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***  7BW1-COM MEMBRANA-TESTE  ***

elNémo ID: 21060222025986620

Job options:

ID        	=	 21060222025986620
JOBID     	=	 7BW1-COM MEMBRANA-TESTE
USERID    	=	 7BW1-COMMEMBRANA-TESTE
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -3
DQMAX     	=	 3
DQSTEP    	=	 1
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 7BW1-COM MEMBRANA-TESTE

REMARK      1/2 of bilayer thickness:   15.2
TITLE     CRYSTAL STRUCTURE OF STEROID 5-ALPHA-REDUCTASE 2 IN COMPLEX WITH      
TITLE    2 FINASTERIDE                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 3-OXO-5-ALPHA-STEROID 4-DEHYDROGENASE 2;                   
COMPND   4 SYNONYM: 5 ALPHA-SR2,SR TYPE 2,STEROID 5-ALPHA-REDUCTASE 2,S5AR 2,   
COMPND   5 TYPE II 5-ALPHA REDUCTASE;                                           
COMPND   6 EC: 1.3.1.22;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SRD5A2;                                                        
SOURCE   6 EXPRESSION_SYSTEM: BACULOVIRUS EXPRESSION VECTOR PFASTBAC1-HM;       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 274590                                      
KEYWDS    INTEGRAL MEMBRANE PROTEIN, REDUCTASE, STEROID, OXIDOREDUCTASE         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Q.XIAO,C.ZHANG,Z.WEI                                                  
REVDAT   1   05-AUG-20 7BW1    0                                                
JRNL        AUTH   Q.XIAO,L.WANG,S.SUPEKAR,T.SHEN,H.LIU,F.YE,J.HUANG,H.FAN,     
JRNL        AUTH 2 Z.WEI,C.ZHANG                                                
JRNL        TITL   STRUCTURE OF HUMAN STEROID 5 ALPHA-REDUCTASE 2 WITH          
JRNL        TITL 2 ANTI-ANDROGEN DRUG FINASTERIDE.                              
JRNL        REF    RES SQ                                     2020              
JRNL        PMID   32702725                                                     
JRNL        DOI    10.21203/RS.3.RS-40159/V1                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.17                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 9155                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.241                           
REMARK   3   R VALUE            (WORKING SET) : 0.239                           
REMARK   3   FREE R VALUE                     : 0.265                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.170                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 473                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 35.1710 -  4.0118    1.00     3053   190  0.2196 0.2511        
REMARK   3     2  4.0118 -  3.1850    1.00     2898   157  0.2531 0.2724        
REMARK   3     3  3.1850 -  2.8000    0.95     2731   126  0.2966 0.3358        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.200           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 68.94                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 75.84                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           2107                                  
REMARK   3   ANGLE     :  0.765           2881                                  
REMARK   3   CHIRALITY :  0.032            310                                  
REMARK   3   PLANARITY :  0.004            350                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 5 THROUGH 48 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -22.0636  10.6766  33.7347              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5349 T22:   0.7199                                     
REMARK   3      T33:   0.5411 T12:   0.0367                                     
REMARK   3      T13:   0.1064 T23:   0.0167                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1226 L22:   7.4782                                     
REMARK   3      L33:   0.9887 L12:  -2.2432                                     
REMARK   3      L13:   0.6597 L23:   1.7446                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1604 S12:  -0.7409 S13:   0.3732                       
REMARK   3      S21:   0.6728 S22:   0.8475 S23:  -0.0205                       
REMARK   3      S31:  -0.3619 S32:   1.0998 S33:  -0.7074                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 49 THROUGH 180 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -33.5553  17.2465  24.3089              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6125 T22:   0.5054                                     
REMARK   3      T33:   0.4389 T12:  -0.0019                                     
REMARK   3      T13:  -0.1344 T23:   0.0353                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1800 L22:   3.1583                                     
REMARK   3      L33:   3.2868 L12:   0.0964                                     
REMARK   3      L13:  -1.5144 L23:   0.2809                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0638 S12:   0.3617 S13:  -0.0248                       
REMARK   3      S21:  -0.8240 S22:   0.0847 S23:   0.2007                       
REMARK   3      S31:  -0.6971 S32:  -0.0082 S33:  -0.0309                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 181 THROUGH 254 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -37.5839   6.4171  36.0828              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5512 T22:   0.3800                                     
REMARK   3      T33:   0.4045 T12:  -0.0150                                     
REMARK   3      T13:  -0.1061 T23:  -0.0406                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7658 L22:   4.1148                                     
REMARK   3      L33:   4.8818 L12:   0.8886                                     
REMARK   3      L13:  -0.2105 L23:   1.4299                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0554 S12:   0.0197 S13:   0.0172                       
REMARK   3      S21:  -0.2388 S22:  -0.0508 S23:  -0.0377                       
REMARK   3      S31:   0.5997 S32:  -0.1664 S33:   0.0642                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 7BW1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-AUG-19                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9161                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 9.600                              
REMARK 200  R MERGE                    (I) : 0.24800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 3.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.27400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.02                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% V/V PEG600, 100MM TRIS-SODIUM        
REMARK 280  CITRATE PH5.0, 100MM SODIUM CHLORIDE, 100MM LITHIUM SULFATE,        
REMARK 280  LIPIDIC CUBIC PHASE, TEMPERATURE 293K                               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 6 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z                                                
REMARK 290       6555   X-Y,X,Z                                                 
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z                                              
REMARK 290      10555   -Y,-X,-Z                                                
REMARK 290      11555   -X+Y,Y,-Z                                               
REMARK 290      12555   X,X-Y,-Z                                                
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000        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 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 210 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 12020 ANGSTROM**2                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 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     GLY A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     THR A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLN A     2                                                      
REMARK 465     VAL A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     SER A    39                                                      
REMARK 465     LEU A    40                                                      
REMARK 465     LYS A    41                                                      
REMARK 465     PRO A    42                                                      
REMARK 465     ALA A    43                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A   7    CG   CD   OE1  NE2                                  
REMARK 470     ARG A  70    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A  73    CG   CD1  CD2                                       
REMARK 470     LEU A  75    CG   CD1  CD2                                       
REMARK 470     PHE A  76    CG   CD1  CD2  CE1  CE2  CZ                         
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                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  28      -45.79     66.41                                   
REMARK 500    LYS A  35      -72.75    -72.57                                   
REMARK 500    PHE A  76       43.77    -83.03                                   
REMARK 500    VAL A  97      -61.19   -108.18                                   
REMARK 500    LEU A 185      -15.45     67.37                                   
REMARK 500    LEU A 249      -59.15   -144.35                                   
REMARK 500    ILE A 253      -69.09   -128.70                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NDX A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 604                 
DBREF  7BW1 A    1   254  UNP    P31213   S5A2_HUMAN       1    254             
SEQADV 7BW1 GLY A   -3  UNP  P31213              EXPRESSION TAG                 
SEQADV 7BW1 GLY A   -2  UNP  P31213              EXPRESSION TAG                 
SEQADV 7BW1 GLY A   -1  UNP  P31213              EXPRESSION TAG                 
SEQRES   1 A  258  GLY GLY GLY THR MET GLN VAL GLN CYS GLN GLN SER PRO          
SEQRES   2 A  258  VAL LEU ALA GLY SER ALA THR LEU VAL ALA LEU GLY ALA          
SEQRES   3 A  258  LEU ALA LEU TYR VAL ALA LYS PRO SER GLY TYR GLY LYS          
SEQRES   4 A  258  HIS THR GLU SER LEU LYS PRO ALA ALA THR ARG LEU PRO          
SEQRES   5 A  258  ALA ARG ALA ALA TRP PHE LEU GLN GLU LEU PRO SER PHE          
SEQRES   6 A  258  ALA VAL PRO ALA GLY ILE LEU ALA ARG GLN PRO LEU SER          
SEQRES   7 A  258  LEU PHE GLY PRO PRO GLY THR VAL LEU LEU GLY LEU PHE          
SEQRES   8 A  258  CYS VAL HIS TYR PHE HIS ARG THR PHE VAL TYR SER LEU          
SEQRES   9 A  258  LEU ASN ARG GLY ARG PRO TYR PRO ALA ILE LEU ILE LEU          
SEQRES  10 A  258  ARG GLY THR ALA PHE CYS THR GLY ASN GLY VAL LEU GLN          
SEQRES  11 A  258  GLY TYR TYR LEU ILE TYR CYS ALA GLU TYR PRO ASP GLY          
SEQRES  12 A  258  TRP TYR THR ASP ILE ARG PHE SER LEU GLY VAL PHE LEU          
SEQRES  13 A  258  PHE ILE LEU GLY MET GLY ILE ASN ILE HIS SER ASP TYR          
SEQRES  14 A  258  ILE LEU ARG GLN LEU ARG LYS PRO GLY GLU ILE SER TYR          
SEQRES  15 A  258  ARG ILE PRO GLN GLY GLY LEU PHE THR TYR VAL SER GLY          
SEQRES  16 A  258  ALA ASN PHE LEU GLY GLU ILE ILE GLU TRP ILE GLY TYR          
SEQRES  17 A  258  ALA LEU ALA THR TRP SER LEU PRO ALA LEU ALA PHE ALA          
SEQRES  18 A  258  PHE PHE SER LEU CYS PHE LEU GLY LEU ARG ALA PHE HIS          
SEQRES  19 A  258  HIS HIS ARG PHE TYR LEU LYS MET PHE GLU ASP TYR PRO          
SEQRES  20 A  258  LYS SER ARG LYS ALA LEU ILE PRO PHE ILE PHE                  
HET    OLC  A 601      25                                                       
HET    NDX  A 602      75                                                       
HET    SO4  A 603       5                                                       
HET    SO4  A 604       5                                                       
HETNAM     OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE                   
HETNAM     NDX [[(2~{R},3~{S},4~{R},5~{R})-5-[4-[(1~{S},3~{A}~{S},              
HETNAM   2 NDX  3~{B}~{S},5~{A}~{R},8~{S},9~{A}~{R},9~{B}~{S},                  
HETNAM   3 NDX  11~{A}~{S})-1-(~{TERT}-BUTYLCARBAMOYL)-9~{A},11~{A}-            
HETNAM   4 NDX  DIMETHYL-7-OXIDANYLIDENE-1,2,3,3~{A},3~{B},4,5,5~{A},           
HETNAM   5 NDX  6,8,9,9~{B},10,11-TETRADECAHYDROINDENO[5,4-F]QUINOLIN-          
HETNAM   6 NDX  8-YL]-3-AMINOCARBONYL-4~{H}-PYRIDIN-1-YL]-3,4-                  
HETNAM   7 NDX  BIS(OXIDANYL)OXOLAN-2-YL]METHOXY-OXIDANYL-PHOSPHORYL]           
HETNAM   8 NDX  [(2~{R},3~{R},4~{R},5~{R})-5-(6-AMINOPURIN-9-YL)-3-             
HETNAM   9 NDX  OXIDANYL-4-PHOSPHONOOXY-OXOLAN-2-YL]METHYL HYDROGEN             
HETNAM  10 NDX  PHOSPHATE                                                       
HETNAM     SO4 SULFATE ION                                                      
HETSYN     OLC 1-OLEOYL-R-GLYCEROL                                              
FORMUL   2  OLC    C21 H40 O4                                                   
FORMUL   4  SO4    2(O4 S 2-)                                                   
HELIX    1 AA1 GLN A    7  ALA A   28  1                                  22    
HELIX    2 AA2 PRO A   48  LEU A   58  1                                  11    
HELIX    3 AA3 LEU A   58  ALA A   69  1                                  12    
HELIX    4 AA4 PRO A   78  VAL A   97  1                                  20    
HELIX    5 AA5 TYR A   98  ASN A  102  5                                   5    
HELIX    6 AA6 ALA A  109  CYS A  133  1                                  25    
HELIX    7 AA7 ASP A  143  GLN A  169  1                                  27    
HELIX    8 AA8 GLY A  191  TRP A  209  1                                  19    
HELIX    9 AA9 SER A  210  PHE A  239  1                                  30    
SHEET    1 AA1 2 ARG A  46  LEU A  47  0                                        
SHEET    2 AA1 2 TYR A 107  PRO A 108 -1  O  TYR A 107   N  LEU A  47           
SSBOND   1 CYS A    5    CYS A  133                          1555   1555  2.03  
SITE     1 AC1  4 ALA A 205  LEU A 206  TRP A 209  LEU A 214                    
SITE     1 AC2 31 ALA A  24  SER A  31  TYR A  33  GLY A  34                    
SITE     2 AC2 31 LYS A  35  TRP A  53  GLU A  57  ARG A  94                    
SITE     3 AC2 31 TYR A  98  ASN A 102  GLY A 104  ARG A 105                    
SITE     4 AC2 31 ARG A 114  PHE A 118  ASN A 160  ASP A 164                    
SITE     5 AC2 31 LEU A 167  ARG A 171  SER A 177  TYR A 178                    
SITE     6 AC2 31 ARG A 179  ASN A 193  PHE A 194  GLU A 197                    
SITE     7 AC2 31 TRP A 201  PHE A 219  SER A 220  PHE A 223                    
SITE     8 AC2 31 ARG A 227  HIS A 231  TYR A 235                               
SITE     1 AC3  9 PRO A  30  GLY A  32  TYR A  33  GLY A  34                    
SITE     2 AC3  9 LYS A  35  HIS A  36  THR A  37  ARG A 227                    
SITE     3 AC3  9 HIS A 231                                                     
SITE     1 AC4  2 HIS A 162  GLY A 184                                          
CRYST1  107.449  107.449  103.372  90.00  90.00 120.00 P 6 2 2      12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009307  0.005373  0.000000        0.00000                         
SCALE2      0.000000  0.010746  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009674        0.00000                         
ATOM      1  N   CYS A   5      -6.252  -3.731  21.445  1.00126.60           N  
ATOM      2  CA  CYS A   5      -5.883  -4.080  20.076  1.00120.35           C  
ATOM      3  C   CYS A   5      -6.219  -5.534  19.753  1.00117.41           C  
ATOM      4  O   CYS A   5      -5.485  -6.447  20.128  1.00116.19           O  
ATOM      5  CB  CYS A   5      -4.392  -3.829  19.843  1.00117.53           C  
ATOM      6  SG  CYS A   5      -3.798  -4.320  18.201  1.00152.38           S  
ATOM      7  N   GLN A   6      -7.331  -5.747  19.056  1.00117.44           N  
ATOM      8  CA  GLN A   6      -7.734  -7.091  18.651  1.00116.56           C  
ATOM      9  C   GLN A   6      -6.792  -7.641  17.584  1.00110.39           C  
ATOM     10  O   GLN A   6      -6.651  -7.059  16.511  1.00105.65           O  
ATOM     11  CB  GLN A   6      -9.174  -7.090  18.133  1.00120.89           C  
ATOM     12  CG  GLN A   6     -10.222  -6.829  19.201  1.00129.61           C  
ATOM     13  CD  GLN A   6     -11.630  -6.800  18.638  1.00134.79           C  
ATOM     14  OE1 GLN A   6     -11.823  -6.683  17.428  1.00133.70           O  
ATOM     15  NE2 GLN A   6     -12.620  -6.910  19.514  1.00141.07           N  
ATOM     16  N   GLN A   7      -6.153  -8.769  17.884  1.00112.60           N  
ATOM     17  CA  GLN A   7      -5.165  -9.348  16.979  1.00110.56           C  
ATOM     18  C   GLN A   7      -5.785 -10.299  15.955  1.00107.41           C  
ATOM     19  O   GLN A   7      -5.149 -10.644  14.963  1.00105.25           O  
ATOM     20  CB  GLN A   7      -4.084 -10.083  17.777  1.00112.82           C  
ATOM     21  N   SER A   8      -7.023 -10.719  16.196  1.00107.59           N  
ATOM     22  CA  SER A   8      -7.704 -11.645  15.287  1.00107.96           C  
ATOM     23  C   SER A   8      -8.136 -11.002  13.958  1.00102.50           C  
ATOM     24  O   SER A   8      -7.930 -11.599  12.901  1.00 99.77           O  
ATOM     25  CB  SER A   8      -8.918 -12.277  15.978  1.00116.76           C  
ATOM     26  OG  SER A   8      -8.525 -13.060  17.090  1.00125.74           O  
ATOM     27  N   PRO A   9      -8.747  -9.799  13.995  1.00104.66           N  
ATOM     28  CA  PRO A   9      -9.079  -9.192  12.699  1.00102.71           C  
ATOM     29  C   PRO A   9      -7.844  -8.821  11.872  1.00 95.78           C  
ATOM     30  O   PRO A   9      -7.923  -8.776  10.645  1.00 93.65           O  
ATOM     31  CB  PRO A   9      -9.866  -7.935  13.091  1.00106.75           C  
ATOM     32  CG  PRO A   9     -10.399  -8.229  14.442  1.00111.70           C  
ATOM     33  CD  PRO A   9      -9.327  -9.027  15.110  1.00109.92           C  
ATOM     34  N   VAL A  10      -6.725  -8.563  12.539  1.00 94.41           N  
ATOM     35  CA  VAL A  10      -5.485  -8.211  11.856  1.00 89.22           C  
ATOM     36  C   VAL A  10      -4.907  -9.395  11.081  1.00 89.07           C  
ATOM     37  O   VAL A  10      -4.587  -9.271   9.898  1.00 90.22           O  
ATOM     38  CB  VAL A  10      -4.426  -7.689  12.848  1.00 87.44           C  
ATOM     39  CG1 VAL A  10      -3.039  -7.728  12.222  1.00 83.23           C  
ATOM     40  CG2 VAL A  10      -4.778  -6.281  13.305  1.00 88.53           C  
ATOM     41  N   LEU A  11      -4.778 -10.539  11.750  1.00 88.31           N  
ATOM     42  CA  LEU A  11      -4.244 -11.743  11.116  1.00 86.10           C  
ATOM     43  C   LEU A  11      -5.117 -12.196   9.946  1.00 83.75           C  
ATOM     44  O   LEU A  11      -4.622 -12.767   8.975  1.00 79.61           O  
ATOM     45  CB  LEU A  11      -4.106 -12.877  12.141  1.00 89.22           C  
ATOM     46  CG  LEU A  11      -2.924 -12.809  13.115  1.00 92.61           C  
ATOM     47  CD1 LEU A  11      -3.024 -13.888  14.185  1.00 97.13           C  
ATOM     48  CD2 LEU A  11      -1.608 -12.931  12.367  1.00 89.94           C  
ATOM     49  N   ALA A  12      -6.416 -11.930  10.042  1.00 86.84           N  
ATOM     50  CA  ALA A  12      -7.358 -12.320   9.001  1.00 87.49           C  
ATOM     51  C   ALA A  12      -7.237 -11.426   7.769  1.00 85.28           C  
ATOM     52  O   ALA A  12      -7.369 -11.893   6.638  1.00 84.64           O  
ATOM     53  CB  ALA A  12      -8.779 -12.286   9.539  1.00 92.30           C  
ATOM     54  N   GLY A  13      -6.992 -10.140   7.995  1.00 84.39           N  
ATOM     55  CA  GLY A  13      -6.842  -9.191   6.907  1.00 83.53           C  
ATOM     56  C   GLY A  13      -5.605  -9.487   6.082  1.00 81.76           C  
ATOM     57  O   GLY A  13      -5.625  -9.406   4.853  1.00 80.11           O  
ATOM     58  N   SER A  14      -4.525  -9.838   6.771  1.00 83.93           N  
ATOM     59  CA  SER A  14      -3.272 -10.195   6.118  1.00 82.61           C  
ATOM     60  C   SER A  14      -3.401 -11.524   5.387  1.00 78.84           C  
ATOM     61  O   SER A  14      -2.711 -11.772   4.401  1.00 76.94           O  
ATOM     62  CB  SER A  14      -2.138 -10.265   7.141  1.00 84.51           C  
ATOM     63  OG  SER A  14      -2.053  -9.068   7.897  1.00 85.26           O  
ATOM     64  N   ALA A  15      -4.289 -12.378   5.882  1.00 79.22           N  
ATOM     65  CA  ALA A  15      -4.518 -13.682   5.275  1.00 78.94           C  
ATOM     66  C   ALA A  15      -5.224 -13.537   3.931  1.00 78.82           C  
ATOM     67  O   ALA A  15      -4.756 -14.065   2.922  1.00 78.23           O  
ATOM     68  CB  ALA A  15      -5.326 -14.567   6.207  1.00 80.34           C  
ATOM     69  N   THR A  16      -6.346 -12.820   3.923  1.00 78.09           N  
ATOM     70  CA  THR A  16      -7.098 -12.591   2.693  1.00 77.37           C  
ATOM     71  C   THR A  16      -6.227 -11.876   1.672  1.00 74.56           C  
ATOM     72  O   THR A  16      -6.218 -12.227   0.495  1.00 74.38           O  
ATOM     73  CB  THR A  16      -8.375 -11.756   2.938  1.00 77.67           C  
ATOM     74  OG1 THR A  16      -8.024 -10.509   3.547  1.00 76.91           O  
ATOM     75  CG2 THR A  16      -9.347 -12.503   3.838  1.00 79.70           C  
ATOM     76  N   LEU A  17      -5.485 -10.883   2.149  1.00 73.28           N  
ATOM     77  CA  LEU A  17      -4.586 -10.093   1.318  1.00 69.11           C  
ATOM     78  C   LEU A  17      -3.530 -10.971   0.651  1.00 70.45           C  
ATOM     79  O   LEU A  17      -3.051 -10.664  -0.442  1.00 72.49           O  
ATOM     80  CB  LEU A  17      -3.924  -9.007   2.168  1.00 66.83           C  
ATOM     81  CG  LEU A  17      -3.174  -7.865   1.492  1.00 64.72           C  
ATOM     82  CD1 LEU A  17      -3.962  -7.329   0.316  1.00 65.28           C  
ATOM     83  CD2 LEU A  17      -2.929  -6.764   2.511  1.00 65.22           C  
ATOM     84  N   VAL A  18      -3.177 -12.066   1.315  1.00 69.39           N  
ATOM     85  CA  VAL A  18      -2.236 -13.036   0.766  1.00 68.27           C  
ATOM     86  C   VAL A  18      -2.964 -14.031  -0.125  1.00 68.61           C  
ATOM     87  O   VAL A  18      -2.494 -14.375  -1.210  1.00 72.24           O  
ATOM     88  CB  VAL A  18      -1.487 -13.793   1.885  1.00 65.86           C  
ATOM     89  CG1 VAL A  18      -0.937 -15.121   1.376  1.00 65.81           C  
ATOM     90  CG2 VAL A  18      -0.374 -12.930   2.449  1.00 63.65           C  
ATOM     91  N   ALA A  19      -4.122 -14.484   0.342  1.00 68.27           N  
ATOM     92  CA  ALA A  19      -4.953 -15.407  -0.418  1.00 67.61           C  
ATOM     93  C   ALA A  19      -5.381 -14.777  -1.736  1.00 68.73           C  
ATOM     94  O   ALA A  19      -5.480 -15.461  -2.755  1.00 68.00           O  
ATOM     95  CB  ALA A  19      -6.171 -15.823   0.391  1.00 67.67           C  
ATOM     96  N   LEU A  20      -5.640 -13.472  -1.714  1.00 67.74           N  
ATOM     97  CA  LEU A  20      -5.967 -12.756  -2.936  1.00 68.40           C  
ATOM     98  C   LEU A  20      -4.801 -12.864  -3.899  1.00 70.49           C  
ATOM     99  O   LEU A  20      -4.986 -13.175  -5.075  1.00 76.14           O  
ATOM    100  CB  LEU A  20      -6.296 -11.290  -2.653  1.00 64.72           C  
ATOM    101  CG  LEU A  20      -7.629 -10.986  -1.966  1.00 64.81           C  
ATOM    102  CD1 LEU A  20      -7.826  -9.485  -1.842  1.00 63.93           C  
ATOM    103  CD2 LEU A  20      -8.794 -11.629  -2.705  1.00 66.48           C  
ATOM    104  N   GLY A  21      -3.600 -12.614  -3.385  1.00 67.93           N  
ATOM    105  CA  GLY A  21      -2.387 -12.717  -4.177  1.00 66.73           C  
ATOM    106  C   GLY A  21      -2.242 -14.088  -4.810  1.00 67.92           C  
ATOM    107  O   GLY A  21      -1.871 -14.211  -5.978  1.00 68.52           O  
ATOM    108  N   ALA A  22      -2.550 -15.122  -4.036  1.00 68.63           N  
ATOM    109  CA  ALA A  22      -2.480 -16.486  -4.536  1.00 71.11           C  
ATOM    110  C   ALA A  22      -3.566 -16.729  -5.578  1.00 72.30           C  
ATOM    111  O   ALA A  22      -3.351 -17.428  -6.566  1.00 73.95           O  
ATOM    112  CB  ALA A  22      -2.606 -17.481  -3.390  1.00 72.10           C  
ATOM    113  N   LEU A  23      -4.735 -16.138  -5.348  1.00 70.84           N  
ATOM    114  CA  LEU A  23      -5.874 -16.309  -6.241  1.00 70.82           C  
ATOM    115  C   LEU A  23      -5.592 -15.711  -7.615  1.00 72.93           C  
ATOM    116  O   LEU A  23      -5.964 -16.285  -8.640  1.00 75.74           O  
ATOM    117  CB  LEU A  23      -7.127 -15.668  -5.641  1.00 67.25           C  
ATOM    118  CG  LEU A  23      -8.440 -16.043  -6.326  1.00 67.09           C  
ATOM    119  CD1 LEU A  23      -8.759 -17.512  -6.088  1.00 66.87           C  
ATOM    120  CD2 LEU A  23      -9.573 -15.154  -5.846  1.00 67.57           C  
ATOM    121  N   ALA A  24      -4.930 -14.559  -7.627  1.00 70.49           N  
ATOM    122  CA  ALA A  24      -4.594 -13.875  -8.871  1.00 71.34           C  
ATOM    123  C   ALA A  24      -3.623 -14.702  -9.714  1.00 73.34           C  
ATOM    124  O   ALA A  24      -3.641 -14.638 -10.943  1.00 75.57           O  
ATOM    125  CB  ALA A  24      -4.008 -12.502  -8.577  1.00 68.77           C  
ATOM    126  N   LEU A  25      -2.781 -15.480  -9.045  1.00 73.17           N  
ATOM    127  CA  LEU A  25      -1.840 -16.353  -9.732  1.00 75.42           C  
ATOM    128  C   LEU A  25      -2.535 -17.596 -10.277  1.00 79.33           C  
ATOM    129  O   LEU A  25      -2.166 -18.112 -11.333  1.00 81.88           O  
ATOM    130  CB  LEU A  25      -0.712 -16.763  -8.791  1.00 73.33           C  
ATOM    131  CG  LEU A  25       0.098 -15.622  -8.181  1.00 71.25           C  
ATOM    132  CD1 LEU A  25       0.983 -16.160  -7.080  1.00 68.53           C  
ATOM    133  CD2 LEU A  25       0.925 -14.919  -9.242  1.00 73.06           C  
ATOM    134  N   TYR A  26      -3.538 -18.076  -9.549  1.00 80.94           N  
ATOM    135  CA  TYR A  26      -4.256 -19.285  -9.938  1.00 85.08           C  
ATOM    136  C   TYR A  26      -5.052 -19.062 -11.222  1.00 90.19           C  
ATOM    137  O   TYR A  26      -5.131 -19.948 -12.072  1.00 93.27           O  
ATOM    138  CB  TYR A  26      -5.181 -19.744  -8.807  1.00 82.93           C  
ATOM    139  CG  TYR A  26      -5.946 -21.014  -9.108  1.00 86.04           C  
ATOM    140  CD1 TYR A  26      -5.361 -22.260  -8.928  1.00 86.36           C  
ATOM    141  CD2 TYR A  26      -7.258 -20.966  -9.563  1.00 88.54           C  
ATOM    142  CE1 TYR A  26      -6.059 -23.425  -9.200  1.00 88.88           C  
ATOM    143  CE2 TYR A  26      -7.962 -22.125  -9.839  1.00 91.85           C  
ATOM    144  CZ  TYR A  26      -7.359 -23.350  -9.654  1.00 91.80           C  
ATOM    145  OH  TYR A  26      -8.061 -24.503  -9.926  1.00 95.61           O  
ATOM    146  N   VAL A  27      -5.637 -17.876 -11.358  1.00 92.03           N  
ATOM    147  CA  VAL A  27      -6.402 -17.531 -12.550  1.00 98.55           C  
ATOM    148  C   VAL A  27      -5.484 -17.398 -13.768  1.00103.05           C  
ATOM    149  O   VAL A  27      -5.898 -17.664 -14.899  1.00106.49           O  
ATOM    150  CB  VAL A  27      -7.194 -16.219 -12.349  1.00 97.83           C  
ATOM    151  CG1 VAL A  27      -8.079 -15.930 -13.558  1.00101.44           C  
ATOM    152  CG2 VAL A  27      -8.035 -16.300 -11.088  1.00 96.23           C  
ATOM    153  N   ALA A  28      -4.241 -16.984 -13.517  1.00103.67           N  
ATOM    154  CA  ALA A  28      -3.208 -16.798 -14.545  1.00104.57           C  
ATOM    155  C   ALA A  28      -3.533 -15.659 -15.516  1.00107.68           C  
ATOM    156  O   ALA A  28      -2.666 -14.841 -15.824  1.00108.41           O  
ATOM    157  CB  ALA A  28      -2.971 -18.100 -15.315  1.00107.97           C  
ATOM    158  N   LYS A  29      -4.773 -15.611 -15.999  1.00109.61           N  
ATOM    159  CA  LYS A  29      -5.215 -14.533 -16.880  1.00110.21           C  
ATOM    160  C   LYS A  29      -5.257 -13.207 -16.120  1.00105.02           C  
ATOM    161  O   LYS A  29      -5.576 -13.182 -14.929  1.00102.84           O  
ATOM    162  CB  LYS A  29      -6.589 -14.855 -17.474  1.00113.37           C  
ATOM    163  CG  LYS A  29      -6.624 -16.136 -18.292  1.00116.91           C  
ATOM    164  CD  LYS A  29      -8.037 -16.465 -18.742  1.00118.45           C  
ATOM    165  CE  LYS A  29      -8.081 -17.779 -19.504  1.00121.38           C  
ATOM    166  NZ  LYS A  29      -9.470 -18.151 -19.889  1.00123.70           N  
ATOM    167  N   PRO A  30      -4.929 -12.099 -16.807  1.00104.10           N  
ATOM    168  CA  PRO A  30      -4.886 -10.772 -16.177  1.00 99.29           C  
ATOM    169  C   PRO A  30      -6.239 -10.332 -15.616  1.00 98.84           C  
ATOM    170  O   PRO A  30      -7.247 -11.001 -15.844  1.00100.84           O  
ATOM    171  CB  PRO A  30      -4.456  -9.848 -17.323  1.00100.65           C  
ATOM    172  CG  PRO A  30      -3.813 -10.741 -18.326  1.00103.46           C  
ATOM    173  CD  PRO A  30      -4.538 -12.044 -18.226  1.00106.10           C  
ATOM    174  N   SER A  31      -6.257  -9.214 -14.896  1.00 97.58           N  
ATOM    175  CA  SER A  31      -7.495  -8.699 -14.319  1.00 98.09           C  
ATOM    176  C   SER A  31      -8.373  -8.070 -15.403  1.00 99.38           C  
ATOM    177  O   SER A  31      -9.545  -7.771 -15.172  1.00100.62           O  
ATOM    178  CB  SER A  31      -7.194  -7.684 -13.214  1.00 97.42           C  
ATOM    179  OG  SER A  31      -8.276  -7.589 -12.303  1.00 99.54           O  
ATOM    180  N   GLY A  32      -7.789  -7.867 -16.581  1.00 98.86           N  
ATOM    181  CA  GLY A  32      -8.521  -7.458 -17.769  1.00 98.61           C  
ATOM    182  C   GLY A  32      -9.213  -6.104 -17.741  1.00 95.20           C  
ATOM    183  O   GLY A  32     -10.433  -6.028 -17.891  1.00 97.78           O  
ATOM    184  N   TYR A  33      -8.441  -5.036 -17.561  1.00 89.96           N  
ATOM    185  CA  TYR A  33      -8.995  -3.685 -17.633  1.00 86.69           C  
ATOM    186  C   TYR A  33      -8.091  -2.760 -18.445  1.00 86.35           C  
ATOM    187  O   TYR A  33      -8.358  -1.562 -18.572  1.00 86.14           O  
ATOM    188  CB  TYR A  33      -9.236  -3.110 -16.229  1.00 79.98           C  
ATOM    189  CG  TYR A  33      -8.049  -3.116 -15.285  1.00 74.29           C  
ATOM    190  CD1 TYR A  33      -6.954  -2.282 -15.498  1.00 71.66           C  
ATOM    191  CD2 TYR A  33      -8.043  -3.925 -14.152  1.00 70.99           C  
ATOM    192  CE1 TYR A  33      -5.875  -2.277 -14.627  1.00 68.38           C  
ATOM    193  CE2 TYR A  33      -6.970  -3.924 -13.273  1.00 67.38           C  
ATOM    194  CZ  TYR A  33      -5.890  -3.099 -13.517  1.00 65.49           C  
ATOM    195  OH  TYR A  33      -4.819  -3.092 -12.650  1.00 60.20           O  
ATOM    196  N   GLY A  34      -7.027  -3.331 -18.998  1.00 87.06           N  
ATOM    197  CA  GLY A  34      -6.079  -2.584 -19.804  1.00 89.12           C  
ATOM    198  C   GLY A  34      -5.899  -3.174 -21.192  1.00 94.01           C  
ATOM    199  O   GLY A  34      -6.736  -2.971 -22.068  1.00 95.99           O  
ATOM    200  N   LYS A  35      -4.807  -3.908 -21.396  1.00 96.11           N  
ATOM    201  CA  LYS A  35      -4.506  -4.475 -22.707  1.00101.97           C  
ATOM    202  C   LYS A  35      -5.440  -5.640 -23.039  1.00110.32           C  
ATOM    203  O   LYS A  35      -6.337  -5.504 -23.868  1.00114.78           O  
ATOM    204  CB  LYS A  35      -3.044  -4.928 -22.776  1.00 98.18           C  
ATOM    205  CG  LYS A  35      -2.047  -3.883 -22.286  1.00 92.35           C  
ATOM    206  CD  LYS A  35      -0.620  -4.244 -22.667  1.00 90.81           C  
ATOM    207  CE  LYS A  35       0.393  -3.313 -22.013  1.00 86.24           C  
ATOM    208  NZ  LYS A  35       0.060  -1.877 -22.198  1.00 84.20           N  
ATOM    209  N   HIS A  36      -5.239  -6.777 -22.379  1.00113.86           N  
ATOM    210  CA  HIS A  36      -6.035  -7.974 -22.645  1.00119.13           C  
ATOM    211  C   HIS A  36      -7.456  -7.888 -22.068  1.00119.20           C  
ATOM    212  O   HIS A  36      -7.859  -8.750 -21.284  1.00124.54           O  
ATOM    213  CB  HIS A  36      -5.332  -9.219 -22.082  1.00119.79           C  
ATOM    214  CG  HIS A  36      -3.986  -9.493 -22.684  1.00125.89           C  
ATOM    215  ND1 HIS A  36      -3.827 -10.024 -23.947  1.00129.82           N  
ATOM    216  CD2 HIS A  36      -2.737  -9.333 -22.184  1.00123.24           C  
ATOM    217  CE1 HIS A  36      -2.540 -10.167 -24.203  1.00129.85           C  
ATOM    218  NE2 HIS A  36      -1.857  -9.756 -23.150  1.00125.56           N  
ATOM    219  N   THR A  37      -8.212  -6.862 -22.455  1.00120.74           N  
ATOM    220  CA  THR A  37      -9.583  -6.690 -21.969  1.00120.94           C  
ATOM    221  C   THR A  37     -10.607  -6.778 -23.091  1.00122.98           C  
ATOM    222  O   THR A  37     -11.802  -6.935 -22.844  1.00125.73           O  
ATOM    223  CB  THR A  37      -9.779  -5.339 -21.262  1.00119.74           C  
ATOM    224  OG1 THR A  37     -11.092  -5.286 -20.691  1.00120.38           O  
ATOM    225  CG2 THR A  37      -9.625  -4.196 -22.251  1.00 79.36           C  
ATOM    226  N   GLU A  38     -10.130  -6.663 -24.324  1.00120.57           N  
ATOM    227  CA  GLU A  38     -10.999  -6.692 -25.488  1.00123.72           C  
ATOM    228  C   GLU A  38     -11.426  -8.120 -25.804  1.00125.19           C  
ATOM    229  O   GLU A  38     -12.247  -8.703 -25.095  1.00123.76           O  
ATOM    230  CB  GLU A  38     -10.294  -6.059 -26.689  1.00127.44           C  
ATOM    231  CG  GLU A  38      -9.876  -4.610 -26.458  1.00126.93           C  
ATOM    232  CD  GLU A  38      -9.047  -4.034 -27.598  1.00133.17           C  
ATOM    233  OE1 GLU A  38      -8.382  -4.812 -28.311  1.00138.53           O  
ATOM    234  OE2 GLU A  38      -9.057  -2.799 -27.782  1.00132.62           O  
ATOM    235  N   ALA A  44     -21.475   0.095 -23.217  1.00102.44           N  
ATOM    236  CA  ALA A  44     -22.162   0.923 -22.232  1.00101.20           C  
ATOM    237  C   ALA A  44     -21.867   0.454 -20.809  1.00105.62           C  
ATOM    238  O   ALA A  44     -22.256   1.107 -19.840  1.00104.23           O  
ATOM    239  CB  ALA A  44     -23.659   0.918 -22.492  1.00106.31           C  
ATOM    240  N   THR A  45     -21.171  -0.674 -20.687  1.00104.12           N  
ATOM    241  CA  THR A  45     -20.833  -1.241 -19.381  1.00 98.46           C  
ATOM    242  C   THR A  45     -19.533  -0.675 -18.816  1.00 91.03           C  
ATOM    243  O   THR A  45     -18.910  -1.284 -17.947  1.00 83.67           O  
ATOM    244  CB  THR A  45     -20.696  -2.778 -19.446  1.00 92.72           C  
ATOM    245  OG1 THR A  45     -19.663  -3.128 -20.376  1.00 92.45           O  
ATOM    246  CG2 THR A  45     -22.000  -3.420 -19.881  1.00 98.90           C  
ATOM    247  N   ARG A  46     -19.125   0.487 -19.314  1.00 89.21           N  
ATOM    248  CA  ARG A  46     -17.867   1.103 -18.902  1.00 83.37           C  
ATOM    249  C   ARG A  46     -18.039   2.583 -18.574  1.00 81.32           C  
ATOM    250  O   ARG A  46     -19.033   3.204 -18.954  1.00 87.64           O  
ATOM    251  CB  ARG A  46     -16.807   0.939 -19.995  1.00 82.17           C  
ATOM    252  CG  ARG A  46     -16.271  -0.478 -20.157  1.00 84.01           C  
ATOM    253  CD  ARG A  46     -15.466  -0.606 -21.442  1.00 85.81           C  
ATOM    254  NE  ARG A  46     -14.171  -1.245 -21.227  1.00 81.14           N  
ATOM    255  CZ  ARG A  46     -13.936  -2.541 -21.405  1.00 85.17           C  
ATOM    256  NH1 ARG A  46     -14.910  -3.347 -21.802  1.00 89.71           N  
ATOM    257  NH2 ARG A  46     -12.723  -3.029 -21.188  1.00 83.46           N  
ATOM    258  N   LEU A  47     -17.062   3.141 -17.866  1.00 77.57           N  
ATOM    259  CA  LEU A  47     -17.066   4.561 -17.530  1.00 81.25           C  
ATOM    260  C   LEU A  47     -15.641   5.116 -17.604  1.00 73.93           C  
ATOM    261  O   LEU A  47     -14.684   4.345 -17.528  1.00 71.91           O  
ATOM    262  CB  LEU A  47     -17.683   4.772 -16.141  1.00 80.74           C  
ATOM    263  CG  LEU A  47     -17.080   4.031 -14.948  1.00 76.56           C  
ATOM    264  CD1 LEU A  47     -16.035   4.885 -14.253  1.00 73.81           C  
ATOM    265  CD2 LEU A  47     -18.177   3.623 -13.980  1.00 74.03           C  
ATOM    266  N   PRO A  48     -15.495   6.446 -17.772  1.00 74.06           N  
ATOM    267  CA  PRO A  48     -14.186   7.106 -17.890  1.00 71.92           C  
ATOM    268  C   PRO A  48     -13.168   6.636 -16.851  1.00 76.66           C  
ATOM    269  O   PRO A  48     -13.490   6.547 -15.665  1.00 76.58           O  
ATOM    270  CB  PRO A  48     -14.528   8.579 -17.686  1.00 72.55           C  
ATOM    271  CG  PRO A  48     -15.892   8.705 -18.226  1.00 76.10           C  
ATOM    272  CD  PRO A  48     -16.597   7.415 -17.911  1.00 76.70           C  
ATOM    273  N   ALA A  49     -11.955   6.334 -17.302  1.00 55.31           N  
ATOM    274  CA  ALA A  49     -10.934   5.746 -16.440  1.00 52.37           C  
ATOM    275  C   ALA A  49     -10.455   6.709 -15.357  1.00 51.80           C  
ATOM    276  O   ALA A  49     -10.027   6.277 -14.284  1.00 46.63           O  
ATOM    277  CB  ALA A  49      -9.759   5.270 -17.273  1.00 44.76           C  
ATOM    278  N   ARG A  50     -10.523   8.008 -15.638  1.00 53.96           N  
ATOM    279  CA  ARG A  50     -10.138   9.020 -14.660  1.00 53.52           C  
ATOM    280  C   ARG A  50     -11.055   8.960 -13.440  1.00 55.92           C  
ATOM    281  O   ARG A  50     -10.594   9.057 -12.302  1.00 54.88           O  
ATOM    282  CB  ARG A  50     -10.164  10.423 -15.282  1.00 56.67           C  
ATOM    283  CG  ARG A  50      -9.040  10.689 -16.281  1.00 58.61           C  
ATOM    284  CD  ARG A  50      -8.929  12.169 -16.649  1.00 65.43           C  
ATOM    285  NE  ARG A  50      -9.738  12.545 -17.809  1.00 72.14           N  
ATOM    286  CZ  ARG A  50     -10.908  13.173 -17.739  1.00 79.74           C  
ATOM    287  NH1 ARG A  50     -11.421  13.506 -16.561  1.00 82.84           N  
ATOM    288  NH2 ARG A  50     -11.569  13.474 -18.849  1.00 82.87           N  
ATOM    289  N   ALA A  51     -12.350   8.788 -13.684  1.00 60.72           N  
ATOM    290  CA  ALA A  51     -13.324   8.664 -12.606  1.00 66.21           C  
ATOM    291  C   ALA A  51     -13.226   7.299 -11.940  1.00 68.83           C  
ATOM    292  O   ALA A  51     -13.465   7.163 -10.742  1.00 72.63           O  
ATOM    293  CB  ALA A  51     -14.726   8.895 -13.131  1.00 69.34           C  
ATOM    294  N   ALA A  52     -12.864   6.293 -12.729  1.00 69.60           N  
ATOM    295  CA  ALA A  52     -12.777   4.918 -12.249  1.00 69.45           C  
ATOM    296  C   ALA A  52     -11.676   4.743 -11.214  1.00 71.48           C  
ATOM    297  O   ALA A  52     -11.917   4.248 -10.115  1.00 77.17           O  
ATOM    298  CB  ALA A  52     -12.551   3.974 -13.408  1.00 67.09           C  
ATOM    299  N   TRP A  53     -10.465   5.148 -11.570  1.00 68.78           N  
ATOM    300  CA  TRP A  53      -9.340   5.012 -10.663  1.00 66.64           C  
ATOM    301  C   TRP A  53      -9.435   6.008  -9.518  1.00 65.57           C  
ATOM    302  O   TRP A  53      -8.883   5.773  -8.444  1.00 63.31           O  
ATOM    303  CB  TRP A  53      -8.024   5.169 -11.424  1.00 66.73           C  
ATOM    304  CG  TRP A  53      -7.695   3.927 -12.185  1.00 68.12           C  
ATOM    305  CD1 TRP A  53      -8.135   3.587 -13.432  1.00 69.46           C  
ATOM    306  CD2 TRP A  53      -6.889   2.832 -11.732  1.00 68.71           C  
ATOM    307  NE1 TRP A  53      -7.639   2.356 -13.791  1.00 68.43           N  
ATOM    308  CE2 TRP A  53      -6.871   1.872 -12.763  1.00 68.52           C  
ATOM    309  CE3 TRP A  53      -6.173   2.576 -10.559  1.00 69.46           C  
ATOM    310  CZ2 TRP A  53      -6.166   0.675 -12.656  1.00 69.64           C  
ATOM    311  CZ3 TRP A  53      -5.475   1.389 -10.455  1.00 69.90           C  
ATOM    312  CH2 TRP A  53      -5.475   0.454 -11.497  1.00 71.11           C  
ATOM    313  N   PHE A  54     -10.151   7.108  -9.735  1.00 66.92           N  
ATOM    314  CA  PHE A  54     -10.401   8.053  -8.654  1.00 68.59           C  
ATOM    315  C   PHE A  54     -11.215   7.376  -7.556  1.00 67.46           C  
ATOM    316  O   PHE A  54     -10.815   7.368  -6.396  1.00 68.31           O  
ATOM    317  CB  PHE A  54     -11.124   9.303  -9.166  1.00 72.69           C  
ATOM    318  CG  PHE A  54     -11.456  10.299  -8.084  1.00 75.10           C  
ATOM    319  CD1 PHE A  54     -10.491  11.170  -7.602  1.00 76.30           C  
ATOM    320  CD2 PHE A  54     -12.734  10.366  -7.555  1.00 76.11           C  
ATOM    321  CE1 PHE A  54     -10.795  12.084  -6.607  1.00 77.20           C  
ATOM    322  CE2 PHE A  54     -13.046  11.277  -6.562  1.00 77.84           C  
ATOM    323  CZ  PHE A  54     -12.078  12.136  -6.087  1.00 78.70           C  
ATOM    324  N   LEU A  55     -12.349   6.793  -7.936  1.00 66.17           N  
ATOM    325  CA  LEU A  55     -13.233   6.122  -6.987  1.00 66.35           C  
ATOM    326  C   LEU A  55     -12.598   4.886  -6.351  1.00 67.19           C  
ATOM    327  O   LEU A  55     -12.801   4.613  -5.168  1.00 66.69           O  
ATOM    328  CB  LEU A  55     -14.541   5.725  -7.676  1.00 64.78           C  
ATOM    329  CG  LEU A  55     -15.460   6.869  -8.103  1.00 64.94           C  
ATOM    330  CD1 LEU A  55     -16.683   6.328  -8.823  1.00 65.41           C  
ATOM    331  CD2 LEU A  55     -15.874   7.705  -6.902  1.00 66.71           C  
ATOM    332  N   GLN A  56     -11.835   4.138  -7.138  1.00 68.46           N  
ATOM    333  CA  GLN A  56     -11.222   2.908  -6.651  1.00 69.33           C  
ATOM    334  C   GLN A  56     -10.157   3.152  -5.591  1.00 69.55           C  
ATOM    335  O   GLN A  56     -10.142   2.490  -4.554  1.00 69.58           O  
ATOM    336  CB  GLN A  56     -10.602   2.133  -7.807  1.00 70.20           C  
ATOM    337  CG  GLN A  56     -11.562   1.243  -8.540  1.00 73.67           C  
ATOM    338  CD  GLN A  56     -10.876   0.458  -9.629  1.00 75.54           C  
ATOM    339  OE1 GLN A  56     -11.338  -0.610 -10.029  1.00 79.68           O  
ATOM    340  NE2 GLN A  56      -9.757   0.981 -10.115  1.00 73.45           N  
ATOM    341  N   GLU A  57      -9.260   4.093  -5.862  1.00 70.20           N  
ATOM    342  CA  GLU A  57      -8.107   4.306  -4.999  1.00 71.20           C  
ATOM    343  C   GLU A  57      -8.390   5.290  -3.866  1.00 74.06           C  
ATOM    344  O   GLU A  57      -7.608   5.385  -2.923  1.00 79.49           O  
ATOM    345  CB  GLU A  57      -6.912   4.796  -5.821  1.00 72.02           C  
ATOM    346  CG  GLU A  57      -6.655   3.993  -7.087  1.00 73.18           C  
ATOM    347  CD  GLU A  57      -6.347   2.537  -6.809  1.00 71.81           C  
ATOM    348  OE1 GLU A  57      -5.213   2.245  -6.369  1.00 69.43           O  
ATOM    349  OE2 GLU A  57      -7.235   1.687  -7.039  1.00 73.24           O  
ATOM    350  N   LEU A  58      -9.506   6.011  -3.954  1.00 71.82           N  
ATOM    351  CA  LEU A  58      -9.856   7.015  -2.942  1.00 71.16           C  
ATOM    352  C   LEU A  58      -9.931   6.473  -1.503  1.00 71.45           C  
ATOM    353  O   LEU A  58      -9.471   7.150  -0.582  1.00 70.61           O  
ATOM    354  CB  LEU A  58     -11.183   7.697  -3.299  1.00 70.92           C  
ATOM    355  CG  LEU A  58     -11.645   8.828  -2.370  1.00 71.51           C  
ATOM    356  CD1 LEU A  58     -10.711  10.028  -2.453  1.00 71.46           C  
ATOM    357  CD2 LEU A  58     -13.081   9.243  -2.669  1.00 72.95           C  
ATOM    358  N   PRO A  59     -10.516   5.271  -1.292  1.00 71.74           N  
ATOM    359  CA  PRO A  59     -10.568   4.768   0.089  1.00 76.32           C  
ATOM    360  C   PRO A  59      -9.202   4.580   0.756  1.00 78.64           C  
ATOM    361  O   PRO A  59      -9.084   4.803   1.961  1.00 80.49           O  
ATOM    362  CB  PRO A  59     -11.273   3.418  -0.063  1.00 72.74           C  
ATOM    363  CG  PRO A  59     -12.144   3.599  -1.240  1.00 71.58           C  
ATOM    364  CD  PRO A  59     -11.343   4.439  -2.189  1.00 69.99           C  
ATOM    365  N   SER A  60      -8.190   4.182  -0.010  1.00 81.34           N  
ATOM    366  CA  SER A  60      -6.852   3.976   0.543  1.00 74.18           C  
ATOM    367  C   SER A  60      -6.175   5.294   0.903  1.00 71.89           C  
ATOM    368  O   SER A  60      -5.080   5.306   1.467  1.00 71.53           O  
ATOM    369  CB  SER A  60      -5.975   3.192  -0.437  1.00 69.57           C  
ATOM    370  OG  SER A  60      -6.132   1.794  -0.266  1.00 67.54           O  
ATOM    371  N   PHE A  61      -6.822   6.404   0.569  1.00 69.91           N  
ATOM    372  CA  PHE A  61      -6.350   7.704   1.017  1.00 70.37           C  
ATOM    373  C   PHE A  61      -7.213   8.245   2.161  1.00 71.96           C  
ATOM    374  O   PHE A  61      -6.691   8.619   3.209  1.00 73.47           O  
ATOM    375  CB  PHE A  61      -6.326   8.713  -0.133  1.00 68.11           C  
ATOM    376  CG  PHE A  61      -6.248  10.143   0.329  1.00 69.52           C  
ATOM    377  CD1 PHE A  61      -5.038  10.696   0.712  1.00 70.13           C  
ATOM    378  CD2 PHE A  61      -7.388  10.928   0.398  1.00 70.16           C  
ATOM    379  CE1 PHE A  61      -4.963  12.003   1.150  1.00 72.13           C  
ATOM    380  CE2 PHE A  61      -7.319  12.232   0.836  1.00 72.91           C  
ATOM    381  CZ  PHE A  61      -6.106  12.773   1.212  1.00 73.91           C  
ATOM    382  N   ALA A  62      -8.527   8.289   1.952  1.00 72.14           N  
ATOM    383  CA  ALA A  62      -9.439   8.920   2.901  1.00 74.99           C  
ATOM    384  C   ALA A  62      -9.429   8.237   4.264  1.00 75.87           C  
ATOM    385  O   ALA A  62      -9.426   8.910   5.301  1.00 77.85           O  
ATOM    386  CB  ALA A  62     -10.851   8.937   2.339  1.00 75.15           C  
ATOM    387  N   VAL A  63      -9.430   6.906   4.263  1.00 73.14           N  
ATOM    388  CA  VAL A  63      -9.465   6.159   5.515  1.00 75.33           C  
ATOM    389  C   VAL A  63      -8.199   6.405   6.356  1.00 75.08           C  
ATOM    390  O   VAL A  63      -8.314   6.747   7.532  1.00 77.67           O  
ATOM    391  CB  VAL A  63      -9.677   4.646   5.263  1.00 72.66           C  
ATOM    392  CG1 VAL A  63      -9.322   3.833   6.502  1.00 73.47           C  
ATOM    393  CG2 VAL A  63     -11.116   4.380   4.830  1.00 73.21           C  
ATOM    394  N   PRO A  64      -6.993   6.261   5.768  1.00 75.29           N  
ATOM    395  CA  PRO A  64      -5.836   6.626   6.597  1.00 75.94           C  
ATOM    396  C   PRO A  64      -5.781   8.119   6.919  1.00 80.93           C  
ATOM    397  O   PRO A  64      -5.244   8.495   7.958  1.00 86.94           O  
ATOM    398  CB  PRO A  64      -4.635   6.220   5.731  1.00 73.32           C  
ATOM    399  CG  PRO A  64      -5.177   5.228   4.764  1.00 71.28           C  
ATOM    400  CD  PRO A  64      -6.569   5.684   4.480  1.00 71.97           C  
ATOM    401  N   ALA A  65      -6.325   8.954   6.040  1.00 79.01           N  
ATOM    402  CA  ALA A  65      -6.354  10.392   6.276  1.00 81.06           C  
ATOM    403  C   ALA A  65      -7.264  10.724   7.456  1.00 82.14           C  
ATOM    404  O   ALA A  65      -6.990  11.642   8.229  1.00 84.61           O  
ATOM    405  CB  ALA A  65      -6.812  11.132   5.027  1.00 59.70           C  
ATOM    406  N   GLY A  66      -8.348   9.970   7.589  1.00 79.07           N  
ATOM    407  CA  GLY A  66      -9.274  10.160   8.687  1.00 78.33           C  
ATOM    408  C   GLY A  66      -8.690   9.659   9.992  1.00 78.08           C  
ATOM    409  O   GLY A  66      -8.858  10.282  11.040  1.00 81.61           O  
ATOM    410  N   ILE A  67      -8.001   8.524   9.923  1.00 75.38           N  
ATOM    411  CA  ILE A  67      -7.348   7.942  11.088  1.00 75.61           C  
ATOM    412  C   ILE A  67      -6.262   8.880  11.617  1.00 80.77           C  
ATOM    413  O   ILE A  67      -6.139   9.086  12.827  1.00 87.05           O  
ATOM    414  CB  ILE A  67      -6.744   6.564  10.751  1.00 70.46           C  
ATOM    415  CG1 ILE A  67      -7.856   5.581  10.381  1.00 67.43           C  
ATOM    416  CG2 ILE A  67      -5.933   6.025  11.922  1.00 70.13           C  
ATOM    417  CD1 ILE A  67      -7.361   4.260   9.830  1.00 63.66           C  
ATOM    418  N   LEU A  68      -5.492   9.465  10.703  1.00 78.70           N  
ATOM    419  CA  LEU A  68      -4.457  10.429  11.065  1.00 81.24           C  
ATOM    420  C   LEU A  68      -5.035  11.684  11.713  1.00 84.62           C  
ATOM    421  O   LEU A  68      -4.425  12.267  12.612  1.00 87.24           O  
ATOM    422  CB  LEU A  68      -3.640  10.825   9.833  1.00 78.80           C  
ATOM    423  CG  LEU A  68      -2.568   9.847   9.356  1.00 76.98           C  
ATOM    424  CD1 LEU A  68      -1.931  10.352   8.070  1.00 62.17           C  
ATOM    425  CD2 LEU A  68      -1.516   9.648  10.437  1.00 65.59           C  
ATOM    426  N   ALA A  69      -6.215  12.092  11.254  1.00 85.33           N  
ATOM    427  CA  ALA A  69      -6.824  13.349  11.679  1.00 89.91           C  
ATOM    428  C   ALA A  69      -7.244  13.349  13.150  1.00 94.63           C  
ATOM    429  O   ALA A  69      -7.605  14.394  13.694  1.00 97.65           O  
ATOM    430  CB  ALA A  69      -8.021  13.668  10.794  1.00 88.57           C  
ATOM    431  N   ARG A  70      -7.200  12.183  13.788  1.00 95.14           N  
ATOM    432  CA  ARG A  70      -7.564  12.069  15.197  1.00100.43           C  
ATOM    433  C   ARG A  70      -6.328  11.977  16.093  1.00106.33           C  
ATOM    434  O   ARG A  70      -6.441  11.877  17.317  1.00111.29           O  
ATOM    435  CB  ARG A  70      -8.470  10.855  15.417  1.00 97.75           C  
ATOM    436  N   GLN A  71      -5.149  12.020  15.475  1.00107.60           N  
ATOM    437  CA  GLN A  71      -3.877  11.940  16.189  1.00113.47           C  
ATOM    438  C   GLN A  71      -3.238  13.322  16.351  1.00120.71           C  
ATOM    439  O   GLN A  71      -3.460  14.207  15.524  1.00121.79           O  
ATOM    440  CB  GLN A  71      -2.917  10.997  15.453  1.00110.21           C  
ATOM    441  CG  GLN A  71      -2.738   9.644  16.117  1.00110.21           C  
ATOM    442  CD  GLN A  71      -4.049   8.916  16.327  1.00111.26           C  
ATOM    443  OE1 GLN A  71      -4.282   8.338  17.389  1.00114.76           O  
ATOM    444  NE2 GLN A  71      -4.910   8.934  15.316  1.00108.81           N  
ATOM    445  N   PRO A  72      -2.440  13.512  17.418  1.00127.58           N  
ATOM    446  CA  PRO A  72      -1.768  14.796  17.649  1.00132.76           C  
ATOM    447  C   PRO A  72      -0.816  15.173  16.518  1.00131.68           C  
ATOM    448  O   PRO A  72      -0.248  14.296  15.868  1.00128.69           O  
ATOM    449  CB  PRO A  72      -0.995  14.562  18.953  1.00136.76           C  
ATOM    450  CG  PRO A  72      -0.848  13.080  19.050  1.00133.63           C  
ATOM    451  CD  PRO A  72      -2.112  12.529  18.466  1.00129.56           C  
ATOM    452  N   LEU A  73      -0.647  16.471  16.291  1.00135.74           N  
ATOM    453  CA  LEU A  73       0.232  16.945  15.231  1.00137.43           C  
ATOM    454  C   LEU A  73       1.636  17.216  15.763  1.00144.25           C  
ATOM    455  O   LEU A  73       1.934  18.316  16.228  1.00147.90           O  
ATOM    456  CB  LEU A  73      -0.341  18.208  14.584  1.00138.61           C  
ATOM    457  N   SER A  74       2.490  16.199  15.697  1.00143.13           N  
ATOM    458  CA  SER A  74       3.891  16.335  16.082  1.00146.51           C  
ATOM    459  C   SER A  74       4.752  15.285  15.384  1.00143.72           C  
ATOM    460  O   SER A  74       4.550  14.084  15.565  1.00142.36           O  
ATOM    461  CB  SER A  74       4.053  16.223  17.601  1.00150.51           C  
ATOM    462  OG  SER A  74       3.663  14.944  18.067  1.00148.77           O  
ATOM    463  N   LEU A  75       5.707  15.745  14.583  1.00143.17           N  
ATOM    464  CA  LEU A  75       6.642  14.848  13.912  1.00139.40           C  
ATOM    465  C   LEU A  75       7.587  14.217  14.929  1.00146.17           C  
ATOM    466  O   LEU A  75       8.219  13.194  14.654  1.00137.20           O  
ATOM    467  CB  LEU A  75       7.436  15.596  12.838  1.00137.00           C  
ATOM    468  N   PHE A  76       7.675  14.833  16.105  1.00162.12           N  
ATOM    469  CA  PHE A  76       8.451  14.290  17.215  1.00177.09           C  
ATOM    470  C   PHE A  76       7.638  13.250  17.981  1.00177.15           C  
ATOM    471  O   PHE A  76       7.631  13.239  19.211  1.00188.80           O  
ATOM    472  CB  PHE A  76       8.899  15.409  18.158  1.00188.71           C  
ATOM    473  N   GLY A  77       6.956  12.379  17.241  1.00160.78           N  
ATOM    474  CA  GLY A  77       6.106  11.361  17.834  1.00157.60           C  
ATOM    475  C   GLY A  77       6.369   9.974  17.279  1.00152.47           C  
ATOM    476  O   GLY A  77       7.412   9.738  16.668  1.00151.72           O  
ATOM    477  N   PRO A  78       5.416   9.051  17.484  1.00141.91           N  
ATOM    478  CA  PRO A  78       5.540   7.630  17.129  1.00131.29           C  
ATOM    479  C   PRO A  78       5.894   7.393  15.663  1.00116.18           C  
ATOM    480  O   PRO A  78       5.401   8.104  14.788  1.00113.14           O  
ATOM    481  CB  PRO A  78       4.148   7.071  17.440  1.00133.52           C  
ATOM    482  CG  PRO A  78       3.598   7.983  18.468  1.00139.94           C  
ATOM    483  CD  PRO A  78       4.113   9.344  18.104  1.00142.75           C  
ATOM    484  N   PRO A  79       6.749   6.393  15.401  1.00106.52           N  
ATOM    485  CA  PRO A  79       7.166   6.032  14.043  1.00 98.26           C  
ATOM    486  C   PRO A  79       6.017   5.462  13.220  1.00 90.30           C  
ATOM    487  O   PRO A  79       6.000   5.623  12.001  1.00 87.71           O  
ATOM    488  CB  PRO A  79       8.246   4.967  14.277  1.00 98.96           C  
ATOM    489  CG  PRO A  79       8.677   5.153  15.700  1.00103.40           C  
ATOM    490  CD  PRO A  79       7.447   5.594  16.420  1.00106.00           C  
ATOM    491  N   GLY A  80       5.071   4.805  13.884  1.00 87.94           N  
ATOM    492  CA  GLY A  80       3.957   4.173  13.198  1.00 83.44           C  
ATOM    493  C   GLY A  80       3.013   5.168  12.551  1.00 83.33           C  
ATOM    494  O   GLY A  80       2.343   4.860  11.564  1.00 83.18           O  
ATOM    495  N   THR A  81       2.962   6.368  13.115  1.00 85.63           N  
ATOM    496  CA  THR A  81       2.107   7.425  12.596  1.00 85.30           C  
ATOM    497  C   THR A  81       2.713   8.049  11.344  1.00 83.01           C  
ATOM    498  O   THR A  81       2.038   8.195  10.322  1.00 79.89           O  
ATOM    499  CB  THR A  81       1.879   8.518  13.649  1.00 88.87           C  
ATOM    500  OG1 THR A  81       3.127   9.150  13.952  1.00 92.79           O  
ATOM    501  CG2 THR A  81       1.308   7.909  14.918  1.00 90.94           C  
ATOM    502  N   VAL A  82       3.989   8.416  11.436  1.00 84.41           N  
ATOM    503  CA  VAL A  82       4.712   9.000  10.312  1.00 83.48           C  
ATOM    504  C   VAL A  82       4.699   8.059   9.112  1.00 81.83           C  
ATOM    505  O   VAL A  82       4.571   8.497   7.968  1.00 79.39           O  
ATOM    506  CB  VAL A  82       6.172   9.327  10.681  1.00 84.64           C  
ATOM    507  CG1 VAL A  82       6.845  10.101   9.559  1.00 82.59           C  
ATOM    508  CG2 VAL A  82       6.232  10.116  11.984  1.00 89.31           C  
ATOM    509  N   LEU A  83       4.820   6.764   9.379  1.00 82.84           N  
ATOM    510  CA  LEU A  83       4.777   5.766   8.320  1.00 81.23           C  
ATOM    511  C   LEU A  83       3.388   5.696   7.699  1.00 80.49           C  
ATOM    512  O   LEU A  83       3.250   5.498   6.494  1.00 84.01           O  
ATOM    513  CB  LEU A  83       5.197   4.395   8.853  1.00 82.62           C  
ATOM    514  CG  LEU A  83       6.691   4.240   9.151  1.00 86.06           C  
ATOM    515  CD1 LEU A  83       6.964   2.949   9.901  1.00 88.82           C  
ATOM    516  CD2 LEU A  83       7.509   4.302   7.868  1.00 82.91           C  
ATOM    517  N   LEU A  84       2.357   5.866   8.521  1.00 78.26           N  
ATOM    518  CA  LEU A  84       0.991   5.882   8.013  1.00 75.49           C  
ATOM    519  C   LEU A  84       0.773   7.120   7.151  1.00 72.73           C  
ATOM    520  O   LEU A  84      -0.017   7.105   6.211  1.00 70.98           O  
ATOM    521  CB  LEU A  84      -0.021   5.840   9.158  1.00 78.46           C  
ATOM    522  CG  LEU A  84      -1.493   5.778   8.745  1.00 78.30           C  
ATOM    523  CD1 LEU A  84      -1.729   4.645   7.757  1.00 76.16           C  
ATOM    524  CD2 LEU A  84      -2.379   5.613   9.967  1.00 80.23           C  
ATOM    525  N   GLY A  85       1.492   8.187   7.474  1.00 74.04           N  
ATOM    526  CA  GLY A  85       1.460   9.399   6.680  1.00 72.53           C  
ATOM    527  C   GLY A  85       2.029   9.177   5.293  1.00 68.68           C  
ATOM    528  O   GLY A  85       1.524   9.718   4.315  1.00 67.08           O  
ATOM    529  N   LEU A  86       3.085   8.374   5.207  1.00 68.74           N  
ATOM    530  CA  LEU A  86       3.687   8.041   3.921  1.00 68.14           C  
ATOM    531  C   LEU A  86       2.731   7.194   3.085  1.00 66.33           C  
ATOM    532  O   LEU A  86       2.677   7.324   1.862  1.00 64.03           O  
ATOM    533  CB  LEU A  86       5.014   7.309   4.120  1.00 68.07           C  
ATOM    534  CG  LEU A  86       6.110   8.139   4.788  1.00 73.08           C  
ATOM    535  CD1 LEU A  86       7.343   7.292   5.055  1.00 75.08           C  
ATOM    536  CD2 LEU A  86       6.460   9.350   3.936  1.00 73.78           C  
ATOM    537  N   PHE A  87       1.977   6.329   3.755  1.00 67.31           N  
ATOM    538  CA  PHE A  87       0.945   5.543   3.093  1.00 68.58           C  
ATOM    539  C   PHE A  87      -0.101   6.487   2.514  1.00 68.33           C  
ATOM    540  O   PHE A  87      -0.596   6.289   1.403  1.00 64.52           O  
ATOM    541  CB  PHE A  87       0.302   4.558   4.074  1.00 72.06           C  
ATOM    542  CG  PHE A  87      -0.577   3.524   3.421  1.00 73.13           C  
ATOM    543  CD1 PHE A  87      -0.065   2.286   3.068  1.00 73.82           C  
ATOM    544  CD2 PHE A  87      -1.916   3.785   3.171  1.00 74.57           C  
ATOM    545  CE1 PHE A  87      -0.871   1.327   2.471  1.00 74.58           C  
ATOM    546  CE2 PHE A  87      -2.727   2.831   2.574  1.00 74.09           C  
ATOM    547  CZ  PHE A  87      -2.204   1.601   2.225  1.00 73.09           C  
ATOM    548  N   CYS A  88      -0.417   7.523   3.286  1.00 70.71           N  
ATOM    549  CA  CYS A  88      -1.394   8.522   2.886  1.00 70.35           C  
ATOM    550  C   CYS A  88      -0.844   9.397   1.757  1.00 72.01           C  
ATOM    551  O   CYS A  88      -1.581   9.796   0.857  1.00 72.48           O  
ATOM    552  CB  CYS A  88      -1.792   9.375   4.093  1.00 72.71           C  
ATOM    553  SG  CYS A  88      -3.350  10.277   3.924  1.00 90.10           S  
ATOM    554  N   VAL A  89       0.455   9.684   1.804  1.00 74.27           N  
ATOM    555  CA  VAL A  89       1.105  10.490   0.771  1.00 76.01           C  
ATOM    556  C   VAL A  89       1.097   9.779  -0.584  1.00 74.72           C  
ATOM    557  O   VAL A  89       0.819  10.399  -1.613  1.00 76.08           O  
ATOM    558  CB  VAL A  89       2.564  10.844   1.159  1.00 78.13           C  
ATOM    559  CG1 VAL A  89       3.350  11.322  -0.055  1.00 77.78           C  
ATOM    560  CG2 VAL A  89       2.585  11.898   2.256  1.00 80.92           C  
ATOM    561  N   HIS A  90       1.394   8.481  -0.582  1.00 74.55           N  
ATOM    562  CA  HIS A  90       1.356   7.687  -1.808  1.00 75.87           C  
ATOM    563  C   HIS A  90      -0.020   7.734  -2.468  1.00 75.99           C  
ATOM    564  O   HIS A  90      -0.141   8.056  -3.652  1.00 79.22           O  
ATOM    565  CB  HIS A  90       1.741   6.228  -1.528  1.00 78.35           C  
ATOM    566  CG  HIS A  90       1.466   5.294  -2.672  1.00 80.12           C  
ATOM    567  ND1 HIS A  90       2.349   5.111  -3.716  1.00 81.19           N  
ATOM    568  CD2 HIS A  90       0.407   4.490  -2.933  1.00 79.44           C  
ATOM    569  CE1 HIS A  90       1.846   4.237  -4.570  1.00 78.94           C  
ATOM    570  NE2 HIS A  90       0.668   3.844  -4.118  1.00 78.69           N  
ATOM    571  N   TYR A  91      -1.056   7.418  -1.698  1.00 73.57           N  
ATOM    572  CA  TYR A  91      -2.398   7.299  -2.258  1.00 71.68           C  
ATOM    573  C   TYR A  91      -3.047   8.657  -2.500  1.00 68.59           C  
ATOM    574  O   TYR A  91      -4.113   8.748  -3.110  1.00 67.18           O  
ATOM    575  CB  TYR A  91      -3.278   6.438  -1.352  1.00 74.09           C  
ATOM    576  CG  TYR A  91      -3.128   4.949  -1.603  1.00 75.93           C  
ATOM    577  CD1 TYR A  91      -3.658   4.358  -2.748  1.00 77.12           C  
ATOM    578  CD2 TYR A  91      -2.461   4.137  -0.700  1.00 77.54           C  
ATOM    579  CE1 TYR A  91      -3.526   2.999  -2.983  1.00 76.41           C  
ATOM    580  CE2 TYR A  91      -2.323   2.779  -0.928  1.00 78.34           C  
ATOM    581  CZ  TYR A  91      -2.857   2.215  -2.068  1.00 78.20           C  
ATOM    582  OH  TYR A  91      -2.721   0.863  -2.296  1.00 79.84           O  
ATOM    583  N   PHE A  92      -2.398   9.716  -2.034  1.00 67.03           N  
ATOM    584  CA  PHE A  92      -2.820  11.059  -2.398  1.00 66.59           C  
ATOM    585  C   PHE A  92      -2.444  11.332  -3.846  1.00 66.21           C  
ATOM    586  O   PHE A  92      -3.234  11.877  -4.619  1.00 66.09           O  
ATOM    587  CB  PHE A  92      -2.193  12.112  -1.492  1.00 64.18           C  
ATOM    588  CG  PHE A  92      -2.424  13.508  -1.966  1.00 62.15           C  
ATOM    589  CD1 PHE A  92      -3.677  14.086  -1.849  1.00 62.36           C  
ATOM    590  CD2 PHE A  92      -1.402  14.236  -2.557  1.00 61.47           C  
ATOM    591  CE1 PHE A  92      -3.907  15.372  -2.298  1.00 63.64           C  
ATOM    592  CE2 PHE A  92      -1.623  15.524  -3.008  1.00 62.47           C  
ATOM    593  CZ  PHE A  92      -2.877  16.094  -2.879  1.00 63.58           C  
ATOM    594  N   HIS A  93      -1.219  10.958  -4.200  1.00 65.05           N  
ATOM    595  CA  HIS A  93      -0.766  11.036  -5.580  1.00 66.28           C  
ATOM    596  C   HIS A  93      -1.577  10.098  -6.481  1.00 62.06           C  
ATOM    597  O   HIS A  93      -2.024  10.494  -7.555  1.00 61.94           O  
ATOM    598  CB  HIS A  93       0.725  10.702  -5.675  1.00 68.67           C  
ATOM    599  CG  HIS A  93       1.178  10.359  -7.060  1.00 70.71           C  
ATOM    600  ND1 HIS A  93       1.497  11.316  -8.001  1.00 73.00           N  
ATOM    601  CD2 HIS A  93       1.351   9.161  -7.669  1.00 70.02           C  
ATOM    602  CE1 HIS A  93       1.852  10.722  -9.127  1.00 72.25           C  
ATOM    603  NE2 HIS A  93       1.771   9.416  -8.952  1.00 72.52           N  
ATOM    604  N   ARG A  94      -1.768   8.862  -6.032  1.00 58.48           N  
ATOM    605  CA  ARG A  94      -2.465   7.848  -6.818  1.00 60.44           C  
ATOM    606  C   ARG A  94      -3.893   8.263  -7.167  1.00 61.83           C  
ATOM    607  O   ARG A  94      -4.398   7.933  -8.240  1.00 61.79           O  
ATOM    608  CB  ARG A  94      -2.475   6.512  -6.063  1.00 61.21           C  
ATOM    609  CG  ARG A  94      -3.324   5.414  -6.702  1.00 59.09           C  
ATOM    610  CD  ARG A  94      -2.738   4.897  -8.015  1.00 56.69           C  
ATOM    611  NE  ARG A  94      -1.456   4.219  -7.829  1.00 54.77           N  
ATOM    612  CZ  ARG A  94      -0.301   4.665  -8.313  1.00 53.84           C  
ATOM    613  NH1 ARG A  94      -0.265   5.785  -9.021  1.00 52.81           N  
ATOM    614  NH2 ARG A  94       0.820   3.990  -8.096  1.00 53.87           N  
ATOM    615  N   THR A  95      -4.532   9.000  -6.266  1.00 64.13           N  
ATOM    616  CA  THR A  95      -5.929   9.388  -6.442  1.00 65.39           C  
ATOM    617  C   THR A  95      -6.089  10.722  -7.157  1.00 65.87           C  
ATOM    618  O   THR A  95      -6.745  10.810  -8.199  1.00 66.64           O  
ATOM    619  CB  THR A  95      -6.652   9.477  -5.082  1.00 69.84           C  
ATOM    620  OG1 THR A  95      -6.776   8.168  -4.517  1.00 72.93           O  
ATOM    621  CG2 THR A  95      -8.038  10.083  -5.246  1.00 70.41           C  
ATOM    622  N   PHE A  96      -5.488  11.762  -6.586  1.00 63.72           N  
ATOM    623  CA  PHE A  96      -5.714  13.124  -7.051  1.00 65.20           C  
ATOM    624  C   PHE A  96      -4.755  13.544  -8.159  1.00 65.42           C  
ATOM    625  O   PHE A  96      -5.016  14.511  -8.874  1.00 66.38           O  
ATOM    626  CB  PHE A  96      -5.609  14.101  -5.880  1.00 64.78           C  
ATOM    627  CG  PHE A  96      -6.631  13.865  -4.806  1.00 62.08           C  
ATOM    628  CD1 PHE A  96      -6.389  12.956  -3.788  1.00 59.02           C  
ATOM    629  CD2 PHE A  96      -7.835  14.550  -4.816  1.00 62.21           C  
ATOM    630  CE1 PHE A  96      -7.327  12.734  -2.799  1.00 53.73           C  
ATOM    631  CE2 PHE A  96      -8.780  14.334  -3.830  1.00 62.25           C  
ATOM    632  CZ  PHE A  96      -8.524  13.423  -2.819  1.00 55.86           C  
ATOM    633  N   VAL A  97      -3.644  12.831  -8.306  1.00 65.50           N  
ATOM    634  CA  VAL A  97      -2.690  13.187  -9.350  1.00 69.08           C  
ATOM    635  C   VAL A  97      -2.695  12.176 -10.493  1.00 68.07           C  
ATOM    636  O   VAL A  97      -2.997  12.530 -11.633  1.00 71.01           O  
ATOM    637  CB  VAL A  97      -1.261  13.322  -8.796  1.00 67.81           C  
ATOM    638  CG1 VAL A  97      -0.298  13.678  -9.920  1.00 66.06           C  
ATOM    639  CG2 VAL A  97      -1.218  14.381  -7.702  1.00 70.15           C  
ATOM    640  N   TYR A  98      -2.365  10.925 -10.190  1.00 64.03           N  
ATOM    641  CA  TYR A  98      -2.322   9.894 -11.216  1.00 61.76           C  
ATOM    642  C   TYR A  98      -3.679   9.671 -11.873  1.00 64.49           C  
ATOM    643  O   TYR A  98      -3.800   9.706 -13.096  1.00 65.19           O  
ATOM    644  CB  TYR A  98      -1.830   8.563 -10.644  1.00 56.01           C  
ATOM    645  CG  TYR A  98      -1.999   7.435 -11.635  1.00 52.45           C  
ATOM    646  CD1 TYR A  98      -1.041   7.196 -12.608  1.00 49.74           C  
ATOM    647  CD2 TYR A  98      -3.134   6.628 -11.619  1.00 51.34           C  
ATOM    648  CE1 TYR A  98      -1.196   6.177 -13.529  1.00 48.93           C  
ATOM    649  CE2 TYR A  98      -3.301   5.614 -12.538  1.00 48.87           C  
ATOM    650  CZ  TYR A  98      -2.328   5.389 -13.491  1.00 48.08           C  
ATOM    651  OH  TYR A  98      -2.488   4.375 -14.412  1.00 46.50           O  
ATOM    652  N   SER A  99      -4.687   9.413 -11.048  1.00 64.63           N  
ATOM    653  CA  SER A  99      -5.991   8.999 -11.543  1.00 62.72           C  
ATOM    654  C   SER A  99      -6.708  10.112 -12.293  1.00 63.43           C  
ATOM    655  O   SER A  99      -7.380   9.855 -13.289  1.00 64.76           O  
ATOM    656  CB  SER A  99      -6.861   8.502 -10.388  1.00 61.73           C  
ATOM    657  OG  SER A  99      -6.302   7.341  -9.795  1.00 59.20           O  
ATOM    658  N   LEU A 100      -6.564  11.346 -11.824  1.00 63.87           N  
ATOM    659  CA  LEU A 100      -7.268  12.466 -12.448  1.00 67.29           C  
ATOM    660  C   LEU A 100      -6.580  12.939 -13.733  1.00 68.34           C  
ATOM    661  O   LEU A 100      -7.140  13.735 -14.489  1.00 68.42           O  
ATOM    662  CB  LEU A 100      -7.404  13.626 -11.459  1.00 67.68           C  
ATOM    663  CG  LEU A 100      -8.281  13.327 -10.239  1.00 67.26           C  
ATOM    664  CD1 LEU A 100      -8.483  14.571  -9.384  1.00 69.56           C  
ATOM    665  CD2 LEU A 100      -9.620  12.745 -10.674  1.00 66.94           C  
ATOM    666  N   LEU A 101      -5.371  12.438 -13.976  1.00 69.14           N  
ATOM    667  CA  LEU A 101      -4.613  12.779 -15.178  1.00 71.88           C  
ATOM    668  C   LEU A 101      -4.455  11.559 -16.066  1.00 76.02           C  
ATOM    669  O   LEU A 101      -3.786  11.600 -17.099  1.00 75.02           O  
ATOM    670  CB  LEU A 101      -3.237  13.329 -14.815  1.00 69.45           C  
ATOM    671  CG  LEU A 101      -3.205  14.697 -14.144  1.00 69.25           C  
ATOM    672  CD1 LEU A 101      -1.774  15.066 -13.816  1.00 69.28           C  
ATOM    673  CD2 LEU A 101      -3.838  15.738 -15.050  1.00 70.11           C  
ATOM    674  N   ASN A 102      -5.075  10.471 -15.629  1.00 80.01           N  
ATOM    675  CA  ASN A 102      -5.007   9.191 -16.309  1.00 81.91           C  
ATOM    676  C   ASN A 102      -5.490   9.279 -17.753  1.00 81.31           C  
ATOM    677  O   ASN A 102      -6.465   9.970 -18.051  1.00 89.21           O  
ATOM    678  CB  ASN A 102      -5.824   8.163 -15.531  1.00 86.17           C  
ATOM    679  CG  ASN A 102      -5.639   6.765 -16.043  1.00 91.45           C  
ATOM    680  OD1 ASN A 102      -4.702   6.483 -16.789  1.00 96.94           O  
ATOM    681  ND2 ASN A 102      -6.530   5.871 -15.642  1.00 91.53           N  
ATOM    682  N   ARG A 103      -4.793   8.588 -18.648  1.00 74.04           N  
ATOM    683  CA  ARG A 103      -5.135   8.611 -20.065  1.00 70.11           C  
ATOM    684  C   ARG A 103      -5.493   7.211 -20.556  1.00 64.90           C  
ATOM    685  O   ARG A 103      -5.133   6.821 -21.667  1.00 63.12           O  
ATOM    686  CB  ARG A 103      -3.977   9.183 -20.896  1.00 69.31           C  
ATOM    687  CG  ARG A 103      -3.462  10.540 -20.427  1.00 67.27           C  
ATOM    688  CD  ARG A 103      -3.642  11.610 -21.492  1.00 65.95           C  
ATOM    689  NE  ARG A 103      -2.384  12.008 -22.125  1.00 63.53           N  
ATOM    690  CZ  ARG A 103      -1.734  13.139 -21.862  1.00 63.56           C  
ATOM    691  NH1 ARG A 103      -0.600  13.416 -22.493  1.00 63.06           N  
ATOM    692  NH2 ARG A 103      -2.214  14.000 -20.971  1.00 64.02           N  
ATOM    693  N   GLY A 104      -6.206   6.459 -19.726  1.00 63.13           N  
ATOM    694  CA  GLY A 104      -6.546   5.087 -20.054  1.00 59.42           C  
ATOM    695  C   GLY A 104      -7.888   4.937 -20.745  1.00 60.79           C  
ATOM    696  O   GLY A 104      -8.714   5.849 -20.729  1.00 58.76           O  
ATOM    697  N   ARG A 105      -8.102   3.778 -21.359  1.00 60.27           N  
ATOM    698  CA  ARG A 105      -9.381   3.462 -21.985  1.00 60.49           C  
ATOM    699  C   ARG A 105     -10.474   3.326 -20.925  1.00 58.74           C  
ATOM    700  O   ARG A 105     -10.167   3.141 -19.745  1.00 56.43           O  
ATOM    701  CB  ARG A 105      -9.268   2.175 -22.799  1.00 61.03           C  
ATOM    702  CG  ARG A 105      -8.801   0.985 -21.983  1.00 59.91           C  
ATOM    703  CD  ARG A 105      -8.988  -0.307 -22.738  1.00 63.21           C  
ATOM    704  NE  ARG A 105      -8.287  -0.309 -24.018  1.00 65.66           N  
ATOM    705  CZ  ARG A 105      -8.697  -0.990 -25.082  1.00 67.77           C  
ATOM    706  NH1 ARG A 105      -8.003  -0.947 -26.209  1.00 72.04           N  
ATOM    707  NH2 ARG A 105      -9.807  -1.711 -25.018  1.00 67.44           N  
ATOM    708  N   PRO A 106     -11.751   3.440 -21.338  1.00 61.34           N  
ATOM    709  CA  PRO A 106     -12.913   3.239 -20.462  1.00 62.45           C  
ATOM    710  C   PRO A 106     -12.828   1.968 -19.614  1.00 64.02           C  
ATOM    711  O   PRO A 106     -12.477   0.896 -20.110  1.00 66.95           O  
ATOM    712  CB  PRO A 106     -14.087   3.151 -21.446  1.00 64.75           C  
ATOM    713  CG  PRO A 106     -13.529   3.528 -22.806  1.00 64.17           C  
ATOM    714  CD  PRO A 106     -12.153   4.059 -22.609  1.00 62.09           C  
ATOM    715  N   TYR A 107     -13.167   2.108 -18.337  1.00 62.96           N  
ATOM    716  CA  TYR A 107     -12.970   1.066 -17.338  1.00 62.13           C  
ATOM    717  C   TYR A 107     -14.285   0.350 -17.012  1.00 62.18           C  
ATOM    718  O   TYR A 107     -15.337   0.986 -16.930  1.00 63.93           O  
ATOM    719  CB  TYR A 107     -12.358   1.697 -16.084  1.00 64.06           C  
ATOM    720  CG  TYR A 107     -11.858   0.746 -15.018  1.00 66.45           C  
ATOM    721  CD1 TYR A 107     -10.521   0.371 -14.970  1.00 65.77           C  
ATOM    722  CD2 TYR A 107     -12.711   0.256 -14.034  1.00 69.28           C  
ATOM    723  CE1 TYR A 107     -10.054  -0.483 -13.990  1.00 65.61           C  
ATOM    724  CE2 TYR A 107     -12.251  -0.600 -13.051  1.00 69.74           C  
ATOM    725  CZ  TYR A 107     -10.924  -0.966 -13.034  1.00 66.72           C  
ATOM    726  OH  TYR A 107     -10.466  -1.818 -12.057  1.00 66.44           O  
ATOM    727  N   PRO A 108     -14.229  -0.981 -16.834  1.00 62.90           N  
ATOM    728  CA  PRO A 108     -15.411  -1.790 -16.497  1.00 65.37           C  
ATOM    729  C   PRO A 108     -16.016  -1.412 -15.146  1.00 68.67           C  
ATOM    730  O   PRO A 108     -15.327  -1.484 -14.126  1.00 66.40           O  
ATOM    731  CB  PRO A 108     -14.863  -3.221 -16.457  1.00 64.24           C  
ATOM    732  CG  PRO A 108     -13.591  -3.174 -17.238  1.00 61.75           C  
ATOM    733  CD  PRO A 108     -13.026  -1.810 -17.013  1.00 59.91           C  
ATOM    734  N   ALA A 109     -17.290  -1.026 -15.143  1.00 74.64           N  
ATOM    735  CA  ALA A 109     -17.967  -0.577 -13.928  1.00 79.34           C  
ATOM    736  C   ALA A 109     -17.991  -1.655 -12.847  1.00 82.63           C  
ATOM    737  O   ALA A 109     -17.822  -1.359 -11.663  1.00 81.94           O  
ATOM    738  CB  ALA A 109     -19.384  -0.130 -14.255  1.00 82.53           C  
ATOM    739  N   ILE A 110     -18.202  -2.898 -13.268  1.00 87.53           N  
ATOM    740  CA  ILE A 110     -18.231  -4.047 -12.368  1.00 92.58           C  
ATOM    741  C   ILE A 110     -17.015  -4.109 -11.439  1.00 90.01           C  
ATOM    742  O   ILE A 110     -17.151  -4.368 -10.243  1.00 93.66           O  
ATOM    743  CB  ILE A 110     -18.315  -5.367 -13.167  1.00100.78           C  
ATOM    744  CG1 ILE A 110     -19.558  -5.369 -14.060  1.00112.83           C  
ATOM    745  CG2 ILE A 110     -18.318  -6.573 -12.234  1.00101.12           C  
ATOM    746  CD1 ILE A 110     -19.728  -6.632 -14.883  1.00115.79           C  
ATOM    747  N   LEU A 111     -15.831  -3.850 -11.987  1.00 83.93           N  
ATOM    748  CA  LEU A 111     -14.591  -3.992 -11.226  1.00 77.23           C  
ATOM    749  C   LEU A 111     -14.354  -2.870 -10.217  1.00 74.28           C  
ATOM    750  O   LEU A 111     -13.517  -3.009  -9.326  1.00 73.87           O  
ATOM    751  CB  LEU A 111     -13.392  -4.075 -12.176  1.00 73.58           C  
ATOM    752  CG  LEU A 111     -13.406  -5.248 -13.154  1.00 71.75           C  
ATOM    753  CD1 LEU A 111     -12.051  -5.411 -13.824  1.00 68.58           C  
ATOM    754  CD2 LEU A 111     -13.822  -6.528 -12.441  1.00 72.53           C  
ATOM    755  N   ILE A 112     -15.077  -1.763 -10.356  1.00 73.06           N  
ATOM    756  CA  ILE A 112     -14.867  -0.619  -9.474  1.00 71.74           C  
ATOM    757  C   ILE A 112     -15.209  -0.957  -8.028  1.00 71.36           C  
ATOM    758  O   ILE A 112     -14.420  -0.696  -7.117  1.00 69.07           O  
ATOM    759  CB  ILE A 112     -15.694   0.595  -9.919  1.00 72.70           C  
ATOM    760  CG1 ILE A 112     -15.035   1.259 -11.127  1.00 70.76           C  
ATOM    761  CG2 ILE A 112     -15.824   1.602  -8.783  1.00 73.00           C  
ATOM    762  CD1 ILE A 112     -15.669   2.569 -11.514  1.00 72.12           C  
ATOM    763  N   LEU A 113     -16.377  -1.557  -7.828  1.00 73.42           N  
ATOM    764  CA  LEU A 113     -16.830  -1.915  -6.493  1.00 74.28           C  
ATOM    765  C   LEU A 113     -15.880  -2.897  -5.808  1.00 72.07           C  
ATOM    766  O   LEU A 113     -15.660  -2.807  -4.603  1.00 71.91           O  
ATOM    767  CB  LEU A 113     -18.245  -2.491  -6.554  1.00 77.40           C  
ATOM    768  CG  LEU A 113     -19.301  -1.474  -6.995  1.00 80.23           C  
ATOM    769  CD1 LEU A 113     -20.669  -2.116  -7.082  1.00 83.98           C  
ATOM    770  CD2 LEU A 113     -19.330  -0.283  -6.048  1.00 80.84           C  
ATOM    771  N   ARG A 114     -15.311  -3.824  -6.574  1.00 70.99           N  
ATOM    772  CA  ARG A 114     -14.330  -4.757  -6.021  1.00 69.35           C  
ATOM    773  C   ARG A 114     -13.005  -4.055  -5.752  1.00 67.89           C  
ATOM    774  O   ARG A 114     -12.361  -4.295  -4.732  1.00 69.42           O  
ATOM    775  CB  ARG A 114     -14.107  -5.946  -6.959  1.00 69.01           C  
ATOM    776  CG  ARG A 114     -15.250  -6.941  -6.981  1.00 70.68           C  
ATOM    777  CD  ARG A 114     -14.741  -8.376  -7.064  1.00 71.22           C  
ATOM    778  NE  ARG A 114     -14.104  -8.673  -8.343  1.00 69.90           N  
ATOM    779  CZ  ARG A 114     -14.756  -9.105  -9.418  1.00 71.21           C  
ATOM    780  NH1 ARG A 114     -16.069  -9.284  -9.369  1.00 73.30           N  
ATOM    781  NH2 ARG A 114     -14.098  -9.352 -10.540  1.00 70.80           N  
ATOM    782  N   GLY A 115     -12.602  -3.194  -6.681  1.00 65.20           N  
ATOM    783  CA  GLY A 115     -11.406  -2.394  -6.508  1.00 62.63           C  
ATOM    784  C   GLY A 115     -11.548  -1.472  -5.314  1.00 61.45           C  
ATOM    785  O   GLY A 115     -10.610  -1.293  -4.540  1.00 58.50           O  
ATOM    786  N   THR A 116     -12.733  -0.887  -5.160  1.00 62.71           N  
ATOM    787  CA  THR A 116     -13.001  -0.010  -4.024  1.00 62.79           C  
ATOM    788  C   THR A 116     -13.024  -0.810  -2.726  1.00 60.57           C  
ATOM    789  O   THR A 116     -12.515  -0.354  -1.702  1.00 61.22           O  
ATOM    790  CB  THR A 116     -14.333   0.748  -4.183  1.00 64.27           C  
ATOM    791  OG1 THR A 116     -14.252   1.622  -5.314  1.00 65.23           O  
ATOM    792  CG2 THR A 116     -14.630   1.579  -2.947  1.00 65.48           C  
ATOM    793  N   ALA A 117     -13.608  -2.005  -2.777  1.00 59.79           N  
ATOM    794  CA  ALA A 117     -13.651  -2.890  -1.615  1.00 60.11           C  
ATOM    795  C   ALA A 117     -12.244  -3.241  -1.157  1.00 59.71           C  
ATOM    796  O   ALA A 117     -11.973  -3.309   0.039  1.00 60.73           O  
ATOM    797  CB  ALA A 117     -14.427  -4.151  -1.931  1.00 61.28           C  
ATOM    798  N   PHE A 118     -11.353  -3.464  -2.115  1.00 58.52           N  
ATOM    799  CA  PHE A 118      -9.978  -3.797  -1.794  1.00 57.49           C  
ATOM    800  C   PHE A 118      -9.317  -2.631  -1.061  1.00 60.19           C  
ATOM    801  O   PHE A 118      -8.799  -2.796   0.042  1.00 63.76           O  
ATOM    802  CB  PHE A 118      -9.197  -4.150  -3.059  1.00 56.19           C  
ATOM    803  CG  PHE A 118      -7.788  -4.591  -2.793  1.00 56.48           C  
ATOM    804  CD1 PHE A 118      -6.786  -3.656  -2.561  1.00 55.31           C  
ATOM    805  CD2 PHE A 118      -7.463  -5.938  -2.768  1.00 56.97           C  
ATOM    806  CE1 PHE A 118      -5.490  -4.053  -2.312  1.00 55.27           C  
ATOM    807  CE2 PHE A 118      -6.166  -6.343  -2.518  1.00 56.45           C  
ATOM    808  CZ  PHE A 118      -5.180  -5.397  -2.288  1.00 56.35           C  
ATOM    809  N   CYS A 119      -9.348  -1.455  -1.680  1.00 58.67           N  
ATOM    810  CA  CYS A 119      -8.707  -0.266  -1.125  1.00 57.80           C  
ATOM    811  C   CYS A 119      -9.342   0.208   0.182  1.00 60.92           C  
ATOM    812  O   CYS A 119      -8.725   0.960   0.937  1.00 60.68           O  
ATOM    813  CB  CYS A 119      -8.725   0.871  -2.147  1.00 55.10           C  
ATOM    814  SG  CYS A 119      -7.587   0.632  -3.519  1.00 63.85           S  
ATOM    815  N   THR A 120     -10.572  -0.221   0.449  1.00 62.86           N  
ATOM    816  CA  THR A 120     -11.199   0.098   1.725  1.00 66.17           C  
ATOM    817  C   THR A 120     -10.608  -0.787   2.821  1.00 68.85           C  
ATOM    818  O   THR A 120     -10.011  -0.288   3.777  1.00 68.90           O  
ATOM    819  CB  THR A 120     -12.726  -0.072   1.679  1.00 66.57           C  
ATOM    820  OG1 THR A 120     -13.291   0.957   0.858  1.00 66.62           O  
ATOM    821  CG2 THR A 120     -13.318   0.038   3.077  1.00 68.43           C  
ATOM    822  N   GLY A 121     -10.760  -2.099   2.666  1.00 71.44           N  
ATOM    823  CA  GLY A 121     -10.230  -3.055   3.621  1.00 74.17           C  
ATOM    824  C   GLY A 121      -8.740  -2.898   3.856  1.00 76.51           C  
ATOM    825  O   GLY A 121      -8.268  -3.000   4.986  1.00 77.28           O  
ATOM    826  N   ASN A 122      -8.000  -2.640   2.784  1.00 78.79           N  
ATOM    827  CA  ASN A 122      -6.555  -2.465   2.871  1.00 75.09           C  
ATOM    828  C   ASN A 122      -6.200  -1.192   3.632  1.00 73.22           C  
ATOM    829  O   ASN A 122      -5.302  -1.190   4.472  1.00 73.01           O  
ATOM    830  CB  ASN A 122      -5.936  -2.437   1.471  1.00 73.23           C  
ATOM    831  CG  ASN A 122      -4.423  -2.420   1.503  1.00 73.08           C  
ATOM    832  OD1 ASN A 122      -3.801  -2.998   2.394  1.00 73.52           O  
ATOM    833  ND2 ASN A 122      -3.822  -1.751   0.527  1.00 72.74           N  
ATOM    834  N   GLY A 123      -6.917  -0.116   3.329  1.00 73.15           N  
ATOM    835  CA  GLY A 123      -6.745   1.140   4.033  1.00 73.72           C  
ATOM    836  C   GLY A 123      -7.078   1.002   5.506  1.00 77.33           C  
ATOM    837  O   GLY A 123      -6.408   1.583   6.359  1.00 82.22           O  
ATOM    838  N   VAL A 124      -8.117   0.230   5.812  1.00 74.59           N  
ATOM    839  CA  VAL A 124      -8.493  -0.007   7.199  1.00 73.60           C  
ATOM    840  C   VAL A 124      -7.410  -0.812   7.906  1.00 72.11           C  
ATOM    841  O   VAL A 124      -6.968  -0.451   8.995  1.00 74.01           O  
ATOM    842  CB  VAL A 124      -9.841  -0.746   7.310  1.00 73.60           C  
ATOM    843  CG1 VAL A 124     -10.053  -1.268   8.726  1.00 75.91           C  
ATOM    844  CG2 VAL A 124     -10.983   0.170   6.898  1.00 73.66           C  
ATOM    845  N   LEU A 125      -6.980  -1.896   7.268  1.00 69.85           N  
ATOM    846  CA  LEU A 125      -5.956  -2.774   7.825  1.00 69.16           C  
ATOM    847  C   LEU A 125      -4.662  -2.031   8.153  1.00 68.26           C  
ATOM    848  O   LEU A 125      -4.209  -2.038   9.296  1.00 68.68           O  
ATOM    849  CB  LEU A 125      -5.663  -3.922   6.855  1.00 67.27           C  
ATOM    850  CG  LEU A 125      -4.583  -4.928   7.258  1.00 68.24           C  
ATOM    851  CD1 LEU A 125      -5.019  -5.748   8.462  1.00 70.86           C  
ATOM    852  CD2 LEU A 125      -4.241  -5.834   6.087  1.00 66.91           C  
ATOM    853  N   GLN A 126      -4.074  -1.388   7.148  1.00 67.72           N  
ATOM    854  CA  GLN A 126      -2.798  -0.697   7.319  1.00 68.87           C  
ATOM    855  C   GLN A 126      -2.889   0.442   8.335  1.00 71.33           C  
ATOM    856  O   GLN A 126      -1.962   0.669   9.115  1.00 71.48           O  
ATOM    857  CB  GLN A 126      -2.300  -0.153   5.976  1.00 67.01           C  
ATOM    858  CG  GLN A 126      -2.119  -1.208   4.899  1.00 66.92           C  
ATOM    859  CD  GLN A 126      -1.073  -2.246   5.256  1.00 69.48           C  
ATOM    860  OE1 GLN A 126      -1.299  -3.447   5.104  1.00 68.63           O  
ATOM    861  NE2 GLN A 126       0.082  -1.789   5.728  1.00 72.73           N  
ATOM    862  N   GLY A 127      -4.010   1.154   8.321  1.00 72.64           N  
ATOM    863  CA  GLY A 127      -4.198   2.293   9.199  1.00 75.53           C  
ATOM    864  C   GLY A 127      -4.470   1.895  10.636  1.00 79.83           C  
ATOM    865  O   GLY A 127      -3.983   2.534  11.569  1.00 85.97           O  
ATOM    866  N   TYR A 128      -5.253   0.839  10.817  1.00 76.99           N  
ATOM    867  CA  TYR A 128      -5.584   0.360  12.151  1.00 77.53           C  
ATOM    868  C   TYR A 128      -4.370  -0.265  12.824  1.00 77.12           C  
ATOM    869  O   TYR A 128      -4.139  -0.067  14.020  1.00 79.62           O  
ATOM    870  CB  TYR A 128      -6.729  -0.651  12.091  1.00 75.50           C  
ATOM    871  CG  TYR A 128      -7.036  -1.317  13.413  1.00 76.64           C  
ATOM    872  CD1 TYR A 128      -6.550  -2.584  13.702  1.00 76.02           C  
ATOM    873  CD2 TYR A 128      -7.816  -0.680  14.371  1.00 78.54           C  
ATOM    874  CE1 TYR A 128      -6.829  -3.198  14.910  1.00 77.93           C  
ATOM    875  CE2 TYR A 128      -8.101  -1.285  15.577  1.00 80.02           C  
ATOM    876  CZ  TYR A 128      -7.605  -2.545  15.842  1.00 79.83           C  
ATOM    877  OH  TYR A 128      -7.885  -3.155  17.043  1.00 83.17           O  
ATOM    878  N   TYR A 129      -3.597  -1.021  12.052  1.00 73.75           N  
ATOM    879  CA  TYR A 129      -2.458  -1.735  12.609  1.00 72.79           C  
ATOM    880  C   TYR A 129      -1.387  -0.772  13.100  1.00 75.61           C  
ATOM    881  O   TYR A 129      -0.946  -0.854  14.245  1.00 82.00           O  
ATOM    882  CB  TYR A 129      -1.859  -2.696  11.583  1.00 68.10           C  
ATOM    883  CG  TYR A 129      -0.792  -3.590  12.169  1.00 66.81           C  
ATOM    884  CD1 TYR A 129       0.538  -3.196  12.189  1.00 66.09           C  
ATOM    885  CD2 TYR A 129      -1.116  -4.825  12.714  1.00 67.63           C  
ATOM    886  CE1 TYR A 129       1.514  -4.006  12.733  1.00 67.12           C  
ATOM    887  CE2 TYR A 129      -0.145  -5.644  13.257  1.00 68.98           C  
ATOM    888  CZ  TYR A 129       1.167  -5.229  13.263  1.00 68.00           C  
ATOM    889  OH  TYR A 129       2.138  -6.038  13.800  1.00 68.61           O  
ATOM    890  N   LEU A 130      -0.976   0.141  12.226  1.00 70.78           N  
ATOM    891  CA  LEU A 130       0.112   1.060  12.534  1.00 70.45           C  
ATOM    892  C   LEU A 130      -0.149   1.922  13.764  1.00 73.38           C  
ATOM    893  O   LEU A 130       0.778   2.253  14.500  1.00 74.23           O  
ATOM    894  CB  LEU A 130       0.396   1.958  11.331  1.00 66.71           C  
ATOM    895  CG  LEU A 130       1.147   1.278  10.189  1.00 62.21           C  
ATOM    896  CD1 LEU A 130       1.576   2.305   9.160  1.00 60.78           C  
ATOM    897  CD2 LEU A 130       2.349   0.514  10.725  1.00 63.26           C  
ATOM    898  N   ILE A 131      -1.406   2.281  13.992  1.00 74.72           N  
ATOM    899  CA  ILE A 131      -1.742   3.158  15.107  1.00 81.18           C  
ATOM    900  C   ILE A 131      -1.997   2.390  16.403  1.00 84.24           C  
ATOM    901  O   ILE A 131      -1.488   2.760  17.459  1.00 85.57           O  
ATOM    902  CB  ILE A 131      -2.983   4.020  14.789  1.00 81.19           C  
ATOM    903  CG1 ILE A 131      -2.700   4.949  13.606  1.00 79.08           C  
ATOM    904  CG2 ILE A 131      -3.399   4.833  16.005  1.00 85.45           C  
ATOM    905  CD1 ILE A 131      -1.622   5.973  13.871  1.00 67.73           C  
ATOM    906  N   TYR A 132      -2.773   1.314  16.312  1.00 85.80           N  
ATOM    907  CA  TYR A 132      -3.256   0.617  17.501  1.00 91.95           C  
ATOM    908  C   TYR A 132      -2.436  -0.617  17.871  1.00 96.05           C  
ATOM    909  O   TYR A 132      -2.476  -1.068  19.016  1.00105.43           O  
ATOM    910  CB  TYR A 132      -4.719   0.205  17.309  1.00 93.73           C  
ATOM    911  CG  TYR A 132      -5.704   1.356  17.257  1.00 97.01           C  
ATOM    912  CD1 TYR A 132      -6.401   1.752  18.393  1.00102.41           C  
ATOM    913  CD2 TYR A 132      -5.950   2.037  16.070  1.00 95.67           C  
ATOM    914  CE1 TYR A 132      -7.310   2.798  18.349  1.00103.23           C  
ATOM    915  CE2 TYR A 132      -6.855   3.084  16.017  1.00 97.00           C  
ATOM    916  CZ  TYR A 132      -7.532   3.459  17.160  1.00100.98           C  
ATOM    917  OH  TYR A 132      -8.433   4.499  17.113  1.00102.37           O  
ATOM    918  N   CYS A 133      -1.700  -1.165  16.910  1.00 91.39           N  
ATOM    919  CA  CYS A 133      -1.004  -2.431  17.128  1.00 90.25           C  
ATOM    920  C   CYS A 133       0.516  -2.304  17.085  1.00 90.52           C  
ATOM    921  O   CYS A 133       1.212  -2.833  17.953  1.00 89.44           O  
ATOM    922  CB  CYS A 133      -1.460  -3.467  16.096  1.00 86.68           C  
ATOM    923  SG  CYS A 133      -3.176  -4.005  16.291  1.00107.99           S  
ATOM    924  N   ALA A 134       1.024  -1.606  16.073  1.00 91.75           N  
ATOM    925  CA  ALA A 134       2.464  -1.504  15.842  1.00 95.36           C  
ATOM    926  C   ALA A 134       3.208  -0.928  17.045  1.00100.45           C  
ATOM    927  O   ALA A 134       2.772   0.049  17.655  1.00104.56           O  
ATOM    928  CB  ALA A 134       2.736  -0.664  14.607  1.00 92.69           C  
ATOM    929  N   GLU A 135       4.335  -1.550  17.376  1.00100.45           N  
ATOM    930  CA  GLU A 135       5.157  -1.118  18.499  1.00105.44           C  
ATOM    931  C   GLU A 135       6.631  -1.110  18.112  1.00104.44           C  
ATOM    932  O   GLU A 135       7.198  -2.144  17.753  1.00106.20           O  
ATOM    933  CB  GLU A 135       4.927  -2.023  19.709  1.00110.23           C  
ATOM    934  CG  GLU A 135       3.518  -1.945  20.273  1.00114.15           C  
ATOM    935  CD  GLU A 135       3.256  -2.992  21.333  1.00119.74           C  
ATOM    936  OE1 GLU A 135       4.126  -3.866  21.532  1.00124.38           O  
ATOM    937  OE2 GLU A 135       2.180  -2.942  21.965  1.00120.61           O  
ATOM    938  N   TYR A 136       7.244   0.066  18.192  1.00100.57           N  
ATOM    939  CA  TYR A 136       8.613   0.257  17.732  1.00 97.12           C  
ATOM    940  C   TYR A 136       9.569   0.568  18.883  1.00 97.64           C  
ATOM    941  O   TYR A 136       9.169   1.170  19.878  1.00 99.52           O  
ATOM    942  CB  TYR A 136       8.668   1.383  16.695  1.00 94.89           C  
ATOM    943  CG  TYR A 136       7.858   1.123  15.440  1.00 90.84           C  
ATOM    944  CD1 TYR A 136       8.438   0.528  14.326  1.00 88.11           C  
ATOM    945  CD2 TYR A 136       6.519   1.478  15.366  1.00 88.88           C  
ATOM    946  CE1 TYR A 136       7.708   0.291  13.178  1.00 82.90           C  
ATOM    947  CE2 TYR A 136       5.779   1.242  14.222  1.00 84.91           C  
ATOM    948  CZ  TYR A 136       6.379   0.648  13.131  1.00 81.55           C  
ATOM    949  OH  TYR A 136       5.648   0.412  11.985  1.00 77.85           O  
ATOM    950  N   PRO A 137      10.839   0.150  18.750  1.00 96.26           N  
ATOM    951  CA  PRO A 137      11.903   0.532  19.686  1.00100.98           C  
ATOM    952  C   PRO A 137      12.178   2.034  19.654  1.00107.93           C  
ATOM    953  O   PRO A 137      11.601   2.750  18.835  1.00104.28           O  
ATOM    954  CB  PRO A 137      13.120  -0.250  19.181  1.00 99.01           C  
ATOM    955  CG  PRO A 137      12.554  -1.377  18.396  1.00 94.19           C  
ATOM    956  CD  PRO A 137      11.305  -0.844  17.769  1.00 91.84           C  
ATOM    957  N   ASP A 138      13.065   2.498  20.527  1.00118.72           N  
ATOM    958  CA  ASP A 138      13.315   3.928  20.677  1.00128.48           C  
ATOM    959  C   ASP A 138      14.268   4.490  19.625  1.00135.11           C  
ATOM    960  O   ASP A 138      14.164   5.655  19.245  1.00136.95           O  
ATOM    961  CB  ASP A 138      13.858   4.214  22.077  1.00132.29           C  
ATOM    962  CG  ASP A 138      12.866   3.861  23.165  1.00132.30           C  
ATOM    963  OD1 ASP A 138      11.647   3.924  22.897  1.00101.60           O  
ATOM    964  OD2 ASP A 138      13.303   3.522  24.285  1.00134.50           O  
ATOM    965  N   GLY A 139      15.196   3.663  19.156  1.00140.56           N  
ATOM    966  CA  GLY A 139      16.152   4.095  18.151  1.00139.50           C  
ATOM    967  C   GLY A 139      15.806   3.582  16.768  1.00135.22           C  
ATOM    968  O   GLY A 139      16.666   3.059  16.058  1.00136.26           O  
ATOM    969  N   TRP A 140      14.543   3.741  16.381  1.00125.59           N  
ATOM    970  CA  TRP A 140      14.061   3.206  15.113  1.00114.43           C  
ATOM    971  C   TRP A 140      14.512   4.041  13.918  1.00109.44           C  
ATOM    972  O   TRP A 140      14.823   3.497  12.862  1.00107.55           O  
ATOM    973  CB  TRP A 140      12.535   3.102  15.128  1.00108.96           C  
ATOM    974  CG  TRP A 140      11.979   2.307  13.982  1.00100.52           C  
ATOM    975  CD1 TRP A 140      11.281   2.785  12.909  1.00 95.88           C  
ATOM    976  CD2 TRP A 140      12.084   0.889  13.793  1.00 96.48           C  
ATOM    977  NE1 TRP A 140      10.941   1.752  12.068  1.00 92.04           N  
ATOM    978  CE2 TRP A 140      11.423   0.579  12.587  1.00 92.36           C  
ATOM    979  CE3 TRP A 140      12.671  -0.146  14.526  1.00 97.25           C  
ATOM    980  CZ2 TRP A 140      11.334  -0.726  12.100  1.00 88.87           C  
ATOM    981  CZ3 TRP A 140      12.580  -1.440  14.040  1.00 94.59           C  
ATOM    982  CH2 TRP A 140      11.918  -1.717  12.839  1.00 90.18           C  
ATOM    983  N   TYR A 141      14.555   5.360  14.088  1.00108.13           N  
ATOM    984  CA  TYR A 141      14.898   6.258  12.986  1.00103.84           C  
ATOM    985  C   TYR A 141      16.359   6.129  12.551  1.00103.76           C  
ATOM    986  O   TYR A 141      16.741   6.620  11.484  1.00100.30           O  
ATOM    987  CB  TYR A 141      14.591   7.709  13.370  1.00106.32           C  
ATOM    988  CG  TYR A 141      13.111   8.023  13.431  1.00104.69           C  
ATOM    989  CD1 TYR A 141      12.383   8.256  12.270  1.00101.47           C  
ATOM    990  CD2 TYR A 141      12.442   8.089  14.647  1.00106.85           C  
ATOM    991  CE1 TYR A 141      11.030   8.542  12.316  1.00 99.79           C  
ATOM    992  CE2 TYR A 141      11.089   8.377  14.704  1.00105.87           C  
ATOM    993  CZ  TYR A 141      10.388   8.602  13.535  1.00102.36           C  
ATOM    994  OH  TYR A 141       9.043   8.888  13.585  1.00101.05           O  
ATOM    995  N   THR A 142      17.168   5.467  13.373  1.00107.58           N  
ATOM    996  CA  THR A 142      18.569   5.222  13.044  1.00110.11           C  
ATOM    997  C   THR A 142      18.794   3.756  12.686  1.00106.25           C  
ATOM    998  O   THR A 142      19.879   3.370  12.253  1.00107.26           O  
ATOM    999  CB  THR A 142      19.502   5.611  14.205  1.00118.14           C  
ATOM   1000  OG1 THR A 142      19.137   4.875  15.381  1.00 95.41           O  
ATOM   1001  CG2 THR A 142      19.403   7.102  14.491  1.00 96.80           C  
ATOM   1002  N   ASP A 143      17.758   2.944  12.871  1.00102.71           N  
ATOM   1003  CA  ASP A 143      17.831   1.519  12.573  1.00102.97           C  
ATOM   1004  C   ASP A 143      17.923   1.275  11.070  1.00 97.63           C  
ATOM   1005  O   ASP A 143      17.351   2.021  10.272  1.00 94.65           O  
ATOM   1006  CB  ASP A 143      16.622   0.786  13.151  1.00105.73           C  
ATOM   1007  CG  ASP A 143      16.781  -0.719  13.108  1.00110.89           C  
ATOM   1008  OD1 ASP A 143      17.934  -1.192  13.198  1.00118.91           O  
ATOM   1009  OD2 ASP A 143      15.761  -1.428  12.985  1.00108.06           O  
ATOM   1010  N   ILE A 144      18.640   0.222  10.692  1.00 97.61           N  
ATOM   1011  CA  ILE A 144      18.892  -0.080   9.288  1.00 95.26           C  
ATOM   1012  C   ILE A 144      17.600  -0.431   8.549  1.00 88.94           C  
ATOM   1013  O   ILE A 144      17.481  -0.192   7.351  1.00 86.27           O  
ATOM   1014  CB  ILE A 144      19.906  -1.234   9.145  1.00 98.27           C  
ATOM   1015  CG1 ILE A 144      21.044  -1.063  10.158  1.00104.86           C  
ATOM   1016  CG2 ILE A 144      20.454  -1.295   7.728  1.00 98.23           C  
ATOM   1017  CD1 ILE A 144      22.143  -2.101  10.042  1.00106.04           C  
ATOM   1018  N   ARG A 145      16.630  -0.981   9.271  1.00 86.81           N  
ATOM   1019  CA  ARG A 145      15.349  -1.346   8.674  1.00 81.20           C  
ATOM   1020  C   ARG A 145      14.575  -0.111   8.219  1.00 81.53           C  
ATOM   1021  O   ARG A 145      13.865  -0.147   7.216  1.00 82.08           O  
ATOM   1022  CB  ARG A 145      14.509  -2.157   9.665  1.00 79.74           C  
ATOM   1023  CG  ARG A 145      15.254  -3.327  10.285  1.00 81.68           C  
ATOM   1024  CD  ARG A 145      14.398  -4.065  11.302  1.00 82.62           C  
ATOM   1025  NE  ARG A 145      15.197  -4.948  12.148  1.00 87.37           N  
ATOM   1026  CZ  ARG A 145      15.574  -4.655  13.389  1.00 92.40           C  
ATOM   1027  NH1 ARG A 145      15.213  -3.504  13.938  1.00 93.51           N  
ATOM   1028  NH2 ARG A 145      16.306  -5.516  14.084  1.00 97.47           N  
ATOM   1029  N   PHE A 146      14.716   0.980   8.962  1.00 82.26           N  
ATOM   1030  CA  PHE A 146      14.032   2.227   8.635  1.00 79.69           C  
ATOM   1031  C   PHE A 146      14.800   3.011   7.580  1.00 81.48           C  
ATOM   1032  O   PHE A 146      14.238   3.429   6.569  1.00 79.62           O  
ATOM   1033  CB  PHE A 146      13.849   3.081   9.893  1.00 80.25           C  
ATOM   1034  CG  PHE A 146      13.260   4.445   9.633  1.00 76.69           C  
ATOM   1035  CD1 PHE A 146      14.076   5.534   9.352  1.00 76.44           C  
ATOM   1036  CD2 PHE A 146      11.893   4.644   9.692  1.00 73.55           C  
ATOM   1037  CE1 PHE A 146      13.539   6.786   9.118  1.00 74.92           C  
ATOM   1038  CE2 PHE A 146      11.354   5.893   9.464  1.00 67.95           C  
ATOM   1039  CZ  PHE A 146      12.180   6.966   9.175  1.00 70.00           C  
ATOM   1040  N   SER A 147      16.088   3.214   7.838  1.00 85.80           N  
ATOM   1041  CA  SER A 147      16.938   4.043   6.994  1.00 85.49           C  
ATOM   1042  C   SER A 147      17.046   3.478   5.581  1.00 81.76           C  
ATOM   1043  O   SER A 147      17.191   4.224   4.613  1.00 81.69           O  
ATOM   1044  CB  SER A 147      18.327   4.183   7.619  1.00 88.97           C  
ATOM   1045  OG  SER A 147      19.100   5.145   6.926  1.00 91.48           O  
ATOM   1046  N   LEU A 148      16.972   2.154   5.474  1.00 80.25           N  
ATOM   1047  CA  LEU A 148      16.970   1.487   4.179  1.00 78.04           C  
ATOM   1048  C   LEU A 148      15.544   1.350   3.655  1.00 74.29           C  
ATOM   1049  O   LEU A 148      15.280   1.574   2.477  1.00 71.51           O  
ATOM   1050  CB  LEU A 148      17.636   0.112   4.278  1.00 78.23           C  
ATOM   1051  CG  LEU A 148      17.519  -0.817   3.069  1.00 75.46           C  
ATOM   1052  CD1 LEU A 148      18.161  -0.188   1.840  1.00 74.90           C  
ATOM   1053  CD2 LEU A 148      18.145  -2.169   3.376  1.00 76.98           C  
ATOM   1054  N   GLY A 149      14.629   0.983   4.547  1.00 74.26           N  
ATOM   1055  CA  GLY A 149      13.229   0.838   4.199  1.00 71.45           C  
ATOM   1056  C   GLY A 149      12.618   2.126   3.677  1.00 71.82           C  
ATOM   1057  O   GLY A 149      11.852   2.109   2.714  1.00 70.98           O  
ATOM   1058  N   VAL A 150      12.950   3.245   4.313  1.00 73.21           N  
ATOM   1059  CA  VAL A 150      12.455   4.540   3.861  1.00 74.02           C  
ATOM   1060  C   VAL A 150      13.121   4.899   2.539  1.00 72.57           C  
ATOM   1061  O   VAL A 150      12.487   5.442   1.629  1.00 69.05           O  
ATOM   1062  CB  VAL A 150      12.702   5.640   4.911  1.00 76.42           C  
ATOM   1063  CG1 VAL A 150      12.539   7.026   4.301  1.00 61.51           C  
ATOM   1064  CG2 VAL A 150      11.751   5.457   6.070  1.00 77.02           C  
ATOM   1065  N   PHE A 151      14.404   4.568   2.437  1.00 74.62           N  
ATOM   1066  CA  PHE A 151      15.148   4.746   1.203  1.00 77.10           C  
ATOM   1067  C   PHE A 151      14.503   3.986   0.035  1.00 75.82           C  
ATOM   1068  O   PHE A 151      14.295   4.547  -1.043  1.00 74.58           O  
ATOM   1069  CB  PHE A 151      16.596   4.294   1.395  1.00 80.26           C  
ATOM   1070  CG  PHE A 151      17.312   4.010   0.112  1.00 82.15           C  
ATOM   1071  CD1 PHE A 151      17.821   5.045  -0.657  1.00 84.45           C  
ATOM   1072  CD2 PHE A 151      17.475   2.705  -0.331  1.00 82.16           C  
ATOM   1073  CE1 PHE A 151      18.479   4.783  -1.844  1.00 84.67           C  
ATOM   1074  CE2 PHE A 151      18.129   2.437  -1.517  1.00 81.98           C  
ATOM   1075  CZ  PHE A 151      18.633   3.478  -2.275  1.00 83.66           C  
ATOM   1076  N   LEU A 152      14.189   2.713   0.255  1.00 73.19           N  
ATOM   1077  CA  LEU A 152      13.571   1.885  -0.775  1.00 69.34           C  
ATOM   1078  C   LEU A 152      12.191   2.405  -1.160  1.00 68.43           C  
ATOM   1079  O   LEU A 152      11.773   2.289  -2.311  1.00 67.53           O  
ATOM   1080  CB  LEU A 152      13.467   0.436  -0.304  1.00 67.27           C  
ATOM   1081  CG  LEU A 152      14.792  -0.316  -0.200  1.00 67.78           C  
ATOM   1082  CD1 LEU A 152      14.596  -1.693   0.413  1.00 65.90           C  
ATOM   1083  CD2 LEU A 152      15.440  -0.421  -1.571  1.00 66.44           C  
ATOM   1084  N   PHE A 153      11.492   2.977  -0.187  1.00 70.34           N  
ATOM   1085  CA  PHE A 153      10.152   3.505  -0.410  1.00 68.72           C  
ATOM   1086  C   PHE A 153      10.176   4.671  -1.398  1.00 71.66           C  
ATOM   1087  O   PHE A 153       9.471   4.653  -2.408  1.00 69.67           O  
ATOM   1088  CB  PHE A 153       9.528   3.941   0.920  1.00 68.69           C  
ATOM   1089  CG  PHE A 153       8.093   4.388   0.808  1.00 65.32           C  
ATOM   1090  CD1 PHE A 153       7.059   3.466   0.855  1.00 65.12           C  
ATOM   1091  CD2 PHE A 153       7.780   5.730   0.673  1.00 64.58           C  
ATOM   1092  CE1 PHE A 153       5.739   3.874   0.758  1.00 63.07           C  
ATOM   1093  CE2 PHE A 153       6.466   6.143   0.574  1.00 64.04           C  
ATOM   1094  CZ  PHE A 153       5.444   5.214   0.618  1.00 62.89           C  
ATOM   1095  N   ILE A 154      10.993   5.681  -1.111  1.00 76.28           N  
ATOM   1096  CA  ILE A 154      11.077   6.844  -1.984  1.00 80.50           C  
ATOM   1097  C   ILE A 154      11.723   6.483  -3.320  1.00 79.34           C  
ATOM   1098  O   ILE A 154      11.444   7.108  -4.342  1.00 78.18           O  
ATOM   1099  CB  ILE A 154      11.861   8.003  -1.322  1.00 85.40           C  
ATOM   1100  CG1 ILE A 154      13.281   7.567  -0.963  1.00 89.08           C  
ATOM   1101  CG2 ILE A 154      11.135   8.492  -0.081  1.00 88.02           C  
ATOM   1102  CD1 ILE A 154      14.088   8.638  -0.258  1.00 93.30           C  
ATOM   1103  N   LEU A 155      12.581   5.466  -3.309  1.00 80.02           N  
ATOM   1104  CA  LEU A 155      13.191   4.968  -4.535  1.00 77.39           C  
ATOM   1105  C   LEU A 155      12.132   4.382  -5.455  1.00 75.03           C  
ATOM   1106  O   LEU A 155      12.011   4.776  -6.615  1.00 74.17           O  
ATOM   1107  CB  LEU A 155      14.253   3.913  -4.225  1.00 76.87           C  
ATOM   1108  CG  LEU A 155      14.840   3.190  -5.441  1.00 75.24           C  
ATOM   1109  CD1 LEU A 155      15.547   4.173  -6.362  1.00 76.34           C  
ATOM   1110  CD2 LEU A 155      15.783   2.072  -5.015  1.00 75.71           C  
ATOM   1111  N   GLY A 156      11.369   3.434  -4.922  1.00 74.48           N  
ATOM   1112  CA  GLY A 156      10.319   2.782  -5.675  1.00 73.66           C  
ATOM   1113  C   GLY A 156       9.222   3.729  -6.112  1.00 75.36           C  
ATOM   1114  O   GLY A 156       8.668   3.585  -7.200  1.00 79.43           O  
ATOM   1115  N   MET A 157       8.906   4.704  -5.269  1.00 73.15           N  
ATOM   1116  CA  MET A 157       7.881   5.683  -5.611  1.00 71.47           C  
ATOM   1117  C   MET A 157       8.354   6.597  -6.731  1.00 70.80           C  
ATOM   1118  O   MET A 157       7.577   6.985  -7.598  1.00 70.56           O  
ATOM   1119  CB  MET A 157       7.492   6.517  -4.392  1.00 71.75           C  
ATOM   1120  CG  MET A 157       6.406   7.539  -4.672  1.00 70.16           C  
ATOM   1121  SD  MET A 157       5.962   8.451  -3.194  1.00 74.91           S  
ATOM   1122  CE  MET A 157       4.471   9.283  -3.733  1.00103.09           C  
ATOM   1123  N   GLY A 158       9.635   6.944  -6.699  1.00 71.80           N  
ATOM   1124  CA  GLY A 158      10.225   7.745  -7.752  1.00 71.93           C  
ATOM   1125  C   GLY A 158      10.108   7.008  -9.070  1.00 70.29           C  
ATOM   1126  O   GLY A 158       9.710   7.579 -10.084  1.00 70.51           O  
ATOM   1127  N   ILE A 159      10.437   5.721  -9.041  1.00 67.91           N  
ATOM   1128  CA  ILE A 159      10.392   4.887 -10.231  1.00 64.57           C  
ATOM   1129  C   ILE A 159       8.964   4.695 -10.725  1.00 63.16           C  
ATOM   1130  O   ILE A 159       8.683   4.868 -11.910  1.00 65.15           O  
ATOM   1131  CB  ILE A 159      11.037   3.524  -9.960  1.00 61.67           C  
ATOM   1132  CG1 ILE A 159      12.531   3.715  -9.685  1.00 62.10           C  
ATOM   1133  CG2 ILE A 159      10.816   2.586 -11.137  1.00 60.35           C  
ATOM   1134  CD1 ILE A 159      13.208   2.503  -9.100  1.00 62.00           C  
ATOM   1135  N   ASN A 160       8.068   4.355  -9.805  1.00 62.08           N  
ATOM   1136  CA  ASN A 160       6.662   4.145 -10.136  1.00 60.18           C  
ATOM   1137  C   ASN A 160       6.009   5.362 -10.792  1.00 62.19           C  
ATOM   1138  O   ASN A 160       5.267   5.228 -11.761  1.00 63.17           O  
ATOM   1139  CB  ASN A 160       5.883   3.757  -8.879  1.00 58.55           C  
ATOM   1140  CG  ASN A 160       4.390   3.715  -9.112  1.00 56.37           C  
ATOM   1141  OD1 ASN A 160       3.695   4.712  -8.921  1.00 57.71           O  
ATOM   1142  ND2 ASN A 160       3.885   2.557  -9.522  1.00 54.74           N  
ATOM   1143  N   ILE A 161       6.293   6.549 -10.267  1.00 62.12           N  
ATOM   1144  CA  ILE A 161       5.686   7.773 -10.781  1.00 64.65           C  
ATOM   1145  C   ILE A 161       6.359   8.229 -12.079  1.00 67.16           C  
ATOM   1146  O   ILE A 161       5.692   8.711 -12.996  1.00 66.95           O  
ATOM   1147  CB  ILE A 161       5.742   8.902  -9.727  1.00 64.11           C  
ATOM   1148  CG1 ILE A 161       4.909   8.514  -8.504  1.00 63.58           C  
ATOM   1149  CG2 ILE A 161       5.236  10.211 -10.303  1.00 64.16           C  
ATOM   1150  CD1 ILE A 161       4.884   9.564  -7.414  1.00 65.50           C  
ATOM   1151  N   HIS A 162       7.677   8.059 -12.155  1.00 68.83           N  
ATOM   1152  CA  HIS A 162       8.436   8.411 -13.354  1.00 70.54           C  
ATOM   1153  C   HIS A 162       7.992   7.582 -14.556  1.00 70.12           C  
ATOM   1154  O   HIS A 162       7.976   8.066 -15.688  1.00 70.92           O  
ATOM   1155  CB  HIS A 162       9.937   8.221 -13.104  1.00 72.75           C  
ATOM   1156  CG  HIS A 162      10.799   8.495 -14.297  1.00 72.23           C  
ATOM   1157  ND1 HIS A 162      10.737   9.673 -15.008  1.00 72.11           N  
ATOM   1158  CD2 HIS A 162      11.756   7.746 -14.896  1.00 72.47           C  
ATOM   1159  CE1 HIS A 162      11.612   9.636 -15.997  1.00 73.72           C  
ATOM   1160  NE2 HIS A 162      12.244   8.478 -15.952  1.00 73.10           N  
ATOM   1161  N   SER A 163       7.624   6.332 -14.299  1.00 68.34           N  
ATOM   1162  CA  SER A 163       7.206   5.427 -15.360  1.00 67.63           C  
ATOM   1163  C   SER A 163       5.742   5.631 -15.746  1.00 66.38           C  
ATOM   1164  O   SER A 163       5.382   5.505 -16.916  1.00 67.37           O  
ATOM   1165  CB  SER A 163       7.436   3.977 -14.937  1.00 66.97           C  
ATOM   1166  OG  SER A 163       8.798   3.745 -14.615  1.00 67.65           O  
ATOM   1167  N   ASP A 164       4.897   5.940 -14.767  1.00 65.90           N  
ATOM   1168  CA  ASP A 164       3.486   6.200 -15.043  1.00 65.64           C  
ATOM   1169  C   ASP A 164       3.327   7.461 -15.890  1.00 64.47           C  
ATOM   1170  O   ASP A 164       2.379   7.586 -16.667  1.00 66.33           O  
ATOM   1171  CB  ASP A 164       2.686   6.333 -13.743  1.00 68.19           C  
ATOM   1172  CG  ASP A 164       2.382   4.987 -13.096  1.00 69.64           C  
ATOM   1173  OD1 ASP A 164       2.125   4.008 -13.828  1.00 68.44           O  
ATOM   1174  OD2 ASP A 164       2.396   4.911 -11.849  1.00 73.67           O  
ATOM   1175  N   TYR A 165       4.266   8.391 -15.736  1.00 61.07           N  
ATOM   1176  CA  TYR A 165       4.272   9.621 -16.522  1.00 60.52           C  
ATOM   1177  C   TYR A 165       4.753   9.360 -17.942  1.00 58.75           C  
ATOM   1178  O   TYR A 165       4.234   9.936 -18.896  1.00 58.61           O  
ATOM   1179  CB  TYR A 165       5.158  10.682 -15.859  1.00 58.29           C  
ATOM   1180  CG  TYR A 165       5.279  11.969 -16.644  1.00 57.53           C  
ATOM   1181  CD1 TYR A 165       4.310  12.961 -16.539  1.00 57.78           C  
ATOM   1182  CD2 TYR A 165       6.367  12.200 -17.484  1.00 57.59           C  
ATOM   1183  CE1 TYR A 165       4.417  14.148 -17.252  1.00 60.01           C  
ATOM   1184  CE2 TYR A 165       6.484  13.384 -18.204  1.00 59.17           C  
ATOM   1185  CZ  TYR A 165       5.505  14.354 -18.082  1.00 60.22           C  
ATOM   1186  OH  TYR A 165       5.612  15.531 -18.790  1.00 60.37           O  
ATOM   1187  N   ILE A 166       5.762   8.505 -18.070  1.00 58.04           N  
ATOM   1188  CA  ILE A 166       6.279   8.119 -19.374  1.00 57.62           C  
ATOM   1189  C   ILE A 166       5.169   7.449 -20.172  1.00 59.12           C  
ATOM   1190  O   ILE A 166       4.953   7.769 -21.343  1.00 59.15           O  
ATOM   1191  CB  ILE A 166       7.499   7.181 -19.244  1.00 57.21           C  
ATOM   1192  CG1 ILE A 166       8.774   8.000 -19.014  1.00 56.24           C  
ATOM   1193  CG2 ILE A 166       7.652   6.304 -20.479  1.00 56.10           C  
ATOM   1194  CD1 ILE A 166      10.031   7.160 -18.892  1.00 54.96           C  
ATOM   1195  N   LEU A 167       4.451   6.539 -19.517  1.00 59.26           N  
ATOM   1196  CA  LEU A 167       3.301   5.872 -20.121  1.00 57.72           C  
ATOM   1197  C   LEU A 167       2.192   6.863 -20.477  1.00 58.67           C  
ATOM   1198  O   LEU A 167       1.530   6.721 -21.503  1.00 60.31           O  
ATOM   1199  CB  LEU A 167       2.759   4.791 -19.180  1.00 55.94           C  
ATOM   1200  CG  LEU A 167       3.639   3.557 -18.968  1.00 52.52           C  
ATOM   1201  CD1 LEU A 167       3.042   2.636 -17.917  1.00 50.40           C  
ATOM   1202  CD2 LEU A 167       3.837   2.815 -20.279  1.00 52.35           C  
ATOM   1203  N   ARG A 168       1.993   7.865 -19.626  1.00 59.05           N  
ATOM   1204  CA  ARG A 168       0.960   8.868 -19.858  1.00 64.37           C  
ATOM   1205  C   ARG A 168       1.236   9.699 -21.106  1.00 65.92           C  
ATOM   1206  O   ARG A 168       0.310  10.098 -21.814  1.00 67.08           O  
ATOM   1207  CB  ARG A 168       0.828   9.795 -18.647  1.00 70.67           C  
ATOM   1208  CG  ARG A 168      -0.124  10.970 -18.856  1.00 75.51           C  
ATOM   1209  CD  ARG A 168      -0.068  11.928 -17.689  1.00 79.46           C  
ATOM   1210  NE  ARG A 168      -0.381  11.248 -16.438  1.00 81.09           N  
ATOM   1211  CZ  ARG A 168      -0.118  11.742 -15.234  1.00 85.42           C  
ATOM   1212  NH1 ARG A 168      -0.440  11.047 -14.151  1.00 84.28           N  
ATOM   1213  NH2 ARG A 168       0.468  12.927 -15.115  1.00 88.20           N  
ATOM   1214  N   GLN A 169       2.511   9.962 -21.372  1.00 67.18           N  
ATOM   1215  CA  GLN A 169       2.883  10.809 -22.497  1.00 66.45           C  
ATOM   1216  C   GLN A 169       2.933  10.005 -23.795  1.00 64.47           C  
ATOM   1217  O   GLN A 169       3.307  10.521 -24.844  1.00 66.42           O  
ATOM   1218  CB  GLN A 169       4.227  11.493 -22.237  1.00 68.13           C  
ATOM   1219  CG  GLN A 169       4.262  12.345 -20.969  1.00 68.69           C  
ATOM   1220  CD  GLN A 169       3.251  13.474 -20.987  1.00 71.22           C  
ATOM   1221  OE1 GLN A 169       3.042  14.122 -22.012  1.00 73.69           O  
ATOM   1222  NE2 GLN A 169       2.616  13.716 -19.848  1.00 71.60           N  
ATOM   1223  N   LEU A 170       2.542   8.739 -23.716  1.00 61.18           N  
ATOM   1224  CA  LEU A 170       2.458   7.890 -24.895  1.00 59.39           C  
ATOM   1225  C   LEU A 170       1.119   8.080 -25.609  1.00 63.08           C  
ATOM   1226  O   LEU A 170       0.949   7.655 -26.756  1.00 70.43           O  
ATOM   1227  CB  LEU A 170       2.648   6.424 -24.507  1.00 53.96           C  
ATOM   1228  CG  LEU A 170       4.057   6.025 -24.067  1.00 49.87           C  
ATOM   1229  CD1 LEU A 170       4.095   4.575 -23.616  1.00 47.36           C  
ATOM   1230  CD2 LEU A 170       5.047   6.258 -25.195  1.00 50.25           C  
ATOM   1231  N   ARG A 171       0.172   8.718 -24.924  1.00 58.90           N  
ATOM   1232  CA  ARG A 171      -1.150   8.976 -25.489  1.00 57.89           C  
ATOM   1233  C   ARG A 171      -1.550  10.447 -25.418  1.00 62.33           C  
ATOM   1234  O   ARG A 171      -1.128  11.169 -24.514  1.00 63.02           O  
ATOM   1235  CB  ARG A 171      -2.218   8.153 -24.763  1.00 54.55           C  
ATOM   1236  CG  ARG A 171      -2.239   6.669 -25.075  1.00 50.83           C  
ATOM   1237  CD  ARG A 171      -3.426   6.008 -24.386  1.00 45.17           C  
ATOM   1238  NE  ARG A 171      -3.420   4.557 -24.532  1.00 44.31           N  
ATOM   1239  CZ  ARG A 171      -4.264   3.738 -23.909  1.00 44.86           C  
ATOM   1240  NH1 ARG A 171      -4.181   2.428 -24.104  1.00 43.32           N  
ATOM   1241  NH2 ARG A 171      -5.189   4.226 -23.089  1.00 44.53           N  
ATOM   1242  N   LYS A 172      -2.364  10.881 -26.379  1.00 65.91           N  
ATOM   1243  CA  LYS A 172      -3.168  12.086 -26.210  1.00 68.56           C  
ATOM   1244  C   LYS A 172      -4.429  11.639 -25.486  1.00 70.92           C  
ATOM   1245  O   LYS A 172      -4.826  10.482 -25.612  1.00 70.29           O  
ATOM   1246  CB  LYS A 172      -3.520  12.739 -27.546  1.00 56.70           C  
ATOM   1247  CG  LYS A 172      -2.361  12.965 -28.499  1.00 66.00           C  
ATOM   1248  CD  LYS A 172      -2.875  13.542 -29.817  1.00 69.93           C  
ATOM   1249  CE  LYS A 172      -1.822  13.502 -30.915  1.00 71.04           C  
ATOM   1250  NZ  LYS A 172      -2.403  13.821 -32.253  1.00 73.35           N  
ATOM   1251  N   PRO A 173      -5.060  12.533 -24.709  1.00 74.66           N  
ATOM   1252  CA  PRO A 173      -6.314  12.118 -24.070  1.00 74.71           C  
ATOM   1253  C   PRO A 173      -7.357  11.674 -25.101  1.00 76.67           C  
ATOM   1254  O   PRO A 173      -7.491  12.303 -26.152  1.00 81.07           O  
ATOM   1255  CB  PRO A 173      -6.765  13.382 -23.328  1.00 75.00           C  
ATOM   1256  CG  PRO A 173      -5.512  14.142 -23.084  1.00 74.98           C  
ATOM   1257  CD  PRO A 173      -4.644  13.882 -24.285  1.00 77.60           C  
ATOM   1258  N   GLY A 174      -8.063  10.585 -24.810  1.00 75.27           N  
ATOM   1259  CA  GLY A 174      -9.086  10.075 -25.704  1.00 76.28           C  
ATOM   1260  C   GLY A 174      -8.580   8.998 -26.649  1.00 74.79           C  
ATOM   1261  O   GLY A 174      -9.371   8.243 -27.220  1.00 75.93           O  
ATOM   1262  N   GLU A 175      -7.262   8.929 -26.812  1.00 73.07           N  
ATOM   1263  CA  GLU A 175      -6.645   7.957 -27.712  1.00 72.50           C  
ATOM   1264  C   GLU A 175      -6.780   6.522 -27.213  1.00 72.07           C  
ATOM   1265  O   GLU A 175      -6.750   6.260 -26.007  1.00 70.17           O  
ATOM   1266  CB  GLU A 175      -5.162   8.280 -27.927  1.00 71.29           C  
ATOM   1267  CG  GLU A 175      -4.894   9.422 -28.901  1.00 75.33           C  
ATOM   1268  CD  GLU A 175      -3.435   9.502 -29.324  1.00 76.47           C  
ATOM   1269  OE1 GLU A 175      -2.599   8.787 -28.730  1.00 72.90           O  
ATOM   1270  OE2 GLU A 175      -3.130  10.279 -30.256  1.00 79.09           O  
ATOM   1271  N   ILE A 176      -6.931   5.600 -28.159  1.00 73.35           N  
ATOM   1272  CA  ILE A 176      -6.925   4.175 -27.870  1.00 71.73           C  
ATOM   1273  C   ILE A 176      -5.767   3.548 -28.631  1.00 72.66           C  
ATOM   1274  O   ILE A 176      -5.896   3.198 -29.807  1.00 76.45           O  
ATOM   1275  CB  ILE A 176      -8.252   3.503 -28.262  1.00 72.77           C  
ATOM   1276  CG1 ILE A 176      -9.416   4.169 -27.529  1.00 73.50           C  
ATOM   1277  CG2 ILE A 176      -8.216   2.012 -27.959  1.00 70.96           C  
ATOM   1278  CD1 ILE A 176      -9.338   4.049 -26.024  1.00 72.88           C  
ATOM   1279  N   SER A 177      -4.629   3.425 -27.958  1.00 69.78           N  
ATOM   1280  CA  SER A 177      -3.406   3.002 -28.620  1.00 70.91           C  
ATOM   1281  C   SER A 177      -2.366   2.488 -27.639  1.00 69.04           C  
ATOM   1282  O   SER A 177      -2.357   2.865 -26.469  1.00 67.37           O  
ATOM   1283  CB  SER A 177      -2.817   4.159 -29.424  1.00 72.52           C  
ATOM   1284  OG  SER A 177      -2.590   5.286 -28.599  1.00 72.39           O  
ATOM   1285  N   TYR A 178      -1.484   1.630 -28.133  1.00 69.57           N  
ATOM   1286  CA  TYR A 178      -0.371   1.141 -27.336  1.00 66.12           C  
ATOM   1287  C   TYR A 178       0.934   1.309 -28.095  1.00 65.87           C  
ATOM   1288  O   TYR A 178       1.174   0.637 -29.098  1.00 67.89           O  
ATOM   1289  CB  TYR A 178      -0.588  -0.318 -26.948  1.00 66.87           C  
ATOM   1290  CG  TYR A 178      -1.685  -0.494 -25.932  1.00 67.19           C  
ATOM   1291  CD1 TYR A 178      -1.480  -0.158 -24.598  1.00 67.50           C  
ATOM   1292  CD2 TYR A 178      -2.928  -0.979 -26.304  1.00 67.98           C  
ATOM   1293  CE1 TYR A 178      -2.482  -0.306 -23.661  1.00 67.93           C  
ATOM   1294  CE2 TYR A 178      -3.938  -1.133 -25.375  1.00 70.53           C  
ATOM   1295  CZ  TYR A 178      -3.710  -0.795 -24.054  1.00 72.21           C  
ATOM   1296  OH  TYR A 178      -4.711  -0.946 -23.124  1.00 76.71           O  
ATOM   1297  N   ARG A 179       1.756   2.235 -27.617  1.00 64.72           N  
ATOM   1298  CA  ARG A 179       3.075   2.477 -28.183  1.00 65.98           C  
ATOM   1299  C   ARG A 179       4.132   1.800 -27.321  1.00 63.20           C  
ATOM   1300  O   ARG A 179       3.895   1.512 -26.146  1.00 60.92           O  
ATOM   1301  CB  ARG A 179       3.350   3.982 -28.295  1.00 69.80           C  
ATOM   1302  CG  ARG A 179       2.854   4.613 -29.591  1.00 75.87           C  
ATOM   1303  CD  ARG A 179       2.598   6.112 -29.459  1.00 81.29           C  
ATOM   1304  NE  ARG A 179       3.716   6.849 -28.868  1.00 84.65           N  
ATOM   1305  CZ  ARG A 179       4.814   7.211 -29.524  1.00 90.30           C  
ATOM   1306  NH1 ARG A 179       5.768   7.886 -28.896  1.00 90.72           N  
ATOM   1307  NH2 ARG A 179       4.967   6.894 -30.804  1.00 95.70           N  
ATOM   1308  N   ILE A 180       5.293   1.537 -27.914  1.00 63.19           N  
ATOM   1309  CA  ILE A 180       6.407   0.933 -27.192  1.00 61.05           C  
ATOM   1310  C   ILE A 180       7.002   1.912 -26.182  1.00 56.13           C  
ATOM   1311  O   ILE A 180       7.552   2.942 -26.566  1.00 55.72           O  
ATOM   1312  CB  ILE A 180       7.512   0.473 -28.158  1.00 62.69           C  
ATOM   1313  CG1 ILE A 180       6.964  -0.570 -29.133  1.00 65.43           C  
ATOM   1314  CG2 ILE A 180       8.705  -0.072 -27.384  1.00 61.46           C  
ATOM   1315  CD1 ILE A 180       7.923  -0.916 -30.250  1.00 68.21           C  
ATOM   1316  N   PRO A 181       6.896   1.587 -24.884  1.00 56.12           N  
ATOM   1317  CA  PRO A 181       7.397   2.486 -23.839  1.00 55.94           C  
ATOM   1318  C   PRO A 181       8.912   2.609 -23.869  1.00 60.20           C  
ATOM   1319  O   PRO A 181       9.630   1.640 -23.625  1.00 57.78           O  
ATOM   1320  CB  PRO A 181       6.919   1.825 -22.539  1.00 53.65           C  
ATOM   1321  CG  PRO A 181       6.727   0.393 -22.886  1.00 52.59           C  
ATOM   1322  CD  PRO A 181       6.302   0.358 -24.326  1.00 54.20           C  
ATOM   1323  N   GLN A 182       9.384   3.806 -24.184  1.00 65.92           N  
ATOM   1324  CA  GLN A 182      10.808   4.079 -24.207  1.00 71.91           C  
ATOM   1325  C   GLN A 182      11.157   5.102 -23.139  1.00 73.38           C  
ATOM   1326  O   GLN A 182      10.331   5.933 -22.770  1.00 73.09           O  
ATOM   1327  CB  GLN A 182      11.236   4.570 -25.588  1.00 76.34           C  
ATOM   1328  CG  GLN A 182      10.999   3.555 -26.689  1.00 77.96           C  
ATOM   1329  CD  GLN A 182      11.637   3.962 -28.001  1.00 83.73           C  
ATOM   1330  OE1 GLN A 182      12.228   5.037 -28.112  1.00 86.67           O  
ATOM   1331  NE2 GLN A 182      11.524   3.102 -29.007  1.00 84.90           N  
ATOM   1332  N   GLY A 183      12.384   5.034 -22.640  1.00 77.09           N  
ATOM   1333  CA  GLY A 183      12.819   5.948 -21.605  1.00 81.61           C  
ATOM   1334  C   GLY A 183      13.322   5.224 -20.374  1.00 84.44           C  
ATOM   1335  O   GLY A 183      13.370   3.996 -20.343  1.00 85.82           O  
ATOM   1336  N   GLY A 184      13.680   6.004 -19.358  1.00 87.09           N  
ATOM   1337  CA  GLY A 184      14.323   5.505 -18.156  1.00 86.09           C  
ATOM   1338  C   GLY A 184      13.734   4.249 -17.550  1.00 83.39           C  
ATOM   1339  O   GLY A 184      12.536   4.181 -17.274  1.00 87.08           O  
ATOM   1340  N   LEU A 185      14.593   3.247 -17.376  1.00 79.02           N  
ATOM   1341  CA  LEU A 185      14.257   1.976 -16.729  1.00 74.94           C  
ATOM   1342  C   LEU A 185      13.268   1.110 -17.517  1.00 70.35           C  
ATOM   1343  O   LEU A 185      13.130  -0.080 -17.237  1.00 67.94           O  
ATOM   1344  CB  LEU A 185      13.720   2.224 -15.317  1.00 73.57           C  
ATOM   1345  CG  LEU A 185      14.278   1.271 -14.258  1.00 72.52           C  
ATOM   1346  CD1 LEU A 185      15.787   1.171 -14.387  1.00 74.42           C  
ATOM   1347  CD2 LEU A 185      13.900   1.725 -12.862  1.00 71.89           C  
ATOM   1348  N   PHE A 186      12.586   1.693 -18.499  1.00 70.13           N  
ATOM   1349  CA  PHE A 186      11.767   0.903 -19.416  1.00 66.87           C  
ATOM   1350  C   PHE A 186      12.665   0.190 -20.419  1.00 67.98           C  
ATOM   1351  O   PHE A 186      12.271  -0.803 -21.028  1.00 66.45           O  
ATOM   1352  CB  PHE A 186      10.747   1.774 -20.156  1.00 64.66           C  
ATOM   1353  CG  PHE A 186       9.419   1.885 -19.460  1.00 61.76           C  
ATOM   1354  CD1 PHE A 186       8.593   0.780 -19.328  1.00 60.23           C  
ATOM   1355  CD2 PHE A 186       8.988   3.102 -18.953  1.00 62.12           C  
ATOM   1356  CE1 PHE A 186       7.363   0.884 -18.689  1.00 58.17           C  
ATOM   1357  CE2 PHE A 186       7.767   3.211 -18.319  1.00 60.17           C  
ATOM   1358  CZ  PHE A 186       6.951   2.097 -18.186  1.00 57.94           C  
ATOM   1359  N   THR A 187      13.880   0.706 -20.581  1.00 70.14           N  
ATOM   1360  CA  THR A 187      14.854   0.112 -21.486  1.00 72.78           C  
ATOM   1361  C   THR A 187      15.328  -1.246 -20.973  1.00 70.28           C  
ATOM   1362  O   THR A 187      15.912  -2.034 -21.718  1.00 71.91           O  
ATOM   1363  CB  THR A 187      16.080   1.032 -21.682  1.00 77.61           C  
ATOM   1364  OG1 THR A 187      16.919   0.975 -20.524  1.00 79.48           O  
ATOM   1365  CG2 THR A 187      15.646   2.469 -21.921  1.00 78.78           C  
ATOM   1366  N   TYR A 188      15.074  -1.512 -19.695  1.00 67.54           N  
ATOM   1367  CA  TYR A 188      15.470  -2.773 -19.083  1.00 65.92           C  
ATOM   1368  C   TYR A 188      14.272  -3.684 -18.837  1.00 61.82           C  
ATOM   1369  O   TYR A 188      14.339  -4.885 -19.102  1.00 61.31           O  
ATOM   1370  CB  TYR A 188      16.212  -2.519 -17.767  1.00 66.50           C  
ATOM   1371  CG  TYR A 188      17.358  -1.546 -17.901  1.00 69.26           C  
ATOM   1372  CD1 TYR A 188      18.547  -1.924 -18.510  1.00 73.02           C  
ATOM   1373  CD2 TYR A 188      17.253  -0.248 -17.421  1.00 69.95           C  
ATOM   1374  CE1 TYR A 188      19.597  -1.036 -18.638  1.00 75.81           C  
ATOM   1375  CE2 TYR A 188      18.299   0.646 -17.544  1.00 73.24           C  
ATOM   1376  CZ  TYR A 188      19.467   0.247 -18.153  1.00 76.32           C  
ATOM   1377  OH  TYR A 188      20.508   1.134 -18.278  1.00 80.88           O  
ATOM   1378  N   VAL A 189      13.179  -3.118 -18.325  1.00 57.48           N  
ATOM   1379  CA  VAL A 189      11.989  -3.916 -18.036  1.00 53.35           C  
ATOM   1380  C   VAL A 189      10.715  -3.340 -18.649  1.00 53.03           C  
ATOM   1381  O   VAL A 189      10.546  -2.124 -18.749  1.00 53.31           O  
ATOM   1382  CB  VAL A 189      11.768  -4.080 -16.515  1.00 50.53           C  
ATOM   1383  CG1 VAL A 189      12.934  -4.829 -15.894  1.00 49.75           C  
ATOM   1384  CG2 VAL A 189      11.567  -2.727 -15.846  1.00 50.95           C  
ATOM   1385  N   SER A 190       9.824  -4.241 -19.057  1.00 53.00           N  
ATOM   1386  CA  SER A 190       8.558  -3.872 -19.673  1.00 53.55           C  
ATOM   1387  C   SER A 190       7.616  -3.184 -18.685  1.00 54.83           C  
ATOM   1388  O   SER A 190       6.925  -2.225 -19.043  1.00 53.99           O  
ATOM   1389  CB  SER A 190       7.878  -5.110 -20.264  1.00 53.88           C  
ATOM   1390  OG  SER A 190       8.683  -5.707 -21.265  1.00 56.56           O  
ATOM   1391  N   GLY A 191       7.588  -3.676 -17.448  1.00 55.77           N  
ATOM   1392  CA  GLY A 191       6.738  -3.101 -16.420  1.00 54.23           C  
ATOM   1393  C   GLY A 191       7.527  -2.283 -15.416  1.00 55.41           C  
ATOM   1394  O   GLY A 191       7.646  -2.667 -14.251  1.00 55.54           O  
ATOM   1395  N   ALA A 192       8.058  -1.149 -15.864  1.00 57.78           N  
ATOM   1396  CA  ALA A 192       8.908  -0.307 -15.029  1.00 59.67           C  
ATOM   1397  C   ALA A 192       8.142   0.294 -13.853  1.00 59.94           C  
ATOM   1398  O   ALA A 192       8.643   0.320 -12.731  1.00 60.00           O  
ATOM   1399  CB  ALA A 192       9.539   0.793 -15.863  1.00 60.67           C  
ATOM   1400  N   ASN A 193       6.929   0.770 -14.116  1.00 61.16           N  
ATOM   1401  CA  ASN A 193       6.081   1.330 -13.066  1.00 64.83           C  
ATOM   1402  C   ASN A 193       5.718   0.294 -12.007  1.00 68.84           C  
ATOM   1403  O   ASN A 193       5.564   0.621 -10.833  1.00 76.88           O  
ATOM   1404  CB  ASN A 193       4.808   1.936 -13.666  1.00 63.03           C  
ATOM   1405  CG  ASN A 193       3.999   0.929 -14.458  1.00 60.56           C  
ATOM   1406  OD1 ASN A 193       4.544  -0.028 -15.005  1.00 60.32           O  
ATOM   1407  ND2 ASN A 193       2.688   1.142 -14.524  1.00 58.80           N  
ATOM   1408  N   PHE A 194       5.586  -0.957 -12.430  1.00 66.39           N  
ATOM   1409  CA  PHE A 194       5.296  -2.048 -11.508  1.00 64.80           C  
ATOM   1410  C   PHE A 194       6.510  -2.364 -10.649  1.00 64.61           C  
ATOM   1411  O   PHE A 194       6.381  -2.615  -9.453  1.00 68.54           O  
ATOM   1412  CB  PHE A 194       4.850  -3.298 -12.272  1.00 62.59           C  
ATOM   1413  CG  PHE A 194       3.595  -3.100 -13.065  1.00 61.26           C  
ATOM   1414  CD1 PHE A 194       2.645  -2.173 -12.664  1.00 60.25           C  
ATOM   1415  CD2 PHE A 194       3.366  -3.833 -14.214  1.00 61.44           C  
ATOM   1416  CE1 PHE A 194       1.490  -1.983 -13.391  1.00 58.67           C  
ATOM   1417  CE2 PHE A 194       2.213  -3.646 -14.947  1.00 58.69           C  
ATOM   1418  CZ  PHE A 194       1.273  -2.718 -14.533  1.00 58.36           C  
ATOM   1419  N   LEU A 195       7.686  -2.357 -11.270  1.00 59.59           N  
ATOM   1420  CA  LEU A 195       8.936  -2.570 -10.554  1.00 58.45           C  
ATOM   1421  C   LEU A 195       9.070  -1.557  -9.424  1.00 61.07           C  
ATOM   1422  O   LEU A 195       9.404  -1.915  -8.295  1.00 59.92           O  
ATOM   1423  CB  LEU A 195      10.134  -2.466 -11.504  1.00 56.40           C  
ATOM   1424  CG  LEU A 195      11.510  -2.694 -10.876  1.00 54.35           C  
ATOM   1425  CD1 LEU A 195      11.630  -4.112 -10.335  1.00 39.23           C  
ATOM   1426  CD2 LEU A 195      12.628  -2.400 -11.870  1.00 54.49           C  
ATOM   1427  N   GLY A 196       8.790  -0.296  -9.736  1.00 60.85           N  
ATOM   1428  CA  GLY A 196       8.859   0.763  -8.750  1.00 63.61           C  
ATOM   1429  C   GLY A 196       7.909   0.553  -7.590  1.00 66.05           C  
ATOM   1430  O   GLY A 196       8.310   0.617  -6.432  1.00 67.59           O  
ATOM   1431  N   GLU A 197       6.644   0.293  -7.902  1.00 66.26           N  
ATOM   1432  CA  GLU A 197       5.629   0.075  -6.877  1.00 65.33           C  
ATOM   1433  C   GLU A 197       5.977  -1.115  -5.982  1.00 61.84           C  
ATOM   1434  O   GLU A 197       5.748  -1.073  -4.775  1.00 62.80           O  
ATOM   1435  CB  GLU A 197       4.253  -0.133  -7.519  1.00 62.45           C  
ATOM   1436  CG  GLU A 197       3.107  -0.245  -6.524  1.00 61.07           C  
ATOM   1437  CD  GLU A 197       2.101   0.880  -6.660  1.00 61.00           C  
ATOM   1438  OE1 GLU A 197       1.091   0.865  -5.922  1.00 61.41           O  
ATOM   1439  OE2 GLU A 197       2.323   1.776  -7.507  1.00 60.51           O  
ATOM   1440  N   ILE A 198       6.531  -2.168  -6.575  1.00 58.71           N  
ATOM   1441  CA  ILE A 198       6.921  -3.354  -5.817  1.00 58.99           C  
ATOM   1442  C   ILE A 198       8.059  -3.023  -4.864  1.00 63.78           C  
ATOM   1443  O   ILE A 198       8.033  -3.400  -3.693  1.00 67.76           O  
ATOM   1444  CB  ILE A 198       7.341  -4.510  -6.742  1.00 56.38           C  
ATOM   1445  CG1 ILE A 198       6.106  -5.147  -7.379  1.00 54.13           C  
ATOM   1446  CG2 ILE A 198       8.116  -5.559  -5.969  1.00 57.80           C  
ATOM   1447  CD1 ILE A 198       6.416  -6.369  -8.218  1.00 52.93           C  
ATOM   1448  N   ILE A 199       9.057  -2.313  -5.374  1.00 61.80           N  
ATOM   1449  CA  ILE A 199      10.143  -1.810  -4.543  1.00 61.90           C  
ATOM   1450  C   ILE A 199       9.583  -0.927  -3.425  1.00 62.77           C  
ATOM   1451  O   ILE A 199      10.039  -0.983  -2.281  1.00 64.46           O  
ATOM   1452  CB  ILE A 199      11.168  -1.014  -5.385  1.00 60.40           C  
ATOM   1453  CG1 ILE A 199      11.857  -1.940  -6.392  1.00 60.05           C  
ATOM   1454  CG2 ILE A 199      12.203  -0.351  -4.501  1.00 63.41           C  
ATOM   1455  CD1 ILE A 199      12.637  -1.210  -7.468  1.00 59.63           C  
ATOM   1456  N   GLU A 200       8.569  -0.135  -3.763  1.00 61.63           N  
ATOM   1457  CA  GLU A 200       7.973   0.814  -2.831  1.00 64.57           C  
ATOM   1458  C   GLU A 200       7.349   0.137  -1.611  1.00 65.41           C  
ATOM   1459  O   GLU A 200       7.522   0.603  -0.485  1.00 67.53           O  
ATOM   1460  CB  GLU A 200       6.920   1.664  -3.549  1.00 67.52           C  
ATOM   1461  CG  GLU A 200       6.357   2.821  -2.722  1.00 72.56           C  
ATOM   1462  CD  GLU A 200       5.346   3.660  -3.496  1.00 75.19           C  
ATOM   1463  OE1 GLU A 200       4.945   3.251  -4.609  1.00 72.76           O  
ATOM   1464  OE2 GLU A 200       4.954   4.733  -2.990  1.00 80.11           O  
ATOM   1465  N   TRP A 201       6.624  -0.957  -1.827  1.00 65.07           N  
ATOM   1466  CA  TRP A 201       5.927  -1.623  -0.724  1.00 67.16           C  
ATOM   1467  C   TRP A 201       6.819  -2.592   0.052  1.00 69.11           C  
ATOM   1468  O   TRP A 201       6.552  -2.887   1.220  1.00 70.45           O  
ATOM   1469  CB  TRP A 201       4.686  -2.362  -1.238  1.00 66.17           C  
ATOM   1470  CG  TRP A 201       3.660  -1.454  -1.854  1.00 64.75           C  
ATOM   1471  CD1 TRP A 201       3.124  -1.555  -3.103  1.00 63.43           C  
ATOM   1472  CD2 TRP A 201       3.057  -0.300  -1.252  1.00 66.91           C  
ATOM   1473  NE1 TRP A 201       2.222  -0.542  -3.316  1.00 64.60           N  
ATOM   1474  CE2 TRP A 201       2.164   0.242  -2.196  1.00 65.97           C  
ATOM   1475  CE3 TRP A 201       3.184   0.325  -0.007  1.00 70.00           C  
ATOM   1476  CZ2 TRP A 201       1.403   1.378  -1.935  1.00 68.33           C  
ATOM   1477  CZ3 TRP A 201       2.429   1.454   0.249  1.00 72.36           C  
ATOM   1478  CH2 TRP A 201       1.549   1.969  -0.711  1.00 72.20           C  
ATOM   1479  N   ILE A 202       7.869  -3.092  -0.589  1.00 69.52           N  
ATOM   1480  CA  ILE A 202       8.827  -3.943   0.106  1.00 66.82           C  
ATOM   1481  C   ILE A 202       9.584  -3.107   1.131  1.00 66.96           C  
ATOM   1482  O   ILE A 202       9.765  -3.522   2.277  1.00 69.23           O  
ATOM   1483  CB  ILE A 202       9.816  -4.617  -0.869  1.00 63.69           C  
ATOM   1484  CG1 ILE A 202       9.096  -5.685  -1.695  1.00 60.70           C  
ATOM   1485  CG2 ILE A 202      10.984  -5.242  -0.111  1.00 65.35           C  
ATOM   1486  CD1 ILE A 202       9.969  -6.347  -2.738  1.00 59.48           C  
ATOM   1487  N   GLY A 203      10.010  -1.921   0.716  1.00 66.25           N  
ATOM   1488  CA  GLY A 203      10.655  -0.989   1.621  1.00 68.71           C  
ATOM   1489  C   GLY A 203       9.697  -0.553   2.712  1.00 71.18           C  
ATOM   1490  O   GLY A 203      10.096  -0.364   3.862  1.00 76.57           O  
ATOM   1491  N   TYR A 204       8.427  -0.398   2.345  1.00 66.84           N  
ATOM   1492  CA  TYR A 204       7.395   0.001   3.294  1.00 65.83           C  
ATOM   1493  C   TYR A 204       7.200  -1.069   4.362  1.00 66.33           C  
ATOM   1494  O   TYR A 204       7.021  -0.759   5.539  1.00 69.28           O  
ATOM   1495  CB  TYR A 204       6.077   0.272   2.568  1.00 63.32           C  
ATOM   1496  CG  TYR A 204       4.964   0.743   3.475  1.00 64.90           C  
ATOM   1497  CD1 TYR A 204       4.966   2.031   3.997  1.00 67.24           C  
ATOM   1498  CD2 TYR A 204       3.906  -0.094   3.805  1.00 63.94           C  
ATOM   1499  CE1 TYR A 204       3.949   2.471   4.826  1.00 68.77           C  
ATOM   1500  CE2 TYR A 204       2.888   0.335   4.629  1.00 66.95           C  
ATOM   1501  CZ  TYR A 204       2.913   1.618   5.139  1.00 68.94           C  
ATOM   1502  OH  TYR A 204       1.899   2.052   5.963  1.00 71.36           O  
ATOM   1503  N   ALA A 205       7.240  -2.328   3.945  1.00 63.59           N  
ATOM   1504  CA  ALA A 205       7.157  -3.440   4.884  1.00 63.87           C  
ATOM   1505  C   ALA A 205       8.395  -3.459   5.775  1.00 67.19           C  
ATOM   1506  O   ALA A 205       8.329  -3.809   6.955  1.00 64.70           O  
ATOM   1507  CB  ALA A 205       7.013  -4.761   4.137  1.00 58.98           C  
ATOM   1508  N   LEU A 206       9.525  -3.071   5.194  1.00 65.08           N  
ATOM   1509  CA  LEU A 206      10.796  -3.077   5.903  1.00 68.21           C  
ATOM   1510  C   LEU A 206      10.858  -1.941   6.919  1.00 73.24           C  
ATOM   1511  O   LEU A 206      11.423  -2.092   8.004  1.00 71.03           O  
ATOM   1512  CB  LEU A 206      11.952  -2.973   4.904  1.00 65.71           C  
ATOM   1513  CG  LEU A 206      13.374  -3.133   5.437  1.00 69.24           C  
ATOM   1514  CD1 LEU A 206      13.493  -4.383   6.291  1.00 70.53           C  
ATOM   1515  CD2 LEU A 206      14.358  -3.182   4.278  1.00 69.08           C  
ATOM   1516  N   ALA A 207      10.262  -0.807   6.566  1.00 75.51           N  
ATOM   1517  CA  ALA A 207      10.263   0.365   7.430  1.00 80.62           C  
ATOM   1518  C   ALA A 207       9.252   0.230   8.566  1.00 85.53           C  
ATOM   1519  O   ALA A 207       9.438   0.808   9.635  1.00 89.30           O  
ATOM   1520  CB  ALA A 207       9.980   1.618   6.620  1.00 79.38           C  
ATOM   1521  N   THR A 208       8.182  -0.524   8.331  1.00 85.88           N  
ATOM   1522  CA  THR A 208       7.167  -0.746   9.359  1.00 88.92           C  
ATOM   1523  C   THR A 208       7.459  -2.003  10.161  1.00 92.33           C  
ATOM   1524  O   THR A 208       7.026  -2.125  11.309  1.00 95.17           O  
ATOM   1525  CB  THR A 208       5.751  -0.876   8.765  1.00 87.19           C  
ATOM   1526  OG1 THR A 208       5.701  -2.007   7.885  1.00 85.27           O  
ATOM   1527  CG2 THR A 208       5.361   0.382   8.010  1.00 84.83           C  
ATOM   1528  N   TRP A 209       8.185  -2.934   9.542  1.00 89.40           N  
ATOM   1529  CA  TRP A 209       8.473  -4.232  10.146  1.00 89.34           C  
ATOM   1530  C   TRP A 209       7.179  -4.884  10.621  1.00 90.90           C  
ATOM   1531  O   TRP A 209       7.123  -5.473  11.700  1.00 94.89           O  
ATOM   1532  CB  TRP A 209       9.460  -4.081  11.305  1.00 90.24           C  
ATOM   1533  CG  TRP A 209      10.195  -5.338  11.644  1.00 89.06           C  
ATOM   1534  CD1 TRP A 209      10.049  -6.099  12.767  1.00 91.17           C  
ATOM   1535  CD2 TRP A 209      11.196  -5.982  10.848  1.00 83.98           C  
ATOM   1536  NE1 TRP A 209      10.899  -7.175  12.720  1.00 83.48           N  
ATOM   1537  CE2 TRP A 209      11.615  -7.127  11.552  1.00 85.17           C  
ATOM   1538  CE3 TRP A 209      11.780  -5.700   9.609  1.00 78.99           C  
ATOM   1539  CZ2 TRP A 209      12.591  -7.991  11.059  1.00 84.04           C  
ATOM   1540  CZ3 TRP A 209      12.748  -6.558   9.120  1.00 78.28           C  
ATOM   1541  CH2 TRP A 209      13.144  -7.690   9.844  1.00 81.06           C  
ATOM   1542  N   SER A 210       6.133  -4.758   9.810  1.00 88.77           N  
ATOM   1543  CA  SER A 210       4.814  -5.225  10.208  1.00 89.48           C  
ATOM   1544  C   SER A 210       4.295  -6.329   9.298  1.00 84.95           C  
ATOM   1545  O   SER A 210       4.582  -6.355   8.101  1.00 80.86           O  
ATOM   1546  CB  SER A 210       3.823  -4.060  10.237  1.00 88.76           C  
ATOM   1547  OG  SER A 210       3.749  -3.412   8.984  1.00 83.60           O  
ATOM   1548  N   LEU A 211       3.532  -7.242   9.889  1.00 85.83           N  
ATOM   1549  CA  LEU A 211       2.918  -8.341   9.157  1.00 84.15           C  
ATOM   1550  C   LEU A 211       1.951  -7.882   8.052  1.00 79.99           C  
ATOM   1551  O   LEU A 211       2.045  -8.367   6.923  1.00 74.34           O  
ATOM   1552  CB  LEU A 211       2.189  -9.273  10.130  1.00 88.46           C  
ATOM   1553  CG  LEU A 211       1.808 -10.655   9.604  1.00 88.36           C  
ATOM   1554  CD1 LEU A 211       2.878 -11.676   9.965  1.00 89.93           C  
ATOM   1555  CD2 LEU A 211       0.451 -11.075  10.138  1.00 91.28           C  
ATOM   1556  N   PRO A 212       1.019  -6.953   8.363  1.00 80.71           N  
ATOM   1557  CA  PRO A 212       0.071  -6.595   7.299  1.00 78.85           C  
ATOM   1558  C   PRO A 212       0.716  -5.867   6.118  1.00 76.51           C  
ATOM   1559  O   PRO A 212       0.210  -5.963   5.000  1.00 78.11           O  
ATOM   1560  CB  PRO A 212      -0.930  -5.682   8.016  1.00 81.76           C  
ATOM   1561  CG  PRO A 212      -0.173  -5.118   9.157  1.00 82.23           C  
ATOM   1562  CD  PRO A 212       0.724  -6.224   9.612  1.00 82.92           C  
ATOM   1563  N   ALA A 213       1.812  -5.153   6.359  1.00 75.31           N  
ATOM   1564  CA  ALA A 213       2.522  -4.475   5.280  1.00 71.11           C  
ATOM   1565  C   ALA A 213       3.256  -5.483   4.402  1.00 68.55           C  
ATOM   1566  O   ALA A 213       3.312  -5.325   3.186  1.00 65.45           O  
ATOM   1567  CB  ALA A 213       3.494  -3.449   5.835  1.00 71.42           C  
ATOM   1568  N   LEU A 214       3.818  -6.514   5.027  1.00 70.85           N  
ATOM   1569  CA  LEU A 214       4.508  -7.575   4.300  1.00 68.32           C  
ATOM   1570  C   LEU A 214       3.523  -8.315   3.405  1.00 69.94           C  
ATOM   1571  O   LEU A 214       3.864  -8.751   2.304  1.00 70.58           O  
ATOM   1572  CB  LEU A 214       5.182  -8.549   5.270  1.00 69.11           C  
ATOM   1573  CG  LEU A 214       6.000  -9.693   4.660  1.00 65.92           C  
ATOM   1574  CD1 LEU A 214       7.227  -9.158   3.946  1.00 63.51           C  
ATOM   1575  CD2 LEU A 214       6.397 -10.707   5.720  1.00 67.94           C  
ATOM   1576  N   ALA A 215       2.294  -8.447   3.895  1.00 71.44           N  
ATOM   1577  CA  ALA A 215       1.233  -9.119   3.160  1.00 70.99           C  
ATOM   1578  C   ALA A 215       0.847  -8.333   1.911  1.00 67.77           C  
ATOM   1579  O   ALA A 215       0.776  -8.889   0.815  1.00 66.94           O  
ATOM   1580  CB  ALA A 215       0.016  -9.326   4.059  1.00 73.31           C  
ATOM   1581  N   PHE A 216       0.595  -7.039   2.086  1.00 68.47           N  
ATOM   1582  CA  PHE A 216       0.234  -6.168   0.974  1.00 65.74           C  
ATOM   1583  C   PHE A 216       1.355  -6.113  -0.053  1.00 61.63           C  
ATOM   1584  O   PHE A 216       1.110  -6.053  -1.259  1.00 61.85           O  
ATOM   1585  CB  PHE A 216      -0.096  -4.760   1.473  1.00 68.13           C  
ATOM   1586  CG  PHE A 216      -0.513  -3.813   0.381  1.00 68.44           C  
ATOM   1587  CD1 PHE A 216      -1.489  -4.176  -0.536  1.00 69.32           C  
ATOM   1588  CD2 PHE A 216       0.065  -2.561   0.276  1.00 68.84           C  
ATOM   1589  CE1 PHE A 216      -1.874  -3.310  -1.546  1.00 69.69           C  
ATOM   1590  CE2 PHE A 216      -0.315  -1.687  -0.728  1.00 69.03           C  
ATOM   1591  CZ  PHE A 216      -1.286  -2.062  -1.641  1.00 69.58           C  
ATOM   1592  N   ALA A 217       2.587  -6.140   0.435  1.00 59.87           N  
ATOM   1593  CA  ALA A 217       3.752  -6.172  -0.433  1.00 58.70           C  
ATOM   1594  C   ALA A 217       3.775  -7.471  -1.225  1.00 57.64           C  
ATOM   1595  O   ALA A 217       4.108  -7.486  -2.408  1.00 53.54           O  
ATOM   1596  CB  ALA A 217       5.026  -6.022   0.379  1.00 59.78           C  
ATOM   1597  N   PHE A 218       3.411  -8.562  -0.561  1.00 59.92           N  
ATOM   1598  CA  PHE A 218       3.367  -9.862  -1.212  1.00 60.45           C  
ATOM   1599  C   PHE A 218       2.267  -9.904  -2.265  1.00 63.98           C  
ATOM   1600  O   PHE A 218       2.446 -10.487  -3.336  1.00 66.65           O  
ATOM   1601  CB  PHE A 218       3.158 -10.977  -0.188  1.00 60.54           C  
ATOM   1602  CG  PHE A 218       2.987 -12.329  -0.804  1.00 60.82           C  
ATOM   1603  CD1 PHE A 218       4.088 -13.039  -1.258  1.00 61.09           C  
ATOM   1604  CD2 PHE A 218       1.725 -12.889  -0.946  1.00 61.74           C  
ATOM   1605  CE1 PHE A 218       3.935 -14.289  -1.839  1.00 61.30           C  
ATOM   1606  CE2 PHE A 218       1.565 -14.138  -1.526  1.00 62.45           C  
ATOM   1607  CZ  PHE A 218       2.670 -14.838  -1.971  1.00 61.90           C  
ATOM   1608  N   PHE A 219       1.127  -9.292  -1.956  1.00 63.51           N  
ATOM   1609  CA  PHE A 219       0.030  -9.210  -2.909  1.00 63.58           C  
ATOM   1610  C   PHE A 219       0.471  -8.434  -4.136  1.00 63.24           C  
ATOM   1611  O   PHE A 219       0.327  -8.901  -5.265  1.00 63.80           O  
ATOM   1612  CB  PHE A 219      -1.197  -8.543  -2.280  1.00 65.01           C  
ATOM   1613  CG  PHE A 219      -2.259  -8.166  -3.281  1.00 63.80           C  
ATOM   1614  CD1 PHE A 219      -3.172  -9.109  -3.732  1.00 64.17           C  
ATOM   1615  CD2 PHE A 219      -2.341  -6.873  -3.773  1.00 61.40           C  
ATOM   1616  CE1 PHE A 219      -4.146  -8.770  -4.655  1.00 62.58           C  
ATOM   1617  CE2 PHE A 219      -3.310  -6.528  -4.703  1.00 61.31           C  
ATOM   1618  CZ  PHE A 219      -4.217  -7.476  -5.140  1.00 61.74           C  
ATOM   1619  N   SER A 220       1.011  -7.244  -3.896  1.00 64.67           N  
ATOM   1620  CA  SER A 220       1.472  -6.364  -4.962  1.00 64.29           C  
ATOM   1621  C   SER A 220       2.497  -7.060  -5.847  1.00 62.55           C  
ATOM   1622  O   SER A 220       2.501  -6.883  -7.063  1.00 60.69           O  
ATOM   1623  CB  SER A 220       2.059  -5.078  -4.372  1.00 63.21           C  
ATOM   1624  OG  SER A 220       1.076  -4.364  -3.639  1.00 64.03           O  
ATOM   1625  N   LEU A 221       3.359  -7.859  -5.226  1.00 65.32           N  
ATOM   1626  CA  LEU A 221       4.341  -8.649  -5.958  1.00 63.44           C  
ATOM   1627  C   LEU A 221       3.656  -9.673  -6.859  1.00 62.68           C  
ATOM   1628  O   LEU A 221       3.982  -9.787  -8.040  1.00 61.94           O  
ATOM   1629  CB  LEU A 221       5.288  -9.354  -4.990  1.00 64.45           C  
ATOM   1630  CG  LEU A 221       6.189 -10.427  -5.601  1.00 64.88           C  
ATOM   1631  CD1 LEU A 221       7.156  -9.818  -6.606  1.00 62.04           C  
ATOM   1632  CD2 LEU A 221       6.936 -11.177  -4.510  1.00 68.71           C  
ATOM   1633  N   CYS A 222       2.707 -10.413  -6.294  1.00 62.84           N  
ATOM   1634  CA  CYS A 222       1.928 -11.379  -7.057  1.00 64.28           C  
ATOM   1635  C   CYS A 222       1.138 -10.715  -8.189  1.00 63.83           C  
ATOM   1636  O   CYS A 222       1.237 -11.121  -9.351  1.00 61.28           O  
ATOM   1637  CB  CYS A 222       0.969 -12.139  -6.135  1.00 65.28           C  
ATOM   1638  SG  CYS A 222       1.751 -13.357  -5.051  1.00 62.77           S  
ATOM   1639  N   PHE A 223       0.361  -9.692  -7.846  1.00 62.44           N  
ATOM   1640  CA  PHE A 223      -0.537  -9.066  -8.810  1.00 61.14           C  
ATOM   1641  C   PHE A 223       0.220  -8.320  -9.911  1.00 63.62           C  
ATOM   1642  O   PHE A 223       0.067  -8.626 -11.092  1.00 67.45           O  
ATOM   1643  CB  PHE A 223      -1.503  -8.112  -8.097  1.00 56.96           C  
ATOM   1644  CG  PHE A 223      -2.553  -7.524  -9.000  1.00 50.56           C  
ATOM   1645  CD1 PHE A 223      -3.718  -8.223  -9.276  1.00 49.05           C  
ATOM   1646  CD2 PHE A 223      -2.373  -6.273  -9.575  1.00 45.61           C  
ATOM   1647  CE1 PHE A 223      -4.685  -7.689 -10.111  1.00 48.41           C  
ATOM   1648  CE2 PHE A 223      -3.334  -5.731 -10.407  1.00 44.11           C  
ATOM   1649  CZ  PHE A 223      -4.493  -6.438 -10.675  1.00 46.38           C  
ATOM   1650  N   LEU A 224       1.033  -7.344  -9.519  1.00 63.52           N  
ATOM   1651  CA  LEU A 224       1.774  -6.529 -10.479  1.00 61.80           C  
ATOM   1652  C   LEU A 224       2.850  -7.335 -11.208  1.00 58.85           C  
ATOM   1653  O   LEU A 224       3.216  -7.013 -12.334  1.00 56.02           O  
ATOM   1654  CB  LEU A 224       2.409  -5.324  -9.779  1.00 63.80           C  
ATOM   1655  CG  LEU A 224       1.443  -4.354  -9.089  1.00 67.10           C  
ATOM   1656  CD1 LEU A 224       2.203  -3.300  -8.305  1.00 69.68           C  
ATOM   1657  CD2 LEU A 224       0.514  -3.698 -10.100  1.00 66.33           C  
ATOM   1658  N   GLY A 225       3.356  -8.379 -10.558  1.00 59.54           N  
ATOM   1659  CA  GLY A 225       4.335  -9.256 -11.172  1.00 60.23           C  
ATOM   1660  C   GLY A 225       3.729 -10.071 -12.301  1.00 60.92           C  
ATOM   1661  O   GLY A 225       4.392 -10.371 -13.297  1.00 58.30           O  
ATOM   1662  N   LEU A 226       2.461 -10.436 -12.142  1.00 61.31           N  
ATOM   1663  CA  LEU A 226       1.731 -11.139 -13.189  1.00 62.18           C  
ATOM   1664  C   LEU A 226       1.312 -10.156 -14.272  1.00 63.27           C  
ATOM   1665  O   LEU A 226       1.384 -10.450 -15.467  1.00 68.38           O  
ATOM   1666  CB  LEU A 226       0.505 -11.850 -12.617  1.00 62.19           C  
ATOM   1667  CG  LEU A 226      -0.368 -12.551 -13.657  1.00 61.28           C  
ATOM   1668  CD1 LEU A 226       0.433 -13.617 -14.390  1.00 60.83           C  
ATOM   1669  CD2 LEU A 226      -1.606 -13.149 -13.012  1.00 62.52           C  
ATOM   1670  N   ARG A 227       0.874  -8.981 -13.835  1.00 60.86           N  
ATOM   1671  CA  ARG A 227       0.493  -7.908 -14.740  1.00 58.62           C  
ATOM   1672  C   ARG A 227       1.668  -7.503 -15.634  1.00 56.89           C  
ATOM   1673  O   ARG A 227       1.490  -7.236 -16.821  1.00 56.06           O  
ATOM   1674  CB  ARG A 227      -0.029  -6.706 -13.940  1.00 58.49           C  
ATOM   1675  CG  ARG A 227      -0.572  -5.573 -14.794  1.00 58.26           C  
ATOM   1676  CD  ARG A 227      -1.713  -4.830 -14.116  1.00 54.82           C  
ATOM   1677  NE  ARG A 227      -2.969  -5.064 -14.820  1.00 55.17           N  
ATOM   1678  CZ  ARG A 227      -3.372  -4.375 -15.884  1.00 54.10           C  
ATOM   1679  NH1 ARG A 227      -4.531  -4.659 -16.461  1.00 53.97           N  
ATOM   1680  NH2 ARG A 227      -2.619  -3.399 -16.373  1.00 53.15           N  
ATOM   1681  N   ALA A 228       2.870  -7.479 -15.060  1.00 55.75           N  
ATOM   1682  CA  ALA A 228       4.082  -7.125 -15.795  1.00 53.53           C  
ATOM   1683  C   ALA A 228       4.417  -8.173 -16.845  1.00 52.59           C  
ATOM   1684  O   ALA A 228       4.837  -7.849 -17.961  1.00 48.66           O  
ATOM   1685  CB  ALA A 228       5.246  -6.958 -14.841  1.00 52.22           C  
ATOM   1686  N   PHE A 229       4.239  -9.432 -16.472  1.00 55.93           N  
ATOM   1687  CA  PHE A 229       4.542 -10.537 -17.366  1.00 59.56           C  
ATOM   1688  C   PHE A 229       3.630 -10.516 -18.592  1.00 65.05           C  
ATOM   1689  O   PHE A 229       4.081 -10.735 -19.715  1.00 72.88           O  
ATOM   1690  CB  PHE A 229       4.417 -11.866 -16.623  1.00 58.54           C  
ATOM   1691  CG  PHE A 229       4.330 -13.051 -17.524  1.00 60.83           C  
ATOM   1692  CD1 PHE A 229       5.449 -13.506 -18.195  1.00 61.24           C  
ATOM   1693  CD2 PHE A 229       3.123 -13.710 -17.706  1.00 62.45           C  
ATOM   1694  CE1 PHE A 229       5.368 -14.596 -19.031  1.00 64.16           C  
ATOM   1695  CE2 PHE A 229       3.036 -14.800 -18.541  1.00 64.39           C  
ATOM   1696  CZ  PHE A 229       4.158 -15.243 -19.205  1.00 66.01           C  
ATOM   1697  N   HIS A 230       2.351 -10.240 -18.374  1.00 61.47           N  
ATOM   1698  CA  HIS A 230       1.392 -10.212 -19.468  1.00 57.94           C  
ATOM   1699  C   HIS A 230       1.645  -9.035 -20.390  1.00 56.51           C  
ATOM   1700  O   HIS A 230       1.491  -9.142 -21.607  1.00 58.70           O  
ATOM   1701  CB  HIS A 230      -0.028 -10.180 -18.920  1.00 54.68           C  
ATOM   1702  CG  HIS A 230      -0.500 -11.513 -18.439  1.00 55.43           C  
ATOM   1703  ND1 HIS A 230      -0.586 -12.609 -19.270  1.00 58.14           N  
ATOM   1704  CD2 HIS A 230      -0.888 -11.938 -17.214  1.00 55.89           C  
ATOM   1705  CE1 HIS A 230      -1.018 -13.649 -18.581  1.00 59.00           C  
ATOM   1706  NE2 HIS A 230      -1.209 -13.268 -17.331  1.00 58.25           N  
ATOM   1707  N   HIS A 231       2.036  -7.913 -19.799  1.00 54.50           N  
ATOM   1708  CA  HIS A 231       2.449  -6.744 -20.562  1.00 54.17           C  
ATOM   1709  C   HIS A 231       3.660  -7.065 -21.430  1.00 52.45           C  
ATOM   1710  O   HIS A 231       3.748  -6.639 -22.580  1.00 54.03           O  
ATOM   1711  CB  HIS A 231       2.773  -5.581 -19.624  1.00 55.60           C  
ATOM   1712  CG  HIS A 231       1.567  -4.822 -19.173  1.00 58.43           C  
ATOM   1713  ND1 HIS A 231       0.291  -5.337 -19.256  1.00 63.27           N  
ATOM   1714  CD2 HIS A 231       1.438  -3.579 -18.653  1.00 57.36           C  
ATOM   1715  CE1 HIS A 231      -0.571  -4.446 -18.799  1.00 61.10           C  
ATOM   1716  NE2 HIS A 231       0.100  -3.370 -18.427  1.00 59.17           N  
ATOM   1717  N   HIS A 232       4.593  -7.815 -20.856  1.00 49.93           N  
ATOM   1718  CA  HIS A 232       5.786  -8.250 -21.565  1.00 48.49           C  
ATOM   1719  C   HIS A 232       5.396  -9.160 -22.724  1.00 51.41           C  
ATOM   1720  O   HIS A 232       5.909  -9.016 -23.834  1.00 49.35           O  
ATOM   1721  CB  HIS A 232       6.733  -8.972 -20.610  1.00 46.19           C  
ATOM   1722  CG  HIS A 232       8.111  -9.172 -21.157  1.00 45.58           C  
ATOM   1723  ND1 HIS A 232       8.874  -8.136 -21.653  1.00 44.11           N  
ATOM   1724  CD2 HIS A 232       8.870 -10.289 -21.273  1.00 47.64           C  
ATOM   1725  CE1 HIS A 232      10.041  -8.607 -22.056  1.00 47.39           C  
ATOM   1726  NE2 HIS A 232      10.064  -9.910 -21.835  1.00 48.19           N  
ATOM   1727  N   ARG A 233       4.490 -10.096 -22.452  1.00 52.19           N  
ATOM   1728  CA  ARG A 233       3.945 -10.980 -23.474  1.00 52.83           C  
ATOM   1729  C   ARG A 233       3.325 -10.177 -24.601  1.00 53.20           C  
ATOM   1730  O   ARG A 233       3.568 -10.446 -25.777  1.00 54.82           O  
ATOM   1731  CB  ARG A 233       2.894 -11.920 -22.877  1.00 57.62           C  
ATOM   1732  CG  ARG A 233       3.436 -13.242 -22.382  1.00 66.04           C  
ATOM   1733  CD  ARG A 233       2.749 -14.413 -23.080  1.00 74.66           C  
ATOM   1734  NE  ARG A 233       3.346 -15.694 -22.705  1.00 82.68           N  
ATOM   1735  CZ  ARG A 233       4.452 -16.192 -23.253  1.00 88.69           C  
ATOM   1736  NH1 ARG A 233       4.929 -17.365 -22.852  1.00 90.58           N  
ATOM   1737  NH2 ARG A 233       5.087 -15.514 -24.202  1.00 88.49           N  
ATOM   1738  N   PHE A 234       2.522  -9.188 -24.222  1.00 52.29           N  
ATOM   1739  CA  PHE A 234       1.786  -8.365 -25.174  1.00 52.78           C  
ATOM   1740  C   PHE A 234       2.726  -7.665 -26.155  1.00 52.21           C  
ATOM   1741  O   PHE A 234       2.504  -7.687 -27.363  1.00 54.00           O  
ATOM   1742  CB  PHE A 234       0.931  -7.341 -24.424  1.00 52.91           C  
ATOM   1743  CG  PHE A 234       0.110  -6.457 -25.321  1.00 55.00           C  
ATOM   1744  CD1 PHE A 234      -1.169  -6.822 -25.682  1.00 56.40           C  
ATOM   1745  CD2 PHE A 234       0.620  -5.257 -25.795  1.00 57.03           C  
ATOM   1746  CE1 PHE A 234      -1.921  -6.015 -26.505  1.00 59.87           C  
ATOM   1747  CE2 PHE A 234      -0.128  -4.445 -26.619  1.00 58.30           C  
ATOM   1748  CZ  PHE A 234      -1.403  -4.825 -26.975  1.00 61.05           C  
ATOM   1749  N   TYR A 235       3.778  -7.051 -25.625  1.00 52.31           N  
ATOM   1750  CA  TYR A 235       4.754  -6.337 -26.442  1.00 53.65           C  
ATOM   1751  C   TYR A 235       5.470  -7.258 -27.426  1.00 54.20           C  
ATOM   1752  O   TYR A 235       5.627  -6.924 -28.601  1.00 55.58           O  
ATOM   1753  CB  TYR A 235       5.779  -5.646 -25.548  1.00 54.81           C  
ATOM   1754  CG  TYR A 235       5.199  -4.545 -24.693  1.00 56.33           C  
ATOM   1755  CD1 TYR A 235       4.137  -3.776 -25.146  1.00 56.78           C  
ATOM   1756  CD2 TYR A 235       5.715  -4.276 -23.428  1.00 57.01           C  
ATOM   1757  CE1 TYR A 235       3.604  -2.766 -24.364  1.00 59.30           C  
ATOM   1758  CE2 TYR A 235       5.190  -3.271 -22.643  1.00 56.02           C  
ATOM   1759  CZ  TYR A 235       4.135  -2.518 -23.113  1.00 57.85           C  
ATOM   1760  OH  TYR A 235       3.611  -1.513 -22.329  1.00 57.64           O  
ATOM   1761  N   LEU A 236       5.903  -8.415 -26.935  1.00 53.62           N  
ATOM   1762  CA  LEU A 236       6.591  -9.401 -27.761  1.00 56.78           C  
ATOM   1763  C   LEU A 236       5.654  -9.995 -28.809  1.00 62.35           C  
ATOM   1764  O   LEU A 236       6.093 -10.454 -29.864  1.00 64.95           O  
ATOM   1765  CB  LEU A 236       7.169 -10.512 -26.884  1.00 55.64           C  
ATOM   1766  CG  LEU A 236       8.215 -10.058 -25.868  1.00 53.07           C  
ATOM   1767  CD1 LEU A 236       8.461 -11.141 -24.832  1.00 53.03           C  
ATOM   1768  CD2 LEU A 236       9.502  -9.686 -26.582  1.00 52.36           C  
ATOM   1769  N   LYS A 237       4.362  -9.976 -28.505  1.00 62.83           N  
ATOM   1770  CA  LYS A 237       3.345 -10.521 -29.390  1.00 67.17           C  
ATOM   1771  C   LYS A 237       2.947  -9.521 -30.474  1.00 68.59           C  
ATOM   1772  O   LYS A 237       2.641  -9.911 -31.606  1.00 73.62           O  
ATOM   1773  CB  LYS A 237       2.105 -10.920 -28.586  1.00 70.85           C  
ATOM   1774  CG  LYS A 237       1.790 -12.408 -28.536  1.00 78.44           C  
ATOM   1775  CD  LYS A 237       0.445 -12.618 -27.841  1.00 78.37           C  
ATOM   1776  CE  LYS A 237       0.103 -14.083 -27.627  1.00 81.26           C  
ATOM   1777  NZ  LYS A 237      -1.133 -14.224 -26.798  1.00 81.30           N  
ATOM   1778  N   MET A 238       2.954  -8.235 -30.123  1.00 65.25           N  
ATOM   1779  CA  MET A 238       2.367  -7.202 -30.979  1.00 65.31           C  
ATOM   1780  C   MET A 238       3.390  -6.319 -31.687  1.00 67.21           C  
ATOM   1781  O   MET A 238       3.045  -5.602 -32.626  1.00 67.43           O  
ATOM   1782  CB  MET A 238       1.421  -6.322 -30.159  1.00 61.48           C  
ATOM   1783  CG  MET A 238       0.284  -7.085 -29.502  1.00 60.53           C  
ATOM   1784  SD  MET A 238      -0.974  -7.639 -30.659  1.00 59.46           S  
ATOM   1785  CE  MET A 238      -1.708  -8.979 -29.720  1.00 76.00           C  
ATOM   1786  N   PHE A 239       4.641  -6.366 -31.237  1.00 68.53           N  
ATOM   1787  CA  PHE A 239       5.693  -5.551 -31.838  1.00 70.84           C  
ATOM   1788  C   PHE A 239       6.878  -6.404 -32.281  1.00 78.13           C  
ATOM   1789  O   PHE A 239       7.572  -6.994 -31.453  1.00 78.16           O  
ATOM   1790  CB  PHE A 239       6.160  -4.469 -30.863  1.00 66.27           C  
ATOM   1791  CG  PHE A 239       5.106  -3.441 -30.548  1.00 62.56           C  
ATOM   1792  CD1 PHE A 239       4.861  -2.391 -31.422  1.00 61.82           C  
ATOM   1793  CD2 PHE A 239       4.360  -3.524 -29.382  1.00 58.14           C  
ATOM   1794  CE1 PHE A 239       3.887  -1.438 -31.139  1.00 57.35           C  
ATOM   1795  CE2 PHE A 239       3.385  -2.576 -29.096  1.00 56.17           C  
ATOM   1796  CZ  PHE A 239       3.152  -1.534 -29.977  1.00 54.84           C  
ATOM   1797  N   GLU A 240       7.103  -6.454 -33.591  1.00 85.64           N  
ATOM   1798  CA  GLU A 240       8.160  -7.274 -34.172  1.00 92.20           C  
ATOM   1799  C   GLU A 240       9.540  -6.710 -33.861  1.00 92.64           C  
ATOM   1800  O   GLU A 240      10.531  -7.444 -33.838  1.00 97.79           O  
ATOM   1801  CB  GLU A 240       7.971  -7.395 -35.690  1.00100.41           C  
ATOM   1802  CG  GLU A 240       8.138  -6.091 -36.475  1.00107.42           C  
ATOM   1803  CD  GLU A 240       6.938  -5.157 -36.368  1.00109.27           C  
ATOM   1804  OE1 GLU A 240       5.936  -5.531 -35.721  1.00106.84           O  
ATOM   1805  OE2 GLU A 240       6.997  -4.046 -36.935  1.00110.71           O  
ATOM   1806  N   ASP A 241       9.601  -5.405 -33.618  1.00 90.73           N  
ATOM   1807  CA  ASP A 241      10.869  -4.739 -33.350  1.00 90.61           C  
ATOM   1808  C   ASP A 241      10.986  -4.296 -31.892  1.00 83.38           C  
ATOM   1809  O   ASP A 241      11.706  -3.349 -31.581  1.00 82.74           O  
ATOM   1810  CB  ASP A 241      11.043  -3.539 -34.288  1.00 96.73           C  
ATOM   1811  CG  ASP A 241      11.357  -3.957 -35.722  1.00104.30           C  
ATOM   1812  OD1 ASP A 241      12.258  -4.802 -35.911  1.00107.45           O  
ATOM   1813  OD2 ASP A 241      10.702  -3.447 -36.658  1.00106.62           O  
ATOM   1814  N   TYR A 242      10.282  -4.986 -30.998  1.00 78.03           N  
ATOM   1815  CA  TYR A 242      10.365  -4.692 -29.569  1.00 73.54           C  
ATOM   1816  C   TYR A 242      11.694  -5.192 -29.006  1.00 71.29           C  
ATOM   1817  O   TYR A 242      12.089  -6.328 -29.271  1.00 71.91           O  
ATOM   1818  CB  TYR A 242       9.189  -5.327 -28.815  1.00 69.93           C  
ATOM   1819  CG  TYR A 242       9.106  -4.939 -27.355  1.00 66.75           C  
ATOM   1820  CD1 TYR A 242       8.452  -3.776 -26.960  1.00 64.67           C  
ATOM   1821  CD2 TYR A 242       9.681  -5.734 -26.369  1.00 66.24           C  
ATOM   1822  CE1 TYR A 242       8.378  -3.414 -25.624  1.00 63.67           C  
ATOM   1823  CE2 TYR A 242       9.610  -5.383 -25.028  1.00 63.43           C  
ATOM   1824  CZ  TYR A 242       8.958  -4.224 -24.662  1.00 62.18           C  
ATOM   1825  OH  TYR A 242       8.886  -3.875 -23.333  1.00 60.67           O  
ATOM   1826  N   PRO A 243      12.392  -4.337 -28.237  1.00 70.97           N  
ATOM   1827  CA  PRO A 243      13.712  -4.645 -27.670  1.00 70.97           C  
ATOM   1828  C   PRO A 243      13.729  -5.951 -26.887  1.00 71.54           C  
ATOM   1829  O   PRO A 243      13.059  -6.083 -25.860  1.00 70.28           O  
ATOM   1830  CB  PRO A 243      13.983  -3.453 -26.752  1.00 70.86           C  
ATOM   1831  CG  PRO A 243      13.235  -2.337 -27.383  1.00 70.15           C  
ATOM   1832  CD  PRO A 243      11.974  -2.962 -27.918  1.00 69.48           C  
ATOM   1833  N   LYS A 244      14.507  -6.906 -27.380  1.00 72.81           N  
ATOM   1834  CA  LYS A 244      14.493  -8.262 -26.852  1.00 72.75           C  
ATOM   1835  C   LYS A 244      15.502  -8.455 -25.724  1.00 71.99           C  
ATOM   1836  O   LYS A 244      15.654  -9.556 -25.194  1.00 72.34           O  
ATOM   1837  CB  LYS A 244      14.752  -9.249 -27.988  1.00 75.57           C  
ATOM   1838  CG  LYS A 244      13.695  -9.176 -29.081  1.00 76.64           C  
ATOM   1839  CD  LYS A 244      14.158  -9.828 -30.368  1.00 81.91           C  
ATOM   1840  CE  LYS A 244      13.155  -9.597 -31.485  1.00 82.50           C  
ATOM   1841  NZ  LYS A 244      12.907  -8.146 -31.717  1.00 81.02           N  
ATOM   1842  N   SER A 245      16.185  -7.376 -25.360  1.00 72.54           N  
ATOM   1843  CA  SER A 245      17.061  -7.384 -24.197  1.00 72.27           C  
ATOM   1844  C   SER A 245      16.239  -7.106 -22.949  1.00 69.99           C  
ATOM   1845  O   SER A 245      16.664  -7.378 -21.829  1.00 69.59           O  
ATOM   1846  CB  SER A 245      18.163  -6.340 -24.338  1.00 74.38           C  
ATOM   1847  OG  SER A 245      17.613  -5.033 -24.321  1.00 72.56           O  
ATOM   1848  N   ARG A 246      15.053  -6.549 -23.157  1.00 67.75           N  
ATOM   1849  CA  ARG A 246      14.181  -6.193 -22.053  1.00 64.84           C  
ATOM   1850  C   ARG A 246      13.657  -7.439 -21.353  1.00 63.35           C  
ATOM   1851  O   ARG A 246      13.523  -8.497 -21.964  1.00 62.96           O  
ATOM   1852  CB  ARG A 246      13.015  -5.333 -22.543  1.00 62.11           C  
ATOM   1853  CG  ARG A 246      13.411  -3.957 -23.046  1.00 62.74           C  
ATOM   1854  CD  ARG A 246      12.167  -3.160 -23.404  1.00 62.56           C  
ATOM   1855  NE  ARG A 246      12.464  -1.790 -23.814  1.00 63.68           N  
ATOM   1856  CZ  ARG A 246      11.540  -0.843 -23.947  1.00 62.55           C  
ATOM   1857  NH1 ARG A 246      10.269  -1.122 -23.691  1.00 61.94           N  
ATOM   1858  NH2 ARG A 246      11.879   0.382 -24.323  1.00 63.16           N  
ATOM   1859  N   LYS A 247      13.386  -7.306 -20.061  1.00 61.02           N  
ATOM   1860  CA  LYS A 247      12.731  -8.361 -19.307  1.00 61.26           C  
ATOM   1861  C   LYS A 247      11.358  -7.869 -18.864  1.00 58.06           C  
ATOM   1862  O   LYS A 247      10.976  -6.738 -19.153  1.00 57.08           O  
ATOM   1863  CB  LYS A 247      13.579  -8.785 -18.107  1.00 61.60           C  
ATOM   1864  CG  LYS A 247      14.885  -9.460 -18.486  1.00 63.60           C  
ATOM   1865  CD  LYS A 247      14.650 -10.565 -19.500  1.00 66.54           C  
ATOM   1866  CE  LYS A 247      15.931 -11.310 -19.813  1.00 70.07           C  
ATOM   1867  NZ  LYS A 247      16.414 -12.080 -18.636  1.00 71.89           N  
ATOM   1868  N   ALA A 248      10.615  -8.717 -18.165  1.00 56.86           N  
ATOM   1869  CA  ALA A 248       9.252  -8.375 -17.788  1.00 56.56           C  
ATOM   1870  C   ALA A 248       9.187  -7.467 -16.556  1.00 57.09           C  
ATOM   1871  O   ALA A 248       8.406  -6.512 -16.527  1.00 55.05           O  
ATOM   1872  CB  ALA A 248       8.444  -9.642 -17.547  1.00 56.51           C  
ATOM   1873  N   LEU A 249      10.000  -7.757 -15.542  1.00 56.48           N  
ATOM   1874  CA  LEU A 249       9.850  -7.080 -14.256  1.00 56.86           C  
ATOM   1875  C   LEU A 249      11.167  -6.806 -13.539  1.00 58.23           C  
ATOM   1876  O   LEU A 249      11.489  -5.664 -13.216  1.00 57.94           O  
ATOM   1877  CB  LEU A 249       8.947  -7.905 -13.340  1.00 55.16           C  
ATOM   1878  CG  LEU A 249       8.698  -7.286 -11.968  1.00 53.65           C  
ATOM   1879  CD1 LEU A 249       7.908  -5.995 -12.117  1.00 51.37           C  
ATOM   1880  CD2 LEU A 249       7.980  -8.267 -11.059  1.00 53.95           C  
ATOM   1881  N   ILE A 250      11.905  -7.872 -13.257  1.00 60.80           N  
ATOM   1882  CA  ILE A 250      13.194  -7.755 -12.594  1.00 63.06           C  
ATOM   1883  C   ILE A 250      14.299  -7.745 -13.642  1.00 66.49           C  
ATOM   1884  O   ILE A 250      14.425  -8.691 -14.417  1.00 65.36           O  
ATOM   1885  CB  ILE A 250      13.425  -8.908 -11.592  1.00 65.52           C  
ATOM   1886  CG1 ILE A 250      12.274  -8.969 -10.583  1.00 64.46           C  
ATOM   1887  CG2 ILE A 250      14.768  -8.754 -10.884  1.00 64.88           C  
ATOM   1888  CD1 ILE A 250      12.368 -10.120  -9.605  1.00 65.73           C  
ATOM   1889  N   PRO A 251      15.088  -6.659 -13.680  1.00 67.84           N  
ATOM   1890  CA  PRO A 251      16.187  -6.497 -14.637  1.00 71.66           C  
ATOM   1891  C   PRO A 251      17.116  -7.706 -14.705  1.00 76.86           C  
ATOM   1892  O   PRO A 251      17.558  -8.217 -13.673  1.00 78.75           O  
ATOM   1893  CB  PRO A 251      16.924  -5.271 -14.102  1.00 69.61           C  
ATOM   1894  CG  PRO A 251      15.845  -4.457 -13.487  1.00 68.16           C  
ATOM   1895  CD  PRO A 251      14.893  -5.448 -12.863  1.00 67.20           C  
ATOM   1896  N   PHE A 252      17.370  -8.164 -15.929  1.00 78.79           N  
ATOM   1897  CA  PHE A 252      18.323  -9.235 -16.217  1.00 84.69           C  
ATOM   1898  C   PHE A 252      17.927 -10.589 -15.622  1.00 85.13           C  
ATOM   1899  O   PHE A 252      18.718 -11.532 -15.648  1.00 90.82           O  
ATOM   1900  CB  PHE A 252      19.724  -8.845 -15.725  1.00 91.63           C  
ATOM   1901  CG  PHE A 252      20.121  -7.434 -16.073  1.00 96.73           C  
ATOM   1902  CD1 PHE A 252      20.468  -7.093 -17.372  1.00101.58           C  
ATOM   1903  CD2 PHE A 252      20.157  -6.450 -15.097  1.00 97.31           C  
ATOM   1904  CE1 PHE A 252      20.837  -5.793 -17.694  1.00102.26           C  
ATOM   1905  CE2 PHE A 252      20.521  -5.151 -15.409  1.00 99.47           C  
ATOM   1906  CZ  PHE A 252      20.863  -4.822 -16.709  1.00101.09           C  
ATOM   1907  N   ILE A 253      16.710 -10.692 -15.098  1.00 81.33           N  
ATOM   1908  CA  ILE A 253      16.270 -11.930 -14.453  1.00 81.50           C  
ATOM   1909  C   ILE A 253      14.926 -12.420 -14.990  1.00 78.43           C  
ATOM   1910  O   ILE A 253      14.860 -13.450 -15.663  1.00 79.94           O  
ATOM   1911  CB  ILE A 253      16.171 -11.761 -12.921  1.00 80.04           C  
ATOM   1912  CG1 ILE A 253      17.544 -11.437 -12.333  1.00 79.77           C  
ATOM   1913  CG2 ILE A 253      15.611 -13.018 -12.275  1.00 82.53           C  
ATOM   1914  CD1 ILE A 253      17.567 -11.370 -10.826  1.00 78.43           C  
ATOM   1915  N   PHE A 254      13.857 -11.689 -14.687  1.00 76.02           N  
ATOM   1916  CA  PHE A 254      12.526 -12.064 -15.154  1.00 75.76           C  
ATOM   1917  C   PHE A 254      11.817 -10.911 -15.862  1.00 74.74           C  
ATOM   1918  O   PHE A 254      11.389 -11.046 -17.014  1.00 74.90           O  
ATOM   1919  CB  PHE A 254      11.666 -12.559 -13.990  1.00 76.33           C  
ATOM   1920  CG  PHE A 254      10.235 -12.810 -14.364  1.00 77.24           C  
ATOM   1921  CD1 PHE A 254       9.890 -13.914 -15.130  1.00 79.69           C  
ATOM   1922  CD2 PHE A 254       9.235 -11.941 -13.955  1.00 75.01           C  
ATOM   1923  CE1 PHE A 254       8.572 -14.150 -15.484  1.00 78.63           C  
ATOM   1924  CE2 PHE A 254       7.915 -12.170 -14.303  1.00 74.81           C  
ATOM   1925  CZ  PHE A 254       7.584 -13.278 -15.070  1.00 76.94           C  
ATOM   1926  OXT PHE A 254      11.655  -9.825 -15.299  1.00 72.93           O  
HETATM 1928  C18 OLC A 601      12.958 -11.604  14.076  1.00 73.56           C  
HETATM 1929  C10 OLC A 601      14.584 -11.120   5.265  1.00 86.11           C  
HETATM 1930  C9  OLC A 601      13.813 -11.133   4.177  1.00 87.22           C  
HETATM 1931  C17 OLC A 601      12.908 -11.385  12.579  1.00 74.34           C  
HETATM 1932  C11 OLC A 601      14.433 -10.044   6.317  1.00 83.89           C  
HETATM 1933  C8  OLC A 601      12.748 -10.079   3.959  1.00 88.59           C  
HETATM 1934  C24 OLC A 601       7.368  -9.132  11.075  1.00 88.76           C  
HETATM 1935  C16 OLC A 601      12.935 -12.712  11.830  1.00 74.17           C  
HETATM 1936  C12 OLC A 601      14.790 -10.596   7.692  1.00 81.96           C  
HETATM 1937  C7  OLC A 601      13.212  -9.058   2.921  1.00 89.01           C  
HETATM 1938  C15 OLC A 601      12.736 -12.503  10.334  1.00 76.22           C  
HETATM 1939  C13 OLC A 601      13.703 -11.517   8.232  1.00 79.43           C  
HETATM 1940  C6  OLC A 601      12.066  -8.527   2.058  1.00 89.50           C  
HETATM 1941  C14 OLC A 601      13.936 -11.800   9.711  1.00 77.08           C  
HETATM 1942  C5  OLC A 601      10.909  -7.959   2.879  1.00 90.23           C  
HETATM 1943  C4  OLC A 601      11.319  -6.743   3.704  1.00 90.45           C  
HETATM 1944  C3  OLC A 601      11.202  -7.040   5.198  1.00 91.53           C  
HETATM 1945  C2  OLC A 601       9.799  -6.790   5.744  1.00 91.04           C  
HETATM 1946  C21 OLC A 601       8.035  -8.427   8.752  1.00 89.85           C  
HETATM 1947  C1  OLC A 601       9.457  -7.854   6.762  1.00 90.85           C  
HETATM 1948  C22 OLC A 601       8.505  -8.620  10.195  1.00 89.00           C  
HETATM 1949  O19 OLC A 601       9.653  -9.027   6.495  1.00 91.00           O  
HETATM 1950  O25 OLC A 601       7.878  -9.439  12.379  1.00 87.45           O  
HETATM 1951  O23 OLC A 601       9.558  -9.588  10.217  1.00 88.91           O  
HETATM 1952  O20 OLC A 601       8.893  -7.510   8.064  1.00 90.40           O  
HETATM 1953  N1  NDX A 602      -5.753  -1.143  -7.454  1.00 57.89           N  
HETATM 1954  C2  NDX A 602      -3.877  -2.606  -7.010  1.00 58.25           C  
HETATM 1955  N2  NDX A 602      -9.135 -10.131  -8.876  1.00 67.67           N  
HETATM 1956  C4  NDX A 602      -6.438  -2.232  -8.154  1.00 55.44           C  
HETATM 1957  C5  NDX A 602      -7.922  -1.941  -8.363  1.00 54.83           C  
HETATM 1958  C6  NDX A 602      -8.619  -3.104  -9.066  1.00 53.37           C  
HETATM 1959  O1  NDX A 602      -3.929  -0.316  -6.444  1.00 64.29           O  
HETATM 1960  O2  NDX A 602     -11.199  -9.444  -8.249  1.00 69.27           O  
HETATM 1961  C1  NDX A 602      -4.743  -3.789  -7.251  1.00 57.15           C  
HETATM 1962  C3  NDX A 602      -4.511  -1.269  -6.958  1.00 60.33           C  
HETATM 1963  C7  NDX A 602      -8.435  -4.419  -8.315  1.00 53.11           C  
HETATM 1964  C8  NDX A 602      -6.935  -4.716  -8.102  1.00 50.85           C  
HETATM 1965  C9  NDX A 602      -6.229  -3.540  -7.348  1.00 56.62           C  
HETATM 1966  C10 NDX A 602      -6.716  -6.104  -7.478  1.00 50.25           C  
HETATM 1967  C11 NDX A 602      -7.456  -7.228  -8.215  1.00 49.38           C  
HETATM 1968  C12 NDX A 602      -8.948  -6.940  -8.321  1.00 51.73           C  
HETATM 1969  C13 NDX A 602      -9.083  -5.587  -9.044  1.00 52.36           C  
HETATM 1970  C14 NDX A 602     -10.567  -5.500  -9.416  1.00 55.93           C  
HETATM 1971  C15 NDX A 602     -10.990  -6.964  -9.663  1.00 60.35           C  
HETATM 1972  C16 NDX A 602      -9.764  -7.837  -9.297  1.00 63.06           C  
HETATM 1973  C17 NDX A 602      -9.603  -6.929  -6.931  1.00 51.06           C  
HETATM 1974  C18 NDX A 602      -6.749  -3.375  -5.901  1.00 56.21           C  
HETATM 1975  C19 NDX A 602     -10.106  -9.218  -8.768  1.00 66.49           C  
HETATM 1976  C20 NDX A 602      -9.127 -11.481  -8.263  1.00 67.57           C  
HETATM 1977  C21 NDX A 602      -7.831 -12.176  -8.654  1.00 66.99           C  
HETATM 1978  C22 NDX A 602     -10.315 -12.287  -8.771  1.00 68.87           C  
HETATM 1979  C23 NDX A 602      -9.200 -11.331  -6.750  1.00 68.78           C  
HETATM 1980  O3X NDX A 602      -5.830   1.708 -21.548  1.00 49.95           O  
HETATM 1981  P2B NDX A 602      -4.889   1.408 -20.398  1.00 50.47           P  
HETATM 1982  O1X NDX A 602      -4.160   0.089 -20.577  1.00 54.63           O  
HETATM 1983  O2X NDX A 602      -5.581   1.501 -19.048  1.00 51.99           O  
HETATM 1984  O2B NDX A 602      -3.774   2.570 -20.520  1.00 42.52           O  
HETATM 1985  C2B NDX A 602      -2.750   2.471 -19.531  1.00 44.96           C  
HETATM 1986  C1B NDX A 602      -1.494   3.219 -19.964  1.00 45.15           C  
HETATM 1987  N9A NDX A 602      -0.598   2.409 -20.777  1.00 44.78           N  
HETATM 1988  C4A NDX A 602      -0.141   2.653 -22.053  1.00 45.70           C  
HETATM 1989  N3A NDX A 602      -0.448   3.681 -22.857  1.00 45.16           N  
HETATM 1990  C2A NDX A 602       0.180   3.573 -24.026  1.00 44.32           C  
HETATM 1991  N1A NDX A 602       1.020   2.623 -24.457  1.00 45.68           N  
HETATM 1992  C6A NDX A 602       1.311   1.597 -23.626  1.00 45.21           C  
HETATM 1993  N6A NDX A 602       2.146   0.647 -24.042  1.00 44.17           N  
HETATM 1994  C5A NDX A 602       0.704   1.601 -22.354  1.00 45.14           C  
HETATM 1995  N7A NDX A 602       0.783   0.726 -21.281  1.00 45.54           N  
HETATM 1996  C8A NDX A 602       0.003   1.247 -20.371  1.00 43.57           C  
HETATM 1997  O4B NDX A 602      -0.803   3.529 -18.777  1.00 44.61           O  
HETATM 1998  C3B NDX A 602      -3.083   3.147 -18.203  1.00 44.99           C  
HETATM 1999  O3B NDX A 602      -3.800   4.358 -18.395  1.00 45.82           O  
HETATM 2000  C4B NDX A 602      -1.691   3.452 -17.631  1.00 44.57           C  
HETATM 2001  C5B NDX A 602      -1.138   2.436 -16.661  1.00 45.05           C  
HETATM 2002  O5B NDX A 602      -1.339   1.105 -17.191  1.00 47.34           O  
HETATM 2003  PA  NDX A 602      -0.610  -0.124 -16.469  1.00 48.90           P  
HETATM 2004  O1A NDX A 602      -1.187  -1.409 -16.957  1.00 57.94           O  
HETATM 2005  O2A NDX A 602       0.867   0.058 -16.578  1.00 46.88           O  
HETATM 2006  O3  NDX A 602      -1.053   0.106 -14.946  1.00 63.29           O  
HETATM 2007  PN  NDX A 602      -2.421  -0.041 -14.128  1.00 45.71           P  
HETATM 2008  O1N NDX A 602      -2.752  -1.488 -13.978  1.00 45.24           O  
HETATM 2009  O2N NDX A 602      -3.445   0.850 -14.742  1.00 46.32           O  
HETATM 2010  O5D NDX A 602      -1.969   0.564 -12.715  1.00 55.92           O  
HETATM 2011  C5D NDX A 602      -1.684   1.981 -12.660  1.00 55.21           C  
HETATM 2012  C4D NDX A 602      -0.911   2.297 -11.404  1.00 54.21           C  
HETATM 2013  C3D NDX A 602       0.546   1.817 -11.366  1.00 53.19           C  
HETATM 2014  O3D NDX A 602       1.345   2.717 -10.610  1.00 53.37           O  
HETATM 2015  C2D NDX A 602       0.387   0.505 -10.612  1.00 51.85           C  
HETATM 2016  O2D NDX A 602       1.596   0.007 -10.064  1.00 52.80           O  
HETATM 2017  C1D NDX A 602      -0.623   0.910  -9.545  1.00 52.20           C  
HETATM 2018  O4D NDX A 602      -1.565   1.649 -10.283  1.00 53.66           O  
HETATM 2019  N1N NDX A 602      -1.321  -0.271  -8.962  1.00 54.29           N  
HETATM 2020  C6N NDX A 602      -2.403  -0.820  -9.617  1.00 55.90           C  
HETATM 2021  C5N NDX A 602      -3.051  -1.864  -9.148  1.00 55.49           C  
HETATM 2022  C4N NDX A 602      -2.662  -2.516  -7.889  1.00 55.91           C  
HETATM 2023  C3N NDX A 602      -1.477  -1.910  -7.213  1.00 56.11           C  
HETATM 2024  C2N NDX A 602      -0.882  -0.821  -7.789  1.00 55.22           C  
HETATM 2025  C7N NDX A 602      -0.887  -2.413  -5.948  1.00 56.54           C  
HETATM 2026  O7N NDX A 602      -1.309  -3.460  -5.447  1.00 56.35           O  
HETATM 2027  N7N NDX A 602       0.083  -1.708  -5.384  1.00 56.83           N  
HETATM 2028  S   SO4 A 603      -4.839  -6.312 -19.022  1.00 98.19           S  
HETATM 2029  O1  SO4 A 603      -5.198  -6.566 -17.630  1.00 99.34           O  
HETATM 2030  O2  SO4 A 603      -3.962  -5.146 -19.093  1.00 99.24           O  
HETATM 2031  O3  SO4 A 603      -4.146  -7.475 -19.570  1.00 99.01           O  
HETATM 2032  O4  SO4 A 603      -6.053  -6.054 -19.790  1.00 98.39           O  
HETATM 2033  S   SO4 A 604      15.002   9.253 -18.620  1.00138.17           S  
HETATM 2034  O1  SO4 A 604      15.313  10.670 -18.799  1.00138.13           O  
HETATM 2035  O2  SO4 A 604      15.711   8.741 -17.450  1.00138.23           O  
HETATM 2036  O3  SO4 A 604      15.422   8.510 -19.805  1.00138.29           O  
HETATM 2037  O4  SO4 A 604      13.564   9.094 -18.429  1.00138.45           O  
CONECT    6  923                                                                
CONECT  923    6                                                                
CONECT 1928 1931                                                                
CONECT 1929 1930 1932                                                           
CONECT 1930 1929 1933                                                           
CONECT 1931 1928 1935                                                           
CONECT 1932 1929 1936                                                           
CONECT 1933 1930 1937                                                           
CONECT 1934 1948 1950                                                           
CONECT 1935 1931 1938                                                           
CONECT 1936 1932 1939                                                           
CONECT 1937 1933 1940                                                           
CONECT 1938 1935 1941                                                           
CONECT 1939 1936 1941                                                           
CONECT 1940 1937 1942                                                           
CONECT 1941 1938 1939                                                           
CONECT 1942 1940 1943                                                           
CONECT 1943 1942 1944                                                           
CONECT 1944 1943 1945                                                           
CONECT 1945 1944 1947                                                           
CONECT 1946 1948 1952                                                           
CONECT 1947 1945 1949 1952                                                      
CONECT 1948 1934 1946 1951                                                      
CONECT 1949 1947                                                                
CONECT 1950 1934                                                                
CONECT 1951 1948                                                                
CONECT 1952 1946 1947                                                           
CONECT 1953 1956 1962                                                           
CONECT 1954 1961 1962 2022                                                      
CONECT 1955 1975 1976                                                           
CONECT 1956 1953 1957 1965                                                      
CONECT 1957 1956 1958                                                           
CONECT 1958 1957 1963                                                           
CONECT 1959 1962                                                                
CONECT 1960 1975                                                                
CONECT 1961 1954 1965                                                           
CONECT 1962 1953 1954 1959                                                      
CONECT 1963 1958 1964 1969                                                      
CONECT 1964 1963 1965 1966                                                      
CONECT 1965 1956 1961 1964 1974                                                 
CONECT 1966 1964 1967                                                           
CONECT 1967 1966 1968                                                           
CONECT 1968 1967 1969 1972 1973                                                 
CONECT 1969 1963 1968 1970                                                      
CONECT 1970 1969 1971                                                           
CONECT 1971 1970 1972                                                           
CONECT 1972 1968 1971 1975                                                      
CONECT 1973 1968                                                                
CONECT 1974 1965                                                                
CONECT 1975 1955 1960 1972                                                      
CONECT 1976 1955 1977 1978 1979                                                 
CONECT 1977 1976                                                                
CONECT 1978 1976                                                                
CONECT 1979 1976                                                                
CONECT 1980 1981                                                                
CONECT 1981 1980 1982 1983 1984                                                 
CONECT 1982 1981                                                                
CONECT 1983 1981                                                                
CONECT 1984 1981 1985                                                           
CONECT 1985 1984 1986 1998                                                      
CONECT 1986 1985 1987 1997                                                      
CONECT 1987 1986 1988 1996                                                      
CONECT 1988 1987 1989 1994                                                      
CONECT 1989 1988 1990                                                           
CONECT 1990 1989 1991                                                           
CONECT 1991 1990 1992                                                           
CONECT 1992 1991 1993 1994                                                      
CONECT 1993 1992                                                                
CONECT 1994 1988 1992 1995                                                      
CONECT 1995 1994 1996                                                           
CONECT 1996 1987 1995                                                           
CONECT 1997 1986 2000                                                           
CONECT 1998 1985 1999 2000                                                      
CONECT 1999 1998                                                                
CONECT 2000 1997 1998 2001                                                      
CONECT 2001 2000 2002                                                           
CONECT 2002 2001 2003                                                           
CONECT 2003 2002 2004 2005 2006                                                 
CONECT 2004 2003                                                                
CONECT 2005 2003                                                                
CONECT 2006 2003 2007                                                           
CONECT 2007 2006 2008 2009 2010                                                 
CONECT 2008 2007                                                                
CONECT 2009 2007                                                                
CONECT 2010 2007 2011                                                           
CONECT 2011 2010 2012                                                           
CONECT 2012 2011 2013 2018                                                      
CONECT 2013 2012 2014 2015                                                      
CONECT 2014 2013                                                                
CONECT 2015 2013 2016 2017                                                      
CONECT 2016 2015                                                                
CONECT 2017 2015 2018 2019                                                      
CONECT 2018 2012 2017                                                           
CONECT 2019 2017 2020 2024                                                      
CONECT 2020 2019 2021                                                           
CONECT 2021 2020 2022                                                           
CONECT 2022 1954 2021 2023                                                      
CONECT 2023 2022 2024 2025                                                      
CONECT 2024 2019 2023                                                           
CONECT 2025 2023 2026 2027                                                      
CONECT 2026 2025                                                                
CONECT 2027 2025                                                                
CONECT 2028 2029 2030 2031 2032                                                 
CONECT 2029 2028                                                                
CONECT 2030 2028                                                                
CONECT 2031 2028                                                                
CONECT 2032 2028                                                                
CONECT 2033 2034 2035 2036 2037                                                 
CONECT 2034 2033                                                                
CONECT 2035 2033                                                                
CONECT 2036 2033                                                                
CONECT 2037 2033                                                                
MASTER      344    0    4    9    2    0   13    6 2036    1  112   20          
HETATM 2223  N   DUM  2223     -24.000  -8.000 -15.200
HETATM 2223  O   DUM  2223     -24.000  -8.000  15.200
HETATM 2224  N   DUM  2224     -24.000  -6.000 -15.200
HETATM 2224  O   DUM  2224     -24.000  -6.000  15.200
HETATM 2225  N   DUM  2225     -24.000  -4.000 -15.200
HETATM 2225  O   DUM  2225     -24.000  -4.000  15.200
HETATM 2226  N   DUM  2226     -24.000  -2.000 -15.200
HETATM 2226  O   DUM  2226     -24.000  -2.000  15.200
HETATM 2227  N   DUM  2227     -24.000   0.000 -15.200
HETATM 2227  O   DUM  2227     -24.000   0.000  15.200
HETATM 2228  N   DUM  2228     -24.000   2.000 -15.200
HETATM 2228  O   DUM  2228     -24.000   2.000  15.200
HETATM 2229  N   DUM  2229     -24.000   4.000 -15.200
HETATM 2229  O   DUM  2229     -24.000   4.000  15.200
HETATM 2230  N   DUM  2230     -24.000   6.000 -15.200
HETATM 2230  O   DUM  2230     -24.000   6.000  15.200
HETATM 2231  N   DUM  2231     -24.000   8.000 -15.200
HETATM 2231  O   DUM  2231     -24.000   8.000  15.200
HETATM 2302  N   DUM  2302     -22.000 -12.000 -15.200
HETATM 2302  O   DUM  2302     -22.000 -12.000  15.200
HETATM 2303  N   DUM  2303     -22.000 -10.000 -15.200
HETATM 2303  O   DUM  2303     -22.000 -10.000  15.200
HETATM 2304  N   DUM  2304     -22.000  -8.000 -15.200
HETATM 2304  O   DUM  2304     -22.000  -8.000  15.200
HETATM 2305  N   DUM  2305     -22.000  -6.000 -15.200
HETATM 2305  O   DUM  2305     -22.000  -6.000  15.200
HETATM 2306  N   DUM  2306     -22.000  -4.000 -15.200
HETATM 2306  O   DUM  2306     -22.000  -4.000  15.200
HETATM 2307  N   DUM  2307     -22.000  -2.000 -15.200
HETATM 2307  O   DUM  2307     -22.000  -2.000  15.200
HETATM 2308  N   DUM  2308     -22.000   0.000 -15.200
HETATM 2308  O   DUM  2308     -22.000   0.000  15.200
HETATM 2309  N   DUM  2309     -22.000   2.000 -15.200
HETATM 2309  O   DUM  2309     -22.000   2.000  15.200
HETATM 2310  N   DUM  2310     -22.000   4.000 -15.200
HETATM 2310  O   DUM  2310     -22.000   4.000  15.200
HETATM 2311  N   DUM  2311     -22.000   6.000 -15.200
HETATM 2311  O   DUM  2311     -22.000   6.000  15.200
HETATM 2312  N   DUM  2312     -22.000   8.000 -15.200
HETATM 2312  O   DUM  2312     -22.000   8.000  15.200
HETATM 2313  N   DUM  2313     -22.000  10.000 -15.200
HETATM 2313  O   DUM  2313     -22.000  10.000  15.200
HETATM 2314  N   DUM  2314     -22.000  12.000 -15.200
HETATM 2314  O   DUM  2314     -22.000  12.000  15.200
HETATM 2381  N   DUM  2381     -20.000 -16.000 -15.200
HETATM 2381  O   DUM  2381     -20.000 -16.000  15.200
HETATM 2382  N   DUM  2382     -20.000 -14.000 -15.200
HETATM 2382  O   DUM  2382     -20.000 -14.000  15.200
HETATM 2383  N   DUM  2383     -20.000 -12.000 -15.200
HETATM 2383  O   DUM  2383     -20.000 -12.000  15.200
HETATM 2384  N   DUM  2384     -20.000 -10.000 -15.200
HETATM 2384  O   DUM  2384     -20.000 -10.000  15.200
HETATM 2385  N   DUM  2385     -20.000  -8.000 -15.200
HETATM 2385  O   DUM  2385     -20.000  -8.000  15.200
HETATM 2386  N   DUM  2386     -20.000  -6.000 -15.200
HETATM 2386  O   DUM  2386     -20.000  -6.000  15.200
HETATM 2387  N   DUM  2387     -20.000  -4.000 -15.200
HETATM 2387  O   DUM  2387     -20.000  -4.000  15.200
HETATM 2388  N   DUM  2388     -20.000  -2.000 -15.200
HETATM 2388  O   DUM  2388     -20.000  -2.000  15.200
HETATM 2389  N   DUM  2389     -20.000   0.000 -15.200
HETATM 2389  O   DUM  2389     -20.000   0.000  15.200
HETATM 2390  N   DUM  2390     -20.000   2.000 -15.200
HETATM 2390  O   DUM  2390     -20.000   2.000  15.200
HETATM 2391  N   DUM  2391     -20.000   4.000 -15.200
HETATM 2391  O   DUM  2391     -20.000   4.000  15.200
HETATM 2392  N   DUM  2392     -20.000   6.000 -15.200
HETATM 2392  O   DUM  2392     -20.000   6.000  15.200
HETATM 2393  N   DUM  2393     -20.000   8.000 -15.200
HETATM 2393  O   DUM  2393     -20.000   8.000  15.200
HETATM 2394  N   DUM  2394     -20.000  10.000 -15.200
HETATM 2394  O   DUM  2394     -20.000  10.000  15.200
HETATM 2395  N   DUM  2395     -20.000  12.000 -15.200
HETATM 2395  O   DUM  2395     -20.000  12.000  15.200
HETATM 2396  N   DUM  2396     -20.000  14.000 -15.200
HETATM 2396  O   DUM  2396     -20.000  14.000  15.200
HETATM 2397  N   DUM  2397     -20.000  16.000 -15.200
HETATM 2397  O   DUM  2397     -20.000  16.000  15.200
HETATM 2461  N   DUM  2461     -18.000 -18.000 -15.200
HETATM 2461  O   DUM  2461     -18.000 -18.000  15.200
HETATM 2462  N   DUM  2462     -18.000 -16.000 -15.200
HETATM 2462  O   DUM  2462     -18.000 -16.000  15.200
HETATM 2463  N   DUM  2463     -18.000 -14.000 -15.200
HETATM 2463  O   DUM  2463     -18.000 -14.000  15.200
HETATM 2464  N   DUM  2464     -18.000 -12.000 -15.200
HETATM 2464  O   DUM  2464     -18.000 -12.000  15.200
HETATM 2465  N   DUM  2465     -18.000 -10.000 -15.200
HETATM 2465  O   DUM  2465     -18.000 -10.000  15.200
HETATM 2466  N   DUM  2466     -18.000  -8.000 -15.200
HETATM 2466  O   DUM  2466     -18.000  -8.000  15.200
HETATM 2467  N   DUM  2467     -18.000  -6.000 -15.200
HETATM 2467  O   DUM  2467     -18.000  -6.000  15.200
HETATM 2468  N   DUM  2468     -18.000  -4.000 -15.200
HETATM 2468  O   DUM  2468     -18.000  -4.000  15.200
HETATM 2469  N   DUM  2469     -18.000  -2.000 -15.200
HETATM 2469  O   DUM  2469     -18.000  -2.000  15.200
HETATM 2470  N   DUM  2470     -18.000   0.000 -15.200
HETATM 2470  O   DUM  2470     -18.000   0.000  15.200
HETATM 2471  N   DUM  2471     -18.000   2.000 -15.200
HETATM 2471  O   DUM  2471     -18.000   2.000  15.200
HETATM 2472  N   DUM  2472     -18.000   4.000 -15.200
HETATM 2472  O   DUM  2472     -18.000   4.000  15.200
HETATM 2473  N   DUM  2473     -18.000   6.000 -15.200
HETATM 2473  O   DUM  2473     -18.000   6.000  15.200
HETATM 2474  N   DUM  2474     -18.000   8.000 -15.200
HETATM 2474  O   DUM  2474     -18.000   8.000  15.200
HETATM 2475  N   DUM  2475     -18.000  10.000 -15.200
HETATM 2475  O   DUM  2475     -18.000  10.000  15.200
HETATM 2476  N   DUM  2476     -18.000  12.000 -15.200
HETATM 2476  O   DUM  2476     -18.000  12.000  15.200
HETATM 2477  N   DUM  2477     -18.000  14.000 -15.200
HETATM 2477  O   DUM  2477     -18.000  14.000  15.200
HETATM 2478  N   DUM  2478     -18.000  16.000 -15.200
HETATM 2478  O   DUM  2478     -18.000  16.000  15.200
HETATM 2479  N   DUM  2479     -18.000  18.000 -15.200
HETATM 2479  O   DUM  2479     -18.000  18.000  15.200
HETATM 2541  N   DUM  2541     -16.000 -20.000 -15.200
HETATM 2541  O   DUM  2541     -16.000 -20.000  15.200
HETATM 2542  N   DUM  2542     -16.000 -18.000 -15.200
HETATM 2542  O   DUM  2542     -16.000 -18.000  15.200
HETATM 2543  N   DUM  2543     -16.000 -16.000 -15.200
HETATM 2543  O   DUM  2543     -16.000 -16.000  15.200
HETATM 2544  N   DUM  2544     -16.000 -14.000 -15.200
HETATM 2544  O   DUM  2544     -16.000 -14.000  15.200
HETATM 2545  N   DUM  2545     -16.000 -12.000 -15.200
HETATM 2545  O   DUM  2545     -16.000 -12.000  15.200
HETATM 2546  N   DUM  2546     -16.000 -10.000 -15.200
HETATM 2546  O   DUM  2546     -16.000 -10.000  15.200
HETATM 2547  N   DUM  2547     -16.000  -8.000 -15.200
HETATM 2547  O   DUM  2547     -16.000  -8.000  15.200
HETATM 2548  N   DUM  2548     -16.000  -6.000 -15.200
HETATM 2548  O   DUM  2548     -16.000  -6.000  15.200
HETATM 2549  N   DUM  2549     -16.000  -4.000 -15.200
HETATM 2549  O   DUM  2549     -16.000  -4.000  15.200
HETATM 2550  N   DUM  2550     -16.000  -2.000 -15.200
HETATM 2550  O   DUM  2550     -16.000  -2.000  15.200
HETATM 2551  N   DUM  2551     -16.000   0.000 -15.200
HETATM 2551  O   DUM  2551     -16.000   0.000  15.200
HETATM 2552  N   DUM  2552     -16.000   2.000 -15.200
HETATM 2552  O   DUM  2552     -16.000   2.000  15.200
HETATM 2553  N   DUM  2553     -16.000   4.000 -15.200
HETATM 2553  O   DUM  2553     -16.000   4.000  15.200
HETATM 2554  N   DUM  2554     -16.000   6.000 -15.200
HETATM 2554  O   DUM  2554     -16.000   6.000  15.200
HETATM 2555  N   DUM  2555     -16.000   8.000 -15.200
HETATM 2555  O   DUM  2555     -16.000   8.000  15.200
HETATM 2556  N   DUM  2556     -16.000  10.000 -15.200
HETATM 2556  O   DUM  2556     -16.000  10.000  15.200
HETATM 2557  N   DUM  2557     -16.000  12.000 -15.200
HETATM 2557  O   DUM  2557     -16.000  12.000  15.200
HETATM 2558  N   DUM  2558     -16.000  14.000 -15.200
HETATM 2558  O   DUM  2558     -16.000  14.000  15.200
HETATM 2559  N   DUM  2559     -16.000  16.000 -15.200
HETATM 2559  O   DUM  2559     -16.000  16.000  15.200
HETATM 2560  N   DUM  2560     -16.000  18.000 -15.200
HETATM 2560  O   DUM  2560     -16.000  18.000  15.200
HETATM 2561  N   DUM  2561     -16.000  20.000 -15.200
HETATM 2561  O   DUM  2561     -16.000  20.000  15.200
HETATM 2622  N   DUM  2622     -14.000 -20.000 -15.200
HETATM 2622  O   DUM  2622     -14.000 -20.000  15.200
HETATM 2623  N   DUM  2623     -14.000 -18.000 -15.200
HETATM 2623  O   DUM  2623     -14.000 -18.000  15.200
HETATM 2624  N   DUM  2624     -14.000 -16.000 -15.200
HETATM 2624  O   DUM  2624     -14.000 -16.000  15.200
HETATM 2625  N   DUM  2625     -14.000 -14.000 -15.200
HETATM 2625  O   DUM  2625     -14.000 -14.000  15.200
HETATM 2626  N   DUM  2626     -14.000 -12.000 -15.200
HETATM 2626  O   DUM  2626     -14.000 -12.000  15.200
HETATM 2627  N   DUM  2627     -14.000 -10.000 -15.200
HETATM 2627  O   DUM  2627     -14.000 -10.000  15.200
HETATM 2628  N   DUM  2628     -14.000  -8.000 -15.200
HETATM 2628  O   DUM  2628     -14.000  -8.000  15.200
HETATM 2629  N   DUM  2629     -14.000  -6.000 -15.200
HETATM 2629  O   DUM  2629     -14.000  -6.000  15.200
HETATM 2630  N   DUM  2630     -14.000  -4.000 -15.200
HETATM 2630  O   DUM  2630     -14.000  -4.000  15.200
HETATM 2631  N   DUM  2631     -14.000  -2.000 -15.200
HETATM 2631  O   DUM  2631     -14.000  -2.000  15.200
HETATM 2632  N   DUM  2632     -14.000   0.000 -15.200
HETATM 2632  O   DUM  2632     -14.000   0.000  15.200
HETATM 2633  N   DUM  2633     -14.000   2.000 -15.200
HETATM 2633  O   DUM  2633     -14.000   2.000  15.200
HETATM 2634  N   DUM  2634     -14.000   4.000 -15.200
HETATM 2634  O   DUM  2634     -14.000   4.000  15.200
HETATM 2635  N   DUM  2635     -14.000   6.000 -15.200
HETATM 2635  O   DUM  2635     -14.000   6.000  15.200
HETATM 2636  N   DUM  2636     -14.000   8.000 -15.200
HETATM 2636  O   DUM  2636     -14.000   8.000  15.200
HETATM 2637  N   DUM  2637     -14.000  10.000 -15.200
HETATM 2637  O   DUM  2637     -14.000  10.000  15.200
HETATM 2638  N   DUM  2638     -14.000  12.000 -15.200
HETATM 2638  O   DUM  2638     -14.000  12.000  15.200
HETATM 2639  N   DUM  2639     -14.000  14.000 -15.200
HETATM 2639  O   DUM  2639     -14.000  14.000  15.200
HETATM 2640  N   DUM  2640     -14.000  16.000 -15.200
HETATM 2640  O   DUM  2640     -14.000  16.000  15.200
HETATM 2641  N   DUM  2641     -14.000  18.000 -15.200
HETATM 2641  O   DUM  2641     -14.000  18.000  15.200
HETATM 2642  N   DUM  2642     -14.000  20.000 -15.200
HETATM 2642  O   DUM  2642     -14.000  20.000  15.200
HETATM 2702  N   DUM  2702     -12.000 -22.000 -15.200
HETATM 2702  O   DUM  2702     -12.000 -22.000  15.200
HETATM 2703  N   DUM  2703     -12.000 -20.000 -15.200
HETATM 2703  O   DUM  2703     -12.000 -20.000  15.200
HETATM 2704  N   DUM  2704     -12.000 -18.000 -15.200
HETATM 2704  O   DUM  2704     -12.000 -18.000  15.200
HETATM 2705  N   DUM  2705     -12.000 -16.000 -15.200
HETATM 2705  O   DUM  2705     -12.000 -16.000  15.200
HETATM 2706  N   DUM  2706     -12.000 -14.000 -15.200
HETATM 2706  O   DUM  2706     -12.000 -14.000  15.200
HETATM 2707  N   DUM  2707     -12.000 -12.000 -15.200
HETATM 2707  O   DUM  2707     -12.000 -12.000  15.200
HETATM 2708  N   DUM  2708     -12.000 -10.000 -15.200
HETATM 2708  O   DUM  2708     -12.000 -10.000  15.200
HETATM 2709  N   DUM  2709     -12.000  -8.000 -15.200
HETATM 2709  O   DUM  2709     -12.000  -8.000  15.200
HETATM 2710  N   DUM  2710     -12.000  -6.000 -15.200
HETATM 2710  O   DUM  2710     -12.000  -6.000  15.200
HETATM 2711  N   DUM  2711     -12.000  -4.000 -15.200
HETATM 2711  O   DUM  2711     -12.000  -4.000  15.200
HETATM 2712  N   DUM  2712     -12.000  -2.000 -15.200
HETATM 2712  O   DUM  2712     -12.000  -2.000  15.200
HETATM 2713  N   DUM  2713     -12.000   0.000 -15.200
HETATM 2713  O   DUM  2713     -12.000   0.000  15.200
HETATM 2714  N   DUM  2714     -12.000   2.000 -15.200
HETATM 2714  O   DUM  2714     -12.000   2.000  15.200
HETATM 2715  N   DUM  2715     -12.000   4.000 -15.200
HETATM 2715  O   DUM  2715     -12.000   4.000  15.200
HETATM 2716  N   DUM  2716     -12.000   6.000 -15.200
HETATM 2716  O   DUM  2716     -12.000   6.000  15.200
HETATM 2717  N   DUM  2717     -12.000   8.000 -15.200
HETATM 2717  O   DUM  2717     -12.000   8.000  15.200
HETATM 2718  N   DUM  2718     -12.000  10.000 -15.200
HETATM 2718  O   DUM  2718     -12.000  10.000  15.200
HETATM 2719  N   DUM  2719     -12.000  12.000 -15.200
HETATM 2719  O   DUM  2719     -12.000  12.000  15.200
HETATM 2720  N   DUM  2720     -12.000  14.000 -15.200
HETATM 2720  O   DUM  2720     -12.000  14.000  15.200
HETATM 2721  N   DUM  2721     -12.000  16.000 -15.200
HETATM 2721  O   DUM  2721     -12.000  16.000  15.200
HETATM 2722  N   DUM  2722     -12.000  18.000 -15.200
HETATM 2722  O   DUM  2722     -12.000  18.000  15.200
HETATM 2723  N   DUM  2723     -12.000  20.000 -15.200
HETATM 2723  O   DUM  2723     -12.000  20.000  15.200
HETATM 2724  N   DUM  2724     -12.000  22.000 -15.200
HETATM 2724  O   DUM  2724     -12.000  22.000  15.200
HETATM 2783  N   DUM  2783     -10.000 -22.000 -15.200
HETATM 2783  O   DUM  2783     -10.000 -22.000  15.200
HETATM 2784  N   DUM  2784     -10.000 -20.000 -15.200
HETATM 2784  O   DUM  2784     -10.000 -20.000  15.200
HETATM 2785  N   DUM  2785     -10.000 -18.000 -15.200
HETATM 2785  O   DUM  2785     -10.000 -18.000  15.200
HETATM 2786  N   DUM  2786     -10.000 -16.000 -15.200
HETATM 2786  O   DUM  2786     -10.000 -16.000  15.200
HETATM 2787  N   DUM  2787     -10.000 -14.000 -15.200
HETATM 2787  O   DUM  2787     -10.000 -14.000  15.200
HETATM 2788  N   DUM  2788     -10.000 -12.000 -15.200
HETATM 2788  O   DUM  2788     -10.000 -12.000  15.200
HETATM 2789  N   DUM  2789     -10.000 -10.000 -15.200
HETATM 2789  O   DUM  2789     -10.000 -10.000  15.200
HETATM 2790  N   DUM  2790     -10.000  -8.000 -15.200
HETATM 2790  O   DUM  2790     -10.000  -8.000  15.200
HETATM 2791  N   DUM  2791     -10.000  -6.000 -15.200
HETATM 2791  O   DUM  2791     -10.000  -6.000  15.200
HETATM 2792  N   DUM  2792     -10.000  -4.000 -15.200
HETATM 2792  O   DUM  2792     -10.000  -4.000  15.200
HETATM 2793  N   DUM  2793     -10.000  -2.000 -15.200
HETATM 2793  O   DUM  2793     -10.000  -2.000  15.200
HETATM 2794  N   DUM  2794     -10.000   0.000 -15.200
HETATM 2794  O   DUM  2794     -10.000   0.000  15.200
HETATM 2795  N   DUM  2795     -10.000   2.000 -15.200
HETATM 2795  O   DUM  2795     -10.000   2.000  15.200
HETATM 2796  N   DUM  2796     -10.000   4.000 -15.200
HETATM 2796  O   DUM  2796     -10.000   4.000  15.200
HETATM 2797  N   DUM  2797     -10.000   6.000 -15.200
HETATM 2797  O   DUM  2797     -10.000   6.000  15.200
HETATM 2798  N   DUM  2798     -10.000   8.000 -15.200
HETATM 2798  O   DUM  2798     -10.000   8.000  15.200
HETATM 2799  N   DUM  2799     -10.000  10.000 -15.200
HETATM 2799  O   DUM  2799     -10.000  10.000  15.200
HETATM 2800  N   DUM  2800     -10.000  12.000 -15.200
HETATM 2800  O   DUM  2800     -10.000  12.000  15.200
HETATM 2801  N   DUM  2801     -10.000  14.000 -15.200
HETATM 2801  O   DUM  2801     -10.000  14.000  15.200
HETATM 2802  N   DUM  2802     -10.000  16.000 -15.200
HETATM 2802  O   DUM  2802     -10.000  16.000  15.200
HETATM 2803  N   DUM  2803     -10.000  18.000 -15.200
HETATM 2803  O   DUM  2803     -10.000  18.000  15.200
HETATM 2804  N   DUM  2804     -10.000  20.000 -15.200
HETATM 2804  O   DUM  2804     -10.000  20.000  15.200
HETATM 2805  N   DUM  2805     -10.000  22.000 -15.200
HETATM 2805  O   DUM  2805     -10.000  22.000  15.200
HETATM 2863  N   DUM  2863      -8.000 -24.000 -15.200
HETATM 2863  O   DUM  2863      -8.000 -24.000  15.200
HETATM 2864  N   DUM  2864      -8.000 -22.000 -15.200
HETATM 2864  O   DUM  2864      -8.000 -22.000  15.200
HETATM 2865  N   DUM  2865      -8.000 -20.000 -15.200
HETATM 2865  O   DUM  2865      -8.000 -20.000  15.200
HETATM 2866  N   DUM  2866      -8.000 -18.000 -15.200
HETATM 2866  O   DUM  2866      -8.000 -18.000  15.200
HETATM 2867  N   DUM  2867      -8.000 -16.000 -15.200
HETATM 2867  O   DUM  2867      -8.000 -16.000  15.200
HETATM 2868  N   DUM  2868      -8.000 -14.000 -15.200
HETATM 2868  O   DUM  2868      -8.000 -14.000  15.200
HETATM 2869  N   DUM  2869      -8.000 -12.000 -15.200
HETATM 2869  O   DUM  2869      -8.000 -12.000  15.200
HETATM 2870  N   DUM  2870      -8.000 -10.000 -15.200
HETATM 2870  O   DUM  2870      -8.000 -10.000  15.200
HETATM 2871  N   DUM  2871      -8.000  -8.000 -15.200
HETATM 2871  O   DUM  2871      -8.000  -8.000  15.200
HETATM 2872  N   DUM  2872      -8.000  -6.000 -15.200
HETATM 2872  O   DUM  2872      -8.000  -6.000  15.200
HETATM 2873  N   DUM  2873      -8.000  -4.000 -15.200
HETATM 2873  O   DUM  2873      -8.000  -4.000  15.200
HETATM 2874  N   DUM  2874      -8.000  -2.000 -15.200
HETATM 2874  O   DUM  2874      -8.000  -2.000  15.200
HETATM 2875  N   DUM  2875      -8.000   0.000 -15.200
HETATM 2875  O   DUM  2875      -8.000   0.000  15.200
HETATM 2876  N   DUM  2876      -8.000   2.000 -15.200
HETATM 2876  O   DUM  2876      -8.000   2.000  15.200
HETATM 2877  N   DUM  2877      -8.000   4.000 -15.200
HETATM 2877  O   DUM  2877      -8.000   4.000  15.200
HETATM 2878  N   DUM  2878      -8.000   6.000 -15.200
HETATM 2878  O   DUM  2878      -8.000   6.000  15.200
HETATM 2879  N   DUM  2879      -8.000   8.000 -15.200
HETATM 2879  O   DUM  2879      -8.000   8.000  15.200
HETATM 2880  N   DUM  2880      -8.000  10.000 -15.200
HETATM 2880  O   DUM  2880      -8.000  10.000  15.200
HETATM 2881  N   DUM  2881      -8.000  12.000 -15.200
HETATM 2881  O   DUM  2881      -8.000  12.000  15.200
HETATM 2882  N   DUM  2882      -8.000  14.000 -15.200
HETATM 2882  O   DUM  2882      -8.000  14.000  15.200
HETATM 2883  N   DUM  2883      -8.000  16.000 -15.200
HETATM 2883  O   DUM  2883      -8.000  16.000  15.200
HETATM 2884  N   DUM  2884      -8.000  18.000 -15.200
HETATM 2884  O   DUM  2884      -8.000  18.000  15.200
HETATM 2885  N   DUM  2885      -8.000  20.000 -15.200
HETATM 2885  O   DUM  2885      -8.000  20.000  15.200
HETATM 2886  N   DUM  2886      -8.000  22.000 -15.200
HETATM 2886  O   DUM  2886      -8.000  22.000  15.200
HETATM 2887  N   DUM  2887      -8.000  24.000 -15.200
HETATM 2887  O   DUM  2887      -8.000  24.000  15.200
HETATM 2944  N   DUM  2944      -6.000 -24.000 -15.200
HETATM 2944  O   DUM  2944      -6.000 -24.000  15.200
HETATM 2945  N   DUM  2945      -6.000 -22.000 -15.200
HETATM 2945  O   DUM  2945      -6.000 -22.000  15.200
HETATM 2946  N   DUM  2946      -6.000 -20.000 -15.200
HETATM 2946  O   DUM  2946      -6.000 -20.000  15.200
HETATM 2947  N   DUM  2947      -6.000 -18.000 -15.200
HETATM 2947  O   DUM  2947      -6.000 -18.000  15.200
HETATM 2948  N   DUM  2948      -6.000 -16.000 -15.200
HETATM 2948  O   DUM  2948      -6.000 -16.000  15.200
HETATM 2949  N   DUM  2949      -6.000 -14.000 -15.200
HETATM 2949  O   DUM  2949      -6.000 -14.000  15.200
HETATM 2950  N   DUM  2950      -6.000 -12.000 -15.200
HETATM 2950  O   DUM  2950      -6.000 -12.000  15.200
HETATM 2951  N   DUM  2951      -6.000 -10.000 -15.200
HETATM 2951  O   DUM  2951      -6.000 -10.000  15.200
HETATM 2952  N   DUM  2952      -6.000  -8.000 -15.200
HETATM 2952  O   DUM  2952      -6.000  -8.000  15.200
HETATM 2953  N   DUM  2953      -6.000  -6.000 -15.200
HETATM 2953  O   DUM  2953      -6.000  -6.000  15.200
HETATM 2954  N   DUM  2954      -6.000  -4.000 -15.200
HETATM 2954  O   DUM  2954      -6.000  -4.000  15.200
HETATM 2955  N   DUM  2955      -6.000  -2.000 -15.200
HETATM 2955  O   DUM  2955      -6.000  -2.000  15.200
HETATM 2956  N   DUM  2956      -6.000   0.000 -15.200
HETATM 2956  O   DUM  2956      -6.000   0.000  15.200
HETATM 2957  N   DUM  2957      -6.000   2.000 -15.200
HETATM 2957  O   DUM  2957      -6.000   2.000  15.200
HETATM 2958  N   DUM  2958      -6.000   4.000 -15.200
HETATM 2958  O   DUM  2958      -6.000   4.000  15.200
HETATM 2959  N   DUM  2959      -6.000   6.000 -15.200
HETATM 2959  O   DUM  2959      -6.000   6.000  15.200
HETATM 2960  N   DUM  2960      -6.000   8.000 -15.200
HETATM 2960  O   DUM  2960      -6.000   8.000  15.200
HETATM 2961  N   DUM  2961      -6.000  10.000 -15.200
HETATM 2961  O   DUM  2961      -6.000  10.000  15.200
HETATM 2962  N   DUM  2962      -6.000  12.000 -15.200
HETATM 2962  O   DUM  2962      -6.000  12.000  15.200
HETATM 2963  N   DUM  2963      -6.000  14.000 -15.200
HETATM 2963  O   DUM  2963      -6.000  14.000  15.200
HETATM 2964  N   DUM  2964      -6.000  16.000 -15.200
HETATM 2964  O   DUM  2964      -6.000  16.000  15.200
HETATM 2965  N   DUM  2965      -6.000  18.000 -15.200
HETATM 2965  O   DUM  2965      -6.000  18.000  15.200
HETATM 2966  N   DUM  2966      -6.000  20.000 -15.200
HETATM 2966  O   DUM  2966      -6.000  20.000  15.200
HETATM 2967  N   DUM  2967      -6.000  22.000 -15.200
HETATM 2967  O   DUM  2967      -6.000  22.000  15.200
HETATM 2968  N   DUM  2968      -6.000  24.000 -15.200
HETATM 2968  O   DUM  2968      -6.000  24.000  15.200
HETATM 3025  N   DUM  3025      -4.000 -24.000 -15.200
HETATM 3025  O   DUM  3025      -4.000 -24.000  15.200
HETATM 3026  N   DUM  3026      -4.000 -22.000 -15.200
HETATM 3026  O   DUM  3026      -4.000 -22.000  15.200
HETATM 3027  N   DUM  3027      -4.000 -20.000 -15.200
HETATM 3027  O   DUM  3027      -4.000 -20.000  15.200
HETATM 3028  N   DUM  3028      -4.000 -18.000 -15.200
HETATM 3028  O   DUM  3028      -4.000 -18.000  15.200
HETATM 3029  N   DUM  3029      -4.000 -16.000 -15.200
HETATM 3029  O   DUM  3029      -4.000 -16.000  15.200
HETATM 3030  N   DUM  3030      -4.000 -14.000 -15.200
HETATM 3030  O   DUM  3030      -4.000 -14.000  15.200
HETATM 3031  N   DUM  3031      -4.000 -12.000 -15.200
HETATM 3031  O   DUM  3031      -4.000 -12.000  15.200
HETATM 3032  N   DUM  3032      -4.000 -10.000 -15.200
HETATM 3032  O   DUM  3032      -4.000 -10.000  15.200
HETATM 3033  N   DUM  3033      -4.000  -8.000 -15.200
HETATM 3033  O   DUM  3033      -4.000  -8.000  15.200
HETATM 3034  N   DUM  3034      -4.000  -6.000 -15.200
HETATM 3034  O   DUM  3034      -4.000  -6.000  15.200
HETATM 3035  N   DUM  3035      -4.000  -4.000 -15.200
HETATM 3035  O   DUM  3035      -4.000  -4.000  15.200
HETATM 3036  N   DUM  3036      -4.000  -2.000 -15.200
HETATM 3036  O   DUM  3036      -4.000  -2.000  15.200
HETATM 3037  N   DUM  3037      -4.000   0.000 -15.200
HETATM 3037  O   DUM  3037      -4.000   0.000  15.200
HETATM 3038  N   DUM  3038      -4.000   2.000 -15.200
HETATM 3038  O   DUM  3038      -4.000   2.000  15.200
HETATM 3039  N   DUM  3039      -4.000   4.000 -15.200
HETATM 3039  O   DUM  3039      -4.000   4.000  15.200
HETATM 3040  N   DUM  3040      -4.000   6.000 -15.200
HETATM 3040  O   DUM  3040      -4.000   6.000  15.200
HETATM 3041  N   DUM  3041      -4.000   8.000 -15.200
HETATM 3041  O   DUM  3041      -4.000   8.000  15.200
HETATM 3042  N   DUM  3042      -4.000  10.000 -15.200
HETATM 3042  O   DUM  3042      -4.000  10.000  15.200
HETATM 3043  N   DUM  3043      -4.000  12.000 -15.200
HETATM 3043  O   DUM  3043      -4.000  12.000  15.200
HETATM 3044  N   DUM  3044      -4.000  14.000 -15.200
HETATM 3044  O   DUM  3044      -4.000  14.000  15.200
HETATM 3045  N   DUM  3045      -4.000  16.000 -15.200
HETATM 3045  O   DUM  3045      -4.000  16.000  15.200
HETATM 3046  N   DUM  3046      -4.000  18.000 -15.200
HETATM 3046  O   DUM  3046      -4.000  18.000  15.200
HETATM 3047  N   DUM  3047      -4.000  20.000 -15.200
HETATM 3047  O   DUM  3047      -4.000  20.000  15.200
HETATM 3048  N   DUM  3048      -4.000  22.000 -15.200
HETATM 3048  O   DUM  3048      -4.000  22.000  15.200
HETATM 3049  N   DUM  3049      -4.000  24.000 -15.200
HETATM 3049  O   DUM  3049      -4.000  24.000  15.200
HETATM 3106  N   DUM  3106      -2.000 -24.000 -15.200
HETATM 3106  O   DUM  3106      -2.000 -24.000  15.200
HETATM 3107  N   DUM  3107      -2.000 -22.000 -15.200
HETATM 3107  O   DUM  3107      -2.000 -22.000  15.200
HETATM 3108  N   DUM  3108      -2.000 -20.000 -15.200
HETATM 3108  O   DUM  3108      -2.000 -20.000  15.200
HETATM 3109  N   DUM  3109      -2.000 -18.000 -15.200
HETATM 3109  O   DUM  3109      -2.000 -18.000  15.200
HETATM 3110  N   DUM  3110      -2.000 -16.000 -15.200
HETATM 3110  O   DUM  3110      -2.000 -16.000  15.200
HETATM 3111  N   DUM  3111      -2.000 -14.000 -15.200
HETATM 3111  O   DUM  3111      -2.000 -14.000  15.200
HETATM 3112  N   DUM  3112      -2.000 -12.000 -15.200
HETATM 3112  O   DUM  3112      -2.000 -12.000  15.200
HETATM 3113  N   DUM  3113      -2.000 -10.000 -15.200
HETATM 3113  O   DUM  3113      -2.000 -10.000  15.200
HETATM 3114  N   DUM  3114      -2.000  -8.000 -15.200
HETATM 3114  O   DUM  3114      -2.000  -8.000  15.200
HETATM 3115  N   DUM  3115      -2.000  -6.000 -15.200
HETATM 3115  O   DUM  3115      -2.000  -6.000  15.200
HETATM 3116  N   DUM  3116      -2.000  -4.000 -15.200
HETATM 3116  O   DUM  3116      -2.000  -4.000  15.200
HETATM 3117  N   DUM  3117      -2.000  -2.000 -15.200
HETATM 3117  O   DUM  3117      -2.000  -2.000  15.200
HETATM 3118  N   DUM  3118      -2.000   0.000 -15.200
HETATM 3118  O   DUM  3118      -2.000   0.000  15.200
HETATM 3119  N   DUM  3119      -2.000   2.000 -15.200
HETATM 3119  O   DUM  3119      -2.000   2.000  15.200
HETATM 3120  N   DUM  3120      -2.000   4.000 -15.200
HETATM 3120  O   DUM  3120      -2.000   4.000  15.200
HETATM 3121  N   DUM  3121      -2.000   6.000 -15.200
HETATM 3121  O   DUM  3121      -2.000   6.000  15.200
HETATM 3122  N   DUM  3122      -2.000   8.000 -15.200
HETATM 3122  O   DUM  3122      -2.000   8.000  15.200
HETATM 3123  N   DUM  3123      -2.000  10.000 -15.200
HETATM 3123  O   DUM  3123      -2.000  10.000  15.200
HETATM 3124  N   DUM  3124      -2.000  12.000 -15.200
HETATM 3124  O   DUM  3124      -2.000  12.000  15.200
HETATM 3125  N   DUM  3125      -2.000  14.000 -15.200
HETATM 3125  O   DUM  3125      -2.000  14.000  15.200
HETATM 3126  N   DUM  3126      -2.000  16.000 -15.200
HETATM 3126  O   DUM  3126      -2.000  16.000  15.200
HETATM 3127  N   DUM  3127      -2.000  18.000 -15.200
HETATM 3127  O   DUM  3127      -2.000  18.000  15.200
HETATM 3128  N   DUM  3128      -2.000  20.000 -15.200
HETATM 3128  O   DUM  3128      -2.000  20.000  15.200
HETATM 3129  N   DUM  3129      -2.000  22.000 -15.200
HETATM 3129  O   DUM  3129      -2.000  22.000  15.200
HETATM 3130  N   DUM  3130      -2.000  24.000 -15.200
HETATM 3130  O   DUM  3130      -2.000  24.000  15.200
HETATM 3187  N   DUM  3187       0.000 -24.000 -15.200
HETATM 3187  O   DUM  3187       0.000 -24.000  15.200
HETATM 3188  N   DUM  3188       0.000 -22.000 -15.200
HETATM 3188  O   DUM  3188       0.000 -22.000  15.200
HETATM 3189  N   DUM  3189       0.000 -20.000 -15.200
HETATM 3189  O   DUM  3189       0.000 -20.000  15.200
HETATM 3190  N   DUM  3190       0.000 -18.000 -15.200
HETATM 3190  O   DUM  3190       0.000 -18.000  15.200
HETATM 3191  N   DUM  3191       0.000 -16.000 -15.200
HETATM 3191  O   DUM  3191       0.000 -16.000  15.200
HETATM 3192  N   DUM  3192       0.000 -14.000 -15.200
HETATM 3192  O   DUM  3192       0.000 -14.000  15.200
HETATM 3193  N   DUM  3193       0.000 -12.000 -15.200
HETATM 3193  O   DUM  3193       0.000 -12.000  15.200
HETATM 3194  N   DUM  3194       0.000 -10.000 -15.200
HETATM 3194  O   DUM  3194       0.000 -10.000  15.200
HETATM 3195  N   DUM  3195       0.000  -8.000 -15.200
HETATM 3195  O   DUM  3195       0.000  -8.000  15.200
HETATM 3196  N   DUM  3196       0.000  -6.000 -15.200
HETATM 3196  O   DUM  3196       0.000  -6.000  15.200
HETATM 3197  N   DUM  3197       0.000  -4.000 -15.200
HETATM 3197  O   DUM  3197       0.000  -4.000  15.200
HETATM 3198  N   DUM  3198       0.000  -2.000 -15.200
HETATM 3198  O   DUM  3198       0.000  -2.000  15.200
HETATM 3199  N   DUM  3199       0.000   0.000 -15.200
HETATM 3199  O   DUM  3199       0.000   0.000  15.200
HETATM 3200  N   DUM  3200       0.000   2.000 -15.200
HETATM 3200  O   DUM  3200       0.000   2.000  15.200
HETATM 3201  N   DUM  3201       0.000   4.000 -15.200
HETATM 3201  O   DUM  3201       0.000   4.000  15.200
HETATM 3202  N   DUM  3202       0.000   6.000 -15.200
HETATM 3202  O   DUM  3202       0.000   6.000  15.200
HETATM 3203  N   DUM  3203       0.000   8.000 -15.200
HETATM 3203  O   DUM  3203       0.000   8.000  15.200
HETATM 3204  N   DUM  3204       0.000  10.000 -15.200
HETATM 3204  O   DUM  3204       0.000  10.000  15.200
HETATM 3205  N   DUM  3205       0.000  12.000 -15.200
HETATM 3205  O   DUM  3205       0.000  12.000  15.200
HETATM 3206  N   DUM  3206       0.000  14.000 -15.200
HETATM 3206  O   DUM  3206       0.000  14.000  15.200
HETATM 3207  N   DUM  3207       0.000  16.000 -15.200
HETATM 3207  O   DUM  3207       0.000  16.000  15.200
HETATM 3208  N   DUM  3208       0.000  18.000 -15.200
HETATM 3208  O   DUM  3208       0.000  18.000  15.200
HETATM 3209  N   DUM  3209       0.000  20.000 -15.200
HETATM 3209  O   DUM  3209       0.000  20.000  15.200
HETATM 3210  N   DUM  3210       0.000  22.000 -15.200
HETATM 3210  O   DUM  3210       0.000  22.000  15.200
HETATM 3211  N   DUM  3211       0.000  24.000 -15.200
HETATM 3211  O   DUM  3211       0.000  24.000  15.200
HETATM 3268  N   DUM  3268       2.000 -24.000 -15.200
HETATM 3268  O   DUM  3268       2.000 -24.000  15.200
HETATM 3269  N   DUM  3269       2.000 -22.000 -15.200
HETATM 3269  O   DUM  3269       2.000 -22.000  15.200
HETATM 3270  N   DUM  3270       2.000 -20.000 -15.200
HETATM 3270  O   DUM  3270       2.000 -20.000  15.200
HETATM 3271  N   DUM  3271       2.000 -18.000 -15.200
HETATM 3271  O   DUM  3271       2.000 -18.000  15.200
HETATM 3272  N   DUM  3272       2.000 -16.000 -15.200
HETATM 3272  O   DUM  3272       2.000 -16.000  15.200
HETATM 3273  N   DUM  3273       2.000 -14.000 -15.200
HETATM 3273  O   DUM  3273       2.000 -14.000  15.200
HETATM 3274  N   DUM  3274       2.000 -12.000 -15.200
HETATM 3274  O   DUM  3274       2.000 -12.000  15.200
HETATM 3275  N   DUM  3275       2.000 -10.000 -15.200
HETATM 3275  O   DUM  3275       2.000 -10.000  15.200
HETATM 3276  N   DUM  3276       2.000  -8.000 -15.200
HETATM 3276  O   DUM  3276       2.000  -8.000  15.200
HETATM 3277  N   DUM  3277       2.000  -6.000 -15.200
HETATM 3277  O   DUM  3277       2.000  -6.000  15.200
HETATM 3278  N   DUM  3278       2.000  -4.000 -15.200
HETATM 3278  O   DUM  3278       2.000  -4.000  15.200
HETATM 3279  N   DUM  3279       2.000  -2.000 -15.200
HETATM 3279  O   DUM  3279       2.000  -2.000  15.200
HETATM 3280  N   DUM  3280       2.000   0.000 -15.200
HETATM 3280  O   DUM  3280       2.000   0.000  15.200
HETATM 3281  N   DUM  3281       2.000   2.000 -15.200
HETATM 3281  O   DUM  3281       2.000   2.000  15.200
HETATM 3282  N   DUM  3282       2.000   4.000 -15.200
HETATM 3282  O   DUM  3282       2.000   4.000  15.200
HETATM 3283  N   DUM  3283       2.000   6.000 -15.200
HETATM 3283  O   DUM  3283       2.000   6.000  15.200
HETATM 3284  N   DUM  3284       2.000   8.000 -15.200
HETATM 3284  O   DUM  3284       2.000   8.000  15.200
HETATM 3285  N   DUM  3285       2.000  10.000 -15.200
HETATM 3285  O   DUM  3285       2.000  10.000  15.200
HETATM 3286  N   DUM  3286       2.000  12.000 -15.200
HETATM 3286  O   DUM  3286       2.000  12.000  15.200
HETATM 3287  N   DUM  3287       2.000  14.000 -15.200
HETATM 3287  O   DUM  3287       2.000  14.000  15.200
HETATM 3288  N   DUM  3288       2.000  16.000 -15.200
HETATM 3288  O   DUM  3288       2.000  16.000  15.200
HETATM 3289  N   DUM  3289       2.000  18.000 -15.200
HETATM 3289  O   DUM  3289       2.000  18.000  15.200
HETATM 3290  N   DUM  3290       2.000  20.000 -15.200
HETATM 3290  O   DUM  3290       2.000  20.000  15.200
HETATM 3291  N   DUM  3291       2.000  22.000 -15.200
HETATM 3291  O   DUM  3291       2.000  22.000  15.200
HETATM 3292  N   DUM  3292       2.000  24.000 -15.200
HETATM 3292  O   DUM  3292       2.000  24.000  15.200
HETATM 3349  N   DUM  3349       4.000 -24.000 -15.200
HETATM 3349  O   DUM  3349       4.000 -24.000  15.200
HETATM 3350  N   DUM  3350       4.000 -22.000 -15.200
HETATM 3350  O   DUM  3350       4.000 -22.000  15.200
HETATM 3351  N   DUM  3351       4.000 -20.000 -15.200
HETATM 3351  O   DUM  3351       4.000 -20.000  15.200
HETATM 3352  N   DUM  3352       4.000 -18.000 -15.200
HETATM 3352  O   DUM  3352       4.000 -18.000  15.200
HETATM 3353  N   DUM  3353       4.000 -16.000 -15.200
HETATM 3353  O   DUM  3353       4.000 -16.000  15.200
HETATM 3354  N   DUM  3354       4.000 -14.000 -15.200
HETATM 3354  O   DUM  3354       4.000 -14.000  15.200
HETATM 3355  N   DUM  3355       4.000 -12.000 -15.200
HETATM 3355  O   DUM  3355       4.000 -12.000  15.200
HETATM 3356  N   DUM  3356       4.000 -10.000 -15.200
HETATM 3356  O   DUM  3356       4.000 -10.000  15.200
HETATM 3357  N   DUM  3357       4.000  -8.000 -15.200
HETATM 3357  O   DUM  3357       4.000  -8.000  15.200
HETATM 3358  N   DUM  3358       4.000  -6.000 -15.200
HETATM 3358  O   DUM  3358       4.000  -6.000  15.200
HETATM 3359  N   DUM  3359       4.000  -4.000 -15.200
HETATM 3359  O   DUM  3359       4.000  -4.000  15.200
HETATM 3360  N   DUM  3360       4.000  -2.000 -15.200
HETATM 3360  O   DUM  3360       4.000  -2.000  15.200
HETATM 3361  N   DUM  3361       4.000   0.000 -15.200
HETATM 3361  O   DUM  3361       4.000   0.000  15.200
HETATM 3362  N   DUM  3362       4.000   2.000 -15.200
HETATM 3362  O   DUM  3362       4.000   2.000  15.200
HETATM 3363  N   DUM  3363       4.000   4.000 -15.200
HETATM 3363  O   DUM  3363       4.000   4.000  15.200
HETATM 3364  N   DUM  3364       4.000   6.000 -15.200
HETATM 3364  O   DUM  3364       4.000   6.000  15.200
HETATM 3365  N   DUM  3365       4.000   8.000 -15.200
HETATM 3365  O   DUM  3365       4.000   8.000  15.200
HETATM 3366  N   DUM  3366       4.000  10.000 -15.200
HETATM 3366  O   DUM  3366       4.000  10.000  15.200
HETATM 3367  N   DUM  3367       4.000  12.000 -15.200
HETATM 3367  O   DUM  3367       4.000  12.000  15.200
HETATM 3368  N   DUM  3368       4.000  14.000 -15.200
HETATM 3368  O   DUM  3368       4.000  14.000  15.200
HETATM 3369  N   DUM  3369       4.000  16.000 -15.200
HETATM 3369  O   DUM  3369       4.000  16.000  15.200
HETATM 3370  N   DUM  3370       4.000  18.000 -15.200
HETATM 3370  O   DUM  3370       4.000  18.000  15.200
HETATM 3371  N   DUM  3371       4.000  20.000 -15.200
HETATM 3371  O   DUM  3371       4.000  20.000  15.200
HETATM 3372  N   DUM  3372       4.000  22.000 -15.200
HETATM 3372  O   DUM  3372       4.000  22.000  15.200
HETATM 3373  N   DUM  3373       4.000  24.000 -15.200
HETATM 3373  O   DUM  3373       4.000  24.000  15.200
HETATM 3430  N   DUM  3430       6.000 -24.000 -15.200
HETATM 3430  O   DUM  3430       6.000 -24.000  15.200
HETATM 3431  N   DUM  3431       6.000 -22.000 -15.200
HETATM 3431  O   DUM  3431       6.000 -22.000  15.200
HETATM 3432  N   DUM  3432       6.000 -20.000 -15.200
HETATM 3432  O   DUM  3432       6.000 -20.000  15.200
HETATM 3433  N   DUM  3433       6.000 -18.000 -15.200
HETATM 3433  O   DUM  3433       6.000 -18.000  15.200
HETATM 3434  N   DUM  3434       6.000 -16.000 -15.200
HETATM 3434  O   DUM  3434       6.000 -16.000  15.200
HETATM 3435  N   DUM  3435       6.000 -14.000 -15.200
HETATM 3435  O   DUM  3435       6.000 -14.000  15.200
HETATM 3436  N   DUM  3436       6.000 -12.000 -15.200
HETATM 3436  O   DUM  3436       6.000 -12.000  15.200
HETATM 3437  N   DUM  3437       6.000 -10.000 -15.200
HETATM 3437  O   DUM  3437       6.000 -10.000  15.200
HETATM 3438  N   DUM  3438       6.000  -8.000 -15.200
HETATM 3438  O   DUM  3438       6.000  -8.000  15.200
HETATM 3439  N   DUM  3439       6.000  -6.000 -15.200
HETATM 3439  O   DUM  3439       6.000  -6.000  15.200
HETATM 3440  N   DUM  3440       6.000  -4.000 -15.200
HETATM 3440  O   DUM  3440       6.000  -4.000  15.200
HETATM 3441  N   DUM  3441       6.000  -2.000 -15.200
HETATM 3441  O   DUM  3441       6.000  -2.000  15.200
HETATM 3442  N   DUM  3442       6.000   0.000 -15.200
HETATM 3442  O   DUM  3442       6.000   0.000  15.200
HETATM 3443  N   DUM  3443       6.000   2.000 -15.200
HETATM 3443  O   DUM  3443       6.000   2.000  15.200
HETATM 3444  N   DUM  3444       6.000   4.000 -15.200
HETATM 3444  O   DUM  3444       6.000   4.000  15.200
HETATM 3445  N   DUM  3445       6.000   6.000 -15.200
HETATM 3445  O   DUM  3445       6.000   6.000  15.200
HETATM 3446  N   DUM  3446       6.000   8.000 -15.200
HETATM 3446  O   DUM  3446       6.000   8.000  15.200
HETATM 3447  N   DUM  3447       6.000  10.000 -15.200
HETATM 3447  O   DUM  3447       6.000  10.000  15.200
HETATM 3448  N   DUM  3448       6.000  12.000 -15.200
HETATM 3448  O   DUM  3448       6.000  12.000  15.200
HETATM 3449  N   DUM  3449       6.000  14.000 -15.200
HETATM 3449  O   DUM  3449       6.000  14.000  15.200
HETATM 3450  N   DUM  3450       6.000  16.000 -15.200
HETATM 3450  O   DUM  3450       6.000  16.000  15.200
HETATM 3451  N   DUM  3451       6.000  18.000 -15.200
HETATM 3451  O   DUM  3451       6.000  18.000  15.200
HETATM 3452  N   DUM  3452       6.000  20.000 -15.200
HETATM 3452  O   DUM  3452       6.000  20.000  15.200
HETATM 3453  N   DUM  3453       6.000  22.000 -15.200
HETATM 3453  O   DUM  3453       6.000  22.000  15.200
HETATM 3454  N   DUM  3454       6.000  24.000 -15.200
HETATM 3454  O   DUM  3454       6.000  24.000  15.200
HETATM 3511  N   DUM  3511       8.000 -24.000 -15.200
HETATM 3511  O   DUM  3511       8.000 -24.000  15.200
HETATM 3512  N   DUM  3512       8.000 -22.000 -15.200
HETATM 3512  O   DUM  3512       8.000 -22.000  15.200
HETATM 3513  N   DUM  3513       8.000 -20.000 -15.200
HETATM 3513  O   DUM  3513       8.000 -20.000  15.200
HETATM 3514  N   DUM  3514       8.000 -18.000 -15.200
HETATM 3514  O   DUM  3514       8.000 -18.000  15.200
HETATM 3515  N   DUM  3515       8.000 -16.000 -15.200
HETATM 3515  O   DUM  3515       8.000 -16.000  15.200
HETATM 3516  N   DUM  3516       8.000 -14.000 -15.200
HETATM 3516  O   DUM  3516       8.000 -14.000  15.200
HETATM 3517  N   DUM  3517       8.000 -12.000 -15.200
HETATM 3517  O   DUM  3517       8.000 -12.000  15.200
HETATM 3518  N   DUM  3518       8.000 -10.000 -15.200
HETATM 3518  O   DUM  3518       8.000 -10.000  15.200
HETATM 3519  N   DUM  3519       8.000  -8.000 -15.200
HETATM 3519  O   DUM  3519       8.000  -8.000  15.200
HETATM 3520  N   DUM  3520       8.000  -6.000 -15.200
HETATM 3520  O   DUM  3520       8.000  -6.000  15.200
HETATM 3521  N   DUM  3521       8.000  -4.000 -15.200
HETATM 3521  O   DUM  3521       8.000  -4.000  15.200
HETATM 3522  N   DUM  3522       8.000  -2.000 -15.200
HETATM 3522  O   DUM  3522       8.000  -2.000  15.200
HETATM 3523  N   DUM  3523       8.000   0.000 -15.200
HETATM 3523  O   DUM  3523       8.000   0.000  15.200
HETATM 3524  N   DUM  3524       8.000   2.000 -15.200
HETATM 3524  O   DUM  3524       8.000   2.000  15.200
HETATM 3525  N   DUM  3525       8.000   4.000 -15.200
HETATM 3525  O   DUM  3525       8.000   4.000  15.200
HETATM 3526  N   DUM  3526       8.000   6.000 -15.200
HETATM 3526  O   DUM  3526       8.000   6.000  15.200
HETATM 3527  N   DUM  3527       8.000   8.000 -15.200
HETATM 3527  O   DUM  3527       8.000   8.000  15.200
HETATM 3528  N   DUM  3528       8.000  10.000 -15.200
HETATM 3528  O   DUM  3528       8.000  10.000  15.200
HETATM 3529  N   DUM  3529       8.000  12.000 -15.200
HETATM 3529  O   DUM  3529       8.000  12.000  15.200
HETATM 3530  N   DUM  3530       8.000  14.000 -15.200
HETATM 3530  O   DUM  3530       8.000  14.000  15.200
HETATM 3531  N   DUM  3531       8.000  16.000 -15.200
HETATM 3531  O   DUM  3531       8.000  16.000  15.200
HETATM 3532  N   DUM  3532       8.000  18.000 -15.200
HETATM 3532  O   DUM  3532       8.000  18.000  15.200
HETATM 3533  N   DUM  3533       8.000  20.000 -15.200
HETATM 3533  O   DUM  3533       8.000  20.000  15.200
HETATM 3534  N   DUM  3534       8.000  22.000 -15.200
HETATM 3534  O   DUM  3534       8.000  22.000  15.200
HETATM 3535  N   DUM  3535       8.000  24.000 -15.200
HETATM 3535  O   DUM  3535       8.000  24.000  15.200
HETATM 3593  N   DUM  3593      10.000 -22.000 -15.200
HETATM 3593  O   DUM  3593      10.000 -22.000  15.200
HETATM 3594  N   DUM  3594      10.000 -20.000 -15.200
HETATM 3594  O   DUM  3594      10.000 -20.000  15.200
HETATM 3595  N   DUM  3595      10.000 -18.000 -15.200
HETATM 3595  O   DUM  3595      10.000 -18.000  15.200
HETATM 3596  N   DUM  3596      10.000 -16.000 -15.200
HETATM 3596  O   DUM  3596      10.000 -16.000  15.200
HETATM 3597  N   DUM  3597      10.000 -14.000 -15.200
HETATM 3597  O   DUM  3597      10.000 -14.000  15.200
HETATM 3598  N   DUM  3598      10.000 -12.000 -15.200
HETATM 3598  O   DUM  3598      10.000 -12.000  15.200
HETATM 3599  N   DUM  3599      10.000 -10.000 -15.200
HETATM 3599  O   DUM  3599      10.000 -10.000  15.200
HETATM 3600  N   DUM  3600      10.000  -8.000 -15.200
HETATM 3600  O   DUM  3600      10.000  -8.000  15.200
HETATM 3601  N   DUM  3601      10.000  -6.000 -15.200
HETATM 3601  O   DUM  3601      10.000  -6.000  15.200
HETATM 3602  N   DUM  3602      10.000  -4.000 -15.200
HETATM 3602  O   DUM  3602      10.000  -4.000  15.200
HETATM 3603  N   DUM  3603      10.000  -2.000 -15.200
HETATM 3603  O   DUM  3603      10.000  -2.000  15.200
HETATM 3604  N   DUM  3604      10.000   0.000 -15.200
HETATM 3604  O   DUM  3604      10.000   0.000  15.200
HETATM 3605  N   DUM  3605      10.000   2.000 -15.200
HETATM 3605  O   DUM  3605      10.000   2.000  15.200
HETATM 3606  N   DUM  3606      10.000   4.000 -15.200
HETATM 3606  O   DUM  3606      10.000   4.000  15.200
HETATM 3607  N   DUM  3607      10.000   6.000 -15.200
HETATM 3607  O   DUM  3607      10.000   6.000  15.200
HETATM 3608  N   DUM  3608      10.000   8.000 -15.200
HETATM 3608  O   DUM  3608      10.000   8.000  15.200
HETATM 3609  N   DUM  3609      10.000  10.000 -15.200
HETATM 3609  O   DUM  3609      10.000  10.000  15.200
HETATM 3610  N   DUM  3610      10.000  12.000 -15.200
HETATM 3610  O   DUM  3610      10.000  12.000  15.200
HETATM 3611  N   DUM  3611      10.000  14.000 -15.200
HETATM 3611  O   DUM  3611      10.000  14.000  15.200
HETATM 3612  N   DUM  3612      10.000  16.000 -15.200
HETATM 3612  O   DUM  3612      10.000  16.000  15.200
HETATM 3613  N   DUM  3613      10.000  18.000 -15.200
HETATM 3613  O   DUM  3613      10.000  18.000  15.200
HETATM 3614  N   DUM  3614      10.000  20.000 -15.200
HETATM 3614  O   DUM  3614      10.000  20.000  15.200
HETATM 3615  N   DUM  3615      10.000  22.000 -15.200
HETATM 3615  O   DUM  3615      10.000  22.000  15.200
HETATM 3674  N   DUM  3674      12.000 -22.000 -15.200
HETATM 3674  O   DUM  3674      12.000 -22.000  15.200
HETATM 3675  N   DUM  3675      12.000 -20.000 -15.200
HETATM 3675  O   DUM  3675      12.000 -20.000  15.200
HETATM 3676  N   DUM  3676      12.000 -18.000 -15.200
HETATM 3676  O   DUM  3676      12.000 -18.000  15.200
HETATM 3677  N   DUM  3677      12.000 -16.000 -15.200
HETATM 3677  O   DUM  3677      12.000 -16.000  15.200
HETATM 3678  N   DUM  3678      12.000 -14.000 -15.200
HETATM 3678  O   DUM  3678      12.000 -14.000  15.200
HETATM 3679  N   DUM  3679      12.000 -12.000 -15.200
HETATM 3679  O   DUM  3679      12.000 -12.000  15.200
HETATM 3680  N   DUM  3680      12.000 -10.000 -15.200
HETATM 3680  O   DUM  3680      12.000 -10.000  15.200
HETATM 3681  N   DUM  3681      12.000  -8.000 -15.200
HETATM 3681  O   DUM  3681      12.000  -8.000  15.200
HETATM 3682  N   DUM  3682      12.000  -6.000 -15.200
HETATM 3682  O   DUM  3682      12.000  -6.000  15.200
HETATM 3683  N   DUM  3683      12.000  -4.000 -15.200
HETATM 3683  O   DUM  3683      12.000  -4.000  15.200
HETATM 3684  N   DUM  3684      12.000  -2.000 -15.200
HETATM 3684  O   DUM  3684      12.000  -2.000  15.200
HETATM 3685  N   DUM  3685      12.000   0.000 -15.200
HETATM 3685  O   DUM  3685      12.000   0.000  15.200
HETATM 3686  N   DUM  3686      12.000   2.000 -15.200
HETATM 3686  O   DUM  3686      12.000   2.000  15.200
HETATM 3687  N   DUM  3687      12.000   4.000 -15.200
HETATM 3687  O   DUM  3687      12.000   4.000  15.200
HETATM 3688  N   DUM  3688      12.000   6.000 -15.200
HETATM 3688  O   DUM  3688      12.000   6.000  15.200
HETATM 3689  N   DUM  3689      12.000   8.000 -15.200
HETATM 3689  O   DUM  3689      12.000   8.000  15.200
HETATM 3690  N   DUM  3690      12.000  10.000 -15.200
HETATM 3690  O   DUM  3690      12.000  10.000  15.200
HETATM 3691  N   DUM  3691      12.000  12.000 -15.200
HETATM 3691  O   DUM  3691      12.000  12.000  15.200
HETATM 3692  N   DUM  3692      12.000  14.000 -15.200
HETATM 3692  O   DUM  3692      12.000  14.000  15.200
HETATM 3693  N   DUM  3693      12.000  16.000 -15.200
HETATM 3693  O   DUM  3693      12.000  16.000  15.200
HETATM 3694  N   DUM  3694      12.000  18.000 -15.200
HETATM 3694  O   DUM  3694      12.000  18.000  15.200
HETATM 3695  N   DUM  3695      12.000  20.000 -15.200
HETATM 3695  O   DUM  3695      12.000  20.000  15.200
HETATM 3696  N   DUM  3696      12.000  22.000 -15.200
HETATM 3696  O   DUM  3696      12.000  22.000  15.200
HETATM 3756  N   DUM  3756      14.000 -20.000 -15.200
HETATM 3756  O   DUM  3756      14.000 -20.000  15.200
HETATM 3757  N   DUM  3757      14.000 -18.000 -15.200
HETATM 3757  O   DUM  3757      14.000 -18.000  15.200
HETATM 3758  N   DUM  3758      14.000 -16.000 -15.200
HETATM 3758  O   DUM  3758      14.000 -16.000  15.200
HETATM 3759  N   DUM  3759      14.000 -14.000 -15.200
HETATM 3759  O   DUM  3759      14.000 -14.000  15.200
HETATM 3760  N   DUM  3760      14.000 -12.000 -15.200
HETATM 3760  O   DUM  3760      14.000 -12.000  15.200
HETATM 3761  N   DUM  3761      14.000 -10.000 -15.200
HETATM 3761  O   DUM  3761      14.000 -10.000  15.200
HETATM 3762  N   DUM  3762      14.000  -8.000 -15.200
HETATM 3762  O   DUM  3762      14.000  -8.000  15.200
HETATM 3763  N   DUM  3763      14.000  -6.000 -15.200
HETATM 3763  O   DUM  3763      14.000  -6.000  15.200
HETATM 3764  N   DUM  3764      14.000  -4.000 -15.200
HETATM 3764  O   DUM  3764      14.000  -4.000  15.200
HETATM 3765  N   DUM  3765      14.000  -2.000 -15.200
HETATM 3765  O   DUM  3765      14.000  -2.000  15.200
HETATM 3766  N   DUM  3766      14.000   0.000 -15.200
HETATM 3766  O   DUM  3766      14.000   0.000  15.200
HETATM 3767  N   DUM  3767      14.000   2.000 -15.200
HETATM 3767  O   DUM  3767      14.000   2.000  15.200
HETATM 3768  N   DUM  3768      14.000   4.000 -15.200
HETATM 3768  O   DUM  3768      14.000   4.000  15.200
HETATM 3769  N   DUM  3769      14.000   6.000 -15.200
HETATM 3769  O   DUM  3769      14.000   6.000  15.200
HETATM 3770  N   DUM  3770      14.000   8.000 -15.200
HETATM 3770  O   DUM  3770      14.000   8.000  15.200
HETATM 3771  N   DUM  3771      14.000  10.000 -15.200
HETATM 3771  O   DUM  3771      14.000  10.000  15.200
HETATM 3772  N   DUM  3772      14.000  12.000 -15.200
HETATM 3772  O   DUM  3772      14.000  12.000  15.200
HETATM 3773  N   DUM  3773      14.000  14.000 -15.200
HETATM 3773  O   DUM  3773      14.000  14.000  15.200
HETATM 3774  N   DUM  3774      14.000  16.000 -15.200
HETATM 3774  O   DUM  3774      14.000  16.000  15.200
HETATM 3775  N   DUM  3775      14.000  18.000 -15.200
HETATM 3775  O   DUM  3775      14.000  18.000  15.200
HETATM 3776  N   DUM  3776      14.000  20.000 -15.200
HETATM 3776  O   DUM  3776      14.000  20.000  15.200
HETATM 3837  N   DUM  3837      16.000 -20.000 -15.200
HETATM 3837  O   DUM  3837      16.000 -20.000  15.200
HETATM 3838  N   DUM  3838      16.000 -18.000 -15.200
HETATM 3838  O   DUM  3838      16.000 -18.000  15.200
HETATM 3839  N   DUM  3839      16.000 -16.000 -15.200
HETATM 3839  O   DUM  3839      16.000 -16.000  15.200
HETATM 3840  N   DUM  3840      16.000 -14.000 -15.200
HETATM 3840  O   DUM  3840      16.000 -14.000  15.200
HETATM 3841  N   DUM  3841      16.000 -12.000 -15.200
HETATM 3841  O   DUM  3841      16.000 -12.000  15.200
HETATM 3842  N   DUM  3842      16.000 -10.000 -15.200
HETATM 3842  O   DUM  3842      16.000 -10.000  15.200
HETATM 3843  N   DUM  3843      16.000  -8.000 -15.200
HETATM 3843  O   DUM  3843      16.000  -8.000  15.200
HETATM 3844  N   DUM  3844      16.000  -6.000 -15.200
HETATM 3844  O   DUM  3844      16.000  -6.000  15.200
HETATM 3845  N   DUM  3845      16.000  -4.000 -15.200
HETATM 3845  O   DUM  3845      16.000  -4.000  15.200
HETATM 3846  N   DUM  3846      16.000  -2.000 -15.200
HETATM 3846  O   DUM  3846      16.000  -2.000  15.200
HETATM 3847  N   DUM  3847      16.000   0.000 -15.200
HETATM 3847  O   DUM  3847      16.000   0.000  15.200
HETATM 3848  N   DUM  3848      16.000   2.000 -15.200
HETATM 3848  O   DUM  3848      16.000   2.000  15.200
HETATM 3849  N   DUM  3849      16.000   4.000 -15.200
HETATM 3849  O   DUM  3849      16.000   4.000  15.200
HETATM 3850  N   DUM  3850      16.000   6.000 -15.200
HETATM 3850  O   DUM  3850      16.000   6.000  15.200
HETATM 3851  N   DUM  3851      16.000   8.000 -15.200
HETATM 3851  O   DUM  3851      16.000   8.000  15.200
HETATM 3852  N   DUM  3852      16.000  10.000 -15.200
HETATM 3852  O   DUM  3852      16.000  10.000  15.200
HETATM 3853  N   DUM  3853      16.000  12.000 -15.200
HETATM 3853  O   DUM  3853      16.000  12.000  15.200
HETATM 3854  N   DUM  3854      16.000  14.000 -15.200
HETATM 3854  O   DUM  3854      16.000  14.000  15.200
HETATM 3855  N   DUM  3855      16.000  16.000 -15.200
HETATM 3855  O   DUM  3855      16.000  16.000  15.200
HETATM 3856  N   DUM  3856      16.000  18.000 -15.200
HETATM 3856  O   DUM  3856      16.000  18.000  15.200
HETATM 3857  N   DUM  3857      16.000  20.000 -15.200
HETATM 3857  O   DUM  3857      16.000  20.000  15.200
HETATM 3919  N   DUM  3919      18.000 -18.000 -15.200
HETATM 3919  O   DUM  3919      18.000 -18.000  15.200
HETATM 3920  N   DUM  3920      18.000 -16.000 -15.200
HETATM 3920  O   DUM  3920      18.000 -16.000  15.200
HETATM 3921  N   DUM  3921      18.000 -14.000 -15.200
HETATM 3921  O   DUM  3921      18.000 -14.000  15.200
HETATM 3922  N   DUM  3922      18.000 -12.000 -15.200
HETATM 3922  O   DUM  3922      18.000 -12.000  15.200
HETATM 3923  N   DUM  3923      18.000 -10.000 -15.200
HETATM 3923  O   DUM  3923      18.000 -10.000  15.200
HETATM 3924  N   DUM  3924      18.000  -8.000 -15.200
HETATM 3924  O   DUM  3924      18.000  -8.000  15.200
HETATM 3925  N   DUM  3925      18.000  -6.000 -15.200
HETATM 3925  O   DUM  3925      18.000  -6.000  15.200
HETATM 3926  N   DUM  3926      18.000  -4.000 -15.200
HETATM 3926  O   DUM  3926      18.000  -4.000  15.200
HETATM 3927  N   DUM  3927      18.000  -2.000 -15.200
HETATM 3927  O   DUM  3927      18.000  -2.000  15.200
HETATM 3928  N   DUM  3928      18.000   0.000 -15.200
HETATM 3928  O   DUM  3928      18.000   0.000  15.200
HETATM 3929  N   DUM  3929      18.000   2.000 -15.200
HETATM 3929  O   DUM  3929      18.000   2.000  15.200
HETATM 3930  N   DUM  3930      18.000   4.000 -15.200
HETATM 3930  O   DUM  3930      18.000   4.000  15.200
HETATM 3931  N   DUM  3931      18.000   6.000 -15.200
HETATM 3931  O   DUM  3931      18.000   6.000  15.200
HETATM 3932  N   DUM  3932      18.000   8.000 -15.200
HETATM 3932  O   DUM  3932      18.000   8.000  15.200
HETATM 3933  N   DUM  3933      18.000  10.000 -15.200
HETATM 3933  O   DUM  3933      18.000  10.000  15.200
HETATM 3934  N   DUM  3934      18.000  12.000 -15.200
HETATM 3934  O   DUM  3934      18.000  12.000  15.200
HETATM 3935  N   DUM  3935      18.000  14.000 -15.200
HETATM 3935  O   DUM  3935      18.000  14.000  15.200
HETATM 3936  N   DUM  3936      18.000  16.000 -15.200
HETATM 3936  O   DUM  3936      18.000  16.000  15.200
HETATM 3937  N   DUM  3937      18.000  18.000 -15.200
HETATM 3937  O   DUM  3937      18.000  18.000  15.200
HETATM 4001  N   DUM  4001      20.000 -16.000 -15.200
HETATM 4001  O   DUM  4001      20.000 -16.000  15.200
HETATM 4002  N   DUM  4002      20.000 -14.000 -15.200
HETATM 4002  O   DUM  4002      20.000 -14.000  15.200
HETATM 4003  N   DUM  4003      20.000 -12.000 -15.200
HETATM 4003  O   DUM  4003      20.000 -12.000  15.200
HETATM 4004  N   DUM  4004      20.000 -10.000 -15.200
HETATM 4004  O   DUM  4004      20.000 -10.000  15.200
HETATM 4005  N   DUM  4005      20.000  -8.000 -15.200
HETATM 4005  O   DUM  4005      20.000  -8.000  15.200
HETATM 4006  N   DUM  4006      20.000  -6.000 -15.200
HETATM 4006  O   DUM  4006      20.000  -6.000  15.200
HETATM 4007  N   DUM  4007      20.000  -4.000 -15.200
HETATM 4007  O   DUM  4007      20.000  -4.000  15.200
HETATM 4008  N   DUM  4008      20.000  -2.000 -15.200
HETATM 4008  O   DUM  4008      20.000  -2.000  15.200
HETATM 4009  N   DUM  4009      20.000   0.000 -15.200
HETATM 4009  O   DUM  4009      20.000   0.000  15.200
HETATM 4010  N   DUM  4010      20.000   2.000 -15.200
HETATM 4010  O   DUM  4010      20.000   2.000  15.200
HETATM 4011  N   DUM  4011      20.000   4.000 -15.200
HETATM 4011  O   DUM  4011      20.000   4.000  15.200
HETATM 4012  N   DUM  4012      20.000   6.000 -15.200
HETATM 4012  O   DUM  4012      20.000   6.000  15.200
HETATM 4013  N   DUM  4013      20.000   8.000 -15.200
HETATM 4013  O   DUM  4013      20.000   8.000  15.200
HETATM 4014  N   DUM  4014      20.000  10.000 -15.200
HETATM 4014  O   DUM  4014      20.000  10.000  15.200
HETATM 4015  N   DUM  4015      20.000  12.000 -15.200
HETATM 4015  O   DUM  4015      20.000  12.000  15.200
HETATM 4016  N   DUM  4016      20.000  14.000 -15.200
HETATM 4016  O   DUM  4016      20.000  14.000  15.200
HETATM 4017  N   DUM  4017      20.000  16.000 -15.200
HETATM 4017  O   DUM  4017      20.000  16.000  15.200
HETATM 4084  N   DUM  4084      22.000 -12.000 -15.200
HETATM 4084  O   DUM  4084      22.000 -12.000  15.200
HETATM 4085  N   DUM  4085      22.000 -10.000 -15.200
HETATM 4085  O   DUM  4085      22.000 -10.000  15.200
HETATM 4086  N   DUM  4086      22.000  -8.000 -15.200
HETATM 4086  O   DUM  4086      22.000  -8.000  15.200
HETATM 4087  N   DUM  4087      22.000  -6.000 -15.200
HETATM 4087  O   DUM  4087      22.000  -6.000  15.200
HETATM 4088  N   DUM  4088      22.000  -4.000 -15.200
HETATM 4088  O   DUM  4088      22.000  -4.000  15.200
HETATM 4089  N   DUM  4089      22.000  -2.000 -15.200
HETATM 4089  O   DUM  4089      22.000  -2.000  15.200
HETATM 4090  N   DUM  4090      22.000   0.000 -15.200
HETATM 4090  O   DUM  4090      22.000   0.000  15.200
HETATM 4091  N   DUM  4091      22.000   2.000 -15.200
HETATM 4091  O   DUM  4091      22.000   2.000  15.200
HETATM 4092  N   DUM  4092      22.000   4.000 -15.200
HETATM 4092  O   DUM  4092      22.000   4.000  15.200
HETATM 4093  N   DUM  4093      22.000   6.000 -15.200
HETATM 4093  O   DUM  4093      22.000   6.000  15.200
HETATM 4094  N   DUM  4094      22.000   8.000 -15.200
HETATM 4094  O   DUM  4094      22.000   8.000  15.200
HETATM 4095  N   DUM  4095      22.000  10.000 -15.200
HETATM 4095  O   DUM  4095      22.000  10.000  15.200
HETATM 4096  N   DUM  4096      22.000  12.000 -15.200
HETATM 4096  O   DUM  4096      22.000  12.000  15.200
HETATM 4167  N   DUM  4167      24.000  -8.000 -15.200
HETATM 4167  O   DUM  4167      24.000  -8.000  15.200
HETATM 4168  N   DUM  4168      24.000  -6.000 -15.200
HETATM 4168  O   DUM  4168      24.000  -6.000  15.200
HETATM 4169  N   DUM  4169      24.000  -4.000 -15.200
HETATM 4169  O   DUM  4169      24.000  -4.000  15.200
HETATM 4170  N   DUM  4170      24.000  -2.000 -15.200
HETATM 4170  O   DUM  4170      24.000  -2.000  15.200
HETATM 4171  N   DUM  4171      24.000   0.000 -15.200
HETATM 4171  O   DUM  4171      24.000   0.000  15.200
HETATM 4172  N   DUM  4172      24.000   2.000 -15.200
HETATM 4172  O   DUM  4172      24.000   2.000  15.200
HETATM 4173  N   DUM  4173      24.000   4.000 -15.200
HETATM 4173  O   DUM  4173      24.000   4.000  15.200
HETATM 4174  N   DUM  4174      24.000   6.000 -15.200
HETATM 4174  O   DUM  4174      24.000   6.000  15.200
HETATM 4175  N   DUM  4175      24.000   8.000 -15.200
HETATM 4175  O   DUM  4175      24.000   8.000  15.200



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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.