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***  MEMBRANE PROTEIN 28-DEC-19 6LN2  ***

elNémo ID: 22033117492247294

Job options:

ID        	=	 22033117492247294
JOBID     	=	 MEMBRANE PROTEIN 28-DEC-19 6LN2
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:


REMARK    File generated by Swiss-PdbViewer  4.00b0
REMARK    http://www.expasy.org/spdbv/
REMARK    File generated by Swiss-PdbViewer  4.00b0
REMARK    http://www.expasy.org/spdbv/
HEADER    MEMBRANE PROTEIN                        28-DEC-19   6LN2              
TITLE     CRYSTAL STRUCTURE OF FULL LENGTH HUMAN GLP1 RECEPTOR IN COMPLEX WITH  
TITLE    2 FAB FRAGMENT (FAB7F38)                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUCAGON-LIKE PEPTIDE 1 RECEPTOR,RUBREDOXIN,GLUCAGON-LIKE  
COMPND   3 PEPTIDE 1 RECEPTOR;                                                  
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: GLP-1R,RD,GLP-1R;                                           
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 OTHER_DETAILS: THE FUSION PROTEIN OF GLP1 RECEPTOR (UNP RESIDUES 24- 
COMPND   9 260), RUBREDOXIN (UNP RESIDUES 1-54) AND GLP1 RECEPTOR (UNP RESIDUES 
COMPND  10 262-439);                                                            
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: FAB7F38_LIGHT CHAIN;                                       
COMPND  13 CHAIN: B;                                                            
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: FAB7F38_HEAVY CHAIN;                                       
COMPND  17 CHAIN: C;                                                            
COMPND  18 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, CLOSTRIDIUM PASTEURIANUM;         
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606, 1501;                                          
SOURCE   5 GENE: GLP1R;                                                         
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  10 ORGANISM_TAXID: 10090;                                               
SOURCE  11 EXPRESSION_SYSTEM: MUS MUSCULUS;                                     
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 10090;                                      
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  15 ORGANISM_TAXID: 10090;                                               
SOURCE  16 EXPRESSION_SYSTEM: MUS MUSCULUS;                                     
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 10090                                       
KEYWDS    FULL LENGTH HUMAN GLP1 RECEPTOR, CLASS B, FAB7F38, TMD, NAM           
KEYWDS   2 PF06372222, MEMBRANE PROTEIN, LCP                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.WU,L.YANG,K.HANG,M.LAURSEN,L.WU,G.W.HAN,Q.REN,N.K.ROED,G.LIN,       
AUTHOR   2 M.HANSON,H.JIANG,M.WANG,S.REEDTZ-RUNGE,G.SONG,R.C.STEVENS            
REVDAT   3   29-JUL-20 6LN2    1       COMPND REMARK HETNAM LINK                
REVDAT   3 2                   1       SITE                                     
REVDAT   2   25-MAR-20 6LN2    1       JRNL                                     
REVDAT   1   18-MAR-20 6LN2    0                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.2                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 21990                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.215                          
REMARK   3   R VALUE            (WORKING SET)  : 0.213                          
REMARK   3   FREE R VALUE                      : 0.262                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.990                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1098                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : 0.000                          
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 11                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.20                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.36                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 95.89                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2846                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2450                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2711                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2440                   
REMARK   3   BIN FREE R VALUE                        : 0.2580                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.74                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 135                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6472                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 52                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 136.8                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -27.26660                                            
REMARK   3    B22 (A**2) : 21.85940                                             
REMARK   3    B33 (A**2) : 5.40730                                              
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) : 0.000               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.453               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.924                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.886                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 6720   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 9229   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2848   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 109    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1011   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 6720   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 911    ; 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   : 8084   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.94                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.54                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 2.90                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   20.5302   30.3347   73.4657           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.6079 T22:   -0.4806                                    
REMARK   3     T33:   -0.4293 T12:    0.0321                                    
REMARK   3     T13:    0.1003 T23:   -0.0846                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.3369 L22:    0.6010                                    
REMARK   3     L33:    5.7218 L12:    0.4269                                    
REMARK   3     L13:    0.9876 L23:    0.0661                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1417 S12:   -0.1219 S13:    0.1523                     
REMARK   3     S21:    0.0815 S22:   -0.1915 S23:    0.0186                     
REMARK   3     S31:    0.1344 S32:   -0.3846 S33:    0.0499                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   15.5081   59.7649    0.3000           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2678 T22:    0.0244                                    
REMARK   3     T33:    0.3386 T12:    0.0043                                    
REMARK   3     T13:   -0.0408 T23:   -0.0027                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.7241 L22:    3.5183                                    
REMARK   3     L33:    0.9844 L12:   -0.5759                                    
REMARK   3     L13:   -0.2061 L23:   -0.7068                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0104 S12:    0.0731 S13:    0.2354                     
REMARK   3     S21:   -0.0988 S22:    0.0733 S23:   -0.0689                     
REMARK   3     S31:    0.1788 S32:    0.1585 S33:   -0.0837                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { C|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):    7.2664   61.8005   16.3734           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3047 T22:   -0.1408                                    
REMARK   3     T33:    0.1130 T12:    0.0180                                    
REMARK   3     T13:    0.0517 T23:   -0.0563                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.0976 L22:    4.2593                                    
REMARK   3     L33:    2.1476 L12:   -0.7520                                    
REMARK   3     L13:    0.0528 L23:   -0.9720                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.2367 S12:   -0.3023 S13:    0.0903                     
REMARK   3     S21:    0.6834 S22:    0.2196 S23:    0.3206                     
REMARK   3     S31:    0.1887 S32:   -0.4701 S33:    0.0171                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6LN2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-JAN-20.                  
REMARK 100 THE DEPOSITION ID IS D_1300015051.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAY-19                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : PH 6.2-6.6                         
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL45XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
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                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22019                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : 0.11600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 6.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.37                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.62600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.800                              
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: 5NX2                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.66                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.21                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 200-300 MM AMMONIUM FORMATE, 36% PEG     
REMARK 280  400, 5%-10% (W/V) GUANIDINE HYDROCHLORIDE, LIPIDIC CUBIC PHASE,     
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       31.52000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      161.20000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.33000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      161.20000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.52000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       32.33000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL UNIT IS UNKNOWN.           
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5640 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 41000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ARG A    24                                                      
REMARK 465     PRO A    25                                                      
REMARK 465     GLN A    26                                                      
REMARK 465     GLY A    27                                                      
REMARK 465     ALA A    28                                                      
REMARK 465     SER A   129                                                      
REMARK 465     LYS A   130                                                      
REMARK 465     ARG A   131                                                      
REMARK 465     GLY A   132                                                      
REMARK 465     GLU A   133                                                      
REMARK 465     ARG A   134                                                      
REMARK 465     SER A   258                                                      
REMARK 465     VAL A   259                                                      
REMARK 465     LEU A   260                                                      
REMARK 465     LEU A   422                                                      
REMARK 465     GLU A   423                                                      
REMARK 465     HIS A   424                                                      
REMARK 465     LEU A   425                                                      
REMARK 465     HIS A   426                                                      
REMARK 465     ILE A   427                                                      
REMARK 465     GLN A   428                                                      
REMARK 465     ARG A   429                                                      
REMARK 465     ASP A   430                                                      
REMARK 465     SER A   431                                                      
REMARK 465     SER A   432                                                      
REMARK 465     MET A   433                                                      
REMARK 465     LYS A   434                                                      
REMARK 465     PRO A   435                                                      
REMARK 465     LEU A   436                                                      
REMARK 465     LYS A   437                                                      
REMARK 465     CYS A   438                                                      
REMARK 465     PRO A   439                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     VAL A  30    CG1  CG2                                            
REMARK 470     LEU A  32    CG   CD1  CD2                                       
REMARK 470     GLU A  34    CG   CD   OE1  OE2                                  
REMARK 470     GLN A  37    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  38    CG   CD   CE   NZ                                   
REMARK 470     ARG A  40    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  43    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  44    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A  47    CG   CD   OE1  NE2                                  
REMARK 470     ARG A  48    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A  59    OD1  OD2                                            
REMARK 470     GLU A  76    CG   CD   OE1  OE2                                  
REMARK 470     SER A  79    OG                                                  
REMARK 470     SER A  84    OG                                                  
REMARK 470     GLN A  97    CG   CD   OE1  NE2                                  
REMARK 470     HIS A  99    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 113    CG   CD   CE   NZ                                   
REMARK 470     ASN A 115    CG   OD1  ND2                                       
REMARK 470     SER A 116    OG                                                  
REMARK 470     SER A 117    OG                                                  
REMARK 470     LEU A 118    CG   CD1  CD2                                       
REMARK 470     ARG A 121    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 123    CG   CD1  CD2                                       
REMARK 470     GLU A 125    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 139    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 140    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 141    CG   CD1  CD2                                       
REMARK 470     LEU A 142    CG   CD1  CD2                                       
REMARK 470     LEU A 144    CD1  CD2                                            
REMARK 470     LEU A 159    CG   CD1  CD2                                       
REMARK 470     ARG A 170    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 189    CG   CD1  CD2                                       
REMARK 470     PHE A 195    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE A 196    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 197    CG   CD   CE   NZ                                   
REMARK 470     LYS A 202    CG   CD   CE   NZ                                   
REMARK 470     MET A 204    CG   SD   CE                                        
REMARK 470     TYR A 205    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     SER A 206    OG                                                  
REMARK 470     THR A 207    OG1  CG2                                            
REMARK 470     GLN A 210    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 211    CG   CD   OE1  NE2                                  
REMARK 470     HIS A 212    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU A 217    CG   CD1  CD2                                       
REMARK 470     LEU A 218    CG   CD1  CD2                                       
REMARK 470     TYR A 220    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN A 221    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 222    CG   OD1  OD2                                       
REMARK 470     LEU A 224    CG   CD1  CD2                                       
REMARK 470     LEU A 228    CG   CD1  CD2                                       
REMARK 470     PHE A 257    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     MET A1001    CG   SD   CE                                        
REMARK 470     LYS A1002    CG   CD   CE   NZ                                   
REMARK 470     LYS A1003    CG   CD   CE   NZ                                   
REMARK 470     THR A1005    CB   OG1  CG2                                       
REMARK 470     VAL A1008    CG1  CG2                                            
REMARK 470     GLU A1016    CG   CD   OE1  OE2                                  
REMARK 470     ASP A1017    CG   OD1  OD2                                       
REMARK 470     LYS A1031    CG   CD   CE   NZ                                   
REMARK 470     ASP A1035    CG   OD1  OD2                                       
REMARK 470     ASP A1036    CG   OD1  OD2                                       
REMARK 470     LYS A1046    CG   CD   CE   NZ                                   
REMARK 470     ASP A1047    CG   OD1  OD2                                       
REMARK 470     PHE A1049    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU A1050    CB   CG   CD   OE1  OE2                             
REMARK 470     GLU A1051    CG   CD   OE1  OE2                                  
REMARK 470     GLU A1053    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 262    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 263    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 267    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 272    CG1  CG2  CD1                                       
REMARK 470     LYS A 288    CG   CD   CE   NZ                                   
REMARK 470     GLU A 292    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 294    CG   CD   OE1  OE2                                  
REMARK 470     THR A 298    OG1  CG2                                            
REMARK 470     ARG A 299    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 300    CG   OD1  ND2                                       
REMARK 470     SER A 301    OG                                                  
REMARK 470     ILE A 308    CG1  CG2  CD1                                       
REMARK 470     ILE A 309    CG1  CG2  CD1                                       
REMARK 470     ARG A 310    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 330    CG1  CG2  CD1                                       
REMARK 470     LYS A 334    CG   CD   CE   NZ                                   
REMARK 470     LEU A 339    CD1  CD2                                            
REMARK 470     LYS A 342    CD   CE   NZ                                        
REMARK 470     ARG A 348    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 351    CE   NZ                                             
REMARK 470     ILE A 357    CG1  CG2  CD1                                       
REMARK 470     THR A 362    OG1  CG2                                            
REMARK 470     GLU A 364    CG   CD   OE1  OE2                                  
REMARK 470     VAL A 370    CG1  CG2                                            
REMARK 470     MET A 371    CG   SD   CE                                        
REMARK 470     ASP A 372    CG   OD1  OD2                                       
REMARK 470     GLU A 373    CG   CD   OE1  OE2                                  
REMARK 470     HIS A 374    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU A 379    CG   CD1  CD2                                       
REMARK 470     ARG A 380    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE A 381    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 383    CG   CD   CE   NZ                                   
REMARK 470     PHE A 385    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     MET A 397    CG   SD   CE                                        
REMARK 470     LEU A 401    CG   CD1  CD2                                       
REMARK 470     VAL A 405    CG1  CG2                                            
REMARK 470     LEU A 411    CG   CD1  CD2                                       
REMARK 470     GLU A 412    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 414    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 415    CG   CD   CE   NZ                                   
REMARK 470     TRP A 417    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 417    CZ3  CH2                                            
REMARK 470     ARG A 421    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  44    CE   NZ                                             
REMARK 470     ARG B  49    CZ   NH1  NH2                                       
REMARK 470     LYS B  52    CG   CD   CE   NZ                                   
REMARK 470     LYS C  13    CD   CE   NZ                                        
REMARK 470     LYS C  23    CG   CD   CE   NZ                                   
REMARK 470     PHE C  29    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS C  74    CE   NZ                                             
REMARK 470     VAL C  79    CG1  CG2                                            
REMARK 470     ARG C 103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C 105    CG   OD1  OD2                                       
REMARK 470     GLU C 106    CG   CD   OE1  OE2                                  
REMARK 470     ASN C 109    CG   OD1  ND2                                       
REMARK 470     SER C 140    OG                                                  
REMARK 470     ARG C 141    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR C 143    OG1  CG2                                            
REMARK 470     GLU C 145    CG   CD   OE1  OE2                                  
REMARK 470     SER C 146    OG                                                  
REMARK 470     LYS C 155    CE   NZ                                             
REMARK 470     LYS C 204    CE   NZ                                             
REMARK 470     LYS C 226    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  59      -66.71     69.22                                   
REMARK 500    TYR A  69      -65.82   -131.11                                   
REMARK 500    TRP A  91       11.27    -69.77                                   
REMARK 500    GLN A  97      -53.77     74.82                                   
REMARK 500    GLN A 112      -60.80    -90.67                                   
REMARK 500    LYS A 113      -57.54     75.20                                   
REMARK 500    ALA A 208     -148.06   -167.46                                   
REMARK 500    LEU A 224      -72.84   -105.15                                   
REMARK 500    THR A1005     -152.94   -145.16                                   
REMARK 500    VAL A1008      -74.06    -76.47                                   
REMARK 500    ASP A1019       68.14   -159.30                                   
REMARK 500    GLU A1051     -159.72     63.49                                   
REMARK 500    TYR A 289      -32.04   -134.47                                   
REMARK 500    TYR A 291      -39.98   -131.95                                   
REMARK 500    GLU A 292       87.07   -152.13                                   
REMARK 500    TRP A 297       18.83     54.58                                   
REMARK 500    ALA A 375       35.54    -78.62                                   
REMARK 500    GLN A 394       -6.28    -58.89                                   
REMARK 500    CYS A 403      -68.39   -129.64                                   
REMARK 500    CYS B  23       92.50   -166.78                                   
REMARK 500    THR B  50      -64.40     68.84                                   
REMARK 500    SER B  66      137.96   -173.39                                   
REMARK 500    SER B  75      -79.96    -90.79                                   
REMARK 500    MET B  77      139.76    -35.76                                   
REMARK 500    LEU B 124       35.80    -79.58                                   
REMARK 500    LYS B 125      -32.90   -134.06                                   
REMARK 500    SER B 126        3.26    -68.69                                   
REMARK 500    ALA B 129      108.20   -161.17                                   
REMARK 500    LYS B 189      -72.48   -103.60                                   
REMARK 500    GLU B 212       61.61    -67.46                                   
REMARK 500    ASP C  56       13.87     54.30                                   
REMARK 500    LYS C  67      -57.83   -137.82                                   
REMARK 500    SER C  77       74.67     51.46                                   
REMARK 500    ARG C 103       92.53     64.46                                   
REMARK 500    PRO C 138     -166.70    -77.69                                   
REMARK 500    CYS C 139       30.91    -85.19                                   
REMARK 500    SER C 140       14.28     59.50                                   
REMARK 500    SER C 142      -25.98   -146.02                                   
REMARK 500    SER C 144       66.08     61.05                                   
REMARK 500    SER C 146       -5.37     70.13                                   
REMARK 500    ASP C 156       77.27     50.19                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1006   SG                                                     
REMARK 620 2 CYS A1009   SG  110.8                                              
REMARK 620 3 CYS A1039   SG  125.1  98.4                                        
REMARK 620 4 CYS A1042   SG  127.2  91.8  95.7                                  
REMARK 620 N                    1     2     3                                   
DBREF  6LN2 A   24   260  UNP    P43220   GLP1R_HUMAN     24    260             
DBREF  6LN2 A 1001  1054  UNP    P00268   RUBR_CLOPA       1     54             
DBREF  6LN2 A  262   439  UNP    P43220   GLP1R_HUMAN    262    439             
DBREF  6LN2 B    1   213  PDB    6LN2     6LN2             1    213             
DBREF  6LN2 C    1   226  PDB    6LN2     6LN2             1    226             
CRYST1   63.040   64.660  322.400  90.00  90.00  90.00 P 21 21 21    4   
ATOM      1  N   PRO A 137      11.132  11.309  56.855  1.00169.52
ATOM      2  CA  PRO A 137      12.066  12.288  57.427  1.00165.92
ATOM      3  C   PRO A 137      11.380  13.584  57.869  1.00168.36
ATOM      4  O   PRO A 137      11.783  14.166  58.882  1.00167.37
ATOM      5  CB  PRO A 137      13.080  12.495  56.300  1.00165.96
ATOM      6  CG  PRO A 137      13.061  11.187  55.541  1.00171.34
ATOM      7  CD  PRO A 137      11.590  10.811  55.549  1.00169.97
ATOM      8  N   GLU A 138      10.324  14.014  57.151  1.00164.67
ATOM      9  CA  GLU A 138       9.569  15.216  57.526  1.00163.51
ATOM     10  C   GLU A 138       8.607  14.928  58.670  1.00170.13
ATOM     11  O   GLU A 138       8.141  15.865  59.325  1.00167.84
ATOM     12  CB  GLU A 138       8.803  15.766  56.321  1.00164.47
ATOM     13  CG  GLU A 138       8.048  17.054  56.601  1.00173.67
ATOM     14  CD  GLU A 138       6.729  16.815  57.309  1.00183.51
ATOM     15  OE1 GLU A 138       6.174  15.704  57.171  1.00188.67
ATOM     16  OE2 GLU A 138       6.250  17.736  58.004  1.00161.27
ATOM     17  N   GLU A 139       8.320  13.626  58.922  1.00171.53
ATOM     18  CA  GLU A 139       7.528  13.189  60.079  1.00173.13
ATOM     19  C   GLU A 139       8.383  13.397  61.330  1.00177.42
ATOM     20  O   GLU A 139       7.873  13.841  62.368  1.00177.34
ATOM     21  CB  GLU A 139       7.098  11.730  59.914  1.00176.74
ATOM     22  CG  GLU A 139       6.147  11.491  58.753  0.00 99.99
ATOM     23  CD  GLU A 139       6.874  11.294  57.436  0.00 99.99
ATOM     24  OE1 GLU A 139       8.122  11.345  57.433  0.00 99.99
ATOM     25  OE2 GLU A 139       6.196  11.087  56.408  0.00 99.99
ATOM     26  N   GLN A 140       9.694  13.109  61.213  1.00173.70
ATOM     27  CA  GLN A 140      10.637  13.320  62.306  1.00172.86
ATOM     28  C   GLN A 140      11.009  14.800  62.402  1.00175.21
ATOM     29  O   GLN A 140      11.323  15.268  63.505  1.00175.56
ATOM     30  CB  GLN A 140      11.887  12.460  62.109  1.00174.07
ATOM     31  CG  GLN A 140      11.637  10.965  62.226  0.00 99.99
ATOM     32  CD  GLN A 140      12.897  10.147  62.024  0.00 99.99
ATOM     33  OE1 GLN A 140      13.840  10.591  61.369  0.00 99.99
ATOM     34  NE2 GLN A 140      12.918   8.946  62.590  0.00 99.99
ATOM     35  N   LEU A 141      10.973  15.540  61.262  1.00168.51
ATOM     36  CA  LEU A 141      11.285  16.973  61.253  1.00164.63
ATOM     37  C   LEU A 141      10.210  17.724  62.016  1.00166.77
ATOM     38  O   LEU A 141      10.540  18.463  62.942  1.00166.07
ATOM     39  CB  LEU A 141      11.404  17.487  59.817  1.00163.23
ATOM     40  CG  LEU A 141      12.556  16.917  58.986  0.00 99.99
ATOM     41  CD1 LEU A 141      12.468  17.398  57.546  0.00 99.99
ATOM     42  CD2 LEU A 141      13.896  17.359  59.553  0.00 99.99
ATOM     43  N   LEU A 142       8.923  17.491  61.674  1.00162.93
ATOM     44  CA  LEU A 142       7.802  18.133  62.360  1.00162.73
ATOM     45  C   LEU A 142       7.826  17.796  63.850  1.00167.36
ATOM     46  O   LEU A 142       7.620  18.675  64.691  1.00166.00
ATOM     47  CB  LEU A 142       6.474  17.704  61.734  1.00164.68
ATOM     48  CG  LEU A 142       5.213  18.354  62.306  0.00 99.99
ATOM     49  CD1 LEU A 142       5.208  19.850  62.030  0.00 99.99
ATOM     50  CD2 LEU A 142       3.965  17.751  61.682  0.00 99.99
ATOM     51  N   PHE A 143       8.136  16.538  64.171  1.00165.98
ATOM     52  CA  PHE A 143       8.247  16.086  65.552  1.00166.97
ATOM     53  C   PHE A 143       9.366  16.856  66.296  1.00167.24
ATOM     54  O   PHE A 143       9.177  17.270  67.444  1.00166.27
ATOM     55  CB  PHE A 143       8.514  14.581  65.603  1.00171.15
ATOM     56  CG  PHE A 143       8.572  14.023  66.996  1.00173.95
ATOM     57  CD1 PHE A 143       7.410  13.741  67.694  1.00179.36
ATOM     58  CD2 PHE A 143       9.786  13.777  67.610  1.00175.81
ATOM     59  CE1 PHE A 143       7.461  13.228  68.976  1.00180.71
ATOM     60  CE2 PHE A 143       9.842  13.265  68.892  1.00179.24
ATOM     61  CZ  PHE A 143       8.679  12.989  69.575  1.00178.62
ATOM     62  N   LEU A 144      10.521  17.052  65.635  1.00161.51
ATOM     63  CA  LEU A 144      11.644  17.777  66.223  1.00158.25
ATOM     64  C   LEU A 144      11.270  19.216  66.475  1.00162.19
ATOM     65  O   LEU A 144      11.670  19.775  67.492  1.00161.03
ATOM     66  CB  LEU A 144      12.871  17.694  65.313  1.00156.21
ATOM     67  CG  LEU A 144      13.476  16.303  65.114  1.00159.72
ATOM     68  CD1 LEU A 144      14.589  16.343  64.079  0.00 99.99
ATOM     69  CD2 LEU A 144      14.058  15.780  66.418  0.00 99.99
ATOM     70  N   TYR A 145      10.491  19.812  65.567  1.00161.43
ATOM     71  CA  TYR A 145      10.048  21.191  65.724  1.00162.99
ATOM     72  C   TYR A 145       8.973  21.296  66.777  1.00172.03
ATOM     73  O   TYR A 145       8.887  22.327  67.448  1.00172.72
ATOM     74  CB  TYR A 145       9.540  21.746  64.392  1.00165.35
ATOM     75  CG  TYR A 145      10.608  21.858  63.327  1.00169.30
ATOM     76  CD1 TYR A 145      11.428  22.977  63.258  1.00170.99
ATOM     77  CD2 TYR A 145      10.792  20.846  62.395  1.00171.95
ATOM     78  CE1 TYR A 145      12.406  23.087  62.289  1.00173.89
ATOM     79  CE2 TYR A 145      11.765  20.939  61.418  1.00173.22
ATOM     80  CZ  TYR A 145      12.571  22.060  61.367  1.00183.35
ATOM     81  OH  TYR A 145      13.544  22.164  60.400  1.00186.79
ATOM     82  N   ILE A 146       8.149  20.249  66.925  1.00171.34
ATOM     83  CA  ILE A 146       7.066  20.260  67.904  1.00173.41
ATOM     84  C   ILE A 146       7.629  20.223  69.317  1.00175.43
ATOM     85  O   ILE A 146       7.187  21.001  70.161  1.00176.39
ATOM     86  CB  ILE A 146       6.109  19.072  67.700  1.00179.85
ATOM     87  CG1 ILE A 146       5.391  19.190  66.353  1.00181.67
ATOM     88  CG2 ILE A 146       5.062  19.034  68.803  1.00182.87
ATOM     89  CD1 ILE A 146       4.614  17.953  65.963  1.00191.49
ATOM     90  N   ILE A 147       8.628  19.367  69.564  1.00168.56
ATOM     91  CA  ILE A 147       9.244  19.291  70.894  1.00166.26
ATOM     92  C   ILE A 147      10.108  20.544  71.145  1.00164.41
ATOM     93  O   ILE A 147      10.403  20.867  72.293  1.00163.63
ATOM     94  CB  ILE A 147      10.106  18.024  71.045  1.00169.37
ATOM     95  CG1 ILE A 147       9.231  16.771  70.971  1.00168.51
ATOM     96  CG2 ILE A 147      10.831  18.028  72.382  1.00170.82
ATOM     97  CD1 ILE A 147      10.015  15.482  70.871  1.00171.26
ATOM     98  N   TYR A 148      10.519  21.230  70.067  1.00157.06
ATOM     99  CA  TYR A 148      11.326  22.443  70.152  1.00153.36
ATOM    100  C   TYR A 148      10.459  23.623  70.598  1.00154.13
ATOM    101  O   TYR A 148      10.844  24.351  71.509  1.00152.43
ATOM    102  CB  TYR A 148      11.991  22.740  68.807  1.00152.47
ATOM    103  CG  TYR A 148      12.906  23.944  68.827  1.00152.65
ATOM    104  CD1 TYR A 148      14.196  23.849  69.331  1.00153.17
ATOM    105  CD2 TYR A 148      12.476  25.173  68.342  1.00153.42
ATOM    106  CE1 TYR A 148      15.037  24.943  69.355  1.00151.69
ATOM    107  CE2 TYR A 148      13.303  26.278  68.357  1.00152.81
ATOM    108  CZ  TYR A 148      14.584  26.162  68.863  1.00156.97
ATOM    109  OH  TYR A 148      15.416  27.257  68.882  1.00156.62
ATOM    110  N   THR A 149       9.299  23.804  69.971  1.00150.80
ATOM    111  CA  THR A 149       8.417  24.917  70.303  1.00151.49
ATOM    112  C   THR A 149       7.683  24.677  71.617  1.00156.73
ATOM    113  O   THR A 149       7.535  25.615  72.406  1.00156.24
ATOM    114  CB  THR A 149       7.381  25.167  69.192  1.00161.62
ATOM    115  OG1 THR A 149       6.549  24.010  69.041  1.00170.69
ATOM    116  CG2 THR A 149       8.077  25.448  67.868  1.00153.18
ATOM    117  N   VAL A 150       7.244  23.445  71.871  1.00155.06
ATOM    118  CA  VAL A 150       6.574  23.175  73.148  1.00157.95
ATOM    119  C   VAL A 150       7.600  23.232  74.293  1.00159.22
ATOM    120  O   VAL A 150       7.266  23.649  75.401  1.00157.27
ATOM    121  CB  VAL A 150       5.873  21.804  73.139  1.00165.34
ATOM    122  CG1 VAL A 150       5.292  21.492  74.509  1.00167.07
ATOM    123  CG2 VAL A 150       4.741  21.791  72.122  1.00164.61
ATOM    124  N   GLY A 151       8.839  22.848  73.993  1.00154.89
ATOM    125  CA  GLY A 151       9.927  22.917  74.952  1.00153.29
ATOM    126  C   GLY A 151      10.288  24.350  75.264  1.00156.25
ATOM    127  O   GLY A 151      10.767  24.643  76.356  1.00155.58
ATOM    128  N   TYR A 152      10.058  25.249  74.313  1.00153.74
ATOM    129  CA  TYR A 152      10.313  26.672  74.503  1.00153.78
ATOM    130  C   TYR A 152       9.102  27.362  75.155  1.00160.05
ATOM    131  O   TYR A 152       9.280  28.248  75.999  1.00159.49
ATOM    132  CB  TYR A 152      10.649  27.339  73.168  1.00154.17
ATOM    133  CG  TYR A 152      11.938  26.850  72.546  1.00154.38
ATOM    134  CD1 TYR A 152      13.159  27.405  72.909  1.00155.96
ATOM    135  CD2 TYR A 152      11.930  25.836  71.597  1.00154.08
ATOM    136  CE1 TYR A 152      14.340  26.964  72.346  1.00155.11
ATOM    137  CE2 TYR A 152      13.102  25.382  71.023  1.00153.39
ATOM    138  CZ  TYR A 152      14.306  25.947  71.399  1.00158.23
ATOM    139  OH  TYR A 152      15.479  25.503  70.834  1.00155.36
ATOM    140  N   ALA A 153       7.875  26.955  74.775  1.00158.36
ATOM    141  CA  ALA A 153       6.658  27.489  75.391  1.00160.22
ATOM    142  C   ALA A 153       6.600  27.057  76.854  1.00165.09
ATOM    143  O   ALA A 153       6.223  27.842  77.724  1.00164.24
ATOM    144  CB  ALA A 153       5.413  27.016  74.626  1.00162.89
ATOM    145  N   LEU A 154       6.996  25.805  77.122  1.00162.89
ATOM    146  CA  LEU A 154       7.061  25.264  78.471  1.00163.37
ATOM    147  C   LEU A 154       8.066  26.063  79.305  1.00163.48
ATOM    148  O   LEU A 154       7.741  26.492  80.412  1.00165.18
ATOM    149  CB  LEU A 154       7.440  23.782  78.437  1.00163.89
ATOM    150  CG  LEU A 154       6.431  22.839  77.777  1.00172.69
ATOM    151  CD1 LEU A 154       6.995  21.430  77.681  1.00176.40
ATOM    152  CD2 LEU A 154       5.144  22.781  78.585  1.00177.05
ATOM    153  N   SER A 155       9.272  26.291  78.760  1.00154.50
ATOM    154  CA  SER A 155      10.330  26.978  79.478  1.00151.40
ATOM    155  C   SER A 155       9.966  28.434  79.763  1.00153.53
ATOM    156  O   SER A 155      10.003  28.859  80.920  1.00153.22
ATOM    157  CB  SER A 155      11.640  26.915  78.691  1.00152.42
ATOM    158  OG  SER A 155      12.107  25.582  78.583  1.00162.66
ATOM    159  N   PHE A 156       9.597  29.186  78.719  1.00148.59
ATOM    160  CA  PHE A 156       9.249  30.595  78.855  1.00148.09
ATOM    161  C   PHE A 156       8.173  30.793  79.920  1.00155.24
ATOM    162  O   PHE A 156       8.328  31.652  80.786  1.00153.82
ATOM    163  CB  PHE A 156       8.777  31.162  77.515  1.00149.35
ATOM    164  CG  PHE A 156       8.466  32.630  77.554  1.00150.89
ATOM    165  CD1 PHE A 156       9.480  33.570  77.484  1.00152.22
ATOM    166  CD2 PHE A 156       7.160  33.075  77.660  1.00154.14
ATOM    167  CE1 PHE A 156       9.194  34.922  77.521  1.00153.95
ATOM    168  CE2 PHE A 156       6.871  34.425  77.698  1.00157.82
ATOM    169  CZ  PHE A 156       7.889  35.350  77.627  1.00154.87
ATOM    170  N   SER A 157       7.098  29.986  79.865  1.00155.73
ATOM    171  CA  SER A 157       6.019  30.069  80.841  1.00159.00
ATOM    172  C   SER A 157       6.566  29.818  82.235  1.00164.64
ATOM    173  O   SER A 157       6.310  30.622  83.142  1.00166.36
ATOM    174  CB  SER A 157       4.912  29.069  80.502  1.00165.07
ATOM    175  OG  SER A 157       5.395  27.739  80.548  1.00176.46
ATOM    176  N   ALA A 158       7.361  28.734  82.399  1.00159.35
ATOM    177  CA  ALA A 158       7.953  28.415  83.695  1.00158.62
ATOM    178  C   ALA A 158       8.862  29.539  84.176  1.00161.30
ATOM    179  O   ALA A 158       8.824  29.876  85.353  1.00161.12
ATOM    180  CB  ALA A 158       8.738  27.097  83.620  1.00158.03
ATOM    181  N   LEU A 159       9.641  30.142  83.266  1.00156.50
ATOM    182  CA  LEU A 159      10.572  31.203  83.612  1.00155.17
ATOM    183  C   LEU A 159       9.833  32.513  83.955  1.00162.02
ATOM    184  O   LEU A 159      10.210  33.203  84.909  1.00161.86
ATOM    185  CB  LEU A 159      11.559  31.444  82.468  1.00152.85
ATOM    186  CG  LEU A 159      12.514  30.294  82.142  0.00 99.99
ATOM    187  CD1 LEU A 159      13.332  30.610  80.900  0.00 99.99
ATOM    188  CD2 LEU A 159      13.475  30.051  83.295  0.00 99.99
ATOM    189  N   VAL A 160       8.784  32.850  83.196  1.00159.53
ATOM    190  CA  VAL A 160       8.031  34.084  83.420  1.00160.44
ATOM    191  C   VAL A 160       7.276  33.988  84.745  1.00164.25
ATOM    192  O   VAL A 160       7.276  34.944  85.524  1.00164.44
ATOM    193  CB  VAL A 160       7.045  34.359  82.270  1.00165.35
ATOM    194  CG1 VAL A 160       6.188  35.577  82.583  1.00168.03
ATOM    195  CG2 VAL A 160       7.797  34.621  80.974  1.00163.29
ATOM    196  N   ILE A 161       6.677  32.829  85.016  1.00160.70
ATOM    197  CA  ILE A 161       5.996  32.613  86.289  1.00162.12
ATOM    198  C   ILE A 161       7.047  32.527  87.412  1.00165.63
ATOM    199  O   ILE A 161       6.795  33.000  88.521  1.00166.35
ATOM    200  CB  ILE A 161       5.139  31.334  86.260  1.00165.76
ATOM    201  CG1 ILE A 161       3.998  31.479  85.251  1.00167.03
ATOM    202  CG2 ILE A 161       4.539  31.063  87.632  1.00167.71
ATOM    203  CD1 ILE A 161       3.252  30.191  84.983  1.00162.73
ATOM    204  N   ALA A 162       8.231  31.972  87.113  1.00160.55
ATOM    205  CA  ALA A 162       9.305  31.883  88.102  1.00159.10
ATOM    206  C   ALA A 162       9.796  33.267  88.481  1.00161.96
ATOM    207  O   ALA A 162       9.888  33.579  89.674  1.00162.45
ATOM    208  CB  ALA A 162      10.465  31.031  87.565  1.00157.65
ATOM    209  N   SER A 163      10.080  34.113  87.474  1.00156.58
ATOM    210  CA  SER A 163      10.521  35.484  87.714  1.00156.25
ATOM    211  C   SER A 163       9.409  36.302  88.383  1.00160.46
ATOM    212  O   SER A 163       9.700  37.261  89.104  1.00159.07
ATOM    213  CB  SER A 163      10.954  36.145  86.404  1.00160.44
ATOM    214  OG  SER A 163       9.873  36.223  85.492  1.00173.17
ATOM    215  N   ALA A 164       8.141  35.903  88.170  1.00158.87
ATOM    216  CA  ALA A 164       7.021  36.558  88.827  1.00162.11
ATOM    217  C   ALA A 164       6.970  36.141  90.304  1.00169.56
ATOM    218  O   ALA A 164       6.495  36.912  91.146  1.00171.46
ATOM    219  CB  ALA A 164       5.703  36.216  88.116  1.00164.58
ATOM    220  N   ILE A 165       7.483  34.937  90.626  1.00165.64
ATOM    221  CA  ILE A 165       7.508  34.463  92.012  1.00166.17
ATOM    222  C   ILE A 165       8.520  35.284  92.835  1.00168.66
ATOM    223  O   ILE A 165       8.231  35.667  93.971  1.00169.26
ATOM    224  CB  ILE A 165       7.867  32.968  92.090  1.00167.83
ATOM    225  CG1 ILE A 165       6.776  32.122  91.431  1.00169.72
ATOM    226  CG2 ILE A 165       8.008  32.528  93.540  1.00168.57
ATOM    227  CD1 ILE A 165       7.155  30.669  91.249  1.00173.54
ATOM    228  N   LEU A 166       9.689  35.551  92.265  1.00162.84
ATOM    229  CA  LEU A 166      10.718  36.286  92.980  1.00161.97
ATOM    230  C   LEU A 166      10.423  37.783  93.058  1.00170.73
ATOM    231  O   LEU A 166      10.851  38.440  94.012  1.00171.41
ATOM    232  CB  LEU A 166      12.083  36.072  92.324  1.00158.96
ATOM    233  CG  LEU A 166      12.640  34.647  92.366  1.00161.66
ATOM    234  CD1 LEU A 166      13.923  34.548  91.556  1.00159.13
ATOM    235  CD2 LEU A 166      12.948  34.233  93.796  1.00165.00
ATOM    236  N   LEU A 167       9.702  38.330  92.065  1.00169.94
ATOM    237  CA  LEU A 167       9.377  39.757  92.063  1.00171.85
ATOM    238  C   LEU A 167       8.063  40.060  92.780  1.00180.19
ATOM    239  O   LEU A 167       7.936  41.126  93.386  1.00181.52
ATOM    240  CB  LEU A 167       9.307  40.289  90.630  1.00171.35
ATOM    241  CG  LEU A 167      10.615  40.272  89.836  1.00172.75
ATOM    242  CD1 LEU A 167      10.373  40.686  88.393  1.00173.30
ATOM    243  CD2 LEU A 167      11.624  41.234  90.443  1.00173.16
ATOM    244  N   GLY A 168       7.104  39.141  92.707  1.00178.39
ATOM    245  CA  GLY A 168       5.816  39.319  93.366  1.00181.91
ATOM    246  C   GLY A 168       5.935  39.305  94.877  1.00186.88
ATOM    247  O   GLY A 168       5.449  40.216  95.547  1.00188.42
ATOM    248  N   PHE A 169       6.601  38.273  95.415  1.00182.49
ATOM    249  CA  PHE A 169       6.799  38.106  96.850  1.00183.22
ATOM    250  C   PHE A 169       7.897  39.032  97.347  1.00186.37
ATOM    251  O   PHE A 169       9.030  38.966  96.861  1.00183.76
ATOM    252  CB  PHE A 169       7.136  36.651  97.179  1.00183.63
ATOM    253  CG  PHE A 169       6.022  35.689  96.884  1.00188.40
ATOM    254  CD1 PHE A 169       5.017  35.465  97.810  1.00194.93
ATOM    255  CD2 PHE A 169       5.975  35.007  95.680  1.00191.27
ATOM    256  CE1 PHE A 169       3.991  34.580  97.538  1.00198.52
ATOM    257  CE2 PHE A 169       4.951  34.121  95.407  1.00197.11
ATOM    258  CZ  PHE A 169       3.958  33.907  96.337  1.00197.75
ATOM    259  N   ARG A 170       7.562  39.900  98.316  1.00184.10
ATOM    260  CA  ARG A 170       8.518  40.853  98.876  1.00182.34
ATOM    261  C   ARG A 170       9.590  40.140  99.692  1.00181.30
ATOM    262  O   ARG A 170      10.739  40.583  99.708  1.00177.94
ATOM    263  CB  ARG A 170       7.798  41.888  99.742  1.00186.42
ATOM    264  CG  ARG A 170       6.793  42.740  98.984  0.00 99.99
ATOM    265  CD  ARG A 170       7.486  43.665  97.998  0.00 99.99
ATOM    266  NE  ARG A 170       6.534  44.491  97.259  0.00 99.99
ATOM    267  CZ  ARG A 170       5.904  44.100  96.157  0.00 99.99
ATOM    268  NH1 ARG A 170       6.124  42.891  95.660  0.00 99.99
ATOM    269  NH2 ARG A 170       5.056  44.921  95.554  0.00 99.99
ATOM    270  N   HIS A 171       9.227  39.011 100.327  1.00177.56
ATOM    271  CA  HIS A 171      10.124  38.214 101.161  1.00175.65
ATOM    272  C   HIS A 171      11.339  37.680 100.395  1.00174.95
ATOM    273  O   HIS A 171      12.220  37.074 101.000  1.00172.25
ATOM    274  CB  HIS A 171       9.371  37.039 101.787  1.00178.33
ATOM    275  CG  HIS A 171       8.301  37.450 102.751  1.00184.81
ATOM    276  ND1 HIS A 171       8.581  38.024 103.971  1.00189.99
ATOM    277  CD2 HIS A 171       6.952  37.371 102.673  1.00186.77
ATOM    278  CE1 HIS A 171       7.448  38.279 104.603  1.00190.86
ATOM    279  NE2 HIS A 171       6.447  37.895 103.838  1.00189.29
ATOM    280  N   LEU A 172      11.400  37.925  99.080  1.00171.13
ATOM    281  CA  LEU A 172      12.462  37.413  98.231  1.00168.40
ATOM    282  C   LEU A 172      13.290  38.502  97.559  1.00172.46
ATOM    283  O   LEU A 172      14.174  38.172  96.768  1.00170.12
ATOM    284  CB  LEU A 172      11.888  36.495  97.150  1.00168.29
ATOM    285  CG  LEU A 172      11.234  35.200  97.636  1.00174.31
ATOM    286  CD1 LEU A 172      10.582  34.460  96.479  1.00176.21
ATOM    287  CD2 LEU A 172      12.269  34.280  98.265  1.00175.82
ATOM    288  N   HIS A 173      13.032  39.781  97.861  1.00171.98
ATOM    289  CA  HIS A 173      13.780  40.892  97.263  1.00172.30
ATOM    290  C   HIS A 173      15.180  40.976  97.887  1.00174.89
ATOM    291  O   HIS A 173      15.453  41.832  98.741  1.00176.47
ATOM    292  CB  HIS A 173      13.023  42.209  97.448  1.00176.43
ATOM    293  CG  HIS A 173      11.715  42.261  96.721  1.00181.48
ATOM    294  ND1 HIS A 173      11.629  42.313  95.347  1.00184.40
ATOM    295  CD2 HIS A 173      10.441  42.271  97.178  1.00184.12
ATOM    296  CE1 HIS A 173      10.357  42.352  94.991  1.00185.27
ATOM    297  NE2 HIS A 173       9.616  42.326  96.080  1.00185.48
ATOM    298  N   CYS A 174      16.066  40.074  97.462  1.00168.71
ATOM    299  CA  CYS A 174      17.407  40.019  98.002  1.00167.40
ATOM    300  C   CYS A 174      18.442  39.922  96.894  1.00171.99
ATOM    301  O   CYS A 174      18.145  39.575  95.745  1.00170.84
ATOM    302  CB  CYS A 174      17.551  38.836  98.961  1.00166.68
ATOM    303  SG  CYS A 174      17.292  37.206  98.189  1.00169.03
ATOM    304  N   THR A 175      19.674  40.242  97.272  1.00169.90
ATOM    305  CA  THR A 175      20.868  40.284  96.433  1.00168.38
ATOM    306  C   THR A 175      20.968  39.023  95.553  1.00166.14
ATOM    307  O   THR A 175      21.206  39.128  94.352  1.00163.84
ATOM    308  CB  THR A 175      22.148  40.415  97.279  1.00190.92
ATOM    309  OG1 THR A 175      22.147  41.677  97.960  1.00198.83
ATOM    310  CG2 THR A 175      23.383  40.332  96.395  1.00192.90
ATOM    311  N   ARG A 176      20.751  37.836  96.155  1.00159.73
ATOM    312  CA  ARG A 176      20.871  36.555  95.466  1.00156.85
ATOM    313  C   ARG A 176      19.870  36.416  94.338  1.00158.09
ATOM    314  O   ARG A 176      20.265  36.168  93.196  1.00155.69
ATOM    315  CB  ARG A 176      20.696  35.398  96.451  1.00156.74
ATOM    316  CG  ARG A 176      19.334  35.356  97.124  1.00158.28
ATOM    317  CD  ARG A 176      19.230  34.185  98.087  1.00159.48
ATOM    318  NE  ARG A 176      17.926  34.129  98.743  1.00161.77
ATOM    319  CZ  ARG A 176      17.610  34.811  99.839  1.00175.42
ATOM    320  NH1 ARG A 176      18.509  35.604 100.407  1.00169.43
ATOM    321  NH2 ARG A 176      16.399  34.698 100.365  1.00150.37
ATOM    322  N   ASN A 177      18.580  36.570  94.652  1.00155.11
ATOM    323  CA  ASN A 177      17.515  36.387  93.675  1.00154.66
ATOM    324  C   ASN A 177      17.592  37.386  92.522  1.00157.66
ATOM    325  O   ASN A 177      17.195  37.049  91.402  1.00157.10
ATOM    326  CB  ASN A 177      16.146  36.498  94.348  1.00154.34
ATOM    327  CG  ASN A 177      15.846  35.324  95.258  1.00169.47
ATOM    328  OD1 ASN A 177      16.440  34.255  95.123  1.00167.56
ATOM    329  ND2 ASN A 177      14.923  35.520  96.190  1.00160.62
ATOM    330  N   TYR A 178      18.132  38.588  92.773  1.00153.32
ATOM    331  CA  TYR A 178      18.245  39.576  91.712  1.00153.11
ATOM    332  C   TYR A 178      19.071  39.050  90.550  1.00151.87
ATOM    333  O   TYR A 178      18.694  39.234  89.395  1.00150.10
ATOM    334  CB  TYR A 178      18.860  40.870  92.248  1.00156.74
ATOM    335  CG  TYR A 178      18.003  41.578  93.273  1.00162.41
ATOM    336  CD1 TYR A 178      16.618  41.478  93.233  1.00165.43
ATOM    337  CD2 TYR A 178      18.582  42.345  94.276  1.00165.35
ATOM    338  CE1 TYR A 178      15.828  42.121  94.165  1.00169.06
ATOM    339  CE2 TYR A 178      17.806  42.996  95.216  1.00169.53
ATOM    340  CZ  TYR A 178      16.429  42.883  95.160  1.00182.70
ATOM    341  OH  TYR A 178      15.649  43.527  96.091  1.00190.97
ATOM    342  N   ILE A 179      20.168  38.359  90.853  1.00147.03
ATOM    343  CA  ILE A 179      21.028  37.787  89.825  1.00145.94
ATOM    344  C   ILE A 179      20.260  36.721  89.029  1.00151.11
ATOM    345  O   ILE A 179      20.397  36.645  87.798  1.00151.12
ATOM    346  CB  ILE A 179      22.298  37.166  90.434  1.00148.28
ATOM    347  CG1 ILE A 179      23.165  38.249  91.079  1.00149.66
ATOM    348  CG2 ILE A 179      23.119  36.468  89.359  1.00148.04
ATOM    349  CD1 ILE A 179      24.309  37.705  91.906  1.00159.15
ATOM    350  N   HIS A 180      19.434  35.931  89.718  1.00147.76
ATOM    351  CA  HIS A 180      18.632  34.906  89.067  1.00147.74
ATOM    352  C   HIS A 180      17.671  35.545  88.083  1.00151.57
ATOM    353  O   HIS A 180      17.596  35.120  86.934  1.00150.73
ATOM    354  CB  HIS A 180      17.873  34.079  90.106  1.00150.21
ATOM    355  CG  HIS A 180      18.760  33.281  91.010  1.00153.92
ATOM    356  ND1 HIS A 180      19.492  32.200  90.569  1.00155.79
ATOM    357  CD2 HIS A 180      19.034  33.405  92.330  1.00156.22
ATOM    358  CE1 HIS A 180      20.177  31.695  91.580  1.00154.96
ATOM    359  NE2 HIS A 180      19.919  32.407  92.657  1.00155.66
ATOM    360  N   LEU A 181      16.965  36.594  88.515  1.00149.11
ATOM    361  CA  LEU A 181      16.001  37.290  87.667  1.00149.86
ATOM    362  C   LEU A 181      16.628  37.782  86.376  1.00148.97
ATOM    363  O   LEU A 181      15.960  37.812  85.343  1.00147.96
ATOM    364  CB  LEU A 181      15.379  38.469  88.418  1.00152.91
ATOM    365  CG  LEU A 181      14.520  38.120  89.636  1.00161.50
ATOM    366  CD1 LEU A 181      14.089  39.381  90.368  1.00164.05
ATOM    367  CD2 LEU A 181      13.269  37.367  89.211  1.00167.91
ATOM    368  N   ASN A 182      17.913  38.139  86.423  1.00143.56
ATOM    369  CA  ASN A 182      18.612  38.590  85.227  1.00142.92
ATOM    370  C   ASN A 182      18.971  37.411  84.337  1.00145.63
ATOM    371  O   ASN A 182      18.907  37.518  83.102  1.00145.86
ATOM    372  CB  ASN A 182      19.870  39.374  85.605  1.00142.56
ATOM    373  CG  ASN A 182      19.553  40.720  86.225  1.00160.86
ATOM    374  OD1 ASN A 182      19.271  41.688  85.519  1.00155.73
ATOM    375  ND2 ASN A 182      19.599  40.785  87.550  1.00150.65
ATOM    376  N   LEU A 183      19.321  36.276  84.958  1.00139.26
ATOM    377  CA  LEU A 183      19.590  35.060  84.208  1.00136.80
ATOM    378  C   LEU A 183      18.296  34.555  83.631  1.00142.22
ATOM    379  O   LEU A 183      18.304  34.013  82.534  1.00142.56
ATOM    380  CB  LEU A 183      20.250  34.012  85.105  1.00136.07
ATOM    381  CG  LEU A 183      21.770  34.107  85.254  1.00139.80
ATOM    382  CD1 LEU A 183      22.161  35.396  85.959  1.00139.09
ATOM    383  CD2 LEU A 183      22.306  32.939  86.068  1.00142.66
ATOM    384  N   PHE A 184      17.180  34.766  84.330  1.00141.47
ATOM    385  CA  PHE A 184      15.873  34.445  83.792  1.00143.97
ATOM    386  C   PHE A 184      15.616  35.291  82.548  1.00147.75
ATOM    387  O   PHE A 184      15.231  34.766  81.499  1.00146.77
ATOM    388  CB  PHE A 184      14.789  34.673  84.847  1.00149.02
ATOM    389  CG  PHE A 184      14.893  33.757  86.031  1.00153.00
ATOM    390  CD1 PHE A 184      14.329  32.493  86.001  1.00157.19
ATOM    391  CD2 PHE A 184      15.557  34.156  87.178  1.00158.73
ATOM    392  CE1 PHE A 184      14.426  31.650  87.090  1.00159.62
ATOM    393  CE2 PHE A 184      15.654  33.315  88.270  1.00163.20
ATOM    394  CZ  PHE A 184      15.088  32.060  88.226  1.00160.49
ATOM    395  N   ALA A 185      15.864  36.603  82.665  1.00144.99
ATOM    396  CA  ALA A 185      15.586  37.566  81.607  1.00145.39
ATOM    397  C   ALA A 185      16.252  37.191  80.285  1.00149.48
ATOM    398  O   ALA A 185      15.586  37.187  79.243  1.00150.21
ATOM    399  CB  ALA A 185      16.039  38.973  82.024  1.00146.60
ATOM    400  N   SER A 186      17.549  36.844  80.324  1.00144.58
ATOM    401  CA  SER A 186      18.280  36.503  79.106  1.00143.23
ATOM    402  C   SER A 186      17.669  35.288  78.407  1.00146.57
ATOM    403  O   SER A 186      17.642  35.241  77.167  1.00145.66
ATOM    404  CB  SER A 186      19.753  36.237  79.422  1.00146.56
ATOM    405  OG  SER A 186      20.488  35.972  78.240  1.00160.19
ATOM    406  N   PHE A 187      17.163  34.316  79.199  1.00142.54
ATOM    407  CA  PHE A 187      16.498  33.145  78.639  1.00141.93
ATOM    408  C   PHE A 187      15.099  33.489  78.149  1.00147.64
ATOM    409  O   PHE A 187      14.661  32.982  77.113  1.00145.79
ATOM    410  CB  PHE A 187      16.431  32.020  79.674  1.00143.64
ATOM    411  CG  PHE A 187      17.775  31.480  80.070  1.00144.15
ATOM    412  CD1 PHE A 187      18.391  30.494  79.318  1.00146.77
ATOM    413  CD2 PHE A 187      18.428  31.959  81.192  1.00145.52
ATOM    414  CE1 PHE A 187      19.627  29.997  79.682  1.00146.83
ATOM    415  CE2 PHE A 187      19.664  31.464  81.559  1.00147.77
ATOM    416  CZ  PHE A 187      20.265  30.482  80.803  1.00145.69
ATOM    417  N   ILE A 188      14.400  34.358  78.898  1.00146.89
ATOM    418  CA  ILE A 188      13.051  34.805  78.564  1.00147.60
ATOM    419  C   ILE A 188      13.083  35.556  77.229  1.00151.10
ATOM    420  O   ILE A 188      12.238  35.291  76.370  1.00151.48
ATOM    421  CB  ILE A 188      12.467  35.707  79.666  1.00151.38
ATOM    422  CG1 ILE A 188      12.283  34.915  80.962  1.00152.25
ATOM    423  CG2 ILE A 188      11.114  36.260  79.242  1.00153.21
ATOM    424  CD1 ILE A 188      11.941  35.773  82.160  1.00159.87
ATOM    425  N   LEU A 189      14.077  36.444  77.038  1.00146.51
ATOM    426  CA  LEU A 189      14.216  37.183  75.789  1.00146.54
ATOM    427  C   LEU A 189      14.582  36.222  74.658  1.00151.60
ATOM    428  O   LEU A 189      14.072  36.360  73.544  1.00150.59
ATOM    429  CB  LEU A 189      15.269  38.284  75.932  1.00146.11
ATOM    430  CG  LEU A 189      14.946  39.408  76.918  0.00 99.99
ATOM    431  CD1 LEU A 189      16.132  40.348  77.069  0.00 99.99
ATOM    432  CD2 LEU A 189      13.755  40.220  76.434  0.00 99.99
ATOM    433  N   ARG A 190      15.425  35.220  74.956  1.00148.81
ATOM    434  CA  ARG A 190      15.804  34.205  73.976  1.00148.00
ATOM    435  C   ARG A 190      14.586  33.350  73.565  1.00152.38
ATOM    436  O   ARG A 190      14.494  32.917  72.419  1.00149.90
ATOM    437  CB  ARG A 190      16.914  33.311  74.532  1.00149.53
ATOM    438  CG  ARG A 190      17.422  32.268  73.550  1.00166.21
ATOM    439  CD  ARG A 190      18.102  32.920  72.357  1.00181.85
ATOM    440  NE  ARG A 190      18.596  31.932  71.402  1.00196.30
ATOM    441  CZ  ARG A 190      17.858  31.388  70.440  1.00225.90
ATOM    442  NH1 ARG A 190      16.586  31.735  70.304  1.00219.65
ATOM    443  NH2 ARG A 190      18.394  30.497  69.617  1.00222.17
ATOM    444  N   ALA A 191      13.658  33.114  74.500  1.00152.46
ATOM    445  CA  ALA A 191      12.464  32.310  74.235  1.00153.98
ATOM    446  C   ALA A 191      11.404  33.112  73.463  1.00158.39
ATOM    447  O   ALA A 191      10.643  32.546  72.676  1.00158.75
ATOM    448  CB  ALA A 191      11.867  31.782  75.547  1.00156.09
ATOM    449  N   LEU A 192      11.355  34.425  73.678  1.00154.40
ATOM    450  CA  LEU A 192      10.463  35.272  72.900  1.00155.00
ATOM    451  C   LEU A 192      11.177  35.706  71.602  1.00159.10
ATOM    452  O   LEU A 192      10.556  36.310  70.718  1.00159.56
ATOM    453  CB  LEU A 192      10.025  36.486  73.721  1.00156.12
ATOM    454  CG  LEU A 192       9.170  36.196  74.958  1.00158.82
ATOM    455  CD1 LEU A 192       8.931  37.468  75.756  1.00160.26
ATOM    456  CD2 LEU A 192       7.819  35.627  74.554  1.00159.32
ATOM    457  N   CYS A 193      12.479  35.401  71.495  1.00154.60
ATOM    458  CA  CYS A 193      13.249  35.666  70.283  1.00153.78
ATOM    459  C   CYS A 193      12.912  34.596  69.253  1.00154.99
ATOM    460  O   CYS A 193      12.699  34.905  68.080  1.00154.62
ATOM    461  CB  CYS A 193      14.746  35.694  70.595  1.00153.25
ATOM    462  SG  CYS A 193      15.261  37.054  71.693  1.00156.89
ATOM    463  N   VAL A 194      12.820  33.340  69.707  1.00149.72
ATOM    464  CA  VAL A 194      12.399  32.226  68.858  1.00149.02
ATOM    465  C   VAL A 194      10.902  32.356  68.584  1.00155.49
ATOM    466  O   VAL A 194      10.422  31.846  67.567  1.00155.24
ATOM    467  CB  VAL A 194      12.709  30.868  69.514  1.00151.22
ATOM    468  CG1 VAL A 194      12.153  29.729  68.672  1.00149.39
ATOM    469  CG2 VAL A 194      14.212  30.674  69.652  1.00151.56
ATOM    470  N   PHE A 195      10.164  33.039  69.497  1.00153.54
ATOM    471  CA  PHE A 195       8.727  33.259  69.333  1.00155.23
ATOM    472  C   PHE A 195       8.468  34.337  68.269  1.00158.87
ATOM    473  O   PHE A 195       7.388  34.360  67.676  1.00159.73
ATOM    474  CB  PHE A 195       8.090  33.657  70.666  1.00158.47
ATOM    475  CG  PHE A 195       6.601  33.832  70.597  0.00 99.99
ATOM    476  CD1 PHE A 195       5.757  32.735  70.633  0.00 99.99
ATOM    477  CD2 PHE A 195       6.040  35.093  70.498  0.00 99.99
ATOM    478  CE1 PHE A 195       4.386  32.896  70.569  0.00 99.99
ATOM    479  CE2 PHE A 195       4.670  35.257  70.434  0.00 99.99
ATOM    480  CZ  PHE A 195       3.842  34.158  70.471  0.00 99.99
ATOM    481  N   PHE A 196       9.454  35.209  68.014  1.00154.65
ATOM    482  CA  PHE A 196       9.333  36.230  66.976  1.00155.37
ATOM    483  C   PHE A 196       9.727  35.653  65.617  1.00159.93
ATOM    484  O   PHE A 196       9.074  35.957  64.622  1.00159.52
ATOM    485  CB  PHE A 196      10.198  37.445  67.316  1.00156.67
ATOM    486  CG  PHE A 196      10.074  38.572  66.331  0.00 99.99
ATOM    487  CD1 PHE A 196       9.000  39.443  66.385  0.00 99.99
ATOM    488  CD2 PHE A 196      11.031  38.763  65.351  0.00 99.99
ATOM    489  CE1 PHE A 196       8.885  40.480  65.479  0.00 99.99
ATOM    490  CE2 PHE A 196      10.919  39.798  64.442  0.00 99.99
ATOM    491  CZ  PHE A 196       9.846  40.658  64.507  0.00 99.99
ATOM    492  N   LYS A 197      10.788  34.817  65.572  1.00157.34
ATOM    493  CA  LYS A 197      11.241  34.177  64.331  1.00157.48
ATOM    494  C   LYS A 197      10.181  33.227  63.811  1.00166.96
ATOM    495  O   LYS A 197       9.904  33.221  62.614  1.00166.00
ATOM    496  CB  LYS A 197      12.560  33.437  64.560  1.00158.23
ATOM    497  CG  LYS A 197      13.738  34.348  64.863  0.00 99.99
ATOM    498  CD  LYS A 197      15.014  33.549  65.080  0.00 99.99
ATOM    499  CE  LYS A 197      14.940  32.728  66.357  0.00 99.99
ATOM    500  NZ  LYS A 197      16.182  31.939  66.583  0.00 99.99
ATOM    501  N   ASP A 198       9.560  32.444  64.708  1.00169.32
ATOM    502  CA  ASP A 198       8.484  31.532  64.321  1.00172.39
ATOM    503  C   ASP A 198       7.277  32.319  63.803  1.00180.41
ATOM    504  O   ASP A 198       6.558  31.842  62.921  1.00180.33
ATOM    505  CB  ASP A 198       8.081  30.647  65.502  1.00175.74
ATOM    506  CG  ASP A 198       9.146  29.630  65.859  1.00192.77
ATOM    507  OD1 ASP A 198      10.111  29.481  65.079  1.00193.46
ATOM    508  OD2 ASP A 198       9.018  28.981  66.919  1.00201.97
ATOM    509  N   ALA A 199       7.057  33.513  64.352  1.00180.59
ATOM    510  CA  ALA A 199       5.968  34.354  63.890  1.00184.29
ATOM    511  C   ALA A 199       6.216  34.774  62.437  1.00191.60
ATOM    512  O   ALA A 199       5.281  34.737  61.648  1.00192.98
ATOM    513  CB  ALA A 199       5.815  35.585  64.796  1.00186.33
ATOM    514  N   ALA A 200       7.476  35.118  62.074  1.00188.31
ATOM    515  CA  ALA A 200       7.832  35.483  60.695  1.00188.24
ATOM    516  C   ALA A 200       7.722  34.276  59.774  1.00193.63
ATOM    517  O   ALA A 200       7.426  34.434  58.586  1.00193.77
ATOM    518  CB  ALA A 200       9.251  36.069  60.641  1.00187.25
ATOM    519  N   LEU A 201       7.971  33.070  60.323  1.00190.67
ATOM    520  CA  LEU A 201       7.853  31.807  59.595  1.00190.48
ATOM    521  C   LEU A 201       6.370  31.554  59.279  1.00197.57
ATOM    522  O   LEU A 201       6.036  31.232  58.133  1.00196.93
ATOM    523  CB  LEU A 201       8.453  30.660  60.410  1.00189.71
ATOM    524  CG  LEU A 201       9.961  30.726  60.666  1.00194.96
ATOM    525  CD1 LEU A 201      10.396  29.612  61.605  1.00193.67
ATOM    526  CD2 LEU A 201      10.733  30.579  59.364  1.00199.74
ATOM    527  N   LYS A 202       5.486  31.732  60.288  1.00197.20
ATOM    528  CA  LYS A 202       4.040  31.588  60.109  1.00199.94
ATOM    529  C   LYS A 202       3.465  32.782  59.337  1.00206.87
ATOM    530  O   LYS A 202       2.436  32.641  58.676  1.00207.71
ATOM    531  CB  LYS A 202       3.344  31.446  61.464  1.00203.88
ATOM    532  CG  LYS A 202       3.674  30.159  62.200  0.00 99.99
ATOM    533  CD  LYS A 202       2.951  30.083  63.535  0.00 99.99
ATOM    534  CE  LYS A 202       3.282  28.796  64.271  0.00 99.99
ATOM    535  NZ  LYS A 202       2.579  28.709  65.581  0.00 99.99
ATOM    536  N   TRP A 203       4.124  33.946  59.421  1.00204.90
ATOM    537  CA  TRP A 203       3.710  35.174  58.747  1.00207.12
ATOM    538  C   TRP A 203       3.762  35.010  57.224  1.00212.05
ATOM    539  O   TRP A 203       2.744  35.185  56.553  1.00213.48
ATOM    540  CB  TRP A 203       4.590  36.347  59.182  1.00205.38
ATOM    541  CG  TRP A 203       4.180  37.658  58.585  1.00208.26
ATOM    542  CD1 TRP A 203       3.295  38.556  59.108  1.00210.66
ATOM    543  CD2 TRP A 203       4.641  38.218  57.350  1.00210.78
ATOM    544  NE1 TRP A 203       3.174  39.643  58.277  1.00212.43
ATOM    545  CE2 TRP A 203       3.992  39.459  57.189  1.00215.88
ATOM    546  CE3 TRP A 203       5.538  37.792  56.367  1.00213.70
ATOM    547  CZ2 TRP A 203       4.210  40.278  56.082  1.00217.92
ATOM    548  CZ3 TRP A 203       5.754  38.605  55.270  1.00217.86
ATOM    549  CH2 TRP A 203       5.094  39.838  55.133  1.00219.50
ATOM    550  N   MET A 204       4.939  34.657  56.684  1.00207.16
ATOM    551  CA  MET A 204       5.136  34.525  55.246  1.00206.56
ATOM    552  C   MET A 204       4.443  33.286  54.653  1.00212.80
ATOM    553  O   MET A 204       4.069  33.309  53.475  1.00213.22
ATOM    554  CB  MET A 204       6.628  34.471  54.912  1.00206.30
ATOM    555  CG  MET A 204       7.373  35.767  55.189  0.00 99.99
ATOM    556  SD  MET A 204       9.126  35.661  54.783  0.00 99.99
ATOM    557  CE  MET A 204       9.674  37.310  55.220  0.00 99.99
ATOM    558  N   TYR A 205       4.286  32.207  55.441  1.00210.32
ATOM    559  CA  TYR A 205       3.665  30.972  54.945  1.00210.88
ATOM    560  C   TYR A 205       2.137  31.102  54.776  1.00217.88
ATOM    561  O   TYR A 205       1.558  30.369  53.967  1.00218.41
ATOM    562  CB  TYR A 205       3.973  29.803  55.883  1.00211.26
ATOM    563  CG  TYR A 205       3.429  28.475  55.406  0.00 99.99
ATOM    564  CD1 TYR A 205       4.096  27.740  54.434  0.00 99.99
ATOM    565  CD2 TYR A 205       2.250  27.959  55.930  0.00 99.99
ATOM    566  CE1 TYR A 205       3.605  26.528  53.992  0.00 99.99
ATOM    567  CE2 TYR A 205       1.745  26.748  55.501  0.00 99.99
ATOM    568  CZ  TYR A 205       2.424  26.032  54.532  0.00 99.99
ATOM    569  OH  TYR A 205       1.930  24.825  54.098  0.00 99.99
ATOM    570  N   SER A 206       1.494  32.040  55.513  1.00215.71
ATOM    571  CA  SER A 206       0.049  32.260  55.443  1.00218.33
ATOM    572  C   SER A 206      -0.363  33.099  54.223  1.00224.18
ATOM    573  O   SER A 206      -1.525  33.506  54.140  1.00225.68
ATOM    574  CB  SER A 206      -0.452  32.941  56.718  1.00222.55
ATOM    575  OG  SER A 206      -0.286  32.098  57.845  0.00 99.99
ATOM    576  N   THR A 207       0.567  33.330  53.267  1.00220.77
ATOM    577  CA  THR A 207       0.295  34.089  52.042  1.00222.41
ATOM    578  C   THR A 207      -0.751  33.368  51.190  1.00231.37
ATOM    579  O   THR A 207      -1.679  34.012  50.701  1.00233.67
ATOM    580  CB  THR A 207       1.576  34.302  51.214  1.00225.90
ATOM    581  OG1 THR A 207       2.490  35.127  51.948  0.00 99.99
ATOM    582  CG2 THR A 207       1.250  34.982  49.893  0.00 99.99
ATOM    583  N   ALA A 208      -0.608  32.041  51.022  1.00229.05
ATOM    584  CA  ALA A 208      -1.533  31.177  50.273  1.00231.15
ATOM    585  C   ALA A 208      -1.205  29.709  50.570  1.00236.28
ATOM    586  O   ALA A 208      -0.755  29.398  51.677  1.00234.78
ATOM    587  CB  ALA A 208      -1.447  31.470  48.768  1.00231.30
ATOM    588  N   ALA A 209      -1.418  28.812  49.594  1.00234.90
ATOM    589  CA  ALA A 209      -1.115  27.391  49.751  1.00234.92
ATOM    590  C   ALA A 209      -0.400  26.860  48.508  1.00238.52
ATOM    591  O   ALA A 209      -1.029  26.695  47.464  1.00239.13
ATOM    592  CB  ALA A 209      -2.399  26.591  50.017  1.00238.64
ATOM    593  N   GLN A 210       0.921  26.624  48.613  1.00233.51
ATOM    594  CA  GLN A 210       1.744  26.101  47.523  1.00232.05
ATOM    595  C   GLN A 210       3.022  25.480  48.061  1.00234.71
ATOM    596  O   GLN A 210       3.601  25.985  49.026  1.00232.84
ATOM    597  CB  GLN A 210       2.073  27.209  46.521  1.00232.52
ATOM    598  CG  GLN A 210       2.868  26.738  45.314  0.00 99.99
ATOM    599  CD  GLN A 210       2.090  25.766  44.447  0.00 99.99
ATOM    600  OE1 GLN A 210       2.284  24.555  44.529  0.00 99.99
ATOM    601  NE2 GLN A 210       1.205  26.300  43.614  0.00 99.99
ATOM    602  N   GLN A 211       3.464  24.382  47.433  1.00232.16
ATOM    603  CA  GLN A 211       4.694  23.684  47.814  1.00230.87
ATOM    604  C   GLN A 211       5.916  24.575  47.571  1.00233.73
ATOM    605  O   GLN A 211       6.772  24.686  48.455  1.00231.75
ATOM    606  CB  GLN A 211       4.827  22.371  47.040  1.00232.64
ATOM    607  CG  GLN A 211       3.780  21.330  47.399  0.00 99.99
ATOM    608  CD  GLN A 211       3.943  20.045  46.611  0.00 99.99
ATOM    609  OE1 GLN A 211       4.500  20.044  45.513  0.00 99.99
ATOM    610  NE2 GLN A 211       3.459  18.943  47.172  0.00 99.99
ATOM    611  N   HIS A 212       5.979  25.225  46.382  1.00230.88
ATOM    612  CA  HIS A 212       7.053  26.153  46.019  1.00229.22
ATOM    613  C   HIS A 212       7.014  27.375  46.935  1.00233.99
ATOM    614  O   HIS A 212       8.062  27.816  47.418  1.00232.35
ATOM    615  CB  HIS A 212       6.929  26.568  44.552  1.00229.89
ATOM    616  CG  HIS A 212       7.125  25.442  43.586  0.00 99.99
ATOM    617  ND1 HIS A 212       8.344  24.831  43.392  0.00 99.99
ATOM    618  CD2 HIS A 212       6.256  24.815  42.758  0.00 99.99
ATOM    619  CE1 HIS A 212       8.216  23.877  42.487  0.00 99.99
ATOM    620  NE2 HIS A 212       6.961  23.845  42.087  0.00 99.99
ATOM    621  N   GLN A 213       5.805  27.900  47.200  1.00232.65
ATOM    622  CA  GLN A 213       5.630  29.047  48.088  1.00232.84
ATOM    623  C   GLN A 213       6.125  28.705  49.498  1.00237.09
ATOM    624  O   GLN A 213       6.815  29.525  50.094  1.00236.24
ATOM    625  CB  GLN A 213       4.163  29.480  48.121  1.00236.13
ATOM    626  CG  GLN A 213       3.655  30.051  46.807  1.00246.31
ATOM    627  CD  GLN A 213       2.198  30.467  46.879  1.00261.00
ATOM    628  OE1 GLN A 213       1.434  29.951  47.694  1.00257.93
ATOM    629  NE2 GLN A 213       1.811  31.406  46.024  1.00255.60
ATOM    630  N   TRP A 214       5.791  27.504  50.024  1.00233.96
ATOM    631  CA  TRP A 214       6.286  27.074  51.337  1.00232.88
ATOM    632  C   TRP A 214       7.804  27.318  51.401  1.00232.81
ATOM    633  O   TRP A 214       8.299  27.913  52.362  1.00232.19
ATOM    634  CB  TRP A 214       5.947  25.602  51.582  1.00232.76
ATOM    635  CG  TRP A 214       4.477  25.332  51.675  1.00233.20
ATOM    636  CD1 TRP A 214       3.471  26.255  51.640  1.00234.53
ATOM    637  CD2 TRP A 214       3.847  24.053  51.818  1.00234.19
ATOM    638  NE1 TRP A 214       2.253  25.631  51.753  1.00233.92
ATOM    639  CE2 TRP A 214       2.458  24.277  51.864  1.00236.89
ATOM    640  CE3 TRP A 214       4.326  22.744  51.911  1.00237.45
ATOM    641  CZ2 TRP A 214       1.538  23.239  51.998  1.00236.64
ATOM    642  CZ3 TRP A 214       3.413  21.715  52.045  1.00239.32
ATOM    643  CH2 TRP A 214       2.031  21.964  52.088  1.00238.52
ATOM    644  N   ASP A 215       8.530  26.877  50.366  1.00226.10
ATOM    645  CA  ASP A 215       9.968  27.078  50.300  1.00222.77
ATOM    646  C   ASP A 215      10.316  28.564  50.101  1.00222.81
ATOM    647  O   ASP A 215      11.288  29.043  50.693  1.00220.85
ATOM    648  CB  ASP A 215      10.575  26.241  49.172  1.00223.88
ATOM    649  CG  ASP A 215      10.550  24.756  49.470  1.00227.83
ATOM    650  OD1 ASP A 215      10.239  24.385  50.622  1.00227.15
ATOM    651  OD2 ASP A 215      10.839  23.960  48.552  1.00230.38
ATOM    652  N   GLY A 216       9.519  29.272  49.298  1.00218.21
ATOM    653  CA  GLY A 216       9.722  30.692  49.032  1.00217.11
ATOM    654  C   GLY A 216       9.515  31.572  50.253  1.00219.69
ATOM    655  O   GLY A 216      10.288  32.511  50.475  1.00218.94
ATOM    656  N   LEU A 217       8.474  31.277  51.066  1.00215.09
ATOM    657  CA  LEU A 217       8.171  32.008  52.294  1.00214.11
ATOM    658  C   LEU A 217       9.374  31.980  53.227  1.00213.76
ATOM    659  O   LEU A 217       9.631  32.975  53.904  1.00213.38
ATOM    660  CB  LEU A 217       6.939  31.416  52.980  1.00215.61
ATOM    661  CG  LEU A 217       5.616  31.534  52.220  0.00 99.99
ATOM    662  CD1 LEU A 217       4.511  30.780  52.943  0.00 99.99
ATOM    663  CD2 LEU A 217       5.196  32.990  52.097  0.00 99.99
ATOM    664  N   LEU A 218      10.133  30.865  53.235  1.00206.84
ATOM    665  CA  LEU A 218      11.341  30.750  54.047  1.00204.14
ATOM    666  C   LEU A 218      12.400  31.767  53.605  1.00205.94
ATOM    667  O   LEU A 218      13.064  32.368  54.448  1.00204.42
ATOM    668  CB  LEU A 218      11.906  29.331  53.969  1.00203.17
ATOM    669  CG  LEU A 218      11.035  28.220  54.558  0.00 99.99
ATOM    670  CD1 LEU A 218      11.646  26.854  54.283  0.00 99.99
ATOM    671  CD2 LEU A 218      10.900  28.385  56.063  0.00 99.99
ATOM    672  N   SER A 219      12.534  31.978  52.292  1.00202.00
ATOM    673  CA  SER A 219      13.537  32.881  51.730  1.00200.68
ATOM    674  C   SER A 219      13.222  34.351  52.021  1.00203.42
ATOM    675  O   SER A 219      14.085  35.074  52.527  1.00201.69
ATOM    676  CB  SER A 219      13.659  32.673  50.219  1.00204.28
ATOM    677  OG  SER A 219      14.154  31.380  49.920  1.00211.55
ATOM    678  N   TYR A 220      11.991  34.788  51.700  1.00201.38
ATOM    679  CA  TYR A 220      11.560  36.170  51.915  1.00202.73
ATOM    680  C   TYR A 220      11.746  36.588  53.390  1.00207.46
ATOM    681  O   TYR A 220      12.026  37.760  53.661  1.00207.88
ATOM    682  CB  TYR A 220      10.099  36.347  51.497  1.00205.46
ATOM    683  CG  TYR A 220       9.594  37.767  51.620  0.00 99.99
ATOM    684  CD1 TYR A 220       9.883  38.712  50.645  0.00 99.99
ATOM    685  CD2 TYR A 220       8.829  38.158  52.712  0.00 99.99
ATOM    686  CE1 TYR A 220       9.427  40.011  50.750  0.00 99.99
ATOM    687  CE2 TYR A 220       8.363  39.452  52.834  0.00 99.99
ATOM    688  CZ  TYR A 220       8.662  40.379  51.851  0.00 99.99
ATOM    689  OH  TYR A 220       8.204  41.670  51.963  0.00 99.99
ATOM    690  N   GLN A 221      11.620  35.627  54.332  1.00203.21
ATOM    691  CA  GLN A 221      11.835  35.884  55.760  1.00202.43
ATOM    692  C   GLN A 221      13.319  35.731  56.116  1.00202.12
ATOM    693  O   GLN A 221      13.759  36.315  57.113  1.00202.28
ATOM    694  CB  GLN A 221      10.981  34.941  56.609  1.00204.36
ATOM    695  CG  GLN A 221      11.309  33.467  56.421  0.00 99.99
ATOM    696  CD  GLN A 221      10.444  32.565  57.277  0.00 99.99
ATOM    697  OE1 GLN A 221      10.452  32.663  58.505  0.00 99.99
ATOM    698  NE2 GLN A 221       9.692  31.681  56.631  0.00 99.99
ATOM    699  N   ASP A 222      14.093  34.965  55.299  1.00194.28
ATOM    700  CA  ASP A 222      15.526  34.759  55.518  1.00191.47
ATOM    701  C   ASP A 222      16.322  36.000  55.156  1.00193.48
ATOM    702  O   ASP A 222      17.517  36.032  55.410  1.00191.87
ATOM    703  CB  ASP A 222      16.025  33.560  54.709  1.00191.96
ATOM    704  CG  ASP A 222      17.437  33.153  55.081  0.00 99.99
ATOM    705  OD1 ASP A 222      18.222  34.036  55.487  0.00 99.99
ATOM    706  OD2 ASP A 222      17.759  31.953  54.967  0.00 99.99
ATOM    707  N   SER A 223      15.684  37.018  54.583  1.00190.75
ATOM    708  CA  SER A 223      16.359  38.257  54.194  1.00190.96
ATOM    709  C   SER A 223      16.010  39.444  55.110  1.00194.40
ATOM    710  O   SER A 223      16.873  40.271  55.387  1.00193.45
ATOM    711  CB  SER A 223      16.018  38.622  52.748  1.00195.05
ATOM    712  OG  SER A 223      14.629  38.855  52.595  1.00204.31
ATOM    713  N   LEU A 224      14.756  39.544  55.546  1.00191.38
ATOM    714  CA  LEU A 224      14.320  40.689  56.307  1.00192.87
ATOM    715  C   LEU A 224      14.146  40.409  57.795  1.00198.53
ATOM    716  O   LEU A 224      14.943  40.896  58.601  1.00198.77
ATOM    717  CB  LEU A 224      13.001  41.230  55.753  1.00194.56
ATOM    718  CG  LEU A 224      13.045  41.804  54.335  0.00 99.99
ATOM    719  CD1 LEU A 224      11.647  42.168  53.859  0.00 99.99
ATOM    720  CD2 LEU A 224      13.903  43.058  54.291  0.00 99.99
ATOM    721  N   ALA A 225      13.096  39.673  58.178  1.00195.51
ATOM    722  CA  ALA A 225      12.806  39.415  59.594  1.00195.04
ATOM    723  C   ALA A 225      14.004  38.809  60.344  1.00194.98
ATOM    724  O   ALA A 225      14.258  39.151  61.512  1.00194.13
ATOM    725  CB  ALA A 225      11.595  38.482  59.736  1.00196.26
ATOM    726  N   CYS A 226      14.755  37.938  59.637  1.00188.36
ATOM    727  CA  CYS A 226      15.913  37.238  60.167  1.00185.34
ATOM    728  C   CYS A 226      17.032  38.201  60.554  1.00186.25
ATOM    729  O   CYS A 226      17.825  37.884  61.440  1.00185.05
ATOM    730  CB  CYS A 226      16.435  36.220  59.151  1.00184.34
ATOM    731  SG  CYS A 226      17.839  35.218  59.741  1.00186.98
ATOM    732  N   ARG A 227      17.105  39.355  59.890  1.00181.75
ATOM    733  CA  ARG A 227      18.174  40.315  60.105  1.00180.94
ATOM    734  C   ARG A 227      18.393  40.667  61.591  1.00183.10
ATOM    735  O   ARG A 227      19.465  40.382  62.135  1.00181.27
ATOM    736  CB  ARG A 227      17.902  41.603  59.326  1.00181.40
ATOM    737  CG  ARG A 227      17.959  41.439  57.816  1.00183.05
ATOM    738  CD  ARG A 227      17.998  42.787  57.115  1.00189.17
ATOM    739  NE  ARG A 227      16.770  43.549  57.324  1.00195.59
ATOM    740  CZ  ARG A 227      15.674  43.413  56.585  1.00206.88
ATOM    741  NH1 ARG A 227      15.650  42.543  55.586  1.00192.36
ATOM    742  NH2 ARG A 227      14.603  44.151  56.849  1.00192.54
ATOM    743  N   LEU A 228      17.384  41.283  62.235  1.00179.39
ATOM    744  CA  LEU A 228      17.515  41.830  63.587  1.00178.44
ATOM    745  C   LEU A 228      17.267  40.829  64.709  1.00179.16
ATOM    746  O   LEU A 228      17.807  41.012  65.808  1.00178.86
ATOM    747  CB  LEU A 228      16.561  43.010  63.783  1.00180.11
ATOM    748  CG  LEU A 228      16.829  44.248  62.924  0.00 99.99
ATOM    749  CD1 LEU A 228      15.727  45.280  63.112  0.00 99.99
ATOM    750  CD2 LEU A 228      18.152  44.891  63.308  0.00 99.99
ATOM    751  N   VAL A 229      16.457  39.793  64.460  1.00172.17
ATOM    752  CA  VAL A 229      16.115  38.844  65.512  1.00169.55
ATOM    753  C   VAL A 229      17.319  37.957  65.833  1.00167.67
ATOM    754  O   VAL A 229      17.723  37.860  66.995  1.00168.61
ATOM    755  CB  VAL A 229      14.916  37.965  65.111  1.00173.46
ATOM    756  CG1 VAL A 229      14.656  36.903  66.169  1.00172.58
ATOM    757  CG2 VAL A 229      13.661  38.812  64.961  1.00174.98
ATOM    758  N   PHE A 230      17.922  37.366  64.805  1.00158.42
ATOM    759  CA  PHE A 230      19.086  36.498  64.965  1.00154.74
ATOM    760  C   PHE A 230      20.251  37.241  65.677  1.00152.85
ATOM    761  O   PHE A 230      21.075  36.627  66.358  1.00148.17
ATOM    762  CB  PHE A 230      19.552  35.971  63.607  1.00155.92
ATOM    763  CG  PHE A 230      20.705  35.012  63.692  1.00156.68
ATOM    764  CD1 PHE A 230      20.497  33.685  64.026  1.00158.93
ATOM    765  CD2 PHE A 230      21.997  35.434  63.437  1.00158.94
ATOM    766  CE1 PHE A 230      21.557  32.802  64.105  1.00159.06
ATOM    767  CE2 PHE A 230      23.059  34.555  63.516  1.00160.78
ATOM    768  CZ  PHE A 230      22.839  33.237  63.849  1.00157.90
ATOM    769  N   LEU A 231      20.284  38.563  65.545  1.00150.70
ATOM    770  CA  LEU A 231      21.281  39.373  66.228  1.00150.51
ATOM    771  C   LEU A 231      21.004  39.384  67.732  1.00150.47
ATOM    772  O   LEU A 231      21.899  39.073  68.522  1.00150.39
ATOM    773  CB  LEU A 231      21.291  40.796  65.668  1.00152.14
ATOM    774  CG  LEU A 231      21.722  40.948  64.207  1.00158.14
ATOM    775  CD1 LEU A 231      21.545  42.385  63.741  1.00159.38
ATOM    776  CD2 LEU A 231      23.185  40.570  64.038  1.00160.57
ATOM    777  N   LEU A 232      19.776  39.740  68.123  1.00143.93
ATOM    778  CA  LEU A 232      19.392  39.757  69.532  1.00142.96
ATOM    779  C   LEU A 232      19.487  38.356  70.146  1.00143.51
ATOM    780  O   LEU A 232      19.831  38.233  71.322  1.00141.84
ATOM    781  CB  LEU A 232      17.975  40.309  69.695  1.00144.26
ATOM    782  CG  LEU A 232      17.769  41.775  69.304  1.00149.47
ATOM    783  CD1 LEU A 232      16.296  42.147  69.375  1.00149.31
ATOM    784  CD2 LEU A 232      18.537  42.693  70.241  1.00151.21
ATOM    785  N   CYS A 233      19.200  37.310  69.347  1.00139.09
ATOM    786  CA  CYS A 233      19.301  35.916  69.772  1.00137.40
ATOM    787  C   CYS A 233      20.750  35.621  70.157  1.00138.52
ATOM    788  O   CYS A 233      21.012  35.047  71.223  1.00136.70
ATOM    789  CB  CYS A 233      18.818  34.981  68.662  1.00137.72
ATOM    790  SG  CYS A 233      18.817  33.215  69.111  1.00141.12
ATOM    791  N   GLN A 234      21.694  36.067  69.311  1.00135.03
ATOM    792  CA  GLN A 234      23.114  35.851  69.555  1.00134.65
ATOM    793  C   GLN A 234      23.556  36.595  70.825  1.00140.05
ATOM    794  O   GLN A 234      24.411  36.108  71.568  1.00139.75
ATOM    795  CB  GLN A 234      23.940  36.305  68.350  1.00135.67
ATOM    796  CG  GLN A 234      23.694  35.495  67.088  1.00147.06
ATOM    797  CD  GLN A 234      24.134  34.051  67.228  1.00165.33
ATOM    798  OE1 GLN A 234      25.175  33.764  67.818  1.00162.22
ATOM    799  NE2 GLN A 234      23.338  33.137  66.685  1.00150.97
ATOM    800  N   TYR A 235      22.928  37.739  71.106  1.00138.01
ATOM    801  CA  TYR A 235      23.205  38.482  72.330  1.00138.74
ATOM    802  C   TYR A 235      22.607  37.749  73.541  1.00144.68
ATOM    803  O   TYR A 235      23.253  37.648  74.584  1.00143.83
ATOM    804  CB  TYR A 235      22.650  39.904  72.231  1.00140.36
ATOM    805  CG  TYR A 235      22.958  40.767  73.434  1.00142.51
ATOM    806  CD1 TYR A 235      24.200  41.370  73.578  1.00144.30
ATOM    807  CD2 TYR A 235      22.004  40.978  74.422  1.00144.16
ATOM    808  CE1 TYR A 235      24.490  42.159  74.674  1.00145.04
ATOM    809  CE2 TYR A 235      22.275  41.764  75.524  1.00145.94
ATOM    810  CZ  TYR A 235      23.519  42.355  75.649  1.00152.10
ATOM    811  OH  TYR A 235      23.800  43.140  76.742  1.00152.43
ATOM    812  N   CYS A 236      21.381  37.241  73.402  1.00143.31
ATOM    813  CA  CYS A 236      20.726  36.495  74.468  1.00144.36
ATOM    814  C   CYS A 236      21.576  35.323  74.895  1.00147.59
ATOM    815  O   CYS A 236      21.822  35.139  76.086  1.00148.23
ATOM    816  CB  CYS A 236      19.345  36.017  74.017  1.00146.01
ATOM    817  SG  CYS A 236      18.155  37.357  73.687  1.00152.27
ATOM    818  N   VAL A 237      22.032  34.523  73.920  1.00142.58
ATOM    819  CA  VAL A 237      22.857  33.350  74.212  1.00141.01
ATOM    820  C   VAL A 237      24.129  33.772  74.956  1.00142.84
ATOM    821  O   VAL A 237      24.505  33.159  75.968  1.00139.26
ATOM    822  CB  VAL A 237      23.235  32.592  72.926  1.00143.37
ATOM    823  CG1 VAL A 237      24.192  31.452  73.241  1.00142.63
ATOM    824  CG2 VAL A 237      21.994  32.011  72.266  1.00143.22
ATOM    825  N   ALA A 238      24.757  34.849  74.471  1.00140.65
ATOM    826  CA  ALA A 238      25.938  35.387  75.107  1.00140.62
ATOM    827  C   ALA A 238      25.615  35.805  76.549  1.00145.10
ATOM    828  O   ALA A 238      26.466  35.641  77.430  1.00146.49
ATOM    829  CB  ALA A 238      26.488  36.577  74.307  1.00141.74
ATOM    830  N   ALA A 239      24.380  36.318  76.799  1.00139.02
ATOM    831  CA  ALA A 239      23.953  36.743  78.133  1.00137.44
ATOM    832  C   ALA A 239      23.675  35.562  79.050  1.00139.64
ATOM    833  O   ALA A 239      23.982  35.644  80.231  1.00137.94
ATOM    834  CB  ALA A 239      22.702  37.629  78.043  1.00138.83
ATOM    835  N   ASN A 240      23.135  34.448  78.519  1.00137.17
ATOM    836  CA  ASN A 240      22.927  33.223  79.298  1.00135.77
ATOM    837  C   ASN A 240      24.238  32.768  79.923  1.00137.85
ATOM    838  O   ASN A 240      24.344  32.645  81.146  1.00137.92
ATOM    839  CB  ASN A 240      22.339  32.120  78.416  1.00134.67
ATOM    840  CG  ASN A 240      20.905  32.399  78.012  1.00160.41
ATOM    841  OD1 ASN A 240      20.209  33.180  78.659  1.00150.62
ATOM    842  ND2 ASN A 240      20.460  31.761  76.937  1.00157.44
ATOM    843  N   TYR A 241      25.250  32.577  79.083  1.00133.44
ATOM    844  CA  TYR A 241      26.548  32.076  79.508  1.00133.66
ATOM    845  C   TYR A 241      27.274  33.036  80.463  1.00138.53
ATOM    846  O   TYR A 241      27.981  32.572  81.356  1.00138.16
ATOM    847  CB  TYR A 241      27.440  31.802  78.296  1.00134.97
ATOM    848  CG  TYR A 241      26.933  30.694  77.399  1.00135.83
ATOM    849  CD1 TYR A 241      27.229  29.365  77.674  1.00136.92
ATOM    850  CD2 TYR A 241      26.160  30.981  76.282  1.00137.11
ATOM    851  CE1 TYR A 241      26.769  28.348  76.861  1.00136.72
ATOM    852  CE2 TYR A 241      25.691  29.976  75.457  1.00138.76
ATOM    853  CZ  TYR A 241      25.997  28.661  75.749  1.00146.80
ATOM    854  OH  TYR A 241      25.536  27.652  74.934  1.00147.84
ATOM    855  N   TYR A 242      27.062  34.352  80.314  1.00136.55
ATOM    856  CA  TYR A 242      27.742  35.340  81.145  1.00137.73
ATOM    857  C   TYR A 242      26.991  35.648  82.450  1.00143.19
ATOM    858  O   TYR A 242      27.618  36.060  83.433  1.00144.20
ATOM    859  CB  TYR A 242      27.950  36.641  80.368  1.00139.46
ATOM    860  CG  TYR A 242      28.880  36.506  79.183  1.00142.82
ATOM    861  CD1 TYR A 242      29.910  35.574  79.190  1.00144.64
ATOM    862  CD2 TYR A 242      28.725  37.311  78.062  1.00145.11
ATOM    863  CE1 TYR A 242      30.764  35.444  78.113  1.00146.67
ATOM    864  CE2 TYR A 242      29.570  37.195  76.975  1.00146.63
ATOM    865  CZ  TYR A 242      30.589  36.260  77.001  1.00157.05
ATOM    866  OH  TYR A 242      31.435  36.138  75.925  1.00161.56
ATOM    867  N   TRP A 243      25.672  35.432  82.479  1.00138.13
ATOM    868  CA  TRP A 243      24.943  35.543  83.728  1.00137.24
ATOM    869  C   TRP A 243      25.138  34.246  84.497  1.00139.51
ATOM    870  O   TRP A 243      25.022  34.239  85.732  1.00140.57
ATOM    871  CB  TRP A 243      23.465  35.832  83.462  1.00136.09
ATOM    872  CG  TRP A 243      23.220  37.161  82.814  1.00137.91
ATOM    873  CD1 TRP A 243      23.079  37.408  81.479  1.00141.20
ATOM    874  CD2 TRP A 243      23.089  38.425  83.477  1.00138.98
ATOM    875  NE1 TRP A 243      22.868  38.749  81.265  1.00142.09
ATOM    876  CE2 TRP A 243      22.869  39.395  82.478  1.00144.16
ATOM    877  CE3 TRP A 243      23.135  38.828  84.813  1.00140.88
ATOM    878  CZ2 TRP A 243      22.696  40.746  82.774  1.00145.04
ATOM    879  CZ3 TRP A 243      22.963  40.168  85.106  1.00143.75
ATOM    880  CH2 TRP A 243      22.745  41.116  84.093  1.00145.40
ATOM    881  N   LEU A 244      25.471  33.152  83.774  1.00132.50
ATOM    882  CA  LEU A 244      25.868  31.904  84.410  1.00131.21
ATOM    883  C   LEU A 244      27.220  32.140  85.120  1.00131.42
ATOM    884  O   LEU A 244      27.447  31.614  86.228  1.00130.66
ATOM    885  CB  LEU A 244      25.957  30.780  83.376  1.00131.11
ATOM    886  CG  LEU A 244      24.645  30.375  82.700  1.00136.23
ATOM    887  CD1 LEU A 244      24.900  29.358  81.598  1.00136.36
ATOM    888  CD2 LEU A 244      23.691  29.754  83.708  1.00139.09
ATOM    889  N   LEU A 245      28.093  32.964  84.491  1.00124.12
ATOM    890  CA  LEU A 245      29.383  33.272  85.066  1.00123.42
ATOM    891  C   LEU A 245      29.226  33.989  86.411  1.00131.45
ATOM    892  O   LEU A 245      29.788  33.555  87.426  1.00132.71
ATOM    893  CB  LEU A 245      30.209  34.127  84.103  1.00122.85
ATOM    894  CG  LEU A 245      31.004  33.372  83.037  1.00127.07
ATOM    895  CD1 LEU A 245      30.068  32.654  82.077  1.00127.70
ATOM    896  CD2 LEU A 245      31.870  34.328  82.232  1.00127.88
ATOM    897  N   VAL A 246      28.434  35.059  86.430  1.00128.41
ATOM    898  CA  VAL A 246      28.253  35.849  87.651  1.00128.27
ATOM    899  C   VAL A 246      27.501  35.027  88.679  1.00130.63
ATOM    900  O   VAL A 246      27.700  35.241  89.866  1.00132.25
ATOM    901  CB  VAL A 246      27.496  37.159  87.368  1.00133.08
ATOM    902  CG1 VAL A 246      27.212  37.902  88.665  1.00133.33
ATOM    903  CG2 VAL A 246      28.320  38.066  86.465  1.00132.78
ATOM    904  N   GLU A 247      26.662  34.074  88.234  1.00124.93
ATOM    905  CA  GLU A 247      25.970  33.181  89.160  1.00124.92
ATOM    906  C   GLU A 247      26.987  32.337  89.904  1.00129.47
ATOM    907  O   GLU A 247      26.900  32.164  91.125  1.00127.18
ATOM    908  CB  GLU A 247      24.970  32.300  88.409  1.00125.87
ATOM    909  CG  GLU A 247      24.151  31.387  89.306  1.00136.89
ATOM    910  CD  GLU A 247      23.236  32.155  90.240  1.00160.55
ATOM    911  OE1 GLU A 247      23.099  33.383  90.060  1.00183.07
ATOM    912  OE2 GLU A 247      22.656  31.528  91.151  1.00135.36
ATOM    913  N   GLY A 248      27.953  31.826  89.151  1.00129.82
ATOM    914  CA  GLY A 248      29.032  31.037  89.725  1.00131.91
ATOM    915  C   GLY A 248      29.972  31.888  90.554  1.00139.64
ATOM    916  O   GLY A 248      30.505  31.434  91.576  1.00140.60
ATOM    917  N   VAL A 249      30.170  33.136  90.120  1.00136.60
ATOM    918  CA  VAL A 249      31.044  34.058  90.825  1.00137.21
ATOM    919  C   VAL A 249      30.386  34.445  92.146  1.00142.64
ATOM    920  O   VAL A 249      31.048  34.431  93.184  1.00143.47
ATOM    921  CB  VAL A 249      31.337  35.313  89.983  1.00140.85
ATOM    922  CG1 VAL A 249      32.150  36.317  90.786  1.00141.63
ATOM    923  CG2 VAL A 249      32.125  34.945  88.735  1.00140.44
ATOM    924  N   TYR A 250      29.086  34.766  92.114  1.00139.19
ATOM    925  CA  TYR A 250      28.353  35.099  93.324  1.00139.64
ATOM    926  C   TYR A 250      28.372  33.906  94.290  1.00145.32
ATOM    927  O   TYR A 250      28.457  34.092  95.510  1.00145.24
ATOM    928  CB  TYR A 250      26.917  35.503  92.987  1.00140.88
ATOM    929  CG  TYR A 250      26.104  35.936  94.186  1.00144.23
ATOM    930  CD1 TYR A 250      26.234  37.215  94.711  1.00147.49
ATOM    931  CD2 TYR A 250      25.207  35.063  94.790  1.00145.25
ATOM    932  CE1 TYR A 250      25.496  37.617  95.806  1.00150.06
ATOM    933  CE2 TYR A 250      24.460  35.448  95.886  1.00147.41
ATOM    934  CZ  TYR A 250      24.605  36.726  96.393  1.00159.06
ATOM    935  OH  TYR A 250      23.867  37.120  97.484  1.00164.99
ATOM    936  N   LEU A 251      28.312  32.680  93.745  1.00142.18
ATOM    937  CA  LEU A 251      28.388  31.488  94.576  1.00141.90
ATOM    938  C   LEU A 251      29.784  31.363  95.191  1.00145.64
ATOM    939  O   LEU A 251      29.910  30.892  96.323  1.00144.82
ATOM    940  CB  LEU A 251      28.044  30.242  93.758  1.00141.59
ATOM    941  CG  LEU A 251      26.612  30.153  93.226  1.00146.71
ATOM    942  CD1 LEU A 251      26.451  28.946  92.315  1.00146.67
ATOM    943  CD2 LEU A 251      25.622  30.019  94.372  1.00150.06
ATOM    944  N   TYR A 252      30.826  31.806  94.462  1.00142.74
ATOM    945  CA  TYR A 252      32.175  31.769  95.004  1.00143.82
ATOM    946  C   TYR A 252      32.312  32.798  96.118  1.00146.78
ATOM    947  O   TYR A 252      32.908  32.500  97.153  1.00145.53
ATOM    948  CB  TYR A 252      33.203  32.021  93.900  1.00146.59
ATOM    949  CG  TYR A 252      34.639  31.928  94.366  1.00151.75
ATOM    950  CD1 TYR A 252      35.258  30.695  94.523  1.00153.97
ATOM    951  CD2 TYR A 252      35.371  33.075  94.649  1.00154.73
ATOM    952  CE1 TYR A 252      36.568  30.602  94.949  1.00156.48
ATOM    953  CE2 TYR A 252      36.682  33.001  95.075  1.00157.43
ATOM    954  CZ  TYR A 252      37.280  31.763  95.225  1.00166.02
ATOM    955  OH  TYR A 252      38.585  31.678  95.649  1.00169.95
ATOM    956  N   THR A 253      31.778  34.008  95.899  1.00144.45
ATOM    957  CA  THR A 253      31.836  35.081  96.898  1.00145.78
ATOM    958  C   THR A 253      31.028  34.706  98.136  1.00152.01
ATOM    959  O   THR A 253      31.433  35.029  99.260  1.00153.55
ATOM    960  CB  THR A 253      31.311  36.411  96.328  1.00153.51
ATOM    961  OG1 THR A 253      32.177  36.858  95.276  1.00150.94
ATOM    962  CG2 THR A 253      31.265  37.476  97.414  1.00153.93
ATOM    963  N   LEU A 254      29.903  33.990  97.936  1.00147.33
ATOM    964  CA  LEU A 254      29.043  33.565  99.037  1.00146.19
ATOM    965  C   LEU A 254      29.702  32.472  99.874  1.00146.78
ATOM    966  O   LEU A 254      29.240  32.196 100.984  1.00146.82
ATOM    967  CB  LEU A 254      27.696  33.073  98.505  1.00145.90
ATOM    968  CG  LEU A 254      26.816  34.118  97.816  1.00151.80
ATOM    969  CD1 LEU A 254      25.582  33.467  97.211  1.00153.49
ATOM    970  CD2 LEU A 254      26.357  35.173  98.810  1.00154.21
ATOM    971  N   LEU A 255      30.788  31.871  99.361  1.00140.50
ATOM    972  CA  LEU A 255      31.508  30.819 100.071  1.00139.21
ATOM    973  C   LEU A 255      32.874  31.295 100.566  1.00143.88
ATOM    974  O   LEU A 255      33.332  30.838 101.601  1.00141.54
ATOM    975  CB  LEU A 255      31.683  29.591  99.176  1.00137.99
ATOM    976  CG  LEU A 255      30.402  28.862  98.766  1.00140.62
ATOM    977  CD1 LEU A 255      30.708  27.758  97.765  1.00139.25
ATOM    978  CD2 LEU A 255      29.732  28.232  99.977  1.00142.62
ATOM    979  N   ALA A 256      33.522  32.204  99.839  1.00144.48
ATOM    980  CA  ALA A 256      34.825  32.737 100.241  1.00147.44
ATOM    981  C   ALA A 256      34.704  33.751 101.385  1.00156.96
ATOM    982  O   ALA A 256      35.731  34.101 101.982  1.00158.50
ATOM    983  CB  ALA A 256      35.533  33.391  99.045  1.00148.41
ATOM    984  N   PHE A 257      33.465  34.239 101.683  1.00154.76
ATOM    985  CA  PHE A 257      33.198  35.163 102.799  1.00178.95
ATOM    986  C   PHE A 257      33.402  34.457 104.165  1.00217.12
ATOM    987  O   PHE A 257      33.254  33.231 104.299  1.00171.36
ATOM    988  CB  PHE A 257      31.779  35.726 102.701  1.00180.10
ATOM    989  CG  PHE A 257      31.452  36.733 103.765  0.00 99.99
ATOM    990  CD1 PHE A 257      31.876  38.046 103.651  0.00 99.99
ATOM    991  CD2 PHE A 257      30.719  36.371 104.881  0.00 99.99
ATOM    992  CE1 PHE A 257      31.575  38.974 104.630  0.00 99.99
ATOM    993  CE2 PHE A 257      30.418  37.295 105.863  0.00 99.99
ATOM    994  CZ  PHE A 257      30.845  38.598 105.736  0.00 99.99
ATOM    995  N   MET A1001      37.670  39.086 109.034  1.00151.15
ATOM    996  CA  MET A1001      36.319  38.941 109.597  1.00151.27
ATOM    997  C   MET A1001      35.241  39.287 108.577  1.00157.20
ATOM    998  O   MET A1001      35.452  40.224 107.802  1.00158.91
ATOM    999  CB  MET A1001      36.159  39.820 110.839  1.00154.72
ATOM   1000  CG  MET A1001      37.047  39.417 112.003  0.00 99.99
ATOM   1001  SD  MET A1001      36.639  37.791 112.662  0.00 99.99
ATOM   1002  CE  MET A1001      35.057  38.126 113.433  0.00 99.99
ATOM   1003  N   LYS A1002      34.087  38.553 108.578  1.00152.21
ATOM   1004  CA  LYS A1002      32.989  38.781 107.616  1.00150.69
ATOM   1005  C   LYS A1002      31.755  39.354 108.315  1.00153.11
ATOM   1006  O   LYS A1002      31.352  38.881 109.378  1.00150.29
ATOM   1007  CB  LYS A1002      32.630  37.481 106.894  1.00151.57
ATOM   1008  CG  LYS A1002      33.763  36.898 106.066  0.00 99.99
ATOM   1009  CD  LYS A1002      34.081  37.779 104.869  0.00 99.99
ATOM   1010  CE  LYS A1002      35.215  37.196 104.040  0.00 99.99
ATOM   1011  NZ  LYS A1002      35.539  38.049 102.863  0.00 99.99
ATOM   1012  N   LYS A1003      31.178  40.392 107.688  1.00151.67
ATOM   1013  CA  LYS A1003      30.023  41.149 108.159  1.00153.03
ATOM   1014  C   LYS A1003      28.825  40.967 107.254  1.00157.63
ATOM   1015  O   LYS A1003      28.946  40.423 106.162  1.00157.25
ATOM   1016  CB  LYS A1003      30.366  42.636 108.271  1.00157.49
ATOM   1017  CG  LYS A1003      31.384  42.958 109.352  0.00 99.99
ATOM   1018  CD  LYS A1003      31.678  44.449 109.408  0.00 99.99
ATOM   1019  CE  LYS A1003      32.697  44.770 110.489  0.00 99.99
ATOM   1020  NZ  LYS A1003      32.174  44.473 111.851  0.00 99.99
ATOM   1021  N   TYR A1004      27.665  41.433 107.718  1.00155.55
ATOM   1022  CA  TYR A1004      26.397  41.287 107.031  1.00156.08
ATOM   1023  C   TYR A1004      25.579  42.562 107.095  1.00164.34
ATOM   1024  O   TYR A1004      25.991  43.528 107.728  1.00166.31
ATOM   1025  CB  TYR A1004      25.598  40.125 107.623  1.00157.39
ATOM   1026  CG  TYR A1004      26.243  38.772 107.422  1.00158.83
ATOM   1027  CD1 TYR A1004      26.044  38.056 106.248  1.00161.39
ATOM   1028  CD2 TYR A1004      27.048  38.214 108.407  1.00158.28
ATOM   1029  CE1 TYR A1004      26.630  36.820 106.057  1.00162.08
ATOM   1030  CE2 TYR A1004      27.642  36.979 108.233  1.00158.09
ATOM   1031  CZ  TYR A1004      27.432  36.284 107.057  1.00168.70
ATOM   1032  OH  TYR A1004      28.019  35.054 106.873  1.00174.05
ATOM   1033  N   THR A1005      24.418  42.570 106.439  1.00163.00
ATOM   1034  CA  THR A1005      23.521  43.721 106.411  1.00165.74
ATOM   1035  C   THR A1005      22.063  43.283 106.392  1.00173.93
ATOM   1036  O   THR A1005      21.717  42.202 106.889  1.00174.26
ATOM   1037  CB  THR A1005      23.793  44.618 105.190  0.00 99.99
ATOM   1038  OG1 THR A1005      22.974  45.792 105.263  0.00 99.99
ATOM   1039  CG2 THR A1005      23.475  43.876 103.901  0.00 99.99
ATOM   1040  N   CYS A1006      21.204  44.124 105.826  1.00173.41
ATOM   1041  CA  CYS A1006      19.765  43.861 105.750  1.00175.37
ATOM   1042  C   CYS A1006      19.210  44.372 104.416  1.00181.81
ATOM   1043  O   CYS A1006      19.782  45.297 103.842  1.00183.64
ATOM   1044  CB  CYS A1006      19.038  44.514 106.927  1.00178.15
ATOM   1045  SG  CYS A1006      17.247  44.182 106.985  1.00184.55
ATOM   1046  N   THR A1007      18.109  43.764 103.918  1.00177.38
ATOM   1047  CA  THR A1007      17.475  44.143 102.645  1.00176.88
ATOM   1048  C   THR A1007      16.220  45.015 102.843  1.00181.24
ATOM   1049  O   THR A1007      15.863  45.757 101.927  1.00182.52
ATOM   1050  CB  THR A1007      17.077  42.904 101.822  1.00182.02
ATOM   1051  OG1 THR A1007      16.114  42.132 102.551  1.00180.45
ATOM   1052  CG2 THR A1007      18.295  42.036 101.543  1.00177.45
ATOM   1053  N   VAL A1008      15.544  44.919 103.995  1.00176.59
ATOM   1054  CA  VAL A1008      14.311  45.662 104.202  1.00179.00
ATOM   1055  C   VAL A1008      14.622  47.135 104.488  1.00185.98
ATOM   1056  O   VAL A1008      14.444  47.984 103.608  1.00185.69
ATOM   1057  CB  VAL A1008      13.485  45.073 105.360  1.00183.74
ATOM   1058  CG1 VAL A1008      12.265  45.937 105.639  0.00 99.99
ATOM   1059  CG2 VAL A1008      13.012  43.669 105.017  0.00 99.99
ATOM   1060  N   CYS A1009      15.118  47.423 105.703  1.00184.93
ATOM   1061  CA  CYS A1009      15.480  48.768 106.144  1.00187.29
ATOM   1062  C   CYS A1009      16.948  49.081 105.836  1.00193.18
ATOM   1063  O   CYS A1009      17.312  50.261 105.781  1.00194.19
ATOM   1064  CB  CYS A1009      15.213  48.931 107.641  1.00188.83
ATOM   1065  SG  CYS A1009      16.184  47.815 108.705  1.00189.77
ATOM   1066  N   GLY A1010      17.773  48.041 105.679  1.00189.60
ATOM   1067  CA  GLY A1010      19.199  48.188 105.404  1.00188.72
ATOM   1068  C   GLY A1010      20.095  48.329 106.630  1.00193.59
ATOM   1069  O   GLY A1010      21.167  48.940 106.532  1.00195.18
ATOM   1070  N   TYR A1011      19.682  47.767 107.797  1.00187.08
ATOM   1071  CA  TYR A1011      20.497  47.791 109.015  1.00184.89
ATOM   1072  C   TYR A1011      21.749  46.949 108.813  1.00182.62
ATOM   1073  O   TYR A1011      21.669  45.847 108.258  1.00181.47
ATOM   1074  CB  TYR A1011      19.688  47.287 110.211  1.00186.66
ATOM   1075  CG  TYR A1011      20.434  47.347 111.525  1.00187.14
ATOM   1076  CD1 TYR A1011      20.542  48.539 112.229  1.00190.24
ATOM   1077  CD2 TYR A1011      21.028  46.210 112.059  1.00185.80
ATOM   1078  CE1 TYR A1011      21.223  48.603 113.428  1.00190.01
ATOM   1079  CE2 TYR A1011      21.712  46.254 113.258  1.00186.01
ATOM   1080  CZ  TYR A1011      21.808  47.452 113.942  1.00194.87
ATOM   1081  OH  TYR A1011      22.487  47.507 115.137  1.00196.72
ATOM   1082  N   ILE A1012      22.901  47.468 109.250  1.00175.51
ATOM   1083  CA  ILE A1012      24.162  46.755 109.106  1.00171.92
ATOM   1084  C   ILE A1012      24.498  46.078 110.420  1.00171.25
ATOM   1085  O   ILE A1012      24.745  46.748 111.419  1.00170.84
ATOM   1086  CB  ILE A1012      25.301  47.702 108.686  1.00175.94
ATOM   1087  CG1 ILE A1012      25.036  48.269 107.290  1.00177.36
ATOM   1088  CG2 ILE A1012      26.629  46.962 108.662  1.00174.86
ATOM   1089  CD1 ILE A1012      25.975  49.387 106.896  1.00187.10
ATOM   1090  N   TYR A1013      24.506  44.743 110.414  1.00164.97
ATOM   1091  CA  TYR A1013      24.850  43.977 111.598  1.00163.52
ATOM   1092  C   TYR A1013      26.351  43.837 111.699  1.00166.55
ATOM   1093  O   TYR A1013      26.940  42.985 111.019  1.00163.05
ATOM   1094  CB  TYR A1013      24.176  42.604 111.563  1.00162.24
ATOM   1095  CG  TYR A1013      22.666  42.660 111.629  1.00162.88
ATOM   1096  CD1 TYR A1013      22.022  43.690 112.303  1.00166.07
ATOM   1097  CD2 TYR A1013      21.891  41.683 111.019  1.00162.21
ATOM   1098  CE1 TYR A1013      20.644  43.749 112.369  1.00166.71
ATOM   1099  CE2 TYR A1013      20.511  41.726 111.075  1.00162.89
ATOM   1100  CZ  TYR A1013      19.888  42.760 111.750  1.00172.53
ATOM   1101  OH  TYR A1013      18.516  42.811 111.811  1.00176.44
ATOM   1102  N   ASN A1014      26.969  44.657 112.566  1.00165.19
ATOM   1103  CA  ASN A1014      28.403  44.563 112.807  1.00164.32
ATOM   1104  C   ASN A1014      28.655  43.331 113.663  1.00165.06
ATOM   1105  O   ASN A1014      28.192  43.298 114.800  1.00163.75
ATOM   1106  CB  ASN A1014      28.918  45.837 113.478  1.00168.31
ATOM   1107  CG  ASN A1014      30.428  45.852 113.621  1.00178.30
ATOM   1108  OD1 ASN A1014      30.979  45.250 114.541  1.00163.82
ATOM   1109  ND2 ASN A1014      31.099  46.540 112.705  1.00169.47
ATOM   1110  N   PRO A1015      29.322  42.281 113.139  1.00161.10
ATOM   1111  CA  PRO A1015      29.576  41.106 113.982  1.00161.13
ATOM   1112  C   PRO A1015      30.603  41.408 115.077  1.00168.68
ATOM   1113  O   PRO A1015      30.439  40.946 116.214  1.00168.19
ATOM   1114  CB  PRO A1015      30.037  40.052 112.973  1.00160.70
ATOM   1115  CG  PRO A1015      29.358  40.453 111.683  1.00164.46
ATOM   1116  CD  PRO A1015      29.451  41.968 111.707  1.00161.20
ATOM   1117  N   GLU A1016      31.628  42.219 114.753  1.00168.33
ATOM   1118  CA  GLU A1016      32.643  42.616 115.721  1.00170.92
ATOM   1119  C   GLU A1016      31.985  43.372 116.921  1.00179.69
ATOM   1120  O   GLU A1016      32.511  43.330 118.034  1.00180.17
ATOM   1121  CB  GLU A1016      33.707  43.490 115.054  1.00173.06
ATOM   1122  CG  GLU A1016      34.846  43.893 115.976  0.00 99.99
ATOM   1123  CD  GLU A1016      34.482  45.054 116.880  0.00 99.99
ATOM   1124  OE1 GLU A1016      33.586  45.839 116.506  0.00 99.99
ATOM   1125  OE2 GLU A1016      35.092  45.179 117.963  0.00 99.99
ATOM   1126  N   ASP A1017      30.817  44.015 116.686  1.00178.03
ATOM   1127  CA  ASP A1017      30.031  44.701 117.702  1.00179.34
ATOM   1128  C   ASP A1017      28.890  43.800 118.236  1.00186.69
ATOM   1129  O   ASP A1017      28.467  43.990 119.374  1.00187.63
ATOM   1130  CB  ASP A1017      29.453  46.003 117.144  1.00181.68
ATOM   1131  CG  ASP A1017      30.515  47.057 116.904  0.00 99.99
ATOM   1132  OD1 ASP A1017      31.640  46.898 117.425  0.00 99.99
ATOM   1133  OD2 ASP A1017      30.225  48.043 116.196  0.00 99.99
ATOM   1134  N   GLY A1018      28.419  42.832 117.439  1.00184.97
ATOM   1135  CA  GLY A1018      27.346  41.915 117.826  1.00185.50
ATOM   1136  C   GLY A1018      26.030  42.614 118.107  1.00194.00
ATOM   1137  O   GLY A1018      25.738  43.660 117.510  1.00195.24
ATOM   1138  N   ASP A1019      25.229  42.043 119.025  1.00192.06
ATOM   1139  CA  ASP A1019      23.948  42.622 119.449  1.00194.25
ATOM   1140  C   ASP A1019      23.536  42.053 120.820  1.00197.90
ATOM   1141  O   ASP A1019      22.577  41.286 120.913  1.00196.52
ATOM   1142  CB  ASP A1019      22.865  42.350 118.404  1.00196.35
ATOM   1143  CG  ASP A1019      21.590  43.126 118.670  1.00210.59
ATOM   1144  OD1 ASP A1019      21.298  43.401 119.853  1.00211.32
ATOM   1145  OD2 ASP A1019      20.884  43.460 117.697  1.00217.04
ATOM   1146  N   PRO A1020      24.267  42.390 121.900  1.00196.07
ATOM   1147  CA  PRO A1020      23.929  41.821 123.223  1.00197.07
ATOM   1148  C   PRO A1020      22.690  42.449 123.858  1.00201.64
ATOM   1149  O   PRO A1020      22.060  41.822 124.721  1.00200.88
ATOM   1150  CB  PRO A1020      25.204  42.058 124.035  1.00198.66
ATOM   1151  CG  PRO A1020      26.306  42.062 123.000  1.00201.26
ATOM   1152  CD  PRO A1020      25.674  42.800 121.833  1.00198.27
ATOM   1153  N   ASP A1021      22.326  43.672 123.418  1.00200.24
ATOM   1154  CA  ASP A1021      21.119  44.382 123.850  1.00201.14
ATOM   1155  C   ASP A1021      19.870  43.519 123.586  1.00204.49
ATOM   1156  O   ASP A1021      18.799  43.814 124.110  1.00204.97
ATOM   1157  CB  ASP A1021      21.005  45.729 123.134  1.00202.97
ATOM   1158  CG  ASP A1021      22.051  46.724 123.594  1.00208.18
ATOM   1159  OD1 ASP A1021      22.676  46.486 124.650  1.00206.06
ATOM   1160  OD2 ASP A1021      22.248  47.743 122.900  1.00213.99
ATOM   1161  N   ASN A1022      20.020  42.455 122.773  1.00200.43
ATOM   1162  CA  ASN A1022      18.953  41.519 122.459  1.00200.53
ATOM   1163  C   ASN A1022      19.372  40.050 122.715  1.00203.07
ATOM   1164  O   ASN A1022      18.529  39.161 122.606  1.00203.14
ATOM   1165  CB  ASN A1022      18.509  41.680 121.004  1.00200.39
ATOM   1166  CG  ASN A1022      19.622  41.381 120.019  1.00211.75
ATOM   1167  OD1 ASN A1022      20.515  40.582 120.301  1.00199.87
ATOM   1168  ND2 ASN A1022      19.571  42.022 118.857  1.00202.87
ATOM   1169  N   GLY A1023      20.635  39.806 123.077  1.00198.13
ATOM   1170  CA  GLY A1023      21.086  38.470 123.451  1.00196.36
ATOM   1171  C   GLY A1023      22.121  37.786 122.590  1.00197.60
ATOM   1172  O   GLY A1023      22.111  36.557 122.493  1.00196.58
ATOM   1173  N   VAL A1024      23.030  38.553 121.980  1.00193.46
ATOM   1174  CA  VAL A1024      24.099  38.002 121.134  1.00191.77
ATOM   1175  C   VAL A1024      25.385  38.753 121.464  1.00196.37
ATOM   1176  O   VAL A1024      25.511  39.939 121.154  1.00195.89
ATOM   1177  CB  VAL A1024      23.756  38.127 119.638  1.00194.44
ATOM   1178  CG1 VAL A1024      24.925  37.665 118.782  1.00192.26
ATOM   1179  CG2 VAL A1024      22.543  37.273 119.297  1.00194.34
ATOM   1180  N   ASN A1025      26.345  38.056 122.072  1.00193.10
ATOM   1181  CA  ASN A1025      27.602  38.664 122.490  1.00193.75
ATOM   1182  C   ASN A1025      28.424  39.230 121.313  1.00197.59
ATOM   1183  O   ASN A1025      28.298  38.743 120.183  1.00196.64
ATOM   1184  CB  ASN A1025      28.458  37.653 123.255  1.00195.20
ATOM   1185  CG  ASN A1025      28.842  36.456 122.409  1.00219.06
ATOM   1186  OD1 ASN A1025      27.989  35.824 121.786  1.00219.24
ATOM   1187  ND2 ASN A1025      30.131  36.139 122.384  1.00213.80
ATOM   1188  N   PRO A1026      29.269  40.261 121.559  1.00194.88
ATOM   1189  CA  PRO A1026      30.078  40.822 120.467  1.00194.57
ATOM   1190  C   PRO A1026      31.134  39.834 119.986  1.00197.93
ATOM   1191  O   PRO A1026      31.855  39.250 120.804  1.00197.35
ATOM   1192  CB  PRO A1026      30.657  42.095 121.087  1.00197.83
ATOM   1193  CG  PRO A1026      29.634  42.500 122.124  1.00201.87
ATOM   1194  CD  PRO A1026      29.203  41.169 122.714  1.00197.81
ATOM   1195  N   GLY A1027      31.203  39.658 118.668  1.00193.91
ATOM   1196  CA  GLY A1027      32.139  38.742 118.028  1.00192.78
ATOM   1197  C   GLY A1027      31.472  37.458 117.584  1.00195.76
ATOM   1198  O   GLY A1027      32.057  36.380 117.710  1.00194.83
ATOM   1199  N   THR A1028      30.238  37.571 117.063  1.00192.32
ATOM   1200  CA  THR A1028      29.449  36.435 116.600  1.00191.33
ATOM   1201  C   THR A1028      28.985  36.661 115.161  1.00194.86
ATOM   1202  O   THR A1028      28.405  37.707 114.859  1.00194.84
ATOM   1203  CB  THR A1028      28.226  36.192 117.504  1.00198.75
ATOM   1204  OG1 THR A1028      28.665  35.809 118.814  1.00199.53
ATOM   1205  CG2 THR A1028      27.354  35.084 116.933  1.00195.35
ATOM   1206  N   ASP A1029      29.224  35.669 114.281  1.00190.39
ATOM   1207  CA  ASP A1029      28.817  35.749 112.882  1.00188.94
ATOM   1208  C   ASP A1029      27.323  35.508 112.745  1.00192.10
ATOM   1209  O   ASP A1029      26.727  34.832 113.589  1.00192.49
ATOM   1210  CB  ASP A1029      29.600  34.742 112.038  1.00189.79
ATOM   1211  CG  ASP A1029      29.396  34.946 110.549  1.00205.67
ATOM   1212  OD1 ASP A1029      28.306  35.414 110.158  1.00206.78
ATOM   1213  OD2 ASP A1029      30.324  34.638 109.774  1.00213.50
ATOM   1214  N   PHE A1030      26.718  36.043 111.664  1.00187.26
ATOM   1215  CA  PHE A1030      25.301  35.830 111.370  1.00186.38
ATOM   1216  C   PHE A1030      24.974  34.333 111.326  1.00186.73
ATOM   1217  O   PHE A1030      23.877  33.932 111.730  1.00184.91
ATOM   1218  CB  PHE A1030      24.922  36.496 110.046  1.00187.67
ATOM   1219  CG  PHE A1030      23.464  36.383 109.706  1.00190.42
ATOM   1220  CD1 PHE A1030      22.535  37.231 110.286  1.00193.90
ATOM   1221  CD2 PHE A1030      23.019  35.432 108.806  1.00193.75
ATOM   1222  CE1 PHE A1030      21.193  37.127 109.974  1.00196.24
ATOM   1223  CE2 PHE A1030      21.677  35.325 108.493  1.00198.04
ATOM   1224  CZ  PHE A1030      20.764  36.174 109.076  1.00196.51
ATOM   1225  N   LYS A1031      25.946  33.511 110.865  1.00182.44
ATOM   1226  CA  LYS A1031      25.813  32.060 110.777  1.00182.05
ATOM   1227  C   LYS A1031      25.593  31.438 112.155  1.00187.87
ATOM   1228  O   LYS A1031      25.080  30.316 112.241  1.00188.34
ATOM   1229  CB  LYS A1031      27.049  31.447 110.117  1.00183.16
ATOM   1230  CG  LYS A1031      27.216  31.813 108.651  0.00 99.99
ATOM   1231  CD  LYS A1031      28.461  31.172 108.059  0.00 99.99
ATOM   1232  CE  LYS A1031      28.627  31.539 106.593  0.00 99.99
ATOM   1233  NZ  LYS A1031      28.871  32.996 106.409  0.00 99.99
ATOM   1234  N   ASP A1032      25.966  32.164 113.229  1.00184.59
ATOM   1235  CA  ASP A1032      25.834  31.679 114.599  1.00185.12
ATOM   1236  C   ASP A1032      24.742  32.418 115.385  1.00191.56
ATOM   1237  O   ASP A1032      24.567  32.156 116.574  1.00192.22
ATOM   1238  CB  ASP A1032      27.165  31.804 115.342  1.00186.13
ATOM   1239  CG  ASP A1032      28.209  30.828 114.838  1.00189.87
ATOM   1240  OD1 ASP A1032      27.835  29.873 114.124  1.00188.77
ATOM   1241  OD2 ASP A1032      29.401  31.016 115.154  1.00195.20
ATOM   1242  N   ILE A1033      23.982  33.297 114.722  1.00189.10
ATOM   1243  CA  ILE A1033      22.839  33.965 115.345  1.00190.46
ATOM   1244  C   ILE A1033      21.668  33.000 115.233  1.00198.54
ATOM   1245  O   ILE A1033      21.497  32.393 114.169  1.00198.01
ATOM   1246  CB  ILE A1033      22.535  35.313 114.666  1.00192.97
ATOM   1247  CG1 ILE A1033      23.693  36.290 114.877  1.00192.59
ATOM   1248  CG2 ILE A1033      21.271  35.930 115.247  1.00194.35
ATOM   1249  CD1 ILE A1033      23.588  37.551 114.048  1.00196.03
ATOM   1250  N   PRO A1034      20.847  32.814 116.286  1.00198.76
ATOM   1251  CA  PRO A1034      19.733  31.853 116.163  1.00200.18
ATOM   1252  C   PRO A1034      18.697  32.300 115.132  1.00203.80
ATOM   1253  O   PRO A1034      18.585  33.502 114.853  1.00204.41
ATOM   1254  CB  PRO A1034      19.186  31.776 117.590  1.00203.95
ATOM   1255  CG  PRO A1034      20.381  32.091 118.462  1.00207.49
ATOM   1256  CD  PRO A1034      21.088  33.188 117.685  1.00201.66
ATOM   1257  N   ASP A1035      17.948  31.337 114.561  1.00198.06
ATOM   1258  CA  ASP A1035      16.895  31.630 113.589  1.00197.46
ATOM   1259  C   ASP A1035      15.776  32.482 114.228  1.00203.00
ATOM   1260  O   ASP A1035      15.122  33.249 113.520  1.00202.81
ATOM   1261  CB  ASP A1035      16.315  30.334 113.020  1.00199.14
ATOM   1262  CG  ASP A1035      15.664  29.471 114.083  0.00 99.99
ATOM   1263  OD1 ASP A1035      15.827  29.781 115.283  0.00 99.99
ATOM   1264  OD2 ASP A1035      14.990  28.485 113.719  0.00 99.99
ATOM   1265  N   ASP A1036      15.590  32.381 115.568  1.00200.37
ATOM   1266  CA  ASP A1036      14.598  33.151 116.331  1.00201.85
ATOM   1267  C   ASP A1036      15.123  34.568 116.564  1.00203.80
ATOM   1268  O   ASP A1036      15.286  35.002 117.711  1.00204.46
ATOM   1269  CB  ASP A1036      14.285  32.456 117.657  1.00204.93
ATOM   1270  CG  ASP A1036      13.211  33.173 118.452  0.00 99.99
ATOM   1271  OD1 ASP A1036      12.710  34.211 117.972  0.00 99.99
ATOM   1272  OD2 ASP A1036      12.870  32.696 119.554  0.00 99.99
ATOM   1273  N   TRP A1037      15.404  35.282 115.462  1.00197.88
ATOM   1274  CA  TRP A1037      15.949  36.625 115.510  1.00197.20
ATOM   1275  C   TRP A1037      15.325  37.505 114.443  1.00199.47
ATOM   1276  O   TRP A1037      15.002  37.039 113.347  1.00197.99
ATOM   1277  CB  TRP A1037      17.469  36.593 115.345  1.00193.92
ATOM   1278  CG  TRP A1037      18.113  37.941 115.455  1.00195.81
ATOM   1279  CD1 TRP A1037      18.580  38.536 116.591  1.00199.88
ATOM   1280  CD2 TRP A1037      18.362  38.861 114.385  1.00195.46
ATOM   1281  NE1 TRP A1037      19.105  39.771 116.299  1.00199.73
ATOM   1282  CE2 TRP A1037      18.983  39.993 114.948  1.00200.37
ATOM   1283  CE3 TRP A1037      18.121  38.836 113.009  1.00196.05
ATOM   1284  CZ2 TRP A1037      19.365  41.095 114.183  1.00199.81
ATOM   1285  CZ3 TRP A1037      18.500  39.927 112.251  1.00197.63
ATOM   1286  CH2 TRP A1037      19.117  41.045 112.837  1.00199.13
ATOM   1287  N   VAL A1038      15.145  38.787 114.788  1.00195.91
ATOM   1288  CA  VAL A1038      14.584  39.818 113.917  1.00195.69
ATOM   1289  C   VAL A1038      15.463  41.067 113.950  1.00195.69
ATOM   1290  O   VAL A1038      16.192  41.300 114.921  1.00195.01
ATOM   1291  CB  VAL A1038      13.146  40.183 114.329  1.00202.81
ATOM   1292  CG1 VAL A1038      12.629  41.342 113.489  1.00203.01
ATOM   1293  CG2 VAL A1038      12.217  38.995 114.133  1.00204.50
ATOM   1294  N   CYS A1039      15.387  41.868 112.880  1.00189.48
ATOM   1295  CA  CYS A1039      16.167  43.082 112.749  1.00188.16
ATOM   1296  C   CYS A1039      15.736  44.081 113.807  1.00194.26
ATOM   1297  O   CYS A1039      14.535  44.283 113.973  1.00197.42
ATOM   1298  CB  CYS A1039      16.012  43.670 111.345  1.00188.15
ATOM   1299  SG  CYS A1039      14.310  44.161 110.919  1.00192.90
ATOM   1300  N   PRO A1040      16.681  44.714 114.541  1.00188.56
ATOM   1301  CA  PRO A1040      16.278  45.643 115.604  1.00190.27
ATOM   1302  C   PRO A1040      15.651  46.947 115.096  1.00195.01
ATOM   1303  O   PRO A1040      14.972  47.620 115.880  1.00197.84
ATOM   1304  CB  PRO A1040      17.581  45.874 116.372  1.00191.03
ATOM   1305  CG  PRO A1040      18.369  44.601 116.154  1.00192.34
ATOM   1306  CD  PRO A1040      18.071  44.262 114.704  1.00187.16
ATOM   1307  N   LEU A1041      15.855  47.309 113.816  1.00188.90
ATOM   1308  CA  LEU A1041      15.322  48.569 113.306  1.00190.93
ATOM   1309  C   LEU A1041      13.914  48.429 112.743  1.00195.39
ATOM   1310  O   LEU A1041      13.016  49.167 113.171  1.00197.80
ATOM   1311  CB  LEU A1041      16.242  49.142 112.227  1.00189.66
ATOM   1312  CG  LEU A1041      17.641  49.564 112.681  1.00192.94
ATOM   1313  CD1 LEU A1041      18.492  49.974 111.490  1.00191.82
ATOM   1314  CD2 LEU A1041      17.562  50.743 113.637  1.00199.64
ATOM   1315  N   CYS A1042      13.724  47.509 111.770  1.00189.38
ATOM   1316  CA  CYS A1042      12.430  47.312 111.109  1.00189.80
ATOM   1317  C   CYS A1042      11.604  46.244 111.817  1.00196.46
ATOM   1318  O   CYS A1042      10.453  46.513 112.167  1.00199.03
ATOM   1319  CB  CYS A1042      12.630  46.933 109.641  1.00186.42
ATOM   1320  SG  CYS A1042      13.528  45.369 109.383  1.00184.82
ATOM   1321  N   GLY A1043      12.183  45.060 112.014  1.00192.11
ATOM   1322  CA  GLY A1043      11.515  43.961 112.697  1.00193.37
ATOM   1323  C   GLY A1043      11.279  42.736 111.852  1.00197.61
ATOM   1324  O   GLY A1043      10.597  41.808 112.292  1.00197.09
ATOM   1325  N   VAL A1044      11.844  42.718 110.641  1.00195.00
ATOM   1326  CA  VAL A1044      11.701  41.584 109.742  1.00194.36
ATOM   1327  C   VAL A1044      12.659  40.470 110.176  1.00198.40
ATOM   1328  O   VAL A1044      13.654  40.726 110.857  1.00196.69
ATOM   1329  CB  VAL A1044      11.980  41.983 108.281  1.00197.22
ATOM   1330  CG1 VAL A1044      11.945  40.760 107.378  1.00199.92
ATOM   1331  CG2 VAL A1044      10.933  42.973 107.791  1.00194.39
ATOM   1332  N   GLY A1045      12.341  39.247 109.773  1.00196.34
ATOM   1333  CA  GLY A1045      13.096  38.071 110.170  1.00194.64
ATOM   1334  C   GLY A1045      14.561  38.086 109.801  1.00195.74
ATOM   1335  O   GLY A1045      15.000  38.868 108.947  1.00194.20
ATOM   1336  N   LYS A1046      15.321  37.191 110.449  1.00190.79
ATOM   1337  CA  LYS A1046      16.735  37.000 110.164  1.00187.89
ATOM   1338  C   LYS A1046      16.927  36.388 108.753  1.00190.58
ATOM   1339  O   LYS A1046      17.997  36.573 108.169  1.00189.10
ATOM   1340  CB  LYS A1046      17.380  36.108 111.226  1.00188.95
ATOM   1341  CG  LYS A1046      18.877  35.913 111.048  0.00 99.99
ATOM   1342  CD  LYS A1046      19.451  35.019 112.135  0.00 99.99
ATOM   1343  CE  LYS A1046      20.948  34.824 111.955  0.00 99.99
ATOM   1344  NZ  LYS A1046      21.265  34.087 110.701  0.00 99.99
ATOM   1345  N   ASP A1047      15.889  35.700 108.195  1.00186.71
ATOM   1346  CA  ASP A1047      15.926  35.104 106.855  1.00184.58
ATOM   1347  C   ASP A1047      16.013  36.181 105.750  1.00188.50
ATOM   1348  O   ASP A1047      16.250  35.835 104.592  1.00186.21
ATOM   1349  CB  ASP A1047      14.695  34.225 106.625  1.00187.16
ATOM   1350  CG  ASP A1047      13.400  35.008 106.691  0.00 99.99
ATOM   1351  OD1 ASP A1047      13.207  35.758 107.672  0.00 99.99
ATOM   1352  OD2 ASP A1047      12.575  34.873 105.763  0.00 99.99
ATOM   1353  N   GLN A1048      15.835  37.479 106.111  1.00186.96
ATOM   1354  CA  GLN A1048      15.900  38.610 105.176  1.00186.40
ATOM   1355  C   GLN A1048      17.223  39.395 105.289  1.00189.28
ATOM   1356  O   GLN A1048      17.255  40.586 104.971  1.00188.92
ATOM   1357  CB  GLN A1048      14.724  39.562 105.403  1.00189.94
ATOM   1358  CG  GLN A1048      13.366  38.954 105.094  1.00197.37
ATOM   1359  CD  GLN A1048      12.797  38.174 106.264  1.00223.99
ATOM   1360  OE1 GLN A1048      13.419  38.081 107.322  1.00220.75
ATOM   1361  NE2 GLN A1048      11.608  37.613 106.076  1.00220.76
ATOM   1362  N   PHE A1049      18.317  38.729 105.706  1.00185.00
ATOM   1363  CA  PHE A1049      19.635  39.365 105.788  1.00184.04
ATOM   1364  C   PHE A1049      20.168  39.636 104.382  1.00187.18
ATOM   1365  O   PHE A1049      20.010  38.793 103.488  1.00185.12
ATOM   1366  CB  PHE A1049      20.606  38.486 106.578  1.00184.65
ATOM   1367  CG  PHE A1049      20.856  37.145 105.951  0.00 99.99
ATOM   1368  CD1 PHE A1049      21.887  36.969 105.043  0.00 99.99
ATOM   1369  CD2 PHE A1049      20.063  36.056 106.269  0.00 99.99
ATOM   1370  CE1 PHE A1049      22.117  35.735 104.467  0.00 99.99
ATOM   1371  CE2 PHE A1049      20.290  34.821 105.693  0.00 99.99
ATOM   1372  CZ  PHE A1049      21.319  34.660 104.792  0.00 99.99
ATOM   1373  N   GLU A1050      20.787  40.818 104.188  1.00184.95
ATOM   1374  CA  GLU A1050      21.278  41.284 102.880  1.00184.42
ATOM   1375  C   GLU A1050      22.652  40.796 102.462  1.00185.26
ATOM   1376  O   GLU A1050      23.304  41.444 101.623  1.00184.89
ATOM   1377  CB  GLU A1050      21.306  42.813 102.832  0.00 99.99
ATOM   1378  CG  GLU A1050      21.734  43.383 101.490  0.00 99.99
ATOM   1379  CD  GLU A1050      21.750  44.899 101.479  0.00 99.99
ATOM   1380  OE1 GLU A1050      22.498  45.492 102.286  0.00 99.99
ATOM   1381  OE2 GLU A1050      21.013  45.496 100.665  0.00 99.99
ATOM   1382  N   GLU A1051      23.084  39.641 103.023  1.00178.35
ATOM   1383  CA  GLU A1051      24.394  39.045 102.744  1.00175.51
ATOM   1384  C   GLU A1051      25.473  40.013 103.236  1.00173.46
ATOM   1385  O   GLU A1051      25.178  40.877 104.064  1.00174.14
ATOM   1386  CB  GLU A1051      24.540  38.746 101.251  1.00176.34
ATOM   1387  CG  GLU A1051      23.578  37.689 100.733  0.00 99.99
ATOM   1388  CD  GLU A1051      22.226  38.265 100.357  0.00 99.99
ATOM   1389  OE1 GLU A1051      22.043  39.492 100.502  0.00 99.99
ATOM   1390  OE2 GLU A1051      21.352  37.490  99.916  0.00 99.99
ATOM   1391  N   VAL A1052      26.705  39.886 102.731  1.00165.48
ATOM   1392  CA  VAL A1052      27.771  40.808 103.070  1.00164.88
ATOM   1393  C   VAL A1052      27.359  42.190 102.573  1.00171.17
ATOM   1394  O   VAL A1052      26.845  42.322 101.450  1.00170.39
ATOM   1395  CB  VAL A1052      29.111  40.373 102.449  1.00166.64
ATOM   1396  CG1 VAL A1052      30.185  41.417 102.715  1.00165.48
ATOM   1397  CG2 VAL A1052      29.570  39.050 103.045  1.00167.33
ATOM   1398  N   GLU A1053      27.557  43.215 103.419  1.00169.51
ATOM   1399  CA  GLU A1053      27.211  44.585 103.064  1.00170.56
ATOM   1400  C   GLU A1053      27.752  44.967 101.618  1.00175.62
ATOM   1401  O   GLU A1053      27.203  45.863 100.975  1.00178.05
ATOM   1402  CB  GLU A1053      27.762  45.563 104.103  1.00173.00
ATOM   1403  CG  GLU A1053      27.147  45.414 105.484  0.00 99.99
ATOM   1404  CD  GLU A1053      25.743  45.980 105.562  0.00 99.99
ATOM   1405  OE1 GLU A1053      25.250  46.490 104.532  0.00 99.99
ATOM   1406  OE2 GLU A1053      25.134  45.913 106.650  0.00 99.99
ATOM   1407  N   GLU A1054      28.764  44.237 101.099  1.00168.35
ATOM   1408  CA  GLU A1054      29.370  44.504  99.801  1.00166.73
ATOM   1409  C   GLU A1054      28.563  43.940  98.639  1.00169.51
ATOM   1410  O   GLU A1054      28.805  44.309  97.477  1.00169.40
ATOM   1411  CB  GLU A1054      30.790  43.938  99.746  1.00166.95
ATOM   1412  CG  GLU A1054      31.773  44.635 100.673  1.00174.50
ATOM   1413  CD  GLU A1054      33.167  44.046 100.592  1.00194.05
ATOM   1414  OE1 GLU A1054      33.328  42.980  99.960  1.00206.41
ATOM   1415  OE2 GLU A1054      34.102  44.651 101.159  1.00170.72
ATOM   1416  N   GLU A 262      27.596  43.067  98.938  1.00164.63
ATOM   1417  CA  GLU A 262      26.772  42.447  97.897  1.00162.71
ATOM   1418  C   GLU A 262      25.980  43.515  97.090  1.00165.26
ATOM   1419  O   GLU A 262      25.742  43.354  95.880  1.00164.20
ATOM   1420  CB  GLU A 262      25.806  41.432  98.511  1.00163.31
ATOM   1421  CG  GLU A 262      26.488  40.235  99.151  0.00 99.99
ATOM   1422  CD  GLU A 262      27.225  39.376  98.142  0.00 99.99
ATOM   1423  OE1 GLU A 262      26.691  39.175  97.031  0.00 99.99
ATOM   1424  OE2 GLU A 262      28.338  38.906  98.461  0.00 99.99
ATOM   1425  N   GLN A 263      25.605  44.610  97.766  1.00160.40
ATOM   1426  CA  GLN A 263      24.810  45.657  97.153  1.00160.24
ATOM   1427  C   GLN A 263      25.479  46.232  95.910  1.00157.98
ATOM   1428  O   GLN A 263      24.937  46.104  94.815  1.00157.00
ATOM   1429  CB  GLN A 263      24.538  46.780  98.156  1.00164.56
ATOM   1430  CG  GLN A 263      23.640  46.374  99.313  0.00 99.99
ATOM   1431  CD  GLN A 263      23.394  47.511 100.285  0.00 99.99
ATOM   1432  OE1 GLN A 263      22.858  48.554  99.912  0.00 99.99
ATOM   1433  NE2 GLN A 263      23.785  47.310 101.539  0.00 99.99
ATOM   1434  N   TRP A 264      26.656  46.838  96.082  1.00150.67
ATOM   1435  CA  TRP A 264      27.367  47.493  94.995  1.00148.82
ATOM   1436  C   TRP A 264      27.991  46.500  94.002  1.00148.95
ATOM   1437  O   TRP A 264      28.117  46.811  92.811  1.00147.29
ATOM   1438  CB  TRP A 264      28.463  48.407  95.545  1.00148.25
ATOM   1439  CG  TRP A 264      27.938  49.561  96.343  1.00147.65
ATOM   1440  CD1 TRP A 264      27.788  49.619  97.698  1.00150.24
ATOM   1441  CD2 TRP A 264      27.492  50.823  95.831  1.00146.65
ATOM   1442  NE1 TRP A 264      27.275  50.841  98.067  1.00148.81
ATOM   1443  CE2 TRP A 264      27.085  51.598  96.935  1.00149.95
ATOM   1444  CE3 TRP A 264      27.399  51.371  94.549  1.00147.51
ATOM   1445  CZ2 TRP A 264      26.592  52.895  96.798  1.00148.91
ATOM   1446  CZ3 TRP A 264      26.909  52.657  94.413  1.00148.48
ATOM   1447  CH2 TRP A 264      26.510  53.409  95.530  1.00149.03
ATOM   1448  N   ILE A 265      28.396  45.324  94.487  1.00144.91
ATOM   1449  CA  ILE A 265      29.013  44.341  93.620  1.00144.35
ATOM   1450  C   ILE A 265      28.005  43.803  92.571  1.00143.65
ATOM   1451  O   ILE A 265      28.410  43.244  91.541  1.00141.35
ATOM   1452  CB  ILE A 265      29.581  43.157  94.424  1.00148.52
ATOM   1453  CG1 ILE A 265      30.726  43.625  95.325  1.00150.19
ATOM   1454  CG2 ILE A 265      30.112  42.082  93.488  1.00149.59
ATOM   1455  CD1 ILE A 265      31.183  42.583  96.322  1.00167.49
ATOM   1456  N   PHE A 266      26.705  44.001  92.821  1.00138.17
ATOM   1457  CA  PHE A 266      25.690  43.583  91.874  1.00136.08
ATOM   1458  C   PHE A 266      25.774  44.428  90.600  1.00139.19
ATOM   1459  O   PHE A 266      25.585  43.897  89.502  1.00137.97
ATOM   1460  CB  PHE A 266      24.298  43.688  92.499  1.00138.53
ATOM   1461  CG  PHE A 266      23.193  43.205  91.604  1.00139.95
ATOM   1462  CD1 PHE A 266      22.927  41.852  91.476  1.00141.67
ATOM   1463  CD2 PHE A 266      22.419  44.100  90.890  1.00144.45
ATOM   1464  CE1 PHE A 266      21.911  41.407  90.652  1.00142.95
ATOM   1465  CE2 PHE A 266      21.403  43.659  90.064  1.00147.12
ATOM   1466  CZ  PHE A 266      21.148  42.311  89.947  1.00143.44
ATOM   1467  N   ARG A 267      26.081  45.739  90.741  1.00136.70
ATOM   1468  CA  ARG A 267      26.271  46.636  89.592  1.00137.01
ATOM   1469  C   ARG A 267      27.324  46.016  88.637  1.00139.84
ATOM   1470  O   ARG A 267      27.111  45.947  87.424  1.00135.67
ATOM   1471  CB  ARG A 267      26.699  48.027  90.063  1.00136.05
ATOM   1472  CG  ARG A 267      25.629  48.775  90.841  0.00 99.99
ATOM   1473  CD  ARG A 267      26.120  50.146  91.278  0.00 99.99
ATOM   1474  NE  ARG A 267      27.223  50.054  92.229  0.00 99.99
ATOM   1475  CZ  ARG A 267      28.494  50.299  91.926  0.00 99.99
ATOM   1476  NH1 ARG A 267      28.825  50.650  90.691  0.00 99.99
ATOM   1477  NH2 ARG A 267      29.430  50.190  92.858  0.00 99.99
ATOM   1478  N   LEU A 268      28.410  45.484  89.215  1.00139.26
ATOM   1479  CA  LEU A 268      29.439  44.780  88.461  1.00138.96
ATOM   1480  C   LEU A 268      28.865  43.520  87.850  1.00143.02
ATOM   1481  O   LEU A 268      29.163  43.208  86.698  1.00142.83
ATOM   1482  CB  LEU A 268      30.632  44.450  89.361  1.00139.17
ATOM   1483  CG  LEU A 268      31.417  45.643  89.910  1.00146.45
ATOM   1484  CD1 LEU A 268      32.476  45.180  90.899  1.00147.03
ATOM   1485  CD2 LEU A 268      32.114  46.391  88.784  1.00149.37
ATOM   1486  N   TYR A 269      28.052  42.780  88.619  1.00139.37
ATOM   1487  CA  TYR A 269      27.455  41.555  88.099  1.00138.43
ATOM   1488  C   TYR A 269      26.600  41.864  86.854  1.00144.86
ATOM   1489  O   TYR A 269      26.608  41.097  85.880  1.00144.08
ATOM   1490  CB  TYR A 269      26.611  40.871  89.176  1.00138.61
ATOM   1491  CG  TYR A 269      27.410  40.375  90.360  1.00139.06
ATOM   1492  CD1 TYR A 269      28.029  39.132  90.330  1.00140.31
ATOM   1493  CD2 TYR A 269      27.545  41.152  91.503  1.00139.91
ATOM   1494  CE1 TYR A 269      28.761  38.672  91.406  1.00140.65
ATOM   1495  CE2 TYR A 269      28.274  40.708  92.590  1.00140.67
ATOM   1496  CZ  TYR A 269      28.882  39.468  92.539  1.00149.05
ATOM   1497  OH  TYR A 269      29.610  39.016  93.614  1.00154.83
ATOM   1498  N   VAL A 270      25.905  43.012  86.869  1.00142.66
ATOM   1499  CA  VAL A 270      25.126  43.454  85.711  1.00141.81
ATOM   1500  C   VAL A 270      26.085  43.851  84.604  1.00142.25
ATOM   1501  O   VAL A 270      25.870  43.479  83.450  1.00138.23
ATOM   1502  CB  VAL A 270      24.200  44.631  86.070  1.00147.01
ATOM   1503  CG1 VAL A 270      23.494  45.152  84.827  1.00146.65
ATOM   1504  CG2 VAL A 270      23.145  44.191  87.074  1.00147.02
ATOM   1505  N   ALA A 271      27.168  44.556  84.978  1.00140.76
ATOM   1506  CA  ALA A 271      28.202  44.982  84.037  1.00141.80
ATOM   1507  C   ALA A 271      28.890  43.798  83.375  1.00148.80
ATOM   1508  O   ALA A 271      29.397  43.940  82.259  1.00151.19
ATOM   1509  CB  ALA A 271      29.247  45.859  84.743  1.00143.95
ATOM   1510  N   ILE A 272      28.918  42.636  84.046  1.00144.17
ATOM   1511  CA  ILE A 272      29.553  41.446  83.502  1.00142.21
ATOM   1512  C   ILE A 272      28.522  40.625  82.732  1.00144.21
ATOM   1513  O   ILE A 272      28.851  40.049  81.695  1.00144.13
ATOM   1514  CB  ILE A 272      30.188  40.588  84.612  1.00144.49
ATOM   1515  CG1 ILE A 272      31.336  41.346  85.281  0.00 99.99
ATOM   1516  CG2 ILE A 272      30.737  39.292  84.036  0.00 99.99
ATOM   1517  CD1 ILE A 272      31.860  40.680  86.534  0.00 99.99
ATOM   1518  N   GLY A 273      27.291  40.584  83.242  1.00138.48
ATOM   1519  CA  GLY A 273      26.209  39.792  82.669  1.00135.49
ATOM   1520  C   GLY A 273      25.657  40.327  81.362  1.00134.23
ATOM   1521  O   GLY A 273      25.300  39.560  80.472  1.00129.03
ATOM   1522  N   TRP A 274      25.545  41.651  81.251  1.00133.12
ATOM   1523  CA  TRP A 274      25.058  42.295  80.026  1.00133.16
ATOM   1524  C   TRP A 274      26.158  43.060  79.287  1.00138.22
ATOM   1525  O   TRP A 274      26.139  43.097  78.052  1.00136.38
ATOM   1526  CB  TRP A 274      23.904  43.247  80.344  1.00132.58
ATOM   1527  CG  TRP A 274      23.306  43.891  79.130  1.00132.91
ATOM   1528  CD1 TRP A 274      22.272  43.416  78.377  1.00136.45
ATOM   1529  CD2 TRP A 274      23.708  45.129  78.531  1.00131.80
ATOM   1530  NE1 TRP A 274      22.001  44.280  77.343  1.00135.65
ATOM   1531  CE2 TRP A 274      22.871  45.341  77.417  1.00136.40
ATOM   1532  CE3 TRP A 274      24.691  46.075  78.828  1.00131.77
ATOM   1533  CZ2 TRP A 274      22.989  46.463  76.597  1.00135.49
ATOM   1534  CZ3 TRP A 274      24.807  47.187  78.016  1.00132.63
ATOM   1535  CH2 TRP A 274      23.961  47.375  76.910  1.00133.95
ATOM   1536  N   GLY A 275      27.078  43.675  80.033  1.00137.83
ATOM   1537  CA  GLY A 275      28.145  44.485  79.450  1.00139.96
ATOM   1538  C   GLY A 275      29.084  43.712  78.538  1.00145.45
ATOM   1539  O   GLY A 275      29.301  44.075  77.367  1.00147.27
ATOM   1540  N   VAL A 276      29.642  42.631  79.066  1.00139.19
ATOM   1541  CA  VAL A 276      30.592  41.835  78.306  1.00137.66
ATOM   1542  C   VAL A 276      29.922  41.271  77.028  1.00137.46
ATOM   1543  O   VAL A 276      30.484  41.441  75.940  1.00136.95
ATOM   1544  CB  VAL A 276      31.156  40.675  79.147  1.00141.72
ATOM   1545  CG1 VAL A 276      32.051  39.786  78.297  1.00141.90
ATOM   1546  CG2 VAL A 276      31.977  41.211  80.310  1.00142.29
ATOM   1547  N   PRO A 277      28.720  40.646  77.109  1.00130.50
ATOM   1548  CA  PRO A 277      28.068  40.170  75.872  1.00128.24
ATOM   1549  C   PRO A 277      27.956  41.259  74.782  1.00128.52
ATOM   1550  O   PRO A 277      28.219  40.982  73.616  1.00125.00
ATOM   1551  CB  PRO A 277      26.708  39.674  76.369  1.00129.25
ATOM   1552  CG  PRO A 277      26.966  39.260  77.800  1.00133.62
ATOM   1553  CD  PRO A 277      27.918  40.333  78.298  1.00130.62
ATOM   1554  N   LEU A 278      27.637  42.497  75.158  1.00126.84
ATOM   1555  CA  LEU A 278      27.631  43.582  74.180  1.00128.11
ATOM   1556  C   LEU A 278      29.031  43.792  73.590  1.00132.09
ATOM   1557  O   LEU A 278      29.177  44.010  72.390  1.00129.32
ATOM   1558  CB  LEU A 278      27.124  44.876  74.819  1.00130.07
ATOM   1559  CG  LEU A 278      25.667  44.877  75.286  1.00136.09
ATOM   1560  CD1 LEU A 278      25.341  46.164  76.028  1.00138.64
ATOM   1561  CD2 LEU A 278      24.723  44.762  74.099  1.00139.59
ATOM   1562  N   LEU A 279      30.066  43.687  74.436  1.00131.46
ATOM   1563  CA  LEU A 279      31.458  43.886  74.028  1.00132.83
ATOM   1564  C   LEU A 279      31.936  42.919  72.936  1.00136.26
ATOM   1565  O   LEU A 279      33.025  43.106  72.400  1.00136.78
ATOM   1566  CB  LEU A 279      32.393  43.759  75.232  1.00133.52
ATOM   1567  CG  LEU A 279      32.240  44.819  76.325  1.00141.06
ATOM   1568  CD1 LEU A 279      33.121  44.491  77.520  1.00142.64
ATOM   1569  CD2 LEU A 279      32.641  46.190  75.802  1.00146.47
ATOM   1570  N   PHE A 280      31.169  41.883  72.621  1.00131.82
ATOM   1571  CA  PHE A 280      31.594  41.009  71.543  1.00131.86
ATOM   1572  C   PHE A 280      30.440  40.652  70.587  1.00137.02
ATOM   1573  O   PHE A 280      30.705  40.126  69.504  1.00137.93
ATOM   1574  CB  PHE A 280      32.207  39.724  72.104  1.00133.32
ATOM   1575  CG  PHE A 280      33.477  39.944  72.873  1.00133.38
ATOM   1576  CD1 PHE A 280      34.696  40.014  72.220  1.00133.17
ATOM   1577  CD2 PHE A 280      33.457  40.085  74.249  1.00135.47
ATOM   1578  CE1 PHE A 280      35.866  40.217  72.927  1.00132.70
ATOM   1579  CE2 PHE A 280      34.625  40.286  74.960  1.00136.26
ATOM   1580  CZ  PHE A 280      35.831  40.353  74.297  1.00132.78
ATOM   1581  N   VAL A 281      29.191  40.965  70.936  1.00133.35
ATOM   1582  CA  VAL A 281      28.089  40.672  70.023  1.00132.62
ATOM   1583  C   VAL A 281      27.943  41.806  68.985  1.00138.60
ATOM   1584  O   VAL A 281      27.672  41.542  67.817  1.00138.07
ATOM   1585  CB  VAL A 281      26.762  40.489  70.781  1.00136.01
ATOM   1586  CG1 VAL A 281      25.610  40.308  69.805  1.00135.97
ATOM   1587  CG2 VAL A 281      26.826  39.264  71.681  1.00134.52
ATOM   1588  N   VAL A 282      28.117  43.055  69.396  1.00138.35
ATOM   1589  CA  VAL A 282      27.992  44.167  68.450  1.00140.31
ATOM   1590  C   VAL A 282      29.232  44.199  67.568  1.00146.00
ATOM   1591  O   VAL A 282      29.032  44.347  66.367  1.00147.66
ATOM   1592  CB  VAL A 282      27.816  45.511  69.180  1.00145.76
ATOM   1593  CG1 VAL A 282      27.812  46.662  68.185  1.00145.04
ATOM   1594  CG2 VAL A 282      26.501  45.534  69.945  1.00146.99
ATOM   1595  N   PRO A 283      30.483  43.947  68.065  1.00140.96
ATOM   1596  CA  PRO A 283      31.619  43.879  67.144  1.00141.27
ATOM   1597  C   PRO A 283      31.364  42.859  66.044  1.00144.00
ATOM   1598  O   PRO A 283      31.644  43.139  64.869  1.00142.91
ATOM   1599  CB  PRO A 283      32.789  43.529  68.066  1.00142.85
ATOM   1600  CG  PRO A 283      32.390  44.107  69.405  1.00147.45
ATOM   1601  CD  PRO A 283      30.901  43.815  69.471  1.00141.98
ATOM   1602  N   TRP A 284      30.788  41.697  66.425  1.00139.83
ATOM   1603  CA  TRP A 284      30.491  40.650  65.457  1.00138.75
ATOM   1604  C   TRP A 284      29.396  41.116  64.481  1.00137.36
ATOM   1605  O   TRP A 284      29.562  41.010  63.262  1.00136.20
ATOM   1606  CB  TRP A 284      30.063  39.366  66.170  1.00137.26
ATOM   1607  CG  TRP A 284      29.808  38.220  65.240  1.00137.95
ATOM   1608  CD1 TRP A 284      30.715  37.291  64.817  1.00140.79
ATOM   1609  CD2 TRP A 284      28.562  37.881  64.620  1.00137.05
ATOM   1610  NE1 TRP A 284      30.113  36.393  63.970  1.00138.76
ATOM   1611  CE2 TRP A 284      28.789  36.735  63.833  1.00139.79
ATOM   1612  CE3 TRP A 284      27.280  38.436  64.653  1.00138.38
ATOM   1613  CZ2 TRP A 284      27.780  36.131  63.083  1.00138.55
ATOM   1614  CZ3 TRP A 284      26.281  37.837  63.910  1.00139.32
ATOM   1615  CH2 TRP A 284      26.533  36.693  63.133  1.00139.33
ATOM   1616  N   GLY A 285      28.306  41.641  65.018  1.00131.44
ATOM   1617  CA  GLY A 285      27.229  42.118  64.166  1.00131.16
ATOM   1618  C   GLY A 285      27.675  43.215  63.212  1.00135.50
ATOM   1619  O   GLY A 285      27.219  43.286  62.064  1.00134.03
ATOM   1620  N   ILE A 286      28.589  44.075  63.684  1.00131.67
ATOM   1621  CA  ILE A 286      29.106  45.187  62.897  1.00130.74
ATOM   1622  C   ILE A 286      29.847  44.645  61.673  1.00136.09
ATOM   1623  O   ILE A 286      29.554  45.068  60.558  1.00135.98
ATOM   1624  CB  ILE A 286      30.045  46.079  63.730  1.00132.42
ATOM   1625  CG1 ILE A 286      29.271  46.757  64.863  1.00131.08
ATOM   1626  CG2 ILE A 286      30.668  47.159  62.858  1.00132.80
ATOM   1627  CD1 ILE A 286      30.153  47.460  65.870  1.00134.18
ATOM   1628  N   VAL A 287      30.780  43.712  61.879  1.00133.96
ATOM   1629  CA  VAL A 287      31.579  43.178  60.779  1.00135.40
ATOM   1630  C   VAL A 287      30.740  42.236  59.924  1.00138.74
ATOM   1631  O   VAL A 287      31.004  42.089  58.728  1.00137.09
ATOM   1632  CB  VAL A 287      32.824  42.435  61.296  1.00140.85
ATOM   1633  CG1 VAL A 287      33.573  41.783  60.143  1.00142.57
ATOM   1634  CG2 VAL A 287      33.768  43.400  61.997  1.00139.59
ATOM   1635  N   LYS A 288      29.696  41.637  60.526  1.00136.46
ATOM   1636  CA  LYS A 288      28.772  40.767  59.798  1.00136.16
ATOM   1637  C   LYS A 288      27.746  41.629  59.023  1.00142.88
ATOM   1638  O   LYS A 288      26.715  41.131  58.577  1.00142.03
ATOM   1639  CB  LYS A 288      28.066  39.810  60.760  1.00136.98
ATOM   1640  CG  LYS A 288      27.138  38.818  60.080  0.00 99.99
ATOM   1641  CD  LYS A 288      26.471  37.901  61.093  0.00 99.99
ATOM   1642  CE  LYS A 288      25.492  38.666  61.968  0.00 99.99
ATOM   1643  NZ  LYS A 288      24.831  37.780  62.967  0.00 99.99
ATOM   1644  N   TYR A 289      28.045  42.916  58.863  1.00142.52
ATOM   1645  CA  TYR A 289      27.216  43.881  58.146  1.00144.05
ATOM   1646  C   TYR A 289      28.089  44.723  57.217  1.00150.65
ATOM   1647  O   TYR A 289      27.625  45.164  56.170  1.00151.56
ATOM   1648  CB  TYR A 289      26.454  44.769  59.131  1.00146.05
ATOM   1649  CG  TYR A 289      25.514  45.752  58.469  1.00148.38
ATOM   1650  CD1 TYR A 289      24.263  45.349  58.020  1.00149.58
ATOM   1651  CD2 TYR A 289      25.880  47.081  58.297  1.00150.52
ATOM   1652  CE1 TYR A 289      23.400  46.239  57.414  1.00151.50
ATOM   1653  CE2 TYR A 289      25.029  47.986  57.694  1.00152.33
ATOM   1654  CZ  TYR A 289      23.788  47.564  57.253  1.00156.74
ATOM   1655  OH  TYR A 289      22.933  48.457  56.651  1.00153.45
ATOM   1656  N   LEU A 290      29.334  44.964  57.622  1.00148.06
ATOM   1657  CA  LEU A 290      30.315  45.699  56.844  1.00149.56
ATOM   1658  C   LEU A 290      31.066  44.779  55.915  1.00154.05
ATOM   1659  O   LEU A 290      31.789  45.260  55.054  1.00154.26
ATOM   1660  CB  LEU A 290      31.291  46.431  57.766  1.00150.82
ATOM   1661  CG  LEU A 290      30.698  47.541  58.638  1.00156.04
ATOM   1662  CD1 LEU A 290      31.741  48.080  59.604  1.00157.96
ATOM   1663  CD2 LEU A 290      30.207  48.694  57.777  1.00159.37
ATOM   1664  N   TYR A 291      30.949  43.468  56.105  1.00152.04
ATOM   1665  CA  TYR A 291      31.749  42.542  55.312  1.00154.03
ATOM   1666  C   TYR A 291      30.955  41.386  54.701  1.00158.84
ATOM   1667  O   TYR A 291      31.243  41.011  53.566  1.00159.12
ATOM   1668  CB  TYR A 291      32.883  41.956  56.155  1.00156.24
ATOM   1669  CG  TYR A 291      33.904  42.977  56.605  1.00159.85
ATOM   1670  CD1 TYR A 291      34.963  43.335  55.780  1.00163.86
ATOM   1671  CD2 TYR A 291      33.805  43.579  57.852  1.00160.60
ATOM   1672  CE1 TYR A 291      35.899  44.266  56.183  1.00167.37
ATOM   1673  CE2 TYR A 291      34.733  44.514  58.272  1.00163.79
ATOM   1674  CZ  TYR A 291      35.778  44.856  57.436  1.00174.14
ATOM   1675  OH  TYR A 291      36.707  45.785  57.843  1.00178.04
ATOM   1676  N   GLU A 292      29.999  40.804  55.433  1.00155.26
ATOM   1677  CA  GLU A 292      29.222  39.689  54.914  1.00154.40
ATOM   1678  C   GLU A 292      27.852  39.666  55.565  1.00161.52
ATOM   1679  O   GLU A 292      27.662  38.985  56.572  1.00160.59
ATOM   1680  CB  GLU A 292      29.957  38.368  55.149  1.00155.04
ATOM   1681  CG  GLU A 292      29.249  37.153  54.573  0.00 99.99
ATOM   1682  CD  GLU A 292      28.120  36.663  55.458  0.00 99.99
ATOM   1683  OE1 GLU A 292      28.168  36.921  56.679  0.00 99.99
ATOM   1684  OE2 GLU A 292      27.186  36.022  54.931  0.00 99.99
ATOM   1685  N   ASP A 293      26.894  40.404  54.993  1.00161.83
ATOM   1686  CA  ASP A 293      25.513  40.454  55.509  1.00162.98
ATOM   1687  C   ASP A 293      24.509  39.760  54.576  1.00168.99
ATOM   1688  O   ASP A 293      23.292  39.985  54.667  1.00167.32
ATOM   1689  CB  ASP A 293      25.077  41.903  55.735  1.00166.38
ATOM   1690  CG  ASP A 293      25.067  42.714  54.455  1.00173.24
ATOM   1691  OD1 ASP A 293      25.576  42.214  53.429  1.00173.82
ATOM   1692  OD2 ASP A 293      24.550  43.851  54.475  1.00173.62
ATOM   1693  N   GLU A 294      25.027  38.895  53.704  1.00168.82
ATOM   1694  CA  GLU A 294      24.226  38.108  52.779  1.00169.36
ATOM   1695  C   GLU A 294      23.729  36.845  53.467  1.00175.84
ATOM   1696  O   GLU A 294      24.498  36.175  54.172  1.00174.74
ATOM   1697  CB  GLU A 294      25.037  37.762  51.529  1.00170.91
ATOM   1698  CG  GLU A 294      25.384  38.962  50.663  0.00 99.99
ATOM   1699  CD  GLU A 294      26.188  38.580  49.435  0.00 99.99
ATOM   1700  OE1 GLU A 294      26.636  37.417  49.354  0.00 99.99
ATOM   1701  OE2 GLU A 294      26.370  39.445  48.551  0.00 99.99
ATOM   1702  N   GLY A 295      22.445  36.554  53.262  1.00175.78
ATOM   1703  CA  GLY A 295      21.771  35.374  53.798  1.00176.72
ATOM   1704  C   GLY A 295      21.649  35.332  55.307  1.00183.64
ATOM   1705  O   GLY A 295      21.983  34.315  55.934  1.00182.95
ATOM   1706  N   CYS A 296      21.155  36.447  55.892  1.00181.91
ATOM   1707  CA  CYS A 296      20.943  36.620  57.330  1.00181.94
ATOM   1708  C   CYS A 296      22.229  36.369  58.129  1.00185.52
ATOM   1709  O   CYS A 296      22.185  35.847  59.249  1.00183.84
ATOM   1710  CB  CYS A 296      19.835  35.688  57.824  1.00182.11
ATOM   1711  SG  CYS A 296      19.423  35.877  59.589  1.00186.51
ATOM   1712  N   TRP A 297      23.381  36.729  57.543  1.00183.67
ATOM   1713  CA  TRP A 297      24.689  36.607  58.176  1.00184.16
ATOM   1714  C   TRP A 297      24.936  35.171  58.654  1.00189.59
ATOM   1715  O   TRP A 297      25.796  34.964  59.505  1.00189.42
ATOM   1716  CB  TRP A 297      24.810  37.583  59.348  1.00183.51
ATOM   1717  CG  TRP A 297      24.772  39.022  58.937  1.00185.81
ATOM   1718  CD1 TRP A 297      24.720  39.509  57.662  1.00189.25
ATOM   1719  CD2 TRP A 297      24.782  40.163  59.804  1.00186.74
ATOM   1720  NE1 TRP A 297      24.698  40.882  57.680  1.00189.97
ATOM   1721  CE2 TRP A 297      24.736  41.307  58.985  1.00191.80
ATOM   1722  CE3 TRP A 297      24.826  40.323  61.191  1.00188.19
ATOM   1723  CZ2 TRP A 297      24.730  42.599  59.508  1.00192.41
ATOM   1724  CZ3 TRP A 297      24.822  41.605  61.709  1.00190.82
ATOM   1725  CH2 TRP A 297      24.774  42.732  60.871  1.00192.65
ATOM   1726  N   THR A 298      24.175  34.181  58.117  1.00187.34
ATOM   1727  CA  THR A 298      24.293  32.763  58.485  1.00186.87
ATOM   1728  C   THR A 298      25.462  32.108  57.762  1.00192.56
ATOM   1729  O   THR A 298      26.158  31.295  58.363  1.00191.56
ATOM   1730  CB  THR A 298      23.001  31.988  58.166  1.00190.16
ATOM   1731  OG1 THR A 298      22.751  32.030  56.755  0.00 99.99
ATOM   1732  CG2 THR A 298      21.817  32.604  58.895  0.00 99.99
ATOM   1733  N   ARG A 299      25.690  32.463  56.492  1.00192.36
ATOM   1734  CA  ARG A 299      26.802  31.912  55.717  1.00194.58
ATOM   1735  C   ARG A 299      28.150  32.456  56.237  1.00204.31
ATOM   1736  O   ARG A 299      28.453  33.632  56.044  1.00205.55
ATOM   1737  CB  ARG A 299      26.633  32.237  54.232  1.00194.03
ATOM   1738  CG  ARG A 299      25.451  31.544  53.575  0.00 99.99
ATOM   1739  CD  ARG A 299      25.342  31.910  52.104  0.00 99.99
ATOM   1740  NE  ARG A 299      25.047  33.327  51.914  0.00 99.99
ATOM   1741  CZ  ARG A 299      24.995  33.927  50.728  0.00 99.99
ATOM   1742  NH1 ARG A 299      25.221  33.231  49.623  0.00 99.99
ATOM   1743  NH2 ARG A 299      24.720  35.221  50.654  0.00 99.99
ATOM   1744  N   ASN A 300      28.946  31.605  56.907  1.00203.41
ATOM   1745  CA  ASN A 300      30.264  31.973  57.442  1.00205.20
ATOM   1746  C   ASN A 300      31.355  31.132  56.758  1.00213.19
ATOM   1747  O   ASN A 300      32.214  30.542  57.426  1.00213.80
ATOM   1748  CB  ASN A 300      30.299  31.782  58.959  1.00204.61
ATOM   1749  CG  ASN A 300      31.616  32.217  59.571  0.00 99.99
ATOM   1750  OD1 ASN A 300      32.288  33.107  59.053  0.00 99.99
ATOM   1751  ND2 ASN A 300      31.987  31.590  60.681  0.00 99.99
ATOM   1752  N   SER A 301      31.306  31.071  55.417  1.00211.40
ATOM   1753  CA  SER A 301      32.220  30.247  54.630  1.00212.79
ATOM   1754  C   SER A 301      33.511  30.961  54.261  1.00218.13
ATOM   1755  O   SER A 301      34.582  30.348  54.342  1.00219.60
ATOM   1756  CB  SER A 301      31.538  29.763  53.349  1.00216.32
ATOM   1757  OG  SER A 301      31.168  30.855  52.525  0.00 99.99
ATOM   1758  N   ASN A 302      33.421  32.233  53.829  1.00213.51
ATOM   1759  CA  ASN A 302      34.603  32.970  53.375  1.00214.03
ATOM   1760  C   ASN A 302      35.660  33.094  54.478  1.00215.17
ATOM   1761  O   ASN A 302      36.823  32.729  54.264  1.00216.93
ATOM   1762  CB  ASN A 302      34.209  34.363  52.880  1.00214.65
ATOM   1763  CG  ASN A 302      33.587  35.214  53.969  1.00238.03
ATOM   1764  OD1 ASN A 302      33.259  34.718  55.047  1.00233.77
ATOM   1765  ND2 ASN A 302      33.424  36.501  53.692  1.00229.76
ATOM   1766  N   MET A 303      35.254  33.575  55.654  1.00206.67
ATOM   1767  CA  MET A 303      36.183  33.733  56.748  1.00205.76
ATOM   1768  C   MET A 303      35.505  33.410  58.050  1.00205.28
ATOM   1769  O   MET A 303      34.285  33.557  58.175  1.00202.90
ATOM   1770  CB  MET A 303      36.749  35.154  56.770  1.00209.27
ATOM   1771  CG  MET A 303      37.600  35.502  55.560  1.00215.18
ATOM   1772  SD  MET A 303      39.107  34.519  55.462  1.00221.38
ATOM   1773  CE  MET A 303      40.036  35.187  56.840  1.00220.85
ATOM   1774  N   ASN A 304      36.305  32.945  59.019  1.00200.28
ATOM   1775  CA  ASN A 304      35.842  32.591  60.351  1.00197.16
ATOM   1776  C   ASN A 304      35.831  33.834  61.239  1.00195.81
ATOM   1777  O   ASN A 304      36.698  34.037  62.089  1.00195.97
ATOM   1778  CB  ASN A 304      36.726  31.497  60.953  1.00198.44
ATOM   1779  CG  ASN A 304      36.202  30.989  62.282  1.00219.56
ATOM   1780  OD1 ASN A 304      35.426  31.667  62.953  1.00213.30
ATOM   1781  ND2 ASN A 304      36.624  29.790  62.662  1.00212.01
ATOM   1782  N   TYR A 305      34.828  34.676  61.013  1.00187.85
ATOM   1783  CA  TYR A 305      34.580  35.877  61.807  1.00185.94
ATOM   1784  C   TYR A 305      33.676  35.539  63.009  1.00183.63
ATOM   1785  O   TYR A 305      33.476  36.394  63.876  1.00182.35
ATOM   1786  CB  TYR A 305      33.946  36.969  60.943  1.00186.92
ATOM   1787  CG  TYR A 305      32.599  36.592  60.370  1.00189.83
ATOM   1788  CD1 TYR A 305      31.428  36.865  61.064  1.00193.26
ATOM   1789  CD2 TYR A 305      32.502  35.963  59.135  1.00190.79
ATOM   1790  CE1 TYR A 305      30.194  36.525  60.549  1.00196.75
ATOM   1791  CE2 TYR A 305      31.276  35.614  58.603  1.00193.51
ATOM   1792  CZ  TYR A 305      30.122  35.896  59.311  1.00203.72
ATOM   1793  OH  TYR A 305      28.897  35.552  58.790  1.00208.40
ATOM   1794  N   TRP A 306      33.132  34.301  63.061  1.00176.23
ATOM   1795  CA  TRP A 306      32.248  33.875  64.144  1.00173.43
ATOM   1796  C   TRP A 306      33.022  33.637  65.455  1.00170.91
ATOM   1797  O   TRP A 306      32.403  33.430  66.502  1.00169.31
ATOM   1798  CB  TRP A 306      31.493  32.604  63.751  1.00171.83
ATOM   1799  CG  TRP A 306      30.512  32.145  64.786  1.00173.93
ATOM   1800  CD1 TRP A 306      30.655  31.090  65.640  1.00177.05
ATOM   1801  CD2 TRP A 306      29.235  32.731  65.075  1.00174.79
ATOM   1802  NE1 TRP A 306      29.548  30.979  66.445  1.00177.50
ATOM   1803  CE2 TRP A 306      28.661  31.976  66.116  1.00179.55
ATOM   1804  CE3 TRP A 306      28.526  33.816  64.554  1.00176.46
ATOM   1805  CZ2 TRP A 306      27.406  32.272  66.649  1.00180.00
ATOM   1806  CZ3 TRP A 306      27.284  34.108  65.082  1.00178.80
ATOM   1807  CH2 TRP A 306      26.732  33.342  66.122  1.00180.26
ATOM   1808  N   LEU A 307      34.360  33.680  65.403  1.00163.55
ATOM   1809  CA  LEU A 307      35.185  33.541  66.600  1.00161.52
ATOM   1810  C   LEU A 307      34.936  34.706  67.575  1.00159.91
ATOM   1811  O   LEU A 307      35.152  34.553  68.784  1.00158.55
ATOM   1812  CB  LEU A 307      36.666  33.470  66.225  1.00163.28
ATOM   1813  CG  LEU A 307      37.102  32.251  65.409  1.00167.92
ATOM   1814  CD1 LEU A 307      38.556  32.381  64.984  1.00170.46
ATOM   1815  CD2 LEU A 307      36.960  30.978  66.230  1.00168.14
ATOM   1816  N   ILE A 308      34.436  35.856  67.050  1.00152.58
ATOM   1817  CA  ILE A 308      34.074  37.038  67.842  1.00149.58
ATOM   1818  C   ILE A 308      32.954  36.675  68.846  1.00146.96
ATOM   1819  O   ILE A 308      32.765  37.386  69.818  1.00147.73
ATOM   1820  CB  ILE A 308      33.613  38.200  66.943  1.00152.20
ATOM   1821  CG1 ILE A 308      34.768  38.684  66.064  0.00 99.99
ATOM   1822  CG2 ILE A 308      33.127  39.368  67.788  0.00 99.99
ATOM   1823  CD1 ILE A 308      34.348  39.658  64.985  0.00 99.99
ATOM   1824  N   ILE A 309      32.250  35.571  68.642  1.00137.33
ATOM   1825  CA  ILE A 309      31.220  35.167  69.567  1.00134.16
ATOM   1826  C   ILE A 309      31.611  33.836  70.229  1.00138.02
ATOM   1827  O   ILE A 309      31.279  33.601  71.386  1.00137.54
ATOM   1828  CB  ILE A 309      29.857  35.023  68.866  1.00135.32
ATOM   1829  CG1 ILE A 309      29.377  36.382  68.349  0.00 99.99
ATOM   1830  CG2 ILE A 309      28.815  34.479  69.831  0.00 99.99
ATOM   1831  CD1 ILE A 309      28.169  36.299  67.443  0.00 99.99
ATOM   1832  N   ARG A 310      32.345  32.980  69.518  1.00136.42
ATOM   1833  CA  ARG A 310      32.706  31.648  70.042  1.00136.30
ATOM   1834  C   ARG A 310      33.776  31.736  71.130  1.00139.18
ATOM   1835  O   ARG A 310      33.588  31.158  72.201  1.00138.60
ATOM   1836  CB  ARG A 310      33.192  30.741  68.910  1.00135.23
ATOM   1837  CG  ARG A 310      32.149  30.472  67.839  0.00 99.99
ATOM   1838  CD  ARG A 310      31.010  29.623  68.379  0.00 99.99
ATOM   1839  NE  ARG A 310      31.454  28.285  68.756  0.00 99.99
ATOM   1840  CZ  ARG A 310      30.680  27.378  69.344  0.00 99.99
ATOM   1841  NH1 ARG A 310      29.417  27.666  69.622  0.00 99.99
ATOM   1842  NH2 ARG A 310      31.172  26.185  69.650  0.00 99.99
ATOM   1843  N   LEU A 311      34.870  32.473  70.872  1.00134.33
ATOM   1844  CA  LEU A 311      35.976  32.567  71.819  1.00134.07
ATOM   1845  C   LEU A 311      35.570  33.193  73.164  1.00136.96
ATOM   1846  O   LEU A 311      35.920  32.629  74.206  1.00136.39
ATOM   1847  CB  LEU A 311      37.127  33.376  71.220  1.00135.08
ATOM   1848  CG  LEU A 311      37.821  32.768  69.999  1.00140.09
ATOM   1849  CD1 LEU A 311      38.840  33.738  69.421  1.00141.61
ATOM   1850  CD2 LEU A 311      38.546  31.486  70.377  1.00143.40
ATOM   1851  N   PRO A 312      34.806  34.305  73.193  1.00132.74
ATOM   1852  CA  PRO A 312      34.389  34.857  74.489  1.00131.60
ATOM   1853  C   PRO A 312      33.445  33.904  75.238  1.00134.09
ATOM   1854  O   PRO A 312      33.548  33.782  76.474  1.00134.86
ATOM   1855  CB  PRO A 312      33.744  36.190  74.104  1.00132.90
ATOM   1856  CG  PRO A 312      34.447  36.585  72.825  1.00138.51
ATOM   1857  CD  PRO A 312      34.596  35.262  72.096  1.00134.51
ATOM   1858  N   ILE A 313      32.547  33.203  74.492  1.00126.51
ATOM   1859  CA  ILE A 313      31.641  32.227  75.096  1.00123.86
ATOM   1860  C   ILE A 313      32.452  31.022  75.577  1.00130.12
ATOM   1861  O   ILE A 313      32.134  30.419  76.608  1.00130.79
ATOM   1862  CB  ILE A 313      30.555  31.776  74.103  1.00124.11
ATOM   1863  CG1 ILE A 313      29.643  32.950  73.739  1.00123.28
ATOM   1864  CG2 ILE A 313      29.701  30.673  74.710  1.00121.76
ATOM   1865  CD1 ILE A 313      28.700  32.660  72.594  1.00117.10
ATOM   1866  N   LEU A 314      33.509  30.688  74.856  1.00128.01
ATOM   1867  CA  LEU A 314      34.378  29.606  75.272  1.00129.47
ATOM   1868  C   LEU A 314      35.136  30.033  76.534  1.00137.09
ATOM   1869  O   LEU A 314      35.250  29.220  77.468  1.00137.28
ATOM   1870  CB  LEU A 314      35.342  29.229  74.145  1.00130.39
ATOM   1871  CG  LEU A 314      34.711  28.645  72.879  1.00137.63
ATOM   1872  CD1 LEU A 314      35.759  28.455  71.795  1.00138.43
ATOM   1873  CD2 LEU A 314      34.077  27.294  73.170  1.00144.58
ATOM   1874  N   PHE A 315      35.618  31.302  76.571  1.00135.30
ATOM   1875  CA  PHE A 315      36.314  31.857  77.730  1.00136.94
ATOM   1876  C   PHE A 315      35.415  31.752  78.963  1.00142.38
ATOM   1877  O   PHE A 315      35.865  31.286  80.035  1.00143.27
ATOM   1878  CB  PHE A 315      36.719  33.309  77.468  1.00139.61
ATOM   1879  CG  PHE A 315      37.503  33.931  78.586  1.00142.39
ATOM   1880  CD1 PHE A 315      38.858  33.680  78.725  1.00147.96
ATOM   1881  CD2 PHE A 315      36.890  34.767  79.501  1.00143.25
ATOM   1882  CE1 PHE A 315      39.581  34.252  79.755  1.00149.41
ATOM   1883  CE2 PHE A 315      37.609  35.340  80.532  1.00146.47
ATOM   1884  CZ  PHE A 315      38.956  35.084  80.658  1.00146.21
ATOM   1885  N   ALA A 316      34.131  32.166  78.804  1.00137.20
ATOM   1886  CA  ALA A 316      33.160  32.068  79.890  1.00135.70
ATOM   1887  C   ALA A 316      33.034  30.617  80.379  1.00141.47
ATOM   1888  O   ALA A 316      33.021  30.361  81.576  1.00140.01
ATOM   1889  CB  ALA A 316      31.791  32.600  79.440  1.00134.96
ATOM   1890  N   CYS A 317      33.017  29.670  79.448  1.00142.17
ATOM   1891  CA  CYS A 317      32.864  28.258  79.754  1.00143.49
ATOM   1892  C   CYS A 317      34.055  27.694  80.538  1.00140.22
ATOM   1893  O   CYS A 317      33.855  26.938  81.495  1.00138.28
ATOM   1894  CB  CYS A 317      32.673  27.449  78.470  1.00146.58
ATOM   1895  SG  CYS A 317      31.136  27.824  77.566  1.00151.24
ATOM   1896  N   ILE A 318      35.270  28.071  80.153  1.00133.76
ATOM   1897  CA  ILE A 318      36.455  27.585  80.843  1.00133.45
ATOM   1898  C   ILE A 318      36.449  28.069  82.300  1.00137.16
ATOM   1899  O   ILE A 318      36.704  27.267  83.212  1.00138.05
ATOM   1900  CB  ILE A 318      37.745  28.052  80.145  1.00136.32
ATOM   1901  CG1 ILE A 318      37.851  27.432  78.749  1.00135.10
ATOM   1902  CG2 ILE A 318      38.968  27.637  80.950  1.00137.70
ATOM   1903  CD1 ILE A 318      38.959  28.018  77.903  1.00140.36
ATOM   1904  N   VAL A 319      36.125  29.344  82.527  1.00131.76
ATOM   1905  CA  VAL A 319      36.113  29.831  83.916  1.00132.37
ATOM   1906  C   VAL A 319      34.870  29.390  84.676  1.00134.69
ATOM   1907  O   VAL A 319      34.899  29.318  85.909  1.00132.98
ATOM   1908  CB  VAL A 319      36.200  31.367  83.976  1.00136.85
ATOM   1909  CG1 VAL A 319      36.062  31.854  85.411  1.00138.65
ATOM   1910  CG2 VAL A 319      37.538  31.846  83.433  1.00136.03
ATOM   1911  N   ASN A 320      33.791  29.082  83.955  1.00131.02
ATOM   1912  CA  ASN A 320      32.590  28.585  84.607  1.00129.87
ATOM   1913  C   ASN A 320      32.853  27.180  85.147  1.00131.65
ATOM   1914  O   ASN A 320      32.358  26.813  86.214  1.00130.35
ATOM   1915  CB  ASN A 320      31.410  28.590  83.633  1.00134.54
ATOM   1916  CG  ASN A 320      30.941  29.990  83.292  1.00170.83
ATOM   1917  OD1 ASN A 320      31.203  30.939  84.029  1.00172.06
ATOM   1918  ND2 ASN A 320      30.247  30.122  82.169  1.00164.35
ATOM   1919  N   PHE A 321      33.669  26.413  84.428  1.00127.87
ATOM   1920  CA  PHE A 321      34.056  25.084  84.867  1.00128.20
ATOM   1921  C   PHE A 321      35.143  25.172  85.931  1.00131.41
ATOM   1922  O   PHE A 321      35.216  24.309  86.802  1.00130.98
ATOM   1923  CB  PHE A 321      34.533  24.245  83.680  1.00131.15
ATOM   1924  CG  PHE A 321      34.886  22.831  84.040  1.00131.80
ATOM   1925  CD1 PHE A 321      33.898  21.873  84.195  1.00135.00
ATOM   1926  CD2 PHE A 321      36.204  22.455  84.224  1.00132.48
ATOM   1927  CE1 PHE A 321      34.221  20.571  84.526  1.00135.67
ATOM   1928  CE2 PHE A 321      36.531  21.155  84.557  1.00135.41
ATOM   1929  CZ  PHE A 321      35.539  20.212  84.707  1.00134.21
ATOM   1930  N   LEU A 322      35.987  26.214  85.868  1.00128.99
ATOM   1931  CA  LEU A 322      37.026  26.433  86.873  1.00130.38
ATOM   1932  C   LEU A 322      36.389  26.850  88.200  1.00135.31
ATOM   1933  O   LEU A 322      36.882  26.484  89.286  1.00135.35
ATOM   1934  CB  LEU A 322      38.022  27.490  86.393  1.00131.00
ATOM   1935  CG  LEU A 322      38.857  27.127  85.163  1.00137.54
ATOM   1936  CD1 LEU A 322      39.692  28.315  84.711  1.00137.67
ATOM   1937  CD2 LEU A 322      39.800  25.976  85.477  1.00141.95
ATOM   1938  N   ILE A 323      35.263  27.586  88.105  1.00131.20
ATOM   1939  CA  ILE A 323      34.477  27.961  89.277  1.00130.34
ATOM   1940  C   ILE A 323      33.845  26.712  89.825  1.00131.66
ATOM   1941  O   ILE A 323      33.950  26.441  91.013  1.00133.32
ATOM   1942  CB  ILE A 323      33.407  29.011  88.926  1.00132.72
ATOM   1943  CG1 ILE A 323      34.067  30.321  88.490  1.00133.94
ATOM   1944  CG2 ILE A 323      32.522  29.294  90.131  1.00132.54
ATOM   1945  CD1 ILE A 323      33.102  31.326  87.902  1.00147.82
ATOM   1946  N   PHE A 324      33.207  25.954  88.952  1.00125.11
ATOM   1947  CA  PHE A 324      32.579  24.683  89.273  1.00125.43
ATOM   1948  C   PHE A 324      33.536  23.804  90.075  1.00130.54
ATOM   1949  O   PHE A 324      33.150  23.269  91.113  1.00129.10
ATOM   1950  CB  PHE A 324      32.135  23.967  87.996  1.00127.11
ATOM   1951  CG  PHE A 324      31.412  22.675  88.246  1.00127.89
ATOM   1952  CD1 PHE A 324      30.073  22.671  88.598  1.00132.09
ATOM   1953  CD2 PHE A 324      32.067  21.463  88.129  1.00127.69
ATOM   1954  CE1 PHE A 324      29.406  21.483  88.828  1.00133.68
ATOM   1955  CE2 PHE A 324      31.405  20.273  88.360  1.00131.83
ATOM   1956  CZ  PHE A 324      30.073  20.282  88.708  1.00131.48
ATOM   1957  N   VAL A 325      34.786  23.673  89.595  1.00130.51
ATOM   1958  CA  VAL A 325      35.801  22.817  90.214  1.00132.93
ATOM   1959  C   VAL A 325      36.223  23.365  91.586  1.00140.37
ATOM   1960  O   VAL A 325      36.287  22.616  92.572  1.00137.48
ATOM   1961  CB  VAL A 325      37.046  22.681  89.319  1.00136.90
ATOM   1962  CG1 VAL A 325      38.133  21.892  90.033  1.00138.20
ATOM   1963  CG2 VAL A 325      36.697  21.957  88.027  1.00136.86
ATOM   1964  N   ARG A 326      36.497  24.677  91.641  1.00141.83
ATOM   1965  CA  ARG A 326      36.920  25.307  92.889  1.00143.37
ATOM   1966  C   ARG A 326      35.818  25.288  93.928  1.00146.06
ATOM   1967  O   ARG A 326      36.122  25.151  95.110  1.00147.45
ATOM   1968  CB  ARG A 326      37.371  26.747  92.637  1.00146.49
ATOM   1969  CG  ARG A 326      38.639  26.865  91.808  1.00168.37
ATOM   1970  CD  ARG A 326      39.028  28.319  91.596  1.00195.48
ATOM   1971  NE  ARG A 326      38.039  29.038  90.799  1.00210.09
ATOM   1972  CZ  ARG A 326      38.088  30.343  90.547  1.00216.78
ATOM   1973  NH1 ARG A 326      39.081  31.075  91.035  1.00188.94
ATOM   1974  NH2 ARG A 326      37.144  30.911  89.812  1.00204.83
ATOM   1975  N   VAL A 327      34.549  25.396  93.503  1.00139.58
ATOM   1976  CA  VAL A 327      33.411  25.376  94.417  1.00137.95
ATOM   1977  C   VAL A 327      33.352  24.029  95.155  1.00142.43
ATOM   1978  O   VAL A 327      33.237  23.990  96.389  1.00142.62
ATOM   1979  CB  VAL A 327      32.085  25.619  93.673  1.00140.17
ATOM   1980  CG1 VAL A 327      30.906  25.472  94.622  1.00139.90
ATOM   1981  CG2 VAL A 327      32.055  27.022  93.083  1.00139.32
ATOM   1982  N   ILE A 328      33.486  22.934  94.410  1.00138.58
ATOM   1983  CA  ILE A 328      33.480  21.618  95.032  1.00139.37
ATOM   1984  C   ILE A 328      34.654  21.507  96.020  1.00145.68
ATOM   1985  O   ILE A 328      34.473  21.017  97.128  1.00144.26
ATOM   1986  CB  ILE A 328      33.571  20.497  93.981  1.00142.33
ATOM   1987  CG1 ILE A 328      32.322  20.493  93.096  1.00140.87
ATOM   1988  CG2 ILE A 328      33.687  19.139  94.657  1.00144.30
ATOM   1989  CD1 ILE A 328      32.430  19.585  91.891  1.00144.64
ATOM   1990  N   CYS A 329      35.831  22.010  95.633  1.00145.82
ATOM   1991  CA  CYS A 329      37.015  21.980  96.487  1.00148.74
ATOM   1992  C   CYS A 329      36.713  22.609  97.821  1.00148.70
ATOM   1993  O   CYS A 329      37.136  22.084  98.846  1.00149.17
ATOM   1994  CB  CYS A 329      38.184  22.695  95.807  1.00152.08
ATOM   1995  SG  CYS A 329      38.777  21.889  94.285  1.00158.92
ATOM   1996  N   ILE A 330      36.009  23.756  97.817  1.00141.60
ATOM   1997  CA  ILE A 330      35.711  24.487  99.049  1.00139.21
ATOM   1998  C   ILE A 330      34.617  23.786  99.845  1.00139.58
ATOM   1999  O   ILE A 330      34.807  23.529 101.027  1.00140.29
ATOM   2000  CB  ILE A 330      35.277  25.935  98.755  1.00140.19
ATOM   2001  CG1 ILE A 330      36.432  26.721  98.129  0.00 99.99
ATOM   2002  CG2 ILE A 330      34.855  26.636 100.037  0.00 99.99
ATOM   2003  CD1 ILE A 330      36.028  28.075  97.591  0.00 99.99
ATOM   2004  N   VAL A 331      33.502  23.443  99.204  1.00132.21
ATOM   2005  CA  VAL A 331      32.373  22.849  99.907  1.00131.11
ATOM   2006  C   VAL A 331      32.784  21.608 100.683  1.00137.27
ATOM   2007  O   VAL A 331      32.419  21.465 101.847  1.00136.23
ATOM   2008  CB  VAL A 331      31.238  22.475  98.936  1.00133.91
ATOM   2009  CG1 VAL A 331      30.124  21.746  99.674  1.00133.65
ATOM   2010  CG2 VAL A 331      30.652  23.724  98.295  1.00132.43
ATOM   2011  N   VAL A 332      33.559  20.726 100.054  1.00137.30
ATOM   2012  CA  VAL A 332      33.977  19.484 100.703  1.00139.77
ATOM   2013  C   VAL A 332      34.851  19.797 101.915  1.00145.07
ATOM   2014  O   VAL A 332      34.692  19.181 102.963  1.00144.67
ATOM   2015  CB  VAL A 332      34.744  18.570  99.730  1.00145.60
ATOM   2016  CG1 VAL A 332      35.275  17.343 100.457  1.00145.01
ATOM   2017  CG2 VAL A 332      33.832  18.105  98.605  1.00145.92
ATOM   2018  N   SER A 333      35.734  20.778 101.788  1.00143.69
ATOM   2019  CA  SER A 333      36.593  21.147 102.897  1.00145.38
ATOM   2020  C   SER A 333      35.783  21.799 103.984  1.00148.07
ATOM   2021  O   SER A 333      35.955  21.430 105.142  1.00149.03
ATOM   2022  CB  SER A 333      37.710  22.078 102.423  1.00151.39
ATOM   2023  OG  SER A 333      37.181  23.286 101.904  1.00169.02
ATOM   2024  N   LYS A 334      34.867  22.717 103.620  1.00142.88
ATOM   2025  CA  LYS A 334      34.041  23.453 104.580  1.00141.93
ATOM   2026  C   LYS A 334      33.092  22.511 105.319  1.00145.72
ATOM   2027  O   LYS A 334      32.972  22.605 106.550  1.00145.91
ATOM   2028  CB  LYS A 334      33.249  24.554 103.872  1.00142.71
ATOM   2029  CG  LYS A 334      34.109  25.674 103.311  0.00 99.99
ATOM   2030  CD  LYS A 334      33.260  26.731 102.623  0.00 99.99
ATOM   2031  CE  LYS A 334      34.121  27.851 102.061  0.00 99.99
ATOM   2032  NZ  LYS A 334      34.811  28.614 103.138  0.00 99.99
ATOM   2033  N   LEU A 335      32.450  21.588 104.586  1.00141.10
ATOM   2034  CA  LEU A 335      31.548  20.632 105.213  1.00141.56
ATOM   2035  C   LEU A 335      32.305  19.742 106.215  1.00152.13
ATOM   2036  O   LEU A 335      31.897  19.641 107.383  1.00153.33
ATOM   2037  CB  LEU A 335      30.858  19.771 104.153  1.00140.47
ATOM   2038  CG  LEU A 335      29.914  20.501 103.196  1.00141.84
ATOM   2039  CD1 LEU A 335      29.415  19.559 102.111  1.00142.26
ATOM   2040  CD2 LEU A 335      28.707  21.044 103.944  1.00140.91
ATOM   2041  N   LYS A 336      33.422  19.122 105.768  1.00151.49
ATOM   2042  CA  LYS A 336      34.211  18.229 106.626  1.00153.84
ATOM   2043  C   LYS A 336      34.764  18.979 107.832  1.00160.26
ATOM   2044  O   LYS A 336      34.754  18.434 108.939  1.00162.18
ATOM   2045  CB  LYS A 336      35.352  17.592 105.831  1.00156.84
ATOM   2046  CG  LYS A 336      34.893  16.626 104.752  1.00164.02
ATOM   2047  CD  LYS A 336      36.074  16.030 104.002  1.00174.85
ATOM   2048  CE  LYS A 336      35.614  15.065 102.923  1.00192.37
ATOM   2049  NZ  LYS A 336      36.762  14.474 102.181  1.00201.71
ATOM   2050  N   ALA A 337      35.190  20.239 107.643  1.00155.37
ATOM   2051  CA  ALA A 337      35.702  21.033 108.742  1.00155.78
ATOM   2052  C   ALA A 337      34.593  21.516 109.679  1.00162.95
ATOM   2053  O   ALA A 337      34.895  22.268 110.617  1.00163.75
ATOM   2054  CB  ALA A 337      36.487  22.243 108.214  1.00155.56
ATOM   2055  N   ASN A 338      33.317  21.093 109.443  1.00160.68
ATOM   2056  CA  ASN A 338      32.125  21.455 110.242  1.00160.88
ATOM   2057  C   ASN A 338      31.794  22.951 110.146  1.00162.33
ATOM   2058  O   ASN A 338      30.874  23.416 110.829  1.00161.20
ATOM   2059  CB  ASN A 338      32.325  21.068 111.708  1.00166.34
ATOM   2060  CG  ASN A 338      32.437  19.569 111.906  1.00197.92
ATOM   2061  OD1 ASN A 338      31.438  18.852 111.859  1.00194.47
ATOM   2062  ND2 ASN A 338      33.654  19.091 112.127  1.00188.71
ATOM   2063  N   LEU A 339      32.527  23.696 109.293  1.00157.64
ATOM   2064  CA  LEU A 339      32.367  25.141 109.138  1.00155.93
ATOM   2065  C   LEU A 339      31.179  25.501 108.255  1.00159.76
ATOM   2066  O   LEU A 339      30.892  26.686 108.090  1.00157.45
ATOM   2067  CB  LEU A 339      33.640  25.762 108.559  1.00155.24
ATOM   2068  CG  LEU A 339      34.891  25.685 109.436  1.00160.56
ATOM   2069  CD1 LEU A 339      36.107  26.205 108.684  0.00 99.99
ATOM   2070  CD2 LEU A 339      34.718  26.522 110.693  0.00 99.99
ATOM   2071  N   MET A 340      30.466  24.499 107.728  1.00158.93
ATOM   2072  CA  MET A 340      29.332  24.710 106.834  1.00159.51
ATOM   2073  C   MET A 340      28.410  23.524 106.900  1.00168.82
ATOM   2074  O   MET A 340      28.871  22.398 107.105  1.00169.97
ATOM   2075  CB  MET A 340      29.815  24.949 105.402  1.00160.79
ATOM   2076  CG  MET A 340      30.577  23.778 104.801  1.00162.99
ATOM   2077  SD  MET A 340      31.130  24.098 103.116  1.00166.13
ATOM   2078  CE  MET A 340      29.589  23.931 102.217  1.00161.97
ATOM   2079  N   CYS A 341      27.111  23.765 106.709  1.00168.52
ATOM   2080  CA  CYS A 341      26.106  22.706 106.728  1.00171.26
ATOM   2081  C   CYS A 341      25.338  22.671 105.409  1.00170.58
ATOM   2082  O   CYS A 341      25.248  23.680 104.698  1.00167.61
ATOM   2083  CB  CYS A 341      25.144  22.901 107.901  1.00174.59
ATOM   2084  SG  CYS A 341      24.187  24.450 107.841  1.00180.57
ATOM   2085  N   LYS A 342      24.756  21.505 105.104  1.00166.30
ATOM   2086  CA  LYS A 342      23.948  21.318 103.900  1.00164.71
ATOM   2087  C   LYS A 342      22.671  22.154 103.965  1.00167.84
ATOM   2088  O   LYS A 342      22.136  22.529 102.930  1.00167.57
ATOM   2089  CB  LYS A 342      23.604  19.840 103.709  1.00167.51
ATOM   2090  CG  LYS A 342      24.802  18.959 103.394  1.00174.90
ATOM   2091  CD  LYS A 342      24.390  17.507 103.218  0.00 99.99
ATOM   2092  CE  LYS A 342      25.588  16.627 102.904  0.00 99.99
ATOM   2093  NZ  LYS A 342      25.198  15.200 102.728  0.00 99.99
ATOM   2094  N   THR A 343      22.197  22.458 105.172  1.00164.27
ATOM   2095  CA  THR A 343      20.977  23.221 105.384  1.00164.20
ATOM   2096  C   THR A 343      21.083  24.652 104.866  1.00165.51
ATOM   2097  O   THR A 343      20.050  25.263 104.644  1.00165.11
ATOM   2098  CB  THR A 343      20.596  23.273 106.875  1.00175.33
ATOM   2099  OG1 THR A 343      21.632  23.934 107.613  1.00178.06
ATOM   2100  CG2 THR A 343      20.418  21.868 107.429  1.00171.50
ATOM   2101  N   ASP A 344      22.297  25.176 104.670  1.00161.40
ATOM   2102  CA  ASP A 344      22.518  26.567 104.285  1.00161.18
ATOM   2103  C   ASP A 344      22.030  26.927 102.889  1.00164.08
ATOM   2104  O   ASP A 344      21.799  26.058 102.055  1.00163.92
ATOM   2105  CB  ASP A 344      24.004  26.919 104.376  1.00163.02
ATOM   2106  CG  ASP A 344      24.857  26.091 103.435  1.00184.07
ATOM   2107  OD1 ASP A 344      24.349  25.692 102.366  1.00186.65
ATOM   2108  OD2 ASP A 344      26.036  25.842 103.766  1.00193.01
ATOM   2109  N   ILE A 345      21.851  28.226 102.650  1.00160.56
ATOM   2110  CA  ILE A 345      21.462  28.750 101.335  1.00160.28
ATOM   2111  C   ILE A 345      22.608  28.597 100.358  1.00161.20
ATOM   2112  O   ILE A 345      22.369  28.372  99.175  1.00160.74
ATOM   2113  CB  ILE A 345      21.043  30.229 101.419  1.00164.07
ATOM   2114  CG1 ILE A 345      19.776  30.378 102.265  1.00164.90
ATOM   2115  CG2 ILE A 345      20.763  30.784 100.030  1.00166.22
ATOM   2116  CD1 ILE A 345      19.429  31.811 102.598  1.00168.48
ATOM   2117  N   ALA A 346      23.849  28.729 100.851  1.00155.10
ATOM   2118  CA  ALA A 346      25.035  28.645 100.024  1.00152.80
ATOM   2119  C   ALA A 346      25.213  27.211  99.461  1.00155.46
ATOM   2120  O   ALA A 346      25.667  27.051  98.316  1.00154.62
ATOM   2121  CB  ALA A 346      26.280  29.063 100.821  1.00153.16
ATOM   2122  N   PHE A 347      24.795  26.181 100.231  1.00150.06
ATOM   2123  CA  PHE A 347      24.873  24.805  99.757  1.00148.57
ATOM   2124  C   PHE A 347      23.678  24.487  98.879  1.00152.82
ATOM   2125  O   PHE A 347      23.845  23.869  97.825  1.00152.39
ATOM   2126  CB  PHE A 347      24.950  23.835 100.937  1.00150.48
ATOM   2127  CG  PHE A 347      25.104  22.398 100.532  1.00151.95
ATOM   2128  CD1 PHE A 347      26.341  21.895 100.164  1.00154.80
ATOM   2129  CD2 PHE A 347      24.015  21.546 100.517  1.00154.03
ATOM   2130  CE1 PHE A 347      26.484  20.573  99.790  1.00156.25
ATOM   2131  CE2 PHE A 347      24.153  20.223 100.143  1.00157.72
ATOM   2132  CZ  PHE A 347      25.389  19.736  99.781  1.00155.91
ATOM   2133  N   ARG A 348      22.473  24.887  99.313  1.00149.76
ATOM   2134  CA  ARG A 348      21.265  24.681  98.521  1.00149.91
ATOM   2135  C   ARG A 348      21.456  25.286  97.091  1.00151.88
ATOM   2136  O   ARG A 348      21.124  24.634  96.090  1.00150.04
ATOM   2137  CB  ARG A 348      20.054  25.305  99.218  1.00149.87
ATOM   2138  CG  ARG A 348      19.741  24.701 100.577  0.00 99.99
ATOM   2139  CD  ARG A 348      19.253  23.268 100.443  0.00 99.99
ATOM   2140  NE  ARG A 348      18.947  22.670 101.741  0.00 99.99
ATOM   2141  CZ  ARG A 348      18.502  21.429 101.906  0.00 99.99
ATOM   2142  NH1 ARG A 348      18.312  20.648 100.852  0.00 99.99
ATOM   2143  NH2 ARG A 348      18.251  20.973 103.124  0.00 99.99
ATOM   2144  N   LEU A 349      22.034  26.511  97.008  1.00147.16
ATOM   2145  CA  LEU A 349      22.302  27.151  95.718  1.00145.38
ATOM   2146  C   LEU A 349      23.423  26.425  94.992  1.00149.07
ATOM   2147  O   LEU A 349      23.342  26.257  93.773  1.00149.22
ATOM   2148  CB  LEU A 349      22.655  28.626  95.915  1.00144.23
ATOM   2149  CG  LEU A 349      21.547  29.520  96.475  1.00147.31
ATOM   2150  CD1 LEU A 349      22.075  30.919  96.757  1.00148.76
ATOM   2151  CD2 LEU A 349      20.399  29.637  95.485  1.00147.77
ATOM   2152  N   ALA A 350      24.464  25.973  95.735  1.00143.25
ATOM   2153  CA  ALA A 350      25.572  25.222  95.136  1.00140.62
ATOM   2154  C   ALA A 350      25.032  24.024  94.375  1.00139.80
ATOM   2155  O   ALA A 350      25.413  23.817  93.229  1.00138.43
ATOM   2156  CB  ALA A 350      26.569  24.777  96.216  1.00141.68
ATOM   2157  N   LYS A 351      24.084  23.287  94.983  1.00134.26
ATOM   2158  CA  LYS A 351      23.449  22.149  94.329  1.00133.24
ATOM   2159  C   LYS A 351      22.911  22.566  92.959  1.00133.89
ATOM   2160  O   LYS A 351      23.092  21.843  91.975  1.00132.37
ATOM   2161  CB  LYS A 351      22.327  21.586  95.203  1.00135.34
ATOM   2162  CG  LYS A 351      22.808  20.946  96.495  1.00129.18
ATOM   2163  CD  LYS A 351      21.645  20.409  97.313  1.00135.40
ATOM   2164  CE  LYS A 351      22.127  19.771  98.605  0.00 99.99
ATOM   2165  NZ  LYS A 351      20.997  19.239  99.417  0.00 99.99
ATOM   2166  N   SER A 352      22.281  23.745  92.897  1.00129.54
ATOM   2167  CA  SER A 352      21.685  24.222  91.664  1.00129.48
ATOM   2168  C   SER A 352      22.727  24.758  90.680  1.00132.85
ATOM   2169  O   SER A 352      22.722  24.363  89.511  1.00132.82
ATOM   2170  CB  SER A 352      20.652  25.312  91.955  1.00133.91
ATOM   2171  OG  SER A 352      19.556  24.794  92.689  1.00145.98
ATOM   2172  N   THR A 353      23.610  25.641  91.141  1.00128.74
ATOM   2173  CA  THR A 353      24.604  26.275  90.275  1.00128.23
ATOM   2174  C   THR A 353      25.590  25.242  89.708  1.00133.19
ATOM   2175  O   THR A 353      25.962  25.315  88.518  1.00132.51
ATOM   2176  CB  THR A 353      25.393  27.364  91.025  1.00132.08
ATOM   2177  OG1 THR A 353      26.111  26.772  92.115  1.00135.68
ATOM   2178  CG2 THR A 353      24.450  28.423  91.574  1.00125.71
ATOM   2179  N   LEU A 354      25.980  24.270  90.543  1.00129.76
ATOM   2180  CA  LEU A 354      26.877  23.220  90.110  1.00130.16
ATOM   2181  C   LEU A 354      26.184  22.276  89.148  1.00136.70
ATOM   2182  O   LEU A 354      26.837  21.381  88.645  1.00139.11
ATOM   2183  CB  LEU A 354      27.417  22.446  91.314  1.00131.02
ATOM   2184  CG  LEU A 354      28.307  23.229  92.281  1.00135.54
ATOM   2185  CD1 LEU A 354      28.650  22.386  93.499  1.00137.53
ATOM   2186  CD2 LEU A 354      29.606  23.636  91.604  1.00135.00
ATOM   2187  N   THR A 355      24.881  22.455  88.894  1.00132.26
ATOM   2188  CA  THR A 355      24.119  21.601  87.989  1.00132.44
ATOM   2189  C   THR A 355      23.945  22.259  86.619  1.00135.51
ATOM   2190  O   THR A 355      23.900  21.554  85.605  1.00134.69
ATOM   2191  CB  THR A 355      22.731  21.265  88.565  1.00141.85
ATOM   2192  OG1 THR A 355      22.882  20.478  89.754  1.00145.60
ATOM   2193  CG2 THR A 355      21.910  20.479  87.554  1.00140.92
ATOM   2194  N   LEU A 356      23.848  23.599  86.584  1.00131.36
ATOM   2195  CA  LEU A 356      23.686  24.339  85.342  1.00129.47
ATOM   2196  C   LEU A 356      25.006  24.489  84.661  1.00131.85
ATOM   2197  O   LEU A 356      25.096  24.227  83.465  1.00132.39
ATOM   2198  CB  LEU A 356      23.056  25.707  85.611  1.00129.19
ATOM   2199  CG  LEU A 356      22.760  26.570  84.384  1.00135.29
ATOM   2200  CD1 LEU A 356      21.700  25.916  83.511  1.00137.20
ATOM   2201  CD2 LEU A 356      22.254  27.943  84.800  1.00137.56
ATOM   2202  N   ILE A 357      26.046  24.876  85.414  1.00127.40
ATOM   2203  CA  ILE A 357      27.376  25.068  84.848  1.00127.45
ATOM   2204  C   ILE A 357      27.844  23.840  84.017  1.00136.29
ATOM   2205  O   ILE A 357      28.271  24.024  82.864  1.00136.77
ATOM   2206  CB  ILE A 357      28.421  25.344  85.944  1.00130.12
ATOM   2207  CG1 ILE A 357      28.122  26.672  86.644  0.00 99.99
ATOM   2208  CG2 ILE A 357      29.817  25.418  85.344  0.00 99.99
ATOM   2209  CD1 ILE A 357      28.952  26.908  87.886  0.00 99.99
ATOM   2210  N   PRO A 358      27.714  22.591  84.518  1.00136.18
ATOM   2211  CA  PRO A 358      28.215  21.451  83.737  1.00137.32
ATOM   2212  C   PRO A 358      27.465  21.205  82.449  1.00144.66
ATOM   2213  O   PRO A 358      28.106  20.980  81.422  1.00145.24
ATOM   2214  CB  PRO A 358      28.101  20.284  84.720  1.00140.01
ATOM   2215  CG  PRO A 358      28.235  20.931  86.080  1.00144.29
ATOM   2216  CD  PRO A 358      27.456  22.225  85.919  1.00138.66
ATOM   2217  N   LEU A 359      26.132  21.222  82.489  1.00143.72
ATOM   2218  CA  LEU A 359      25.384  20.861  81.296  1.00145.33
ATOM   2219  C   LEU A 359      25.363  21.973  80.242  1.00151.06
ATOM   2220  O   LEU A 359      25.418  21.672  79.031  1.00152.68
ATOM   2221  CB  LEU A 359      23.946  20.487  81.658  1.00145.84
ATOM   2222  CG  LEU A 359      23.766  19.236  82.522  1.00149.38
ATOM   2223  CD1 LEU A 359      22.310  19.066  82.926  1.00148.89
ATOM   2224  CD2 LEU A 359      24.196  17.993  81.760  1.00151.05
ATOM   2225  N   LEU A 360      25.305  23.231  80.684  1.00145.68
ATOM   2226  CA  LEU A 360      25.184  24.327  79.750  1.00145.29
ATOM   2227  C   LEU A 360      26.474  24.710  79.054  1.00148.70
ATOM   2228  O   LEU A 360      26.417  25.293  77.962  1.00146.95
ATOM   2229  CB  LEU A 360      24.632  25.570  80.451  1.00145.91
ATOM   2230  CG  LEU A 360      23.203  25.467  80.988  1.00152.66
ATOM   2231  CD1 LEU A 360      22.837  26.711  81.783  1.00153.26
ATOM   2232  CD2 LEU A 360      22.209  25.324  79.846  1.00155.60
ATOM   2233  N   CYS A 361      27.628  24.387  79.650  1.00147.09
ATOM   2234  CA  CYS A 361      28.909  24.710  79.027  1.00147.97
ATOM   2235  C   CYS A 361      29.678  23.472  78.545  1.00153.43
ATOM   2236  O   CYS A 361      30.721  23.639  77.908  1.00153.12
ATOM   2237  CB  CYS A 361      29.792  25.499  79.996  1.00148.57
ATOM   2238  SG  CYS A 361      31.388  26.033  79.296  1.00151.90
ATOM   2239  N   THR A 362      29.184  22.249  78.841  1.00151.17
ATOM   2240  CA  THR A 362      29.889  21.019  78.498  1.00152.59
ATOM   2241  C   THR A 362      30.223  20.974  77.012  1.00158.59
ATOM   2242  O   THR A 362      31.394  20.860  76.643  1.00157.76
ATOM   2243  CB  THR A 362      29.063  19.774  78.868  1.00158.36
ATOM   2244  OG1 THR A 362      29.837  18.592  78.623  0.00 99.99
ATOM   2245  CG2 THR A 362      27.792  19.710  78.035  0.00 99.99
ATOM   2246  N   HIS A 363      29.208  21.096  76.155  1.00157.72
ATOM   2247  CA  HIS A 363      29.405  21.037  74.693  1.00158.72
ATOM   2248  C   HIS A 363      30.315  22.144  74.197  1.00158.52
ATOM   2249  O   HIS A 363      31.133  21.920  73.314  1.00156.44
ATOM   2250  CB  HIS A 363      28.060  21.112  73.968  1.00160.13
ATOM   2251  CG  HIS A 363      27.314  22.387  74.209  1.00163.43
ATOM   2252  ND1 HIS A 363      27.631  23.568  73.575  1.00165.82
ATOM   2253  CD2 HIS A 363      26.263  22.666  75.017  1.00164.54
ATOM   2254  CE1 HIS A 363      26.808  24.517  73.984  1.00164.62
ATOM   2255  NE2 HIS A 363      25.969  23.997  74.857  1.00164.24
ATOM   2256  N   GLU A 364      30.191  23.325  74.800  1.00155.15
ATOM   2257  CA  GLU A 364      30.909  24.516  74.392  1.00155.43
ATOM   2258  C   GLU A 364      32.379  24.531  74.838  1.00163.31
ATOM   2259  O   GLU A 364      33.045  25.543  74.623  1.00163.60
ATOM   2260  CB  GLU A 364      30.218  25.770  74.931  1.00155.53
ATOM   2261  CG  GLU A 364      28.830  26.008  74.359  0.00 99.99
ATOM   2262  CD  GLU A 364      28.867  26.528  72.935  0.00 99.99
ATOM   2263  OE1 GLU A 364      29.981  26.703  72.396  0.00 99.99
ATOM   2264  OE2 GLU A 364      27.784  26.760  72.359  0.00 99.99
ATOM   2265  N   VAL A 365      32.895  23.434  75.420  1.00162.60
ATOM   2266  CA  VAL A 365      34.301  23.353  75.830  1.00164.36
ATOM   2267  C   VAL A 365      35.028  22.250  75.043  1.00171.04
ATOM   2268  O   VAL A 365      36.078  22.516  74.447  1.00172.13
ATOM   2269  CB  VAL A 365      34.434  23.080  77.339  1.00168.25
ATOM   2270  CG1 VAL A 365      35.893  22.877  77.719  1.00166.92
ATOM   2271  CG2 VAL A 365      33.886  24.250  78.143  1.00168.01
ATOM   2272  N   ILE A 366      34.472  21.033  75.027  1.00168.17
ATOM   2273  CA  ILE A 366      35.090  19.901  74.326  1.00170.38
ATOM   2274  C   ILE A 366      35.203  20.158  72.804  1.00176.47
ATOM   2275  O   ILE A 366      36.296  20.060  72.223  1.00178.33
ATOM   2276  CB  ILE A 366      34.299  18.599  74.550  1.00173.71
ATOM   2277  CG1 ILE A 366      34.349  18.192  76.024  1.00171.44
ATOM   2278  CG2 ILE A 366      34.885  17.469  73.718  1.00175.79
ATOM   2279  CD1 ILE A 366      33.407  17.063  76.379  1.00173.33
ATOM   2280  N   PHE A 367      34.090  20.527  72.176  1.00171.42
ATOM   2281  CA  PHE A 367      34.095  20.795  70.753  1.00170.39
ATOM   2282  C   PHE A 367      34.849  22.051  70.429  1.00176.03
ATOM   2283  O   PHE A 367      35.598  22.075  69.458  1.00176.26
ATOM   2284  CB  PHE A 367      32.664  20.896  70.222  1.00170.01
ATOM   2285  CG  PHE A 367      31.891  19.613  70.314  1.00171.55
ATOM   2286  CD1 PHE A 367      31.989  18.654  69.320  1.00175.53
ATOM   2287  CD2 PHE A 367      31.066  19.359  71.396  1.00172.93
ATOM   2288  CE1 PHE A 367      31.279  17.472  69.405  1.00176.99
ATOM   2289  CE2 PHE A 367      30.353  18.179  71.484  1.00176.58
ATOM   2290  CZ  PHE A 367      30.460  17.234  70.487  1.00175.87
ATOM   2291  N   ALA A 368      34.647  23.102  71.237  1.00174.78
ATOM   2292  CA  ALA A 368      35.124  24.459  70.984  1.00176.04
ATOM   2293  C   ALA A 368      36.472  24.516  70.280  1.00184.34
ATOM   2294  O   ALA A 368      36.575  25.102  69.188  1.00184.55
ATOM   2295  CB  ALA A 368      35.222  25.250  72.297  1.00176.26
ATOM   2296  N   PHE A 369      37.482  23.878  70.870  1.00182.89
ATOM   2297  CA  PHE A 369      38.800  23.976  70.291  1.00185.16
ATOM   2298  C   PHE A 369      39.198  22.753  69.515  1.00192.47
ATOM   2299  O   PHE A 369      39.834  22.897  68.463  1.00191.72
ATOM   2300  CB  PHE A 369      39.844  24.239  71.377  1.00188.21
ATOM   2301  CG  PHE A 369      41.237  24.424  70.847  1.00190.62
ATOM   2302  CD1 PHE A 369      41.633  25.637  70.310  1.00195.72
ATOM   2303  CD2 PHE A 369      42.153  23.389  70.885  1.00191.80
ATOM   2304  CE1 PHE A 369      42.914  25.809  69.821  1.00197.99
ATOM   2305  CE2 PHE A 369      43.434  23.556  70.397  1.00196.30
ATOM   2306  CZ  PHE A 369      43.816  24.768  69.866  1.00196.52
ATOM   2307  N   VAL A 370      38.857  21.550  70.043  1.00192.31
ATOM   2308  CA  VAL A 370      39.208  20.271  69.417  1.00194.81
ATOM   2309  C   VAL A 370      38.678  20.230  67.960  1.00200.26
ATOM   2310  O   VAL A 370      39.466  19.999  67.032  1.00201.28
ATOM   2311  CB  VAL A 370      38.640  19.080  70.211  1.00198.38
ATOM   2312  CG1 VAL A 370      38.910  17.774  69.479  0.00 99.99
ATOM   2313  CG2 VAL A 370      39.284  19.002  71.587  0.00 99.99
ATOM   2314  N   MET A 371      37.363  20.518  67.764  1.00195.20
ATOM   2315  CA  MET A 371      36.722  20.494  66.436  1.00193.68
ATOM   2316  C   MET A 371      37.186  21.639  65.570  1.00196.24
ATOM   2317  O   MET A 371      37.244  21.492  64.338  1.00196.01
ATOM   2318  CB  MET A 371      35.199  20.534  66.575  1.00193.66
ATOM   2319  CG  MET A 371      34.606  19.309  67.251  0.00 99.99
ATOM   2320  SD  MET A 371      34.838  17.802  66.291  0.00 99.99
ATOM   2321  CE  MET A 371      36.183  17.031  67.189  0.00 99.99
ATOM   2322  N   ASP A 372      37.523  22.775  66.198  1.00191.48
ATOM   2323  CA  ASP A 372      37.958  23.943  65.449  1.00190.98
ATOM   2324  C   ASP A 372      39.195  23.649  64.572  1.00194.48
ATOM   2325  O   ASP A 372      39.348  24.255  63.507  1.00194.08
ATOM   2326  CB  ASP A 372      38.268  25.103  66.397  1.00192.50
ATOM   2327  CG  ASP A 372      38.657  26.370  65.661  0.00 99.99
ATOM   2328  OD1 ASP A 372      37.835  26.872  64.866  0.00 99.99
ATOM   2329  OD2 ASP A 372      39.785  26.861  65.879  0.00 99.99
ATOM   2330  N   GLU A 373      40.039  22.697  65.003  1.00190.56
ATOM   2331  CA  GLU A 373      41.288  22.361  64.340  1.00192.06
ATOM   2332  C   GLU A 373      41.133  22.104  62.856  1.00194.27
ATOM   2333  O   GLU A 373      41.971  22.576  62.093  1.00195.18
ATOM   2334  CB  GLU A 373      41.927  21.133  64.991  1.00195.69
ATOM   2335  CG  GLU A 373      43.276  20.751  64.405  0.00 99.99
ATOM   2336  CD  GLU A 373      43.151  19.978  63.107  0.00 99.99
ATOM   2337  OE1 GLU A 373      42.100  19.336  62.898  0.00 99.99
ATOM   2338  OE2 GLU A 373      44.102  20.015  62.298  0.00 99.99
ATOM   2339  N   HIS A 374      40.074  21.381  62.439  1.00188.46
ATOM   2340  CA  HIS A 374      39.889  21.035  61.031  1.00188.12
ATOM   2341  C   HIS A 374      38.464  21.316  60.545  1.00188.17
ATOM   2342  O   HIS A 374      37.631  21.820  61.308  1.00185.50
ATOM   2343  CB  HIS A 374      40.229  19.563  60.792  1.00191.04
ATOM   2344  CG  HIS A 374      40.132  19.145  59.357  0.00 99.99
ATOM   2345  ND1 HIS A 374      38.936  18.827  58.753  0.00 99.99
ATOM   2346  CD2 HIS A 374      41.085  18.995  58.407  0.00 99.99
ATOM   2347  CE1 HIS A 374      39.158  18.498  57.492  0.00 99.99
ATOM   2348  NE2 HIS A 374      40.452  18.591  57.257  0.00 99.99
ATOM   2349  N   ALA A 375      38.190  20.996  59.259  1.00184.18
ATOM   2350  CA  ALA A 375      36.891  21.201  58.618  1.00181.22
ATOM   2351  C   ALA A 375      35.903  20.123  59.010  1.00181.60
ATOM   2352  O   ALA A 375      35.095  19.696  58.175  1.00178.83
ATOM   2353  CB  ALA A 375      37.043  21.241  57.090  1.00182.88
ATOM   2354  N   ARG A 376      35.974  19.648  60.274  1.00177.83
ATOM   2355  CA  ARG A 376      34.946  18.708  60.649  1.00176.00
ATOM   2356  C   ARG A 376      34.069  19.292  61.738  1.00171.50
ATOM   2357  O   ARG A 376      32.988  18.757  61.941  1.00169.99
ATOM   2358  CB  ARG A 376      35.568  17.389  61.110  1.00181.94
ATOM   2359  CG  ARG A 376      36.380  16.678  60.040  1.00200.25
ATOM   2360  CD  ARG A 376      35.487  16.166  58.921  1.00208.97
ATOM   2361  NE  ARG A 376      36.251  15.479  57.882  1.00197.55
ATOM   2362  CZ  ARG A 376      36.848  16.092  56.867  1.00183.93
ATOM   2363  NH1 ARG A 376      36.771  17.410  56.749  1.00162.97
ATOM   2364  NH2 ARG A 376      37.520  15.384  55.969  1.00142.45
ATOM   2365  N   GLY A 377      34.372  20.508  62.193  1.00163.22
ATOM   2366  CA  GLY A 377      33.436  21.303  62.976  1.00159.27
ATOM   2367  C   GLY A 377      32.326  21.791  62.052  1.00156.47
ATOM   2368  O   GLY A 377      31.348  22.403  62.491  1.00151.64
ATOM   2369  N   THR A 378      32.480  21.505  60.747  1.00153.87
ATOM   2370  CA  THR A 378      31.476  21.772  59.723  1.00152.87
ATOM   2371  C   THR A 378      30.289  20.833  59.985  1.00152.00
ATOM   2372  O   THR A 378      29.178  21.298  60.256  1.00147.99
ATOM   2373  CB  THR A 378      32.045  21.565  58.308  1.00173.09
ATOM   2374  OG1 THR A 378      32.448  20.199  58.146  1.00174.53
ATOM   2375  CG2 THR A 378      33.251  22.463  58.081  1.00174.34
ATOM   2376  N   LEU A 379      30.548  19.499  59.946  1.00148.57
ATOM   2377  CA  LEU A 379      29.511  18.497  60.160  1.00147.21
ATOM   2378  C   LEU A 379      29.074  18.457  61.633  1.00147.34
ATOM   2379  O   LEU A 379      28.023  17.887  61.928  1.00147.26
ATOM   2380  CB  LEU A 379      30.000  17.117  59.718  1.00148.93
ATOM   2381  CG  LEU A 379      28.988  15.974  59.819  0.00 99.99
ATOM   2382  CD1 LEU A 379      27.825  16.202  58.865  0.00 99.99
ATOM   2383  CD2 LEU A 379      29.638  14.646  59.467  0.00 99.99
ATOM   2384  N   ARG A 380      29.848  19.078  62.544  1.00140.15
ATOM   2385  CA  ARG A 380      29.477  19.133  63.957  1.00138.55
ATOM   2386  C   ARG A 380      28.440  20.231  64.162  1.00141.70
ATOM   2387  O   ARG A 380      27.628  20.124  65.083  1.00141.05
ATOM   2388  CB  ARG A 380      30.713  19.371  64.827  1.00135.76
ATOM   2389  CG  ARG A 380      31.756  18.270  64.737  0.00 99.99
ATOM   2390  CD  ARG A 380      31.249  16.979  65.357  0.00 99.99
ATOM   2391  NE  ARG A 380      32.240  15.908  65.279  0.00 99.99
ATOM   2392  CZ  ARG A 380      32.050  14.679  65.746  0.00 99.99
ATOM   2393  NH1 ARG A 380      30.902  14.361  66.326  0.00 99.99
ATOM   2394  NH2 ARG A 380      33.009  13.771  65.631  0.00 99.99
ATOM   2395  N   PHE A 381      28.462  21.287  63.310  1.00137.19
ATOM   2396  CA  PHE A 381      27.505  22.398  63.376  1.00134.69
ATOM   2397  C   PHE A 381      26.130  21.963  62.875  1.00135.83
ATOM   2398  O   PHE A 381      25.114  22.564  63.253  1.00132.30
ATOM   2399  CB  PHE A 381      28.012  23.591  62.564  1.00136.21
ATOM   2400  CG  PHE A 381      27.121  24.797  62.638  0.00 99.99
ATOM   2401  CD1 PHE A 381      27.169  25.646  63.731  0.00 99.99
ATOM   2402  CD2 PHE A 381      26.235  25.087  61.616  0.00 99.99
ATOM   2403  CE1 PHE A 381      26.349  26.756  63.801  0.00 99.99
ATOM   2404  CE2 PHE A 381      25.413  26.195  61.683  0.00 99.99
ATOM   2405  CZ  PHE A 381      25.471  27.031  62.775  0.00 99.99
ATOM   2406  N   ILE A 382      26.095  20.908  62.029  1.00133.98
ATOM   2407  CA  ILE A 382      24.820  20.331  61.601  1.00133.40
ATOM   2408  C   ILE A 382      24.214  19.591  62.811  1.00142.71
ATOM   2409  O   ILE A 382      23.009  19.685  63.065  1.00142.78
ATOM   2410  CB  ILE A 382      25.005  19.378  60.406  1.00134.89
ATOM   2411  CG1 ILE A 382      25.491  20.151  59.178  1.00131.60
ATOM   2412  CG2 ILE A 382      23.690  18.697  60.058  1.00135.61
ATOM   2413  CD1 ILE A 382      25.926  19.266  58.031  1.00106.36
ATOM   2414  N   LYS A 383      25.071  18.908  63.586  1.00142.21
ATOM   2415  CA  LYS A 383      24.645  18.249  64.812  1.00143.58
ATOM   2416  C   LYS A 383      24.232  19.316  65.849  1.00150.46
ATOM   2417  O   LYS A 383      23.276  19.123  66.589  1.00151.72
ATOM   2418  CB  LYS A 383      25.761  17.355  65.356  1.00146.72
ATOM   2419  CG  LYS A 383      26.080  16.157  64.478  0.00 99.99
ATOM   2420  CD  LYS A 383      27.195  15.313  65.076  0.00 99.99
ATOM   2421  CE  LYS A 383      27.514  14.115  64.197  0.00 99.99
ATOM   2422  NZ  LYS A 383      28.605  13.280  64.772  0.00 99.99
ATOM   2423  N   LEU A 384      24.918  20.452  65.888  1.00148.04
ATOM   2424  CA  LEU A 384      24.525  21.474  66.836  1.00148.85
ATOM   2425  C   LEU A 384      23.142  22.010  66.501  1.00152.50
ATOM   2426  O   LEU A 384      22.377  22.302  67.412  1.00152.88
ATOM   2427  CB  LEU A 384      25.549  22.611  66.854  1.00149.34
ATOM   2428  CG  LEU A 384      26.951  22.253  67.353  1.00155.45
ATOM   2429  CD1 LEU A 384      27.899  23.430  67.180  1.00155.96
ATOM   2430  CD2 LEU A 384      26.917  21.883  68.827  1.00159.40
ATOM   2431  N   PHE A 385      22.795  22.082  65.210  1.00148.59
ATOM   2432  CA  PHE A 385      21.459  22.509  64.788  1.00148.09
ATOM   2433  C   PHE A 385      20.408  21.571  65.395  1.00154.73
ATOM   2434  O   PHE A 385      19.398  22.032  65.931  1.00154.52
ATOM   2435  CB  PHE A 385      21.360  22.531  63.262  1.00149.00
ATOM   2436  CG  PHE A 385      20.041  23.027  62.746  0.00 99.99
ATOM   2437  CD1 PHE A 385      19.770  24.383  62.686  0.00 99.99
ATOM   2438  CD2 PHE A 385      19.068  22.140  62.321  0.00 99.99
ATOM   2439  CE1 PHE A 385      18.555  24.841  62.212  0.00 99.99
ATOM   2440  CE2 PHE A 385      17.852  22.594  61.848  0.00 99.99
ATOM   2441  CZ  PHE A 385      17.595  23.945  61.792  0.00 99.99
ATOM   2442  N   THR A 386      20.677  20.268  65.365  1.00153.52
ATOM   2443  CA  THR A 386      19.776  19.281  65.955  1.00155.79
ATOM   2444  C   THR A 386      19.767  19.424  67.488  1.00159.63
ATOM   2445  O   THR A 386      18.705  19.303  68.115  1.00159.42
ATOM   2446  CB  THR A 386      20.181  17.846  65.569  1.00176.66
ATOM   2447  OG1 THR A 386      20.026  17.667  64.155  1.00182.48
ATOM   2448  CG2 THR A 386      19.306  16.833  66.292  1.00177.33
ATOM   2449  N   ASP A 387      20.939  19.707  68.088  1.00155.60
ATOM   2450  CA  ASP A 387      21.027  19.941  69.522  1.00155.06
ATOM   2451  C   ASP A 387      20.114  21.058  69.924  1.00160.44
ATOM   2452  O   ASP A 387      19.341  20.892  70.857  1.00159.91
ATOM   2453  CB  ASP A 387      22.469  20.253  69.927  1.00155.97
ATOM   2454  CG  ASP A 387      22.628  20.434  71.423  1.00169.78
ATOM   2455  OD1 ASP A 387      22.329  19.481  72.173  1.00172.69
ATOM   2456  OD2 ASP A 387      23.054  21.530  71.848  1.00177.54
ATOM   2457  N   LEU A 388      20.199  22.201  69.209  1.00158.43
ATOM   2458  CA  LEU A 388      19.405  23.387  69.488  1.00158.49
ATOM   2459  C   LEU A 388      17.910  23.063  69.521  1.00165.20
ATOM   2460  O   LEU A 388      17.162  23.760  70.206  1.00167.32
ATOM   2461  CB  LEU A 388      19.682  24.474  68.448  1.00157.59
ATOM   2462  CG  LEU A 388      21.099  25.052  68.431  1.00161.21
ATOM   2463  CD1 LEU A 388      21.275  26.009  67.262  1.00161.06
ATOM   2464  CD2 LEU A 388      21.383  25.814  69.716  1.00163.25
ATOM   2465  N   SER A 389      17.480  22.013  68.810  1.00161.20
ATOM   2466  CA  SER A 389      16.086  21.601  68.807  1.00162.61
ATOM   2467  C   SER A 389      15.760  20.696  70.002  1.00168.95
ATOM   2468  O   SER A 389      14.618  20.286  70.145  1.00169.17
ATOM   2469  CB  SER A 389      15.743  20.881  67.502  1.00168.74
ATOM   2470  OG  SER A 389      16.512  19.701  67.353  1.00180.12
ATOM   2471  N   PHE A 390      16.744  20.405  70.858  1.00167.27
ATOM   2472  CA  PHE A 390      16.607  19.668  72.125  1.00168.46
ATOM   2473  C   PHE A 390      16.985  20.624  73.318  1.00168.81
ATOM   2474  O   PHE A 390      16.539  20.420  74.450  1.00167.10
ATOM   2475  CB  PHE A 390      17.488  18.417  72.115  1.00171.78
ATOM   2476  CG  PHE A 390      17.080  17.396  71.093  1.00174.51
ATOM   2477  CD1 PHE A 390      16.093  16.467  71.375  1.00176.89
ATOM   2478  CD2 PHE A 390      17.679  17.365  69.846  1.00178.05
ATOM   2479  CE1 PHE A 390      15.717  15.528  70.434  1.00177.74
ATOM   2480  CE2 PHE A 390      17.306  16.426  68.903  1.00180.72
ATOM   2481  CZ  PHE A 390      16.323  15.507  69.198  1.00177.52
ATOM   2482  N   THR A 391      17.796  21.666  73.039  1.00163.98
ATOM   2483  CA  THR A 391      18.247  22.677  74.010  1.00162.35
ATOM   2484  C   THR A 391      17.155  23.764  74.207  1.00162.46
ATOM   2485  O   THR A 391      17.399  24.798  74.820  1.00161.25
ATOM   2486  CB  THR A 391      19.561  23.343  73.562  1.00173.79
ATOM   2487  OG1 THR A 391      20.613  22.369  73.549  1.00176.35
ATOM   2488  CG2 THR A 391      19.942  24.466  74.514  1.00170.83
ATOM   2489  N   SER A 392      15.944  23.504  73.724  1.00157.46
ATOM   2490  CA  SER A 392      14.809  24.392  73.944  1.00156.59
ATOM   2491  C   SER A 392      14.376  24.353  75.423  1.00160.34
ATOM   2492  O   SER A 392      13.889  25.357  75.965  1.00159.47
ATOM   2493  CB  SER A 392      13.642  24.007  73.032  1.00159.98
ATOM   2494  OG  SER A 392      13.188  22.695  73.314  1.00165.30
ATOM   2495  N   PHE A 393      14.561  23.186  76.070  1.00157.00
ATOM   2496  CA  PHE A 393      14.185  22.979  77.460  1.00157.05
ATOM   2497  C   PHE A 393      15.129  23.632  78.439  1.00158.98
ATOM   2498  O   PHE A 393      14.741  23.900  79.580  1.00159.33
ATOM   2499  CB  PHE A 393      14.099  21.485  77.775  1.00160.20
ATOM   2500  CG  PHE A 393      13.012  20.769  77.028  1.00164.36
ATOM   2501  CD1 PHE A 393      11.714  20.751  77.512  1.00170.48
ATOM   2502  CD2 PHE A 393      13.282  20.115  75.839  1.00167.89
ATOM   2503  CE1 PHE A 393      10.713  20.093  76.824  1.00173.85
ATOM   2504  CE2 PHE A 393      12.283  19.454  75.149  1.00173.20
ATOM   2505  CZ  PHE A 393      10.997  19.444  75.642  1.00173.22
ATOM   2506  N   GLN A 394      16.362  23.890  78.015  1.00153.62
ATOM   2507  CA  GLN A 394      17.402  24.402  78.894  1.00152.01
ATOM   2508  C   GLN A 394      17.014  25.771  79.555  1.00154.96
ATOM   2509  O   GLN A 394      17.698  26.214  80.486  1.00153.38
ATOM   2510  CB  GLN A 394      18.718  24.563  78.130  1.00151.82
ATOM   2511  CG  GLN A 394      19.314  23.255  77.639  1.00154.76
ATOM   2512  CD  GLN A 394      19.735  22.343  78.774  1.00170.85
ATOM   2513  OE1 GLN A 394      19.020  21.407  79.128  1.00169.07
ATOM   2514  NE2 GLN A 394      20.901  22.615  79.349  1.00158.46
ATOM   2515  N   GLY A 395      15.884  26.349  79.151  1.00152.19
ATOM   2516  CA  GLY A 395      15.346  27.539  79.805  1.00152.10
ATOM   2517  C   GLY A 395      14.566  27.153  81.057  1.00155.12
ATOM   2518  O   GLY A 395      14.693  27.790  82.117  1.00153.61
ATOM   2519  N   LEU A 396      13.750  26.079  80.940  1.00150.84
ATOM   2520  CA  LEU A 396      12.963  25.552  82.055  1.00150.29
ATOM   2521  C   LEU A 396      13.891  25.031  83.133  1.00149.39
ATOM   2522  O   LEU A 396      13.631  25.237  84.316  1.00147.92
ATOM   2523  CB  LEU A 396      12.016  24.452  81.570  1.00151.54
ATOM   2524  CG  LEU A 396      11.077  23.856  82.620  1.00157.57
ATOM   2525  CD1 LEU A 396      10.093  24.904  83.117  1.00159.05
ATOM   2526  CD2 LEU A 396      10.284  22.697  82.036  1.00160.93
ATOM   2527  N   MET A 397      14.986  24.378  82.724  1.00144.12
ATOM   2528  CA  MET A 397      15.960  23.842  83.658  1.00143.75
ATOM   2529  C   MET A 397      16.464  24.946  84.615  1.00148.13
ATOM   2530  O   MET A 397      16.598  24.716  85.820  1.00146.19
ATOM   2531  CB  MET A 397      17.134  23.212  82.906  1.00144.81
ATOM   2532  CG  MET A 397      16.769  21.963  82.119  0.00 99.99
ATOM   2533  SD  MET A 397      18.178  21.253  81.248  0.00 99.99
ATOM   2534  CE  MET A 397      19.065  20.491  82.606  0.00 99.99
ATOM   2535  N   VAL A 398      16.698  26.150  84.077  1.00147.02
ATOM   2536  CA  VAL A 398      17.132  27.297  84.880  1.00147.90
ATOM   2537  C   VAL A 398      15.980  27.728  85.790  1.00157.07
ATOM   2538  O   VAL A 398      16.199  28.096  86.951  1.00157.45
ATOM   2539  CB  VAL A 398      17.580  28.471  83.990  1.00150.87
ATOM   2540  CG1 VAL A 398      17.908  29.689  84.840  1.00150.46
ATOM   2541  CG2 VAL A 398      18.820  28.093  83.194  1.00149.84
ATOM   2542  N   ALA A 399      14.752  27.682  85.263  1.00156.45
ATOM   2543  CA  ALA A 399      13.590  28.114  86.031  1.00158.10
ATOM   2544  C   ALA A 399      13.345  27.200  87.246  1.00160.68
ATOM   2545  O   ALA A 399      13.180  27.678  88.376  1.00160.49
ATOM   2546  CB  ALA A 399      12.338  28.150  85.142  1.00160.29
ATOM   2547  N   ILE A 400      13.357  25.893  87.019  1.00155.66
ATOM   2548  CA  ILE A 400      13.111  24.962  88.100  1.00155.60
ATOM   2549  C   ILE A 400      14.187  25.078  89.159  1.00156.48
ATOM   2550  O   ILE A 400      13.911  25.493  90.284  1.00155.63
ATOM   2551  CB  ILE A 400      13.048  23.510  87.591  1.00158.92
ATOM   2552  CG1 ILE A 400      11.848  23.322  86.661  1.00159.47
ATOM   2553  CG2 ILE A 400      12.913  22.542  88.756  1.00160.67
ATOM   2554  CD1 ILE A 400      11.843  21.999  85.929  1.00166.10
ATOM   2555  N   LEU A 401      15.412  24.739  88.779  1.00152.00
ATOM   2556  CA  LEU A 401      16.530  24.638  89.693  1.00151.45
ATOM   2557  C   LEU A 401      16.769  25.899  90.509  1.00152.84
ATOM   2558  O   LEU A 401      17.253  25.776  91.635  1.00151.79
ATOM   2559  CB  LEU A 401      17.813  24.293  88.935  1.00150.57
ATOM   2560  CG  LEU A 401      17.851  22.924  88.252  0.00 99.99
ATOM   2561  CD1 LEU A 401      19.114  22.773  87.419  0.00 99.99
ATOM   2562  CD2 LEU A 401      17.828  21.809  89.286  0.00 99.99
ATOM   2563  N   TYR A 402      16.420  27.089  89.968  1.00148.58
ATOM   2564  CA  TYR A 402      16.670  28.364  90.664  1.00148.19
ATOM   2565  C   TYR A 402      15.450  28.966  91.344  1.00156.95
ATOM   2566  O   TYR A 402      15.598  29.910  92.124  1.00155.65
ATOM   2567  CB  TYR A 402      17.237  29.402  89.694  1.00146.07
ATOM   2568  CG  TYR A 402      18.602  29.049  89.146  1.00143.87
ATOM   2569  CD1 TYR A 402      19.755  29.364  89.853  1.00145.22
ATOM   2570  CD2 TYR A 402      18.732  28.401  87.925  1.00143.03
ATOM   2571  CE1 TYR A 402      21.005  29.044  89.360  1.00143.89
ATOM   2572  CE2 TYR A 402      19.974  28.073  87.416  1.00142.42
ATOM   2573  CZ  TYR A 402      21.109  28.395  88.135  1.00145.24
ATOM   2574  OH  TYR A 402      22.351  28.074  87.639  1.00141.06
ATOM   2575  N   CYS A 403      14.257  28.449  91.054  1.00158.19
ATOM   2576  CA  CYS A 403      13.058  28.990  91.672  1.00160.96
ATOM   2577  C   CYS A 403      12.247  27.871  92.259  1.00168.48
ATOM   2578  O   CYS A 403      12.158  27.767  93.476  1.00168.46
ATOM   2579  CB  CYS A 403      12.240  29.783  90.651  1.00162.03
ATOM   2580  SG  CYS A 403      10.752  30.583  91.335  1.00168.72
ATOM   2581  N   PHE A 404      11.671  27.014  91.405  1.00167.66
ATOM   2582  CA  PHE A 404      10.806  25.924  91.861  1.00170.15
ATOM   2583  C   PHE A 404      11.488  25.028  92.917  1.00173.78
ATOM   2584  O   PHE A 404      10.833  24.588  93.867  1.00174.51
ATOM   2585  CB  PHE A 404      10.360  25.063  90.678  1.00172.37
ATOM   2586  CG  PHE A 404       9.487  25.789  89.695  1.00174.20
ATOM   2587  CD1 PHE A 404       8.120  25.883  89.896  1.00174.61
ATOM   2588  CD2 PHE A 404      10.031  26.382  88.569  1.00179.08
ATOM   2589  CE1 PHE A 404       7.318  26.552  88.992  1.00176.28
ATOM   2590  CE2 PHE A 404       9.231  27.050  87.662  1.00182.50
ATOM   2591  CZ  PHE A 404       7.872  27.135  87.875  1.00178.56
ATOM   2592  N   VAL A 405      12.803  24.813  92.776  1.00168.63
ATOM   2593  CA  VAL A 405      13.559  23.988  93.705  1.00168.33
ATOM   2594  C   VAL A 405      13.952  24.760  94.982  1.00174.49
ATOM   2595  O   VAL A 405      14.354  24.126  95.964  1.00176.06
ATOM   2596  CB  VAL A 405      14.839  23.434  93.054  1.00169.71
ATOM   2597  CG1 VAL A 405      15.674  22.678  94.077  0.00 99.99
ATOM   2598  CG2 VAL A 405      14.491  22.481  91.920  0.00 99.99
ATOM   2599  N   ASN A 406      13.867  26.104  94.975  1.00170.06
ATOM   2600  CA  ASN A 406      14.262  26.922  96.127  1.00169.34
ATOM   2601  C   ASN A 406      13.424  26.608  97.352  1.00173.90
ATOM   2602  O   ASN A 406      12.195  26.605  97.276  1.00174.93
ATOM   2603  CB  ASN A 406      14.152  28.410  95.791  1.00170.65
ATOM   2604  CG  ASN A 406      14.685  29.299  96.897  1.00190.34
ATOM   2605  OD1 ASN A 406      13.996  29.562  97.882  1.00188.49
ATOM   2606  ND2 ASN A 406      15.919  29.763  96.737  1.00176.67
ATOM   2607  N   ASN A 407      14.088  26.353  98.487  1.00170.04
ATOM   2608  CA  ASN A 407      13.411  26.061  99.767  1.00171.21
ATOM   2609  C   ASN A 407      12.664  27.285 100.312  1.00172.94
ATOM   2610  O   ASN A 407      11.717  27.127 101.088  1.00173.55
ATOM   2611  CB  ASN A 407      14.419  25.567 100.806  1.00172.09
ATOM   2612  CG  ASN A 407      14.951  24.183 100.490  1.00200.04
ATOM   2613  OD1 ASN A 407      14.331  23.425  99.747  1.00194.87
ATOM   2614  ND2 ASN A 407      16.106  23.852 101.054  1.00190.69
ATOM   2615  N   GLU A 408      13.077  28.498  99.887  1.00166.38
ATOM   2616  CA  GLU A 408      12.478  29.764 100.322  1.00165.69
ATOM   2617  C   GLU A 408      11.134  30.001  99.655  1.00167.48
ATOM   2618  O   GLU A 408      10.175  30.360 100.339  1.00167.06
ATOM   2619  CB  GLU A 408      13.421  30.932 100.027  1.00165.52
ATOM   2620  CG  GLU A 408      12.910  32.279 100.511  1.00178.37
ATOM   2621  CD  GLU A 408      13.869  33.411 100.203  1.00211.34
ATOM   2622  OE1 GLU A 408      14.160  33.636  99.008  1.00212.11
ATOM   2623  OE2 GLU A 408      14.332  34.076 101.155  1.00213.09
ATOM   2624  N   VAL A 409      11.046  29.783  98.322  1.00163.11
ATOM   2625  CA  VAL A 409       9.778  29.957  97.607  1.00164.30
ATOM   2626  C   VAL A 409       8.806  28.858  98.037  1.00172.15
ATOM   2627  O   VAL A 409       7.596  29.057  97.967  1.00174.28
ATOM   2628  CB  VAL A 409       9.981  29.921  96.081  1.00165.77
ATOM   2629  CG1 VAL A 409       8.642  29.979  95.363  1.00162.87
ATOM   2630  CG2 VAL A 409      10.822  31.106  95.628  1.00164.89
ATOM   2631  N   GLN A 410       9.336  27.707  98.489  1.00169.36
ATOM   2632  CA  GLN A 410       8.518  26.617  99.001  1.00171.86
ATOM   2633  C   GLN A 410       7.871  27.037 100.342  1.00177.97
ATOM   2634  O   GLN A 410       6.734  26.646 100.624  1.00180.18
ATOM   2635  CB  GLN A 410       9.359  25.351  99.173  1.00172.51
ATOM   2636  CG  GLN A 410       9.854  24.752  97.866  1.00191.57
ATOM   2637  CD  GLN A 410      10.684  23.501  98.076  1.00206.66
ATOM   2638  OE1 GLN A 410      10.205  22.514  98.633  1.00199.09
ATOM   2639  NE2 GLN A 410      11.933  23.540  97.628  1.00196.12
ATOM   2640  N   LEU A 411       8.574  27.866 101.146  1.00173.45
ATOM   2641  CA  LEU A 411       8.007  28.405 102.388  1.00175.14
ATOM   2642  C   LEU A 411       6.970  29.472 102.043  1.00181.39
ATOM   2643  O   LEU A 411       5.986  29.621 102.771  1.00182.74
ATOM   2644  CB  LEU A 411       9.112  28.975 103.279  1.00173.37
ATOM   2645  CG  LEU A 411       9.832  27.976 104.188  0.00 99.99
ATOM   2646  CD1 LEU A 411      10.604  26.959 103.363  0.00 99.99
ATOM   2647  CD2 LEU A 411      10.815  28.692 105.102  0.00 99.99
ATOM   2648  N   GLU A 412       7.173  30.195 100.913  1.00177.68
ATOM   2649  CA  GLU A 412       6.208  31.184 100.439  1.00179.59
ATOM   2650  C   GLU A 412       5.005  30.476  99.846  1.00187.55
ATOM   2651  O   GLU A 412       3.886  30.971  99.968  1.00189.64
ATOM   2652  CB  GLU A 412       6.856  32.116  99.414  1.00178.70
ATOM   2653  CG  GLU A 412       7.936  33.018  99.990  0.00 99.99
ATOM   2654  CD  GLU A 412       8.554  33.925  98.944  0.00 99.99
ATOM   2655  OE1 GLU A 412       8.280  33.723  97.743  0.00 99.99
ATOM   2656  OE2 GLU A 412       9.314  34.841  99.327  0.00 99.99
ATOM   2657  N   PHE A 413       5.222  29.306  99.234  1.00185.71
ATOM   2658  CA  PHE A 413       4.132  28.481  98.735  1.00189.49
ATOM   2659  C   PHE A 413       3.237  28.065  99.905  1.00199.57
ATOM   2660  O   PHE A 413       2.011  28.177  99.826  1.00202.53
ATOM   2661  CB  PHE A 413       4.680  27.258  97.997  1.00189.96
ATOM   2662  CG  PHE A 413       3.616  26.390  97.389  1.00190.80
ATOM   2663  CD1 PHE A 413       3.028  26.733  96.183  1.00196.39
ATOM   2664  CD2 PHE A 413       3.203  25.231  98.020  1.00190.51
ATOM   2665  CE1 PHE A 413       2.048  25.935  95.623  1.00196.21
ATOM   2666  CE2 PHE A 413       2.223  24.431  97.463  1.00191.98
ATOM   2667  CZ  PHE A 413       1.646  24.783  96.263  1.00191.77
ATOM   2668  N   ARG A 414       3.859  27.605 101.003  1.00196.98
ATOM   2669  CA  ARG A 414       3.126  27.166 102.180  1.00200.83
ATOM   2670  C   ARG A 414       2.452  28.343 102.902  1.00209.11
ATOM   2671  O   ARG A 414       1.402  28.151 103.524  1.00212.46
ATOM   2672  CB  ARG A 414       4.055  26.428 103.146  1.00200.66
ATOM   2673  CG  ARG A 414       4.575  25.102 102.616  0.00 99.99
ATOM   2674  CD  ARG A 414       5.220  24.281 103.720  0.00 99.99
ATOM   2675  NE  ARG A 414       6.420  24.924 104.250  0.00 99.99
ATOM   2676  CZ  ARG A 414       7.630  24.800 103.716  0.00 99.99
ATOM   2677  NH1 ARG A 414       7.805  24.057 102.632  0.00 99.99
ATOM   2678  NH2 ARG A 414       8.664  25.422 104.268  0.00 99.99
ATOM   2679  N   LYS A 415       3.044  29.549 102.821  1.00204.91
ATOM   2680  CA  LYS A 415       2.455  30.734 103.438  1.00207.35
ATOM   2681  C   LYS A 415       1.223  31.177 102.657  1.00216.21
ATOM   2682  O   LYS A 415       0.224  31.569 103.260  1.00219.71
ATOM   2683  CB  LYS A 415       3.482  31.866 103.513  1.00207.16
ATOM   2684  CG  LYS A 415       4.639  31.592 104.458  0.00 99.99
ATOM   2685  CD  LYS A 415       5.619  32.754 104.485  0.00 99.99
ATOM   2686  CE  LYS A 415       4.999  33.983 105.127  0.00 99.99
ATOM   2687  NZ  LYS A 415       5.948  35.131 105.159  0.00 99.99
ATOM   2688  N   SER A 416       1.282  31.094 101.318  1.00212.78
ATOM   2689  CA  SER A 416       0.158  31.481 100.464  1.00215.96
ATOM   2690  C   SER A 416      -1.006  30.496 100.603  1.00224.68
ATOM   2691  O   SER A 416      -2.164  30.924 100.664  1.00224.92
ATOM   2692  CB  SER A 416       0.601  31.570  99.003  1.00216.39
ATOM   2693  OG  SER A 416       1.547  32.609  98.818  1.00221.17
ATOM   2694  N   TRP A 417      -0.701  29.190 100.683  1.00222.13
ATOM   2695  CA  TRP A 417      -1.726  28.160 100.846  1.00222.53
ATOM   2696  C   TRP A 417      -2.392  28.257 102.223  1.00227.94
ATOM   2697  O   TRP A 417      -3.595  28.014 102.333  1.00228.40
ATOM   2698  CB  TRP A 417      -1.123  26.768 100.649  1.00219.77
ATOM   2699  CG  TRP A 417      -2.130  25.662 100.731  0.00 99.99
ATOM   2700  CD1 TRP A 417      -2.853  25.134  99.701  0.00 99.99
ATOM   2701  CD2 TRP A 417      -2.523  24.947 101.909  0.00 99.99
ATOM   2702  NE1 TRP A 417      -3.674  24.133 100.161  0.00 99.99
ATOM   2703  CE2 TRP A 417      -3.489  24.000 101.516  0.00 99.99
ATOM   2704  CE3 TRP A 417      -2.152  25.017 103.254  0.00 99.99
ATOM   2705  CZ2 TRP A 417      -4.092  23.128 102.422  0.00 99.99
ATOM   2706  CZ3 TRP A 417      -2.750  24.152 104.151  0.00 99.99
ATOM   2707  CH2 TRP A 417      -3.711  23.216 103.734  0.00 99.99
ATOM   2708  N   GLU A 418      -1.622  28.621 103.264  1.00226.16
ATOM   2709  CA  GLU A 418      -2.165  28.765 104.613  1.00227.13
ATOM   2710  C   GLU A 418      -3.017  30.034 104.736  1.00231.95
ATOM   2711  O   GLU A 418      -3.968  30.054 105.522  1.00232.02
ATOM   2712  CB  GLU A 418      -1.036  28.788 105.645  1.00227.45
ATOM   2713  CG  GLU A 418      -1.515  28.863 107.086  1.00237.79
ATOM   2714  CD  GLU A 418      -1.899  30.270 107.499  1.00256.02
ATOM   2715  OE1 GLU A 418      -1.379  31.230 106.892  1.00256.46
ATOM   2716  OE2 GLU A 418      -2.721  30.414 108.429  1.00250.97
ATOM   2717  N   ARG A 419      -2.692  31.084 103.954  1.00230.43
ATOM   2718  CA  ARG A 419      -3.439  32.341 103.990  1.00232.05
ATOM   2719  C   ARG A 419      -4.865  32.183 103.453  1.00235.68
ATOM   2720  O   ARG A 419      -5.717  33.002 103.786  1.00235.96
ATOM   2721  CB  ARG A 419      -2.708  33.422 103.192  1.00232.14
ATOM   2722  CG  ARG A 419      -1.330  33.768 103.732  1.00238.93
ATOM   2723  CD  ARG A 419      -1.426  34.462 105.080  1.00249.39
ATOM   2724  NE  ARG A 419      -0.110  34.802 105.616  1.00255.49
ATOM   2725  CZ  ARG A 419       0.650  33.967 106.315  1.00257.99
ATOM   2726  NH1 ARG A 419       0.226  32.736 106.566  1.00253.57
ATOM   2727  NH2 ARG A 419       1.833  34.365 106.762  1.00252.10
ATOM   2728  N   TRP A 420      -5.134  31.130 102.658  1.00232.96
ATOM   2729  CA  TRP A 420      -6.478  30.840 102.166  1.00233.47
ATOM   2730  C   TRP A 420      -7.256  29.993 103.189  1.00236.10
ATOM   2731  O   TRP A 420      -8.408  30.310 103.498  1.00236.92
ATOM   2732  CB  TRP A 420      -6.412  30.122 100.817  1.00231.76
ATOM   2733  CG  TRP A 420      -5.829  30.958  99.720  1.00233.04
ATOM   2734  CD1 TRP A 420      -4.528  30.975  99.305  1.00234.96
ATOM   2735  CD2 TRP A 420      -6.528  31.902  98.899  1.00233.89
ATOM   2736  NE1 TRP A 420      -4.371  31.871  98.274  1.00235.28
ATOM   2737  CE2 TRP A 420      -5.587  32.453  98.006  1.00236.52
ATOM   2738  CE3 TRP A 420      -7.856  32.332  98.832  1.00235.13
ATOM   2739  CZ2 TRP A 420      -5.930  33.414  97.057  1.00236.45
ATOM   2740  CZ3 TRP A 420      -8.196  33.285  97.890  1.00236.57
ATOM   2741  CH2 TRP A 420      -7.239  33.819  97.012  1.00237.06
ATOM   2742  N   ARG A 421      -6.629  28.926 103.717  1.00231.87
ATOM   2743  CA  ARG A 421      -7.252  28.046 104.704  1.00237.88
ATOM   2744  C   ARG A 421      -6.471  28.068 106.011  1.00219.03
ATOM   2745  O   ARG A 421      -6.808  28.820 106.926  1.00177.36
ATOM   2746  CB  ARG A 421      -7.348  26.618 104.164  1.00236.81
ATOM   2747  CG  ARG A 421      -8.208  26.483 102.918  0.00 99.99
ATOM   2748  CD  ARG A 421      -9.673  26.741 103.229  0.00 99.99
ATOM   2749  NE  ARG A 421     -10.516  26.616 102.042  0.00 99.99
ATOM   2750  CZ  ARG A 421     -10.726  27.594 101.169  0.00 99.99
ATOM   2751  NH1 ARG A 421     -10.155  28.777 101.348  0.00 99.99
ATOM   2752  NH2 ARG A 421     -11.508  27.387 100.119  0.00 99.99
SPDBVT        1.0000000000         0.0000000000         0.0000000000 
SPDBVT        0.0000000000         1.0000000000         0.0000000000 
SPDBVT        0.0000000000         0.0000000000         1.0000000000 
SPDBVT        0.0000000000         0.0000000000         0.0000000000 
SPDBVT        0.0000000000         0.0000000000         0.0000000000 
SPDBVV default;
SPDBVV      6.800789717232    1701.384545885313      20.000000000000
SPDBVV       -0.8615116481         0.0305328387         0.5068189281 
SPDBVV        0.5032613521         0.1836065708         0.8444031257 
SPDBVV       -0.0672732610         0.9825255075        -0.1735451971 
SPDBVV       16.7814998627        26.3269996643        75.0595016479 
SPDBVV        0.0000000000         0.0000000000         0.0000000000 
SPDBVf 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51
SPDBVf 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51
SPDBVf 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51
SPDBVf 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51
SPDBVf 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51
SPDBVf 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51
SPDBVf 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51
SPDBVf 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51
SPDBVf 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51
SPDBVf 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51
SPDBVf 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51
SPDBVf 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51
SPDBVf 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51
SPDBVf 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51
SPDBVf 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51
SPDBVf 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51
SPDBVf 51 51 51 51 51 51 51 51 51 51 51 51 51 51 51
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 1.00 0.00 1.00 
SPDBVc 1.00 0.00 1.00 1.00 0.00 1.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 1.00 0.00 1.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 1.00 0.00 1.00 
SPDBVc 1.00 0.00 1.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVc 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 1.00 0.00 1.00 1.00 0.00 1.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVc 1.00 0.00 1.00 1.00 0.00 1.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 
SPDBVc 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 1.00 0.00 1.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 1.00 0.00 1.00 1.00 0.00 1.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVc 1.00 0.00 1.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 1.00 0.00 1.00 
SPDBVc 0.00 0.00 0.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 
SPDBVc 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVc 1.00 0.00 1.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 1.00 0.00 1.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVc 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 1.00 0.00 1.00 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 1.00 0.00 1.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVc 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVc 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 0.00 0.00 0.00 
SPDBVc 1.00 0.00 1.00 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVc 1.00 0.00 1.00 1.00 0.00 1.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVc 1.00 0.00 1.00 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 
SPDBVc 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 1.00 0.00 1.00 
SPDBVC 1.00 0.00 1.00 1.00 0.00 1.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 1.00 0.00 1.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 1.00 0.00 1.00 
SPDBVC 1.00 0.00 1.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVC 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 1.00 0.00 1.00 1.00 0.00 1.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVC 1.00 0.00 1.00 1.00 0.00 1.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 
SPDBVC 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 1.00 0.00 1.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 1.00 0.00 1.00 1.00 0.00 1.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVC 1.00 0.00 1.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 1.00 0.00 1.00 
SPDBVC 0.00 0.00 0.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 
SPDBVC 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVC 1.00 0.00 1.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 1.00 0.00 1.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVC 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 1.00 0.00 1.00 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 1.00 0.00 1.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVC 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVC 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 0.00 0.00 0.00 
SPDBVC 1.00 0.00 1.00 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 
SPDBVC 1.00 0.00 1.00 1.00 0.00 1.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVC 1.00 0.00 1.00 0.00 0.00 0.00 1.00 0.00 1.00 0.00 0.00 0.00 
SPDBVC 0.00 0.00 0.00 0.00 0.00 0.00 1.00 0.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVb 0.00 0.00 0.00
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64
SPDBVi        1 1 1 0 1 0 1 1 0 1 0 1 1 0  0
SPDBVp    10090
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.