLN A 185     -12.064 -27.784  15.229  1.00 71.32           C  
ANISOU  483  CD  GLN A 185     9388   9536   8176    524    272   -497       C  
ATOM    484  OE1 GLN A 185     -12.595 -26.963  14.475  1.00 61.32           O  
ANISOU  484  OE1 GLN A 185     8132   8166   7000    524    273   -531       O  
ATOM    485  NE2 GLN A 185     -11.058 -28.522  14.837  1.00 56.14           N  
ANISOU  485  NE2 GLN A 185     7492   7570   6270    499    247   -444       N  
ATOM    486  N   SER A 186     -11.454 -26.400  20.792  1.00 54.88           N  
ANISOU  486  N   SER A 186     7208   8097   5547    635    245   -895       N  
ATOM    487  CA  SER A 186     -10.467 -26.480  21.868  1.00 56.02           C  
ANISOU  487  CA  SER A 186     7385   8351   5549    654    154   -945       C  
ATOM    488  C   SER A 186     -11.030 -27.243  23.072  1.00 61.49           C  
ANISOU  488  C   SER A 186     8146   9252   5966    616    186   -864       C  
ATOM    489  O   SER A 186     -10.250 -27.777  23.840  1.00 64.01           O  
ANISOU  489  O   SER A 186     8541   9642   6139    617     78   -814       O  
ATOM    490  CB  SER A 186      -9.943 -25.103  22.247  1.00 58.52           C  
ANISOU  490  CB  SER A 186     7638   8668   5928    705    118  -1181       C  
ATOM    491  OG  SER A 186     -11.017 -24.273  22.622  1.00 64.36           O  
ANISOU  491  OG  SER A 186     8319   9489   6647    719    211  -1319       O  
ATOM    492  N   HIS A 187     -12.366 -27.332  23.213  1.00 57.68           N  
ANISOU  492  N   HIS A 187     7639   8860   5415    573    327   -847       N  
ATOM    493  CA  HIS A 187     -12.981 -27.996  24.362  1.00 60.89           C  
ANISOU  493  CA  HIS A 187     8115   9480   5543    503    399   -775       C  
ATOM    494  C   HIS A 187     -13.441 -29.410  24.111  1.00 63.89           C  
ANISOU  494  C   HIS A 187     8566   9835   5875    423    427   -517       C  
ATOM    495  O   HIS A 187     -13.500 -30.193  25.053  1.00 65.96           O  
ANISOU  495  O   HIS A 187     8938  10232   5891    351    427   -392       O  
ATOM    496  CB  HIS A 187     -14.115 -27.160  24.966  1.00 64.49           C  
ANISOU  496  CB  HIS A 187     8480  10096   5926    488    561   -968       C  
ATOM    497  CG  HIS A 187     -13.586 -25.896  25.580  1.00 70.12           C  
ANISOU  497  CG  HIS A 187     9145  10871   6627    560    514  -1229       C  
ATOM    498  ND1 HIS A 187     -13.614 -24.705  24.873  1.00 71.66           N  
ANISOU  498  ND1 HIS A 187     9219  10921   7087    637    500  -1413       N  
ATOM    499  CD2 HIS A 187     -12.844 -25.716  26.703  1.00 73.98           C  
ANISOU  499  CD2 HIS A 187     9704  11508   6897    570    437  -1312       C  
ATOM    500  CE1 HIS A 187     -13.016 -23.813  25.645  1.00 72.63           C  
ANISOU  500  CE1 HIS A 187     9322  11120   7153    686    442  -1622       C  
ATOM    501  NE2 HIS A 187     -12.497 -24.381  26.737  1.00 74.27           N  
ANISOU  501  NE2 HIS A 187     9641  11507   7073    653    397  -1575       N  
ATOM    502  N   LEU A 188     -13.774 -29.748  22.873  1.00 59.04           N  
ANISOU  502  N   LEU A 188     7905   9047   5482    425    442   -433       N  
ATOM    503  CA  LEU A 188     -14.184 -31.107  22.515  1.00 59.77           C  
ANISOU  503  CA  LEU A 188     8051   9085   5575    354    454   -201       C  
ATOM    504  C   LEU A 188     -12.986 -32.063  22.610  1.00 62.94           C  
ANISOU  504  C   LEU A 188     8561   9409   5944    363    281    -46       C  
ATOM    505  O   LEU A 188     -11.862 -31.695  22.258  1.00 62.36           O  
ANISOU  505  O   LEU A 188     8473   9238   5981    437    160   -122       O  
ATOM    506  CB  LEU A 188     -14.756 -31.185  21.077  1.00 58.88           C  
ANISOU  506  CB  LEU A 188     7860   8795   5718    368    487   -177       C  
ATOM    507  CG  LEU A 188     -15.796 -30.161  20.601  1.00 64.98           C  
ANISOU  507  CG  LEU A 188     8510   9557   6622    394    589   -342       C  
ATOM    508  CD1 LEU A 188     -16.133 -30.384  19.124  1.00 65.35           C  
ANISOU  508  CD1 LEU A 188     8525   9407   6896    409    560   -284       C  
ATOM    509  CD2 LEU A 188     -17.042 -30.211  21.437  1.00 71.68           C  
ANISOU  509  CD2 LEU A 188     9302  10583   7352    326    747   -384       C  
ATOM    510  N   ARG A 189     -13.243 -33.278  23.114  1.00 59.11           N  
ANISOU  510  N   ARG A 189     8176   8960   5322    281    267    164       N  
ATOM    511  CA  ARG A 189     -12.247 -34.332  23.229  1.00 58.96           C  
ANISOU  511  CA  ARG A 189     8260   8844   5297    289     77    328       C  
ATOM    512  C   ARG A 189     -12.914 -35.602  22.785  1.00 62.11           C  
ANISOU  512  C   ARG A 189     8691   9150   5757    210    102    541       C  
ATOM    513  O   ARG A 189     -13.812 -36.106  23.454  1.00 65.25           O  
ANISOU  513  O   ARG A 189     9151   9656   5985     98    203    666       O  
ATOM    514  CB  ARG A 189     -11.706 -34.507  24.664  1.00 62.53           C  
ANISOU  514  CB  ARG A 189     8855   9441   5463    265    -33    381       C  
ATOM    515  CG  ARG A 189     -11.024 -33.307  25.290  1.00 73.90           C  
ANISOU  515  CG  ARG A 189    10272  10989   6818    340    -80    160       C  
ATOM    516  CD  ARG A 189      -9.716 -32.887  24.649  1.00 84.41           C  
ANISOU  516  CD  ARG A 189    11526  12166   8381    457   -238     33       C  
ATOM    517  NE  ARG A 189      -9.612 -31.430  24.712  1.00 94.89           N  
ANISOU  517  NE  ARG A 189    12756  13559   9738    511   -172   -223       N  
ATOM    518  CZ  ARG A 189      -8.937 -30.769  25.648  1.00107.04           C  
ANISOU  518  CZ  ARG A 189    14320  15205  11147    555   -269   -362       C  
ATOM    519  NH1 ARG A 189      -8.246 -31.428  26.567  1.00 96.38           N  
ANISOU  519  NH1 ARG A 189    13096  13904   9620    557   -456   -268       N  
ATOM    520  NH2 ARG A 189      -8.923 -29.444  25.651  1.00 92.79           N  
ANISOU  520  NH2 ARG A 189    12415  13440   9401    600   -205   -601       N  
ATOM    521  N   HIS A 190     -12.481 -36.090  21.621  1.00 55.65           N  
ANISOU  521  N   HIS A 190     7821   8133   5191    258     24    566       N  
ATOM    522  CA  HIS A 190     -12.958 -37.300  20.989  1.00 53.34           C  
ANISOU  522  CA  HIS A 190     7536   7709   5021    205     17    736       C  
ATOM    523  C   HIS A 190     -11.905 -37.734  19.964  1.00 56.02           C  
ANISOU  523  C   HIS A 190     7834   7847   5602    288   -131    707       C  
ATOM    524  O   HIS A 190     -11.353 -36.874  19.275  1.00 53.40           O  
ANISOU  524  O   HIS A 190     7423   7480   5386    359   -120    532       O  
ATOM    525  CB  HIS A 190     -14.300 -37.037  20.291  1.00 51.56           C  
ANISOU  525  CB  HIS A 190     7216   7495   4881    160    204    696       C  
ATOM    526  CG  HIS A 190     -15.011 -38.295  19.911  1.00 54.83           C  
ANISOU  526  CG  HIS A 190     7641   7811   5382     79    216    874       C  
ATOM    527  ND1 HIS A 190     -14.704 -38.973  18.735  1.00 54.93           N  
ANISOU  527  ND1 HIS A 190     7616   7628   5627    119    129    896       N  
ATOM    528  CD2 HIS A 190     -15.974 -38.977  20.573  1.00 57.21           C  
ANISOU  528  CD2 HIS A 190     7985   8183   5570    -48    311   1024       C  
ATOM    529  CE1 HIS A 190     -15.478 -40.043  18.733  1.00 54.99           C  
ANISOU  529  CE1 HIS A 190     7641   7583   5671     28    152   1058       C  
ATOM    530  NE2 HIS A 190     -16.263 -40.083  19.817  1.00 57.06           N  
ANISOU  530  NE2 HIS A 190     7951   7996   5733    -81    266   1148       N  
ATOM    531  N   PRO A 191     -11.615 -39.055  19.829  1.00 55.94           N  
ANISOU  531  N   PRO A 191     7872   7700   5683    272   -262    866       N  
ATOM    532  CA  PRO A 191     -10.615 -39.488  18.831  1.00 53.62           C  
ANISOU  532  CA  PRO A 191     7511   7222   5639    351   -388    796       C  
ATOM    533  C   PRO A 191     -10.995 -39.218  17.374  1.00 52.80           C  
ANISOU  533  C   PRO A 191     7305   7040   5719    362   -271    682       C  
ATOM    534  O   PRO A 191     -10.116 -39.268  16.526  1.00 52.33           O  
ANISOU  534  O   PRO A 191     7182   6871   5830    418   -328    569       O  
ATOM    535  CB  PRO A 191     -10.454 -40.989  19.109  1.00 56.94           C  
ANISOU  535  CB  PRO A 191     8005   7510   6119    324   -555    994       C  
ATOM    536  CG  PRO A 191     -11.718 -41.396  19.754  1.00 64.13           C  
ANISOU  536  CG  PRO A 191     9001   8505   6861    201   -449   1182       C  
ATOM    537  CD  PRO A 191     -12.139 -40.210  20.599  1.00 60.30           C  
ANISOU  537  CD  PRO A 191     8540   8247   6123    174   -307   1108       C  
ATOM    538  N   ASN A 192     -12.285 -38.932  17.082  1.00 47.76           N  
ANISOU  538  N   ASN A 192     6648   6458   5042    305   -114    702       N  
ATOM    539  CA  ASN A 192     -12.751 -38.680  15.723  1.00 47.66           C  
ANISOU  539  CA  ASN A 192     6563   6368   5176    313    -33    611       C  
ATOM    540  C   ASN A 192     -13.116 -37.230  15.465  1.00 49.41           C  
ANISOU  540  C   ASN A 192     6749   6674   5352    332     81    465       C  
ATOM    541  O   ASN A 192     -13.839 -36.930  14.517  1.00 48.19           O  
ANISOU  541  O   ASN A 192     6559   6475   5276    325    146    419       O  
ATOM    542  CB  ASN A 192     -13.909 -39.618  15.354  1.00 53.49           C  
ANISOU  542  CB  ASN A 192     7292   7049   5981    246      6    733       C  
ATOM    543  CG  ASN A 192     -13.598 -41.069  15.519  1.00 62.74           C  
ANISOU  543  CG  ASN A 192     8500   8102   7236    223   -121    880       C  
ATOM    544  OD1 ASN A 192     -14.296 -41.799  16.228  1.00 64.23           O  
ANISOU  544  OD1 ASN A 192     8735   8305   7364    142   -113   1048       O  
ATOM    545  ND2 ASN A 192     -12.564 -41.513  14.849  1.00 48.48           N  
ANISOU  545  ND2 ASN A 192     6668   6167   5583    285   -235    812       N  
ATOM    546  N   ILE A 193     -12.597 -36.335  16.310  1.00 46.51           N  
ANISOU  546  N   ILE A 193     6394   6412   4867    361     81    389       N  
ATOM    547  CA  ILE A 193     -12.773 -34.896  16.203  1.00 44.82           C  
ANISOU  547  CA  ILE A 193     6145   6259   4627    387    161    239       C  
ATOM    548  C   ILE A 193     -11.378 -34.270  16.291  1.00 47.26           C  
ANISOU  548  C   ILE A 193     6449   6552   4956    439     92    120       C  
ATOM    549  O   ILE A 193     -10.621 -34.533  17.222  1.00 46.71           O  
ANISOU  549  O   ILE A 193     6405   6531   4812    458      3    137       O  
ATOM    550  CB  ILE A 193     -13.758 -34.333  17.261  1.00 48.43           C  
ANISOU  550  CB  ILE A 193     6594   6878   4929    360    254    228       C  
ATOM    551  CG1 ILE A 193     -15.192 -34.764  16.925  1.00 50.26           C  
ANISOU  551  CG1 ILE A 193     6788   7108   5202    306    345    294       C  
ATOM    552  CG2 ILE A 193     -13.672 -32.797  17.302  1.00 48.63           C  
ANISOU  552  CG2 ILE A 193     6578   6949   4952    408    295     44       C  
ATOM    553  CD1 ILE A 193     -16.094 -34.978  18.053  1.00 57.46           C  
ANISOU  553  CD1 ILE A 193     7696   8171   5964    236    441    349       C  
ATOM    554  N   LEU A 194     -11.047 -33.469  15.298  1.00 44.24           N  
ANISOU  554  N   LEU A 194     6038   6092   4679    452    125      4       N  
ATOM    555  CA  LEU A 194      -9.779 -32.781  15.234  1.00 43.24           C  
ANISOU  555  CA  LEU A 194     5887   5938   4604    479     90   -126       C  
ATOM    556  C   LEU A 194      -9.601 -31.771  16.378  1.00 47.55           C  
ANISOU  556  C   LEU A 194     6423   6599   5043    509     82   -218       C  
ATOM    557  O   LEU A 194     -10.426 -30.870  16.558  1.00 47.85           O  
ANISOU  557  O   LEU A 194     6455   6692   5034    509    152   -268       O  
ATOM    558  CB  LEU A 194      -9.635 -32.098  13.876  1.00 41.37           C  
ANISOU  558  CB  LEU A 194     5646   5595   4478    453    155   -208       C  
ATOM    559  CG  LEU A 194      -8.207 -31.650  13.509  1.00 43.43           C  
ANISOU  559  CG  LEU A 194     5870   5798   4834    446    147   -339       C  
ATOM    560  CD1 LEU A 194      -7.364 -32.855  13.023  1.00 41.99           C  
ANISOU  560  CD1 LEU A 194     5653   5547   4756    443    101   -335       C  
ATOM    561  CD2 LEU A 194      -8.275 -30.564  12.457  1.00 44.77           C  
ANISOU  561  CD2 LEU A 194     6071   5892   5049    396    232   -407       C  
ATOM    562  N   ARG A 195      -8.501 -31.917  17.130  1.00 44.64           N  
ANISOU  562  N   ARG A 195     6044   6259   4657    542    -19   -262       N  
ATOM    563  CA  ARG A 195      -8.153 -31.043  18.251  1.00 45.39           C  
ANISOU  563  CA  ARG A 195     6133   6465   4650    576    -56   -369       C  
ATOM    564  C   ARG A 195      -7.611 -29.691  17.773  1.00 49.81           C  
ANISOU  564  C   ARG A 195     6634   6970   5322    583    -14   -548       C  
ATOM    565  O   ARG A 195      -6.858 -29.613  16.798  1.00 46.28           O  
ANISOU  565  O   ARG A 195     6151   6402   5032    562      0   -600       O  
ATOM    566  CB  ARG A 195      -7.074 -31.691  19.113  1.00 47.56           C  
ANISOU  566  CB  ARG A 195     6417   6761   4890    615   -218   -362       C  
ATOM    567  CG  ARG A 195      -7.544 -32.819  20.072  1.00 59.82           C  
ANISOU  567  CG  ARG A 195     8066   8394   6267    602   -297   -178       C  
ATOM    568  CD  ARG A 195      -8.292 -32.331  21.320  1.00 79.76           C  
ANISOU  568  CD  ARG A 195    10656  11110   8537    583   -255   -173       C  
ATOM    569  NE  ARG A 195      -7.904 -30.983  21.766  1.00 89.21           N  
ANISOU  569  NE  ARG A 195    11805  12381   9710    623   -245   -380       N  
ATOM    570  CZ  ARG A 195      -6.891 -30.714  22.587  1.00107.87           C  
ANISOU  570  CZ  ARG A 195    14174  14788  12024    672   -390   -477       C  
ATOM    571  NH1 ARG A 195      -6.124 -31.697  23.058  1.00 93.71           N  
ANISOU  571  NH1 ARG A 195    12439  12967  10201    695   -576   -380       N  
ATOM    572  NH2 ARG A 195      -6.630 -29.458  22.940  1.00 90.11           N  
ANISOU  572  NH2 ARG A 195    11869  12596   9773    704   -374   -678       N  
ATOM    573  N   LEU A 196      -8.008 -28.629  18.460  1.00 47.40           N  
ANISOU  573  N   LEU A 196     6318   6750   4940    602     15   -648       N  
ATOM    574  CA  LEU A 196      -7.448 -27.298  18.269  1.00 47.85           C  
ANISOU  574  CA  LEU A 196     6323   6752   5104    610     27   -822       C  
ATOM    575  C   LEU A 196      -6.710 -27.052  19.597  1.00 53.37           C  
ANISOU  575  C   LEU A 196     7001   7566   5712    659    -78   -932       C  
ATOM    576  O   LEU A 196      -7.327 -27.138  20.653  1.00 54.35           O  
ANISOU  576  O   LEU A 196     7162   7841   5647    679    -89   -917       O  
ATOM    577  CB  LEU A 196      -8.518 -26.220  18.007  1.00 47.60           C  
ANISOU  577  CB  LEU A 196     6287   6706   5091    605    111   -876       C  
ATOM    578  CG  LEU A 196      -8.009 -24.855  17.553  1.00 52.27           C  
ANISOU  578  CG  LEU A 196     6843   7184   5833    596    118  -1024       C  
ATOM    579  CD1 LEU A 196      -8.998 -24.213  16.631  1.00 54.11           C  
ANISOU  579  CD1 LEU A 196     7105   7307   6148    574    174   -996       C  
ATOM    580  CD2 LEU A 196      -7.840 -23.903  18.726  1.00 56.65           C  
ANISOU  580  CD2 LEU A 196     7346   7833   6346    648     74  -1200       C  
ATOM    581  N   TYR A 197      -5.395 -26.843  19.541  1.00 49.10           N  
ANISOU  581  N   TYR A 197     6401   6959   5296    671   -156  -1042       N  
ATOM    582  CA  TYR A 197      -4.543 -26.673  20.712  1.00 49.95           C  
ANISOU  582  CA  TYR A 197     6483   7153   5344    726   -295  -1159       C  
ATOM    583  C   TYR A 197      -4.465 -25.251  21.225  1.00 57.52           C  
ANISOU  583  C   TYR A 197     7391   8145   6319    746   -289  -1359       C  
ATOM    584  O   TYR A 197      -4.129 -25.040  22.374  1.00 60.16           O  
ANISOU  584  O   TYR A 197     7726   8595   6537    795   -396  -1458       O  
ATOM    585  CB  TYR A 197      -3.125 -27.210  20.443  1.00 50.10           C  
ANISOU  585  CB  TYR A 197     6431   7075   5532    738   -407  -1210       C  
ATOM    586  CG  TYR A 197      -3.106 -28.681  20.088  1.00 50.42           C  
ANISOU  586  CG  TYR A 197     6507   7075   5575    736   -453  -1040       C  
ATOM    587  CD1 TYR A 197      -3.495 -29.647  21.011  1.00 54.11           C  
ANISOU  587  CD1 TYR A 197     7071   7638   5849    767   -564   -892       C  
ATOM    588  CD2 TYR A 197      -2.694 -29.106  18.838  1.00 49.02           C  
ANISOU  588  CD2 TYR A 197     6274   6760   5592    694   -386  -1031       C  
ATOM    589  CE1 TYR A 197      -3.489 -31.002  20.686  1.00 56.18           C  
ANISOU  589  CE1 TYR A 197     7368   7836   6143    764   -625   -733       C  
ATOM    590  CE2 TYR A 197      -2.659 -30.457  18.509  1.00 50.33           C  
ANISOU  590  CE2 TYR A 197     6457   6876   5788    700   -440   -904       C  
ATOM    591  CZ  TYR A 197      -3.075 -31.404  19.431  1.00 61.70           C  
ANISOU  591  CZ  TYR A 197     7989   8389   7066    739   -568   -750       C  
ATOM    592  OH  TYR A 197      -3.042 -32.747  19.127  1.00 68.35           O  
ANISOU  592  OH  TYR A 197     8850   9156   7965    746   -642   -621       O  
ATOM    593  N   GLY A 198      -4.700 -24.290  20.355  1.00 54.66           N  
ANISOU  593  N   GLY A 198     6993   7667   6107    707   -183  -1420       N  
ATOM    594  CA  GLY A 198      -4.624 -22.886  20.715  1.00 54.91           C  
ANISOU  594  CA  GLY A 198     6970   7686   6207    723   -184  -1615       C  
ATOM    595  C   GLY A 198      -4.686 -21.996  19.503  1.00 58.10           C  
ANISOU  595  C   GLY A 198     7357   7901   6816    658    -90  -1634       C  
ATOM    596  O   GLY A 198      -4.878 -22.472  18.380  1.00 54.54           O  
ANISOU  596  O   GLY A 198     6951   7352   6418    598    -14  -1493       O  
ATOM    597  N   TYR A 199      -4.494 -20.707  19.731  1.00 59.11           N  
ANISOU  597  N   TYR A 199     7431   7972   7056    663   -106  -1808       N  
ATOM    598  CA  TYR A 199      -4.555 -19.670  18.718  1.00 60.71           C  
ANISOU  598  CA  TYR A 199     7637   7977   7452    594    -44  -1829       C  
ATOM    599  C   TYR A 199      -3.680 -18.483  19.110  1.00 66.67           C  
ANISOU  599  C   TYR A 199     8304   8655   8373    587    -99  -2044       C  
ATOM    600  O   TYR A 199      -3.179 -18.403  20.234  1.00 68.06           O  
ANISOU  600  O   TYR A 199     8411   8950   8499    654   -192  -2197       O  
ATOM    601  CB  TYR A 199      -6.030 -19.225  18.508  1.00 63.06           C  
ANISOU  601  CB  TYR A 199     7988   8255   7715    619     -7  -1777       C  
ATOM    602  CG  TYR A 199      -6.652 -18.562  19.724  1.00 68.41           C  
ANISOU  602  CG  TYR A 199     8609   9059   8326    710    -53  -1951       C  
ATOM    603  CD1 TYR A 199      -7.262 -19.318  20.724  1.00 71.20           C  
ANISOU  603  CD1 TYR A 199     8967   9638   8449    769    -50  -1939       C  
ATOM    604  CD2 TYR A 199      -6.600 -17.179  19.892  1.00 71.26           C  
ANISOU  604  CD2 TYR A 199     8911   9313   8851    727    -96  -2137       C  
ATOM    605  CE1 TYR A 199      -7.807 -18.715  21.860  1.00 74.29           C  
ANISOU  605  CE1 TYR A 199     9304  10171   8751    837    -67  -2125       C  
ATOM    606  CE2 TYR A 199      -7.138 -16.564  21.024  1.00 73.93           C  
ANISOU  606  CE2 TYR A 199     9180   9776   9133    814   -134  -2338       C  
ATOM    607  CZ  TYR A 199      -7.741 -17.336  22.005  1.00 84.35           C  
ANISOU  607  CZ  TYR A 199    10504  11346  10199    866   -108  -2339       C  
ATOM    608  OH  TYR A 199      -8.252 -16.725  23.125  1.00 90.40           O  
ANISOU  608  OH  TYR A 199    11203  12259  10887    936   -121  -2561       O  
ATOM    609  N   PHE A 200      -3.504 -17.569  18.159  1.00 62.56           N  
ANISOU  609  N   PHE A 200     7796   7928   8045    498    -49  -2049       N  
ATOM    610  CA  PHE A 200      -2.784 -16.306  18.282  1.00 63.07           C  
ANISOU  610  CA  PHE A 200     7788   7860   8317    460    -84  -2231       C  
ATOM    611  C   PHE A 200      -3.063 -15.461  17.048  1.00 70.96           C  
ANISOU  611  C   PHE A 200     8872   8618   9473    346    -21  -2139       C  
ATOM    612  O   PHE A 200      -3.736 -15.936  16.123  1.00 70.54           O  
ANISOU  612  O   PHE A 200     8933   8522   9347    304     42  -1942       O  
ATOM    613  CB  PHE A 200      -1.282 -16.476  18.584  1.00 64.39           C  
ANISOU  613  CB  PHE A 200     7842   8039   8586    428   -113  -2362       C  
ATOM    614  CG  PHE A 200      -0.435 -17.228  17.585  1.00 64.16           C  
ANISOU  614  CG  PHE A 200     7811   7946   8621    315    -16  -2263       C  
ATOM    615  CD1 PHE A 200      -0.529 -18.610  17.471  1.00 63.81           C  
ANISOU  615  CD1 PHE A 200     7798   8019   8429    347     -3  -2131       C  
ATOM    616  CD2 PHE A 200       0.515 -16.565  16.822  1.00 65.99           C  
ANISOU  616  CD2 PHE A 200     7994   8004   9074    171     65  -2327       C  
ATOM    617  CE1 PHE A 200       0.288 -19.313  16.583  1.00 64.20           C  
ANISOU  617  CE1 PHE A 200     7819   8015   8557    252     86  -2085       C  
ATOM    618  CE2 PHE A 200       1.326 -17.268  15.920  1.00 68.58           C  
ANISOU  618  CE2 PHE A 200     8301   8296   9461     57    182  -2275       C  
ATOM    619  CZ  PHE A 200       1.214 -18.639  15.816  1.00 64.87           C  
ANISOU  619  CZ  PHE A 200     7848   7948   8851    107    187  -2169       C  
ATOM    620  N   HIS A 201      -2.632 -14.194  17.063  1.00 70.17           N  
ANISOU  620  N   HIS A 201     8728   8354   9579    299    -55  -2275       N  
ATOM    621  CA  HIS A 201      -2.839 -13.270  15.957  1.00 71.65           C  
ANISOU  621  CA  HIS A 201     9019   8283   9922    178    -23  -2180       C  
ATOM    622  C   HIS A 201      -1.779 -12.176  15.949  1.00 75.70           C  
ANISOU  622  C   HIS A 201     9460   8622  10682     75    -30  -2328       C  
ATOM    623  O   HIS A 201      -1.173 -11.900  16.983  1.00 74.47           O  
ANISOU  623  O   HIS A 201     9157   8543  10595    143    -99  -2549       O  
ATOM    624  CB  HIS A 201      -4.282 -12.699  15.940  1.00 73.64           C  
ANISOU  624  CB  HIS A 201     9342   8467  10171    264   -104  -2140       C  
ATOM    625  CG  HIS A 201      -4.623 -11.858  17.132  1.00 79.73           C  
ANISOU  625  CG  HIS A 201     9995   9275  11024    395   -218  -2384       C  
ATOM    626  ND1 HIS A 201      -4.766 -10.476  17.028  1.00 84.29           N  
ANISOU  626  ND1 HIS A 201    10566   9617  11841    378   -306  -2483       N  
ATOM    627  CD2 HIS A 201      -4.798 -12.217  18.426  1.00 82.56           C  
ANISOU  627  CD2 HIS A 201    10244   9875  11252    531   -258  -2551       C  
ATOM    628  CE1 HIS A 201      -5.014 -10.042  18.257  1.00 85.09           C  
ANISOU  628  CE1 HIS A 201    10535   9831  11963    514   -389  -2734       C  
ATOM    629  NE2 HIS A 201      -5.050 -11.052  19.133  1.00 84.68           N  
ANISOU  629  NE2 HIS A 201    10426  10078  11672    603   -356  -2781       N  
ATOM    630  N   ASP A 202      -1.601 -11.575  14.787  1.00 74.49           N  
ANISOU  630  N   ASP A 202     9417   8237  10649   -103     44  -2200       N  
ATOM    631  CA  ASP A 202      -0.683 -10.484  14.585  1.00 77.81           C  
ANISOU  631  CA  ASP A 202     9793   8451  11320   -246     63  -2302       C  
ATOM    632  C   ASP A 202      -1.339  -9.334  13.810  1.00 85.80           C  
ANISOU  632  C   ASP A 202    10955   9182  12465   -310     -9  -2199       C  
ATOM    633  O   ASP A 202      -2.541  -9.330  13.626  1.00 84.86           O  
ANISOU  633  O   ASP A 202    10921   9059  12265   -196   -103  -2116       O  
ATOM    634  CB  ASP A 202       0.603 -10.994  13.939  1.00 80.09           C  
ANISOU  634  CB  ASP A 202    10069   8725  11637   -444    244  -2254       C  
ATOM    635  CG  ASP A 202       0.511 -11.132  12.454  1.00 89.80           C  
ANISOU  635  CG  ASP A 202    11506   9782  12831   -655    377  -2010       C  
ATOM    636  OD1 ASP A 202      -0.565 -10.963  11.885  1.00 87.96           O  
ANISOU  636  OD1 ASP A 202    11424   9591  12407   -622    378  -1818       O  
ATOM    637  OD2 ASP A 202       1.540 -11.410  11.842  1.00105.55           O  
ANISOU  637  OD2 ASP A 202    13521  11593  14989   -863    472  -2014       O  
ATOM    638  N   ALA A 203      -0.561  -8.340  13.396  1.00 86.26           N  
ANISOU  638  N   ALA A 203    11040   8994  12740   -493     25  -2206       N  
ATOM    639  CA  ALA A 203      -1.122  -7.158  12.742  1.00 88.13           C  
ANISOU  639  CA  ALA A 203    11438   8919  13130   -577    -66  -2091       C  
ATOM    640  C   ALA A 203      -2.170  -7.473  11.660  1.00 90.37           C  
ANISOU  640  C   ALA A 203    11965   9129  13241   -606    -79  -1801       C  
ATOM    641  O   ALA A 203      -3.166  -6.756  11.564  1.00 90.88           O  
ANISOU  641  O   ALA A 203    12122   9019  13388   -530   -250  -1751       O  
ATOM    642  CB  ALA A 203       0.001  -6.314  12.153  1.00 91.35           C  
ANISOU  642  CB  ALA A 203    11869   9091  13750   -831     28  -2085       C  
ATOM    643  N   THR A 204      -1.972  -8.557  10.881  1.00 84.71           N  
ANISOU  643  N   THR A 204    11340   8544  12300   -699     81  -1633       N  
ATOM    644  CA  THR A 204      -2.868  -8.887   9.772  1.00 83.63           C  
ANISOU  644  CA  THR A 204    11445   8339  11990   -747     69  -1362       C  
ATOM    645  C   THR A 204      -3.418 -10.349   9.745  1.00 82.04           C  
ANISOU  645  C   THR A 204    11236   8410  11525   -629    123  -1295       C  
ATOM    646  O   THR A 204      -4.351 -10.627   8.984  1.00 81.06           O  
ANISOU  646  O   THR A 204    11288   8241  11270   -621     69  -1104       O  
ATOM    647  CB  THR A 204      -2.160  -8.530   8.441  1.00 99.70           C  
ANISOU  647  CB  THR A 204    13688  10180  14012  -1050    210  -1168       C  
ATOM    648  OG1 THR A 204      -2.960  -8.935   7.330  1.00104.19           O  
ANISOU  648  OG1 THR A 204    14510  10704  14372  -1105    195   -907       O  
ATOM    649  CG2 THR A 204      -0.764  -9.133   8.320  1.00 98.99           C  
ANISOU  649  CG2 THR A 204    13480  10232  13898  -1210    460  -1256       C  
ATOM    650  N   ARG A 205      -2.867 -11.239  10.567  1.00 74.17           N  
ANISOU  650  N   ARG A 205    10047   7671  10462   -541    205  -1444       N  
ATOM    651  CA  ARG A 205      -3.267 -12.646  10.522  1.00 70.85           C  
ANISOU  651  CA  ARG A 205     9626   7478   9817   -452    254  -1370       C  
ATOM    652  C   ARG A 205      -3.696 -13.264  11.859  1.00 71.50           C  
ANISOU  652  C   ARG A 205     9529   7791   9846   -228    178  -1523       C  
ATOM    653  O   ARG A 205      -3.225 -12.874  12.927  1.00 72.93           O  
ANISOU  653  O   ARG A 205     9548   8028  10134   -161    138  -1729       O  
ATOM    654  CB  ARG A 205      -2.152 -13.492   9.898  1.00 69.00           C  
ANISOU  654  CB  ARG A 205     9384   7336   9496   -607    456  -1335       C  
ATOM    655  CG  ARG A 205      -1.940 -13.241   8.414  1.00 74.09           C  
ANISOU  655  CG  ARG A 205    10235   7805  10109   -859    581  -1162       C  
ATOM    656  CD  ARG A 205      -1.060 -14.314   7.793  1.00 91.45           C  
ANISOU  656  CD  ARG A 205    12342  10070  12336  -1035    801  -1249       C  
ATOM    657  NE  ARG A 205       0.283 -14.320   8.367  1.00114.56           N  
ANISOU  657  NE  ARG A 205    15079  12950  15498  -1065    812  -1460       N  
ATOM    658  CZ  ARG A 205       1.280 -13.552   7.942  1.00137.04           C  
ANISOU  658  CZ  ARG A 205    17963  15610  18495  -1287    911  -1471       C  
ATOM    659  NH1 ARG A 205       1.089 -12.711   6.935  1.00130.25           N  
ANISOU  659  NH1 ARG A 205    17349  14597  17545  -1512   1015  -1264       N  
ATOM    660  NH2 ARG A 205       2.470 -13.624   8.524  1.00122.52           N  
ANISOU  660  NH2 ARG A 205    15925  13734  16892  -1296    904  -1687       N  
ATOM    661  N   VAL A 206      -4.595 -14.242  11.765  1.00 62.45           N  
ANISOU  661  N   VAL A 206     8422   6785   8521   -128    166  -1420       N  
ATOM    662  CA  VAL A 206      -5.041 -15.051  12.888  1.00 59.83           C  
ANISOU  662  CA  VAL A 206     7962   6691   8079     50    125  -1510       C  
ATOM    663  C   VAL A 206      -4.480 -16.450  12.575  1.00 62.83           C  
ANISOU  663  C   VAL A 206     8333   7221   8317     10    236  -1432       C  
ATOM    664  O   VAL A 206      -4.521 -16.899  11.424  1.00 61.44           O  
ANISOU  664  O   VAL A 206     8282   6988   8075    -96    315  -1274       O  
ATOM    665  CB  VAL A 206      -6.584 -15.053  13.047  1.00 62.32           C  
ANISOU  665  CB  VAL A 206     8316   7025   8337    180     26  -1459       C  
ATOM    666  CG1 VAL A 206      -7.023 -15.998  14.159  1.00 60.78           C  
ANISOU  666  CG1 VAL A 206     8006   7092   7995    323     24  -1529       C  
ATOM    667  CG2 VAL A 206      -7.114 -13.645  13.317  1.00 63.16           C  
ANISOU  667  CG2 VAL A 206     8410   6958   8629    228   -100  -1566       C  
ATOM    668  N   TYR A 207      -3.917 -17.100  13.596  1.00 59.34           N  
ANISOU  668  N   TYR A 207     7749   6962   7837     94    228  -1555       N  
ATOM    669  CA  TYR A 207      -3.282 -18.418  13.501  1.00 57.82           C  
ANISOU  669  CA  TYR A 207     7515   6899   7555     83    294  -1520       C  
ATOM    670  C   TYR A 207      -3.959 -19.424  14.399  1.00 56.41           C  
ANISOU  670  C   TYR A 207     7301   6916   7215    229    228  -1495       C  
ATOM    671  O   TYR A 207      -4.013 -19.213  15.620  1.00 55.40           O  
ANISOU  671  O   TYR A 207     7091   6896   7062    334    144  -1619       O  
ATOM    672  CB  TYR A 207      -1.819 -18.323  13.934  1.00 60.72           C  
ANISOU  672  CB  TYR A 207     7739   7281   8052     43    311  -1693       C  
ATOM    673  CG  TYR A 207      -0.977 -17.369  13.121  1.00 65.42           C  
ANISOU  673  CG  TYR A 207     8345   7691   8823   -131    406  -1738       C  
ATOM    674  CD1 TYR A 207      -0.270 -17.809  12.011  1.00 68.15           C  
ANISOU  674  CD1 TYR A 207     8720   7987   9189   -290    558  -1683       C  
ATOM    675  CD2 TYR A 207      -0.829 -16.037  13.505  1.00 67.97           C  
ANISOU  675  CD2 TYR A 207     8635   7892   9298   -149    351  -1853       C  
ATOM    676  CE1 TYR A 207       0.524 -16.937  11.265  1.00 72.06           C  
ANISOU  676  CE1 TYR A 207     9231   8320   9829   -484    675  -1720       C  
ATOM    677  CE2 TYR A 207      -0.042 -15.153  12.766  1.00 70.99           C  
ANISOU  677  CE2 TYR A 207     9035   8089   9851   -333    444  -1880       C  
ATOM    678  CZ  TYR A 207       0.627 -15.605  11.640  1.00 81.30           C  
ANISOU  678  CZ  TYR A 207    10386   9354  11151   -510    616  -1804       C  
ATOM    679  OH  TYR A 207       1.401 -14.734  10.912  1.00 85.17           O  
ANISOU  679  OH  TYR A 207    10900   9669  11790   -722    735  -1824       O  
ATOM    680  N   LEU A 208      -4.432 -20.540  13.813  1.00 49.62           N  
ANISOU  680  N   LEU A 208     6507   6104   6240    225    270  -1340       N  
ATOM    681  CA  LEU A 208      -5.041 -21.634  14.573  1.00 49.22           C  
ANISOU  681  CA  LEU A 208     6437   6225   6040    334    222  -1285       C  
ATOM    682  C   LEU A 208      -4.038 -22.785  14.652  1.00 52.54           C  
ANISOU  682  C   LEU A 208     6795   6712   6454    328    226  -1290       C  
ATOM    683  O   LEU A 208      -3.454 -23.142  13.627  1.00 50.89           O  
ANISOU  683  O   LEU A 208     6600   6426   6310    234    308  -1260       O  
ATOM    684  CB  LEU A 208      -6.347 -22.115  13.923  1.00 49.01           C  
ANISOU  684  CB  LEU A 208     6511   6190   5922    341    243  -1119       C  
ATOM    685  CG  LEU A 208      -7.498 -21.095  13.693  1.00 53.99           C  
ANISOU  685  CG  LEU A 208     7198   6728   6586    361    212  -1107       C  
ATOM    686  CD1 LEU A 208      -8.859 -21.807  13.563  1.00 52.45           C  
ANISOU  686  CD1 LEU A 208     7042   6592   6296    414    201   -989       C  
ATOM    687  CD2 LEU A 208      -7.593 -20.120  14.806  1.00 55.64           C  
ANISOU  687  CD2 LEU A 208     7325   6976   6841    435    151  -1273       C  
ATOM    688  N   ILE A 209      -3.816 -23.348  15.862  1.00 49.08           N  
ANISOU  688  N   ILE A 209     6291   6415   5943    424    130  -1341       N  
ATOM    689  CA  ILE A 209      -2.870 -24.453  16.087  1.00 47.07           C  
ANISOU  689  CA  ILE A 209     5971   6206   5707    443     78  -1355       C  
ATOM    690  C   ILE A 209      -3.679 -25.721  16.155  1.00 49.93           C  
ANISOU  690  C   ILE A 209     6398   6644   5928    485     56  -1184       C  
ATOM    691  O   ILE A 209      -4.365 -25.986  17.143  1.00 49.57           O  
ANISOU  691  O   ILE A 209     6384   6718   5730    555     -9  -1135       O  
ATOM    692  CB  ILE A 209      -1.997 -24.225  17.353  1.00 49.91           C  
ANISOU  692  CB  ILE A 209     6235   6642   6087    516    -56  -1516       C  
ATOM    693  CG1 ILE A 209      -1.372 -22.821  17.334  1.00 49.95           C  
ANISOU  693  CG1 ILE A 209     6171   6562   6246    472    -33  -1695       C  
ATOM    694  CG2 ILE A 209      -0.951 -25.330  17.495  1.00 47.13           C  
ANISOU  694  CG2 ILE A 209     5806   6299   5804    543   -145  -1543       C  
ATOM    695  CD1 ILE A 209      -0.836 -22.374  18.705  1.00 48.42           C  
ANISOU  695  CD1 ILE A 209     5899   6458   6041    559   -180  -1868       C  
ATOM    696  N   LEU A 210      -3.647 -26.476  15.065  1.00 44.28           N  
ANISOU  696  N   LEU A 210     5707   5858   5258    429    125  -1097       N  
ATOM    697  CA  LEU A 210      -4.469 -27.670  14.916  1.00 42.26           C  
ANISOU  697  CA  LEU A 210     5512   5640   4904    453    114   -933       C  
ATOM    698  C   LEU A 210      -3.669 -28.934  15.030  1.00 46.47           C  
ANISOU  698  C   LEU A 210     5989   6174   5492    481     35   -927       C  
ATOM    699  O   LEU A 210      -2.471 -28.950  14.767  1.00 44.85           O  
ANISOU  699  O   LEU A 210     5689   5913   5438    461     28  -1057       O  
ATOM    700  CB  LEU A 210      -5.192 -27.662  13.522  1.00 40.58           C  
ANISOU  700  CB  LEU A 210     5380   5337   4700    375    229   -840       C  
ATOM    701  CG  LEU A 210      -6.011 -26.410  13.113  1.00 46.49           C  
ANISOU  701  CG  LEU A 210     6200   6031   5433    342    282   -833       C  
ATOM    702  CD1 LEU A 210      -6.382 -26.474  11.671  1.00 47.79           C  
ANISOU  702  CD1 LEU A 210     6456   6092   5610    257    360   -751       C  
ATOM    703  CD2 LEU A 210      -7.312 -26.306  13.886  1.00 49.46           C  
ANISOU  703  CD2 LEU A 210     6600   6492   5700    414    242   -773       C  
ATOM    704  N   GLU A 211      -4.366 -30.028  15.334  1.00 45.09           N  
ANISOU  704  N   GLU A 211     5866   6045   5221    519    -21   -778       N  
ATOM    705  CA  GLU A 211      -3.810 -31.366  15.316  1.00 43.75           C  
ANISOU  705  CA  GLU A 211     5660   5841   5123    548   -114   -741       C  
ATOM    706  C   GLU A 211      -3.538 -31.638  13.823  1.00 46.22           C  
ANISOU  706  C   GLU A 211     5944   6047   5569    476      3   -780       C  
ATOM    707  O   GLU A 211      -4.359 -31.275  12.969  1.00 42.49           O  
ANISOU  707  O   GLU A 211     5545   5552   5045    416    121   -721       O  
ATOM    708  CB  GLU A 211      -4.864 -32.334  15.856  1.00 43.50           C  
ANISOU  708  CB  GLU A 211     5716   5864   4949    575   -172   -546       C  
ATOM    709  CG  GLU A 211      -4.562 -33.805  15.638  1.00 47.97           C  
ANISOU  709  CG  GLU A 211     6266   6356   5605    595   -268   -470       C  
ATOM    710  CD  GLU A 211      -5.683 -34.753  16.031  1.00 57.35           C  
ANISOU  710  CD  GLU A 211     7547   7574   6670    592   -301   -261       C  
ATOM    711  OE1 GLU A 211      -6.698 -34.311  16.617  1.00 44.64           O  
ANISOU  711  OE1 GLU A 211     6007   6068   4887    574   -245   -180       O  
ATOM    712  OE2 GLU A 211      -5.527 -35.962  15.783  1.00 56.34           O  
ANISOU  712  OE2 GLU A 211     7411   7361   6634    603   -384   -190       O  
ATOM    713  N   TYR A 212      -2.376 -32.234  13.515  1.00 43.79           N  
ANISOU  713  N   TYR A 212     5527   5676   5433    480    -34   -898       N  
ATOM    714  CA  TYR A 212      -2.062 -32.566  12.145  1.00 43.22           C  
ANISOU  714  CA  TYR A 212     5422   5527   5472    403     92   -964       C  
ATOM    715  C   TYR A 212      -2.570 -33.986  11.902  1.00 46.76           C  
ANISOU  715  C   TYR A 212     5894   5944   5931    439     26   -851       C  
ATOM    716  O   TYR A 212      -2.225 -34.898  12.644  1.00 46.91           O  
ANISOU  716  O   TYR A 212     5864   5946   6014    520   -140   -829       O  
ATOM    717  CB  TYR A 212      -0.550 -32.448  11.894  1.00 45.09           C  
ANISOU  717  CB  TYR A 212     5496   5716   5919    378    113  -1194       C  
ATOM    718  CG  TYR A 212      -0.011 -33.254  10.727  1.00 46.40           C  
ANISOU  718  CG  TYR A 212     5583   5817   6229    323    205  -1302       C  
ATOM    719  CD1 TYR A 212      -0.394 -32.971   9.415  1.00 47.54           C  
ANISOU  719  CD1 TYR A 212     5807   5948   6308    200    404  -1295       C  
ATOM    720  CD2 TYR A 212       0.964 -34.226  10.923  1.00 48.72           C  
ANISOU  720  CD2 TYR A 212     5716   6061   6735    390     88  -1439       C  
ATOM    721  CE1 TYR A 212       0.135 -33.684   8.335  1.00 47.99           C  
ANISOU  721  CE1 TYR A 212     5791   5967   6476    137    507  -1425       C  
ATOM    722  CE2 TYR A 212       1.517 -34.921   9.852  1.00 49.42           C  
ANISOU  722  CE2 TYR A 212     5702   6096   6979    339    187  -1589       C  
ATOM    723  CZ  TYR A 212       1.094 -34.647   8.562  1.00 52.75           C  
ANISOU  723  CZ  TYR A 212     6210   6530   7304    207    411  -1586       C  
ATOM    724  OH  TYR A 212       1.619 -35.330   7.513  1.00 53.90           O  
ANISOU  724  OH  TYR A 212     6262   6644   7575    148    523  -1752       O  
ATOM    725  N   ALA A 213      -3.431 -34.143  10.898  1.00 43.69           N  
ANISOU  725  N   ALA A 213     5588   5535   5477    378    135   -771       N  
ATOM    726  CA  ALA A 213      -3.983 -35.438  10.472  1.00 43.00           C  
ANISOU  726  CA  ALA A 213     5520   5403   5416    396     91   -680       C  
ATOM    727  C   ALA A 213      -3.044 -35.935   9.358  1.00 46.88           C  
ANISOU  727  C   ALA A 213     5914   5827   6072    350    168   -860       C  
ATOM    728  O   ALA A 213      -3.013 -35.300   8.316  1.00 46.38           O  
ANISOU  728  O   ALA A 213     5889   5766   5967    250    332   -929       O  
ATOM    729  CB  ALA A 213      -5.403 -35.236   9.954  1.00 41.72           C  
ANISOU  729  CB  ALA A 213     5487   5257   5106    356    163   -534       C  
ATOM    730  N   PRO A 214      -2.190 -36.977   9.563  1.00 48.18           N  
ANISOU  730  N   PRO A 214     5948   5930   6429    413     53   -959       N  
ATOM    731  CA  PRO A 214      -1.186 -37.315   8.522  1.00 49.76           C  
ANISOU  731  CA  PRO A 214     6016   6081   6808    362    154  -1193       C  
ATOM    732  C   PRO A 214      -1.674 -37.897   7.204  1.00 53.44           C  
ANISOU  732  C   PRO A 214     6527   6524   7254    294    272  -1214       C  
ATOM    733  O   PRO A 214      -0.952 -37.797   6.198  1.00 53.03           O  
ANISOU  733  O   PRO A 214     6404   6473   7271    206    431  -1417       O  
ATOM    734  CB  PRO A 214      -0.240 -38.324   9.209  1.00 53.27           C  
ANISOU  734  CB  PRO A 214     6297   6447   7496    474    -47  -1299       C  
ATOM    735  CG  PRO A 214      -0.627 -38.319  10.665  1.00 58.60           C  
ANISOU  735  CG  PRO A 214     7045   7141   8080    568   -251  -1107       C  
ATOM    736  CD  PRO A 214      -2.038 -37.826  10.763  1.00 51.49           C  
ANISOU  736  CD  PRO A 214     6331   6316   6917    526   -179   -878       C  
ATOM    737  N   LEU A 215      -2.836 -38.547   7.194  1.00 49.31           N  
ANISOU  737  N   LEU A 215     6108   5981   6645    325    200  -1030       N  
ATOM    738  CA  LEU A 215      -3.273 -39.231   5.979  1.00 49.78           C  
ANISOU  738  CA  LEU A 215     6197   6009   6707    275    275  -1070       C  
ATOM    739  C   LEU A 215      -4.182 -38.376   5.070  1.00 52.52           C  
ANISOU  739  C   LEU A 215     6716   6412   6827    171    423   -989       C  
ATOM    740  O   LEU A 215      -4.727 -38.880   4.104  1.00 53.16           O  
ANISOU  740  O   LEU A 215     6855   6475   6868    131    463   -996       O  
ATOM    741  CB  LEU A 215      -3.883 -40.597   6.316  1.00 50.73           C  
ANISOU  741  CB  LEU A 215     6305   6046   6925    361    100   -958       C  
ATOM    742  CG  LEU A 215      -2.924 -41.656   6.927  1.00 57.47           C  
ANISOU  742  CG  LEU A 215     6994   6799   8044    461    -77  -1059       C  
ATOM    743  CD1 LEU A 215      -3.547 -43.041   6.899  1.00 56.67           C  
ANISOU  743  CD1 LEU A 215     6893   6585   8054    515   -225   -965       C  
ATOM    744  CD2 LEU A 215      -1.602 -41.696   6.209  1.00 63.68           C  
ANISOU  744  CD2 LEU A 215     7610   7570   9014    436     17  -1370       C  
ATOM    745  N   GLY A 216      -4.272 -37.076   5.354  1.00 49.14           N  
ANISOU  745  N   GLY A 216     6366   6037   6267    128    488   -932       N  
ATOM    746  CA  GLY A 216      -4.985 -36.106   4.533  1.00 48.14           C  
ANISOU  746  CA  GLY A 216     6406   5937   5948     31    599   -862       C  
ATOM    747  C   GLY A 216      -6.485 -36.122   4.604  1.00 51.12           C  
ANISOU  747  C   GLY A 216     6907   6309   6206     66    518   -665       C  
ATOM    748  O   GLY A 216      -7.035 -36.631   5.565  1.00 48.80           O  
ANISOU  748  O   GLY A 216     6577   6015   5951    158    396   -553       O  
ATOM    749  N   THR A 217      -7.145 -35.522   3.594  1.00 49.91           N  
ANISOU  749  N   THR A 217     6904   6150   5908    -15    582   -623       N  
ATOM    750  CA  THR A 217      -8.598 -35.434   3.533  1.00 48.78           C  
ANISOU  750  CA  THR A 217     6867   5992   5677     18    496   -464       C  
ATOM    751  C   THR A 217      -9.217 -36.675   2.890  1.00 52.28           C  
ANISOU  751  C   THR A 217     7308   6401   6154     36    440   -458       C  
ATOM    752  O   THR A 217      -8.633 -37.286   1.996  1.00 52.97           O  
ANISOU  752  O   THR A 217     7382   6479   6265    -15    501   -587       O  
ATOM    753  CB  THR A 217      -9.071 -34.174   2.776  1.00 54.17           C  
ANISOU  753  CB  THR A 217     7720   6656   6205    -63    537   -415       C  
ATOM    754  OG1 THR A 217      -8.784 -34.314   1.381  1.00 53.82           O  
ANISOU  754  OG1 THR A 217     7779   6599   6071   -173    621   -490       O  
ATOM    755  CG2 THR A 217      -8.522 -32.882   3.339  1.00 50.79           C  
ANISOU  755  CG2 THR A 217     7300   6238   5761    -89    584   -424       C  
ATOM    756  N   VAL A 218     -10.472 -36.965   3.297  1.00 47.62           N  
ANISOU  756  N   VAL A 218     6731   5795   5569     98    334   -322       N  
ATOM    757  CA  VAL A 218     -11.304 -38.020   2.730  1.00 46.50           C  
ANISOU  757  CA  VAL A 218     6592   5609   5469    115    262   -299       C  
ATOM    758  C   VAL A 218     -11.626 -37.575   1.275  1.00 47.88           C  
ANISOU  758  C   VAL A 218     6920   5768   5505     35    293   -342       C  
ATOM    759  O   VAL A 218     -11.727 -38.403   0.384  1.00 47.78           O  
ANISOU  759  O   VAL A 218     6923   5730   5502     13    280   -413       O  
ATOM    760  CB  VAL A 218     -12.579 -38.214   3.599  1.00 50.62           C  
ANISOU  760  CB  VAL A 218     7080   6124   6029    179    165   -148       C  
ATOM    761  CG1 VAL A 218     -13.592 -39.120   2.897  1.00 50.25           C  
ANISOU  761  CG1 VAL A 218     7041   6019   6032    183     89   -128       C  
ATOM    762  CG2 VAL A 218     -12.213 -38.798   4.976  1.00 50.78           C  
ANISOU  762  CG2 VAL A 218     6985   6163   6146    234    133    -92       C  
ATOM    763  N   TYR A 219     -11.736 -36.257   1.054  1.00 45.66           N  
ANISOU  763  N   TYR A 219     6762   5495   5092    -12    323   -301       N  
ATOM    764  CA  TYR A 219     -11.942 -35.651  -0.262  1.00 48.74           C  
ANISOU  764  CA  TYR A 219     7341   5862   5316   -105    337   -313       C  
ATOM    765  C   TYR A 219     -10.883 -36.162  -1.225  1.00 54.94           C  
ANISOU  765  C   TYR A 219     8147   6678   6049   -203    465   -469       C  
ATOM    766  O   TYR A 219     -11.242 -36.667  -2.290  1.00 56.19           O  
ANISOU  766  O   TYR A 219     8398   6828   6125   -245    442   -513       O  
ATOM    767  CB  TYR A 219     -11.895 -34.108  -0.172  1.00 51.86           C  
ANISOU  767  CB  TYR A 219     7854   6241   5611   -149    355   -247       C  
ATOM    768  CG  TYR A 219     -12.013 -33.437  -1.533  1.00 57.80           C  
ANISOU  768  CG  TYR A 219     8841   6953   6168   -266    358   -231       C  
ATOM    769  CD1 TYR A 219     -13.254 -33.109  -2.065  1.00 59.59           C  
ANISOU  769  CD1 TYR A 219     9201   7110   6330   -240    194   -134       C  
ATOM    770  CD2 TYR A 219     -10.883 -33.169  -2.304  1.00 60.78           C  
ANISOU  770  CD2 TYR A 219     9307   7361   6424   -412    520   -319       C  
ATOM    771  CE1 TYR A 219     -13.372 -32.531  -3.329  1.00 62.80           C  
ANISOU  771  CE1 TYR A 219     9857   7470   6534   -350    162   -101       C  
ATOM    772  CE2 TYR A 219     -10.990 -32.604  -3.577  1.00 63.85           C  
ANISOU  772  CE2 TYR A 219     9947   7722   6593   -545    529   -287       C  
ATOM    773  CZ  TYR A 219     -12.240 -32.297  -4.090  1.00 70.92           C  
ANISOU  773  CZ  TYR A 219    11003   8538   7404   -511    335   -166       C  
ATOM    774  OH  TYR A 219     -12.356 -31.704  -5.324  1.00 76.07           O  
ANISOU  774  OH  TYR A 219    11936   9150   7818   -644    308   -111       O  
ATOM    775  N   ARG A 220      -9.588 -36.055  -0.832  1.00 52.52           N  
ANISOU  775  N   ARG A 220     7741   6412   5803   -237    596   -574       N  
ATOM    776  CA  ARG A 220      -8.458 -36.511  -1.620  1.00 54.70           C  
ANISOU  776  CA  ARG A 220     7987   6728   6069   -333    747   -766       C  
ATOM    777  C   ARG A 220      -8.444 -38.030  -1.786  1.00 59.55           C  
ANISOU  777  C   ARG A 220     8468   7331   6827   -270    702   -880       C  
ATOM    778  O   ARG A 220      -8.110 -38.501  -2.866  1.00 61.59           O  
ANISOU  778  O   ARG A 220     8763   7616   7022   -350    786  -1031       O  
ATOM    779  CB  ARG A 220      -7.112 -35.998  -1.064  1.00 57.48           C  
ANISOU  779  CB  ARG A 220     8227   7115   6499   -376    883   -871       C  
ATOM    780  CG  ARG A 220      -5.990 -36.024  -2.129  1.00 72.80           C  
ANISOU  780  CG  ARG A 220    10179   9107   8373   -533   1093  -1078       C  
ATOM    781  CD  ARG A 220      -4.603 -36.126  -1.549  1.00 83.19           C  
ANISOU  781  CD  ARG A 220    11279  10450   9882   -535   1201  -1260       C  
ATOM    782  NE  ARG A 220      -3.588 -36.392  -2.577  1.00 94.33           N  
ANISOU  782  NE  ARG A 220    12649  11919  11272   -680   1415  -1506       N  
ATOM    783  CZ  ARG A 220      -2.639 -35.537  -2.952  1.00104.78           C  
ANISOU  783  CZ  ARG A 220    13992  13287  12531   -844   1624  -1608       C  
ATOM    784  NH1 ARG A 220      -2.539 -34.347  -2.371  1.00 89.45           N  
ANISOU  784  NH1 ARG A 220    12111  11321  10556   -876   1628  -1481       N  
ATOM    785  NH2 ARG A 220      -1.765 -35.876  -3.887  1.00 88.99           N  
ANISOU  785  NH2 ARG A 220    11939  11358  10516   -984   1839  -1855       N  
ATOM    786  N   GLU A 221      -8.813 -38.790  -0.743  1.00 55.23           N  
ANISOU  786  N   GLU A 221     7776   6742   6467   -137    571   -812       N  
ATOM    787  CA  GLU A 221      -8.855 -40.266  -0.802  1.00 55.38           C  
ANISOU  787  CA  GLU A 221     7667   6713   6661    -71    495   -897       C  
ATOM    788  C   GLU A 221      -9.871 -40.754  -1.823  1.00 57.92           C  
ANISOU  788  C   GLU A 221     8095   7011   6900    -89    431   -891       C  
ATOM    789  O   GLU A 221      -9.638 -41.746  -2.504  1.00 56.22           O  
ANISOU  789  O   GLU A 221     7825   6778   6759    -95    436  -1049       O  
ATOM    790  CB  GLU A 221      -9.234 -40.860   0.561  1.00 56.22           C  
ANISOU  790  CB  GLU A 221     7650   6765   6946     52    352   -764       C  
ATOM    791  CG  GLU A 221      -8.046 -41.377   1.343  1.00 75.78           C  
ANISOU  791  CG  GLU A 221     9955   9222   9615    103    346   -862       C  
ATOM    792  CD  GLU A 221      -7.388 -42.651   0.861  1.00 98.25           C  
ANISOU  792  CD  GLU A 221    12667  12006  12657    126    325  -1057       C  
ATOM    793  OE1 GLU A 221      -8.068 -43.702   0.841  1.00102.54           O  
ANISOU  793  OE1 GLU A 221    13181  12468  13312    179    202  -1012       O  
ATOM    794  OE2 GLU A 221      -6.176 -42.605   0.551  1.00 92.83           O  
ANISOU  794  OE2 GLU A 221    11887  11345  12040     93    429  -1269       O  
ATOM    795  N   LEU A 222     -11.015 -40.055  -1.897  1.00 54.38           N  
ANISOU  795  N   LEU A 222     7786   6554   6320    -88    353   -725       N  
ATOM    796  CA  LEU A 222     -12.098 -40.392  -2.815  1.00 54.86           C  
ANISOU  796  CA  LEU A 222     7955   6584   6305    -96    255   -707       C  
ATOM    797  C   LEU A 222     -11.713 -40.066  -4.276  1.00 59.46           C  
ANISOU  797  C   LEU A 222     8712   7218   6663   -222    350   -836       C  
ATOM    798  O   LEU A 222     -12.090 -40.796  -5.173  1.00 58.84           O  
ANISOU  798  O   LEU A 222     8673   7130   6554   -236    301   -929       O  
ATOM    799  CB  LEU A 222     -13.367 -39.653  -2.360  1.00 53.33           C  
ANISOU  799  CB  LEU A 222     7832   6359   6073    -49    132   -512       C  
ATOM    800  CG  LEU A 222     -14.715 -40.111  -2.890  1.00 57.95           C  
ANISOU  800  CG  LEU A 222     8458   6886   6673    -13    -25   -471       C  
ATOM    801  CD1 LEU A 222     -14.963 -41.588  -2.679  1.00 57.19           C  
ANISOU  801  CD1 LEU A 222     8202   6738   6791     44    -89   -522       C  
ATOM    802  CD2 LEU A 222     -15.778 -39.331  -2.224  1.00 63.80           C  
ANISOU  802  CD2 LEU A 222     9210   7601   7429     40   -121   -315       C  
ATOM    803  N   GLN A 223     -10.929 -38.998  -4.502  1.00 58.60           N  
ANISOU  803  N   GLN A 223     8708   7166   6394   -326    493   -847       N  
ATOM    804  CA  GLN A 223     -10.444 -38.655  -5.841  1.00 61.01           C  
ANISOU  804  CA  GLN A 223     9195   7533   6454   -483    621   -961       C  
ATOM    805  C   GLN A 223      -9.483 -39.747  -6.344  1.00 66.52           C  
ANISOU  805  C   GLN A 223     9757   8283   7235   -519    753  -1227       C  
ATOM    806  O   GLN A 223      -9.540 -40.129  -7.520  1.00 69.44           O  
ANISOU  806  O   GLN A 223    10237   8697   7450   -602    791  -1356       O  
ATOM    807  CB  GLN A 223      -9.748 -37.297  -5.841  1.00 62.68           C  
ANISOU  807  CB  GLN A 223     9527   7778   6511   -602    760   -906       C  
ATOM    808  CG  GLN A 223     -10.703 -36.120  -5.693  1.00 80.28           C  
ANISOU  808  CG  GLN A 223    11938   9943   8624   -591    622   -676       C  
ATOM    809  CD  GLN A 223     -10.026 -34.836  -6.051  1.00101.32           C  
ANISOU  809  CD  GLN A 223    14774  12621  11103   -746    755   -634       C  
ATOM    810  OE1 GLN A 223      -8.832 -34.632  -5.761  1.00 94.88           O  
ANISOU  810  OE1 GLN A 223    13857  11855  10337   -818    946   -738       O  
ATOM    811  NE2 GLN A 223     -10.783 -33.938  -6.685  1.00 92.52           N  
ANISOU  811  NE2 GLN A 223    13919  11446   9788   -802    641   -480       N  
ATOM    812  N   LYS A 224      -8.706 -40.288  -5.438  1.00 62.47           N  
ANISOU  812  N   LYS A 224     8998   7757   6980   -444    796  -1317       N  
ATOM    813  CA  LYS A 224      -7.747 -41.303  -5.761  1.00 63.83           C  
ANISOU  813  CA  LYS A 224     8984   7950   7321   -445    890  -1589       C  
ATOM    814  C   LYS A 224      -8.314 -42.712  -5.994  1.00 66.51           C  
ANISOU  814  C   LYS A 224     9249   8227   7796   -357    748  -1670       C  
ATOM    815  O   LYS A 224      -7.909 -43.360  -6.918  1.00 68.14           O  
ANISOU  815  O   LYS A 224     9455   8479   7955   -423    833  -1901       O  
ATOM    816  CB  LYS A 224      -6.632 -41.260  -4.735  1.00 67.58           C  
ANISOU  816  CB  LYS A 224     9224   8396   8060   -366    910  -1635       C  
ATOM    817  CG  LYS A 224      -6.015 -42.582  -4.366  1.00 92.14           C  
ANISOU  817  CG  LYS A 224    12335  11579  11096   -479   1109  -1704       C  
ATOM    818  CD  LYS A 224      -4.984 -42.368  -3.273  1.00103.96           C  
ANISOU  818  CD  LYS A 224    13613  13035  12852   -379   1071  -1712       C  
ATOM    819  CE  LYS A 224      -4.700 -43.639  -2.501  1.00116.55           C  
ANISOU  819  CE  LYS A 224    14944  14586  14753   -298   1051  -1957       C  
ATOM    820  NZ  LYS A 224      -4.242 -43.318  -1.127  1.00118.00           N  
ANISOU  820  NZ  LYS A 224    15043  14655  15138   -135    809  -1852       N  
ATOM    821  N   LEU A 225      -9.264 -43.171  -5.193  1.00 60.93           N  
ANISOU  821  N   LEU A 225     8475   7417   7257   -222    543  -1492       N  
ATOM    822  CA  LEU A 225      -9.884 -44.467  -5.367  1.00 60.58           C  
ANISOU  822  CA  LEU A 225     8340   7285   7391   -140    393  -1550       C  
ATOM    823  C   LEU A 225     -11.172 -44.427  -6.159  1.00 61.91           C  
ANISOU  823  C   LEU A 225     8683   7447   7394   -159    281  -1478       C  
ATOM    824  O   LEU A 225     -11.728 -45.451  -6.476  1.00 62.47           O  
ANISOU  824  O   LEU A 225     8687   7449   7599   -109    167  -1562       O  
ATOM    825  CB  LEU A 225     -10.181 -45.095  -4.021  1.00 60.02           C  
ANISOU  825  CB  LEU A 225     8105   7100   7601     -8    240  -1395       C  
ATOM    826  CG  LEU A 225      -9.134 -45.103  -2.926  1.00 64.84           C  
ANISOU  826  CG  LEU A 225     8537   7687   8413     42    276  -1445       C  
ATOM    827  CD1 LEU A 225      -9.601 -45.902  -1.731  1.00 63.06           C  
ANISOU  827  CD1 LEU A 225     8240   7371   8348    142    121  -1214       C  
ATOM    828  CD2 LEU A 225      -7.861 -45.688  -3.462  1.00 71.10           C  
ANISOU  828  CD2 LEU A 225     9152   8428   9434     67    288  -1729       C  
ATOM    829  N   SER A 226     -11.662 -43.246  -6.458  1.00 56.86           N  
ANISOU  829  N   SER A 226     8258   6859   6488   -224    289  -1327       N  
ATOM    830  CA  SER A 226     -12.917 -43.109  -7.163  1.00 57.17           C  
ANISOU  830  CA  SER A 226     8482   6879   6361   -234    144  -1230       C  
ATOM    831  C   SER A 226     -14.144 -43.409  -6.317  1.00 57.62           C  
ANISOU  831  C   SER A 226     8450   6833   6612   -114    -51  -1046       C  
ATOM    832  O   SER A 226     -15.048 -42.620  -6.256  1.00 56.95           O  
ANISOU  832  O   SER A 226     8479   6731   6430   -104   -150   -887       O  
ATOM    833  CB  SER A 226     -12.920 -43.961  -8.417  1.00 61.41           C  
ANISOU  833  CB  SER A 226     9103   7448   6782   -292    134  -1437       C  
ATOM    834  OG  SER A 226     -12.506 -43.203  -9.519  1.00 74.36           O  
ANISOU  834  OG  SER A 226    10896   9208   8149   -441    329  -1567       O  
ATOM    835  N   LYS A 227     -14.166 -44.555  -5.673  1.00 53.87           N  
ANISOU  835  N   LYS A 227     7768   6281   6420    -32   -106  -1078       N  
ATOM    836  CA  LYS A 227     -15.209 -44.852  -4.736  1.00 53.30           C  
ANISOU  836  CA  LYS A 227     7583   6113   6554     55   -251   -914       C  
ATOM    837  C   LYS A 227     -14.724 -45.853  -3.734  1.00 55.67           C  
ANISOU  837  C   LYS A 227     7679   6346   7126    113   -245   -911       C  
ATOM    838  O   LYS A 227     -13.691 -46.420  -3.907  1.00 56.30           O  
ANISOU  838  O   LYS A 227     7685   6432   7275    106   -168  -1073       O  
ATOM    839  CB  LYS A 227     -16.465 -45.323  -5.438  1.00 57.38           C  
ANISOU  839  CB  LYS A 227     8130   6564   7109     75   -419   -934       C  
ATOM    840  CG  LYS A 227     -16.340 -46.598  -6.215  1.00 66.26           C  
ANISOU  840  CG  LYS A 227     9246   7669   8260     57   -448  -1164       C  
ATOM    841  CD  LYS A 227     -17.609 -46.839  -6.989  1.00 72.84           C  
ANISOU  841  CD  LYS A 227    10142   8449   9085     72   -633  -1178       C  
ATOM    842  CE  LYS A 227     -17.388 -46.611  -8.460  1.00 88.69           C  
ANISOU  842  CE  LYS A 227    12201  10470  11025     39   -661  -1430       C  
ATOM    843  NZ  LYS A 227     -17.152 -47.903  -9.135  1.00104.44           N  
ANISOU  843  NZ  LYS A 227    13982  12359  13341     89   -701  -1564       N  
ATOM    844  N   PHE A 228     -15.470 -46.028  -2.662  1.00 50.87           N  
ANISOU  844  N   PHE A 228     6985   5675   6666    163   -325   -727       N  
ATOM    845  CA  PHE A 228     -15.061 -46.881  -1.562  1.00 49.90           C  
ANISOU  845  CA  PHE A 228     6708   5475   6778    209   -351   -665       C  
ATOM    846  C   PHE A 228     -15.906 -48.130  -1.499  1.00 54.82           C  
ANISOU  846  C   PHE A 228     7231   5963   7635    233   -486   -640       C  
ATOM    847  O   PHE A 228     -17.092 -48.126  -1.908  1.00 52.85           O  
ANISOU  847  O   PHE A 228     7012   5692   7378    223   -560   -604       O  
ATOM    848  CB  PHE A 228     -15.147 -46.123  -0.228  1.00 50.00           C  
ANISOU  848  CB  PHE A 228     6715   5532   6751    222   -316   -459       C  
ATOM    849  CG  PHE A 228     -14.354 -44.845  -0.071  1.00 49.41           C  
ANISOU  849  CG  PHE A 228     6721   5573   6482    201   -195   -462       C  
ATOM    850  CD1 PHE A 228     -13.144 -44.669  -0.735  1.00 51.36           C  
ANISOU  850  CD1 PHE A 228     6987   5865   6664    170    -97   -641       C  
ATOM    851  CD2 PHE A 228     -14.767 -43.861   0.819  1.00 48.33           C  
ANISOU  851  CD2 PHE A 228     6617   5494   6252    206   -169   -303       C  
ATOM    852  CE1 PHE A 228     -12.401 -43.510  -0.558  1.00 50.00           C  
ANISOU  852  CE1 PHE A 228     6876   5784   6338    136     19   -643       C  
ATOM    853  CE2 PHE A 228     -14.017 -42.697   0.999  1.00 49.37           C  
ANISOU  853  CE2 PHE A 228     6813   5714   6233    187    -70   -313       C  
ATOM    854  CZ  PHE A 228     -12.831 -42.537   0.327  1.00 48.28           C  
ANISOU  854  CZ  PHE A 228     6698   5608   6039    149     22   -473       C  
ATOM    855  N   ASP A 229     -15.301 -49.212  -0.947  1.00 52.52           N  
ANISOU  855  N   ASP A 229     6814   5562   7578    265   -536   -658       N  
ATOM    856  CA  ASP A 229     -16.034 -50.478  -0.758  1.00 52.47           C  
ANISOU  856  CA  ASP A 229     6708   5394   7832    277   -672   -611       C  
ATOM    857  C   ASP A 229     -16.940 -50.326   0.457  1.00 54.27           C  
ANISOU  857  C   ASP A 229     6925   5607   8088    255   -689   -340       C  
ATOM    858  O   ASP A 229     -16.803 -49.358   1.210  1.00 53.01           O  
ANISOU  858  O   ASP A 229     6818   5557   7766    248   -604   -216       O  
ATOM    859  CB  ASP A 229     -15.075 -51.700  -0.618  1.00 56.54           C  
ANISOU  859  CB  ASP A 229     7102   5767   8612    319   -748   -723       C  
ATOM    860  CG  ASP A 229     -13.978 -51.609   0.425  1.00 69.42           C  
ANISOU  860  CG  ASP A 229     8696   7393  10286    351   -734   -651       C  
ATOM    861  OD1 ASP A 229     -14.293 -51.307   1.601  1.00 70.06           O  
ANISOU  861  OD1 ASP A 229     8805   7485  10329    339   -740   -406       O  
ATOM    862  OD2 ASP A 229     -12.820 -51.949   0.093  1.00 78.39           O  
ANISOU  862  OD2 ASP A 229     9763   8502  11521    391   -733   -854       O  
ATOM    863  N   GLU A 230     -17.823 -51.277   0.662  1.00 53.25           N  
ANISOU  863  N   GLU A 230     6722   5348   8164    234   -786   -261       N  
ATOM    864  CA  GLU A 230     -18.777 -51.188   1.731  1.00 53.01           C  
ANISOU  864  CA  GLU A 230     6666   5302   8173    184   -778    -19       C  
ATOM    865  C   GLU A 230     -18.131 -51.188   3.085  1.00 55.10           C  
ANISOU  865  C   GLU A 230     6941   5574   8422    177   -750    157       C  
ATOM    866  O   GLU A 230     -18.627 -50.590   3.999  1.00 53.12           O  
ANISOU  866  O   GLU A 230     6723   5423   8038    140   -669    318       O  
ATOM    867  CB  GLU A 230     -19.771 -52.321   1.636  1.00 55.40           C  
ANISOU  867  CB  GLU A 230     6875   5437   8737    142   -884     13       C  
ATOM    868  CG  GLU A 230     -20.536 -52.340   0.335  1.00 64.85           C  
ANISOU  868  CG  GLU A 230     8062   6628   9949    153   -939   -171       C  
ATOM    869  CD  GLU A 230     -21.838 -53.090   0.448  1.00 79.05           C  
ANISOU  869  CD  GLU A 230     9760   8311  11964     97  -1010   -109       C  
ATOM    870  OE1 GLU A 230     -21.827 -54.306   0.260  1.00 72.99           O  
ANISOU  870  OE1 GLU A 230     8909   7365  11458     69  -1096    -78       O  
ATOM    871  OE2 GLU A 230     -22.869 -52.475   0.726  1.00 70.11           O  
ANISOU  871  OE2 GLU A 230     8625   7251  10762     81   -993   -106       O  
ATOM    872  N   GLN A 231     -17.020 -51.881   3.207  1.00 52.48           N  
ANISOU  872  N   GLN A 231     6579   5139   8224    219   -827    106       N  
ATOM    873  CA  GLN A 231     -16.352 -52.030   4.477  1.00 52.51           C  
ANISOU  873  CA  GLN A 231     6599   5121   8231    227   -853    258       C  
ATOM    874  C   GLN A 231     -15.735 -50.715   4.908  1.00 53.49           C  
ANISOU  874  C   GLN A 231     6796   5439   8090    245   -731    271       C  
ATOM    875  O   GLN A 231     -15.891 -50.284   6.022  1.00 52.18           O  
ANISOU  875  O   GLN A 231     6675   5343   7807    209   -690    464       O  
ATOM    876  CB  GLN A 231     -15.299 -53.122   4.374  1.00 56.01           C  
ANISOU  876  CB  GLN A 231     6975   5390   8918    290   -998    147       C  
ATOM    877  CG  GLN A 231     -15.848 -54.546   4.399  1.00 87.36           C  
ANISOU  877  CG  GLN A 231    10964   9361  12867    335  -1044    215       C  
ATOM    878  CD  GLN A 231     -16.708 -54.945   3.196  1.00122.10           C  
ANISOU  878  CD  GLN A 231    15344  13538  17510    335  -1240    373       C  
ATOM    879  OE1 GLN A 231     -16.318 -54.813   2.038  1.00119.13           O  
ANISOU  879  OE1 GLN A 231    14879  12971  17414    386  -1384    237       O  
ATOM    880  NE2 GLN A 231     -17.874 -55.474   3.484  1.00119.76           N  
ANISOU  880  NE2 GLN A 231    15139  13257  17107    277  -1258    656       N  
ATOM    881  N   ARG A 232     -15.051 -50.068   3.991  1.00 50.05           N  
ANISOU  881  N   ARG A 232     6374   5094   7548    288   -664     61       N  
ATOM    882  CA  ARG A 232     -14.511 -48.760   4.242  1.00 48.26           C  
ANISOU  882  CA  ARG A 232     6212   5034   7092    298   -548     46       C  
ATOM    883  C   ARG A 232     -15.574 -47.722   4.524  1.00 49.85           C  
ANISOU  883  C   ARG A 232     6477   5359   7103    256   -458    166       C  
ATOM    884  O   ARG A 232     -15.434 -46.972   5.439  1.00 49.38           O  
ANISOU  884  O   ARG A 232     6454   5397   6911    254   -401    269       O  
ATOM    885  CB  ARG A 232     -13.654 -48.315   3.089  1.00 48.28           C  
ANISOU  885  CB  ARG A 232     6219   5090   7033    321   -481   -207       C  
ATOM    886  CG  ARG A 232     -12.959 -47.020   3.375  1.00 53.85           C  
ANISOU  886  CG  ARG A 232     6981   5940   7539    321   -367   -222       C  
ATOM    887  CD  ARG A 232     -12.142 -46.549   2.206  1.00 60.38           C  
ANISOU  887  CD  ARG A 232     7845   6840   8259    299   -263   -440       C  
ATOM    888  NE  ARG A 232     -10.874 -47.239   2.175  1.00 86.53           N  
ANISOU  888  NE  ARG A 232    11057  10094  11727    327   -273   -645       N  
ATOM    889  CZ  ARG A 232      -9.702 -46.636   2.201  1.00 98.98           C  
ANISOU  889  CZ  ARG A 232    12595  11725  13289    334   -202   -753       C  
ATOM    890  NH1 ARG A 232      -9.630 -45.321   2.246  1.00 79.93           N  
ANISOU  890  NH1 ARG A 232    10251   9421  10696    312   -116   -670       N  
ATOM    891  NH2 ARG A 232      -8.607 -47.355   2.172  1.00 87.91           N  
ANISOU  891  NH2 ARG A 232    11068  10260  12073    365   -218   -969       N  
ATOM    892  N   THR A 233     -16.639 -47.710   3.737  1.00 48.03           N  
ANISOU  892  N   THR A 233     6249   5118   6883    230   -461    139       N  
ATOM    893  CA  THR A 233     -17.781 -46.794   3.908  1.00 47.41           C  
ANISOU  893  CA  THR A 233     6200   5131   6682    202   -402    217       C  
ATOM    894  C   THR A 233     -18.443 -46.949   5.286  1.00 51.73           C  
ANISOU  894  C   THR A 233     6710   5694   7252    157   -376    420       C  
ATOM    895  O   THR A 233     -18.594 -45.945   5.993  1.00 49.69           O  
ANISOU  895  O   THR A 233     6481   5559   6841    152   -292    480       O  
ATOM    896  CB  THR A 233     -18.774 -46.945   2.741  1.00 51.44           C  
ANISOU  896  CB  THR A 233     6705   5597   7242    195   -455    120       C  
ATOM    897  OG1 THR A 233     -18.089 -46.623   1.539  1.00 49.25           O  
ANISOU  897  OG1 THR A 233     6502   5343   6869    218   -455    -59       O  
ATOM    898  CG2 THR A 233     -20.027 -46.077   2.904  1.00 42.16           C  
ANISOU  898  CG2 THR A 233     5530   4489   5999    180   -429    178       C  
ATOM    899  N   ALA A 234     -18.820 -48.206   5.660  1.00 50.23           N  
ANISOU  899  N   ALA A 234     6460   5378   7249    114   -444    518       N  
ATOM    900  CA  ALA A 234     -19.443 -48.513   6.946  1.00 51.40           C  
ANISOU  900  CA  ALA A 234     6589   5533   7408     37   -407    725       C  
ATOM    901  C   ALA A 234     -18.531 -48.133   8.102  1.00 54.76           C  
ANISOU  901  C   ALA A 234     7081   6038   7687     44   -378    831       C  
ATOM    902  O   ALA A 234     -19.028 -47.629   9.107  1.00 54.58           O  
ANISOU  902  O   ALA A 234     7077   6127   7535    -10   -286    952       O  
ATOM    903  CB  ALA A 234     -19.816 -49.986   7.025  1.00 53.73           C  
ANISOU  903  CB  ALA A 234     6830   5646   7941    -22   -501    815       C  
ATOM    904  N   THR A 235     -17.203 -48.306   7.943  1.00 52.69           N  
ANISOU  904  N   THR A 235     6846   5731   7442    113   -454    759       N  
ATOM    905  CA  THR A 235     -16.229 -47.956   8.987  1.00 52.50           C  
ANISOU  905  CA  THR A 235     6879   5770   7300    136   -463    834       C  
ATOM    906  C   THR A 235     -16.254 -46.455   9.192  1.00 54.22           C  
ANISOU  906  C   THR A 235     7132   6177   7292    152   -335    783       C  
ATOM    907  O   THR A 235     -16.445 -46.013  10.327  1.00 55.16           O  
ANISOU  907  O   THR A 235     7290   6400   7269    117   -281    904       O  
ATOM    908  CB  THR A 235     -14.824 -48.526   8.704  1.00 52.65           C  
ANISOU  908  CB  THR A 235     6881   5678   7446    213   -589    731       C  
ATOM    909  OG1 THR A 235     -14.940 -49.932   8.423  1.00 50.01           O  
ANISOU  909  OG1 THR A 235     6499   5143   7358    202   -721    760       O  
ATOM    910  CG2 THR A 235     -13.874 -48.324   9.878  1.00 51.41           C  
ANISOU  910  CG2 THR A 235     6775   5558   7202    240   -646    821       C  
ATOM    911  N   TYR A 236     -16.126 -45.683   8.093  1.00 47.91           N  
ANISOU  911  N   TYR A 236     6328   5419   6457    196   -288    606       N  
ATOM    912  CA  TYR A 236     -16.199 -44.209   8.120  1.00 46.15           C  
ANISOU  912  CA  TYR A 236     6143   5343   6051    211   -185    547       C  
ATOM    913  C   TYR A 236     -17.524 -43.707   8.689  1.00 48.56           C  
ANISOU  913  C   TYR A 236     6431   5732   6288    164   -107    633       C  
ATOM    914  O   TYR A 236     -17.516 -42.749   9.449  1.00 46.93           O  
ANISOU  914  O   TYR A 236     6245   5646   5940    167    -36    648       O  
ATOM    915  CB  TYR A 236     -16.005 -43.606   6.718  1.00 45.55           C  
ANISOU  915  CB  TYR A 236     6090   5262   5954    239   -166    373       C  
ATOM    916  CG  TYR A 236     -14.598 -43.631   6.193  1.00 47.91           C  
ANISOU  916  CG  TYR A 236     6400   5539   6267    272   -176    239       C  
ATOM    917  CD1 TYR A 236     -13.512 -43.794   7.051  1.00 50.24           C  
ANISOU  917  CD1 TYR A 236     6675   5837   6579    300   -205    257       C  
ATOM    918  CD2 TYR A 236     -14.337 -43.417   4.843  1.00 49.92           C  
ANISOU  918  CD2 TYR A 236     6685   5778   6505    269   -153     82       C  
ATOM    919  CE1 TYR A 236     -12.208 -43.785   6.571  1.00 50.29           C  
ANISOU  919  CE1 TYR A 236     6655   5822   6630    329   -206    100       C  
ATOM    920  CE2 TYR A 236     -13.035 -43.396   4.353  1.00 51.17           C  
ANISOU  920  CE2 TYR A 236     6836   5932   6674    279   -124    -68       C  
ATOM    921  CZ  TYR A 236     -11.979 -43.608   5.216  1.00 55.92           C  
ANISOU  921  CZ  TYR A 236     7381   6528   7339    312   -149    -69       C  
ATOM    922  OH  TYR A 236     -10.722 -43.587   4.706  1.00 57.34           O  
ANISOU  922  OH  TYR A 236     7521   6703   7563    319   -113   -249       O  
ATOM    923  N   ILE A 237     -18.653 -44.348   8.335  1.00 46.49           N  
ANISOU  923  N   ILE A 237     6113   5404   6145    121   -120    664       N  
ATOM    924  CA  ILE A 237     -19.975 -43.930   8.820  1.00 46.52           C  
ANISOU  924  CA  ILE A 237     6063   5483   6129     71    -37    709       C  
ATOM    925  C   ILE A 237     -20.087 -44.169  10.325  1.00 51.73           C  
ANISOU  925  C   ILE A 237     6727   6221   6709     -2     34    868       C  
ATOM    926  O   ILE A 237     -20.600 -43.289  11.027  1.00 51.61           O  
ANISOU  926  O   ILE A 237     6692   6341   6575    -21    141    862       O  
ATOM    927  CB  ILE A 237     -21.168 -44.523   7.998  1.00 49.05           C  
ANISOU  927  CB  ILE A 237     6302   5710   6626     42    -76    674       C  
ATOM    928  CG1 ILE A 237     -21.126 -44.080   6.489  1.00 48.46           C  
ANISOU  928  CG1 ILE A 237     6257   5585   6570    112   -155    509       C  
ATOM    929  CG2 ILE A 237     -22.528 -44.146   8.623  1.00 49.23           C  
ANISOU  929  CG2 ILE A 237     6229   5810   6665    -18     22    700       C  
ATOM    930  CD1 ILE A 237     -21.104 -42.526   6.180  1.00 51.16           C  
ANISOU  930  CD1 ILE A 237     6654   6019   6764    166   -127    416       C  
ATOM    931  N   THR A 238     -19.541 -45.297  10.822  1.00 47.32           N  
ANISOU  931  N   THR A 238     6204   5575   6200    -40    -34   1000       N  
ATOM    932  CA  THR A 238     -19.485 -45.600  12.260  1.00 48.19           C  
ANISOU  932  CA  THR A 238     6368   5748   6194   -121      6   1180       C  
ATOM    933  C   THR A 238     -18.695 -44.513  13.002  1.00 49.92           C  
ANISOU  933  C   THR A 238     6653   6119   6197    -71     44   1146       C  
ATOM    934  O   THR A 238     -19.226 -43.958  13.965  1.00 49.37           O  
ANISOU  934  O   THR A 238     6590   6197   5970   -130    161   1190       O  
ATOM    935  CB  THR A 238     -18.934 -47.028  12.518  1.00 53.99           C  
ANISOU  935  CB  THR A 238     7151   6315   7046   -157   -132   1332       C  
ATOM    936  OG1 THR A 238     -19.826 -47.987  11.955  1.00 56.90           O  
ANISOU  936  OG1 THR A 238     7449   6549   7623   -221   -151   1364       O  
ATOM    937  CG2 THR A 238     -18.733 -47.337  13.996  1.00 49.77           C  
ANISOU  937  CG2 THR A 238     6721   5834   6355   -243   -129   1543       C  
ATOM    938  N   GLU A 239     -17.494 -44.202  12.539  1.00 45.72           N  
ANISOU  938  N   GLU A 239     6154   5555   5664     30    -44   1044       N  
ATOM    939  CA  GLU A 239     -16.634 -43.205  13.153  1.00 46.92           C  
ANISOU  939  CA  GLU A 239     6356   5826   5647     83    -31    993       C  
ATOM    940  C   GLU A 239     -17.266 -41.841  13.213  1.00 50.69           C  
ANISOU  940  C   GLU A 239     6801   6448   6011     92    101    887       C  
ATOM    941  O   GLU A 239     -17.195 -41.176  14.200  1.00 49.44           O  
ANISOU  941  O   GLU A 239     6671   6426   5687     82    160    897       O  
ATOM    942  CB  GLU A 239     -15.303 -43.134  12.425  1.00 47.82           C  
ANISOU  942  CB  GLU A 239     6474   5862   5835    177   -129    867       C  
ATOM    943  CG  GLU A 239     -14.568 -44.443  12.454  1.00 53.18           C  
ANISOU  943  CG  GLU A 239     7163   6387   6657    189   -284    936       C  
ATOM    944  CD  GLU A 239     -13.229 -44.426  11.779  1.00 60.63           C  
ANISOU  944  CD  GLU A 239     8072   7255   7710    276   -365    772       C  
ATOM    945  OE1 GLU A 239     -13.111 -44.008  10.646  1.00 61.37           O  
ANISOU  945  OE1 GLU A 239     8126   7337   7856    299   -307    613       O  
ATOM    946  OE2 GLU A 239     -12.280 -44.894  12.380  1.00 81.69           O  
ANISOU  946  OE2 GLU A 239    10753   9867  10419    314   -494    799       O  
ATOM    947  N   LEU A 240     -17.874 -41.440  12.120  1.00 48.22           N  
ANISOU  947  N   LEU A 240     6430   6096   5794    113    130    780       N  
ATOM    948  CA  LEU A 240     -18.630 -40.224  12.019  1.00 48.04           C  
ANISOU  948  CA  LEU A 240     6366   6161   5727    133    213    669       C  
ATOM    949  C   LEU A 240     -19.824 -40.206  12.962  1.00 50.76           C  
ANISOU  949  C   LEU A 240     6645   6614   6028     55    330    722       C  
ATOM    950  O   LEU A 240     -20.066 -39.246  13.635  1.00 48.90           O  
ANISOU  950  O   LEU A 240     6392   6511   5679     64    414    656       O  
ATOM    951  CB  LEU A 240     -19.135 -40.127  10.611  1.00 48.53           C  
ANISOU  951  CB  LEU A 240     6402   6117   5921    165    165    575       C  
ATOM    952  CG  LEU A 240     -19.162 -38.834   9.851  1.00 57.04           C  
ANISOU  952  CG  LEU A 240     7504   7197   6970    227    155    439       C  
ATOM    953  CD1 LEU A 240     -18.140 -37.878  10.398  1.00 58.34           C  
ANISOU  953  CD1 LEU A 240     7720   7439   7006    262    184    393       C  
ATOM    954  CD2 LEU A 240     -18.865 -39.181   8.416  1.00 58.60           C  
ANISOU  954  CD2 LEU A 240     7748   7272   7245    247     69    380       C  
ATOM    955  N   ALA A 241     -20.581 -41.283  12.992  1.00 47.17           N  
ANISOU  955  N   ALA A 241     6146   6104   5671    -29    346    825       N  
ATOM    956  CA  ALA A 241     -21.737 -41.340  13.858  1.00 49.09           C  
ANISOU  956  CA  ALA A 241     6313   6451   5886   -135    487    870       C  
ATOM    957  C   ALA A 241     -21.364 -41.255  15.321  1.00 54.51           C  
ANISOU  957  C   ALA A 241     7079   7287   6345   -198    566    968       C  
ATOM    958  O   ALA A 241     -21.999 -40.571  16.064  1.00 58.81           O  
ANISOU  958  O   ALA A 241     7570   7990   6783   -236    706    899       O  
ATOM    959  CB  ALA A 241     -22.536 -42.576  13.585  1.00 50.30           C  
ANISOU  959  CB  ALA A 241     6414   6494   6204   -229    481    974       C  
ATOM    960  N   ASN A 242     -20.306 -41.929  15.717  1.00 49.11           N  
ANISOU  960  N   ASN A 242     6520   6555   5586   -197    461   1100       N  
ATOM    961  CA  ASN A 242     -19.768 -41.842  17.088  1.00 50.42           C  
ANISOU  961  CA  ASN A 242     6793   6852   5511   -246    487   1199       C  
ATOM    962  C   ASN A 242     -19.357 -40.403  17.435  1.00 55.07           C  
ANISOU  962  C   ASN A 242     7378   7589   5958   -162    531   1031       C  
ATOM    963  O   ASN A 242     -19.729 -39.914  18.488  1.00 57.97           O  
ANISOU  963  O   ASN A 242     7755   8133   6140   -222    653   1018       O  
ATOM    964  CB  ASN A 242     -18.566 -42.774  17.277  1.00 52.40           C  
ANISOU  964  CB  ASN A 242     7170   6982   5757   -226    305   1346       C  
ATOM    965  CG  ASN A 242     -18.929 -44.221  17.417  1.00 70.03           C  
ANISOU  965  CG  ASN A 242     9444   9084   8080   -336    255   1554       C  
ATOM    966  OD1 ASN A 242     -20.008 -44.586  17.891  1.00 64.24           O  
ANISOU  966  OD1 ASN A 242     8690   8402   7317   -477    390   1648       O  
ATOM    967  ND2 ASN A 242     -18.027 -45.081  16.993  1.00 61.47           N  
ANISOU  967  ND2 ASN A 242     8409   7818   7130   -280     62   1617       N  
ATOM    968  N   ALA A 243     -18.618 -39.727  16.548  1.00 51.47           N  
ANISOU  968  N   ALA A 243     6906   7062   5587    -36    442    896       N  
ATOM    969  CA  ALA A 243     -18.194 -38.331  16.747  1.00 51.39           C  
ANISOU  969  CA  ALA A 243     6886   7155   5484     44    468    732       C  
ATOM    970  C   ALA A 243     -19.399 -37.397  16.825  1.00 55.59           C  
ANISOU  970  C   ALA A 243     7307   7790   6025     32    609    596       C  
ATOM    971  O   ALA A 243     -19.399 -36.483  17.646  1.00 56.47           O  
ANISOU  971  O   ALA A 243     7408   8047   6000     42    682    498       O  
ATOM    972  CB  ALA A 243     -17.262 -37.891  15.632  1.00 49.73           C  
ANISOU  972  CB  ALA A 243     6682   6823   5390    149    362    630       C  
ATOM    973  N   LEU A 244     -20.447 -37.670  16.018  1.00 51.77           N  
ANISOU  973  N   LEU A 244     6729   7227   5715     13    638    575       N  
ATOM    974  CA  LEU A 244     -21.669 -36.877  16.014  1.00 51.94           C  
ANISOU  974  CA  LEU A 244     6614   7317   5803     12    745    427       C  
ATOM    975  C   LEU A 244     -22.515 -37.113  17.256  1.00 57.94           C  
ANISOU  975  C   LEU A 244     7319   8250   6446   -112    924    451       C  
ATOM    976  O   LEU A 244     -23.074 -36.147  17.760  1.00 58.43           O  
ANISOU  976  O   LEU A 244     7286   8439   6474   -101   1031    287       O  
ATOM    977  CB  LEU A 244     -22.472 -37.058  14.713  1.00 51.24           C  
ANISOU  977  CB  LEU A 244     6440   7078   5950     42    683    379       C  
ATOM    978  CG  LEU A 244     -21.839 -36.451  13.432  1.00 51.99           C  
ANISOU  978  CG  LEU A 244     6591   7034   6130    155    535    306       C  
ATOM    979  CD1 LEU A 244     -22.575 -36.910  12.221  1.00 50.89           C  
ANISOU  979  CD1 LEU A 244     6405   6752   6179    166    454    295       C  
ATOM    980  CD2 LEU A 244     -21.746 -34.901  13.494  1.00 51.21           C  
ANISOU  980  CD2 LEU A 244     6474   6977   6006    239    531    142       C  
ATOM    981  N   SER A 245     -22.575 -38.369  17.787  1.00 56.12           N  
ANISOU  981  N   SER A 245     7152   8024   6146   -238    961    651       N  
ATOM    982  CA  SER A 245     -23.290 -38.666  19.045  1.00 59.21           C  
ANISOU  982  CA  SER A 245     7529   8593   6373   -396   1153    706       C  
ATOM    983  C   SER A 245     -22.684 -37.836  20.160  1.00 63.38           C  
ANISOU  983  C   SER A 245     8136   9311   6635   -383   1204    643       C  
ATOM    984  O   SER A 245     -23.425 -37.169  20.894  1.00 65.87           O  
ANISOU  984  O   SER A 245     8359   9808   6861   -435   1382    498       O  
ATOM    985  CB  SER A 245     -23.188 -40.143  19.418  1.00 64.24           C  
ANISOU  985  CB  SER A 245     8280   9170   6958   -535   1138    973       C  
ATOM    986  OG  SER A 245     -24.204 -40.897  18.790  1.00 82.76           O  
ANISOU  986  OG  SER A 245    10511  11409   9528   -608   1181   1005       O  
ATOM    987  N   TYR A 246     -21.324 -37.848  20.255  1.00 57.38           N  
ANISOU  987  N   TYR A 246     7529   8507   5768   -308   1041    720       N  
ATOM    988  CA  TYR A 246     -20.561 -37.084  21.242  1.00 57.31           C  
ANISOU  988  CA  TYR A 246     7605   8653   5517   -277   1039    656       C  
ATOM    989  C   TYR A 246     -20.888 -35.586  21.083  1.00 61.57           C  
ANISOU  989  C   TYR A 246     8007   9266   6119   -176   1103    374       C  
ATOM    990  O   TYR A 246     -21.158 -34.924  22.080  1.00 62.56           O  
ANISOU  990  O   TYR A 246     8111   9588   6070   -211   1229    253       O  
ATOM    991  CB  TYR A 246     -19.046 -37.362  21.118  1.00 55.34           C  
ANISOU  991  CB  TYR A 246     7500   8295   5233   -191    821    754       C  
ATOM    992  CG  TYR A 246     -18.188 -36.394  21.906  1.00 55.59           C  
ANISOU  992  CG  TYR A 246     7588   8454   5078   -124    782    636       C  
ATOM    993  CD1 TYR A 246     -17.946 -36.588  23.264  1.00 60.09           C  
ANISOU  993  CD1 TYR A 246     8289   9194   5349   -208    804    719       C  
ATOM    994  CD2 TYR A 246     -17.686 -35.239  21.314  1.00 53.45           C  
ANISOU  994  CD2 TYR A 246     7245   8140   4922     11    727    437       C  
ATOM    995  CE1 TYR A 246     -17.160 -35.691  23.996  1.00 61.74           C  
ANISOU  995  CE1 TYR A 246     8546   9522   5388   -142    752    590       C  
ATOM    996  CE2 TYR A 246     -16.932 -34.321  22.042  1.00 54.27           C  
ANISOU  996  CE2 TYR A 246     7384   8353   4882     69    691    310       C  
ATOM    997  CZ  TYR A 246     -16.669 -34.549  23.386  1.00 61.81           C  
ANISOU  997  CZ  TYR A 246     8459   9478   5549     -1    699    375       C  
ATOM    998  OH  TYR A 246     -15.904 -33.668  24.109  1.00 63.80           O  
ANISOU  998  OH  TYR A 246     8745   9837   5660     62    643    236       O  
ATOM    999  N   CYS A 247     -20.873 -35.075  19.826  1.00 55.24           N  
ANISOU  999  N   CYS A 247     7124   8300   5563    -58   1008    271       N  
ATOM   1000  CA  CYS A 247     -21.198 -33.687  19.493  1.00 54.91           C  
ANISOU 1000  CA  CYS A 247     6963   8266   5633     44   1022     26       C  
ATOM   1001  C   CYS A 247     -22.573 -33.289  19.960  1.00 60.16           C  
ANISOU 1001  C   CYS A 247     7462   9061   6335    -11   1203   -129       C  
ATOM   1002  O   CYS A 247     -22.734 -32.223  20.555  1.00 60.47           O  
ANISOU 1002  O   CYS A 247     7428   9220   6325     28   1271   -333       O  
ATOM   1003  CB  CYS A 247     -21.066 -33.445  17.997  1.00 54.04           C  
ANISOU 1003  CB  CYS A 247     6830   7938   5764    145    881     -1       C  
ATOM   1004  SG  CYS A 247     -19.388 -33.149  17.469  1.00 56.93           S  
ANISOU 1004  SG  CYS A 247     7332   8189   6108    236    710     33       S  
ATOM   1005  N   HIS A 248     -23.585 -34.097  19.602  1.00 57.21           N  
ANISOU 1005  N   HIS A 248     7003   8645   6089    -92   1273    -65       N  
ATOM   1006  CA  HIS A 248     -24.973 -33.832  19.930  1.00 58.87           C  
ANISOU 1006  CA  HIS A 248     7015   8960   6392   -153   1451   -232       C  
ATOM   1007  C   HIS A 248     -25.255 -33.927  21.429  1.00 67.39           C  
ANISOU 1007  C   HIS A 248     8100  10304   7203   -297   1677   -254       C  
ATOM   1008  O   HIS A 248     -26.114 -33.195  21.917  1.00 68.50           O  
ANISOU 1008  O   HIS A 248     8068  10581   7376   -312   1835   -491       O  
ATOM   1009  CB  HIS A 248     -25.919 -34.718  19.103  1.00 58.87           C  
ANISOU 1009  CB  HIS A 248     6915   8830   6622   -206   1452   -163       C  
ATOM   1010  CG  HIS A 248     -25.815 -34.507  17.622  1.00 59.28           C  
ANISOU 1010  CG  HIS A 248     6955   8647   6921    -69   1239   -183       C  
ATOM   1011  ND1 HIS A 248     -26.253 -35.462  16.739  1.00 60.33           N  
ANISOU 1011  ND1 HIS A 248     7066   8631   7225    -99   1172    -76       N  
ATOM   1012  CD2 HIS A 248     -25.321 -33.455  16.920  1.00 58.91           C  
ANISOU 1012  CD2 HIS A 248     6932   8496   6954     81   1084   -294       C  
ATOM   1013  CE1 HIS A 248     -26.018 -34.972  15.533  1.00 57.84           C  
ANISOU 1013  CE1 HIS A 248     6772   8143   7062     33    981   -128       C  
ATOM   1014  NE2 HIS A 248     -25.452 -33.765  15.596  1.00 57.21           N  
ANISOU 1014  NE2 HIS A 248     6728   8080   6929    137    925   -246       N  
ATOM   1015  N   SER A 249     -24.481 -34.758  22.160  1.00 67.30           N  
ANISOU 1015  N   SER A 249     8290  10359   6921   -395   1676    -23       N  
ATOM   1016  CA  SER A 249     -24.584 -34.908  23.627  1.00 72.11           C  
ANISOU 1016  CA  SER A 249     8973  11225   7200   -550   1867      1       C  
ATOM   1017  C   SER A 249     -24.010 -33.669  24.366  1.00 80.85           C  
ANISOU 1017  C   SER A 249    10097  12488   8132   -462   1869   -210       C  
ATOM   1018  O   SER A 249     -23.951 -33.650  25.594  1.00 85.87           O  
ANISOU 1018  O   SER A 249    10817  13353   8457   -572   2004   -218       O  
ATOM   1019  CB  SER A 249     -23.875 -36.184  24.083  1.00 75.01           C  
ANISOU 1019  CB  SER A 249     9580  11571   7350   -668   1801    335       C  
ATOM   1020  OG  SER A 249     -22.469 -36.011  24.173  1.00 79.37           O  
ANISOU 1020  OG  SER A 249    10307  12072   7778   -558   1589    409       O  
ATOM   1021  N   LYS A 250     -23.562 -32.661  23.609  1.00 75.85           N  
ANISOU 1021  N   LYS A 250     9401  11726   7692   -274   1713   -371       N  
ATOM   1022  CA  LYS A 250     -23.011 -31.397  24.088  1.00 75.75           C  
ANISOU 1022  CA  LYS A 250     9378  11803   7600   -167   1679   -592       C  
ATOM   1023  C   LYS A 250     -23.734 -30.271  23.319  1.00 78.55           C  
ANISOU 1023  C   LYS A 250     9511  12058   8279    -38   1663   -868       C  
ATOM   1024  O   LYS A 250     -23.285 -29.124  23.294  1.00 79.42           O  
ANISOU 1024  O   LYS A 250     9589  12142   8443     86   1577  -1056       O  
ATOM   1025  CB  LYS A 250     -21.472 -31.366  23.885  1.00 76.41           C  
ANISOU 1025  CB  LYS A 250     9646  11775   7611    -71   1449   -466       C  
ATOM   1026  CG  LYS A 250     -20.717 -32.518  24.583  1.00 87.81           C  
ANISOU 1026  CG  LYS A 250    11310  13274   8779   -176   1404   -189       C  
ATOM   1027  CD  LYS A 250     -19.231 -32.229  24.832  1.00 95.98           C  
ANISOU 1027  CD  LYS A 250    12490  14280   9696    -83   1207   -162       C  
ATOM   1028  CE  LYS A 250     -18.905 -31.109  25.802  1.00100.67           C  
ANISOU 1028  CE  LYS A 250    13079  15059  10111    -42   1237   -390       C  
ATOM   1029  NZ  LYS A 250     -17.440 -30.869  25.924  1.00106.42           N  
ANISOU 1029  NZ  LYS A 250    13926  15727  10780     54   1023   -371       N  
ATOM   1030  N   ARG A 251     -24.881 -30.637  22.706  1.00 73.70           N  
ANISOU 1030  N   ARG A 251     8740  11371   7890    -74   1733   -889       N  
ATOM   1031  CA  ARG A 251     -25.810 -29.847  21.899  1.00 73.53           C  
ANISOU 1031  CA  ARG A 251     8499  11228   8212     31   1698  -1117       C  
ATOM   1032  C   ARG A 251     -25.172 -29.160  20.677  1.00 74.63           C  
ANISOU 1032  C   ARG A 251     8685  11108   8563    203   1434  -1117       C  
ATOM   1033  O   ARG A 251     -25.863 -28.390  19.996  1.00 75.21           O  
ANISOU 1033  O   ARG A 251     8606  11055   8915    304   1357  -1299       O  
ATOM   1034  CB  ARG A 251     -26.615 -28.839  22.744  1.00 79.66           C  
ANISOU 1034  CB  ARG A 251     9069  12188   9013     37   1869  -1464       C  
ATOM   1035  CG  ARG A 251     -27.779 -29.444  23.562  1.00 99.15           C  
ANISOU 1035  CG  ARG A 251    11390  14872  11409   -143   2164  -1537       C  
ATOM   1036  CD  ARG A 251     -28.889 -30.124  22.746  1.00115.83           C  
ANISOU 1036  CD  ARG A 251    13340  16859  13811   -186   2188  -1508       C  
ATOM   1037  NE  ARG A 251     -29.709 -29.188  21.967  1.00130.09           N  
ANISOU 1037  NE  ARG A 251    14901  18515  16011    -33   2084  -1787       N  
ATOM   1038  CZ  ARG A 251     -30.918 -29.469  21.483  1.00146.08           C  
ANISOU 1038  CZ  ARG A 251    16700  20475  18327    -57   2130  -1894       C  
ATOM   1039  NH1 ARG A 251     -31.589 -28.559  20.788  1.00134.97           N  
ANISOU 1039  NH1 ARG A 251    15086  18913  17285    102   1986  -2150       N  
ATOM   1040  NH2 ARG A 251     -31.468 -30.658  21.697  1.00133.04           N  
ANISOU 1040  NH2 ARG A 251    15027  18900  16620   -240   2306  -1747       N  
ATOM   1041  N   VAL A 252     -23.906 -29.519  20.338  1.00 66.94           N  
ANISOU 1041  N   VAL A 252     7921  10041   7471    226   1291   -905       N  
ATOM   1042  CA  VAL A 252     -23.173 -28.990  19.185  1.00 63.21           C  
ANISOU 1042  CA  VAL A 252     7525   9340   7153    349   1073   -875       C  
ATOM   1043  C   VAL A 252     -23.626 -29.694  17.901  1.00 64.83           C  
ANISOU 1043  C   VAL A 252     7728   9353   7552    353    976   -745       C  
ATOM   1044  O   VAL A 252     -23.537 -30.920  17.807  1.00 64.47           O  
ANISOU 1044  O   VAL A 252     7753   9306   7436    267   1001   -545       O  
ATOM   1045  CB  VAL A 252     -21.626 -29.089  19.378  1.00 64.60           C  
ANISOU 1045  CB  VAL A 252     7895   9511   7142    361    983   -742       C  
ATOM   1046  CG1 VAL A 252     -20.878 -28.712  18.100  1.00 61.75           C  
ANISOU 1046  CG1 VAL A 252     7614   8918   6932    449    796   -692       C  
ATOM   1047  CG2 VAL A 252     -21.149 -28.235  20.549  1.00 65.28           C  
ANISOU 1047  CG2 VAL A 252     7981   9765   7058    378   1037   -902       C  
ATOM   1048  N   ILE A 253     -24.076 -28.921  16.906  1.00 60.36           N  
ANISOU 1048  N   ILE A 253     7094   8613   7228    453    843   -856       N  
ATOM   1049  CA  ILE A 253     -24.468 -29.448  15.593  1.00 59.32           C  
ANISOU 1049  CA  ILE A 253     6979   8289   7270    471    715   -754       C  
ATOM   1050  C   ILE A 253     -23.498 -28.912  14.566  1.00 57.39           C  
ANISOU 1050  C   ILE A 253     6894   7862   7050    545    529   -690       C  
ATOM   1051  O   ILE A 253     -23.331 -27.702  14.467  1.00 56.88           O  
ANISOU 1051  O   ILE A 253     6823   7731   7056    625    450   -821       O  
ATOM   1052  CB  ILE A 253     -25.964 -29.261  15.213  1.00 65.50           C  
ANISOU 1052  CB  ILE A 253     7559   9016   8312    500    702   -909       C  
ATOM   1053  CG1 ILE A 253     -26.424 -27.790  15.199  1.00 69.45           C  
ANISOU 1053  CG1 ILE A 253     7939   9455   8994    618    620  -1162       C  
ATOM   1054  CG2 ILE A 253     -26.829 -30.076  16.156  1.00 68.06           C  
ANISOU 1054  CG2 ILE A 253     7738   9526   8594    380    925   -933       C  
ATOM   1055  CD1 ILE A 253     -27.845 -27.502  14.465  1.00 86.05           C  
ANISOU 1055  CD1 ILE A 253     9847  11417  11431    689    506  -1323       C  
ATOM   1056  N   HIS A 254     -22.805 -29.804  13.858  1.00 49.43           N  
ANISOU 1056  N   HIS A 254     6027   6776   5979    509    472   -499       N  
ATOM   1057  CA  HIS A 254     -21.767 -29.415  12.922  1.00 47.19           C  
ANISOU 1057  CA  HIS A 254     5901   6348   5680    545    341   -435       C  
ATOM   1058  C   HIS A 254     -22.276 -28.612  11.730  1.00 53.04           C  
ANISOU 1058  C   HIS A 254     6661   6897   6595    613    177   -494       C  
ATOM   1059  O   HIS A 254     -21.701 -27.553  11.431  1.00 51.31           O  
ANISOU 1059  O   HIS A 254     6519   6588   6388    655     95   -540       O  
ATOM   1060  CB  HIS A 254     -20.958 -30.621  12.478  1.00 45.84           C  
ANISOU 1060  CB  HIS A 254     5848   6153   5415    486    336   -254       C  
ATOM   1061  CG  HIS A 254     -19.690 -30.234  11.803  1.00 48.39           C  
ANISOU 1061  CG  HIS A 254     6316   6383   5688    498    262   -217       C  
ATOM   1062  ND1 HIS A 254     -19.661 -29.861  10.468  1.00 49.37           N  
ANISOU 1062  ND1 HIS A 254     6530   6342   5886    515    146   -206       N  
ATOM   1063  CD2 HIS A 254     -18.448 -30.122  12.320  1.00 49.01           C  
ANISOU 1063  CD2 HIS A 254     6455   6516   5651    487    294   -203       C  
ATOM   1064  CE1 HIS A 254     -18.396 -29.586  10.211  1.00 47.95           C  
ANISOU 1064  CE1 HIS A 254     6459   6131   5628    496    142   -182       C  
ATOM   1065  NE2 HIS A 254     -17.628 -29.733  11.298  1.00 47.80           N  
ANISOU 1065  NE2 HIS A 254     6412   6236   5514    486    224   -190       N  
ATOM   1066  N   ARG A 255     -23.343 -29.122  11.048  1.00 51.00           N  
ANISOU 1066  N   ARG A 255     6340   6564   6474    618    114   -486       N  
ATOM   1067  CA  ARG A 255     -23.998 -28.520   9.868  1.00 51.57           C  
ANISOU 1067  CA  ARG A 255     6438   6443   6714    683    -83   -529       C  
ATOM   1068  C   ARG A 255     -23.104 -28.361   8.633  1.00 56.21           C  
ANISOU 1068  C   ARG A 255     7253   6881   7224    672   -214   -410       C  
ATOM   1069  O   ARG A 255     -23.546 -27.768   7.664  1.00 56.41           O  
ANISOU 1069  O   ARG A 255     7346   6741   7348    717   -394   -426       O  
ATOM   1070  CB  ARG A 255     -24.672 -27.156  10.182  1.00 48.93           C  
ANISOU 1070  CB  ARG A 255     5988   6056   6545    775   -158   -721       C  
ATOM   1071  CG  ARG A 255     -25.427 -27.084  11.515  1.00 57.23           C  
ANISOU 1071  CG  ARG A 255     6807   7285   7653    778      7   -891       C  
ATOM   1072  CD  ARG A 255     -26.107 -25.735  11.685  1.00 61.04           C  
ANISOU 1072  CD  ARG A 255     7158   7688   8344    883    -92  -1116       C  
ATOM   1073  NE  ARG A 255     -25.175 -24.621  11.510  1.00 71.60           N  
ANISOU 1073  NE  ARG A 255     8638   8922   9645    926   -193  -1117       N  
ATOM   1074  CZ  ARG A 255     -25.524 -23.390  11.142  1.00 87.41           C  
ANISOU 1074  CZ  ARG A 255    10622  10746  11845   1023   -379  -1242       C  
ATOM   1075  NH1 ARG A 255     -26.791 -23.104  10.878  1.00 73.08           N  
ANISOU 1075  NH1 ARG A 255     8645   8830  10291   1105   -507  -1389       N  
ATOM   1076  NH2 ARG A 255     -24.602 -22.441  11.013  1.00 72.64           N  
ANISOU 1076  NH2 ARG A 255     8890   8776   9934   1038   -454  -1223       N  
ATOM   1077  N   ASP A 256     -21.884 -28.905   8.626  1.00 54.69           N  
ANISOU 1077  N   ASP A 256     7179   6739   6860    608   -131   -299       N  
ATOM   1078  CA  ASP A 256     -20.956 -28.719   7.505  1.00 53.62           C  
ANISOU 1078  CA  ASP A 256     7246   6487   6639    574   -209   -214       C  
ATOM   1079  C   ASP A 256     -20.087 -29.957   7.195  1.00 54.61           C  
ANISOU 1079  C   ASP A 256     7443   6661   6644    502   -130   -107       C  
ATOM   1080  O   ASP A 256     -18.979 -29.809   6.685  1.00 53.74           O  
ANISOU 1080  O   ASP A 256     7464   6518   6436    457   -115    -70       O  
ATOM   1081  CB  ASP A 256     -20.103 -27.464   7.787  1.00 56.16           C  
ANISOU 1081  CB  ASP A 256     7634   6780   6923    582   -206   -259       C  
ATOM   1082  CG  ASP A 256     -19.393 -26.850   6.581  1.00 63.13           C  
ANISOU 1082  CG  ASP A 256     8727   7510   7751    536   -299   -194       C  
ATOM   1083  OD1 ASP A 256     -19.950 -26.904   5.474  1.00 61.03           O  
ANISOU 1083  OD1 ASP A 256     8561   7122   7504    533   -433   -144       O  
ATOM   1084  OD2 ASP A 256     -18.264 -26.331   6.753  1.00 73.85           O  
ANISOU 1084  OD2 ASP A 256    10152   8873   9034    493   -235   -193       O  
ATOM   1085  N   ILE A 257     -20.600 -31.172   7.486  1.00 51.84           N  
ANISOU 1085  N   ILE A 257     6997   6377   6322    486    -80    -71       N  
ATOM   1086  CA  ILE A 257     -19.924 -32.442   7.220  1.00 51.46           C  
ANISOU 1086  CA  ILE A 257     6991   6351   6210    430    -33     15       C  
ATOM   1087  C   ILE A 257     -19.847 -32.609   5.700  1.00 56.54           C  
ANISOU 1087  C   ILE A 257     7771   6870   6841    411   -140     36       C  
ATOM   1088  O   ILE A 257     -20.881 -32.599   5.029  1.00 57.94           O  
ANISOU 1088  O   ILE A 257     7945   6969   7102    436   -255     20       O  
ATOM   1089  CB  ILE A 257     -20.673 -33.643   7.869  1.00 54.38           C  
ANISOU 1089  CB  ILE A 257     7229   6789   6643    410     23     55       C  
ATOM   1090  CG1 ILE A 257     -20.908 -33.418   9.392  1.00 55.18           C  
ANISOU 1090  CG1 ILE A 257     7214   7033   6719    409    140     32       C  
ATOM   1091  CG2 ILE A 257     -19.956 -34.982   7.589  1.00 55.85           C  
ANISOU 1091  CG2 ILE A 257     7456   6964   6799    362     41    139       C  
ATOM   1092  CD1 ILE A 257     -19.673 -33.566  10.334  1.00 60.29           C  
ANISOU 1092  CD1 ILE A 257     7901   7779   7227    386    223     75       C  
ATOM   1093  N   LYS A 258     -18.634 -32.740   5.172  1.00 50.15           N  
ANISOU 1093  N   LYS A 258     7078   6049   5929    362   -103     56       N  
ATOM   1094  CA  LYS A 258     -18.361 -32.911   3.737  1.00 48.28           C  
ANISOU 1094  CA  LYS A 258     6992   5724   5628    317   -167     64       C  
ATOM   1095  C   LYS A 258     -16.962 -33.469   3.608  1.00 49.07           C  
ANISOU 1095  C   LYS A 258     7129   5865   5649    258    -59     55       C  
ATOM   1096  O   LYS A 258     -16.185 -33.265   4.547  1.00 47.52           O  
ANISOU 1096  O   LYS A 258     6872   5737   5446    262     28     43       O  
ATOM   1097  CB  LYS A 258     -18.569 -31.604   2.933  1.00 48.50           C  
ANISOU 1097  CB  LYS A 258     7169   5648   5609    313   -272     60       C  
ATOM   1098  CG  LYS A 258     -17.778 -30.405   3.363  1.00 55.62           C  
ANISOU 1098  CG  LYS A 258     8118   6550   6466    297   -218     45       C  
ATOM   1099  CD  LYS A 258     -17.878 -29.322   2.311  1.00 62.18           C  
ANISOU 1099  CD  LYS A 258     9144   7245   7236    262   -337     73       C  
ATOM   1100  CE  LYS A 258     -18.633 -28.118   2.744  1.00 71.06           C  
ANISOU 1100  CE  LYS A 258    10240   8290   8470    335   -453     51       C  
ATOM   1101  NZ  LYS A 258     -18.327 -26.950   1.876  1.00 88.61           N  
ANISOU 1101  NZ  LYS A 258    12678  10367  10623    278   -550     99       N  
ATOM   1102  N   PRO A 259     -16.639 -34.260   2.546  1.00 44.31           N  
ANISOU 1102  N   PRO A 259     6600   5230   5006    210    -66     38       N  
ATOM   1103  CA  PRO A 259     -15.319 -34.894   2.485  1.00 44.23           C  
ANISOU 1103  CA  PRO A 259     6579   5260   4967    162     41    -10       C  
ATOM   1104  C   PRO A 259     -14.119 -33.957   2.700  1.00 50.66           C  
ANISOU 1104  C   PRO A 259     7434   6102   5712    118    139    -49       C  
ATOM   1105  O   PRO A 259     -13.142 -34.406   3.259  1.00 49.13           O  
ANISOU 1105  O   PRO A 259     7153   5956   5558    116    215    -94       O  
ATOM   1106  CB  PRO A 259     -15.322 -35.552   1.091  1.00 46.72           C  
ANISOU 1106  CB  PRO A 259     6993   5531   5229    110     12    -55       C  
ATOM   1107  CG  PRO A 259     -16.746 -35.832   0.791  1.00 49.97           C  
ANISOU 1107  CG  PRO A 259     7401   5890   5696    156   -125    -14       C  
ATOM   1108  CD  PRO A 259     -17.452 -34.642   1.366  1.00 45.05           C  
ANISOU 1108  CD  PRO A 259     6778   5251   5088    200   -180     36       C  
ATOM   1109  N   GLU A 260     -14.210 -32.648   2.321  1.00 50.04           N  
ANISOU 1109  N   GLU A 260     7478   5977   5556     85    120    -33       N  
ATOM   1110  CA  GLU A 260     -13.159 -31.616   2.472  1.00 49.14           C  
ANISOU 1110  CA  GLU A 260     7411   5868   5395     27    208    -67       C  
ATOM   1111  C   GLU A 260     -12.902 -31.262   3.949  1.00 53.93           C  
ANISOU 1111  C   GLU A 260     7874   6535   6082     96    234    -82       C  
ATOM   1112  O   GLU A 260     -11.852 -30.702   4.253  1.00 53.59           O  
ANISOU 1112  O   GLU A 260     7819   6509   6035     57    313   -137       O  
ATOM   1113  CB  GLU A 260     -13.564 -30.303   1.770  1.00 51.02           C  
ANISOU 1113  CB  GLU A 260     7824   6007   5553    -19    140    -18       C  
ATOM   1114  CG  GLU A 260     -13.903 -30.423   0.299  1.00 66.29           C  
ANISOU 1114  CG  GLU A 260     9950   7875   7362    -96     83     16       C  
ATOM   1115  CD  GLU A 260     -15.387 -30.610   0.028  1.00 87.19           C  
ANISOU 1115  CD  GLU A 260    12616  10461  10050    -14   -102     70       C  
ATOM   1116  OE1 GLU A 260     -16.060 -29.607  -0.298  1.00 97.46           O  
ANISOU 1116  OE1 GLU A 260    14035  11658  11338     -3   -238    127       O  
ATOM   1117  OE2 GLU A 260     -15.877 -31.755   0.136  1.00 67.66           O  
ANISOU 1117  OE2 GLU A 260    10034   8029   7644     40   -124     50       O  
ATOM   1118  N   ASN A 261     -13.897 -31.515   4.846  1.00 48.66           N  
ANISOU 1118  N   ASN A 261     7104   5902   5481    187    170    -43       N  
ATOM   1119  CA  ASN A 261     -13.835 -31.255   6.284  1.00 46.62           C  
ANISOU 1119  CA  ASN A 261     6726   5725   5264    248    191    -58       C  
ATOM   1120  C   ASN A 261     -13.617 -32.529   7.089  1.00 48.10           C  
ANISOU 1120  C   ASN A 261     6803   5991   5483    276    213    -36       C  
ATOM   1121  O   ASN A 261     -13.777 -32.540   8.314  1.00 46.27           O  
ANISOU 1121  O   ASN A 261     6488   5839   5253    320    219    -24       O  
ATOM   1122  CB  ASN A 261     -15.109 -30.533   6.754  1.00 47.94           C  
ANISOU 1122  CB  ASN A 261     6860   5884   5470    310    123    -47       C  
ATOM   1123  CG  ASN A 261     -15.305 -29.191   6.123  1.00 57.00           C  
ANISOU 1123  CG  ASN A 261     8113   6926   6616    297     62    -64       C  
ATOM   1124  OD1 ASN A 261     -14.403 -28.605   5.532  1.00 64.49           O  
ANISOU 1124  OD1 ASN A 261     9167   7820   7516    228     92    -75       O  
ATOM   1125  ND2 ASN A 261     -16.511 -28.691   6.187  1.00 47.54           N  
ANISOU 1125  ND2 ASN A 261     6891   5684   5489    355    -33    -69       N  
ATOM   1126  N   LEU A 262     -13.263 -33.619   6.410  1.00 44.93           N  
ANISOU 1126  N   LEU A 262     6410   5562   5101    247    217    -33       N  
ATOM   1127  CA  LEU A 262     -12.994 -34.875   7.107  1.00 44.29           C  
ANISOU 1127  CA  LEU A 262     6235   5517   5075    273    208     -3       C  
ATOM   1128  C   LEU A 262     -11.561 -35.262   6.840  1.00 48.79           C  
ANISOU 1128  C   LEU A 262     6787   6074   5678    248    243    -87       C  
ATOM   1129  O   LEU A 262     -11.151 -35.358   5.675  1.00 47.63           O  
ANISOU 1129  O   LEU A 262     6691   5879   5526    194    281   -155       O  
ATOM   1130  CB  LEU A 262     -13.946 -36.015   6.675  1.00 43.31           C  
ANISOU 1130  CB  LEU A 262     6095   5352   5010    275    156     59       C  
ATOM   1131  CG  LEU A 262     -15.442 -35.774   6.776  1.00 44.74           C  
ANISOU 1131  CG  LEU A 262     6265   5533   5202    294    120    115       C  
ATOM   1132  CD1 LEU A 262     -16.171 -36.960   6.254  1.00 43.16           C  
ANISOU 1132  CD1 LEU A 262     6037   5277   5083    285     69    153       C  
ATOM   1133  CD2 LEU A 262     -15.867 -35.449   8.196  1.00 40.89           C  
ANISOU 1133  CD2 LEU A 262     5702   5137   4696    322    148    155       C  
ATOM   1134  N   LEU A 263     -10.798 -35.447   7.918  1.00 44.53           N  
ANISOU 1134  N   LEU A 263     6172   5580   5167    283    230    -99       N  
ATOM   1135  CA  LEU A 263      -9.385 -35.782   7.830  1.00 44.39           C  
ANISOU 1135  CA  LEU A 263     6098   5546   5223    275    244   -207       C  
ATOM   1136  C   LEU A 263      -9.126 -37.194   8.287  1.00 48.31           C  
ANISOU 1136  C   LEU A 263     6519   6013   5824    319    155   -176       C  
ATOM   1137  O   LEU A 263     -10.004 -37.815   8.876  1.00 48.18           O  
ANISOU 1137  O   LEU A 263     6507   6001   5798    343     93    -46       O  
ATOM   1138  CB  LEU A 263      -8.567 -34.756   8.615  1.00 45.17           C  
ANISOU 1138  CB  LEU A 263     6168   5695   5300    285    264   -272       C  
ATOM   1139  CG  LEU A 263      -8.537 -33.349   8.032  1.00 50.89           C  
ANISOU 1139  CG  LEU A 263     6964   6411   5962    227    348   -324       C  
ATOM   1140  CD1 LEU A 263      -8.064 -32.358   9.072  1.00 51.24           C  
ANISOU 1140  CD1 LEU A 263     6971   6504   5995    254    340   -369       C  
ATOM   1141  CD2 LEU A 263      -7.641 -33.275   6.819  1.00 53.75           C  
ANISOU 1141  CD2 LEU A 263     7347   6723   6352    137    444   -437       C  
ATOM   1142  N   LEU A 264      -7.952 -37.732   7.973  1.00 44.56           N  
ANISOU 1142  N   LEU A 264     5971   5495   5467    321    148   -300       N  
ATOM   1143  CA  LEU A 264      -7.610 -39.084   8.339  1.00 45.31           C  
ANISOU 1143  CA  LEU A 264     5989   5525   5701    372     31   -286       C  
ATOM   1144  C   LEU A 264      -6.365 -39.089   9.205  1.00 50.17           C  
ANISOU 1144  C   LEU A 264     6517   6141   6406    423    -47   -365       C  
ATOM   1145  O   LEU A 264      -5.348 -38.510   8.808  1.00 47.53           O  
ANISOU 1145  O   LEU A 264     6121   5814   6123    400     26   -537       O  
ATOM   1146  CB  LEU A 264      -7.427 -39.942   7.067  1.00 45.58           C  
ANISOU 1146  CB  LEU A 264     5989   5480   5848    345     58   -398       C  
ATOM   1147  CG  LEU A 264      -8.670 -40.044   6.174  1.00 49.55           C  
ANISOU 1147  CG  LEU A 264     6582   5973   6271    302     99   -329       C  
ATOM   1148  CD1 LEU A 264      -8.285 -40.411   4.780  1.00 50.09           C  
ANISOU 1148  CD1 LEU A 264     6642   6005   6383    252    169   -493       C  
ATOM   1149  CD2 LEU A 264      -9.701 -41.005   6.759  1.00 48.62           C  
ANISOU 1149  CD2 LEU A 264     6464   5811   6197    336    -12   -162       C  
ATOM   1150  N   GLY A 265      -6.462 -39.724  10.380  1.00 46.99           N  
ANISOU 1150  N   GLY A 265     6113   5726   6016    481   -197   -238       N  
ATOM   1151  CA  GLY A 265      -5.351 -39.856  11.320  1.00 48.70           C  
ANISOU 1151  CA  GLY A 265     6261   5928   6315    546   -332   -291       C  
ATOM   1152  C   GLY A 265      -4.327 -40.875  10.857  1.00 54.34           C  
ANISOU 1152  C   GLY A 265     6849   6517   7281    589   -428   -438       C  
ATOM   1153  O   GLY A 265      -4.502 -41.484   9.802  1.00 52.57           O  
ANISOU 1153  O   GLY A 265     6594   6230   7151    562   -371   -503       O  
ATOM   1154  N   SER A 266      -3.261 -41.095  11.661  1.00 53.26           N  
ANISOU 1154  N   SER A 266     6631   6338   7266    663   -592   -506       N  
ATOM   1155  CA  SER A 266      -2.189 -42.037  11.313  1.00 54.52           C  
ANISOU 1155  CA  SER A 266     6635   6363   7716    723   -713   -684       C  
ATOM   1156  C   SER A 266      -2.644 -43.506  11.167  1.00 58.79           C  
ANISOU 1156  C   SER A 266     7184   6762   8392    756   -856   -581       C  
ATOM   1157  O   SER A 266      -2.038 -44.245  10.392  1.00 59.83           O  
ANISOU 1157  O   SER A 266     7181   6786   8767    782   -880   -768       O  
ATOM   1158  CB  SER A 266      -1.016 -41.928  12.287  1.00 58.57           C  
ANISOU 1158  CB  SER A 266     7058   6848   8347    808   -901   -776       C  
ATOM   1159  OG  SER A 266      -1.431 -42.334  13.575  1.00 70.61           O  
ANISOU 1159  OG  SER A 266     8708   8361   9760    857  -1114   -535       O  
ATOM   1160  N   ALA A 267      -3.712 -43.919  11.876  1.00 55.34           N  
ANISOU 1160  N   ALA A 267     6893   6323   7811    743   -935   -303       N  
ATOM   1161  CA  ALA A 267      -4.256 -45.286  11.755  1.00 56.23           C  
ANISOU 1161  CA  ALA A 267     7026   6286   8052    753  -1064   -180       C  
ATOM   1162  C   ALA A 267      -5.415 -45.319  10.732  1.00 59.49           C  
ANISOU 1162  C   ALA A 267     7484   6732   8387    672   -878   -145       C  
ATOM   1163  O   ALA A 267      -6.161 -46.294  10.673  1.00 62.05           O  
ANISOU 1163  O   ALA A 267     7846   6956   8774    657   -950    -11       O  
ATOM   1164  CB  ALA A 267      -4.731 -45.791  13.115  1.00 57.81           C  
ANISOU 1164  CB  ALA A 267     7363   6454   8148    760  -1256    109       C  
ATOM   1165  N   GLY A 268      -5.546 -44.256   9.947  1.00 53.19           N  
ANISOU 1165  N   GLY A 268     6689   6060   7462    618   -658   -262       N  
ATOM   1166  CA  GLY A 268      -6.593 -44.126   8.945  1.00 52.13           C  
ANISOU 1166  CA  GLY A 268     6610   5961   7237    547   -503   -245       C  
ATOM   1167  C   GLY A 268      -7.969 -43.828   9.510  1.00 56.01           C  
ANISOU 1167  C   GLY A 268     7227   6525   7530    501   -467     -8       C  
ATOM   1168  O   GLY A 268      -8.969 -43.991   8.806  1.00 55.60           O  
ANISOU 1168  O   GLY A 268     7210   6467   7447    456   -398     32       O  
ATOM   1169  N   GLU A 269      -8.034 -43.406  10.786  1.00 50.81           N  
ANISOU 1169  N   GLU A 269     6628   5937   6741    511   -518    133       N  
ATOM   1170  CA  GLU A 269      -9.281 -43.063  11.465  1.00 49.33           C  
ANISOU 1170  CA  GLU A 269     6539   5842   6363    460   -463    328       C  
ATOM   1171  C   GLU A 269      -9.756 -41.677  11.021  1.00 51.51           C  
ANISOU 1171  C   GLU A 269     6841   6245   6483    428   -287    258       C  
ATOM   1172  O   GLU A 269      -8.950 -40.752  10.855  1.00 49.20           O  
ANISOU 1172  O   GLU A 269     6527   6005   6163    444   -234    120       O  
ATOM   1173  CB  GLU A 269      -9.151 -43.172  13.016  1.00 51.19           C  
ANISOU 1173  CB  GLU A 269     6840   6118   6492    471   -577    491       C  
ATOM   1174  CG  GLU A 269      -8.325 -42.090  13.720  1.00 54.63           C  
ANISOU 1174  CG  GLU A 269     7278   6664   6813    508   -576    408       C  
ATOM   1175  CD  GLU A 269      -6.812 -42.198  13.689  1.00 68.24           C  
ANISOU 1175  CD  GLU A 269     8913   8315   8699    585   -701    245       C  
ATOM   1176  OE1 GLU A 269      -6.267 -42.908  12.819  1.00 66.11           O  
ANISOU 1176  OE1 GLU A 269     8552   7920   8647    612   -742    125       O  
ATOM   1177  OE2 GLU A 269      -6.164 -41.552  14.538  1.00 74.35           O  
ANISOU 1177  OE2 GLU A 269     9697   9162   9393    619   -757    211       O  
ATOM   1178  N   LEU A 270     -11.053 -41.553  10.806  1.00 47.91           N  
ANISOU 1178  N   LEU A 270     6426   5823   5954    381   -210    346       N  
ATOM   1179  CA  LEU A 270     -11.705 -40.334  10.376  1.00 47.82           C  
ANISOU 1179  CA  LEU A 270     6444   5900   5825    358    -83    297       C  
ATOM   1180  C   LEU A 270     -11.691 -39.307  11.524  1.00 49.83           C  
ANISOU 1180  C   LEU A 270     6724   6282   5926    366    -50    324       C  
ATOM   1181  O   LEU A 270     -11.886 -39.675  12.680  1.00 49.37           O  
ANISOU 1181  O   LEU A 270     6686   6270   5801    360    -95    444       O  
ATOM   1182  CB  LEU A 270     -13.149 -40.682   9.965  1.00 48.78           C  
ANISOU 1182  CB  LEU A 270     6576   6003   5956    318    -53    380       C  
ATOM   1183  CG  LEU A 270     -13.905 -39.688   9.124  1.00 55.12           C  
ANISOU 1183  CG  LEU A 270     7403   6837   6704    304     27    313       C  
ATOM   1184  CD1 LEU A 270     -14.969 -40.377   8.312  1.00 55.63           C  
ANISOU 1184  CD1 LEU A 270     7455   6829   6852    280      6    340       C  
ATOM   1185  CD2 LEU A 270     -14.541 -38.625   9.988  1.00 61.23           C  
ANISOU 1185  CD2 LEU A 270     8184   7723   7358    304     86    343       C  
ATOM   1186  N   LYS A 271     -11.463 -38.033  11.189  1.00 44.57           N  
ANISOU 1186  N   LYS A 271     6067   5668   5200    372     26    212       N  
ATOM   1187  CA  LYS A 271     -11.479 -36.915  12.130  1.00 45.67           C  
ANISOU 1187  CA  LYS A 271     6219   5919   5215    385     62    195       C  
ATOM   1188  C   LYS A 271     -12.246 -35.739  11.540  1.00 49.25           C  
ANISOU 1188  C   LYS A 271     6692   6393   5629    371    148    138       C  
ATOM   1189  O   LYS A 271     -11.863 -35.252  10.489  1.00 48.17           O  
ANISOU 1189  O   LYS A 271     6576   6196   5531    358    175     52       O  
ATOM   1190  CB  LYS A 271     -10.057 -36.489  12.522  1.00 48.13           C  
ANISOU 1190  CB  LYS A 271     6506   6243   5538    418     22     91       C  
ATOM   1191  CG  LYS A 271      -9.465 -37.375  13.624  1.00 55.08           C  
ANISOU 1191  CG  LYS A 271     7381   7130   6416    449   -105    166       C  
ATOM   1192  CD  LYS A 271      -7.958 -37.331  13.663  1.00 51.81           C  
ANISOU 1192  CD  LYS A 271     6910   6674   6102    493   -185     36       C  
ATOM   1193  CE  LYS A 271      -7.376 -38.401  14.594  1.00 46.49           C  
ANISOU 1193  CE  LYS A 271     6238   5961   5464    536   -366    119       C  
ATOM   1194  NZ  LYS A 271      -7.577 -38.092  16.025  1.00 50.07           N  
ANISOU 1194  NZ  LYS A 271     6764   6531   5729    543   -425    212       N  
ATOM   1195  N   ILE A 272     -13.327 -35.292  12.200  1.00 45.98           N  
ANISOU 1195  N   ILE A 272     6271   6059   5141    369    186    178       N  
ATOM   1196  CA  ILE A 272     -14.116 -34.119  11.769  1.00 45.51           C  
ANISOU 1196  CA  ILE A 272     6214   6002   5075    375    232    111       C  
ATOM   1197  C   ILE A 272     -13.273 -32.846  12.034  1.00 48.46           C  
ANISOU 1197  C   ILE A 272     6599   6401   5414    397    245     -1       C  
ATOM   1198  O   ILE A 272     -12.811 -32.654  13.168  1.00 47.24           O  
ANISOU 1198  O   ILE A 272     6422   6339   5188    417    241    -22       O  
ATOM   1199  CB  ILE A 272     -15.473 -34.025  12.484  1.00 48.70           C  
ANISOU 1199  CB  ILE A 272     6569   6487   5446    370    275    144       C  
ATOM   1200  CG1 ILE A 272     -16.209 -35.378  12.475  1.00 50.14           C  
ANISOU 1200  CG1 ILE A 272     6729   6652   5669    329    272    264       C  
ATOM   1201  CG2 ILE A 272     -16.302 -32.914  11.827  1.00 46.64           C  
ANISOU 1201  CG2 ILE A 272     6297   6183   5240    393    280     58       C  
ATOM   1202  CD1 ILE A 272     -17.577 -35.327  13.142  1.00 61.23           C  
ANISOU 1202  CD1 ILE A 272     8063   8142   7059    300    345    280       C  
ATOM   1203  N   ALA A 273     -13.149 -31.959  11.050  1.00 47.69           N  
ANISOU 1203  N   ALA A 273     6543   6221   5357    387    252    -68       N  
ATOM   1204  CA  ALA A 273     -12.240 -30.806  11.164  1.00 49.46           C  
ANISOU 1204  CA  ALA A 273     6780   6437   5577    388    265   -170       C  
ATOM   1205  C   ALA A 273     -12.803 -29.387  11.244  1.00 63.06           C  
ANISOU 1205  C   ALA A 273     8511   8141   7309    407    264   -239       C  
ATOM   1206  O   ALA A 273     -12.172 -28.581  11.932  1.00 70.83           O  
ANISOU 1206  O   ALA A 273     9468   9161   8284    423    269   -326       O  
ATOM   1207  CB  ALA A 273     -11.250 -30.834  10.019  1.00 49.05           C  
ANISOU 1207  CB  ALA A 273     6779   6290   5568    333    284   -204       C  
ATOM   1208  N   ASP A 274     -13.783 -28.980  10.465  1.00 58.42           N  
ANISOU 1208  N   ASP A 274     7961   7474   6762    406    236   -221       N  
ATOM   1209  CA  ASP A 274     -14.078 -27.508  10.467  1.00 55.89           C  
ANISOU 1209  CA  ASP A 274     7654   7094   6489    429    203   -303       C  
ATOM   1210  C   ASP A 274     -15.413 -27.110  11.131  1.00 53.22           C  
ANISOU 1210  C   ASP A 274     7229   6800   6193    494    180   -352       C  
ATOM   1211  O   ASP A 274     -16.470 -27.122  10.499  1.00 50.13           O  
ANISOU 1211  O   ASP A 274     6842   6338   5867    510    125   -328       O  
ATOM   1212  CB  ASP A 274     -14.001 -26.929   9.041  1.00 57.92           C  
ANISOU 1212  CB  ASP A 274     8042   7186   6779    376    157   -271       C  
ATOM   1213  CG  ASP A 274     -12.596 -26.713   8.473  1.00 78.88           C  
ANISOU 1213  CG  ASP A 274    10774   9791   9407    291    210   -283       C  
ATOM   1214  OD1 ASP A 274     -11.729 -26.191   9.205  1.00 82.83           O  
ANISOU 1214  OD1 ASP A 274    11221  10330   9922    291    246   -364       O  
ATOM   1215  OD2 ASP A 274     -12.405 -26.939   7.258  1.00 87.65           O  
ANISOU 1215  OD2 ASP A 274    11999  10820  10486    216    216   -229       O  
ATOM   1216  N   PHE A 275     -15.329 -26.761  12.412  1.00 48.65           N  
ANISOU 1216  N   PHE A 275     6562   6345   5578    530    221   -441       N  
ATOM   1217  CA  PHE A 275     -16.448 -26.397  13.267  1.00 50.29           C  
ANISOU 1217  CA  PHE A 275     6658   6639   5810    581    241   -532       C  
ATOM   1218  C   PHE A 275     -16.861 -24.915  13.153  1.00 59.88           C  
ANISOU 1218  C   PHE A 275     7845   7753   7154    635    172   -670       C  
ATOM   1219  O   PHE A 275     -17.592 -24.432  14.010  1.00 58.95           O  
ANISOU 1219  O   PHE A 275     7610   7719   7070    684    198   -804       O  
ATOM   1220  CB  PHE A 275     -16.169 -26.806  14.745  1.00 51.03           C  
ANISOU 1220  CB  PHE A 275     6688   6937   5765    580    326   -567       C  
ATOM   1221  CG  PHE A 275     -16.431 -28.267  15.024  1.00 50.15           C  
ANISOU 1221  CG  PHE A 275     6576   6918   5561    535    379   -431       C  
ATOM   1222  CD1 PHE A 275     -15.474 -29.230  14.739  1.00 51.62           C  
ANISOU 1222  CD1 PHE A 275     6836   7079   5697    499    356   -311       C  
ATOM   1223  CD2 PHE A 275     -17.651 -28.685  15.516  1.00 52.17           C  
ANISOU 1223  CD2 PHE A 275     6749   7267   5807    521    448   -433       C  
ATOM   1224  CE1 PHE A 275     -15.725 -30.586  14.964  1.00 52.26           C  
ANISOU 1224  CE1 PHE A 275     6924   7212   5723    458    379   -177       C  
ATOM   1225  CE2 PHE A 275     -17.895 -30.036  15.771  1.00 55.38           C  
ANISOU 1225  CE2 PHE A 275     7164   7738   6138    460    495   -291       C  
ATOM   1226  CZ  PHE A 275     -16.936 -30.983  15.481  1.00 52.75           C  
ANISOU 1226  CZ  PHE A 275     6921   7360   5761    432    449   -155       C  
ATOM   1227  N   GLY A 276     -16.428 -24.244  12.085  1.00 63.55           N  
ANISOU 1227  N   GLY A 276     8419   8034   7692    617     86   -639       N  
ATOM   1228  CA  GLY A 276     -16.761 -22.859  11.765  1.00 67.60           C  
ANISOU 1228  CA  GLY A 276     8943   8392   8351    658    -20   -732       C  
ATOM   1229  C   GLY A 276     -18.245 -22.579  11.613  1.00 77.20           C  
ANISOU 1229  C   GLY A 276    10074   9550   9709    730   -104   -797       C  
ATOM   1230  O   GLY A 276     -18.745 -21.630  12.223  1.00 78.91           O  
ANISOU 1230  O   GLY A 276    10183   9754  10046    801   -142   -963       O  
ATOM   1231  N   TRP A 277     -18.974 -23.433  10.865  1.00 76.01           N  
ANISOU 1231  N   TRP A 277     9946   9371   9564    718   -136   -694       N  
ATOM   1232  CA  TRP A 277     -20.417 -23.304  10.637  1.00 79.09           C  
ANISOU 1232  CA  TRP A 277    10237   9697  10114    787   -231   -762       C  
ATOM   1233  C   TRP A 277     -21.269 -24.016  11.689  1.00 77.88           C  
ANISOU 1233  C   TRP A 277     9888   9745   9959    806    -99   -852       C  
ATOM   1234  O   TRP A 277     -22.470 -24.171  11.490  1.00 76.25           O  
ANISOU 1234  O   TRP A 277     9572   9509   9892    846   -148   -910       O  
ATOM   1235  CB  TRP A 277     -20.774 -23.789   9.227  1.00 80.83           C  
ANISOU 1235  CB  TRP A 277    10590   9771  10351    760   -355   -618       C  
ATOM   1236  CG  TRP A 277     -20.276 -22.894   8.136  1.00 85.04           C  
ANISOU 1236  CG  TRP A 277    11323  10086  10900    736   -507   -544       C  
ATOM   1237  CD1 TRP A 277     -18.977 -22.703   7.750  1.00 87.87           C  
ANISOU 1237  CD1 TRP A 277    11843  10410  11132    647   -460   -454       C  
ATOM   1238  CD2 TRP A 277     -21.080 -22.105   7.255  1.00 87.92           C  
ANISOU 1238  CD2 TRP A 277    11756  10230  11418    788   -737   -548       C  
ATOM   1239  NE1 TRP A 277     -18.922 -21.822   6.698  1.00 89.64           N  
ANISOU 1239  NE1 TRP A 277    12246  10413  11398    620   -622   -389       N  
ATOM   1240  CE2 TRP A 277     -20.203 -21.468   6.344  1.00 93.26           C  
ANISOU 1240  CE2 TRP A 277    12669  10745  12019    710   -814   -430       C  
ATOM   1241  CE3 TRP A 277     -22.467 -21.888   7.131  1.00 91.66           C  
ANISOU 1241  CE3 TRP A 277    12113  10618  12097    889   -896   -643       C  
ATOM   1242  CZ2 TRP A 277     -20.665 -20.579   5.354  1.00 95.05           C  
ANISOU 1242  CZ2 TRP A 277    13050  10719  12345    727  -1060   -378       C  
ATOM   1243  CZ3 TRP A 277     -22.926 -21.035   6.132  1.00 95.46           C  
ANISOU 1243  CZ3 TRP A 277    12725  10842  12704    928  -1163   -611       C  
ATOM   1244  CH2 TRP A 277     -22.032 -20.375   5.271  1.00 96.65           C  
ANISOU 1244  CH2 TRP A 277    13142  10828  12754    846  -1251   -467       C  
ATOM   1245  N   SER A 278     -20.657 -24.439  12.813  1.00 72.44           N  
ANISOU 1245  N   SER A 278     9156   9257   9112    768     64   -868       N  
ATOM   1246  CA  SER A 278     -21.353 -25.134  13.889  1.00 73.38           C  
ANISOU 1246  CA  SER A 278     9124   9583   9174    751    215   -928       C  
ATOM   1247  C   SER A 278     -21.903 -24.182  14.934  1.00 82.34           C  
ANISOU 1247  C   SER A 278    10095  10812  10377    807    268  -1169       C  
ATOM   1248  O   SER A 278     -21.226 -23.231  15.321  1.00 84.18           O  
ANISOU 1248  O   SER A 278    10350  11032  10603    841    241  -1267       O  
ATOM   1249  CB  SER A 278     -20.468 -26.210  14.523  1.00 76.49           C  
ANISOU 1249  CB  SER A 278     9586  10136   9340    670    339   -793       C  
ATOM   1250  OG  SER A 278     -19.462 -25.707  15.381  1.00 87.45           O  
ANISOU 1250  OG  SER A 278    11005  11616  10606    672    378   -851       O  
ATOM   1251  N   VAL A 279     -23.152 -24.399  15.334  1.00 81.02           N  
ANISOU 1251  N   VAL A 279     9751  10729  10303    815    341  -1287       N  
ATOM   1252  CA  VAL A 279     -23.825 -23.611  16.363  1.00 84.04           C  
ANISOU 1252  CA  VAL A 279     9941  11232  10759    859    426  -1557       C  
ATOM   1253  C   VAL A 279     -24.516 -24.607  17.316  1.00 88.37           C  
ANISOU 1253  C   VAL A 279    10371  12028  11178    766    654  -1575       C  
ATOM   1254  O   VAL A 279     -24.424 -25.821  17.116  1.00 84.57           O  
ANISOU 1254  O   VAL A 279     9969  11586  10579    679    709  -1364       O  
ATOM   1255  CB  VAL A 279     -24.788 -22.483  15.849  1.00 90.22           C  
ANISOU 1255  CB  VAL A 279    10582  11828  11869    977    267  -1769       C  
ATOM   1256  CG1 VAL A 279     -24.739 -21.256  16.770  1.00 92.03           C  
ANISOU 1256  CG1 VAL A 279    10693  12112  12164   1046    289  -2045       C  
ATOM   1257  CG2 VAL A 279     -24.509 -22.081  14.406  1.00 88.96           C  
ANISOU 1257  CG2 VAL A 279    10583  11373  11844   1026     15  -1630       C  
ATOM   1258  N   HIS A 280     -25.152 -24.095  18.378  1.00 89.91           N  
ANISOU 1258  N   HIS A 280    10384  12392  11385    772    793  -1828       N  
ATOM   1259  CA  HIS A 280     -25.860 -24.905  19.356  1.00 92.27           C  
ANISOU 1259  CA  HIS A 280    10567  12942  11547    658   1039  -1870       C  
ATOM   1260  C   HIS A 280     -27.336 -24.991  18.951  1.00 99.50           C  
ANISOU 1260  C   HIS A 280    11255  13804  12746    673   1058  -2014       C  
ATOM   1261  O   HIS A 280     -28.012 -23.969  18.794  1.00102.19           O  
ANISOU 1261  O   HIS A 280    11420  14052  13356    783    974  -2276       O  
ATOM   1262  CB  HIS A 280     -25.615 -24.384  20.782  1.00 94.89           C  
ANISOU 1262  CB  HIS A 280    10852  13523  11679    630   1207  -2064       C  
ATOM   1263  CG  HIS A 280     -24.215 -24.663  21.286  1.00 97.41           C  
ANISOU 1263  CG  HIS A 280    11397  13927  11687    586   1200  -1886       C  
ATOM   1264  ND1 HIS A 280     -23.132 -23.854  20.940  1.00 97.68           N  
ANISOU 1264  ND1 HIS A 280    11545  13820  11750    678   1024  -1881       N  
ATOM   1265  CD2 HIS A 280     -23.767 -25.659  22.090  1.00 99.74           C  
ANISOU 1265  CD2 HIS A 280    11817  14416  11662    460   1331  -1713       C  
ATOM   1266  CE1 HIS A 280     -22.077 -24.383  21.544  1.00 96.53           C  
ANISOU 1266  CE1 HIS A 280    11563  13793  11320    615   1055  -1731       C  
ATOM   1267  NE2 HIS A 280     -22.408 -25.461  22.257  1.00 98.06           N  
ANISOU 1267  NE2 HIS A 280    11780  14184  11293    490   1221  -1620       N  
ATOM   1268  N   ALA A 281     -27.788 -26.229  18.687  1.00 95.44           N  
ANISOU 1268  N   ALA A 281    10747  13315  12203    570   1134  -1837       N  
ATOM   1269  CA  ALA A 281     -29.118 -26.590  18.199  1.00 96.41           C  
ANISOU 1269  CA  ALA A 281    10664  13375  12591    563   1145  -1927       C  
ATOM   1270  C   ALA A 281     -30.273 -26.153  19.104  1.00103.15           C  
ANISOU 1270  C   ALA A 281    11218  14401  13572    540   1346  -2265       C  
ATOM   1271  O   ALA A 281     -30.111 -26.210  20.325  1.00104.49           O  
ANISOU 1271  O   ALA A 281    11376  14830  13496    440   1584  -2335       O  
ATOM   1272  CB  ALA A 281     -29.184 -28.093  17.995  1.00 96.57           C  
ANISOU 1272  CB  ALA A 281    10767  13426  12497    425   1228  -1661       C  
ATOM   1273  N   PRO A 282     -31.461 -25.763  18.561  1.00 99.94           N  
ANISOU 1273  N   PRO A 282    10562  13867  13541    622   1261  -2489       N  
ATOM   1274  CA  PRO A 282     -31.886 -25.699  17.151  1.00 98.86           C  
ANISOU 1274  CA  PRO A 282    10417  13434  13713    737    967  -2441       C  
ATOM   1275  C   PRO A 282     -31.886 -24.281  16.553  1.00103.46           C  
ANISOU 1275  C   PRO A 282    10969  13784  14557    934    682  -2621       C  
ATOM   1276  O   PRO A 282     -32.893 -23.577  16.628  1.00106.33           O  
ANISOU 1276  O   PRO A 282    11062  14099  15240   1024    638  -2937       O  
ATOM   1277  CB  PRO A 282     -33.289 -26.334  17.210  1.00102.71           C  
ANISOU 1277  CB  PRO A 282    10619  13975  14429    668   1099  -2591       C  
ATOM   1278  CG  PRO A 282     -33.760 -26.133  18.678  1.00109.99           C  
ANISOU 1278  CG  PRO A 282    11326  15203  15261    566   1445  -2859       C  
ATOM   1279  CD  PRO A 282     -32.611 -25.469  19.422  1.00104.59           C  
ANISOU 1279  CD  PRO A 282    10827  14633  14278    584   1484  -2839       C  
ATOM   1280  N   SER A 283     -30.769 -23.873  15.927  1.00 98.25           N  
ANISOU 1280  N   SER A 283    10581  12965  13783    995    481  -2423       N  
ATOM   1281  CA  SER A 283     -30.588 -22.530  15.356  1.00 98.22           C  
ANISOU 1281  CA  SER A 283    10610  12721  13987   1155    203  -2535       C  
ATOM   1282  C   SER A 283     -31.211 -22.318  13.932  1.00101.05           C  
ANISOU 1282  C   SER A 283    10984  12763  14648   1265   -134  -2499       C  
ATOM   1283  O   SER A 283     -31.995 -23.155  13.473  1.00 99.50           O  
ANISOU 1283  O   SER A 283    10700  12550  14555   1233   -142  -2462       O  
ATOM   1284  CB  SER A 283     -29.106 -22.160  15.377  1.00 99.92           C  
ANISOU 1284  CB  SER A 283    11105  12916  13944   1145    163  -2351       C  
ATOM   1285  OG  SER A 283     -28.641 -22.045  16.715  1.00111.90           O  
ANISOU 1285  OG  SER A 283    12579  14692  15244   1085    407  -2460       O  
ATOM   1286  N   SER A 284     -30.862 -21.181  13.346  1.00 97.97           N  
ANISOU 1286  N   SER A 284    10701  12117  14407   1391   -422  -2521       N  
ATOM   1287  CA  SER A 284     -31.027 -20.864  11.942  1.00120.03           C  
ANISOU 1287  CA  SER A 284    13581  14581  17444   1499   -795  -2461       C  
ATOM   1288  C   SER A 284     -29.876 -19.950  11.509  1.00140.78           C  
ANISOU 1288  C   SER A 284    16429  16977  20085   1571  -1034  -2393       C  
ATOM   1289  O   SER A 284     -28.833 -19.890  12.160  1.00100.80           O  
ANISOU 1289  O   SER A 284    11614  11947  14739   1493   -969  -2180       O  
ATOM   1290  CB  SER A 284     -32.345 -20.182  11.669  1.00126.68           C  
ANISOU 1290  CB  SER A 284    14101  15325  18708   1615   -926  -2769       C  
ATOM   1291  OG  SER A 284     -32.324 -19.677  10.355  1.00136.04           O  
ANISOU 1291  OG  SER A 284    15393  16193  20104   1714  -1313  -2685       O  
ATOM   1292  N   CYS A 290     -22.184 -19.037   1.904  1.00108.75           N  
ANISOU 1292  N   CYS A 290    15392  11743  14187    726  -1866    -71       N  
ATOM   1293  CA  CYS A 290     -22.415 -20.427   1.518  1.00107.30           C  
ANISOU 1293  CA  CYS A 290    15192  11719  13858    699  -1774    -28       C  
ATOM   1294  C   CYS A 290     -21.784 -20.802   0.161  1.00106.37           C  
ANISOU 1294  C   CYS A 290    15406  11552  13457    545  -1797    175       C  
ATOM   1295  O   CYS A 290     -21.792 -20.007  -0.790  1.00108.53           O  
ANISOU 1295  O   CYS A 290    15948  11606  13682    493  -2015    301       O  
ATOM   1296  CB  CYS A 290     -23.902 -20.779   1.563  1.00109.48           C  
ANISOU 1296  CB  CYS A 290    15280  11967  14351    846  -1954   -144       C  
ATOM   1297  SG  CYS A 290     -24.857 -20.204   0.131  1.00116.85           S  
ANISOU 1297  SG  CYS A 290    16448  12584  15364    896  -2405    -49       S  
ATOM   1298  N   GLY A 291     -21.241 -22.018   0.109  1.00 95.29           N  
ANISOU 1298  N   GLY A 291    13981  10353  11870    468  -1570    198       N  
ATOM   1299  CA  GLY A 291     -20.620 -22.579  -1.084  1.00 91.95           C  
ANISOU 1299  CA  GLY A 291    13822   9941  11172    320  -1532    339       C  
ATOM   1300  C   GLY A 291     -21.585 -23.486  -1.820  1.00 87.37           C  
ANISOU 1300  C   GLY A 291    13255   9363  10577    370  -1682    343       C  
ATOM   1301  O   GLY A 291     -22.718 -23.085  -2.126  1.00 88.82           O  
ANISOU 1301  O   GLY A 291    13441   9391  10917    477  -1969    327       O  
ATOM   1302  N   THR A 292     -21.139 -24.729  -2.071  1.00 75.14           N  
ANISOU 1302  N   THR A 292    11693   7985   8874    301  -1499    345       N  
ATOM   1303  CA  THR A 292     -21.901 -25.786  -2.737  1.00 71.29           C  
ANISOU 1303  CA  THR A 292    11199   7525   8364    333  -1601    331       C  
ATOM   1304  C   THR A 292     -22.972 -26.314  -1.751  1.00 66.71           C  
ANISOU 1304  C   THR A 292    10280   7006   8059    486  -1616    196       C  
ATOM   1305  O   THR A 292     -22.713 -26.446  -0.556  1.00 65.11           O  
ANISOU 1305  O   THR A 292     9856   6930   7954    517  -1419    122       O  
ATOM   1306  CB  THR A 292     -20.917 -26.817  -3.356  1.00 76.14           C  
ANISOU 1306  CB  THR A 292    11924   8280   8726    195  -1394    363       C  
ATOM   1307  OG1 THR A 292     -20.644 -26.488  -4.727  1.00 80.38           O  
ANISOU 1307  OG1 THR A 292    12804   8721   9014     73  -1508    473       O  
ATOM   1308  CG2 THR A 292     -21.388 -28.241  -3.258  1.00 66.25           C  
ANISOU 1308  CG2 THR A 292    10492   7146   7534    246  -1345    284       C  
ATOM   1309  N   LEU A 293     -24.189 -26.568  -2.248  1.00 59.32           N  
ANISOU 1309  N   LEU A 293     9311   5981   7249    573  -1857    160       N  
ATOM   1310  CA  LEU A 293     -25.318 -27.032  -1.430  1.00 55.92           C  
ANISOU 1310  CA  LEU A 293     8558   5593   7097    700  -1879     20       C  
ATOM   1311  C   LEU A 293     -25.333 -28.524  -1.176  1.00 54.69           C  
ANISOU 1311  C   LEU A 293     8245   5605   6931    672  -1696    -16       C  
ATOM   1312  O   LEU A 293     -26.121 -28.990  -0.364  1.00 52.87           O  
ANISOU 1312  O   LEU A 293     7741   5438   6908    740  -1645   -120       O  
ATOM   1313  CB  LEU A 293     -26.636 -26.671  -2.141  1.00 57.87           C  
ANISOU 1313  CB  LEU A 293     8820   5648   7518    806  -2241    -24       C  
ATOM   1314  CG  LEU A 293     -26.951 -25.222  -2.404  1.00 63.88           C  
ANISOU 1314  CG  LEU A 293     9707   6189   8374    868  -2511     -4       C  
ATOM   1315  CD1 LEU A 293     -28.075 -25.107  -3.396  1.00 65.27           C  
ANISOU 1315  CD1 LEU A 293     9968   6172   8661    953  -2902    -16       C  
ATOM   1316  CD2 LEU A 293     -27.252 -24.460  -1.105  1.00 64.84           C  
ANISOU 1316  CD2 LEU A 293     9557   6320   8760    966  -2439   -145       C  
ATOM   1317  N   ASP A 294     -24.509 -29.273  -1.899  1.00 50.32           N  
ANISOU 1317  N   ASP A 294     7862   5112   6146    566  -1603     60       N  
ATOM   1318  CA  ASP A 294     -24.491 -30.738  -1.982  1.00 50.53           C  
ANISOU 1318  CA  ASP A 294     7793   5250   6154    534  -1490     34       C  
ATOM   1319  C   ASP A 294     -24.779 -31.506  -0.715  1.00 52.26           C  
ANISOU 1319  C   ASP A 294     7709   5595   6551    569  -1306    -33       C  
ATOM   1320  O   ASP A 294     -25.485 -32.513  -0.795  1.00 51.47           O  
ANISOU 1320  O   ASP A 294     7480   5510   6566    586  -1334    -78       O  
ATOM   1321  CB  ASP A 294     -23.185 -31.250  -2.598  1.00 52.85           C  
ANISOU 1321  CB  ASP A 294     8277   5620   6184    408  -1333     95       C  
ATOM   1322  CG  ASP A 294     -23.231 -31.269  -4.127  1.00 64.05           C  
ANISOU 1322  CG  ASP A 294     9975   6952   7410    351  -1513    135       C  
ATOM   1323  OD1 ASP A 294     -24.250 -31.735  -4.684  1.00 67.48           O  
ANISOU 1323  OD1 ASP A 294    10387   7322   7931    409  -1716     93       O  
ATOM   1324  OD2 ASP A 294     -22.221 -30.894  -4.759  1.00 65.36           O  
ANISOU 1324  OD2 ASP A 294    10375   7127   7332    237  -1438    198       O  
ATOM   1325  N   TYR A 295     -24.314 -31.035   0.442  1.00 47.61           N  
ANISOU 1325  N   TYR A 295     7012   5090   5988    573  -1134    -41       N  
ATOM   1326  CA  TYR A 295     -24.519 -31.754   1.708  1.00 47.65           C  
ANISOU 1326  CA  TYR A 295     6764   5230   6112    583   -948    -84       C  
ATOM   1327  C   TYR A 295     -25.581 -31.160   2.623  1.00 52.35           C  
ANISOU 1327  C   TYR A 295     7140   5829   6924    664   -970   -188       C  
ATOM   1328  O   TYR A 295     -25.872 -31.757   3.657  1.00 51.69           O  
ANISOU 1328  O   TYR A 295     6856   5865   6922    653   -808   -224       O  
ATOM   1329  CB  TYR A 295     -23.178 -31.888   2.467  1.00 48.78           C  
ANISOU 1329  CB  TYR A 295     6927   5498   6109    519   -718    -34       C  
ATOM   1330  CG  TYR A 295     -22.112 -32.426   1.545  1.00 51.39           C  
ANISOU 1330  CG  TYR A 295     7444   5825   6257    439   -685     27       C  
ATOM   1331  CD1 TYR A 295     -21.404 -31.576   0.699  1.00 54.59           C  
ANISOU 1331  CD1 TYR A 295     8074   6162   6507    393   -736     62       C  
ATOM   1332  CD2 TYR A 295     -21.877 -33.789   1.445  1.00 51.37           C  
ANISOU 1332  CD2 TYR A 295     7394   5877   6249    401   -610     37       C  
ATOM   1333  CE1 TYR A 295     -20.487 -32.072  -0.220  1.00 55.64           C  
ANISOU 1333  CE1 TYR A 295     8369   6304   6466    304   -685     89       C  
ATOM   1334  CE2 TYR A 295     -20.979 -34.300   0.511  1.00 52.13           C  
ANISOU 1334  CE2 TYR A 295     7640   5967   6200    332   -584     49       C  
ATOM   1335  CZ  TYR A 295     -20.281 -33.436  -0.314  1.00 57.27           C  
ANISOU 1335  CZ  TYR A 295     8503   6575   6680    280   -608     66       C  
ATOM   1336  OH  TYR A 295     -19.381 -33.924  -1.234  1.00 54.30           O  
ANISOU 1336  OH  TYR A 295     8267   6214   6149    194   -550     53       O  
ATOM   1337  N   LEU A 296     -26.165 -30.027   2.259  1.00 50.21           N  
ANISOU 1337  N   LEU A 296     6904   5425   6749    738  -1168   -242       N  
ATOM   1338  CA  LEU A 296     -27.158 -29.375   3.098  1.00 52.45           C  
ANISOU 1338  CA  LEU A 296     6958   5704   7266    825  -1194   -384       C  
ATOM   1339  C   LEU A 296     -28.552 -29.985   2.941  1.00 56.98           C  
ANISOU 1339  C   LEU A 296     7330   6240   8079    874  -1301   -489       C  
ATOM   1340  O   LEU A 296     -28.968 -30.287   1.821  1.00 56.96           O  
ANISOU 1340  O   LEU A 296     7427   6117   8099    891  -1511   -466       O  
ATOM   1341  CB  LEU A 296     -27.179 -27.857   2.849  1.00 54.17           C  
ANISOU 1341  CB  LEU A 296     7275   5772   7536    895  -1378   -419       C  
ATOM   1342  CG  LEU A 296     -25.866 -27.120   3.206  1.00 59.75           C  
ANISOU 1342  CG  LEU A 296     8130   6516   8058    843  -1252   -347       C  
ATOM   1343  CD1 LEU A 296     -25.944 -25.644   2.791  1.00 60.78           C  
ANISOU 1343  CD1 LEU A 296     8384   6451   8259    902  -1473   -362       C  
ATOM   1344  CD2 LEU A 296     -25.501 -27.285   4.722  1.00 61.89           C  
ANISOU 1344  CD2 LEU A 296     8206   6989   8322    827   -975   -415       C  
ATOM   1345  N   PRO A 297     -29.299 -30.153   4.048  1.00 53.69           N  
ANISOU 1345  N   PRO A 297     6628   5929   7843    888  -1156   -617       N  
ATOM   1346  CA  PRO A 297     -30.654 -30.696   3.939  1.00 54.99           C  
ANISOU 1346  CA  PRO A 297     6566   6057   8271    922  -1239   -742       C  
ATOM   1347  C   PRO A 297     -31.687 -29.667   3.448  1.00 60.25           C  
ANISOU 1347  C   PRO A 297     7153   6542   9196   1055  -1533   -898       C  
ATOM   1348  O   PRO A 297     -31.402 -28.449   3.439  1.00 57.88           O  
ANISOU 1348  O   PRO A 297     6945   6155   8889   1120  -1643   -919       O  
ATOM   1349  CB  PRO A 297     -30.955 -31.165   5.362  1.00 56.64           C  
ANISOU 1349  CB  PRO A 297     6514   6460   8544    861   -938   -819       C  
ATOM   1350  CG  PRO A 297     -29.885 -30.635   6.211  1.00 60.46           C  
ANISOU 1350  CG  PRO A 297     7087   7064   8822    829   -757   -763       C  
ATOM   1351  CD  PRO A 297     -28.990 -29.783   5.440  1.00 55.29           C  
ANISOU 1351  CD  PRO A 297     6696   6290   8020    869   -915   -675       C  
ATOM   1352  N   PRO A 298     -32.914 -30.123   3.081  1.00 58.33           N  
ANISOU 1352  N   PRO A 298     6721   6224   9216   1099  -1677  -1023       N  
ATOM   1353  CA  PRO A 298     -33.941 -29.170   2.619  1.00 60.11           C  
ANISOU 1353  CA  PRO A 298     6850   6258   9733   1242  -1996  -1192       C  
ATOM   1354  C   PRO A 298     -34.258 -28.049   3.608  1.00 66.75           C  
ANISOU 1354  C   PRO A 298     7488   7117  10756   1316  -1937  -1377       C  
ATOM   1355  O   PRO A 298     -34.205 -26.889   3.209  1.00 67.01           O  
ANISOU 1355  O   PRO A 298     7637   6981  10845   1416  -2182  -1400       O  
ATOM   1356  CB  PRO A 298     -35.150 -30.080   2.328  1.00 62.41           C  
ANISOU 1356  CB  PRO A 298     6904   6517  10290   1253  -2078  -1319       C  
ATOM   1357  CG  PRO A 298     -34.558 -31.417   2.064  1.00 63.24           C  
ANISOU 1357  CG  PRO A 298     7132   6722  10174   1126  -1922  -1147       C  
ATOM   1358  CD  PRO A 298     -33.430 -31.507   3.036  1.00 57.90           C  
ANISOU 1358  CD  PRO A 298     6529   6235   9238   1026  -1583  -1024       C  
ATOM   1359  N   GLU A 299     -34.491 -28.385   4.902  1.00 65.25           N  
ANISOU 1359  N   GLU A 299     7028   7137  10628   1254  -1604  -1496       N  
ATOM   1360  CA  GLU A 299     -34.799 -27.409   5.963  1.00 66.97           C  
ANISOU 1360  CA  GLU A 299     7025   7416  11004   1310  -1496  -1711       C  
ATOM   1361  C   GLU A 299     -33.733 -26.304   6.099  1.00 71.56           C  
ANISOU 1361  C   GLU A 299     7832   7961  11397   1342  -1525  -1629       C  
ATOM   1362  O   GLU A 299     -34.052 -25.211   6.568  1.00 71.77           O  
ANISOU 1362  O   GLU A 299     7724   7934  11610   1438  -1586  -1820       O  
ATOM   1363  CB  GLU A 299     -35.084 -28.105   7.325  1.00 68.55           C  
ANISOU 1363  CB  GLU A 299     6953   7886  11205   1193  -1089  -1815       C  
ATOM   1364  CG  GLU A 299     -33.861 -28.682   8.043  1.00 74.33           C  
ANISOU 1364  CG  GLU A 299     7860   8826  11557   1053   -781  -1604       C  
ATOM   1365  CD  GLU A 299     -33.635 -30.181   7.920  1.00 86.75           C  
ANISOU 1365  CD  GLU A 299     9497  10486  12976    917   -636  -1414       C  
ATOM   1366  OE1 GLU A 299     -33.917 -30.729   6.831  1.00 69.26           O  
ANISOU 1366  OE1 GLU A 299     7354   8128  10832    937   -842  -1347       O  
ATOM   1367  OE2 GLU A 299     -33.167 -30.811   8.894  1.00 67.53           O  
ANISOU 1367  OE2 GLU A 299     7053   8253  10352    792   -338  -1332       O  
ATOM   1368  N   MET A 300     -32.476 -26.592   5.704  1.00 67.61           N  
ANISOU 1368  N   MET A 300     7651   7485  10553   1261  -1475  -1367       N  
ATOM   1369  CA  MET A 300     -31.397 -25.614   5.785  1.00 67.36           C  
ANISOU 1369  CA  MET A 300     7834   7415  10344   1269  -1488  -1281       C  
ATOM   1370  C   MET A 300     -31.328 -24.744   4.559  1.00 72.42           C  
ANISOU 1370  C   MET A 300     8715   7781  11020   1348  -1858  -1204       C  
ATOM   1371  O   MET A 300     -31.152 -23.534   4.695  1.00 73.77           O  
ANISOU 1371  O   MET A 300     8923   7834  11270   1417  -1976  -1265       O  
ATOM   1372  CB  MET A 300     -30.048 -26.277   6.031  1.00 67.64           C  
ANISOU 1372  CB  MET A 300     8068   7611  10020   1138  -1244  -1068       C  
ATOM   1373  CG  MET A 300     -29.672 -26.326   7.469  1.00 72.14           C  
ANISOU 1373  CG  MET A 300     8493   8412  10505   1084   -929  -1138       C  
ATOM   1374  SD  MET A 300     -27.892 -26.663   7.646  1.00 75.23           S  
ANISOU 1374  SD  MET A 300     9156   8916  10512    972   -750   -906       S  
ATOM   1375  CE  MET A 300     -27.250 -24.983   7.376  1.00 72.78           C  
ANISOU 1375  CE  MET A 300     9001   8432  10220   1047   -929   -935       C  
ATOM   1376  N   ILE A 301     -31.443 -25.349   3.356  1.00 67.91           N  
ANISOU 1376  N   ILE A 301     8323   7101  10378   1329  -2048  -1067       N  
ATOM   1377  CA  ILE A 301     -31.411 -24.604   2.091  1.00 67.79           C  
ANISOU 1377  CA  ILE A 301     8585   6825  10350   1383  -2418   -965       C  
ATOM   1378  C   ILE A 301     -32.644 -23.684   1.952  1.00 73.33           C  
ANISOU 1378  C   ILE A 301     9115   7308  11440   1548  -2750  -1168       C  
ATOM   1379  O   ILE A 301     -32.543 -22.623   1.319  1.00 71.96           O  
ANISOU 1379  O   ILE A 301     9142   6901  11299   1610  -3048  -1114       O  
ATOM   1380  CB  ILE A 301     -31.179 -25.517   0.842  1.00 69.74           C  
ANISOU 1380  CB  ILE A 301     9084   7034  10380   1310  -2528   -779       C  
ATOM   1381  CG1 ILE A 301     -32.381 -26.448   0.524  1.00 70.02           C  
ANISOU 1381  CG1 ILE A 301     8918   7060  10628   1355  -2639   -893       C  
ATOM   1382  CG2 ILE A 301     -29.870 -26.319   0.988  1.00 65.76           C  
ANISOU 1382  CG2 ILE A 301     8736   6724   9526   1158  -2212   -606       C  
ATOM   1383  CD1 ILE A 301     -32.459 -26.902  -0.928  1.00 72.02           C  
ANISOU 1383  CD1 ILE A 301     9432   7182  10749   1340  -2910   -767       C  
ATOM   1384  N   GLU A 302     -33.782 -24.077   2.579  1.00 72.82           N  
ANISOU 1384  N   GLU A 302     8673   7315  11681   1611  -2693  -1409       N  
ATOM   1385  CA  GLU A 302     -35.049 -23.315   2.586  1.00 76.54           C  
ANISOU 1385  CA  GLU A 302     8891   7601  12588   1777  -2978  -1670       C  
ATOM   1386  C   GLU A 302     -35.086 -22.244   3.707  1.00 83.24           C  
ANISOU 1386  C   GLU A 302     9526   8476  13624   1846  -2869  -1883       C  
ATOM   1387  O   GLU A 302     -36.040 -21.466   3.781  1.00 86.78           O  
ANISOU 1387  O   GLU A 302     9754   8760  14459   1995  -3104  -2128       O  
ATOM   1388  CB  GLU A 302     -36.260 -24.268   2.677  1.00 78.62           C  
ANISOU 1388  CB  GLU A 302     8827   7931  13115   1798  -2954  -1856       C  
ATOM   1389  CG  GLU A 302     -36.537 -25.035   1.394  1.00 89.53           C  
ANISOU 1389  CG  GLU A 302    10386   9196  14436   1790  -3211  -1721       C  
ATOM   1390  CD  GLU A 302     -37.337 -26.325   1.489  1.00115.00           C  
ANISOU 1390  CD  GLU A 302    13353  12542  17798   1743  -3083  -1823       C  
ATOM   1391  OE1 GLU A 302     -38.086 -26.509   2.475  1.00115.57           O  
ANISOU 1391  OE1 GLU A 302    13037  12740  18136   1746  -2872  -2062       O  
ATOM   1392  OE2 GLU A 302     -37.227 -27.151   0.555  1.00110.57           O  
ANISOU 1392  OE2 GLU A 302    12979  11949  17082   1694  -3194  -1673       O  
ATOM   1393  N   GLY A 303     -34.074 -22.228   4.550  1.00 78.67           N  
ANISOU 1393  N   GLY A 303     9005   8100  12787   1745  -2530  -1808       N  
ATOM   1394  CA  GLY A 303     -33.968 -21.242   5.592  1.00 79.97           C  
ANISOU 1394  CA  GLY A 303     8998   8325  13062   1790  -2389  -2001       C  
ATOM   1395  C   GLY A 303     -34.842 -21.523   6.784  1.00 86.10           C  
ANISOU 1395  C   GLY A 303     9346   9322  14047   1797  -2109  -2307       C  
ATOM   1396  O   GLY A 303     -35.121 -20.622   7.538  1.00 87.78           O  
ANISOU 1396  O   GLY A 303     9387   9595  14369   1842  -1995  -2517       O  
ATOM   1397  N   ARG A 304     -35.261 -22.763   6.967  1.00 81.43           N  
ANISOU 1397  N   ARG A 304     8581   8856  13503   1739  -1981  -2341       N  
ATOM   1398  CA  ARG A 304     -36.133 -23.113   8.077  1.00 82.16           C  
ANISOU 1398  CA  ARG A 304     8271   9170  13777   1703  -1686  -2613       C  
ATOM   1399  C   ARG A 304     -35.434 -23.445   9.376  1.00 86.42           C  
ANISOU 1399  C   ARG A 304     8790  10032  14015   1560  -1233  -2582       C  
ATOM   1400  O   ARG A 304     -34.256 -23.241   9.533  1.00 81.89           O  
ANISOU 1400  O   ARG A 304     8505   9507  13102   1494  -1157  -2345       O  
ATOM   1401  CB  ARG A 304     -37.010 -24.295   7.717  1.00 79.54           C  
ANISOU 1401  CB  ARG A 304     7808   8860  13553   1652  -1684  -2606       C  
ATOM   1402  CG  ARG A 304     -37.959 -24.041   6.583  1.00 87.01           C  
ANISOU 1402  CG  ARG A 304     8699   9514  14847   1800  -2129  -2704       C  
ATOM   1403  CD  ARG A 304     -38.771 -25.274   6.277  1.00 93.09           C  
ANISOU 1403  CD  ARG A 304     9280  10333  15756   1742  -2085  -2749       C  
ATOM   1404  NE  ARG A 304     -38.376 -25.833   5.003  1.00 94.58           N  
ANISOU 1404  NE  ARG A 304     9788  10516  15634   1646  -2121  -2422       N  
ATOM   1405  CZ  ARG A 304     -38.198 -27.124   4.794  1.00109.45           C  
ANISOU 1405  CZ  ARG A 304    11605  12553  17430   1510  -1892  -2346       C  
ATOM   1406  NH1 ARG A 304     -38.398 -27.969   5.779  1.00103.23           N  
ANISOU 1406  NH1 ARG A 304    10463  11950  16811   1428  -1585  -2542       N  
ATOM   1407  NH2 ARG A 304     -37.835 -27.565   3.603  1.00 94.84           N  
ANISOU 1407  NH2 ARG A 304    10040  10671  15324   1443  -1960  -2079       N  
ATOM   1408  N   MET A 305     -36.199 -23.931  10.334  1.00 88.09           N  
ANISOU 1408  N   MET A 305     8657  10463  14351   1503   -935  -2830       N  
ATOM   1409  CA  MET A 305     -35.642 -24.270  11.625  1.00 88.54           C  
ANISOU 1409  CA  MET A 305     8683  10841  14117   1354   -508  -2817       C  
ATOM   1410  C   MET A 305     -35.114 -25.681  11.590  1.00 87.12           C  
ANISOU 1410  C   MET A 305     8720  10784  13597   1190   -340  -2484       C  
ATOM   1411  O   MET A 305     -35.742 -26.587  11.073  1.00 86.81           O  
ANISOU 1411  O   MET A 305     8620  10714  13650   1141   -364  -2425       O  
ATOM   1412  CB  MET A 305     -36.671 -24.113  12.738  1.00 94.90           C  
ANISOU 1412  CB  MET A 305     9077  11854  15126   1307   -223  -3164       C  
ATOM   1413  CG  MET A 305     -36.095 -24.239  14.143  1.00103.56           C  
ANISOU 1413  CG  MET A 305     9836  12773  16739   1465   -447  -3531       C  
ATOM   1414  SD  MET A 305     -35.933 -22.709  15.095  1.00111.85           S  
ANISOU 1414  SD  MET A 305    10529  13880  18088   1384   -334  -3694       S  
ATOM   1415  CE  MET A 305     -35.756 -21.518  13.785  1.00110.21           C  
ANISOU 1415  CE  MET A 305    10064  14095  17714   1177    258  -3891       C  
ATOM   1416  N   HIS A 306     -33.938 -25.853  12.148  1.00 80.09           N  
ANISOU 1416  N   HIS A 306     8068  10020  12342   1111   -187  -2283       N  
ATOM   1417  CA  HIS A 306     -33.232 -27.105  12.031  1.00 76.50           C  
ANISOU 1417  CA  HIS A 306     7830   9661  11575    971    -54  -1972       C  
ATOM   1418  C   HIS A 306     -32.479 -27.455  13.280  1.00 79.01           C  
ANISOU 1418  C   HIS A 306     8177  10258  11584    836    286  -1915       C  
ATOM   1419  O   HIS A 306     -32.164 -26.599  14.065  1.00 78.50           O  
ANISOU 1419  O   HIS A 306     8104  10278  11443    870    358  -2034       O  
ATOM   1420  CB  HIS A 306     -32.297 -27.078  10.833  1.00 74.05           C  
ANISOU 1420  CB  HIS A 306     7859   9159  11118   1015   -303  -1715       C  
ATOM   1421  CG  HIS A 306     -31.252 -26.017  10.894  1.00 76.40           C  
ANISOU 1421  CG  HIS A 306     8337   9421  11272   1067   -359  -1683       C  
ATOM   1422  ND1 HIS A 306     -31.338 -24.850  10.176  1.00 79.06           N  
ANISOU 1422  ND1 HIS A 306     8707   9533  11797   1204   -637  -1782       N  
ATOM   1423  CD2 HIS A 306     -30.082 -25.958  11.560  1.00 76.58           C  
ANISOU 1423  CD2 HIS A 306     8512   9584  11000    996   -189  -1561       C  
ATOM   1424  CE1 HIS A 306     -30.273 -24.112  10.404  1.00 77.56           C  
ANISOU 1424  CE1 HIS A 306     8682   9361  11427   1200   -605  -1720       C  
ATOM   1425  NE2 HIS A 306     -29.494 -24.763  11.241  1.00 76.46           N  
ANISOU 1425  NE2 HIS A 306     8610   9443  11000   1082   -340  -1599       N  
ATOM   1426  N   ASP A 307     -32.208 -28.732  13.456  1.00 73.30           N  
ANISOU 1426  N   ASP A 307     7497   9665  10690    686    475  -1734       N  
ATOM   1427  CA  ASP A 307     -31.493 -29.187  14.614  1.00 72.21           C  
ANISOU 1427  CA  ASP A 307     7418   9779  10240    544    769  -1640       C  
ATOM   1428  C   ASP A 307     -30.473 -30.245  14.269  1.00 69.94           C  
ANISOU 1428  C   ASP A 307     7411   9476   9687    464    757  -1302       C  
ATOM   1429  O   ASP A 307     -29.837 -30.189  13.255  1.00 67.50           O  
ANISOU 1429  O   ASP A 307     7287   8988   9372    540    535  -1172       O  
ATOM   1430  CB  ASP A 307     -32.471 -29.751  15.618  1.00 77.24           C  
ANISOU 1430  CB  ASP A 307     7791  10615  10942    407   1057  -1787       C  
ATOM   1431  CG  ASP A 307     -33.411 -30.727  14.998  1.00 88.54           C  
ANISOU 1431  CG  ASP A 307     9129  11982  12530    320   1066  -1703       C  
ATOM   1432  OD1 ASP A 307     -33.451 -30.793  13.766  1.00 87.40           O  
ANISOU 1432  OD1 ASP A 307     9047  11613  12546    411    802  -1630       O  
ATOM   1433  OD2 ASP A 307     -34.109 -31.425  15.734  1.00 97.79           O  
ANISOU 1433  OD2 ASP A 307    10166  13327  13665    153   1338  -1720       O  
ATOM   1434  N   GLU A 308     -30.333 -31.208  15.150  1.00 64.12           N  
ANISOU 1434  N   GLU A 308     6705   8926   8730    307    993  -1173       N  
ATOM   1435  CA  GLU A 308     -29.342 -32.235  15.008  1.00 61.49           C  
ANISOU 1435  CA  GLU A 308     6597   8598   8168    218   1008   -876       C  
ATOM   1436  C   GLU A 308     -29.554 -33.094  13.782  1.00 60.46           C  
ANISOU 1436  C   GLU A 308     6520   8271   8182    228    836   -738       C  
ATOM   1437  O   GLU A 308     -28.630 -33.690  13.287  1.00 54.46           O  
ANISOU 1437  O   GLU A 308     5969   7432   7293    232    737   -541       O  
ATOM   1438  CB  GLU A 308     -29.360 -33.121  16.242  1.00 65.08           C  
ANISOU 1438  CB  GLU A 308     7025   9271   8430     32   1285   -793       C  
ATOM   1439  CG  GLU A 308     -28.739 -32.497  17.460  1.00 81.70           C  
ANISOU 1439  CG  GLU A 308     9203  11582  10258      1   1430   -830       C  
ATOM   1440  CD  GLU A 308     -29.763 -31.829  18.338  1.00116.37           C  
ANISOU 1440  CD  GLU A 308    13382  16158  14674    -15   1619  -1119       C  
ATOM   1441  OE1 GLU A 308     -30.962 -31.991  18.056  1.00112.65           O  
ANISOU 1441  OE1 GLU A 308    12683  15620  14500     60   1585  -1359       O  
ATOM   1442  OE2 GLU A 308     -29.362 -31.146  19.301  1.00117.74           O  
ANISOU 1442  OE2 GLU A 308    13621  16544  14570    -98   1790  -1119       O  
ATOM   1443  N   LYS A 309     -30.785 -33.161  13.312  1.00 57.36           N  
ANISOU 1443  N   LYS A 309     5923   7802   8070    239    797   -871       N  
ATOM   1444  CA  LYS A 309     -31.148 -34.058  12.240  1.00 56.37           C  
ANISOU 1444  CA  LYS A 309     5799   7500   8120    248    634   -797       C  
ATOM   1445  C   LYS A 309     -30.521 -33.636  10.940  1.00 60.30           C  
ANISOU 1445  C   LYS A 309     6485   7796   8630    384    342   -742       C  
ATOM   1446  O   LYS A 309     -30.533 -34.343   9.969  1.00 60.82           O  
ANISOU 1446  O   LYS A 309     6615   7730   8765    385    203   -652       O  
ATOM   1447  CB  LYS A 309     -32.655 -34.113  12.089  1.00 59.47           C  
ANISOU 1447  CB  LYS A 309     5895   7868   8834    238    654  -1004       C  
ATOM   1448  CG  LYS A 309     -33.355 -34.803  13.234  1.00 70.92           C  
ANISOU 1448  CG  LYS A 309     7167   9507  10271     51    970  -1023       C  
ATOM   1449  CD  LYS A 309     -32.884 -36.230  13.394  1.00 79.40           C  
ANISOU 1449  CD  LYS A 309     8353  10568  11246    -99   1041   -763       C  
ATOM   1450  CE  LYS A 309     -33.840 -37.021  14.254  1.00 82.68           C  
ANISOU 1450  CE  LYS A 309     8557  11103  11755   -291   1305   -802       C  
ATOM   1451  NZ  LYS A 309     -33.522 -38.461  14.247  1.00 85.49           N  
ANISOU 1451  NZ  LYS A 309     9064  11461  11957   -455   1394   -516       N  
ATOM   1452  N   VAL A 310     -29.983 -32.450  10.943  1.00 54.41           N  
ANISOU 1452  N   VAL A 310     5834   7029   7812    483    257   -798       N  
ATOM   1453  CA  VAL A 310     -29.300 -31.886   9.783  1.00 52.44           C  
ANISOU 1453  CA  VAL A 310     5791   6605   7530    582     14   -736       C  
ATOM   1454  C   VAL A 310     -28.017 -32.721   9.504  1.00 54.63           C  
ANISOU 1454  C   VAL A 310     6300   6888   7567    518     38   -506       C  
ATOM   1455  O   VAL A 310     -27.710 -33.009   8.343  1.00 53.92           O  
ANISOU 1455  O   VAL A 310     6352   6662   7472    541   -125   -424       O  
ATOM   1456  CB  VAL A 310     -28.997 -30.408  10.117  1.00 57.42           C  
ANISOU 1456  CB  VAL A 310     6435   7232   8151    674    -29   -861       C  
ATOM   1457  CG1 VAL A 310     -27.727 -29.917   9.462  1.00 55.43           C  
ANISOU 1457  CG1 VAL A 310     6449   6888   7726    707   -149   -732       C  
ATOM   1458  CG2 VAL A 310     -30.191 -29.518   9.771  1.00 59.16           C  
ANISOU 1458  CG2 VAL A 310     6473   7332   8672    785   -193  -1084       C  
ATOM   1459  N   ASP A 311     -27.291 -33.132  10.574  1.00 50.20           N  
ANISOU 1459  N   ASP A 311     5774   6487   6814    436    234   -418       N  
ATOM   1460  CA  ASP A 311     -26.074 -33.944  10.497  1.00 48.46           C  
ANISOU 1460  CA  ASP A 311     5734   6276   6402    381    258   -229       C  
ATOM   1461  C   ASP A 311     -26.384 -35.380  10.054  1.00 51.05           C  
ANISOU 1461  C   ASP A 311     6050   6550   6795    308    251   -118       C  
ATOM   1462  O   ASP A 311     -25.527 -36.034   9.476  1.00 50.04           O  
ANISOU 1462  O   ASP A 311     6065   6358   6591    296    191      0       O  
ATOM   1463  CB  ASP A 311     -25.327 -33.935  11.844  1.00 49.88           C  
ANISOU 1463  CB  ASP A 311     5941   6631   6380    324    432   -182       C  
ATOM   1464  CG  ASP A 311     -24.715 -32.591  12.217  1.00 52.29           C  
ANISOU 1464  CG  ASP A 311     6291   6976   6602    396    422   -282       C  
ATOM   1465  OD1 ASP A 311     -24.408 -31.796  11.296  1.00 48.79           O  
ANISOU 1465  OD1 ASP A 311     5929   6399   6208    476    271   -320       O  
ATOM   1466  OD2 ASP A 311     -24.488 -32.361  13.412  1.00 54.97           O  
ANISOU 1466  OD2 ASP A 311     6598   7474   6814    362    560   -314       O  
ATOM   1467  N   LEU A 312     -27.597 -35.849  10.309  1.00 48.86           N  
ANISOU 1467  N   LEU A 312     5589   6292   6681    259    313   -176       N  
ATOM   1468  CA  LEU A 312     -28.053 -37.172   9.873  1.00 50.61           C  
ANISOU 1468  CA  LEU A 312     5771   6442   7016    187    296    -93       C  
ATOM   1469  C   LEU A 312     -28.320 -37.212   8.362  1.00 52.11           C  
ANISOU 1469  C   LEU A 312     6004   6452   7342    267     65   -135       C  
ATOM   1470  O   LEU A 312     -28.045 -38.235   7.729  1.00 51.49           O  
ANISOU 1470  O   LEU A 312     5997   6291   7275    235      2    -42       O  
ATOM   1471  CB  LEU A 312     -29.268 -37.634  10.684  1.00 53.52           C  
ANISOU 1471  CB  LEU A 312     5917   6895   7524     85    460   -150       C  
ATOM   1472  CG  LEU A 312     -28.829 -38.263  12.010  1.00 59.89           C  
ANISOU 1472  CG  LEU A 312     6759   7856   8140    -52    679     -8       C  
ATOM   1473  CD1 LEU A 312     -29.583 -37.690  13.153  1.00 64.04           C  
ANISOU 1473  CD1 LEU A 312     7121   8557   8655   -113    885   -135       C  
ATOM   1474  CD2 LEU A 312     -28.875 -39.790  11.947  1.00 60.87           C  
ANISOU 1474  CD2 LEU A 312     6904   7913   8311   -172    700    165       C  
ATOM   1475  N   TRP A 313     -28.783 -36.082   7.784  1.00 47.93           N  
ANISOU 1475  N   TRP A 313     5452   5855   6904    373    -77   -275       N  
ATOM   1476  CA  TRP A 313     -28.976 -35.941   6.333  1.00 47.99           C  
ANISOU 1476  CA  TRP A 313     5550   5693   6992    452   -327   -308       C  
ATOM   1477  C   TRP A 313     -27.608 -36.011   5.662  1.00 50.20           C  
ANISOU 1477  C   TRP A 313     6087   5936   7050    455   -381   -187       C  
ATOM   1478  O   TRP A 313     -27.436 -36.764   4.712  1.00 50.25           O  
ANISOU 1478  O   TRP A 313     6183   5857   7052    444   -482   -143       O  
ATOM   1479  CB  TRP A 313     -29.661 -34.598   6.003  1.00 46.66           C  
ANISOU 1479  CB  TRP A 313     5329   5450   6949    565   -485   -464       C  
ATOM   1480  CG  TRP A 313     -29.679 -34.269   4.534  1.00 46.49           C  
ANISOU 1480  CG  TRP A 313     5471   5254   6941    642   -766   -466       C  
ATOM   1481  CD1 TRP A 313     -28.679 -33.696   3.812  1.00 47.41           C  
ANISOU 1481  CD1 TRP A 313     5844   5311   6859    666   -865   -384       C  
ATOM   1482  CD2 TRP A 313     -30.754 -34.505   3.615  1.00 47.68           C  
ANISOU 1482  CD2 TRP A 313     5548   5270   7300    692   -985   -555       C  
ATOM   1483  NE1 TRP A 313     -29.053 -33.566   2.503  1.00 47.13           N  
ANISOU 1483  NE1 TRP A 313     5925   5121   6860    716  -1125   -400       N  
ATOM   1484  CE2 TRP A 313     -30.335 -34.029   2.356  1.00 50.64           C  
ANISOU 1484  CE2 TRP A 313     6170   5512   7558    746  -1224   -510       C  
ATOM   1485  CE3 TRP A 313     -32.050 -35.042   3.743  1.00 50.46           C  
ANISOU 1485  CE3 TRP A 313     5642   5600   7931    690  -1006   -679       C  
ATOM   1486  CZ2 TRP A 313     -31.172 -34.033   1.240  1.00 51.42           C  
ANISOU 1486  CZ2 TRP A 313     6289   5457   7792    811  -1509   -578       C  
ATOM   1487  CZ3 TRP A 313     -32.874 -35.078   2.622  1.00 52.73           C  
ANISOU 1487  CZ3 TRP A 313     5918   5727   8389    762  -1290   -764       C  
ATOM   1488  CH2 TRP A 313     -32.431 -34.577   1.391  1.00 53.19           C  
ANISOU 1488  CH2 TRP A 313     6247   5655   8307    827  -1550   -709       C  
ATOM   1489  N   SER A 314     -26.651 -35.221   6.172  1.00 47.08           N  
ANISOU 1489  N   SER A 314     5793   5610   6485    467   -305   -156       N  
ATOM   1490  CA  SER A 314     -25.257 -35.147   5.743  1.00 45.82           C  
ANISOU 1490  CA  SER A 314     5845   5441   6124    457   -310    -67       C  
ATOM   1491  C   SER A 314     -24.606 -36.509   5.717  1.00 47.89           C  
ANISOU 1491  C   SER A 314     6144   5721   6332    387   -242     36       C  
ATOM   1492  O   SER A 314     -23.934 -36.803   4.743  1.00 47.81           O  
ANISOU 1492  O   SER A 314     6274   5642   6249    384   -318     61       O  
ATOM   1493  CB  SER A 314     -24.469 -34.190   6.638  1.00 47.67           C  
ANISOU 1493  CB  SER A 314     6111   5767   6232    468   -205    -72       C  
ATOM   1494  OG  SER A 314     -24.846 -32.853   6.340  1.00 55.25           O  
ANISOU 1494  OG  SER A 314     7088   6660   7245    542   -318   -166       O  
ATOM   1495  N   LEU A 315     -24.850 -37.337   6.743  1.00 44.56           N  
ANISOU 1495  N   LEU A 315     5599   5379   5951    325   -108     88       N  
ATOM   1496  CA  LEU A 315     -24.382 -38.718   6.840  1.00 45.13           C  
ANISOU 1496  CA  LEU A 315     5686   5441   6020    258    -66    193       C  
ATOM   1497  C   LEU A 315     -24.864 -39.550   5.643  1.00 45.97           C  
ANISOU 1497  C   LEU A 315     5792   5418   6255    259   -199    168       C  
ATOM   1498  O   LEU A 315     -24.089 -40.344   5.109  1.00 43.52           O  
ANISOU 1498  O   LEU A 315     5568   5055   5912    243   -233    207       O  
ATOM   1499  CB  LEU A 315     -24.934 -39.377   8.122  1.00 47.04           C  
ANISOU 1499  CB  LEU A 315     5795   5771   6308    173     81    260       C  
ATOM   1500  CG  LEU A 315     -24.016 -39.725   9.257  1.00 52.22           C  
ANISOU 1500  CG  LEU A 315     6505   6523   6815    120    197    378       C  
ATOM   1501  CD1 LEU A 315     -24.611 -40.778  10.097  1.00 52.97           C  
ANISOU 1501  CD1 LEU A 315     6513   6647   6967      8    296    481       C  
ATOM   1502  CD2 LEU A 315     -22.628 -40.121   8.792  1.00 54.21           C  
ANISOU 1502  CD2 LEU A 315     6899   6716   6981    145    128    432       C  
ATOM   1503  N   GLY A 316     -26.146 -39.398   5.272  1.00 45.59           N  
ANISOU 1503  N   GLY A 316     5631   5319   6372    279   -278     83       N  
ATOM   1504  CA  GLY A 316     -26.762 -40.103   4.132  1.00 45.76           C  
ANISOU 1504  CA  GLY A 316     5639   5218   6532    289   -432     33       C  
ATOM   1505  C   GLY A 316     -26.155 -39.689   2.810  1.00 49.38           C  
ANISOU 1505  C   GLY A 316     6291   5603   6868    344   -586     -7       C  
ATOM   1506  O   GLY A 316     -25.902 -40.538   1.946  1.00 49.28           O  
ANISOU 1506  O   GLY A 316     6343   5523   6860    330   -663    -16       O  
ATOM   1507  N   VAL A 317     -25.857 -38.372   2.677  1.00 45.53           N  
ANISOU 1507  N   VAL A 317     5907   5133   6258    396   -620    -31       N  
ATOM   1508  CA  VAL A 317     -25.179 -37.806   1.500  1.00 44.88           C  
ANISOU 1508  CA  VAL A 317     6046   4995   6012    419   -738    -44       C  
ATOM   1509  C   VAL A 317     -23.766 -38.392   1.381  1.00 47.19           C  
ANISOU 1509  C   VAL A 317     6452   5329   6148    366   -630      7       C  
ATOM   1510  O   VAL A 317     -23.371 -38.818   0.294  1.00 45.85           O  
ANISOU 1510  O   VAL A 317     6405   5113   5904    348   -701    -24       O  
ATOM   1511  CB  VAL A 317     -25.176 -36.251   1.481  1.00 47.06           C  
ANISOU 1511  CB  VAL A 317     6408   5259   6213    470   -797    -63       C  
ATOM   1512  CG1 VAL A 317     -24.382 -35.719   0.284  1.00 46.17           C  
ANISOU 1512  CG1 VAL A 317     6554   5090   5899    455   -892    -45       C  
ATOM   1513  CG2 VAL A 317     -26.611 -35.702   1.445  1.00 47.53           C  
ANISOU 1513  CG2 VAL A 317     6340   5248   6470    540   -947   -149       C  
ATOM   1514  N   LEU A 318     -23.038 -38.447   2.511  1.00 45.38           N  
ANISOU 1514  N   LEU A 318     6172   5190   5881    342   -467     67       N  
ATOM   1515  CA  LEU A 318     -21.699 -39.014   2.583  1.00 46.71           C  
ANISOU 1515  CA  LEU A 318     6406   5391   5952    304   -375     98       C  
ATOM   1516  C   LEU A 318     -21.686 -40.505   2.317  1.00 47.65           C  
ANISOU 1516  C   LEU A 318     6468   5459   6179    275   -393     99       C  
ATOM   1517  O   LEU A 318     -20.907 -40.947   1.483  1.00 47.73           O  
ANISOU 1517  O   LEU A 318     6564   5439   6132    261   -411     48       O  
ATOM   1518  CB  LEU A 318     -21.027 -38.653   3.898  1.00 48.49           C  
ANISOU 1518  CB  LEU A 318     6588   5713   6123    298   -239    156       C  
ATOM   1519  CG  LEU A 318     -20.199 -37.376   3.779  1.00 58.57           C  
ANISOU 1519  CG  LEU A 318     7984   7021   7251    310   -213    129       C  
ATOM   1520  CD1 LEU A 318     -20.998 -36.175   4.187  1.00 61.90           C  
ANISOU 1520  CD1 LEU A 318     8373   7456   7689    351   -238    110       C  
ATOM   1521  CD2 LEU A 318     -19.039 -37.442   4.653  1.00 66.98           C  
ANISOU 1521  CD2 LEU A 318     9039   8158   8251    295   -103    158       C  
ATOM   1522  N   CYS A 319     -22.596 -41.266   2.930  1.00 44.20           N  
ANISOU 1522  N   CYS A 319     5884   5003   5908    259   -389    141       N  
ATOM   1523  CA  CYS A 319     -22.688 -42.706   2.679  1.00 44.65           C  
ANISOU 1523  CA  CYS A 319     5878   4980   6105    227   -426    145       C  
ATOM   1524  C   CYS A 319     -22.921 -42.994   1.203  1.00 47.22           C  
ANISOU 1524  C   CYS A 319     6272   5223   6447    245   -565     32       C  
ATOM   1525  O   CYS A 319     -22.298 -43.891   0.643  1.00 45.38           O  
ANISOU 1525  O   CYS A 319     6067   4941   6236    232   -588    -15       O  
ATOM   1526  CB  CYS A 319     -23.749 -43.358   3.555  1.00 45.82           C  
ANISOU 1526  CB  CYS A 319     5862   5114   6431    183   -392    215       C  
ATOM   1527  SG  CYS A 319     -23.729 -45.160   3.485  1.00 50.81           S  
ANISOU 1527  SG  CYS A 319     6422   5625   7260    127   -431    255       S  
ATOM   1528  N   TYR A 320     -23.777 -42.184   0.548  1.00 44.71           N  
ANISOU 1528  N   TYR A 320     5991   4887   6110    280   -671    -25       N  
ATOM   1529  CA  TYR A 320     -24.032 -42.326  -0.894  1.00 43.80           C  
ANISOU 1529  CA  TYR A 320     5977   4701   5963    296   -830   -130       C  
ATOM   1530  C   TYR A 320     -22.735 -42.000  -1.683  1.00 47.82           C  
ANISOU 1530  C   TYR A 320     6683   5248   6238    277   -794   -171       C  
ATOM   1531  O   TYR A 320     -22.341 -42.786  -2.545  1.00 45.55           O  
ANISOU 1531  O   TYR A 320     6446   4930   5930    257   -830   -259       O  
ATOM   1532  CB  TYR A 320     -25.142 -41.360  -1.339  1.00 43.07           C  
ANISOU 1532  CB  TYR A 320     5906   4574   5886    345   -980   -167       C  
ATOM   1533  CG  TYR A 320     -25.545 -41.517  -2.790  1.00 44.77           C  
ANISOU 1533  CG  TYR A 320     6240   4712   6060    363  -1182   -266       C  
ATOM   1534  CD1 TYR A 320     -24.774 -40.965  -3.817  1.00 46.52           C  
ANISOU 1534  CD1 TYR A 320     6704   4949   6021    346  -1225   -292       C  
ATOM   1535  CD2 TYR A 320     -26.700 -42.212  -3.142  1.00 45.57           C  
ANISOU 1535  CD2 TYR A 320     6215   4728   6371    384  -1330   -339       C  
ATOM   1536  CE1 TYR A 320     -25.163 -41.073  -5.154  1.00 48.79           C  
ANISOU 1536  CE1 TYR A 320     7133   5178   6225    352  -1420   -378       C  
ATOM   1537  CE2 TYR A 320     -27.095 -42.330  -4.475  1.00 46.96           C  
ANISOU 1537  CE2 TYR A 320     6512   4836   6496    406  -1544   -441       C  
ATOM   1538  CZ  TYR A 320     -26.325 -41.755  -5.477  1.00 52.76           C  
ANISOU 1538  CZ  TYR A 320     7514   5597   6935    391  -1592   -455       C  
ATOM   1539  OH  TYR A 320     -26.680 -41.887  -6.797  1.00 53.72           O  
ANISOU 1539  OH  TYR A 320     7786   5666   6959    399  -1803   -551       O  
ATOM   1540  N   GLU A 321     -22.119 -40.819  -1.419  1.00 43.03           N  
ANISOU 1540  N   GLU A 321     6179   4706   5465    276   -720   -126       N  
ATOM   1541  CA  GLU A 321     -20.925 -40.416  -2.142  1.00 43.31           C  
ANISOU 1541  CA  GLU A 321     6392   4780   5285    234   -661   -167       C  
ATOM   1542  C   GLU A 321     -19.760 -41.373  -1.961  1.00 47.34           C  
ANISOU 1542  C   GLU A 321     6851   5319   5816    202   -537   -212       C  
ATOM   1543  O   GLU A 321     -18.987 -41.566  -2.889  1.00 48.50           O  
ANISOU 1543  O   GLU A 321     7103   5481   5845    159   -509   -312       O  
ATOM   1544  CB  GLU A 321     -20.516 -38.996  -1.762  1.00 43.24           C  
ANISOU 1544  CB  GLU A 321     6475   4816   5138    230   -603   -106       C  
ATOM   1545  CG  GLU A 321     -19.306 -38.511  -2.531  1.00 46.59           C  
ANISOU 1545  CG  GLU A 321     7083   5277   5342    160   -523   -147       C  
ATOM   1546  CD  GLU A 321     -18.948 -37.074  -2.257  1.00 51.84           C  
ANISOU 1546  CD  GLU A 321     7849   5959   5887    145   -482    -85       C  
ATOM   1547  OE1 GLU A 321     -19.500 -36.497  -1.292  1.00 52.40           O  
ANISOU 1547  OE1 GLU A 321     7824   6028   6059    202   -499    -25       O  
ATOM   1548  OE2 GLU A 321     -18.130 -36.522  -3.025  1.00 49.66           O  
ANISOU 1548  OE2 GLU A 321     7750   5698   5420     65   -429   -106       O  
ATOM   1549  N   PHE A 322     -19.606 -41.932  -0.765  1.00 44.55           N  
ANISOU 1549  N   PHE A 322     6342   4974   5609    218   -466   -146       N  
ATOM   1550  CA  PHE A 322     -18.527 -42.889  -0.497  1.00 44.23           C  
ANISOU 1550  CA  PHE A 322     6238   4930   5635    205   -391   -185       C  
ATOM   1551  C   PHE A 322     -18.642 -44.108  -1.408  1.00 50.88           C  
ANISOU 1551  C   PHE A 322     7054   5696   6581    198   -469   -301       C  
ATOM   1552  O   PHE A 322     -17.650 -44.492  -2.003  1.00 52.28           O  
ANISOU 1552  O   PHE A 322     7261   5882   6720    179   -422   -425       O  
ATOM   1553  CB  PHE A 322     -18.498 -43.302   0.982  1.00 44.65           C  
ANISOU 1553  CB  PHE A 322     6156   4987   5821    220   -345    -62       C  
ATOM   1554  CG  PHE A 322     -18.004 -42.254   1.960  1.00 43.95           C  
ANISOU 1554  CG  PHE A 322     6086   4988   5624    226   -252     13       C  
ATOM   1555  CD1 PHE A 322     -17.350 -41.105   1.510  1.00 44.84           C  
ANISOU 1555  CD1 PHE A 322     6317   5157   5565    215   -199    -38       C  
ATOM   1556  CD2 PHE A 322     -18.183 -42.421   3.332  1.00 44.02           C  
ANISOU 1556  CD2 PHE A 322     6004   5024   5696    232   -217    133       C  
ATOM   1557  CE1 PHE A 322     -16.896 -40.142   2.423  1.00 45.09           C  
ANISOU 1557  CE1 PHE A 322     6352   5260   5520    223   -124     14       C  
ATOM   1558  CE2 PHE A 322     -17.732 -41.459   4.235  1.00 45.59           C  
ANISOU 1558  CE2 PHE A 322     6221   5314   5788    241   -141    180       C  
ATOM   1559  CZ  PHE A 322     -17.066 -40.344   3.776  1.00 43.70           C  
ANISOU 1559  CZ  PHE A 322     6076   5117   5409    243   -100    111       C  
ATOM   1560  N   LEU A 323     -19.863 -44.643  -1.584  1.00 46.63           N  
ANISOU 1560  N   LEU A 323     6453   5086   6177    213   -585   -287       N  
ATOM   1561  CA  LEU A 323     -20.144 -45.827  -2.401  1.00 47.67           C  
ANISOU 1561  CA  LEU A 323     6542   5130   6441    212   -683   -404       C  
ATOM   1562  C   LEU A 323     -20.221 -45.573  -3.902  1.00 50.14           C  
ANISOU 1562  C   LEU A 323     7005   5457   6587    198   -757   -552       C  
ATOM   1563  O   LEU A 323     -19.795 -46.414  -4.697  1.00 48.62           O  
ANISOU 1563  O   LEU A 323     6816   5237   6419    186   -778   -706       O  
ATOM   1564  CB  LEU A 323     -21.450 -46.503  -1.924  1.00 48.21           C  
ANISOU 1564  CB  LEU A 323     6466   5107   6742    220   -775   -331       C  
ATOM   1565  CG  LEU A 323     -21.476 -47.072  -0.510  1.00 52.00           C  
ANISOU 1565  CG  LEU A 323     6808   5557   7393    203   -709   -181       C  
ATOM   1566  CD1 LEU A 323     -22.889 -47.329  -0.063  1.00 53.75           C  
ANISOU 1566  CD1 LEU A 323     6909   5727   7788    183   -758   -105       C  
ATOM   1567  CD2 LEU A 323     -20.646 -48.326  -0.405  1.00 50.01           C  
ANISOU 1567  CD2 LEU A 323     6494   5217   7291    198   -717   -216       C  
ATOM   1568  N   VAL A 324     -20.787 -44.423  -4.292  1.00 47.31           N  
ANISOU 1568  N   VAL A 324     6778   5137   6060    199   -810   -511       N  
ATOM   1569  CA  VAL A 324     -21.007 -44.086  -5.696  1.00 47.39           C  
ANISOU 1569  CA  VAL A 324     6973   5155   5879    177   -916   -617       C  
ATOM   1570  C   VAL A 324     -19.848 -43.245  -6.310  1.00 52.08           C  
ANISOU 1570  C   VAL A 324     7769   5845   6173    109   -795   -656       C  
ATOM   1571  O   VAL A 324     -19.555 -43.402  -7.496  1.00 51.90           O  
ANISOU 1571  O   VAL A 324     7892   5851   5977     58   -816   -786       O  
ATOM   1572  CB  VAL A 324     -22.391 -43.414  -5.838  1.00 50.32           C  
ANISOU 1572  CB  VAL A 324     7371   5476   6272    219  -1096   -553       C  
ATOM   1573  CG1 VAL A 324     -22.695 -43.006  -7.288  1.00 50.79           C  
ANISOU 1573  CG1 VAL A 324     7656   5529   6112    201  -1256   -638       C  
ATOM   1574  CG2 VAL A 324     -23.477 -44.331  -5.291  1.00 50.01           C  
ANISOU 1574  CG2 VAL A 324     7109   5347   6544    261  -1183   -546       C  
ATOM   1575  N   GLY A 325     -19.241 -42.372  -5.520  1.00 48.26           N  
ANISOU 1575  N   GLY A 325     7295   5413   5629     98   -669   -553       N  
ATOM   1576  CA  GLY A 325     -18.135 -41.533  -5.974  1.00 49.20           C  
ANISOU 1576  CA  GLY A 325     7582   5614   5498     18   -534   -579       C  
ATOM   1577  C   GLY A 325     -18.554 -40.115  -6.292  1.00 53.77           C  
ANISOU 1577  C   GLY A 325     8358   6190   5882     -6   -604   -472       C  
ATOM   1578  O   GLY A 325     -17.722 -39.274  -6.642  1.00 54.98           O  
ANISOU 1578  O   GLY A 325     8670   6395   5823    -90   -497   -464       O  
ATOM   1579  N   LYS A 326     -19.847 -39.855  -6.188  1.00 49.51           N  
ANISOU 1579  N   LYS A 326     7802   5576   5433     64   -791   -397       N  
ATOM   1580  CA  LYS A 326     -20.447 -38.540  -6.403  1.00 51.11           C  
ANISOU 1580  CA  LYS A 326     8163   5736   5521     72   -918   -296       C  
ATOM   1581  C   LYS A 326     -21.657 -38.351  -5.445  1.00 53.89           C  
ANISOU 1581  C   LYS A 326     8330   6022   6123    180  -1034   -226       C  
ATOM   1582  O   LYS A 326     -22.334 -39.347  -5.163  1.00 53.29           O  
ANISOU 1582  O   LYS A 326     8074   5919   6255    227  -1083   -269       O  
ATOM   1583  CB  LYS A 326     -20.777 -38.255  -7.902  1.00 54.58           C  
ANISOU 1583  CB  LYS A 326     8873   6143   5722     19  -1085   -330       C  
ATOM   1584  CG  LYS A 326     -21.947 -39.004  -8.491  1.00 72.36           C  
ANISOU 1584  CG  LYS A 326    11087   8324   8080     83  -1313   -399       C  
ATOM   1585  CD  LYS A 326     -22.102 -38.681  -9.959  1.00 87.49           C  
ANISOU 1585  CD  LYS A 326    13307  10227   9707     18  -1471   -432       C  
ATOM   1586  CE  LYS A 326     -23.011 -39.655 -10.646  1.00 98.83           C  
ANISOU 1586  CE  LYS A 326    14697  11613  11240     71  -1677   -549       C  
ATOM   1587  NZ  LYS A 326     -23.159 -39.326 -12.090  1.00110.97           N  
ANISOU 1587  NZ  LYS A 326    16559  13145  12459      7  -1858   -580       N  
ATOM   1588  N   PRO A 327     -21.895 -37.120  -4.893  1.00 48.85           N  
ANISOU 1588  N   PRO A 327     7717   5360   5483    209  -1061   -135       N  
ATOM   1589  CA  PRO A 327     -23.049 -36.919  -3.989  1.00 46.02           C  
ANISOU 1589  CA  PRO A 327     7162   4955   5367    305  -1148   -109       C  
ATOM   1590  C   PRO A 327     -24.388 -37.098  -4.714  1.00 49.58           C  
ANISOU 1590  C   PRO A 327     7608   5305   5923    364  -1407   -159       C  
ATOM   1591  O   PRO A 327     -24.447 -36.915  -5.928  1.00 48.03           O  
ANISOU 1591  O   PRO A 327     7630   5061   5558    339  -1563   -176       O  
ATOM   1592  CB  PRO A 327     -22.822 -35.500  -3.433  1.00 46.58           C  
ANISOU 1592  CB  PRO A 327     7290   5022   5387    316  -1121    -37       C  
ATOM   1593  CG  PRO A 327     -22.002 -34.816  -4.418  1.00 53.52           C  
ANISOU 1593  CG  PRO A 327     8449   5888   5999    233  -1129     -5       C  
ATOM   1594  CD  PRO A 327     -21.149 -35.851  -5.097  1.00 50.54           C  
ANISOU 1594  CD  PRO A 327     8130   5580   5490    150  -1011    -69       C  
ATOM   1595  N   PRO A 328     -25.467 -37.517  -4.014  1.00 47.40           N  
ANISOU 1595  N   PRO A 328     7086   5000   5923    432  -1455   -191       N  
ATOM   1596  CA  PRO A 328     -26.717 -37.864  -4.727  1.00 47.23           C  
ANISOU 1596  CA  PRO A 328     7023   4879   6044    486  -1704   -270       C  
ATOM   1597  C   PRO A 328     -27.471 -36.747  -5.425  1.00 52.19           C  
ANISOU 1597  C   PRO A 328     7791   5394   6644    548  -1980   -273       C  
ATOM   1598  O   PRO A 328     -28.307 -37.047  -6.282  1.00 50.49           O  
ANISOU 1598  O   PRO A 328     7605   5092   6487    587  -2223   -344       O  
ATOM   1599  CB  PRO A 328     -27.583 -38.498  -3.634  1.00 48.69           C  
ANISOU 1599  CB  PRO A 328     6885   5070   6543    520  -1634   -304       C  
ATOM   1600  CG  PRO A 328     -27.036 -37.984  -2.336  1.00 50.94           C  
ANISOU 1600  CG  PRO A 328     7083   5447   6824    506  -1408   -230       C  
ATOM   1601  CD  PRO A 328     -25.562 -37.827  -2.564  1.00 46.42           C  
ANISOU 1601  CD  PRO A 328     6711   4941   5986    443  -1273   -167       C  
ATOM   1602  N   PHE A 329     -27.177 -35.473  -5.092  1.00 49.78           N  
ANISOU 1602  N   PHE A 329     7578   5075   6261    561  -1971   -201       N  
ATOM   1603  CA  PHE A 329     -27.897 -34.326  -5.648  1.00 50.68           C  
ANISOU 1603  CA  PHE A 329     7821   5050   6386    629  -2260   -193       C  
ATOM   1604  C   PHE A 329     -27.017 -33.423  -6.502  1.00 58.67           C  
ANISOU 1604  C   PHE A 329     9195   6029   7069    556  -2312    -85       C  
ATOM   1605  O   PHE A 329     -27.474 -32.366  -6.964  1.00 61.59           O  
ANISOU 1605  O   PHE A 329     9719   6262   7422    600  -2563    -43       O  
ATOM   1606  CB  PHE A 329     -28.604 -33.551  -4.521  1.00 51.46           C  
ANISOU 1606  CB  PHE A 329     7684   5117   6752    720  -2259   -229       C  
ATOM   1607  CG  PHE A 329     -29.404 -34.429  -3.578  1.00 50.26           C  
ANISOU 1607  CG  PHE A 329     7175   5023   6899    754  -2145   -329       C  
ATOM   1608  CD1 PHE A 329     -30.590 -35.011  -3.986  1.00 53.68           C  
ANISOU 1608  CD1 PHE A 329     7464   5376   7556    810  -2342   -438       C  
ATOM   1609  CD2 PHE A 329     -28.990 -34.629  -2.270  1.00 50.18           C  
ANISOU 1609  CD2 PHE A 329     6980   5142   6943    720  -1848   -313       C  
ATOM   1610  CE1 PHE A 329     -31.342 -35.799  -3.113  1.00 55.15           C  
ANISOU 1610  CE1 PHE A 329     7319   5611   8025    815  -2217   -527       C  
ATOM   1611  CE2 PHE A 329     -29.713 -35.457  -1.406  1.00 53.26           C  
ANISOU 1611  CE2 PHE A 329     7071   5589   7576    719  -1727   -383       C  
ATOM   1612  CZ  PHE A 329     -30.902 -36.018  -1.826  1.00 53.67           C  
ANISOU 1612  CZ  PHE A 329     6973   5559   7862    760  -1901   -490       C  
ATOM   1613  N   GLU A 330     -25.800 -33.914  -6.815  1.00 55.31           N  
ANISOU 1613  N   GLU A 330     8909   5715   6391    438  -2096    -49       N  
ATOM   1614  CA  GLU A 330     -24.836 -33.234  -7.682  1.00 56.85           C  
ANISOU 1614  CA  GLU A 330     9448   5909   6245    324  -2081     42       C  
ATOM   1615  C   GLU A 330     -25.460 -32.787  -8.994  1.00 64.38           C  
ANISOU 1615  C   GLU A 330    10686   6733   7044    323  -2416     74       C  
ATOM   1616  O   GLU A 330     -26.363 -33.454  -9.536  1.00 64.49           O  
ANISOU 1616  O   GLU A 330    10658   6701   7146    385  -2625     -8       O  
ATOM   1617  CB  GLU A 330     -23.626 -34.114  -7.967  1.00 57.60           C  
ANISOU 1617  CB  GLU A 330     9598   6148   6139    202  -1815     10       C  
ATOM   1618  CG  GLU A 330     -22.336 -33.323  -7.995  1.00 72.04           C  
ANISOU 1618  CG  GLU A 330    11610   8027   7734     80  -1618     91       C  
ATOM   1619  CD  GLU A 330     -21.105 -34.085  -8.426  1.00 92.07           C  
ANISOU 1619  CD  GLU A 330    14211  10700  10070    -49  -1366     28       C  
ATOM   1620  OE1 GLU A 330     -21.155 -34.752  -9.482  1.00 89.69           O  
ANISOU 1620  OE1 GLU A 330    14044  10423   9612   -101  -1428    -40       O  
ATOM   1621  OE2 GLU A 330     -20.071 -33.975  -7.730  1.00 97.24           O  
ANISOU 1621  OE2 GLU A 330    14782  11436  10728    -98  -1114     30       O  
ATOM   1622  N   ALA A 331     -24.988 -31.629  -9.483  1.00 62.37           N  
ANISOU 1622  N   ALA A 331    10728   6406   6563    249  -2483    201       N  
ATOM   1623  CA  ALA A 331     -25.489 -30.983 -10.694  1.00 64.85           C  
ANISOU 1623  CA  ALA A 331    11377   6574   6687    231  -2824    279       C  
ATOM   1624  C   ALA A 331     -24.447 -30.035 -11.226  1.00 67.19           C  
ANISOU 1624  C   ALA A 331    12024   6859   6645     67  -2740    432       C  
ATOM   1625  O   ALA A 331     -23.442 -29.805 -10.567  1.00 64.23           O  
ANISOU 1625  O   ALA A 331    11587   6575   6243     -9  -2434    456       O  
ATOM   1626  CB  ALA A 331     -26.736 -30.224 -10.358  1.00 66.61           C  
ANISOU 1626  CB  ALA A 331    11489   6609   7209    396  -3153    278       C  
ATOM   1627  N   ASN A 332     -24.658 -29.497 -12.425  1.00 65.45           N  
ANISOU 1627  N   ASN A 332    12183   6526   6158     -2  -3008    536       N  
ATOM   1628  CA  ASN A 332     -23.670 -28.579 -12.968  1.00 66.12           C  
ANISOU 1628  CA  ASN A 332    12626   6594   5903   -192  -2913    700       C  
ATOM   1629  C   ASN A 332     -23.928 -27.149 -12.479  1.00 65.93           C  
ANISOU 1629  C   ASN A 332    12651   6364   6034   -137  -3089    835       C  
ATOM   1630  O   ASN A 332     -23.124 -26.283 -12.791  1.00 66.41           O  
ANISOU 1630  O   ASN A 332    12987   6381   5863   -296  -3011    984       O  
ATOM   1631  CB  ASN A 332     -23.547 -28.685 -14.542  1.00 70.11           C  
ANISOU 1631  CB  ASN A 332    13578   7103   5956   -351  -3058    770       C  
ATOM   1632  CG  ASN A 332     -22.526 -29.722 -15.021  1.00 90.12           C  
ANISOU 1632  CG  ASN A 332    16147   9880   8214   -514  -2705    658       C  
ATOM   1633  OD1 ASN A 332     -21.394 -29.803 -14.520  1.00 89.72           O  
ANISOU 1633  OD1 ASN A 332    15994   9965   8131   -619  -2319    628       O  
ATOM   1634  ND2 ASN A 332     -22.893 -30.566 -15.980  1.00 76.93           N  
ANISOU 1634  ND2 ASN A 332    14598   8268   6362   -530  -2833    566       N  
ATOM   1635  N   THR A 333     -25.069 -26.892 -11.775  1.00 60.07           N  
ANISOU 1635  N   THR A 333    11648   5487   5688     78  -3335    771       N  
ATOM   1636  CA  THR A 333     -25.460 -25.566 -11.254  1.00 61.30           C  
ANISOU 1636  CA  THR A 333    11796   5430   6064    166  -3538    850       C  
ATOM   1637  C   THR A 333     -26.025 -25.668  -9.886  1.00 62.18           C  
ANISOU 1637  C   THR A 333    11446   5564   6616    349  -3464    693       C  
ATOM   1638  O   THR A 333     -26.581 -26.698  -9.536  1.00 61.99           O  
ANISOU 1638  O   THR A 333    11139   5648   6767    442  -3412    541       O  
ATOM   1639  CB  THR A 333     -26.468 -24.738 -12.142  1.00 72.97           C  
ANISOU 1639  CB  THR A 333    13550   6628   7547    237  -4073    954       C  
ATOM   1640  OG1 THR A 333     -27.831 -25.043 -11.812  1.00 73.20           O  
ANISOU 1640  OG1 THR A 333    13282   6570   7961    465  -4354    794       O  
ATOM   1641  CG2 THR A 333     -26.219 -24.859 -13.614  1.00 75.24           C  
ANISOU 1641  CG2 THR A 333    14306   6901   7381     74  -4221   1091       C  
ATOM   1642  N   TYR A 334     -25.939 -24.564  -9.137  1.00 58.06           N  
ANISOU 1642  N   TYR A 334    10857   4928   6274    394  -3476    725       N  
ATOM   1643  CA  TYR A 334     -26.441 -24.387  -7.773  1.00 56.82           C  
ANISOU 1643  CA  TYR A 334    10287   4783   6520    555  -3404    573       C  
ATOM   1644  C   TYR A 334     -27.974 -24.470  -7.797  1.00 61.96           C  
ANISOU 1644  C   TYR A 334    10746   5298   7499    752  -3760    444       C  
ATOM   1645  O   TYR A 334     -28.580 -25.051  -6.888  1.00 58.65           O  
ANISOU 1645  O   TYR A 334     9938   4977   7368    866  -3651    266       O  
ATOM   1646  CB  TYR A 334     -26.028 -22.973  -7.305  1.00 58.13           C  
ANISOU 1646  CB  TYR A 334    10524   4801   6761    545  -3430    649       C  
ATOM   1647  CG  TYR A 334     -26.501 -22.543  -5.935  1.00 58.94           C  
ANISOU 1647  CG  TYR A 334    10242   4899   7255    703  -3376    484       C  
ATOM   1648  CD1 TYR A 334     -27.764 -21.963  -5.759  1.00 62.77           C  
ANISOU 1648  CD1 TYR A 334    10571   5187   8090    889  -3720    375       C  
ATOM   1649  CD2 TYR A 334     -25.623 -22.525  -4.850  1.00 56.59           C  
ANISOU 1649  CD2 TYR A 334     9763   4768   6969    658  -3006    436       C  
ATOM   1650  CE1 TYR A 334     -28.180 -21.499  -4.510  1.00 62.51           C  
ANISOU 1650  CE1 TYR A 334    10184   5159   8407   1022  -3654    196       C  
ATOM   1651  CE2 TYR A 334     -26.023 -22.050  -3.602  1.00 56.54           C  
ANISOU 1651  CE2 TYR A 334     9433   4766   7283    788  -2956    279       C  
ATOM   1652  CZ  TYR A 334     -27.308 -21.547  -3.436  1.00 67.61           C  
ANISOU 1652  CZ  TYR A 334    10668   5997   9024    966  -3265    152       C  
ATOM   1653  OH  TYR A 334     -27.724 -21.068  -2.218  1.00 70.82           O  
ANISOU 1653  OH  TYR A 334    10744   6421   9743   1088  -3201    -36       O  
ATOM   1654  N   GLN A 335     -28.579 -23.778  -8.786  1.00 62.12           N  
ANISOU 1654  N   GLN A 335    11040   5074   7488    787  -4194    535       N  
ATOM   1655  CA  GLN A 335     -30.025 -23.683  -9.003  1.00 64.84           C  
ANISOU 1655  CA  GLN A 335    11251   5235   8149    977  -4617    418       C  
ATOM   1656  C   GLN A 335     -30.664 -25.082  -9.154  1.00 68.67           C  
ANISOU 1656  C   GLN A 335    11526   5866   8700   1024  -4584    270       C  
ATOM   1657  O   GLN A 335     -31.619 -25.410  -8.453  1.00 69.40           O  
ANISOU 1657  O   GLN A 335    11230   5967   9173   1171  -4616     71       O  
ATOM   1658  CB  GLN A 335     -30.305 -22.796 -10.208  1.00 69.50           C  
ANISOU 1658  CB  GLN A 335    12266   5547   8593    966  -5087    589       C  
ATOM   1659  CG  GLN A 335     -30.063 -21.308  -9.903  1.00 75.99           C  
ANISOU 1659  CG  GLN A 335    13203   6146   9521    979  -5218    691       C  
ATOM   1660  CD  GLN A 335     -28.658 -20.787 -10.146  1.00 84.32           C  
ANISOU 1660  CD  GLN A 335    14605   7240  10194    751  -4973    916       C  
ATOM   1661  OE1 GLN A 335     -27.699 -21.489 -10.491  1.00 74.60           O  
ANISOU 1661  OE1 GLN A 335    13523   6225   8597    566  -4646    993       O  
ATOM   1662  NE2 GLN A 335     -28.544 -19.483 -10.095  1.00 77.29           N  
ANISOU 1662  NE2 GLN A 335    13874   6104   9388    753  -5169   1029       N  
ATOM   1663  N   GLU A 336     -30.073 -25.907  -9.994  1.00 64.25           N  
ANISOU 1663  N   GLU A 336    11202   5435   7777    884  -4477    353       N  
ATOM   1664  CA  GLU A 336     -30.470 -27.281 -10.204  1.00 65.12           C  
ANISOU 1664  CA  GLU A 336    11149   5686   7907    898  -4414    226       C  
ATOM   1665  C   GLU A 336     -30.248 -28.159  -8.921  1.00 65.02           C  
ANISOU 1665  C   GLU A 336    10715   5896   8092    908  -3983     89       C  
ATOM   1666  O   GLU A 336     -31.196 -28.842  -8.513  1.00 63.49           O  
ANISOU 1666  O   GLU A 336    10196   5721   8205   1015  -4025    -78       O  
ATOM   1667  CB  GLU A 336     -29.731 -27.815 -11.423  1.00 67.78           C  
ANISOU 1667  CB  GLU A 336    11872   6105   7777    731  -4387    342       C  
ATOM   1668  CG  GLU A 336     -30.102 -29.230 -11.807  1.00 89.24           C  
ANISOU 1668  CG  GLU A 336    14466   8946  10493    740  -4362    207       C  
ATOM   1669  CD  GLU A 336     -28.915 -30.021 -12.297  1.00129.11           C  
ANISOU 1669  CD  GLU A 336    19702  14201  15152    554  -4040    251       C  
ATOM   1670  OE1 GLU A 336     -28.038 -29.418 -12.960  1.00131.53           O  
ANISOU 1670  OE1 GLU A 336    20385  14506  15085    404  -4000    409       O  
ATOM   1671  OE2 GLU A 336     -28.890 -31.257 -12.086  1.00130.93           O  
ANISOU 1671  OE2 GLU A 336    19712  14581  15454    553  -3845    121       O  
ATOM   1672  N   THR A 337     -29.052 -28.068  -8.242  1.00 58.65           N  
ANISOU 1672  N   THR A 337     9910   5240   7135    797  -3593    158       N  
ATOM   1673  CA  THR A 337     -28.784 -28.815  -6.993  1.00 54.77           C  
ANISOU 1673  CA  THR A 337     9063   4945   6802    800  -3214     56       C  
ATOM   1674  C   THR A 337     -29.854 -28.498  -5.955  1.00 56.61           C  
ANISOU 1674  C   THR A 337     8926   5124   7459    955  -3280    -94       C  
ATOM   1675  O   THR A 337     -30.311 -29.399  -5.252  1.00 54.33           O  
ANISOU 1675  O   THR A 337     8323   4950   7369    988  -3123   -218       O  
ATOM   1676  CB  THR A 337     -27.355 -28.544  -6.445  1.00 53.05           C  
ANISOU 1676  CB  THR A 337     8924   4857   6374    675  -2858    151       C  
ATOM   1677  OG1 THR A 337     -26.423 -28.919  -7.443  1.00 61.80           O  
ANISOU 1677  OG1 THR A 337    10340   6027   7115    524  -2780    251       O  
ATOM   1678  CG2 THR A 337     -27.039 -29.339  -5.188  1.00 44.13           C  
ANISOU 1678  CG2 THR A 337     7468   3922   5378    676  -2504     65       C  
ATOM   1679  N   TYR A 338     -30.248 -27.216  -5.863  1.00 55.87           N  
ANISOU 1679  N   TYR A 338     8870   4852   7508   1040  -3509    -91       N  
ATOM   1680  CA  TYR A 338     -31.263 -26.742  -4.921  1.00 56.47           C  
ANISOU 1680  CA  TYR A 338     8594   4863   7998   1191  -3586   -268       C  
ATOM   1681  C   TYR A 338     -32.579 -27.499  -5.184  1.00 61.37           C  
ANISOU 1681  C   TYR A 338     8988   5438   8891   1293  -3793   -429       C  
ATOM   1682  O   TYR A 338     -33.199 -27.963  -4.227  1.00 59.28           O  
ANISOU 1682  O   TYR A 338     8344   5272   8909   1343  -3629   -598       O  
ATOM   1683  CB  TYR A 338     -31.451 -25.217  -5.046  1.00 59.15           C  
ANISOU 1683  CB  TYR A 338     9065   4967   8443   1270  -3876   -237       C  
ATOM   1684  CG  TYR A 338     -32.363 -24.603  -4.010  1.00 63.88           C  
ANISOU 1684  CG  TYR A 338     9292   5506   9475   1424  -3926   -451       C  
ATOM   1685  CD1 TYR A 338     -33.750 -24.649  -4.155  1.00 67.65           C  
ANISOU 1685  CD1 TYR A 338     9539   5852  10315   1575  -4226   -637       C  
ATOM   1686  CD2 TYR A 338     -31.846 -23.858  -2.957  1.00 65.93           C  
ANISOU 1686  CD2 TYR A 338     9437   5819   9794   1423  -3707   -487       C  
ATOM   1687  CE1 TYR A 338     -34.595 -24.075  -3.210  1.00 70.99           C  
ANISOU 1687  CE1 TYR A 338     9592   6228  11154   1711  -4253   -873       C  
ATOM   1688  CE2 TYR A 338     -32.684 -23.230  -2.036  1.00 68.90           C  
ANISOU 1688  CE2 TYR A 338     9474   6143  10561   1562  -3753   -713       C  
ATOM   1689  CZ  TYR A 338     -34.056 -23.363  -2.151  1.00 79.69           C  
ANISOU 1689  CZ  TYR A 338    10588   7402  12289   1703  -4009   -913       C  
ATOM   1690  OH  TYR A 338     -34.879 -22.780  -1.222  1.00 86.34           O  
ANISOU 1690  OH  TYR A 338    11062   8211  13531   1832  -4022  -1175       O  
ATOM   1691  N   LYS A 339     -32.994 -27.598  -6.480  1.00 61.36           N  
ANISOU 1691  N   LYS A 339     9227   5290   8796   1311  -4153   -380       N  
ATOM   1692  CA  LYS A 339     -34.203 -28.305  -6.928  1.00 63.38           C  
ANISOU 1692  CA  LYS A 339     9308   5479   9294   1406  -4406   -533       C  
ATOM   1693  C   LYS A 339     -34.114 -29.771  -6.509  1.00 61.82           C  
ANISOU 1693  C   LYS A 339     8887   5500   9100   1330  -4075   -601       C  
ATOM   1694  O   LYS A 339     -35.010 -30.258  -5.811  1.00 61.34           O  
ANISOU 1694  O   LYS A 339     8443   5474   9387   1394  -4014   -783       O  
ATOM   1695  CB  LYS A 339     -34.409 -28.157  -8.455  1.00 68.78           C  
ANISOU 1695  CB  LYS A 339    10370   5987   9776   1413  -4841   -435       C  
ATOM   1696  CG  LYS A 339     -35.034 -26.827  -8.872  1.00 92.53           C  
ANISOU 1696  CG  LYS A 339    13511   8709  12938   1539  -5304   -421       C  
ATOM   1697  CD  LYS A 339     -35.381 -26.805 -10.353  1.00104.66           C  
ANISOU 1697  CD  LYS A 339    15415  10073  14278   1549  -5767   -330       C  
ATOM   1698  CE  LYS A 339     -36.719 -26.166 -10.581  1.00122.43           C  
ANISOU 1698  CE  LYS A 339    17531  12053  16935   1752  -6284   -476       C  
ATOM   1699  NZ  LYS A 339     -36.649 -24.689 -10.580  1.00135.74           N  
ANISOU 1699  NZ  LYS A 339    19398  13495  18681   1816  -6560   -377       N  
ATOM   1700  N  AARG A 340     -33.003 -30.448  -6.875  0.50 56.58           N  
ANISOU 1700  N  AARG A 340     8451   4980   8067   1185  -3844   -461       N  
ATOM   1701  N  BARG A 340     -32.998 -30.434  -6.869  0.50 57.07           N  
ANISOU 1701  N  BARG A 340     8514   5041   8128   1185  -3844   -460       N  
ATOM   1702  CA AARG A 340     -32.742 -31.856  -6.554  0.50 54.72           C  
ANISOU 1702  CA AARG A 340     8052   4929   7809   1104  -3545   -500       C  
ATOM   1703  CA BARG A 340     -32.703 -31.835  -6.567  0.50 55.45           C  
ANISOU 1703  CA BARG A 340     8157   5022   7888   1101  -3543   -494       C  
ATOM   1704  C  AARG A 340     -32.821 -32.150  -5.054  0.50 57.09           C  
ANISOU 1704  C  AARG A 340     7981   5368   8342   1102  -3202   -581       C  
ATOM   1705  C  BARG A 340     -32.757 -32.167  -5.067  0.50 57.36           C  
ANISOU 1705  C  BARG A 340     8028   5407   8358   1096  -3192   -573       C  
ATOM   1706  O  AARG A 340     -33.430 -33.147  -4.681  0.50 56.51           O  
ANISOU 1706  O  AARG A 340     7640   5355   8476   1100  -3109   -688       O  
ATOM   1707  O  BARG A 340     -33.284 -33.213  -4.707  0.50 56.73           O  
ANISOU 1707  O  BARG A 340     7694   5396   8465   1087  -3085   -671       O  
ATOM   1708  CB AARG A 340     -31.393 -32.325  -7.124  0.50 53.78           C  
ANISOU 1708  CB AARG A 340     8238   4928   7268    957  -3349   -353       C  
ATOM   1709  CB BARG A 340     -31.360 -32.242  -7.185  0.50 56.02           C  
ANISOU 1709  CB BARG A 340     8549   5204   7532    955  -3363   -343       C  
ATOM   1710  CG AARG A 340     -31.363 -32.495  -8.642  0.50 60.34           C  
ANISOU 1710  CG AARG A 340     9409   5680   7838    923  -3627   -306       C  
ATOM   1711  CG BARG A 340     -31.484 -33.318  -8.253  0.50 67.58           C  
ANISOU 1711  CG BARG A 340    10129   6680   8869    915  -3477   -376       C  
ATOM   1712  CD AARG A 340     -31.535 -33.940  -9.116  0.50 73.95           C  
ANISOU 1712  CD AARG A 340    11061   7481   9557    888  -3595   -398       C  
ATOM   1713  CD BARG A 340     -31.195 -32.811  -9.653  0.50 74.44           C  
ANISOU 1713  CD BARG A 340    11429   7454   9401    874  -3752   -278       C  
ATOM   1714  NE AARG A 340     -30.461 -34.852  -8.687  0.50 76.06           N  
ANISOU 1714  NE AARG A 340    11283   7933   9683    773  -3201   -372       N  
ATOM   1715  NE BARG A 340     -32.408 -32.764 -10.472  0.50 82.56           N  
ANISOU 1715  NE BARG A 340    12479   8315  10575    983  -4193   -365       N  
ATOM   1716  CZ AARG A 340     -29.289 -34.983  -9.300  0.50 81.03           C  
ANISOU 1716  CZ AARG A 340    12189   8649   9949    652  -3061   -289       C  
ATOM   1717  CZ BARG A 340     -32.425 -32.635 -11.796  0.50 92.43           C  
ANISOU 1717  CZ BARG A 340    14086   9483  11551    955  -4492   -311       C  
ATOM   1718  NH1AARG A 340     -28.995 -34.230 -10.353  0.50 72.18           N  
ANISOU 1718  NH1AARG A 340    11438   7463   8524    605  -3248   -201       N  
ATOM   1719  NH1BARG A 340     -31.290 -32.559 -12.477  0.50 77.65           N  
ANISOU 1719  NH1BARG A 340    12578   7695   9232    804  -4363   -176       N  
ATOM   1720  NH2AARG A 340     -28.387 -35.847  -8.846  0.50 54.89           N  
ANISOU 1720  NH2AARG A 340     8788   5486   6580    570  -2731   -297       N  
ATOM   1721  NH2BARG A 340     -33.578 -32.608 -12.451  0.50 75.92           N  
ANISOU 1721  NH2BARG A 340    11987   7231   9628   1070  -4919   -404       N  
ATOM   1722  N   ILE A 341     -32.257 -31.270  -4.196  1.00 53.38           N  
ANISOU 1722  N   ILE A 341     7498   4941   7842   1097  -3028   -534       N  
ATOM   1723  CA  ILE A 341     -32.298 -31.435  -2.713  1.00 52.32           C  
ANISOU 1723  CA  ILE A 341     7041   4953   7884   1087  -2702   -609       C  
ATOM   1724  C   ILE A 341     -33.725 -31.182  -2.185  1.00 57.42           C  
ANISOU 1724  C   ILE A 341     7339   5529   8949   1202  -2828   -817       C  
ATOM   1725  O   ILE A 341     -34.238 -32.009  -1.444  1.00 55.81           O  
ANISOU 1725  O   ILE A 341     6842   5433   8930   1172  -2631   -916       O  
ATOM   1726  CB  ILE A 341     -31.265 -30.515  -1.948  1.00 54.13           C  
ANISOU 1726  CB  ILE A 341     7360   5254   7955   1052  -2495   -523       C  
ATOM   1727  CG1 ILE A 341     -29.817 -30.922  -2.249  1.00 52.64           C  
ANISOU 1727  CG1 ILE A 341     7431   5169   7400    924  -2296   -355       C  
ATOM   1728  CG2 ILE A 341     -31.523 -30.540  -0.433  1.00 53.53           C  
ANISOU 1728  CG2 ILE A 341     6951   5316   8072   1060  -2220   -632       C  
ATOM   1729  CD1 ILE A 341     -28.815 -29.799  -2.095  1.00 55.15           C  
ANISOU 1729  CD1 ILE A 341     7946   5473   7533    892  -2236   -257       C  
ATOM   1730  N   SER A 342     -34.356 -30.047  -2.557  1.00 57.83           N  
ANISOU 1730  N   SER A 342     7418   5394   9162   1324  -3152   -890       N  
ATOM   1731  CA  SER A 342     -35.707 -29.724  -2.068  1.00 61.40           C  
ANISOU 1731  CA  SER A 342     7509   5766  10052   1445  -3284  -1129       C  
ATOM   1732  C   SER A 342     -36.748 -30.800  -2.440  1.00 66.70           C  
ANISOU 1732  C   SER A 342     7966   6418  10959   1460  -3387  -1261       C  
ATOM   1733  O   SER A 342     -37.720 -31.043  -1.699  1.00 67.58           O  
ANISOU 1733  O   SER A 342     7691   6567  11420   1490  -3298  -1467       O  
ATOM   1734  CB  SER A 342     -36.162 -28.355  -2.568  1.00 67.33           C  
ANISOU 1734  CB  SER A 342     8356   6278  10949   1587  -3681  -1180       C  
ATOM   1735  OG  SER A 342     -35.952 -28.222  -3.963  1.00 81.04           O  
ANISOU 1735  OG  SER A 342    10467   7852  12472   1595  -4026  -1032       O  
ATOM   1736  N   ARG A 343     -36.521 -31.449  -3.587  1.00 61.78           N  
ANISOU 1736  N   ARG A 343     7592   5742  10137   1426  -3559  -1154       N  
ATOM   1737  CA  ARG A 343     -37.392 -32.491  -4.106  1.00 60.82           C  
ANISOU 1737  CA  ARG A 343     7318   5586  10206   1435  -3693  -1267       C  
ATOM   1738  C   ARG A 343     -36.927 -33.919  -3.755  1.00 62.92           C  
ANISOU 1738  C   ARG A 343     7513   6032  10361   1291  -3346  -1207       C  
ATOM   1739  O   ARG A 343     -37.651 -34.863  -4.067  1.00 61.44           O  
ANISOU 1739  O   ARG A 343     7165   5819  10362   1285  -3421  -1310       O  
ATOM   1740  CB  ARG A 343     -37.581 -32.300  -5.616  1.00 57.05           C  
ANISOU 1740  CB  ARG A 343     7146   4920   9612   1501  -4151  -1224       C  
ATOM   1741  CG  ARG A 343     -38.405 -31.053  -5.922  1.00 59.54           C  
ANISOU 1741  CG  ARG A 343     7449   5009  10165   1665  -4566  -1325       C  
ATOM   1742  CD  ARG A 343     -38.309 -30.638  -7.355  1.00 69.84           C  
ANISOU 1742  CD  ARG A 343     9166   6131  11239   1707  -5008  -1207       C  
ATOM   1743  NE  ARG A 343     -39.071 -29.411  -7.582  1.00 77.39           N  
ANISOU 1743  NE  ARG A 343    10117   6843  12446   1869  -5432  -1290       N  
ATOM   1744  CZ  ARG A 343     -39.291 -28.886  -8.779  1.00 91.91           C  
ANISOU 1744  CZ  ARG A 343    12277   8468  14178   1938  -5917  -1217       C  
ATOM   1745  NH1 ARG A 343     -38.830 -29.488  -9.871  1.00 82.69           N  
ANISOU 1745  NH1 ARG A 343    11461   7324  12634   1851  -6019  -1074       N  
ATOM   1746  NH2 ARG A 343     -39.963 -27.749  -8.896  1.00 83.15           N  
ANISOU 1746  NH2 ARG A 343    11150   7113  13329   2093  -6314  -1289       N  
ATOM   1747  N   VAL A 344     -35.748 -34.066  -3.070  1.00 58.25           N  
ANISOU 1747  N   VAL A 344     7026   5609   9499   1181  -2987  -1053       N  
ATOM   1748  CA  VAL A 344     -35.120 -35.342  -2.645  1.00 56.56           C  
ANISOU 1748  CA  VAL A 344     6775   5552   9163   1047  -2661   -970       C  
ATOM   1749  C   VAL A 344     -35.009 -36.314  -3.848  1.00 59.76           C  
ANISOU 1749  C   VAL A 344     7351   5903   9451   1017  -2826   -941       C  
ATOM   1750  O   VAL A 344     -35.436 -37.464  -3.790  1.00 59.16           O  
ANISOU 1750  O   VAL A 344     7099   5847   9532    968  -2759  -1001       O  
ATOM   1751  CB  VAL A 344     -35.764 -35.991  -1.384  1.00 60.63           C  
ANISOU 1751  CB  VAL A 344     6905   6177   9956    990  -2378  -1069       C  
ATOM   1752  CG1 VAL A 344     -34.813 -36.986  -0.741  1.00 58.17           C  
ANISOU 1752  CG1 VAL A 344     6627   6022   9452    850  -2032   -924       C  
ATOM   1753  CG2 VAL A 344     -36.168 -34.937  -0.366  1.00 60.72           C  
ANISOU 1753  CG2 VAL A 344     6719   6224  10129   1042  -2286  -1172       C  
ATOM   1754  N   GLU A 345     -34.446 -35.812  -4.941  1.00 56.83           N  
ANISOU 1754  N   GLU A 345     7330   5460   8801   1038  -3042   -854       N  
ATOM   1755  CA  GLU A 345     -34.283 -36.535  -6.197  1.00 57.73           C  
ANISOU 1755  CA  GLU A 345     7660   5531   8746   1012  -3224   -842       C  
ATOM   1756  C   GLU A 345     -32.950 -37.270  -6.343  1.00 61.76           C  
ANISOU 1756  C   GLU A 345     8362   6170   8933    890  -2969   -721       C  
ATOM   1757  O   GLU A 345     -31.998 -36.740  -6.922  1.00 63.08           O  
ANISOU 1757  O   GLU A 345     8846   6356   8764    850  -2975   -611       O  
ATOM   1758  CB  GLU A 345     -34.496 -35.588  -7.375  1.00 60.36           C  
ANISOU 1758  CB  GLU A 345     8285   5712   8937   1089  -3621   -824       C  
ATOM   1759  CG  GLU A 345     -35.950 -35.360  -7.707  1.00 68.21           C  
ANISOU 1759  CG  GLU A 345     9096   6539  10283   1222  -3988   -991       C  
ATOM   1760  CD  GLU A 345     -36.220 -34.194  -8.632  1.00 84.81           C  
ANISOU 1760  CD  GLU A 345    11476   8461  12287   1316  -4414   -958       C  
ATOM   1761  OE1 GLU A 345     -37.349 -33.651  -8.585  1.00 79.13           O  
ANISOU 1761  OE1 GLU A 345    10571   7589  11906   1448  -4704  -1097       O  
ATOM   1762  OE2 GLU A 345     -35.323 -33.851  -9.435  1.00 80.40           O  
ANISOU 1762  OE2 GLU A 345    11321   7906  11322   1251  -4470   -800       O  
ATOM   1763  N   PHE A 346     -32.907 -38.500  -5.855  1.00 57.14           N  
ANISOU 1763  N   PHE A 346     7581   5661   8468    826  -2758   -751       N  
ATOM   1764  CA  PHE A 346     -31.738 -39.371  -6.001  1.00 56.52           C  
ANISOU 1764  CA  PHE A 346     7635   5681   8158    725  -2546   -677       C  
ATOM   1765  C   PHE A 346     -32.151 -40.762  -6.512  1.00 58.69           C  
ANISOU 1765  C   PHE A 346     7805   5920   8573    701  -2610   -779       C  
ATOM   1766  O   PHE A 346     -33.235 -41.246  -6.184  1.00 56.93           O  
ANISOU 1766  O   PHE A 346     7313   5637   8682    727  -2673   -878       O  
ATOM   1767  CB  PHE A 346     -30.930 -39.483  -4.688  1.00 55.64           C  
ANISOU 1767  CB  PHE A 346     7413   5697   8029    659  -2185   -578       C  
ATOM   1768  CG  PHE A 346     -31.659 -40.188  -3.569  1.00 56.18           C  
ANISOU 1768  CG  PHE A 346     7143   5790   8414    637  -2030   -616       C  
ATOM   1769  CD1 PHE A 346     -32.461 -39.476  -2.686  1.00 58.59           C  
ANISOU 1769  CD1 PHE A 346     7242   6099   8921    678  -1999   -657       C  
ATOM   1770  CD2 PHE A 346     -31.546 -41.566  -3.399  1.00 57.50           C  
ANISOU 1770  CD2 PHE A 346     7198   5970   8681    565  -1912   -619       C  
ATOM   1771  CE1 PHE A 346     -33.164 -40.128  -1.674  1.00 59.24           C  
ANISOU 1771  CE1 PHE A 346     7019   6217   9274    630  -1832   -698       C  
ATOM   1772  CE2 PHE A 346     -32.273 -42.223  -2.404  1.00 60.78           C  
ANISOU 1772  CE2 PHE A 346     7319   6393   9379    519  -1772   -636       C  
ATOM   1773  CZ  PHE A 346     -33.069 -41.497  -1.540  1.00 59.39           C  
ANISOU 1773  CZ  PHE A 346     6950   6243   9372    542  -1717   -673       C  
ATOM   1774  N   THR A 347     -31.258 -41.383  -7.283  1.00 55.74           N  
ANISOU 1774  N   THR A 347     7633   5585   7960    643  -2580   -771       N  
ATOM   1775  CA  THR A 347     -31.385 -42.720  -7.843  1.00 56.27           C  
ANISOU 1775  CA  THR A 347     7641   5623   8116    614  -2625   -876       C  
ATOM   1776  C   THR A 347     -30.087 -43.451  -7.555  1.00 59.82           C  
ANISOU 1776  C   THR A 347     8138   6168   8421    527  -2350   -820       C  
ATOM   1777  O   THR A 347     -29.017 -42.844  -7.622  1.00 58.81           O  
ANISOU 1777  O   THR A 347     8213   6123   8008    493  -2227   -739       O  
ATOM   1778  CB  THR A 347     -31.723 -42.694  -9.337  1.00 58.02           C  
ANISOU 1778  CB  THR A 347     8077   5777   8191    650  -2947   -982       C  
ATOM   1779  OG1 THR A 347     -30.711 -41.971 -10.026  1.00 58.69           O  
ANISOU 1779  OG1 THR A 347     8510   5928   7863    611  -2935   -908       O  
ATOM   1780  CG2 THR A 347     -33.095 -42.074  -9.630  1.00 56.33           C  
ANISOU 1780  CG2 THR A 347     7786   5437   8180    753  -3275  -1058       C  
ATOM   1781  N   PHE A 348     -30.183 -44.741  -7.232  1.00 55.31           N  
ANISOU 1781  N   PHE A 348     7373   5571   8071    491  -2265   -870       N  
ATOM   1782  CA  PHE A 348     -29.029 -45.584  -6.925  1.00 53.84           C  
ANISOU 1782  CA  PHE A 348     7194   5440   7823    424  -2043   -838       C  
ATOM   1783  C   PHE A 348     -28.502 -46.321  -8.153  1.00 60.11           C  
ANISOU 1783  C   PHE A 348     8138   6226   8475    407  -2133   -977       C  
ATOM   1784  O   PHE A 348     -29.288 -46.972  -8.830  1.00 60.42           O  
ANISOU 1784  O   PHE A 348     8118   6180   8660    430  -2327  -1109       O  
ATOM   1785  CB  PHE A 348     -29.398 -46.640  -5.860  1.00 54.60           C  
ANISOU 1785  CB  PHE A 348     7006   5486   8253    384  -1914   -803       C  
ATOM   1786  CG  PHE A 348     -29.752 -46.102  -4.493  1.00 54.30           C  
ANISOU 1786  CG  PHE A 348     6812   5489   8331    369  -1756   -671       C  
ATOM   1787  CD1 PHE A 348     -28.767 -45.611  -3.645  1.00 52.52           C  
ANISOU 1787  CD1 PHE A 348     6652   5365   7939    343  -1542   -537       C  
ATOM   1788  CD2 PHE A 348     -31.069 -46.126  -4.035  1.00 56.20           C  
ANISOU 1788  CD2 PHE A 348     6826   5672   8857    375  -1811   -701       C  
ATOM   1789  CE1 PHE A 348     -29.088 -45.157  -2.367  1.00 52.10           C  
ANISOU 1789  CE1 PHE A 348     6460   5364   7972    323  -1392   -433       C  
ATOM   1790  CE2 PHE A 348     -31.381 -45.682  -2.745  1.00 57.65           C  
ANISOU 1790  CE2 PHE A 348     6857   5914   9134    344  -1632   -604       C  
ATOM   1791  CZ  PHE A 348     -30.386 -45.198  -1.924  1.00 52.62           C  
ANISOU 1791  CZ  PHE A 348     6309   5386   8297    319  -1426   -468       C  
ATOM   1792  N   PRO A 349     -27.176 -46.312  -8.425  1.00 56.94           N  
ANISOU 1792  N   PRO A 349     7904   5913   7816    361  -1983   -975       N  
ATOM   1793  CA  PRO A 349     -26.644 -47.192  -9.496  1.00 57.96           C  
ANISOU 1793  CA  PRO A 349     8126   6045   7849    335  -2027  -1149       C  
ATOM   1794  C   PRO A 349     -26.802 -48.675  -9.082  1.00 59.81           C  
ANISOU 1794  C   PRO A 349     8113   6184   8428    329  -2000  -1220       C  
ATOM   1795  O   PRO A 349     -27.020 -48.972  -7.902  1.00 56.33           O  
ANISOU 1795  O   PRO A 349     7473   5699   8231    322  -1893  -1098       O  
ATOM   1796  CB  PRO A 349     -25.151 -46.821  -9.573  1.00 58.72           C  
ANISOU 1796  CB  PRO A 349     8389   6263   7658    278  -1812  -1129       C  
ATOM   1797  CG  PRO A 349     -24.996 -45.550  -8.711  1.00 60.62           C  
ANISOU 1797  CG  PRO A 349     8673   6557   7802    281  -1708   -936       C  
ATOM   1798  CD  PRO A 349     -26.091 -45.611  -7.708  1.00 55.80           C  
ANISOU 1798  CD  PRO A 349     7833   5870   7500    329  -1754   -846       C  
ATOM   1799  N   ASP A 350     -26.691 -49.595 -10.057  1.00 59.72           N  
ANISOU 1799  N   ASP A 350     8126   6137   8427    325  -2100  -1418       N  
ATOM   1800  CA  ASP A 350     -26.847 -51.049  -9.899  1.00 61.72           C  
ANISOU 1800  CA  ASP A 350     8166   6269   9016    321  -2120  -1521       C  
ATOM   1801  C   ASP A 350     -26.027 -51.707  -8.797  1.00 63.40           C  
ANISOU 1801  C   ASP A 350     8233   6451   9406    291  -1915  -1422       C  
ATOM   1802  O   ASP A 350     -26.544 -52.610  -8.141  1.00 63.77           O  
ANISOU 1802  O   ASP A 350     8069   6366   9793    279  -1932  -1381       O  
ATOM   1803  CB  ASP A 350     -26.566 -51.752 -11.225  1.00 66.60           C  
ANISOU 1803  CB  ASP A 350     8880   6886   9538    322  -2236  -1781       C  
ATOM   1804  CG  ASP A 350     -27.342 -51.103 -12.337  1.00 89.37           C  
ANISOU 1804  CG  ASP A 350    11945   9801  12209    347  -2468  -1870       C  
ATOM   1805  OD1 ASP A 350     -28.502 -51.494 -12.542  1.00 89.57           O  
ANISOU 1805  OD1 ASP A 350    11851   9715  12467    385  -2682  -1937       O  
ATOM   1806  OD2 ASP A 350     -26.848 -50.080 -12.891  1.00103.83           O  
ANISOU 1806  OD2 ASP A 350    14040  11758  13651    326  -2444  -1840       O  
ATOM   1807  N   PHE A 351     -24.783 -51.271  -8.590  1.00 57.86           N  
ANISOU 1807  N   PHE A 351     7640   5857   8488    273  -1734  -1380       N  
ATOM   1808  CA  PHE A 351     -23.889 -51.857  -7.592  1.00 56.97           C  
ANISOU 1808  CA  PHE A 351     7408   5711   8526    256  -1573  -1298       C  
ATOM   1809  C   PHE A 351     -24.227 -51.530  -6.129  1.00 62.35           C  
ANISOU 1809  C   PHE A 351     7979   6375   9336    242  -1478  -1042       C  
ATOM   1810  O   PHE A 351     -23.667 -52.159  -5.239  1.00 63.67           O  
ANISOU 1810  O   PHE A 351     8045   6485   9661    225  -1389   -954       O  
ATOM   1811  CB  PHE A 351     -22.429 -51.471  -7.895  1.00 57.72           C  
ANISOU 1811  CB  PHE A 351     7640   5929   8364    242  -1419  -1372       C  
ATOM   1812  CG  PHE A 351     -22.153 -49.986  -8.039  1.00 56.42           C  
ANISOU 1812  CG  PHE A 351     7674   5916   7845    224  -1337  -1285       C  
ATOM   1813  CD1 PHE A 351     -21.875 -49.203  -6.926  1.00 54.81           C  
ANISOU 1813  CD1 PHE A 351     7458   5762   7607    221  -1209  -1081       C  
ATOM   1814  CD2 PHE A 351     -22.053 -49.398  -9.297  1.00 58.08           C  
ANISOU 1814  CD2 PHE A 351     8100   6220   7746    200  -1383  -1414       C  
ATOM   1815  CE1 PHE A 351     -21.592 -47.845  -7.060  1.00 53.75           C  
ANISOU 1815  CE1 PHE A 351     7501   5746   7176    202  -1142  -1008       C  
ATOM   1816  CE2 PHE A 351     -21.744 -48.040  -9.428  1.00 58.24           C  
ANISOU 1816  CE2 PHE A 351     8320   6357   7452    168  -1312  -1316       C  
ATOM   1817  CZ  PHE A 351     -21.525 -47.274  -8.308  1.00 53.66           C  
ANISOU 1817  CZ  PHE A 351     7703   5803   6882    173  -1195  -1117       C  
ATOM   1818  N   VAL A 352     -25.108 -50.548  -5.863  1.00 58.69           N  
ANISOU 1818  N   VAL A 352     7538   5960   8801    248  -1503   -930       N  
ATOM   1819  CA  VAL A 352     -25.466 -50.204  -4.480  1.00 56.47           C  
ANISOU 1819  CA  VAL A 352     7148   5687   8621    225  -1393   -718       C  
ATOM   1820  C   VAL A 352     -26.394 -51.306  -3.954  1.00 59.96           C  
ANISOU 1820  C   VAL A 352     7378   5983   9421    186  -1444   -683       C  
ATOM   1821  O   VAL A 352     -27.441 -51.554  -4.537  1.00 58.02           O  
ANISOU 1821  O   VAL A 352     7060   5666   9317    195  -1591   -781       O  
ATOM   1822  CB  VAL A 352     -26.049 -48.777  -4.326  1.00 58.50           C  
ANISOU 1822  CB  VAL A 352     7476   6039   8711    248  -1392   -642       C  
ATOM   1823  CG1 VAL A 352     -26.213 -48.406  -2.856  1.00 56.67           C  
ANISOU 1823  CG1 VAL A 352     7138   5847   8547    219  -1240   -453       C  
ATOM   1824  CG2 VAL A 352     -25.162 -47.764  -5.024  1.00 57.66           C  
ANISOU 1824  CG2 VAL A 352     7599   6046   8263    268  -1366   -682       C  
ATOM   1825  N   THR A 353     -25.953 -52.010  -2.893  1.00 58.09           N  
ANISOU 1825  N   THR A 353     7050   5690   9330    138  -1335   -545       N  
ATOM   1826  CA  THR A 353     -26.686 -53.138  -2.301  1.00 58.94           C  
ANISOU 1826  CA  THR A 353     6977   5644   9773     69  -1360   -476       C  
ATOM   1827  C   THR A 353     -27.908 -52.656  -1.545  1.00 62.64           C  
ANISOU 1827  C   THR A 353     7331   6140  10329     16  -1305   -362       C  
ATOM   1828  O   THR A 353     -27.962 -51.491  -1.165  1.00 62.09           O  
ANISOU 1828  O   THR A 353     7318   6210  10065     37  -1220   -301       O  
ATOM   1829  CB  THR A 353     -25.753 -53.980  -1.402  1.00 64.17           C  
ANISOU 1829  CB  THR A 353     7620   6230  10533     28  -1281   -341       C  
ATOM   1830  OG1 THR A 353     -25.421 -53.218  -0.229  1.00 56.65           O  
ANISOU 1830  OG1 THR A 353     6714   5395   9417      1  -1122   -141       O  
ATOM   1831  CG2 THR A 353     -24.486 -54.454  -2.128  1.00 61.16           C  
ANISOU 1831  CG2 THR A 353     7316   5817  10105     89  -1330   -494       C  
ATOM   1832  N   GLU A 354     -28.876 -53.551  -1.316  1.00 62.49           N  
ANISOU 1832  N   GLU A 354     7136   5985  10620    -58  -1345   -350       N  
ATOM   1833  CA  GLU A 354     -30.134 -53.274  -0.603  1.00 62.91           C  
ANISOU 1833  CA  GLU A 354     7032   6053  10819   -133  -1274   -277       C  
ATOM   1834  C   GLU A 354     -29.911 -52.689   0.787  1.00 62.02           C  
ANISOU 1834  C   GLU A 354     6933   6061  10570   -198  -1056    -64       C  
ATOM   1835  O   GLU A 354     -30.636 -51.780   1.164  1.00 60.16           O  
ANISOU 1835  O   GLU A 354     6636   5932  10290   -203   -983    -64       O  
ATOM   1836  CB  GLU A 354     -31.029 -54.518  -0.532  1.00 67.05           C  
ANISOU 1836  CB  GLU A 354     7363   6393  11722   -232  -1327   -289       C  
ATOM   1837  CG  GLU A 354     -31.500 -55.007  -1.893  1.00 88.54           C  
ANISOU 1837  CG  GLU A 354    10039   9000  14602   -167  -1559   -531       C  
ATOM   1838  CD  GLU A 354     -32.156 -56.379  -1.922  1.00131.63           C  
ANISOU 1838  CD  GLU A 354    15317  14243  20453   -260  -1632   -562       C  
ATOM   1839  OE1 GLU A 354     -31.956 -57.171  -0.970  1.00137.32           O  
ANISOU 1839  OE1 GLU A 354    15989  14871  21315   -378  -1516   -373       O  
ATOM   1840  OE2 GLU A 354     -32.852 -56.672  -2.922  1.00131.50           O  
ANISOU 1840  OE2 GLU A 354    15220  14141  20602   -216  -1822   -773       O  
ATOM   1841  N   GLY A 355     -28.916 -53.202   1.522  1.00 59.24           N  
ANISOU 1841  N   GLY A 355     6659   5690  10160   -241   -971     96       N  
ATOM   1842  CA  GLY A 355     -28.553 -52.709   2.855  1.00 58.21           C  
ANISOU 1842  CA  GLY A 355     6575   5679   9864   -302   -783    300       C  
ATOM   1843  C   GLY A 355     -28.154 -51.244   2.855  1.00 58.53           C  
ANISOU 1843  C   GLY A 355     6722   5911   9605   -210   -723    263       C  
ATOM   1844  O   GLY A 355     -28.591 -50.474   3.720  1.00 57.52           O  
ANISOU 1844  O   GLY A 355     6557   5908   9391   -251   -584    336       O  
ATOM   1845  N   ALA A 356     -27.319 -50.862   1.874  1.00 53.28           N  
ANISOU 1845  N   ALA A 356     6190   5267   8787    -97   -823    139       N  
ATOM   1846  CA  ALA A 356     -26.840 -49.489   1.667  1.00 52.06           C  
ANISOU 1846  CA  ALA A 356     6161   5265   8356    -13   -793     94       C  
ATOM   1847  C   ALA A 356     -28.003 -48.600   1.227  1.00 56.05           C  
ANISOU 1847  C   ALA A 356     6603   5811   8881     22   -849    -10       C  
ATOM   1848  O   ALA A 356     -28.183 -47.533   1.808  1.00 55.00           O  
ANISOU 1848  O   ALA A 356     6474   5793   8628     35   -761     26       O  
ATOM   1849  CB  ALA A 356     -25.736 -49.473   0.635  1.00 52.09           C  
ANISOU 1849  CB  ALA A 356     6312   5262   8218     65   -877    -21       C  
ATOM   1850  N   ARG A 357     -28.831 -49.089   0.266  1.00 52.48           N  
ANISOU 1850  N   ARG A 357     6077   5251   8611     39  -1010   -149       N  
ATOM   1851  CA  ARG A 357     -30.039 -48.433  -0.214  1.00 54.22           C  
ANISOU 1851  CA  ARG A 357     6212   5471   8919     80  -1118   -269       C  
ATOM   1852  C   ARG A 357     -31.002 -48.178   0.933  1.00 59.76           C  
ANISOU 1852  C   ARG A 357     6722   6218   9766      8   -975   -204       C  
ATOM   1853  O   ARG A 357     -31.563 -47.095   0.980  1.00 58.93           O  
ANISOU 1853  O   ARG A 357     6584   6181   9624     59   -990   -266       O  
ATOM   1854  CB  ARG A 357     -30.740 -49.263  -1.309  1.00 54.36           C  
ANISOU 1854  CB  ARG A 357     6159   5348   9148     96  -1323   -425       C  
ATOM   1855  CG  ARG A 357     -29.968 -49.271  -2.619  1.00 58.75           C  
ANISOU 1855  CG  ARG A 357     6914   5889   9520    173  -1477   -543       C  
ATOM   1856  CD  ARG A 357     -30.714 -49.998  -3.703  1.00 58.78           C  
ANISOU 1856  CD  ARG A 357     6856   5769   9709    196  -1696   -719       C  
ATOM   1857  NE  ARG A 357     -29.856 -50.200  -4.868  1.00 60.10           N  
ANISOU 1857  NE  ARG A 357     7217   5938   9682    243  -1803   -836       N  
ATOM   1858  CZ  ARG A 357     -30.261 -50.105  -6.127  1.00 70.85           C  
ANISOU 1858  CZ  ARG A 357     8663   7269  10990    300  -2024  -1008       C  
ATOM   1859  NH1 ARG A 357     -31.525 -49.818  -6.405  1.00 59.11           N  
ANISOU 1859  NH1 ARG A 357     7073   5727   9660    333  -2195  -1084       N  
ATOM   1860  NH2 ARG A 357     -29.407 -50.301  -7.119  1.00 54.74           N  
ANISOU 1860  NH2 ARG A 357     6806   5255   8736    320  -2078  -1117       N  
ATOM   1861  N   ASP A 358     -31.149 -49.136   1.888  1.00 57.38           N  
ANISOU 1861  N   ASP A 358     6305   5881   9617   -120   -831    -79       N  
ATOM   1862  CA  ASP A 358     -32.037 -48.948   3.037  1.00 58.26           C  
ANISOU 1862  CA  ASP A 358     6240   6059   9839   -223   -651    -19       C  
ATOM   1863  C   ASP A 358     -31.558 -47.848   4.002  1.00 59.83           C  
ANISOU 1863  C   ASP A 358     6513   6435   9786   -214   -480     67       C  
ATOM   1864  O   ASP A 358     -32.368 -47.016   4.398  1.00 60.45           O  
ANISOU 1864  O   ASP A 358     6467   6598   9903   -211   -412     -9       O  
ATOM   1865  CB  ASP A 358     -32.318 -50.264   3.785  1.00 61.61           C  
ANISOU 1865  CB  ASP A 358     6552   6393  10464   -390   -537    114       C  
ATOM   1866  CG  ASP A 358     -33.213 -50.058   4.994  1.00 75.73           C  
ANISOU 1866  CG  ASP A 358     8171   8276  12328   -529   -309    174       C  
ATOM   1867  OD1 ASP A 358     -34.324 -49.532   4.823  1.00 82.33           O  
ANISOU 1867  OD1 ASP A 358     8822   9135  13324   -517   -316     13       O  
ATOM   1868  OD2 ASP A 358     -32.772 -50.353   6.118  1.00 77.70           O  
ANISOU 1868  OD2 ASP A 358     8477   8586  12458   -646   -126    370       O  
ATOM   1869  N   LEU A 359     -30.262 -47.852   4.377  1.00 53.01           N  
ANISOU 1869  N   LEU A 359     5832   5622   8689   -205   -422    199       N  
ATOM   1870  CA  LEU A 359     -29.675 -46.855   5.265  1.00 52.00           C  
ANISOU 1870  CA  LEU A 359     5787   5655   8315   -191   -280    273       C  
ATOM   1871  C   LEU A 359     -29.711 -45.451   4.656  1.00 53.69           C  
ANISOU 1871  C   LEU A 359     6054   5933   8411    -59   -365    134       C  
ATOM   1872  O   LEU A 359     -30.134 -44.527   5.331  1.00 53.45           O  
ANISOU 1872  O   LEU A 359     5956   6013   8340    -56   -264    105       O  
ATOM   1873  CB  LEU A 359     -28.235 -47.255   5.664  1.00 51.72           C  
ANISOU 1873  CB  LEU A 359     5927   5630   8095   -197   -246    422       C  
ATOM   1874  CG  LEU A 359     -27.473 -46.289   6.578  1.00 54.69           C  
ANISOU 1874  CG  LEU A 359     6402   6165   8212   -179   -120    494       C  
ATOM   1875  CD1 LEU A 359     -28.127 -46.207   7.976  1.00 56.68           C  
ANISOU 1875  CD1 LEU A 359     6554   6531   8451   -302     82    588       C  
ATOM   1876  CD2 LEU A 359     -26.042 -46.671   6.669  1.00 53.29           C  
ANISOU 1876  CD2 LEU A 359     6382   5967   7898   -155   -149    588       C  
ATOM   1877  N   ILE A 360     -29.288 -45.298   3.389  1.00 50.57           N  
ANISOU 1877  N   ILE A 360     5784   5467   7962     41   -551     47       N  
ATOM   1878  CA  ILE A 360     -29.274 -44.022   2.671  1.00 48.75           C  
ANISOU 1878  CA  ILE A 360     5649   5264   7609    153   -667    -58       C  
ATOM   1879  C   ILE A 360     -30.702 -43.435   2.562  1.00 53.99           C  
ANISOU 1879  C   ILE A 360     6138   5907   8470    186   -744   -191       C  
ATOM   1880  O   ILE A 360     -30.905 -42.269   2.898  1.00 51.46           O  
ANISOU 1880  O   ILE A 360     5805   5655   8095    238   -724   -235       O  
ATOM   1881  CB  ILE A 360     -28.546 -44.127   1.294  1.00 50.49           C  
ANISOU 1881  CB  ILE A 360     6060   5414   7710    218   -839   -115       C  
ATOM   1882  CG1 ILE A 360     -27.027 -44.461   1.463  1.00 48.69           C  
ANISOU 1882  CG1 ILE A 360     5983   5225   7292    198   -745    -24       C  
ATOM   1883  CG2 ILE A 360     -28.739 -42.833   0.460  1.00 48.77           C  
ANISOU 1883  CG2 ILE A 360     5957   5197   7378    313   -990   -207       C  
ATOM   1884  CD1 ILE A 360     -26.374 -45.115   0.183  1.00 51.44           C  
ANISOU 1884  CD1 ILE A 360     6458   5495   7592    221   -870   -105       C  
ATOM   1885  N   SER A 361     -31.692 -44.258   2.118  1.00 55.06           N  
ANISOU 1885  N   SER A 361     6118   5937   8864    158   -839   -273       N  
ATOM   1886  CA  SER A 361     -33.110 -43.856   1.969  1.00 56.01           C  
ANISOU 1886  CA  SER A 361     6030   6017   9236    190   -934   -430       C  
ATOM   1887  C   SER A 361     -33.704 -43.385   3.278  1.00 59.52           C  
ANISOU 1887  C   SER A 361     6281   6575   9759    127   -713   -435       C  
ATOM   1888  O   SER A 361     -34.450 -42.413   3.280  1.00 60.37           O  
ANISOU 1888  O   SER A 361     6277   6695   9965    199   -775   -574       O  
ATOM   1889  CB  SER A 361     -33.952 -44.988   1.390  1.00 60.58           C  
ANISOU 1889  CB  SER A 361     6460   6464  10094    149  -1048   -512       C  
ATOM   1890  OG  SER A 361     -33.637 -45.180   0.024  1.00 70.38           O  
ANISOU 1890  OG  SER A 361     7866   7606  11268    232  -1296   -574       O  
ATOM   1891  N   ARG A 362     -33.325 -44.041   4.407  1.00 54.36           N  
ANISOU 1891  N   ARG A 362     5602   6005   9048     -7   -463   -285       N  
ATOM   1892  CA  ARG A 362     -33.770 -43.674   5.758  1.00 54.21           C  
ANISOU 1892  CA  ARG A 362     5430   6127   9039    -99   -210   -275       C  
ATOM   1893  C   ARG A 362     -33.162 -42.349   6.192  1.00 56.39           C  
ANISOU 1893  C   ARG A 362     5814   6526   9083    -15   -162   -284       C  
ATOM   1894  O   ARG A 362     -33.806 -41.575   6.891  1.00 56.85           O  
ANISOU 1894  O   ARG A 362     5719   6681   9201    -18    -50   -393       O  
ATOM   1895  CB  ARG A 362     -33.414 -44.778   6.764  1.00 54.79           C  
ANISOU 1895  CB  ARG A 362     5511   6244   9061   -275     11    -79       C  
ATOM   1896  CG  ARG A 362     -34.397 -45.940   6.789  1.00 66.12           C  
ANISOU 1896  CG  ARG A 362     6748   7583  10790   -410     51    -89       C  
ATOM   1897  CD  ARG A 362     -34.240 -46.759   8.054  1.00 81.78           C  
ANISOU 1897  CD  ARG A 362     8729   9634  12708   -612    309    111       C  
ATOM   1898  NE  ARG A 362     -34.287 -48.197   7.793  1.00 96.66           N  
ANISOU 1898  NE  ARG A 362    10608  11357  14762   -719    262    221       N  
ATOM   1899  CZ  ARG A 362     -35.399 -48.930   7.782  1.00120.63           C  
ANISOU 1899  CZ  ARG A 362    13424  14308  18102   -843    307    164       C  
ATOM   1900  NH1 ARG A 362     -36.581 -48.362   7.999  1.00104.39           N  
ANISOU 1900  NH1 ARG A 362    11118  12322  16225   -873    403    -22       N  
ATOM   1901  NH2 ARG A 362     -35.339 -50.232   7.539  1.00116.78           N  
ANISOU 1901  NH2 ARG A 362    12949  13653  17771   -936    248    272       N  
ATOM   1902  N   LEU A 363     -31.917 -42.071   5.774  1.00 51.71           N  
ANISOU 1902  N   LEU A 363     5475   5930   8244     57   -241   -190       N  
ATOM   1903  CA  LEU A 363     -31.250 -40.821   6.126  1.00 49.19           C  
ANISOU 1903  CA  LEU A 363     5268   5707   7714    132   -209   -195       C  
ATOM   1904  C   LEU A 363     -31.689 -39.658   5.261  1.00 52.74           C  
ANISOU 1904  C   LEU A 363     5726   6086   8226    273   -419   -351       C  
ATOM   1905  O   LEU A 363     -31.810 -38.524   5.748  1.00 51.26           O  
ANISOU 1905  O   LEU A 363     5500   5965   8011    326   -383   -430       O  
ATOM   1906  CB  LEU A 363     -29.729 -41.005   6.086  1.00 47.94           C  
ANISOU 1906  CB  LEU A 363     5354   5569   7292    135   -194    -42       C  
ATOM   1907  CG  LEU A 363     -29.163 -41.928   7.173  1.00 51.68           C  
ANISOU 1907  CG  LEU A 363     5843   6118   7676     11     -3    125       C  
ATOM   1908  CD1 LEU A 363     -27.808 -42.438   6.806  1.00 49.92           C  
ANISOU 1908  CD1 LEU A 363     5818   5852   7299     26    -58    238       C  
ATOM   1909  CD2 LEU A 363     -29.101 -41.224   8.492  1.00 52.26           C  
ANISOU 1909  CD2 LEU A 363     5879   6359   7619    -29    191    142       C  
ATOM   1910  N   LEU A 364     -31.973 -39.925   3.991  1.00 51.46           N  
ANISOU 1910  N   LEU A 364     5614   5782   8157    333   -655   -404       N  
ATOM   1911  CA  LEU A 364     -32.412 -38.881   3.074  1.00 52.46           C  
ANISOU 1911  CA  LEU A 364     5784   5813   8337    463   -905   -530       C  
ATOM   1912  C   LEU A 364     -33.933 -38.678   3.049  1.00 60.37           C  
ANISOU 1912  C   LEU A 364     6513   6754   9672    502  -1004   -721       C  
ATOM   1913  O   LEU A 364     -34.553 -38.750   1.996  1.00 62.67           O  
ANISOU 1913  O   LEU A 364     6799   6908  10106    572  -1263   -813       O  
ATOM   1914  CB  LEU A 364     -31.849 -39.136   1.670  1.00 51.76           C  
ANISOU 1914  CB  LEU A 364     5933   5612   8121    508  -1128   -491       C  
ATOM   1915  CG  LEU A 364     -30.308 -39.159   1.541  1.00 51.21           C  
ANISOU 1915  CG  LEU A 364     6123   5596   7738    480  -1046   -348       C  
ATOM   1916  CD1 LEU A 364     -29.907 -39.286   0.086  1.00 50.64           C  
ANISOU 1916  CD1 LEU A 364     6272   5427   7542    516  -1257   -354       C  
ATOM   1917  CD2 LEU A 364     -29.682 -37.915   2.157  1.00 47.39           C  
ANISOU 1917  CD2 LEU A 364     5721   5191   7093    512   -958   -316       C  
ATOM   1918  N   LYS A 365     -34.517 -38.364   4.218  1.00 57.70           N  
ANISOU 1918  N   LYS A 365     5947   6523   9454    459   -800   -800       N  
ATOM   1919  CA  LYS A 365     -35.944 -38.054   4.369  1.00 59.78           C  
ANISOU 1919  CA  LYS A 365     5903   6750  10060    492   -850  -1023       C  
ATOM   1920  C   LYS A 365     -36.116 -36.532   4.436  1.00 63.56           C  
ANISOU 1920  C   LYS A 365     6368   7214  10569    627   -963  -1157       C  
ATOM   1921  O   LYS A 365     -35.278 -35.858   5.053  1.00 61.67           O  
ANISOU 1921  O   LYS A 365     6252   7074  10104    628   -833  -1084       O  
ATOM   1922  CB  LYS A 365     -36.517 -38.680   5.651  1.00 62.67           C  
ANISOU 1922  CB  LYS A 365     6007   7257  10547    337   -519  -1052       C  
ATOM   1923  CG  LYS A 365     -36.496 -40.202   5.675  1.00 71.37           C  
ANISOU 1923  CG  LYS A 365     7095   8345  11678    189   -412   -921       C  
ATOM   1924  CD  LYS A 365     -37.739 -40.872   5.094  1.00 69.69           C  
ANISOU 1924  CD  LYS A 365     6640   8007  11831    173   -537  -1073       C  
ATOM   1925  CE  LYS A 365     -37.713 -42.356   5.431  1.00 70.80           C  
ANISOU 1925  CE  LYS A 365     6741   8150  12011     -8   -363   -934       C  
ATOM   1926  NZ  LYS A 365     -38.881 -43.105   4.908  1.00 73.68           N  
ANISOU 1926  NZ  LYS A 365     6864   8386  12746    -43   -471  -1079       N  
ATOM   1927  N   HIS A 366     -37.178 -35.985   3.797  1.00 62.19           N  
ANISOU 1927  N   HIS A 366     6043   6900  10688    745  -1229  -1360       N  
ATOM   1928  CA  HIS A 366     -37.469 -34.544   3.810  1.00 64.42           C  
ANISOU 1928  CA  HIS A 366     6287   7123  11067    887  -1388  -1510       C  
ATOM   1929  C   HIS A 366     -37.789 -34.093   5.231  1.00 68.63           C  
ANISOU 1929  C   HIS A 366     6566   7826  11684    838  -1082  -1645       C  
ATOM   1930  O   HIS A 366     -37.316 -33.037   5.648  1.00 67.02           O  
ANISOU 1930  O   HIS A 366     6436   7659  11370    899  -1061  -1664       O  
ATOM   1931  CB  HIS A 366     -38.658 -34.188   2.877  1.00 67.70           C  
ANISOU 1931  CB  HIS A 366     6554   7334  11834   1026  -1760  -1717       C  
ATOM   1932  CG  HIS A 366     -38.682 -32.742   2.462  1.00 72.12           C  
ANISOU 1932  CG  HIS A 366     7210   7756  12436   1193  -2049  -1797       C  
ATOM   1933  ND1 HIS A 366     -39.418 -31.792   3.166  1.00 76.23           N  
ANISOU 1933  ND1 HIS A 366     7455   8275  13233   1274  -2037  -2039       N  
ATOM   1934  CD2 HIS A 366     -38.057 -32.126   1.427  1.00 73.64           C  
ANISOU 1934  CD2 HIS A 366     7747   7802  12433   1280  -2349  -1664       C  
ATOM   1935  CE1 HIS A 366     -39.223 -30.640   2.536  1.00 76.25           C  
ANISOU 1935  CE1 HIS A 366     7643   8109  13222   1419  -2355  -2038       C  
ATOM   1936  NE2 HIS A 366     -38.416 -30.788   1.481  1.00 75.45           N  
ANISOU 1936  NE2 HIS A 366     7925   7914  12828   1419  -2549  -1803       N  
ATOM   1937  N   ASN A 367     -38.596 -34.900   5.958  1.00 67.70           N  
ANISOU 1937  N   ASN A 367     6154   7812  11758    715   -842  -1745       N  
ATOM   1938  CA  ASN A 367     -39.008 -34.618   7.326  1.00 69.30           C  
ANISOU 1938  CA  ASN A 367     6098   8204  12029    632   -512  -1894       C  
ATOM   1939  C   ASN A 367     -37.906 -35.033   8.307  1.00 69.29           C  
ANISOU 1939  C   ASN A 367     6279   8405  11643    484   -182  -1666       C  
ATOM   1940  O   ASN A 367     -37.617 -36.227   8.439  1.00 66.42           O  
ANISOU 1940  O   ASN A 367     5984   8089  11163    340    -37  -1482       O  
ATOM   1941  CB  ASN A 367     -40.356 -35.263   7.646  1.00 75.82           C  
ANISOU 1941  CB  ASN A 367     6535   9053  13220    542   -387  -2105       C  
ATOM   1942  CG  ASN A 367     -40.931 -34.806   8.966  1.00117.54           C  
ANISOU 1942  CG  ASN A 367    11523  14531  18607    464    -60  -2323       C  
ATOM   1943  OD1 ASN A 367     -41.168 -35.609   9.874  1.00115.79           O  
ANISOU 1943  OD1 ASN A 367    11167  14481  18349    260    294  -2298       O  
ATOM   1944  ND2 ASN A 367     -41.169 -33.503   9.103  1.00115.77           N  
ANISOU 1944  ND2 ASN A 367    11196  14282  18509    616   -169  -2547       N  
ATOM   1945  N   PRO A 368     -37.282 -34.038   8.999  1.00 65.07           N  
ANISOU 1945  N   PRO A 368     5823   7975  10926    526    -87  -1684       N  
ATOM   1946  CA  PRO A 368     -36.157 -34.358   9.906  1.00 63.15           C  
ANISOU 1946  CA  PRO A 368     5775   7915  10307    404    179  -1471       C  
ATOM   1947  C   PRO A 368     -36.459 -35.405  10.978  1.00 67.41           C  
ANISOU 1947  C   PRO A 368     6181   8638  10794    189    532  -1418       C  
ATOM   1948  O   PRO A 368     -35.592 -36.232  11.261  1.00 64.45           O  
ANISOU 1948  O   PRO A 368     6010   8325  10155     79    647  -1164       O  
ATOM   1949  CB  PRO A 368     -35.778 -33.001  10.497  1.00 65.17           C  
ANISOU 1949  CB  PRO A 368     6046   8241  10474    497    203  -1592       C  
ATOM   1950  CG  PRO A 368     -36.307 -31.989   9.510  1.00 68.82           C  
ANISOU 1950  CG  PRO A 368     6459   8489  11201    692   -145  -1766       C  
ATOM   1951  CD  PRO A 368     -37.526 -32.579   8.923  1.00 65.32           C  
ANISOU 1951  CD  PRO A 368     5786   7937  11097    695   -259  -1897       C  
ATOM   1952  N   SER A 369     -37.683 -35.393  11.546  1.00 66.74           N  
ANISOU 1952  N   SER A 369     5758   8630  10971    123    696  -1655       N  
ATOM   1953  CA  SER A 369     -38.114 -36.347  12.577  1.00 69.47           C  
ANISOU 1953  CA  SER A 369     5963   9153  11280   -113   1055  -1618       C  
ATOM   1954  C   SER A 369     -38.211 -37.794  12.052  1.00 75.44           C  
ANISOU 1954  C   SER A 369     6768   9804  12091   -232   1029  -1417       C  
ATOM   1955  O   SER A 369     -38.104 -38.742  12.836  1.00 76.68           O  
ANISOU 1955  O   SER A 369     6954  10077  12105   -441   1290  -1252       O  
ATOM   1956  CB  SER A 369     -39.420 -35.897  13.215  1.00 78.26           C  
ANISOU 1956  CB  SER A 369     6680  10369  12687   -157   1241  -1962       C  
ATOM   1957  OG  SER A 369     -40.181 -35.096  12.328  1.00 93.20           O  
ANISOU 1957  OG  SER A 369     8384  12082  14947     45    944  -2227       O  
ATOM   1958  N   GLN A 370     -38.347 -37.955  10.720  1.00 70.99           N  
ANISOU 1958  N   GLN A 370     6244   9015  11715   -100    697  -1420       N  
ATOM   1959  CA  GLN A 370     -38.419 -39.246  10.034  1.00 70.31           C  
ANISOU 1959  CA  GLN A 370     6206   8797  11713   -176    611  -1266       C  
ATOM   1960  C   GLN A 370     -37.025 -39.858   9.829  1.00 73.28           C  
ANISOU 1960  C   GLN A 370     6943   9149  11753   -194    565   -950       C  
ATOM   1961  O   GLN A 370     -36.917 -41.025   9.444  1.00 74.57           O  
ANISOU 1961  O   GLN A 370     7166   9220  11947   -278    533   -801       O  
ATOM   1962  CB  GLN A 370     -39.153 -39.110   8.691  1.00 72.10           C  
ANISOU 1962  CB  GLN A 370     6328   8804  12264    -20    258  -1431       C  
ATOM   1963  CG  GLN A 370     -40.658 -38.887   8.820  1.00 97.88           C  
ANISOU 1963  CG  GLN A 370     9183  12056  15951    -27    289  -1750       C  
ATOM   1964  CD  GLN A 370     -41.400 -39.178   7.535  1.00124.92           C  
ANISOU 1964  CD  GLN A 370    12507  15254  19704     82    -55  -1871       C  
ATOM   1965  OE1 GLN A 370     -40.898 -38.964   6.421  1.00120.75           O  
ANISOU 1965  OE1 GLN A 370    12212  14573  19096    237   -390  -1797       O  
ATOM   1966  NE2 GLN A 370     -42.627 -39.664   7.661  1.00120.34           N  
ANISOU 1966  NE2 GLN A 370    11573  14651  19499     -5     22  -2072       N  
ATOM   1967  N   ARG A 371     -35.957 -39.067  10.063  1.00 66.49           N  
ANISOU 1967  N   ARG A 371     6306   8359  10600   -112    552   -868       N  
ATOM   1968  CA  ARG A 371     -34.569 -39.521   9.941  1.00 63.06           C  
ANISOU 1968  CA  ARG A 371     6188   7913   9861   -119    516   -605       C  
ATOM   1969  C   ARG A 371     -34.235 -40.302  11.206  1.00 66.78           C  
ANISOU 1969  C   ARG A 371     6693   8537  10141   -316    811   -430       C  
ATOM   1970  O   ARG A 371     -34.730 -39.938  12.264  1.00 66.32           O  
ANISOU 1970  O   ARG A 371     6492   8646  10059   -406   1047   -520       O  
ATOM   1971  CB  ARG A 371     -33.601 -38.339   9.775  1.00 58.94           C  
ANISOU 1971  CB  ARG A 371     5860   7407   9126     29    403   -607       C  
ATOM   1972  CG  ARG A 371     -33.659 -37.700   8.411  1.00 59.94           C  
ANISOU 1972  CG  ARG A 371     6055   7356   9364    203     81   -697       C  
ATOM   1973  CD  ARG A 371     -33.000 -36.344   8.384  1.00 63.75           C  
ANISOU 1973  CD  ARG A 371     6670   7852   9700    328     -3   -740       C  
ATOM   1974  NE  ARG A 371     -33.566 -35.527   7.311  1.00 62.16           N  
ANISOU 1974  NE  ARG A 371     6447   7485   9685    479   -294   -886       N  
ATOM   1975  CZ  ARG A 371     -33.481 -34.205   7.259  1.00 72.35           C  
ANISOU 1975  CZ  ARG A 371     7766   8744  10978    597   -405   -992       C  
ATOM   1976  NH1 ARG A 371     -32.817 -33.542   8.193  1.00 56.20           N  
ANISOU 1976  NH1 ARG A 371     5765   6831   8758    585   -239   -982       N  
ATOM   1977  NH2 ARG A 371     -34.042 -33.535   6.252  1.00 56.86           N  
ANISOU 1977  NH2 ARG A 371     5803   6605   9197    728   -705  -1104       N  
ATOM   1978  N   PRO A 372     -33.428 -41.380  11.151  1.00 63.39           N  
ANISOU 1978  N   PRO A 372     6453   8055   9579   -393    801   -186       N  
ATOM   1979  CA  PRO A 372     -33.157 -42.135  12.375  1.00 64.67           C  
ANISOU 1979  CA  PRO A 372     6669   8341   9563   -586   1048      1       C  
ATOM   1980  C   PRO A 372     -32.270 -41.398  13.369  1.00 70.84           C  
ANISOU 1980  C   PRO A 372     7598   9300  10018   -580   1167     58       C  
ATOM   1981  O   PRO A 372     -31.743 -40.318  13.066  1.00 69.25           O  
ANISOU 1981  O   PRO A 372     7466   9111   9733   -420   1055    -38       O  
ATOM   1982  CB  PRO A 372     -32.487 -43.403  11.846  1.00 65.06           C  
ANISOU 1982  CB  PRO A 372     6880   8232   9606   -624    923    220       C  
ATOM   1983  CG  PRO A 372     -31.815 -42.990  10.633  1.00 66.69           C  
ANISOU 1983  CG  PRO A 372     7212   8316   9811   -432    660    173       C  
ATOM   1984  CD  PRO A 372     -32.711 -41.968  10.003  1.00 62.62           C  
ANISOU 1984  CD  PRO A 372     6530   7780   9481   -311    561    -79       C  
ATOM   1985  N   MET A 373     -32.083 -41.984  14.536  1.00 69.77           N  
ANISOU 1985  N   MET A 373     7521   9296   9694   -763   1388    220       N  
ATOM   1986  CA  MET A 373     -31.172 -41.468  15.526  1.00 69.71           C  
ANISOU 1986  CA  MET A 373     7679   9457   9349   -778   1490    301       C  
ATOM   1987  C   MET A 373     -29.820 -42.049  15.226  1.00 66.76           C  
ANISOU 1987  C   MET A 373     7566   8966   8834   -715   1302    520       C  
ATOM   1988  O   MET A 373     -29.725 -42.977  14.476  1.00 65.44           O  
ANISOU 1988  O   MET A 373     7428   8616   8819   -713   1162    617       O  
ATOM   1989  CB  MET A 373     -31.596 -41.946  16.894  1.00 76.16           C  
ANISOU 1989  CB  MET A 373     8488  10450  10000  -1020   1780    414       C  
ATOM   1990  CG  MET A 373     -32.739 -41.189  17.518  1.00 84.44           C  
ANISOU 1990  CG  MET A 373     9262  11647  11174  -1124   2026    186       C  
ATOM   1991  SD  MET A 373     -33.050 -41.873  19.136  1.00 95.17           S  
ANISOU 1991  SD  MET A 373    10678  13236  12246  -1446   2391    354       S  
ATOM   1992  CE  MET A 373     -33.747 -43.460  18.736  1.00 93.01           C  
ANISOU 1992  CE  MET A 373    10476  12742  12120  -1628   2341    662       C  
ATOM   1993  N   LEU A 374     -28.777 -41.522  15.833  1.00 60.09           N  
ANISOU 1993  N   LEU A 374     6892   8222   7717   -668   1299    581       N  
ATOM   1994  CA  LEU A 374     -27.443 -42.034  15.586  1.00 57.76           C  
ANISOU 1994  CA  LEU A 374     6817   7824   7304   -612   1131    761       C  
ATOM   1995  C   LEU A 374     -27.269 -43.464  16.135  1.00 63.59           C  
ANISOU 1995  C   LEU A 374     7658   8505   7997   -777   1159   1023       C  
ATOM   1996  O   LEU A 374     -26.549 -44.253  15.507  1.00 60.13           O  
ANISOU 1996  O   LEU A 374     7323   7894   7630   -732    981   1140       O  
ATOM   1997  CB  LEU A 374     -26.380 -41.082  16.107  1.00 56.75           C  
ANISOU 1997  CB  LEU A 374     6820   7812   6930   -519   1111    735       C  
ATOM   1998  CG  LEU A 374     -26.281 -39.763  15.334  1.00 58.33           C  
ANISOU 1998  CG  LEU A 374     6966   7996   7200   -341   1016    517       C  
ATOM   1999  CD1 LEU A 374     -25.605 -38.725  16.166  1.00 58.99           C  
ANISOU 1999  CD1 LEU A 374     7118   8235   7060   -294   1068    453       C  
ATOM   2000  CD2 LEU A 374     -25.628 -39.944  13.956  1.00 48.10           C  
ANISOU 2000  CD2 LEU A 374     5746   6504   6025   -219    794    528       C  
ATOM   2001  N   ARG A 375     -27.961 -43.809  17.205  1.00 64.29           N  
ANISOU 2001  N   ARG A 375     7708   8727   7993   -978   1384   1099       N  
ATOM   2002  CA  ARG A 375     -27.969 -45.171  17.714  1.00 67.88           C  
ANISOU 2002  CA  ARG A 375     8264   9121   8408  -1175   1430   1367       C  
ATOM   2003  C   ARG A 375     -28.478 -46.154  16.675  1.00 72.87           C  
ANISOU 2003  C   ARG A 375     8804   9513   9369  -1179   1306   1394       C  
ATOM   2004  O   ARG A 375     -27.881 -47.179  16.447  1.00 73.15           O  
ANISOU 2004  O   ARG A 375     8972   9376   9445  -1191   1150   1583       O  
ATOM   2005  CB  ARG A 375     -28.863 -45.250  18.935  1.00 76.51           C  
ANISOU 2005  CB  ARG A 375     9282  10400   9389  -1416   1734   1394       C  
ATOM   2006  CG  ARG A 375     -28.315 -46.061  20.088  1.00 99.49           C  
ANISOU 2006  CG  ARG A 375    12237  13587  11979  -1448   1914   1314       C  
ATOM   2007  CD  ARG A 375     -29.347 -46.101  21.192  1.00117.39           C  
ANISOU 2007  CD  ARG A 375    14392  16033  14179  -1705   2243   1301       C  
ATOM   2008  NE  ARG A 375     -30.501 -45.300  20.806  1.00135.57           N  
ANISOU 2008  NE  ARG A 375    16740  18621  16150  -1760   2441   1210       N  
ATOM   2009  CZ  ARG A 375     -30.789 -44.110  21.314  1.00161.98           C  
ANISOU 2009  CZ  ARG A 375    20011  22182  19351  -1993   2764   1172       C  
ATOM   2010  NH1 ARG A 375     -30.017 -43.580  22.251  1.00153.36           N  
ANISOU 2010  NH1 ARG A 375    18790  21045  18436  -2205   2934   1228       N  
ATOM   2011  NH2 ARG A 375     -31.857 -43.455  20.884  1.00154.64           N  
ANISOU 2011  NH2 ARG A 375    19132  21520  18104  -2028   2929   1064       N  
ATOM   2012  N   GLU A 376     -29.601 -45.826  16.061  1.00 69.11           N  
ANISOU 2012  N   GLU A 376     8094   9019   9147  -1155   1353   1182       N  
ATOM   2013  CA  GLU A 376     -30.215 -46.626  14.995  1.00 68.47           C  
ANISOU 2013  CA  GLU A 376     7889   8729   9399  -1152   1239   1149       C  
ATOM   2014  C   GLU A 376     -29.234 -46.837  13.844  1.00 67.56           C  
ANISOU 2014  C   GLU A 376     7885   8430   9354   -966    957   1151       C  
ATOM   2015  O   GLU A 376     -29.157 -47.935  13.311  1.00 67.98           O  
ANISOU 2015  O   GLU A 376     7957   8294   9579   -996    836   1247       O  
ATOM   2016  CB  GLU A 376     -31.508 -45.969  14.477  1.00 70.39           C  
ANISOU 2016  CB  GLU A 376     7859   9007   9880  -1120   1307    876       C  
ATOM   2017  CG  GLU A 376     -32.664 -45.862  15.469  1.00 81.46           C  
ANISOU 2017  CG  GLU A 376     9079  10576  11295  -1318   1608    814       C  
ATOM   2018  CD  GLU A 376     -33.853 -45.074  14.936  1.00100.77           C  
ANISOU 2018  CD  GLU A 376    11232  13049  14006  -1246   1638    497       C  
ATOM   2019  OE1 GLU A 376     -34.467 -45.513  13.935  1.00103.43           O  
ANISOU 2019  OE1 GLU A 376    11431  13212  14655  -1204   1498    409       O  
ATOM   2020  OE2 GLU A 376     -34.165 -44.008  15.511  1.00 89.82           O  
ANISOU 2020  OE2 GLU A 376     9750  11849  12529  -1223   1783    321       O  
ATOM   2021  N   VAL A 377     -28.461 -45.796  13.491  1.00 61.08           N  
ANISOU 2021  N   VAL A 377     7139   7668   8401   -786    863   1040       N  
ATOM   2022  CA  VAL A 377     -27.474 -45.833  12.406  1.00 58.73           C  
ANISOU 2022  CA  VAL A 377     6947   7233   8134   -621    633   1012       C  
ATOM   2023  C   VAL A 377     -26.353 -46.841  12.747  1.00 63.02           C  
ANISOU 2023  C   VAL A 377     7666   7680   8597   -656    544   1228       C  
ATOM   2024  O   VAL A 377     -26.044 -47.711  11.931  1.00 61.45           O  
ANISOU 2024  O   VAL A 377     7487   7298   8565   -623    389   1251       O  
ATOM   2025  CB  VAL A 377     -26.916 -44.416  12.041  1.00 60.16           C  
ANISOU 2025  CB  VAL A 377     7172   7505   8182   -452    582    853       C  
ATOM   2026  CG1 VAL A 377     -25.777 -44.504  11.032  1.00 57.41           C  
ANISOU 2026  CG1 VAL A 377     6952   7036   7825   -320    388    840       C  
ATOM   2027  CG2 VAL A 377     -28.006 -43.484  11.521  1.00 59.70           C  
ANISOU 2027  CG2 VAL A 377     6945   7481   8256   -392    599    635       C  
ATOM   2028  N   LEU A 378     -25.784 -46.743  13.960  1.00 61.36           N  
ANISOU 2028  N   LEU A 378     7579   7588   8147   -723    629   1373       N  
ATOM   2029  CA  LEU A 378     -24.707 -47.625  14.438  1.00 62.12           C  
ANISOU 2029  CA  LEU A 378     7848   7592   8163   -750    518   1582       C  
ATOM   2030  C   LEU A 378     -25.129 -49.103  14.541  1.00 68.63           C  
ANISOU 2030  C   LEU A 378     8673   8239   9165   -900    485   1769       C  
ATOM   2031  O   LEU A 378     -24.283 -49.998  14.441  1.00 69.83           O  
ANISOU 2031  O   LEU A 378     8932   8222   9379   -879    312   1895       O  
ATOM   2032  CB  LEU A 378     -24.163 -47.125  15.793  1.00 62.99           C  
ANISOU 2032  CB  LEU A 378     8093   7883   7959   -800    609   1691       C  
ATOM   2033  CG  LEU A 378     -23.418 -45.783  15.789  1.00 64.89           C  
ANISOU 2033  CG  LEU A 378     8365   8264   8026   -647    598   1533       C  
ATOM   2034  CD1 LEU A 378     -23.489 -45.125  17.160  1.00 65.58           C  
ANISOU 2034  CD1 LEU A 378     8514   8578   7825   -731    760   1574       C  
ATOM   2035  CD2 LEU A 378     -21.974 -45.957  15.349  1.00 64.54           C  
ANISOU 2035  CD2 LEU A 378     8434   8105   7983   -512    390   1546       C  
ATOM   2036  N   GLU A 379     -26.440 -49.343  14.720  1.00 65.72           N  
ANISOU 2036  N   GLU A 379     8169   7895   8907  -1050    645   1768       N  
ATOM   2037  CA  GLU A 379     -27.040 -50.666  14.853  1.00 68.18           C  
ANISOU 2037  CA  GLU A 379     8456   8042   9407  -1224    650   1936       C  
ATOM   2038  C   GLU A 379     -27.685 -51.159  13.557  1.00 69.09           C  
ANISOU 2038  C   GLU A 379     8403   7978   9870  -1173    548   1788       C  
ATOM   2039  O   GLU A 379     -28.370 -52.180  13.588  1.00 70.90           O  
ANISOU 2039  O   GLU A 379     8568   8068  10302  -1324    568   1888       O  
ATOM   2040  CB  GLU A 379     -28.124 -50.639  15.949  1.00 73.09           C  
ANISOU 2040  CB  GLU A 379     9021   8818   9932  -1459    928   2022       C  
ATOM   2041  CG  GLU A 379     -27.623 -50.427  17.367  1.00 89.15           C  
ANISOU 2041  CG  GLU A 379    11248  11021  11603  -1570   1040   2212       C  
ATOM   2042  CD  GLU A 379     -28.576 -49.675  18.281  1.00118.26           C  
ANISOU 2042  CD  GLU A 379    14846  14976  15113  -1719   1353   2141       C  
ATOM   2043  OE1 GLU A 379     -29.806 -49.922  18.233  1.00 83.48           O  
ANISOU 2043  OE1 GLU A 379    10253  10579  10885  -1868   1530   2079       O  
ATOM   2044  OE2 GLU A 379     -28.078 -48.822  19.050  1.00129.67           O  
ANISOU 2044  OE2 GLU A 379    16394  16625  16251  -1686   1423   2122       O  
ATOM   2045  N   HIS A 380     -27.528 -50.430  12.436  1.00 60.81           N  
ANISOU 2045  N   HIS A 380     7287   6932   8885   -978    442   1552       N  
ATOM   2046  CA  HIS A 380     -28.136 -50.834  11.171  1.00 58.66           C  
ANISOU 2046  CA  HIS A 380     6873   6505   8908   -922    325   1393       C  
ATOM   2047  C   HIS A 380     -27.467 -52.137  10.680  1.00 64.45           C  
ANISOU 2047  C   HIS A 380     7679   6995   9814   -913    128   1490       C  
ATOM   2048  O   HIS A 380     -26.238 -52.241  10.817  1.00 63.90           O  
ANISOU 2048  O   HIS A 380     7761   6895   9622   -834     23   1564       O  
ATOM   2049  CB  HIS A 380     -28.017 -49.710  10.133  1.00 55.89           C  
ANISOU 2049  CB  HIS A 380     6488   6220   8527   -725    241   1146       C  
ATOM   2050  CG  HIS A 380     -28.825 -49.959   8.902  1.00 57.76           C  
ANISOU 2050  CG  HIS A 380     6583   6334   9028   -675    126    969       C  
ATOM   2051  ND1 HIS A 380     -28.330 -50.715   7.868  1.00 58.20           N  
ANISOU 2051  ND1 HIS A 380     6678   6215   9222   -599    -69    921       N  
ATOM   2052  CD2 HIS A 380     -30.076 -49.554   8.592  1.00 58.92           C  
ANISOU 2052  CD2 HIS A 380     6547   6512   9329   -691    172    815       C  
ATOM   2053  CE1 HIS A 380     -29.291 -50.763   6.967  1.00 57.29           C  
ANISOU 2053  CE1 HIS A 380     6421   6032   9314   -575   -142    755       C  
ATOM   2054  NE2 HIS A 380     -30.348 -50.048   7.347  1.00 58.24           N  
ANISOU 2054  NE2 HIS A 380     6402   6267   9459   -620    -15    685       N  
ATOM   2055  N   PRO A 381     -28.236 -53.131  10.141  1.00 63.32           N  
ANISOU 2055  N   PRO A 381     7415   6670   9974   -989     71   1474       N  
ATOM   2056  CA  PRO A 381     -27.620 -54.409   9.722  1.00 64.62           C  
ANISOU 2056  CA  PRO A 381     7635   6584  10333   -981   -124   1552       C  
ATOM   2057  C   PRO A 381     -26.538 -54.298   8.653  1.00 67.79           C  
ANISOU 2057  C   PRO A 381     8099   6924  10733   -774   -320   1388       C  
ATOM   2058  O   PRO A 381     -25.652 -55.148   8.592  1.00 67.90           O  
ANISOU 2058  O   PRO A 381     8193   6775  10831   -745   -468   1458       O  
ATOM   2059  CB  PRO A 381     -28.814 -55.246   9.238  1.00 68.87           C  
ANISOU 2059  CB  PRO A 381     7996   6966  11205  -1090   -134   1501       C  
ATOM   2060  CG  PRO A 381     -29.886 -54.244   8.921  1.00 73.08           C  
ANISOU 2060  CG  PRO A 381     8369   7662  11736  -1069    -15   1304       C  
ATOM   2061  CD  PRO A 381     -29.701 -53.163   9.943  1.00 67.76           C  
ANISOU 2061  CD  PRO A 381     7769   7235  10743  -1088    173   1372       C  
ATOM   2062  N   TRP A 382     -26.600 -53.253   7.819  1.00 62.55           N  
ANISOU 2062  N   TRP A 382     7401   6386   9978   -637   -324   1167       N  
ATOM   2063  CA  TRP A 382     -25.598 -53.042   6.790  1.00 60.00           C  
ANISOU 2063  CA  TRP A 382     7148   6038   9613   -468   -469   1003       C  
ATOM   2064  C   TRP A 382     -24.319 -52.513   7.438  1.00 61.15           C  
ANISOU 2064  C   TRP A 382     7439   6282   9511   -409   -447   1084       C  
ATOM   2065  O   TRP A 382     -23.221 -52.902   7.043  1.00 57.95           O  
ANISOU 2065  O   TRP A 382     7098   5791   9130   -323   -569   1038       O  
ATOM   2066  CB  TRP A 382     -26.141 -52.099   5.712  1.00 57.92           C  
ANISOU 2066  CB  TRP A 382     6829   5865   9314   -368   -487    771       C  
ATOM   2067  CG  TRP A 382     -25.181 -51.890   4.581  1.00 57.53           C  
ANISOU 2067  CG  TRP A 382     6864   5799   9194   -226   -612    599       C  
ATOM   2068  CD1 TRP A 382     -24.968 -52.728   3.524  1.00 60.84           C  
ANISOU 2068  CD1 TRP A 382     7264   6071   9782   -180   -761    463       C  
ATOM   2069  CD2 TRP A 382     -24.245 -50.807   4.434  1.00 55.03           C  
ANISOU 2069  CD2 TRP A 382     6665   5625   8619   -129   -580    540       C  
ATOM   2070  NE1 TRP A 382     -23.990 -52.216   2.707  1.00 58.99           N  
ANISOU 2070  NE1 TRP A 382     7130   5895   9390    -69   -807    315       N  
ATOM   2071  CE2 TRP A 382     -23.529 -51.035   3.238  1.00 58.16           C  
ANISOU 2071  CE2 TRP A 382     7109   5960   9028    -41   -696    367       C  
ATOM   2072  CE3 TRP A 382     -23.964 -49.648   5.184  1.00 55.32           C  
ANISOU 2072  CE3 TRP A 382     6764   5834   8420   -116   -459    601       C  
ATOM   2073  CZ2 TRP A 382     -22.532 -50.158   2.778  1.00 55.60           C  
ANISOU 2073  CZ2 TRP A 382     6898   5743   8487     41   -678    270       C  
ATOM   2074  CZ3 TRP A 382     -22.970 -48.776   4.733  1.00 55.15           C  
ANISOU 2074  CZ3 TRP A 382     6851   5900   8204    -22   -464    508       C  
ATOM   2075  CH2 TRP A 382     -22.251 -49.046   3.555  1.00 55.23           C  
ANISOU 2075  CH2 TRP A 382     6910   5846   8230     47   -564    352       C  
ATOM   2076  N   ILE A 383     -24.474 -51.657   8.471  1.00 59.23           N  
ANISOU 2076  N   ILE A 383     7234   6220   9050   -458   -291   1187       N  
ATOM   2077  CA  ILE A 383     -23.363 -51.089   9.238  1.00 57.79           C  
ANISOU 2077  CA  ILE A 383     7184   6147   8628   -414   -266   1267       C  
ATOM   2078  C   ILE A 383     -22.670 -52.191  10.044  1.00 63.14           C  
ANISOU 2078  C   ILE A 383     7948   6685   9356   -478   -353   1478       C  
ATOM   2079  O   ILE A 383     -21.480 -52.417   9.853  1.00 61.20           O  
ANISOU 2079  O   ILE A 383     7770   6368   9114   -382   -484   1449       O  
ATOM   2080  CB  ILE A 383     -23.817 -49.879  10.113  1.00 59.51           C  
ANISOU 2080  CB  ILE A 383     7407   6595   8609   -451    -81   1292       C  
ATOM   2081  CG1 ILE A 383     -24.154 -48.630   9.245  1.00 58.03           C  
ANISOU 2081  CG1 ILE A 383     7166   6519   8366   -342    -55   1070       C  
ATOM   2082  CG2 ILE A 383     -22.805 -49.549  11.250  1.00 58.28           C  
ANISOU 2082  CG2 ILE A 383     7390   6540   8215   -452    -53   1428       C  
ATOM   2083  CD1 ILE A 383     -23.001 -48.051   8.364  1.00 53.32           C  
ANISOU 2083  CD1 ILE A 383     6653   5925   7680   -193   -155    931       C  
ATOM   2084  N   THR A 384     -23.423 -52.889  10.920  1.00 64.13           N  
ANISOU 2084  N   THR A 384     8070   6762   9534   -648   -288   1683       N  
ATOM   2085  CA  THR A 384     -22.896 -53.968  11.778  1.00 66.46           C  
ANISOU 2085  CA  THR A 384     8478   6903   9871   -737   -388   1931       C  
ATOM   2086  C   THR A 384     -22.192 -55.079  10.961  1.00 70.45           C  
ANISOU 2086  C   THR A 384     8969   7141  10659   -653   -627   1876       C  
ATOM   2087  O   THR A 384     -21.143 -55.566  11.397  1.00 71.32           O  
ANISOU 2087  O   THR A 384     9183   7143  10774   -613   -779   1979       O  
ATOM   2088  CB  THR A 384     -23.974 -54.515  12.723  1.00 74.88           C  
ANISOU 2088  CB  THR A 384     9545   7960  10947   -967   -253   2156       C  
ATOM   2089  OG1 THR A 384     -25.029 -55.052  11.945  1.00 80.68           O  
ANISOU 2089  OG1 THR A 384    10117   8578  11957  -1024   -237   2065       O  
ATOM   2090  CG2 THR A 384     -24.531 -53.450  13.677  1.00 74.05           C  
ANISOU 2090  CG2 THR A 384     9457   8134  10545  -1056     -8   2195       C  
ATOM   2091  N   ALA A 385     -22.720 -55.415   9.752  1.00 64.31           N  
ANISOU 2091  N   ALA A 385     8057   6262  10116   -610   -673   1684       N  
ATOM   2092  CA  ALA A 385     -22.135 -56.435   8.869  1.00 64.57           C  
ANISOU 2092  CA  ALA A 385     8049   6055  10428   -525   -885   1574       C  
ATOM   2093  C   ALA A 385     -20.866 -56.001   8.098  1.00 69.05           C  
ANISOU 2093  C   ALA A 385     8635   6658  10945   -336   -978   1351       C  
ATOM   2094  O   ALA A 385     -20.132 -56.866   7.613  1.00 69.68           O  
ANISOU 2094  O   ALA A 385     8691   6545  11240   -264  -1154   1266       O  
ATOM   2095  CB  ALA A 385     -23.184 -56.942   7.887  1.00 65.23           C  
ANISOU 2095  CB  ALA A 385     7987   6033  10763   -556   -900   1434       C  
ATOM   2096  N   ASN A 386     -20.593 -54.714   8.013  1.00 63.80           N  
ANISOU 2096  N   ASN A 386     7997   6226  10018   -262   -858   1237       N  
ATOM   2097  CA  ASN A 386     -19.457 -54.261   7.236  1.00 62.03           C  
ANISOU 2097  CA  ASN A 386     7783   6045   9739   -112   -911   1016       C  
ATOM   2098  C   ASN A 386     -18.438 -53.396   7.959  1.00 65.34           C  
ANISOU 2098  C   ASN A 386     8296   6608   9924    -60   -870   1060       C  
ATOM   2099  O   ASN A 386     -17.388 -53.162   7.446  1.00 64.53           O  
ANISOU 2099  O   ASN A 386     8190   6496   9832     46   -933    900       O  
ATOM   2100  CB  ASN A 386     -19.930 -53.515   6.012  1.00 58.10           C  
ANISOU 2100  CB  ASN A 386     7235   5654   9188    -59   -844    782       C  
ATOM   2101  CG  ASN A 386     -20.639 -54.390   5.032  1.00 69.24           C  
ANISOU 2101  CG  ASN A 386     8550   6908  10848    -72   -934    665       C  
ATOM   2102  OD1 ASN A 386     -20.021 -55.100   4.272  1.00 65.00           O  
ANISOU 2102  OD1 ASN A 386     7978   6235  10486     -9  -1058    512       O  
ATOM   2103  ND2 ASN A 386     -21.939 -54.312   5.019  1.00 57.69           N  
ANISOU 2103  ND2 ASN A 386     7030   5467   9423   -152   -874    707       N  
ATOM   2104  N   SER A 387     -18.753 -52.921   9.143  1.00 64.54           N  
ANISOU 2104  N   SER A 387     8264   6639   9621   -138   -763   1253       N  
ATOM   2105  CA  SER A 387     -17.873 -52.025   9.877  1.00 66.24           C  
ANISOU 2105  CA  SER A 387     8568   7000   9600    -95   -728   1296       C  
ATOM   2106  C   SER A 387     -16.726 -52.710  10.635  1.00 80.13           C  
ANISOU 2106  C   SER A 387    10390   8620  11434    -54   -914   1392       C  
ATOM   2107  O   SER A 387     -16.555 -53.898  10.530  1.00 81.18           O  
ANISOU 2107  O   SER A 387    10487   8530  11827    -35  -1080   1386       O  
ATOM   2108  CB  SER A 387     -18.716 -51.223  10.838  1.00 67.62           C  
ANISOU 2108  CB  SER A 387     8792   7356   9545   -199   -562   1453       C  
ATOM   2109  OG  SER A 387     -17.978 -50.166  11.353  1.00 70.21           O  
ANISOU 2109  OG  SER A 387     9190   7852   9633   -148   -512   1442       O  
ATOM   2110  N   SER A 388     -15.945 -51.949  11.400  1.00 83.04           N  
ANISOU 2110  N   SER A 388    10846   9112  11593    -29   -905   1459       N  
ATOM   2111  CA  SER A 388     -14.868 -52.490  12.251  1.00 86.24           C  
ANISOU 2111  CA  SER A 388    11320   9412  12036     22  -1097   1545       C  
ATOM   2112  C   SER A 388     -14.876 -51.938  13.695  1.00 98.18           C  
ANISOU 2112  C   SER A 388    12974  11073  13257    -48  -1054   1760       C  
ATOM   2113  O   SER A 388     -15.542 -50.941  13.966  1.00 96.76           O  
ANISOU 2113  O   SER A 388    12808  11112  12846    -99   -851   1757       O  
ATOM   2114  CB  SER A 388     -13.517 -52.224  11.611  1.00 87.39           C  
ANISOU 2114  CB  SER A 388    11390   9562  12250    173  -1157   1279       C  
ATOM   2115  OG  SER A 388     -13.532 -52.561  10.244  1.00 90.45           O  
ANISOU 2115  OG  SER A 388    11660   9836  12871    225  -1179   1065       O  
ATOM   2116  N   LYS A 389     -14.133 -52.588  14.609  1.00102.22           N  
ANISOU 2116  N   LYS A 389    13594  11461  13783    -50  -1261   1939       N  
ATOM   2117  CA  LYS A 389     -14.052 -52.210  16.037  1.00105.69           C  
ANISOU 2117  CA  LYS A 389    14200  12029  13929   -122  -1261   2155       C  
ATOM   2118  C   LYS A 389     -12.606 -52.184  16.624  1.00114.31           C  
ANISOU 2118  C   LYS A 389    15356  13068  15008     -3  -1498   2141       C  
ATOM   2119  O   LYS A 389     -11.779 -52.997  16.197  1.00114.81           O  
ANISOU 2119  O   LYS A 389    15363  12905  15356     96  -1728   2071       O  
ATOM   2120  CB  LYS A 389     -14.961 -53.116  16.887  1.00112.01           C  
ANISOU 2120  CB  LYS A 389    15132  12746  14683   -310  -1269   2478       C  
ATOM   2121  CG  LYS A 389     -16.383 -52.578  17.040  1.00134.67           C  
ANISOU 2121  CG  LYS A 389    17983  15813  17373   -462   -967   2525       C  
ATOM   2122  CD  LYS A 389     -16.612 -51.871  18.382  1.00148.86           C  
ANISOU 2122  CD  LYS A 389    19929  17847  18784   -570   -838   2677       C  
ATOM   2123  CE  LYS A 389     -17.234 -52.783  19.414  1.00166.05           C  
ANISOU 2123  CE  LYS A 389    22274  19959  20859   -784   -845   3013       C  
ATOM   2124  NZ  LYS A 389     -17.594 -52.049  20.654  1.00177.37           N  
ANISOU 2124  NZ  LYS A 389    23843  21664  21887   -912   -665   3127       N  
ATOM   2125  N   PRO A 390     -12.296 -51.291  17.614  1.00113.40           N  
ANISOU 2125  N   PRO A 390    15347  13152  14587     -9  -1460   2191       N  
ATOM   2126  CA  PRO A 390     -10.924 -51.244  18.180  1.00119.45           C  
ANISOU 2126  CA  PRO A 390    16163  13867  15357    111  -1707   2160       C  
ATOM   2127  C   PRO A 390     -10.454 -52.518  18.884  1.00151.81           C  
ANISOU 2127  C   PRO A 390    20394  17709  19578     99  -2038   2396       C  
ATOM   2128  O   PRO A 390      -9.251 -52.724  19.053  1.00111.75           O  
ANISOU 2128  O   PRO A 390    15308  12512  14640    232  -2303   2321       O  
ATOM   2129  CB  PRO A 390     -10.981 -50.066  19.164  1.00120.41           C  
ANISOU 2129  CB  PRO A 390    16388  14266  15095     73  -1577   2191       C  
ATOM   2130  CG  PRO A 390     -12.429 -49.911  19.498  1.00123.63           C  
ANISOU 2130  CG  PRO A 390    16860  14821  15293   -105  -1321   2347       C  
ATOM   2131  CD  PRO A 390     -13.153 -50.250  18.224  1.00116.32           C  
ANISOU 2131  CD  PRO A 390    15774  13802  14619   -112  -1198   2236       C  
TER    2132      PRO A 390                                                      
HETATM 2133  S   SKE A 401      -2.395 -33.946   1.449  1.00 59.71           S  
HETATM 2134  C1  SKE A 401      -4.975 -30.784   9.283  1.00 46.39           C  
HETATM 2135  F1  SKE A 401      -4.880 -28.579   5.573  1.00 51.73           F  
HETATM 2136  N1  SKE A 401      -5.117 -30.197  10.500  1.00 41.54           N  
HETATM 2137  O1  SKE A 401      -0.975 -33.891   1.316  1.00 63.10           O  
HETATM 2138  C2  SKE A 401      -4.138 -31.944   7.740  1.00 46.08           C  
HETATM 2139  F2  SKE A 401      -9.118 -29.756   7.426  1.00 51.81           F  
HETATM 2140  N2  SKE A 401      -4.098 -31.794   9.090  1.00 44.73           N  
HETATM 2141  O2  SKE A 401      -2.919 -32.967   0.572  1.00 55.97           O  
HETATM 2142  C3  SKE A 401      -3.245 -33.130   5.767  1.00 49.24           C  
HETATM 2143  N3  SKE A 401      -3.495 -32.966   7.103  1.00 50.33           N  
HETATM 2144  O3  SKE A 401      -6.732 -28.579   8.812  1.00 57.98           O  
HETATM 2145  C4  SKE A 401      -2.276 -34.084   5.400  1.00 48.24           C  
HETATM 2146  N4  SKE A 401      -2.946 -35.375   1.036  1.00 63.28           N  
HETATM 2147  C5  SKE A 401      -2.022 -34.332   4.040  1.00 46.59           C  
HETATM 2148  N5  SKE A 401      -4.938 -31.078   7.099  1.00 46.80           N  
HETATM 2149  C6  SKE A 401      -2.733 -33.657   3.021  1.00 53.17           C  
HETATM 2150  N6  SKE A 401      -5.312 -30.210   8.126  1.00 49.69           N  
HETATM 2151  C7  SKE A 401      -3.676 -32.681   3.398  1.00 51.47           C  
HETATM 2152  C8  SKE A 401      -3.941 -32.438   4.751  1.00 48.76           C  
HETATM 2153  C9  SKE A 401      -6.318 -29.284   7.909  1.00 52.86           C  
HETATM 2154  C10 SKE A 401      -6.952 -29.171   6.545  1.00 51.73           C  
HETATM 2155  C11 SKE A 401      -6.172 -28.856   5.424  1.00 50.46           C  
HETATM 2156  C12 SKE A 401      -6.714 -28.791   4.142  1.00 50.35           C  
HETATM 2157  C13 SKE A 401      -8.085 -29.020   3.989  1.00 52.34           C  
HETATM 2158  C14 SKE A 401      -8.874 -29.377   5.091  1.00 51.66           C  
HETATM 2159  C15 SKE A 401      -8.320 -29.430   6.377  1.00 53.33           C  
HETATM 2160  O   HOH A 501     -17.330 -12.483  17.097  1.00 72.35           O  
HETATM 2161  O   HOH A 502     -33.252 -30.190  11.376  1.00 54.40           O  
HETATM 2162  O   HOH A 503      -8.775 -44.599   6.055  1.00 52.21           O  
HETATM 2163  O   HOH A 504     -35.515 -41.147   1.270  1.00 60.80           O  
HETATM 2164  O   HOH A 505      -3.702 -42.305  14.978  1.00 70.79           O  
HETATM 2165  O   HOH A 506     -17.090 -32.859  -1.932  1.00 54.49           O  
HETATM 2166  O   HOH A 507     -18.795 -48.739  -3.950  1.00 53.08           O  
HETATM 2167  O   HOH A 508      -3.999 -36.787  13.766  1.00 46.53           O  
HETATM 2168  O   HOH A 509      -5.591  -9.317   6.955  1.00 65.05           O  
HETATM 2169  O   HOH A 510     -27.930 -32.414   0.256  1.00 43.56           O  
HETATM 2170  O   HOH A 511      -8.459 -36.030  17.692  1.00 46.30           O  
HETATM 2171  O   HOH A 512     -30.472 -49.274  -9.511  1.00 61.66           O  
HETATM 2172  O   HOH A 513     -16.945 -36.945  -5.405  1.00 77.13           O  
HETATM 2173  O   HOH A 514     -28.661 -43.667 -10.496  1.00 62.27           O  
HETATM 2174  O   HOH A 515     -13.511 -36.262  -3.700  1.00 60.31           O  
HETATM 2175  O   HOH A 516     -17.794 -34.586  -6.409  1.00 76.67           O  
HETATM 2176  O   HOH A 517     -28.915 -39.379  -7.512  1.00 49.06           O  
HETATM 2177  O   HOH A 518     -15.093 -39.926  -6.592  1.00 56.73           O  
HETATM 2178  O   HOH A 519     -11.495 -45.717   9.295  1.00 49.59           O  
HETATM 2179  O   HOH A 520     -19.340 -29.175 -12.862  1.00 81.19           O  
HETATM 2180  O   HOH A 521     -40.298 -34.601  -4.621  1.00 56.92           O  
HETATM 2181  O   HOH A 522      -9.110 -26.925   9.198  1.00 57.70           O  
HETATM 2182  O   HOH A 523      -6.021 -38.316   1.776  1.00 51.90           O  
HETATM 2183  O   HOH A 524     -23.725 -31.484   8.414  1.00 47.87           O  
HETATM 2184  O   HOH A 525     -15.793 -35.137  -2.708  1.00 61.46           O  
HETATM 2185  O   HOH A 526     -11.990 -27.755   4.556  1.00 62.94           O  
HETATM 2186  O   HOH A 527     -36.246 -42.390  14.752  1.00 80.09           O  
HETATM 2187  O   HOH A 528     -11.219 -33.988  19.851  1.00 51.23           O  
HETATM 2188  O   HOH A 529     -27.175 -33.344 -12.620  1.00 55.56           O  
HETATM 2189  O   HOH A 530      13.755 -27.545  17.462  1.00 68.98           O  
HETATM 2190  O   HOH A 531      10.553 -33.903  21.826  1.00 58.73           O  
HETATM 2191  O   HOH A 532     -30.183 -39.279 -10.357  1.00 82.39           O  
HETATM 2192  O   HOH A 533     -22.948 -28.546   1.228  1.00 49.55           O  
HETATM 2193  O   HOH A 534     -37.897 -32.070 -10.800  1.00 62.94           O  
HETATM 2194  O   HOH A 535     -25.427 -37.555  -8.467  1.00 58.76           O  
HETATM 2195  O   HOH A 536      -0.119 -35.752  14.281  1.00 54.19           O  
HETATM 2196  O   HOH A 537     -19.085 -26.392  11.197  1.00 46.64           O  
HETATM 2197  O   HOH A 538     -11.448 -31.266  19.516  1.00 48.32           O  
HETATM 2198  O   HOH A 539     -29.106 -39.152  17.305  1.00 69.16           O  
HETATM 2199  O   HOH A 540      -0.560 -32.804  15.768  1.00 43.76           O  
HETATM 2200  O   HOH A 541     -31.265 -51.991 -12.774  1.00 62.69           O  
HETATM 2201  O   HOH A 542     -19.278 -12.307  12.709  1.00 59.59           O  
HETATM 2202  O   HOH A 543     -25.486 -33.902  -3.292  1.00 49.65           O  
HETATM 2203  O   HOH A 544       6.297 -23.270   3.232  1.00 58.01           O  
HETATM 2204  O   HOH A 545     -39.269 -27.719  -5.235  1.00 64.38           O  
HETATM 2205  O   HOH A 546     -15.858 -34.544  26.890  1.00 68.53           O  
HETATM 2206  O   HOH A 547     -29.137 -53.821  -5.258  1.00 69.07           O  
HETATM 2207  O   HOH A 548     -12.403 -49.008  -0.576  1.00 52.26           O  
HETATM 2208  O   HOH A 549     -11.727 -51.949   2.879  1.00 76.19           O  
HETATM 2209  O   HOH A 550     -38.918 -37.911   2.275  1.00 59.15           O  
HETATM 2210  O   HOH A 551     -23.144 -30.481   5.605  1.00 66.25           O  
HETATM 2211  O   HOH A 552     -26.870 -55.374   1.986  1.00 84.48           O  
HETATM 2212  O   HOH A 553     -14.837 -25.615   6.048  1.00 72.89           O  
HETATM 2213  O   HOH A 554     -11.366 -44.197  15.627  1.00 67.42           O  
HETATM 2214  O   HOH A 555     -25.848 -57.764  10.136  1.00 75.94           O  
HETATM 2215  O   HOH A 556     -23.351 -50.781  -1.849  1.00 56.76           O  
HETATM 2216  O   HOH A 557     -37.356 -45.306   3.413  1.00 72.46           O  
HETATM 2217  O   HOH A 558      -2.956 -39.180  14.062  1.00 52.76           O  
HETATM 2218  O   HOH A 559      -5.753 -30.969   0.727  1.00 78.02           O  
HETATM 2219  O   HOH A 560     -31.123 -17.905  -9.314  1.00 63.12           O  
HETATM 2220  O   HOH A 561     -10.321 -50.055   0.905  1.00 78.90           O  
HETATM 2221  O   HOH A 562      -9.872 -20.594   4.332  1.00 79.40           O  
HETATM 2222  O   HOH A 563     -18.665 -49.886 -11.120  1.00 82.91           O  
HETATM 2223  O   HOH A 564      -9.835 -47.985  -5.968  1.00 79.31           O  
HETATM 2224  O   HOH A 565     -20.601 -46.967  19.973  1.00 74.64           O  
HETATM 2225  O   HOH A 566      -8.962 -31.304   0.152  1.00 60.04           O  
HETATM 2226  O   HOH A 567     -22.248 -28.595   3.874  1.00 52.13           O  
HETATM 2227  O   HOH A 568     -11.850 -21.459   8.879  1.00 81.20           O  
HETATM 2228  O   HOH A 569      -3.380  -7.479  16.414  1.00 72.73           O  
HETATM 2229  O   HOH A 570     -11.151 -23.531  29.712  1.00 83.38           O  
HETATM 2230  O   HOH A 571     -26.712 -24.664  14.913  1.00 76.75           O  
HETATM 2231  O   HOH A 572     -12.104 -50.486   6.561  1.00 77.28           O  
HETATM 2232  O   HOH A 573      -2.565 -44.546  16.000  1.00 85.83           O  
HETATM 2233  O   HOH A 574     -13.309 -48.340  -7.633  1.00 81.69           O  
HETATM 2234  O   HOH A 575      -0.675 -17.343   4.548  1.00 74.21           O  
HETATM 2235  O   HOH A 576      -9.629 -25.418   5.734  1.00 69.25           O  
HETATM 2236  O   HOH A 577     -21.122 -50.524  -3.374  1.00 62.94           O  
HETATM 2237  O   HOH A 578     -13.585 -19.810  10.187  1.00 98.06           O  
HETATM 2238  O   HOH A 579       2.880  -7.882  14.317  1.00 79.49           O  
HETATM 2239  O   HOH A 580     -13.723 -37.572  -6.273  1.00 73.19           O  
HETATM 2240  O   HOH A 581     -27.501 -39.168  -9.990  1.00 87.13           O  
HETATM 2241  O   HOH A 582     -25.990 -41.390 -10.403  1.00 79.74           O  
HETATM 2242  O   HOH A 583     -21.394 -24.249   3.331  1.00 91.68           O  
HETATM 2243  O   HOH A 584     -38.820 -26.818 -12.730  1.00 69.65           O  
HETATM 2244  O   HOH A 585     -27.969 -41.165  19.852  1.00 81.58           O  
HETATM 2245  O   HOH A 586       2.016  -8.182   9.954  1.00 86.55           O  
HETATM 2246  O   HOH A 587     -18.309 -31.537  -3.970  1.00 81.15           O  
HETATM 2247  O   HOH A 588     -18.544 -51.418  -8.426  1.00 91.03           O  
HETATM 2248  O   HOH A 589      -0.577 -38.290   2.233  1.00 85.08           O  
HETATM 2249  O   HOH A 590     -26.815 -55.803   4.770  1.00 72.49           O  
HETATM 2250  O   HOH A 591     -21.844 -40.111  23.500  1.00 72.35           O  
HETATM 2251  O   HOH A 592      -7.615 -25.137   3.880  1.00 65.17           O  
HETATM 2252  O   HOH A 593     -22.444 -49.997  18.036  1.00 75.62           O  
HETATM 2253  O   HOH A 594     -17.019 -41.561 -10.070  1.00 85.23           O  
HETATM 2254  O   HOH A 595     -33.037 -28.579 -12.132  1.00 66.27           O  
HETATM 2255  O   HOH A 596     -17.831 -26.951  23.579  1.00 70.69           O  
HETATM 2256  O   HOH A 597     -25.225 -17.989  -4.049  1.00 80.00           O  
HETATM 2257  O   HOH A 598       2.502 -17.874   7.023  1.00 82.69           O  
HETATM 2258  O   HOH A 599     -37.977 -33.417 -13.312  1.00 72.86           O  
HETATM 2259  O   HOH A 600       2.160 -28.386  22.073  1.00 72.62           O  
HETATM 2260  O   HOH A 601     -32.163 -21.041  -5.785  1.00 71.43           O  
HETATM 2261  O   HOH A 602     -31.191 -66.868   6.682  1.00 83.71           O  
CONECT 2133 2137 2141 2146 2149                                                 
CONECT 2134 2136 2140 2150                                                      
CONECT 2135 2155                                                                
CONECT 2136 2134                                                                
CONECT 2137 2133                                                                
CONECT 2138 2140 2143 2148                                                      
CONECT 2139 2159                                                                
CONECT 2140 2134 2138                                                           
CONECT 2141 2133                                                                
CONECT 2142 2143 2145 2152                                                      
CONECT 2143 2138 2142                                                           
CONECT 2144 2153                                                                
CONECT 2145 2142 2147                                                           
CONECT 2146 2133                                                                
CONECT 2147 2145 2149                                                           
CONECT 2148 2138 2150                                                           
CONECT 2149 2133 2147 2151                                                      
CONECT 2150 2134 2148 2153                                                      
CONECT 2151 2149 2152                                                           
CONECT 2152 2142 2151                                                           
CONECT 2153 2144 2150 2154                                                      
CONECT 2154 2153 2155 2159                                                      
CONECT 2155 2135 2154 2156                                                      
CONECT 2156 2155 2157                                                           
CONECT 2157 2156 2158                                                           
CONECT 2158 2157 2159                                                           
CONECT 2159 2139 2154 2158                                                      
MASTER      365    0    1   14    9    0    4    6 2249    1   27   21          
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.