HEADER    PROTON TRANSPORT                        10-JUL-15   5AX0              
TITLE     CRYSTAL STRUCTURE OF THE CELL-FREE SYNTHESIZED MEMBRANE PROTEIN,      
TITLE    2 ACETABULARIA RHODOPSIN I, AT 1.52 ANGSTROM                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RHODOPSIN I;                                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 1-237;                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ACETABULARIA ACETABULUM;                        
SOURCE   3 ORGANISM_COMMON: MERMAID'S WINE GLASS;                               
SOURCE   4 ORGANISM_TAXID: 35845;                                               
SOURCE   5 GENE: AOPI;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PROTON TRANSPORT, MEMBRANE PROTEIN, RETINAL, WATER CLUSTER, GREEN     
KEYWDS   2 ALGAE, PHOTOTAXIS, CELL-FREE SYNTHESIS, MICROBIAL-TYPE RHODOPSIN,    
KEYWDS   3 LIGHT-DRIVEN PROTON PUMP                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.FURUSE,T.HOSAKA,T.KIMURA-SOMEYA,S.YOKOYAMA,M.SHIROUZU               
REVDAT   4   08-NOV-23 5AX0    1       REMARK                                   
REVDAT   3   26-FEB-20 5AX0    1       REMARK                                   
REVDAT   2   18-NOV-15 5AX0    1       JRNL                                     
REVDAT   1   26-AUG-15 5AX0    0                                                
SPRSDE     26-AUG-15 5AX0      3WT9                                             
JRNL        AUTH   M.FURUSE,J.TAMOGAMI,T.HOSAKA,T.KIKUKAWA,N.SHINYA,M.HATO,     
JRNL        AUTH 2 N.OHSAWA,S.Y.KIM,K.H.JUNG,M.DEMURA,S.MIYAUCHI,N.KAMO,        
JRNL        AUTH 3 K.SHIMONO,T.KIMURA-SOMEYA,S.YOKOYAMA,M.SHIROUZU              
JRNL        TITL   STRUCTURAL BASIS FOR THE SLOW PHOTOCYCLE AND LATE PROTON     
JRNL        TITL 2 RELEASE IN ACETABULARIA RHODOPSIN I FROM THE MARINE PLANT    
JRNL        TITL 3 ACETABULARIA ACETABULUM                                      
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  71  2203 2015              
JRNL        REFN                   ESSN 1399-0047                               
JRNL        PMID   26527138                                                     
JRNL        DOI    10.1107/S1399004715015722                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.52 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1690                                      
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.52                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.21                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 44149                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.196                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.160                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1836                            
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 38.2223 -  3.5751    0.96     3206   140  0.2004 0.2224        
REMARK   3     2  3.5751 -  2.8379    1.00     3294   142  0.1702 0.1904        
REMARK   3     3  2.8379 -  2.4793    1.00     3274   143  0.1506 0.1613        
REMARK   3     4  2.4793 -  2.2526    1.00     3271   142  0.1462 0.1595        
REMARK   3     5  2.2526 -  2.0912    1.00     3268   141  0.1370 0.1801        
REMARK   3     6  2.0912 -  1.9679    1.00     3265   142  0.1454 0.1807        
REMARK   3     7  1.9679 -  1.8693    1.00     3263   142  0.1586 0.1685        
REMARK   3     8  1.8693 -  1.7880    1.00     3288   142  0.1678 0.1909        
REMARK   3     9  1.7880 -  1.7191    1.00     3253   141  0.1885 0.2155        
REMARK   3    10  1.7191 -  1.6598    1.00     3264   142  0.2085 0.2096        
REMARK   3    11  1.6598 -  1.6079    1.00     3247   141  0.2312 0.2385        
REMARK   3    12  1.6079 -  1.5619    1.00     3243   142  0.2518 0.2713        
REMARK   3    13  1.5619 -  1.5208    0.97     3177   136  0.2738 0.2761        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.140            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.570           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.49                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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      :  0.006           2030                                  
REMARK   3   ANGLE     :  0.919           2727                                  
REMARK   3   CHIRALITY :  0.046            310                                  
REMARK   3   PLANARITY :  0.006            319                                  
REMARK   3   DIHEDRAL  : 16.304            758                                  
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 9 THROUGH 167 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):    6.125   50.280   25.821              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1547 T22:   0.1644                                     
REMARK   3      T33:   0.1693 T12:   0.0008                                     
REMARK   3      T13:   0.0292 T23:   0.0099                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5350 L22:   1.7107                                     
REMARK   3      L33:   1.3281 L12:  -0.1674                                     
REMARK   3      L13:  -0.2799 L23:   0.0537                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0071 S12:   0.0564 S13:  -0.0203                       
REMARK   3      S21:  -0.0437 S22:   0.0189 S23:   0.0521                       
REMARK   3      S31:  -0.0642 S32:  -0.1581 S33:  -0.0085                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 168 THROUGH 201 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   12.934   48.675   33.746              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2001 T22:   0.1582                                     
REMARK   3      T33:   0.1692 T12:  -0.0148                                     
REMARK   3      T13:   0.0417 T23:  -0.0033                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4011 L22:   2.7373                                     
REMARK   3      L33:   1.9192 L12:   0.1740                                     
REMARK   3      L13:   0.0185 L23:  -0.4465                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0240 S12:   0.1261 S13:  -0.3363                       
REMARK   3      S21:   0.0123 S22:  -0.0021 S23:  -0.1093                       
REMARK   3      S31:   0.3009 S32:  -0.0139 S33:   0.0094                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 202 THROUGH 235 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   16.680   48.097   23.678              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1782 T22:   0.1614                                     
REMARK   3      T33:   0.1811 T12:  -0.0014                                     
REMARK   3      T13:   0.0396 T23:   0.0098                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1537 L22:   3.7045                                     
REMARK   3      L33:   1.7218 L12:  -0.7897                                     
REMARK   3      L13:  -0.4825 L23:   1.4914                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0207 S12:   0.0471 S13:  -0.0315                       
REMARK   3      S21:  -0.0286 S22:   0.0438 S23:   0.0601                       
REMARK   3      S31:  -0.0769 S32:  -0.0180 S33:  -0.0391                       
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 5AX0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-JUL-15.                  
REMARK 100 THE DEPOSITION ID IS D_1300000112.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-JUL-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL32XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44164                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.520                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.210                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07510                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.1900                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.52                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.770                              
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: 1C3W                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG400, 0.1M HEPES/NAOH, 0.2M        
REMARK 280  NACL, 10MM MGCL2, 2.5% MPD, PH 7.0, LIPIDIC CUBIC PHASE,            
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       37.99500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       50.81500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       37.99500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       50.81500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1110 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -6                                                      
REMARK 465     SER A    -5                                                      
REMARK 465     SER A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     LEU A   236                                                      
REMARK 465     GLY A   237                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A 218      -80.72   -115.60                                   
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 RET A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLB A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLB A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLB A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue D12 A 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue C14 A 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue R16 A 308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue D10 A 309                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5AWZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5AX1   RELATED DB: PDB                                   
DBREF  5AX0 A    1   237  UNP    G3CEP6   G3CEP6_ACEAT     1    237             
SEQADV 5AX0 GLY A   -6  UNP  G3CEP6              EXPRESSION TAG                 
SEQADV 5AX0 SER A   -5  UNP  G3CEP6              EXPRESSION TAG                 
SEQADV 5AX0 SER A   -4  UNP  G3CEP6              EXPRESSION TAG                 
SEQADV 5AX0 GLY A   -3  UNP  G3CEP6              EXPRESSION TAG                 
SEQADV 5AX0 SER A   -2  UNP  G3CEP6              EXPRESSION TAG                 
SEQADV 5AX0 SER A   -1  UNP  G3CEP6              EXPRESSION TAG                 
SEQADV 5AX0 GLY A    0  UNP  G3CEP6              EXPRESSION TAG                 
SEQRES   1 A  244  GLY SER SER GLY SER SER GLY MET SER ASN PRO ASN PRO          
SEQRES   2 A  244  PHE GLN THR THR LEU GLY THR ASP ALA GLN TRP VAL VAL          
SEQRES   3 A  244  PHE ALA VAL MET ALA LEU ALA ALA ILE VAL PHE SER ILE          
SEQRES   4 A  244  ALA VAL GLN PHE ARG PRO LEU PRO LEU ARG LEU THR TYR          
SEQRES   5 A  244  TYR VAL ASN ILE ALA ILE CYS THR ILE ALA ALA THR ALA          
SEQRES   6 A  244  TYR TYR ALA MET ALA VAL ASN GLY GLY ASP ASN LYS PRO          
SEQRES   7 A  244  THR ALA GLY THR GLY ALA ASP GLU ARG GLN VAL ILE TYR          
SEQRES   8 A  244  ALA ARG TYR ILE ASP TRP VAL PHE THR THR PRO LEU LEU          
SEQRES   9 A  244  LEU LEU ASP LEU VAL LEU LEU THR ASN MET PRO ALA THR          
SEQRES  10 A  244  MET ILE ALA TRP ILE MET GLY ALA ASP ILE ALA MET ILE          
SEQRES  11 A  244  ALA PHE GLY ILE ILE GLY ALA PHE THR VAL GLY SER TYR          
SEQRES  12 A  244  LYS TRP PHE TYR PHE VAL VAL GLY CYS ILE MET LEU ALA          
SEQRES  13 A  244  VAL LEU ALA TRP GLY MET ILE ASN PRO ILE PHE LYS GLU          
SEQRES  14 A  244  GLU LEU GLN LYS HIS LYS GLU TYR THR GLY ALA TYR THR          
SEQRES  15 A  244  THR LEU LEU ILE TYR LEU ILE VAL LEU TRP VAL ILE TYR          
SEQRES  16 A  244  PRO ILE VAL TRP GLY LEU GLY ALA GLY GLY HIS ILE ILE          
SEQRES  17 A  244  GLY VAL ASP VAL GLU ILE ILE ALA MET GLY ILE LEU ASP          
SEQRES  18 A  244  LEU LEU ALA LYS PRO LEU TYR ALA ILE GLY VAL LEU ILE          
SEQRES  19 A  244  THR VAL GLU VAL VAL TYR GLY LYS LEU GLY                      
HET    RET  A 301      20                                                       
HET    OLB  A 302      25                                                       
HET    OLB  A 303      25                                                       
HET    OLB  A 304      25                                                       
HET    D12  A 305      12                                                       
HET    D12  A 306      12                                                       
HET    C14  A 307      14                                                       
HET    R16  A 308      16                                                       
HET    D10  A 309      10                                                       
HET    D10  A 310      10                                                       
HETNAM     RET RETINAL                                                          
HETNAM     OLB (2S)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE                   
HETNAM     D12 DODECANE                                                         
HETNAM     C14 TETRADECANE                                                      
HETNAM     R16 HEXADECANE                                                       
HETNAM     D10 DECANE                                                           
FORMUL   2  RET    C20 H28 O                                                    
FORMUL   3  OLB    3(C21 H40 O4)                                                
FORMUL   6  D12    2(C12 H26)                                                   
FORMUL   8  C14    C14 H30                                                      
FORMUL   9  R16    C16 H34                                                      
FORMUL  10  D10    2(C10 H22)                                                   
FORMUL  12  HOH   *97(H2 O)                                                     
HELIX    1 AA1 THR A    9  GLN A   35  1                                  27    
HELIX    2 AA2 PRO A   38  GLY A   66  1                                  29    
HELIX    3 AA3 GLY A   67  ASN A   69  5                                   3    
HELIX    4 AA4 THR A   75  GLU A   79  5                                   5    
HELIX    5 AA5 TYR A   84  LEU A  103  1                                  20    
HELIX    6 AA6 PRO A  108  THR A  132  1                                  25    
HELIX    7 AA7 TYR A  136  LYS A  161  1                                  26    
HELIX    8 AA8 GLU A  162  GLN A  165  5                                   4    
HELIX    9 AA9 HIS A  167  GLU A  169  5                                   3    
HELIX   10 AB1 TYR A  170  GLY A  195  1                                  26    
HELIX   11 AB2 GLY A  202  LYS A  218  1                                  17    
HELIX   12 AB3 LYS A  218  LYS A  235  1                                  18    
SHEET    1 AA1 2 THR A  72  ALA A  73  0                                        
SHEET    2 AA1 2 ARG A  80  GLN A  81 -1  O  ARG A  80   N  ALA A  73           
LINK         NZ  LYS A 218                 C15 RET A 301     1555   1555  1.27  
CISPEP   1 LYS A   70    PRO A   71          0        -4.42                     
SITE     1 AC1  8 TRP A  90  MET A 122  GLY A 144  TRP A 185                    
SITE     2 AC1  8 TYR A 188  PRO A 189  ASP A 214  LYS A 218                    
SITE     1 AC2  9 ALA A  58  ASN A  65  LYS A  70  TYR A  84                    
SITE     2 AC2  9 ALA A  85  ILE A  88  PHE A  92  D10 A 309                    
SITE     3 AC2  9 HOH A 465                                                     
SITE     1 AC3  5 LEU A  11  VAL A 183  VAL A 205  ILE A 208                    
SITE     2 AC3  5 C14 A 307                                                     
SITE     1 AC4  7 PRO A  95  LEU A  96  VAL A 102  THR A 105                    
SITE     2 AC4  7 ASN A 106  MET A 107  LYS A 166                               
SITE     1 AC5  3 GLN A  35  TRP A 114  ALA A 121                               
SITE     1 AC6  1 OLB A 303                                                     
SITE     1 AC7  2 TRP A 138  PHE A 141                                          
SITE     1 AC8  3 THR A  53  THR A  57  OLB A 302                               
CRYST1   75.990  101.630   43.760  90.00 119.17  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013160  0.000000  0.007346        0.00000                         
SCALE2      0.000000  0.009840  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.026171        0.00000                         
ATOM      1  N   SER A   2      10.275  75.384  40.821  1.00 54.13           N  
ATOM      2  CA  SER A   2       8.968  75.962  40.538  1.00 49.24           C  
ATOM      3  C   SER A   2       8.509  75.727  39.097  1.00 32.91           C  
ATOM      4  O   SER A   2       8.500  76.658  38.302  1.00 37.18           O  
ATOM      5  CB  SER A   2       8.967  77.461  40.827  1.00 58.06           C  
ATOM      6  OG  SER A   2       7.659  78.000  40.777  1.00 64.03           O  
ATOM      7  N   ASN A   3       8.151  74.486  38.765  1.00 33.23           N  
ATOM      8  CA  ASN A   3       7.682  74.142  37.425  1.00 29.86           C  
ATOM      9  C   ASN A   3       8.632  74.680  36.347  1.00 26.31           C  
ATOM     10  O   ASN A   3       8.217  75.436  35.462  1.00 25.94           O  
ATOM     11  CB  ASN A   3       6.266  74.658  37.201  1.00 30.14           C  
ATOM     12  CG  ASN A   3       5.639  74.158  35.907  1.00 25.52           C  
ATOM     13  OD1 ASN A   3       5.964  73.069  35.417  1.00 24.39           O  
ATOM     14  ND2 ASN A   3       4.753  74.966  35.332  1.00 25.68           N  
ATOM     15  N   PRO A   4       9.904  74.297  36.388  1.00 27.15           N  
ATOM     16  CA  PRO A   4      10.874  74.857  35.440  1.00 27.63           C  
ATOM     17  C   PRO A   4      10.630  74.375  34.016  1.00 26.03           C  
ATOM     18  O   PRO A   4      10.175  73.255  33.785  1.00 25.65           O  
ATOM     19  CB  PRO A   4      12.211  74.332  35.970  1.00 27.73           C  
ATOM     20  CG  PRO A   4      11.847  73.010  36.580  1.00 26.03           C  
ATOM     21  CD  PRO A   4      10.526  73.289  37.270  1.00 27.26           C  
ATOM     22  N   ASN A   5      10.950  75.247  33.060  1.00 29.02           N  
ATOM     23  CA  ASN A   5      10.963  74.947  31.629  1.00 24.94           C  
ATOM     24  C   ASN A   5       9.768  74.072  31.222  1.00 25.12           C  
ATOM     25  O   ASN A   5       9.955  72.945  30.750  1.00 24.00           O  
ATOM     26  CB  ASN A   5      12.282  74.285  31.238  1.00 27.37           C  
ATOM     27  CG  ASN A   5      13.490  75.082  31.708  1.00 36.21           C  
ATOM     28  OD1 ASN A   5      14.307  74.595  32.492  1.00 42.11           O  
ATOM     29  ND2 ASN A   5      13.601  76.312  31.234  1.00 37.44           N  
ATOM     30  N   PRO A   6       8.537  74.550  31.420  1.00 21.01           N  
ATOM     31  CA  PRO A   6       7.360  73.680  31.314  1.00 20.88           C  
ATOM     32  C   PRO A   6       6.834  73.478  29.901  1.00 23.27           C  
ATOM     33  O   PRO A   6       5.763  72.882  29.749  1.00 22.14           O  
ATOM     34  CB  PRO A   6       6.322  74.414  32.181  1.00 22.17           C  
ATOM     35  CG  PRO A   6       6.678  75.848  31.990  1.00 26.38           C  
ATOM     36  CD  PRO A   6       8.179  75.898  31.900  1.00 24.55           C  
ATOM     37  N   PHE A   7       7.564  73.908  28.868  1.00 21.43           N  
ATOM     38  CA  PHE A   7       7.165  73.689  27.485  1.00 22.18           C  
ATOM     39  C   PHE A   7       8.338  73.167  26.671  1.00 22.18           C  
ATOM     40  O   PHE A   7       9.489  73.533  26.910  1.00 25.49           O  
ATOM     41  CB  PHE A   7       6.620  74.973  26.849  1.00 24.13           C  
ATOM     42  CG  PHE A   7       5.351  75.434  27.482  1.00 24.52           C  
ATOM     43  CD1 PHE A   7       4.135  74.946  27.036  1.00 25.98           C  
ATOM     44  CD2 PHE A   7       5.374  76.311  28.555  1.00 24.04           C  
ATOM     45  CE1 PHE A   7       2.952  75.345  27.640  1.00 28.24           C  
ATOM     46  CE2 PHE A   7       4.194  76.704  29.176  1.00 28.64           C  
ATOM     47  CZ  PHE A   7       2.983  76.220  28.711  1.00 28.91           C  
ATOM     48  N   GLN A   8       8.022  72.326  25.688  1.00 21.55           N  
ATOM     49  CA  GLN A   8       9.039  71.830  24.774  1.00 23.00           C  
ATOM     50  C   GLN A   8       9.665  72.974  23.983  1.00 23.11           C  
ATOM     51  O   GLN A   8       8.969  73.876  23.501  1.00 25.11           O  
ATOM     52  CB  GLN A   8       8.419  70.794  23.837  1.00 22.45           C  
ATOM     53  CG  GLN A   8       9.398  70.148  22.858  1.00 20.67           C  
ATOM     54  CD  GLN A   8       8.789  68.974  22.131  1.00 21.32           C  
ATOM     55  OE1 GLN A   8       7.901  68.295  22.656  1.00 21.52           O  
ATOM     56  NE2 GLN A   8       9.265  68.720  20.922  1.00 21.27           N  
ATOM     57  N   THR A   9      10.990  72.955  23.883  1.00 21.98           N  
ATOM     58  CA  THR A   9      11.736  73.881  23.036  1.00 23.29           C  
ATOM     59  C   THR A   9      12.456  73.091  21.949  1.00 22.25           C  
ATOM     60  O   THR A   9      12.336  71.866  21.851  1.00 22.53           O  
ATOM     61  CB  THR A   9      12.753  74.695  23.838  1.00 28.01           C  
ATOM     62  OG1 THR A   9      13.887  73.871  24.143  1.00 29.54           O  
ATOM     63  CG2 THR A   9      12.131  75.234  25.128  1.00 31.38           C  
ATOM     64  N   THR A  10      13.232  73.818  21.138  1.00 24.47           N  
ATOM     65  CA  THR A  10      13.999  73.173  20.075  1.00 25.93           C  
ATOM     66  C   THR A  10      14.960  72.121  20.620  1.00 27.73           C  
ATOM     67  O   THR A  10      15.279  71.153  19.919  1.00 27.88           O  
ATOM     68  CB  THR A  10      14.759  74.226  19.269  1.00 32.69           C  
ATOM     69  OG1 THR A  10      15.616  74.969  20.141  1.00 38.96           O  
ATOM     70  CG2 THR A  10      13.781  75.177  18.624  1.00 33.57           C  
ATOM     71  N   LEU A  11      15.428  72.272  21.862  1.00 26.16           N  
ATOM     72  CA  LEU A  11      16.269  71.225  22.452  1.00 28.16           C  
ATOM     73  C   LEU A  11      15.545  69.884  22.485  1.00 27.45           C  
ATOM     74  O   LEU A  11      16.102  68.844  22.097  1.00 26.35           O  
ATOM     75  CB  LEU A  11      16.699  71.619  23.862  1.00 29.12           C  
ATOM     76  CG  LEU A  11      17.507  70.548  24.599  1.00 38.06           C  
ATOM     77  CD1 LEU A  11      18.839  70.310  23.902  1.00 42.81           C  
ATOM     78  CD2 LEU A  11      17.721  70.922  26.051  1.00 42.65           C  
ATOM     79  N   GLY A  12      14.302  69.880  22.961  1.00 22.90           N  
ATOM     80  CA  GLY A  12      13.569  68.632  23.029  1.00 20.27           C  
ATOM     81  C   GLY A  12      13.206  68.108  21.654  1.00 21.85           C  
ATOM     82  O   GLY A  12      13.243  66.899  21.412  1.00 20.85           O  
ATOM     83  N   THR A  13      12.852  69.011  20.738  1.00 21.79           N  
ATOM     84  CA  THR A  13      12.537  68.608  19.371  1.00 21.37           C  
ATOM     85  C   THR A  13      13.738  67.950  18.711  1.00 23.81           C  
ATOM     86  O   THR A  13      13.610  66.898  18.078  1.00 22.88           O  
ATOM     87  CB  THR A  13      12.079  69.817  18.561  1.00 23.81           C  
ATOM     88  OG1 THR A  13      10.963  70.423  19.219  1.00 24.48           O  
ATOM     89  CG2 THR A  13      11.683  69.407  17.143  1.00 25.72           C  
ATOM     90  N   ASP A  14      14.921  68.549  18.865  1.00 24.38           N  
ATOM     91  CA  ASP A  14      16.119  67.962  18.268  1.00 27.25           C  
ATOM     92  C   ASP A  14      16.391  66.571  18.824  1.00 24.91           C  
ATOM     93  O   ASP A  14      16.767  65.657  18.076  1.00 22.48           O  
ATOM     94  CB  ASP A  14      17.318  68.874  18.498  1.00 27.89           C  
ATOM     95  CG  ASP A  14      17.229  70.146  17.691  1.00 37.01           C  
ATOM     96  OD1 ASP A  14      16.406  70.178  16.748  1.00 35.86           O  
ATOM     97  OD2 ASP A  14      17.973  71.104  17.992  1.00 42.33           O  
ATOM     98  N   ALA A  15      16.190  66.385  20.132  1.00 22.74           N  
ATOM     99  CA  ALA A  15      16.383  65.067  20.727  1.00 20.26           C  
ATOM    100  C   ALA A  15      15.416  64.049  20.135  1.00 19.70           C  
ATOM    101  O   ALA A  15      15.788  62.896  19.884  1.00 21.24           O  
ATOM    102  CB  ALA A  15      16.203  65.151  22.248  1.00 20.07           C  
ATOM    103  N   GLN A  16      14.164  64.456  19.913  1.00 18.41           N  
ATOM    104  CA  GLN A  16      13.168  63.541  19.357  1.00 17.94           C  
ATOM    105  C   GLN A  16      13.517  63.121  17.929  1.00 18.97           C  
ATOM    106  O   GLN A  16      13.304  61.956  17.557  1.00 18.15           O  
ATOM    107  CB  GLN A  16      11.791  64.194  19.392  1.00 18.44           C  
ATOM    108  CG  GLN A  16      11.230  64.276  20.801  1.00 17.91           C  
ATOM    109  CD  GLN A  16      10.081  65.255  20.922  1.00 18.81           C  
ATOM    110  OE1 GLN A  16       9.837  66.073  20.040  1.00 19.69           O  
ATOM    111  NE2 GLN A  16       9.370  65.176  22.036  1.00 20.81           N  
ATOM    112  N   TRP A  17      14.041  64.049  17.120  1.00 19.00           N  
ATOM    113  CA  TRP A  17      14.452  63.693  15.761  1.00 18.36           C  
ATOM    114  C   TRP A  17      15.591  62.688  15.782  1.00 20.71           C  
ATOM    115  O   TRP A  17      15.645  61.786  14.939  1.00 20.68           O  
ATOM    116  CB  TRP A  17      14.868  64.930  14.963  1.00 20.47           C  
ATOM    117  CG  TRP A  17      13.716  65.732  14.431  1.00 20.78           C  
ATOM    118  CD1 TRP A  17      13.429  67.032  14.709  1.00 23.69           C  
ATOM    119  CD2 TRP A  17      12.681  65.270  13.555  1.00 25.70           C  
ATOM    120  NE1 TRP A  17      12.284  67.419  14.054  1.00 24.62           N  
ATOM    121  CE2 TRP A  17      11.810  66.358  13.331  1.00 25.00           C  
ATOM    122  CE3 TRP A  17      12.408  64.045  12.933  1.00 28.21           C  
ATOM    123  CZ2 TRP A  17      10.686  66.257  12.515  1.00 31.03           C  
ATOM    124  CZ3 TRP A  17      11.294  63.949  12.120  1.00 29.98           C  
ATOM    125  CH2 TRP A  17      10.444  65.048  11.921  1.00 32.60           C  
ATOM    126  N   VAL A  18      16.515  62.825  16.736  1.00 18.88           N  
ATOM    127  CA  VAL A  18      17.615  61.862  16.838  1.00 21.04           C  
ATOM    128  C   VAL A  18      17.076  60.475  17.171  1.00 21.02           C  
ATOM    129  O   VAL A  18      17.470  59.471  16.560  1.00 19.85           O  
ATOM    130  CB  VAL A  18      18.648  62.328  17.880  1.00 24.41           C  
ATOM    131  CG1 VAL A  18      19.631  61.190  18.199  1.00 28.47           C  
ATOM    132  CG2 VAL A  18      19.394  63.556  17.379  1.00 27.31           C  
ATOM    133  N   VAL A  19      16.161  60.386  18.140  1.00 18.93           N  
ATOM    134  CA  VAL A  19      15.636  59.080  18.512  1.00 17.53           C  
ATOM    135  C   VAL A  19      14.820  58.503  17.370  1.00 17.93           C  
ATOM    136  O   VAL A  19      14.915  57.312  17.074  1.00 18.36           O  
ATOM    137  CB  VAL A  19      14.812  59.178  19.809  1.00 18.33           C  
ATOM    138  CG1 VAL A  19      14.190  57.815  20.138  1.00 19.05           C  
ATOM    139  CG2 VAL A  19      15.711  59.642  20.935  1.00 19.23           C  
ATOM    140  N   PHE A  20      14.025  59.343  16.701  1.00 18.86           N  
ATOM    141  CA  PHE A  20      13.316  58.917  15.496  1.00 18.01           C  
ATOM    142  C   PHE A  20      14.251  58.224  14.513  1.00 17.44           C  
ATOM    143  O   PHE A  20      13.969  57.112  14.036  1.00 18.56           O  
ATOM    144  CB  PHE A  20      12.655  60.125  14.821  1.00 18.99           C  
ATOM    145  CG  PHE A  20      12.207  59.854  13.408  1.00 20.71           C  
ATOM    146  CD1 PHE A  20      11.119  59.029  13.155  1.00 20.28           C  
ATOM    147  CD2 PHE A  20      12.892  60.419  12.325  1.00 23.69           C  
ATOM    148  CE1 PHE A  20      10.711  58.785  11.844  1.00 23.52           C  
ATOM    149  CE2 PHE A  20      12.481  60.183  11.014  1.00 24.98           C  
ATOM    150  CZ  PHE A  20      11.395  59.352  10.781  1.00 23.68           C  
ATOM    151  N   ALA A  21      15.363  58.884  14.179  1.00 18.09           N  
ATOM    152  CA  ALA A  21      16.298  58.325  13.205  1.00 19.43           C  
ATOM    153  C   ALA A  21      16.848  56.973  13.648  1.00 19.83           C  
ATOM    154  O   ALA A  21      16.963  56.051  12.830  1.00 20.12           O  
ATOM    155  CB  ALA A  21      17.445  59.304  12.962  1.00 22.20           C  
ATOM    156  N   VAL A  22      17.216  56.836  14.925  1.00 18.86           N  
ATOM    157  CA  VAL A  22      17.755  55.558  15.392  1.00 18.06           C  
ATOM    158  C   VAL A  22      16.680  54.471  15.356  1.00 17.83           C  
ATOM    159  O   VAL A  22      16.944  53.342  14.928  1.00 19.62           O  
ATOM    160  CB  VAL A  22      18.370  55.697  16.798  1.00 20.16           C  
ATOM    161  CG1 VAL A  22      18.907  54.328  17.260  1.00 20.45           C  
ATOM    162  CG2 VAL A  22      19.482  56.743  16.803  1.00 21.01           C  
ATOM    163  N   MET A  23      15.455  54.784  15.798  1.00 17.36           N  
ATOM    164  CA  MET A  23      14.380  53.787  15.776  1.00 19.44           C  
ATOM    165  C   MET A  23      14.070  53.344  14.354  1.00 20.03           C  
ATOM    166  O   MET A  23      13.870  52.149  14.090  1.00 18.48           O  
ATOM    167  CB  MET A  23      13.105  54.343  16.416  1.00 18.33           C  
ATOM    168  CG  MET A  23      13.203  54.698  17.887  1.00 18.50           C  
ATOM    169  SD  MET A  23      13.495  53.233  18.874  1.00 20.72           S  
ATOM    170  CE  MET A  23      13.287  53.983  20.489  1.00 20.37           C  
ATOM    171  N   ALA A  24      14.011  54.303  13.425  1.00 18.66           N  
ATOM    172  CA  ALA A  24      13.748  53.967  12.035  1.00 18.68           C  
ATOM    173  C   ALA A  24      14.862  53.109  11.457  1.00 19.88           C  
ATOM    174  O   ALA A  24      14.592  52.136  10.747  1.00 21.06           O  
ATOM    175  CB  ALA A  24      13.569  55.248  11.219  1.00 20.64           C  
ATOM    176  N   LEU A  25      16.121  53.451  11.758  1.00 18.88           N  
ATOM    177  CA  LEU A  25      17.246  52.655  11.259  1.00 19.83           C  
ATOM    178  C   LEU A  25      17.213  51.238  11.815  1.00 20.16           C  
ATOM    179  O   LEU A  25      17.494  50.271  11.095  1.00 19.81           O  
ATOM    180  CB  LEU A  25      18.568  53.321  11.626  1.00 23.31           C  
ATOM    181  CG  LEU A  25      19.820  52.465  11.451  1.00 32.45           C  
ATOM    182  CD1 LEU A  25      20.135  52.307   9.974  1.00 30.62           C  
ATOM    183  CD2 LEU A  25      21.003  53.074  12.204  1.00 37.10           C  
ATOM    184  N   ALA A  26      16.895  51.093  13.103  1.00 19.04           N  
ATOM    185  CA  ALA A  26      16.816  49.757  13.679  1.00 17.47           C  
ATOM    186  C   ALA A  26      15.747  48.933  12.975  1.00 17.49           C  
ATOM    187  O   ALA A  26      15.971  47.764  12.638  1.00 18.83           O  
ATOM    188  CB  ALA A  26      16.519  49.849  15.179  1.00 19.19           C  
ATOM    189  N   ALA A  27      14.576  49.535  12.741  1.00 18.33           N  
ATOM    190  CA  ALA A  27      13.505  48.806  12.066  1.00 20.04           C  
ATOM    191  C   ALA A  27      13.942  48.347  10.680  1.00 19.19           C  
ATOM    192  O   ALA A  27      13.669  47.207  10.277  1.00 21.02           O  
ATOM    193  CB  ALA A  27      12.256  49.683  11.970  1.00 21.79           C  
ATOM    194  N   ILE A  28      14.644  49.214   9.946  1.00 19.40           N  
ATOM    195  CA  ILE A  28      15.117  48.872   8.603  1.00 20.57           C  
ATOM    196  C   ILE A  28      16.161  47.765   8.663  1.00 21.13           C  
ATOM    197  O   ILE A  28      16.127  46.819   7.869  1.00 22.06           O  
ATOM    198  CB  ILE A  28      15.671  50.131   7.913  1.00 22.29           C  
ATOM    199  CG1 ILE A  28      14.548  51.151   7.708  1.00 28.50           C  
ATOM    200  CG2 ILE A  28      16.342  49.785   6.592  1.00 26.55           C  
ATOM    201  CD1 ILE A  28      15.041  52.527   7.312  1.00 29.66           C  
ATOM    202  N   VAL A  29      17.109  47.867   9.596  1.00 19.23           N  
ATOM    203  CA  VAL A  29      18.163  46.861   9.697  1.00 20.00           C  
ATOM    204  C   VAL A  29      17.576  45.498  10.046  1.00 20.94           C  
ATOM    205  O   VAL A  29      17.946  44.479   9.450  1.00 22.50           O  
ATOM    206  CB  VAL A  29      19.218  47.307  10.727  1.00 21.49           C  
ATOM    207  CG1 VAL A  29      20.152  46.153  11.067  1.00 23.74           C  
ATOM    208  CG2 VAL A  29      20.007  48.512  10.181  1.00 21.82           C  
ATOM    209  N   PHE A  30      16.653  45.460  11.006  1.00 19.02           N  
ATOM    210  CA  PHE A  30      16.026  44.195  11.374  1.00 18.89           C  
ATOM    211  C   PHE A  30      15.214  43.632  10.214  1.00 19.47           C  
ATOM    212  O   PHE A  30      15.142  42.410  10.033  1.00 20.99           O  
ATOM    213  CB  PHE A  30      15.119  44.385  12.593  1.00 17.31           C  
ATOM    214  CG  PHE A  30      15.827  44.815  13.857  1.00 17.88           C  
ATOM    215  CD1 PHE A  30      17.162  44.526  14.074  1.00 21.97           C  
ATOM    216  CD2 PHE A  30      15.115  45.470  14.858  1.00 19.79           C  
ATOM    217  CE1 PHE A  30      17.785  44.925  15.266  1.00 23.02           C  
ATOM    218  CE2 PHE A  30      15.724  45.869  16.042  1.00 22.42           C  
ATOM    219  CZ  PHE A  30      17.058  45.593  16.251  1.00 22.42           C  
ATOM    220  N   SER A  31      14.565  44.508   9.438  1.00 20.52           N  
ATOM    221  CA  SER A  31      13.736  44.055   8.321  1.00 21.39           C  
ATOM    222  C   SER A  31      14.579  43.455   7.202  1.00 20.68           C  
ATOM    223  O   SER A  31      14.157  42.503   6.535  1.00 22.98           O  
ATOM    224  CB  SER A  31      12.888  45.203   7.779  1.00 24.04           C  
ATOM    225  OG  SER A  31      11.947  45.654   8.740  1.00 24.32           O  
ATOM    226  N   ILE A  32      15.768  44.005   6.962  1.00 22.54           N  
ATOM    227  CA  ILE A  32      16.648  43.380   5.978  1.00 24.24           C  
ATOM    228  C   ILE A  32      17.229  42.083   6.535  1.00 27.01           C  
ATOM    229  O   ILE A  32      17.291  41.064   5.836  1.00 30.37           O  
ATOM    230  CB  ILE A  32      17.737  44.383   5.548  1.00 24.74           C  
ATOM    231  CG1 ILE A  32      17.069  45.573   4.863  1.00 25.89           C  
ATOM    232  CG2 ILE A  32      18.726  43.738   4.575  1.00 25.91           C  
ATOM    233  CD1 ILE A  32      17.917  46.842   4.759  1.00 30.07           C  
ATOM    234  N   ALA A  33      17.623  42.089   7.809  1.00 22.75           N  
ATOM    235  CA  ALA A  33      18.286  40.926   8.395  1.00 24.49           C  
ATOM    236  C   ALA A  33      17.384  39.693   8.402  1.00 23.62           C  
ATOM    237  O   ALA A  33      17.837  38.587   8.089  1.00 26.12           O  
ATOM    238  CB  ALA A  33      18.749  41.251   9.815  1.00 26.56           C  
ATOM    239  N   VAL A  34      16.106  39.862   8.763  1.00 23.50           N  
ATOM    240  CA  VAL A  34      15.239  38.699   8.970  1.00 20.83           C  
ATOM    241  C   VAL A  34      15.075  37.870   7.702  1.00 22.76           C  
ATOM    242  O   VAL A  34      14.812  36.666   7.787  1.00 23.85           O  
ATOM    243  CB  VAL A  34      13.867  39.146   9.536  1.00 21.00           C  
ATOM    244  CG1 VAL A  34      13.110  40.008   8.539  1.00 22.54           C  
ATOM    245  CG2 VAL A  34      13.018  37.925   9.951  1.00 20.62           C  
ATOM    246  N   GLN A  35      15.268  38.485   6.524  1.00 25.04           N  
ATOM    247  CA  GLN A  35      15.231  37.786   5.242  1.00 28.38           C  
ATOM    248  C   GLN A  35      16.279  36.691   5.135  1.00 26.85           C  
ATOM    249  O   GLN A  35      16.108  35.762   4.342  1.00 32.66           O  
ATOM    250  CB  GLN A  35      15.432  38.792   4.110  1.00 28.45           C  
ATOM    251  CG  GLN A  35      14.600  40.056   4.287  1.00 31.57           C  
ATOM    252  CD  GLN A  35      13.117  39.754   4.329  1.00 39.61           C  
ATOM    253  OE1 GLN A  35      12.642  38.815   3.681  1.00 44.84           O  
ATOM    254  NE2 GLN A  35      12.380  40.531   5.108  1.00 34.03           N  
ATOM    255  N   PHE A  36      17.363  36.793   5.893  1.00 26.69           N  
ATOM    256  CA  PHE A  36      18.467  35.851   5.813  1.00 28.28           C  
ATOM    257  C   PHE A  36      18.395  34.773   6.878  1.00 24.92           C  
ATOM    258  O   PHE A  36      19.272  33.904   6.929  1.00 30.83           O  
ATOM    259  CB  PHE A  36      19.792  36.605   5.936  1.00 29.49           C  
ATOM    260  CG  PHE A  36      20.082  37.486   4.768  1.00 31.93           C  
ATOM    261  CD1 PHE A  36      20.811  37.000   3.698  1.00 34.71           C  
ATOM    262  CD2 PHE A  36      19.611  38.788   4.723  1.00 31.96           C  
ATOM    263  CE1 PHE A  36      21.084  37.803   2.600  1.00 34.62           C  
ATOM    264  CE2 PHE A  36      19.876  39.592   3.624  1.00 33.88           C  
ATOM    265  CZ  PHE A  36      20.617  39.095   2.567  1.00 35.31           C  
ATOM    266  N   ARG A  37      17.377  34.808   7.728  1.00 23.57           N  
ATOM    267  CA  ARG A  37      17.366  33.948   8.895  1.00 24.01           C  
ATOM    268  C   ARG A  37      16.340  32.834   8.745  1.00 25.22           C  
ATOM    269  O   ARG A  37      15.334  33.002   8.050  1.00 25.23           O  
ATOM    270  CB  ARG A  37      17.058  34.771  10.147  1.00 25.47           C  
ATOM    271  CG  ARG A  37      18.023  35.925  10.361  1.00 28.35           C  
ATOM    272  CD  ARG A  37      19.479  35.454  10.296  1.00 31.90           C  
ATOM    273  NE  ARG A  37      19.748  34.340  11.203  1.00 34.31           N  
ATOM    274  CZ  ARG A  37      20.496  33.284  10.888  1.00 39.43           C  
ATOM    275  NH1 ARG A  37      21.032  33.185   9.681  1.00 43.98           N  
ATOM    276  NH2 ARG A  37      20.691  32.314  11.771  1.00 40.96           N  
ATOM    277  N   PRO A  38      16.571  31.679   9.373  1.00 30.69           N  
ATOM    278  CA  PRO A  38      15.644  30.556   9.202  1.00 32.80           C  
ATOM    279  C   PRO A  38      14.294  30.852   9.827  1.00 23.76           C  
ATOM    280  O   PRO A  38      14.172  31.640  10.770  1.00 25.26           O  
ATOM    281  CB  PRO A  38      16.350  29.393   9.914  1.00 35.36           C  
ATOM    282  CG  PRO A  38      17.261  30.049  10.890  1.00 36.48           C  
ATOM    283  CD  PRO A  38      17.718  31.323  10.224  1.00 36.47           C  
ATOM    284  N   LEU A  39      13.271  30.208   9.266  1.00 26.04           N  
ATOM    285  CA  LEU A  39      11.892  30.505   9.644  1.00 24.88           C  
ATOM    286  C   LEU A  39      11.624  30.494  11.144  1.00 25.87           C  
ATOM    287  O   LEU A  39      10.882  31.374  11.605  1.00 26.72           O  
ATOM    288  CB  LEU A  39      10.944  29.528   8.932  1.00 25.18           C  
ATOM    289  CG  LEU A  39      10.748  29.732   7.431  1.00 34.72           C  
ATOM    290  CD1 LEU A  39       9.760  28.717   6.883  1.00 34.79           C  
ATOM    291  CD2 LEU A  39      10.279  31.150   7.134  1.00 38.04           C  
ATOM    292  N   PRO A  40      12.158  29.566  11.949  1.00 23.65           N  
ATOM    293  CA  PRO A  40      11.818  29.563  13.385  1.00 25.54           C  
ATOM    294  C   PRO A  40      12.223  30.820  14.138  1.00 24.56           C  
ATOM    295  O   PRO A  40      11.682  31.071  15.223  1.00 26.18           O  
ATOM    296  CB  PRO A  40      12.572  28.336  13.915  1.00 25.32           C  
ATOM    297  CG  PRO A  40      12.640  27.415  12.762  1.00 26.27           C  
ATOM    298  CD  PRO A  40      12.890  28.341  11.573  1.00 24.23           C  
ATOM    299  N   LEU A  41      13.144  31.622  13.601  1.00 22.84           N  
ATOM    300  CA  LEU A  41      13.614  32.830  14.266  1.00 22.65           C  
ATOM    301  C   LEU A  41      12.848  34.077  13.848  1.00 21.65           C  
ATOM    302  O   LEU A  41      12.987  35.128  14.490  1.00 21.53           O  
ATOM    303  CB  LEU A  41      15.106  33.024  13.982  1.00 24.84           C  
ATOM    304  CG  LEU A  41      15.991  31.887  14.488  1.00 27.42           C  
ATOM    305  CD1 LEU A  41      17.448  32.100  14.112  1.00 35.02           C  
ATOM    306  CD2 LEU A  41      15.828  31.719  15.997  1.00 35.77           C  
ATOM    307  N   ARG A  42      12.041  33.989  12.791  1.00 22.91           N  
ATOM    308  CA  ARG A  42      11.556  35.217  12.167  1.00 21.41           C  
ATOM    309  C   ARG A  42      10.522  35.938  13.027  1.00 20.90           C  
ATOM    310  O   ARG A  42      10.484  37.176  13.021  1.00 21.30           O  
ATOM    311  CB  ARG A  42      11.020  34.913  10.773  1.00 21.50           C  
ATOM    312  CG  ARG A  42      12.125  34.405   9.832  1.00 21.83           C  
ATOM    313  CD  ARG A  42      11.727  34.378   8.382  1.00 25.09           C  
ATOM    314  NE  ARG A  42      12.866  33.983   7.553  1.00 27.98           N  
ATOM    315  CZ  ARG A  42      12.791  33.749   6.248  1.00 46.03           C  
ATOM    316  NH1 ARG A  42      13.879  33.405   5.573  1.00 47.62           N  
ATOM    317  NH2 ARG A  42      11.627  33.855   5.621  1.00 54.71           N  
ATOM    318  N   LEU A  43       9.696  35.204  13.784  1.00 21.22           N  
ATOM    319  CA  LEU A  43       8.735  35.877  14.659  1.00 22.45           C  
ATOM    320  C   LEU A  43       9.431  36.838  15.616  1.00 20.99           C  
ATOM    321  O   LEU A  43       8.972  37.968  15.814  1.00 20.33           O  
ATOM    322  CB  LEU A  43       7.910  34.855  15.446  1.00 23.62           C  
ATOM    323  CG  LEU A  43       6.959  35.504  16.455  1.00 25.58           C  
ATOM    324  CD1 LEU A  43       5.998  36.433  15.738  1.00 29.00           C  
ATOM    325  CD2 LEU A  43       6.196  34.445  17.241  1.00 28.94           C  
ATOM    326  N   THR A  44      10.551  36.422  16.209  1.00 20.45           N  
ATOM    327  CA  THR A  44      11.248  37.313  17.125  1.00 20.80           C  
ATOM    328  C   THR A  44      11.739  38.570  16.412  1.00 18.28           C  
ATOM    329  O   THR A  44      11.635  39.678  16.949  1.00 18.30           O  
ATOM    330  CB  THR A  44      12.397  36.576  17.805  1.00 23.95           C  
ATOM    331  OG1 THR A  44      11.858  35.465  18.544  1.00 27.92           O  
ATOM    332  CG2 THR A  44      13.089  37.477  18.792  1.00 23.87           C  
ATOM    333  N   TYR A  45      12.246  38.429  15.180  1.00 19.76           N  
ATOM    334  CA  TYR A  45      12.615  39.625  14.426  1.00 17.87           C  
ATOM    335  C   TYR A  45      11.403  40.505  14.164  1.00 19.78           C  
ATOM    336  O   TYR A  45      11.483  41.726  14.323  1.00 19.24           O  
ATOM    337  CB  TYR A  45      13.293  39.257  13.096  1.00 19.10           C  
ATOM    338  CG  TYR A  45      14.743  38.850  13.213  1.00 20.75           C  
ATOM    339  CD1 TYR A  45      15.091  37.544  13.501  1.00 19.75           C  
ATOM    340  CD2 TYR A  45      15.769  39.776  13.003  1.00 21.20           C  
ATOM    341  CE1 TYR A  45      16.417  37.159  13.610  1.00 21.36           C  
ATOM    342  CE2 TYR A  45      17.104  39.392  13.091  1.00 22.82           C  
ATOM    343  CZ  TYR A  45      17.418  38.092  13.400  1.00 23.97           C  
ATOM    344  OH  TYR A  45      18.735  37.691  13.497  1.00 25.72           O  
ATOM    345  N   TYR A  46      10.274  39.907  13.760  1.00 19.67           N  
ATOM    346  CA  TYR A  46       9.091  40.713  13.435  1.00 19.87           C  
ATOM    347  C   TYR A  46       8.580  41.485  14.652  1.00 18.50           C  
ATOM    348  O   TYR A  46       8.162  42.647  14.529  1.00 19.42           O  
ATOM    349  CB  TYR A  46       7.964  39.835  12.891  1.00 20.62           C  
ATOM    350  CG  TYR A  46       8.226  39.074  11.605  1.00 27.44           C  
ATOM    351  CD1 TYR A  46       9.003  39.607  10.594  1.00 28.35           C  
ATOM    352  CD2 TYR A  46       7.654  37.820  11.404  1.00 30.33           C  
ATOM    353  CE1 TYR A  46       9.226  38.894   9.398  1.00 28.03           C  
ATOM    354  CE2 TYR A  46       7.868  37.112  10.236  1.00 30.20           C  
ATOM    355  CZ  TYR A  46       8.648  37.653   9.240  1.00 31.44           C  
ATOM    356  OH  TYR A  46       8.849  36.933   8.080  1.00 36.58           O  
ATOM    357  N   VAL A  47       8.588  40.853  15.829  1.00 18.12           N  
ATOM    358  CA  VAL A  47       8.174  41.550  17.049  1.00 18.11           C  
ATOM    359  C   VAL A  47       9.008  42.813  17.242  1.00 17.80           C  
ATOM    360  O   VAL A  47       8.480  43.897  17.526  1.00 18.40           O  
ATOM    361  CB  VAL A  47       8.283  40.604  18.261  1.00 17.68           C  
ATOM    362  CG1 VAL A  47       8.095  41.378  19.567  1.00 18.80           C  
ATOM    363  CG2 VAL A  47       7.246  39.514  18.155  1.00 20.67           C  
ATOM    364  N   ASN A  48      10.319  42.704  17.035  1.00 16.66           N  
ATOM    365  CA  ASN A  48      11.197  43.842  17.265  1.00 16.84           C  
ATOM    366  C   ASN A  48      11.144  44.866  16.136  1.00 16.95           C  
ATOM    367  O   ASN A  48      11.293  46.068  16.396  1.00 17.49           O  
ATOM    368  CB  ASN A  48      12.607  43.327  17.531  1.00 19.40           C  
ATOM    369  CG  ASN A  48      12.660  42.549  18.843  1.00 18.45           C  
ATOM    370  OD1 ASN A  48      12.815  41.320  18.870  1.00 22.93           O  
ATOM    371  ND2 ASN A  48      12.436  43.252  19.922  1.00 16.62           N  
ATOM    372  N   ILE A  49      10.887  44.429  14.901  1.00 16.41           N  
ATOM    373  CA  ILE A  49      10.592  45.371  13.822  1.00 16.21           C  
ATOM    374  C   ILE A  49       9.357  46.192  14.161  1.00 19.68           C  
ATOM    375  O   ILE A  49       9.348  47.421  14.005  1.00 18.46           O  
ATOM    376  CB  ILE A  49      10.409  44.624  12.490  1.00 17.03           C  
ATOM    377  CG1 ILE A  49      11.732  44.010  12.049  1.00 19.31           C  
ATOM    378  CG2 ILE A  49       9.856  45.581  11.450  1.00 19.15           C  
ATOM    379  CD1 ILE A  49      11.580  42.904  11.003  1.00 20.18           C  
ATOM    380  N   ALA A  50       8.307  45.531  14.664  1.00 18.43           N  
ATOM    381  CA  ALA A  50       7.096  46.253  15.040  1.00 18.81           C  
ATOM    382  C   ALA A  50       7.380  47.268  16.139  1.00 18.57           C  
ATOM    383  O   ALA A  50       6.923  48.414  16.064  1.00 18.24           O  
ATOM    384  CB  ALA A  50       6.007  45.273  15.488  1.00 18.17           C  
ATOM    385  N   ILE A  51       8.133  46.859  17.168  1.00 17.09           N  
ATOM    386  CA  ILE A  51       8.436  47.747  18.294  1.00 16.38           C  
ATOM    387  C   ILE A  51       9.132  49.010  17.805  1.00 14.93           C  
ATOM    388  O   ILE A  51       8.741  50.135  18.141  1.00 17.20           O  
ATOM    389  CB  ILE A  51       9.298  47.016  19.336  1.00 16.70           C  
ATOM    390  CG1 ILE A  51       8.466  45.940  20.045  1.00 16.50           C  
ATOM    391  CG2 ILE A  51       9.910  48.015  20.326  1.00 17.83           C  
ATOM    392  CD1 ILE A  51       9.317  44.929  20.800  1.00 18.02           C  
ATOM    393  N   CYS A  52      10.179  48.840  16.995  1.00 17.07           N  
ATOM    394  CA  CYS A  52      10.949  49.995  16.564  1.00 18.28           C  
ATOM    395  C   CYS A  52      10.172  50.844  15.574  1.00 17.25           C  
ATOM    396  O   CYS A  52      10.369  52.063  15.530  1.00 17.20           O  
ATOM    397  CB  CYS A  52      12.277  49.536  15.964  1.00 18.06           C  
ATOM    398  SG  CYS A  52      13.375  48.877  17.272  1.00 22.95           S  
ATOM    399  N   THR A  53       9.300  50.221  14.770  1.00 16.67           N  
ATOM    400  CA  THR A  53       8.485  50.979  13.825  1.00 17.76           C  
ATOM    401  C   THR A  53       7.449  51.822  14.559  1.00 18.18           C  
ATOM    402  O   THR A  53       7.263  53.003  14.243  1.00 19.38           O  
ATOM    403  CB  THR A  53       7.804  50.038  12.828  1.00 20.64           C  
ATOM    404  OG1 THR A  53       8.801  49.314  12.083  1.00 19.91           O  
ATOM    405  CG2 THR A  53       6.957  50.825  11.838  1.00 23.78           C  
ATOM    406  N   ILE A  54       6.790  51.239  15.560  1.00 17.42           N  
ATOM    407  CA  ILE A  54       5.833  52.003  16.355  1.00 18.95           C  
ATOM    408  C   ILE A  54       6.535  53.146  17.070  1.00 17.42           C  
ATOM    409  O   ILE A  54       6.041  54.286  17.089  1.00 19.19           O  
ATOM    410  CB  ILE A  54       5.108  51.071  17.341  1.00 17.20           C  
ATOM    411  CG1 ILE A  54       4.190  50.125  16.562  1.00 18.75           C  
ATOM    412  CG2 ILE A  54       4.325  51.890  18.378  1.00 18.39           C  
ATOM    413  CD1 ILE A  54       3.694  48.956  17.404  1.00 22.39           C  
ATOM    414  N   ALA A  55       7.701  52.872  17.665  1.00 17.34           N  
ATOM    415  CA  ALA A  55       8.429  53.932  18.361  1.00 18.86           C  
ATOM    416  C   ALA A  55       8.868  55.033  17.406  1.00 17.77           C  
ATOM    417  O   ALA A  55       8.804  56.219  17.754  1.00 18.84           O  
ATOM    418  CB  ALA A  55       9.635  53.357  19.106  1.00 20.42           C  
ATOM    419  N   ALA A  56       9.340  54.665  16.208  1.00 17.28           N  
ATOM    420  CA  ALA A  56       9.712  55.673  15.221  1.00 17.39           C  
ATOM    421  C   ALA A  56       8.522  56.556  14.862  1.00 18.91           C  
ATOM    422  O   ALA A  56       8.658  57.783  14.753  1.00 19.74           O  
ATOM    423  CB  ALA A  56      10.287  55.003  13.968  1.00 19.00           C  
ATOM    424  N   THR A  57       7.347  55.948  14.677  1.00 18.25           N  
ATOM    425  CA  THR A  57       6.152  56.714  14.334  1.00 18.82           C  
ATOM    426  C   THR A  57       5.787  57.687  15.454  1.00 18.78           C  
ATOM    427  O   THR A  57       5.455  58.854  15.198  1.00 18.51           O  
ATOM    428  CB  THR A  57       4.994  55.752  14.046  1.00 23.67           C  
ATOM    429  OG1 THR A  57       5.382  54.826  13.018  1.00 22.80           O  
ATOM    430  CG2 THR A  57       3.760  56.501  13.581  1.00 24.11           C  
ATOM    431  N   ALA A  58       5.859  57.226  16.704  1.00 18.27           N  
ATOM    432  CA  ALA A  58       5.550  58.090  17.839  1.00 16.89           C  
ATOM    433  C   ALA A  58       6.538  59.245  17.944  1.00 19.17           C  
ATOM    434  O   ALA A  58       6.137  60.393  18.188  1.00 18.87           O  
ATOM    435  CB  ALA A  58       5.534  57.269  19.128  1.00 18.61           C  
ATOM    436  N   TYR A  59       7.832  58.975  17.739  1.00 18.54           N  
ATOM    437  CA  TYR A  59       8.814  60.053  17.826  1.00 17.54           C  
ATOM    438  C   TYR A  59       8.701  61.022  16.654  1.00 20.41           C  
ATOM    439  O   TYR A  59       8.947  62.220  16.828  1.00 19.61           O  
ATOM    440  CB  TYR A  59      10.232  59.486  17.929  1.00 19.14           C  
ATOM    441  CG  TYR A  59      10.650  59.292  19.367  1.00 18.31           C  
ATOM    442  CD1 TYR A  59      10.435  58.079  20.024  1.00 17.98           C  
ATOM    443  CD2 TYR A  59      11.232  60.326  20.081  1.00 19.37           C  
ATOM    444  CE1 TYR A  59      10.796  57.916  21.352  1.00 18.35           C  
ATOM    445  CE2 TYR A  59      11.589  60.179  21.400  1.00 17.73           C  
ATOM    446  CZ  TYR A  59      11.377  58.966  22.037  1.00 17.46           C  
ATOM    447  OH  TYR A  59      11.742  58.822  23.360  1.00 21.31           O  
ATOM    448  N   TYR A  60       8.340  60.531  15.465  1.00 17.73           N  
ATOM    449  CA  TYR A  60       8.010  61.426  14.360  1.00 18.84           C  
ATOM    450  C   TYR A  60       6.892  62.381  14.766  1.00 20.70           C  
ATOM    451  O   TYR A  60       7.006  63.603  14.598  1.00 20.97           O  
ATOM    452  CB  TYR A  60       7.615  60.614  13.123  1.00 20.15           C  
ATOM    453  CG  TYR A  60       7.271  61.499  11.958  1.00 20.39           C  
ATOM    454  CD1 TYR A  60       8.259  61.961  11.096  1.00 24.27           C  
ATOM    455  CD2 TYR A  60       5.966  61.925  11.749  1.00 26.45           C  
ATOM    456  CE1 TYR A  60       7.950  62.797  10.050  1.00 26.57           C  
ATOM    457  CE2 TYR A  60       5.648  62.763  10.702  1.00 27.39           C  
ATOM    458  CZ  TYR A  60       6.644  63.189   9.848  1.00 25.65           C  
ATOM    459  OH  TYR A  60       6.331  64.025   8.796  1.00 32.12           O  
ATOM    460  N   ALA A  61       5.813  61.835  15.339  1.00 21.93           N  
ATOM    461  CA  ALA A  61       4.684  62.670  15.746  1.00 22.05           C  
ATOM    462  C   ALA A  61       5.097  63.688  16.798  1.00 21.19           C  
ATOM    463  O   ALA A  61       4.704  64.861  16.726  1.00 23.59           O  
ATOM    464  CB  ALA A  61       3.550  61.795  16.276  1.00 22.49           C  
ATOM    465  N   MET A  62       5.885  63.262  17.784  1.00 19.38           N  
ATOM    466  CA  MET A  62       6.324  64.176  18.830  1.00 18.29           C  
ATOM    467  C   MET A  62       7.227  65.267  18.274  1.00 21.08           C  
ATOM    468  O   MET A  62       7.113  66.431  18.671  1.00 22.33           O  
ATOM    469  CB  MET A  62       7.025  63.397  19.941  1.00 19.50           C  
ATOM    470  CG  MET A  62       6.046  62.520  20.733  1.00 19.03           C  
ATOM    471  SD  MET A  62       6.719  61.722  22.213  1.00 19.76           S  
ATOM    472  CE  MET A  62       7.762  60.489  21.432  1.00 23.20           C  
ATOM    473  N   ALA A  63       8.119  64.921  17.346  1.00 18.69           N  
ATOM    474  CA  ALA A  63       9.052  65.923  16.845  1.00 20.53           C  
ATOM    475  C   ALA A  63       8.351  66.928  15.943  1.00 23.02           C  
ATOM    476  O   ALA A  63       8.692  68.119  15.949  1.00 25.22           O  
ATOM    477  CB  ALA A  63      10.198  65.236  16.103  1.00 20.86           C  
ATOM    478  N   VAL A  64       7.367  66.472  15.167  1.00 22.95           N  
ATOM    479  CA  VAL A  64       6.650  67.379  14.269  1.00 24.35           C  
ATOM    480  C   VAL A  64       5.736  68.320  15.051  1.00 28.19           C  
ATOM    481  O   VAL A  64       5.589  69.500  14.695  1.00 31.04           O  
ATOM    482  CB  VAL A  64       5.866  66.565  13.222  1.00 27.70           C  
ATOM    483  CG1 VAL A  64       4.900  67.459  12.445  1.00 34.24           C  
ATOM    484  CG2 VAL A  64       6.834  65.884  12.281  1.00 27.05           C  
ATOM    485  N   ASN A  65       5.120  67.830  16.129  1.00 28.85           N  
ATOM    486  CA  ASN A  65       4.050  68.567  16.799  1.00 29.87           C  
ATOM    487  C   ASN A  65       4.422  69.186  18.140  1.00 30.02           C  
ATOM    488  O   ASN A  65       3.666  70.033  18.630  1.00 27.15           O  
ATOM    489  CB  ASN A  65       2.839  67.649  17.021  1.00 31.74           C  
ATOM    490  CG  ASN A  65       2.209  67.200  15.718  1.00 38.16           C  
ATOM    491  OD1 ASN A  65       1.903  68.018  14.852  1.00 41.54           O  
ATOM    492  ND2 ASN A  65       2.039  65.891  15.560  1.00 42.30           N  
ATOM    493  N   GLY A  66       5.540  68.788  18.753  1.00 26.11           N  
ATOM    494  CA  GLY A  66       5.810  69.204  20.125  1.00 25.53           C  
ATOM    495  C   GLY A  66       6.001  70.698  20.300  1.00 25.02           C  
ATOM    496  O   GLY A  66       5.654  71.252  21.353  1.00 23.69           O  
ATOM    497  N   GLY A  67       6.557  71.369  19.289  1.00 28.29           N  
ATOM    498  CA  GLY A  67       6.719  72.816  19.308  1.00 29.91           C  
ATOM    499  C   GLY A  67       5.419  73.591  19.326  1.00 29.98           C  
ATOM    500  O   GLY A  67       5.444  74.798  19.594  1.00 31.58           O  
ATOM    501  N   ASP A  68       4.289  72.933  19.049  1.00 26.01           N  
ATOM    502  CA  ASP A  68       2.999  73.594  19.194  1.00 27.17           C  
ATOM    503  C   ASP A  68       2.685  73.914  20.650  1.00 22.94           C  
ATOM    504  O   ASP A  68       1.797  74.732  20.903  1.00 27.12           O  
ATOM    505  CB  ASP A  68       1.872  72.733  18.614  1.00 35.63           C  
ATOM    506  CG  ASP A  68       2.014  72.493  17.122  1.00 42.63           C  
ATOM    507  OD1 ASP A  68       2.846  73.165  16.479  1.00 42.03           O  
ATOM    508  OD2 ASP A  68       1.279  71.634  16.591  1.00 47.56           O  
ATOM    509  N   ASN A  69       3.370  73.263  21.604  1.00 24.20           N  
ATOM    510  CA  ASN A  69       3.267  73.586  23.032  1.00 23.54           C  
ATOM    511  C   ASN A  69       1.847  73.389  23.552  1.00 26.93           C  
ATOM    512  O   ASN A  69       1.360  74.148  24.391  1.00 28.44           O  
ATOM    513  CB  ASN A  69       3.780  75.000  23.318  1.00 24.22           C  
ATOM    514  CG  ASN A  69       5.290  75.105  23.194  1.00 23.95           C  
ATOM    515  OD1 ASN A  69       6.020  74.104  23.367  1.00 25.46           O  
ATOM    516  ND2 ASN A  69       5.775  76.301  22.895  1.00 26.93           N  
ATOM    517  N   LYS A  70       1.196  72.339  23.056  1.00 25.24           N  
ATOM    518  CA  LYS A  70      -0.150  71.943  23.439  1.00 26.73           C  
ATOM    519  C   LYS A  70      -0.216  70.425  23.324  1.00 23.53           C  
ATOM    520  O   LYS A  70       0.538  69.839  22.559  1.00 25.14           O  
ATOM    521  CB  LYS A  70      -1.198  72.595  22.527  1.00 32.59           C  
ATOM    522  CG  LYS A  70      -1.390  74.090  22.714  1.00 38.27           C  
ATOM    523  CD  LYS A  70      -2.026  74.408  24.062  1.00 43.22           C  
ATOM    524  CE  LYS A  70      -2.921  75.642  23.977  1.00 47.60           C  
ATOM    525  NZ  LYS A  70      -4.169  75.377  23.212  1.00 50.12           N  
ATOM    526  N   PRO A  71      -1.098  69.768  24.089  1.00 23.58           N  
ATOM    527  CA  PRO A  71      -1.983  70.309  25.120  1.00 26.81           C  
ATOM    528  C   PRO A  71      -1.217  70.590  26.395  1.00 24.51           C  
ATOM    529  O   PRO A  71      -0.049  70.242  26.493  1.00 23.45           O  
ATOM    530  CB  PRO A  71      -2.998  69.183  25.330  1.00 29.08           C  
ATOM    531  CG  PRO A  71      -2.218  67.943  25.058  1.00 27.92           C  
ATOM    532  CD  PRO A  71      -1.267  68.311  23.932  1.00 23.88           C  
ATOM    533  N   THR A  72      -1.879  71.206  27.370  1.00 26.49           N  
ATOM    534  CA  THR A  72      -1.276  71.455  28.667  1.00 25.86           C  
ATOM    535  C   THR A  72      -2.216  70.982  29.764  1.00 30.12           C  
ATOM    536  O   THR A  72      -3.416  70.795  29.547  1.00 32.21           O  
ATOM    537  CB  THR A  72      -0.964  72.938  28.894  1.00 25.69           C  
ATOM    538  OG1 THR A  72      -2.188  73.680  28.936  1.00 29.84           O  
ATOM    539  CG2 THR A  72      -0.107  73.489  27.776  1.00 27.88           C  
ATOM    540  N   ALA A  73      -1.650  70.808  30.950  1.00 25.32           N  
ATOM    541  CA  ALA A  73      -2.418  70.531  32.154  1.00 26.35           C  
ATOM    542  C   ALA A  73      -2.020  71.549  33.212  1.00 30.41           C  
ATOM    543  O   ALA A  73      -0.841  71.889  33.340  1.00 29.50           O  
ATOM    544  CB  ALA A  73      -2.170  69.092  32.649  1.00 25.69           C  
ATOM    545  N   GLY A  74      -3.000  72.039  33.965  1.00 29.84           N  
ATOM    546  CA  GLY A  74      -2.754  73.044  34.977  1.00 31.24           C  
ATOM    547  C   GLY A  74      -2.973  74.453  34.453  1.00 33.77           C  
ATOM    548  O   GLY A  74      -3.129  74.695  33.254  1.00 35.16           O  
ATOM    549  N   THR A  75      -2.991  75.408  35.379  1.00 34.41           N  
ATOM    550  CA  THR A  75      -3.220  76.801  35.024  1.00 37.90           C  
ATOM    551  C   THR A  75      -2.185  77.690  35.697  1.00 32.80           C  
ATOM    552  O   THR A  75      -1.497  77.284  36.638  1.00 31.94           O  
ATOM    553  CB  THR A  75      -4.633  77.272  35.414  1.00 47.81           C  
ATOM    554  OG1 THR A  75      -4.899  76.915  36.774  1.00 52.38           O  
ATOM    555  CG2 THR A  75      -5.684  76.635  34.510  1.00 49.77           C  
ATOM    556  N   GLY A  76      -2.083  78.917  35.187  1.00 32.93           N  
ATOM    557  CA  GLY A  76      -1.178  79.887  35.775  1.00 36.58           C  
ATOM    558  C   GLY A  76       0.245  79.371  35.792  1.00 31.13           C  
ATOM    559  O   GLY A  76       0.711  78.726  34.847  1.00 31.51           O  
ATOM    560  N   ALA A  77       0.937  79.628  36.902  1.00 32.35           N  
ATOM    561  CA  ALA A  77       2.349  79.286  37.002  1.00 35.37           C  
ATOM    562  C   ALA A  77       2.590  77.785  37.003  1.00 32.14           C  
ATOM    563  O   ALA A  77       3.731  77.363  36.800  1.00 33.37           O  
ATOM    564  CB  ALA A  77       2.952  79.907  38.264  1.00 41.04           C  
ATOM    565  N   ASP A  78       1.552  76.976  37.229  1.00 28.37           N  
ATOM    566  CA  ASP A  78       1.668  75.525  37.270  1.00 29.30           C  
ATOM    567  C   ASP A  78       1.362  74.850  35.937  1.00 27.78           C  
ATOM    568  O   ASP A  78       1.443  73.622  35.859  1.00 30.13           O  
ATOM    569  CB  ASP A  78       0.739  74.956  38.345  1.00 34.85           C  
ATOM    570  CG  ASP A  78       1.214  75.268  39.752  1.00 48.32           C  
ATOM    571  OD1 ASP A  78       2.399  75.636  39.917  1.00 47.22           O  
ATOM    572  OD2 ASP A  78       0.402  75.148  40.694  1.00 58.18           O  
ATOM    573  N   GLU A  79       1.020  75.610  34.898  1.00 25.86           N  
ATOM    574  CA  GLU A  79       0.681  75.020  33.607  1.00 25.58           C  
ATOM    575  C   GLU A  79       1.901  74.345  32.988  1.00 24.14           C  
ATOM    576  O   GLU A  79       2.996  74.913  32.978  1.00 25.39           O  
ATOM    577  CB  GLU A  79       0.132  76.089  32.662  1.00 27.14           C  
ATOM    578  CG  GLU A  79      -0.415  75.516  31.371  1.00 29.98           C  
ATOM    579  CD  GLU A  79      -1.218  76.515  30.561  1.00 37.44           C  
ATOM    580  OE1 GLU A  79      -1.292  77.694  30.962  1.00 39.36           O  
ATOM    581  OE2 GLU A  79      -1.783  76.113  29.521  1.00 38.72           O  
ATOM    582  N   ARG A  80       1.717  73.128  32.474  1.00 21.84           N  
ATOM    583  CA  ARG A  80       2.826  72.366  31.911  1.00 20.19           C  
ATOM    584  C   ARG A  80       2.357  71.584  30.695  1.00 20.36           C  
ATOM    585  O   ARG A  80       1.282  70.978  30.710  1.00 24.57           O  
ATOM    586  CB  ARG A  80       3.423  71.415  32.964  1.00 22.07           C  
ATOM    587  CG  ARG A  80       4.762  70.780  32.559  1.00 21.01           C  
ATOM    588  CD  ARG A  80       5.286  69.954  33.734  1.00 22.27           C  
ATOM    589  NE  ARG A  80       6.651  69.466  33.555  1.00 21.13           N  
ATOM    590  CZ  ARG A  80       6.972  68.341  32.925  1.00 20.44           C  
ATOM    591  NH1 ARG A  80       6.030  67.585  32.368  1.00 19.69           N  
ATOM    592  NH2 ARG A  80       8.246  67.983  32.837  1.00 21.07           N  
ATOM    593  N   GLN A  81       3.194  71.552  29.655  1.00 19.38           N  
ATOM    594  CA  GLN A  81       2.846  70.809  28.451  1.00 22.48           C  
ATOM    595  C   GLN A  81       2.715  69.322  28.754  1.00 20.73           C  
ATOM    596  O   GLN A  81       3.504  68.757  29.515  1.00 20.55           O  
ATOM    597  CB  GLN A  81       3.912  71.022  27.380  1.00 22.21           C  
ATOM    598  CG  GLN A  81       3.565  70.393  26.036  1.00 21.31           C  
ATOM    599  CD  GLN A  81       4.518  70.826  24.936  1.00 21.44           C  
ATOM    600  OE1 GLN A  81       5.262  71.798  25.092  1.00 22.58           O  
ATOM    601  NE2 GLN A  81       4.493  70.116  23.815  1.00 24.04           N  
ATOM    602  N   VAL A  82       1.726  68.677  28.137  1.00 19.54           N  
ATOM    603  CA  VAL A  82       1.537  67.231  28.257  1.00 21.23           C  
ATOM    604  C   VAL A  82       1.868  66.594  26.914  1.00 21.21           C  
ATOM    605  O   VAL A  82       1.155  66.799  25.925  1.00 22.11           O  
ATOM    606  CB  VAL A  82       0.110  66.867  28.686  1.00 22.77           C  
ATOM    607  CG1 VAL A  82      -0.027  65.344  28.789  1.00 23.01           C  
ATOM    608  CG2 VAL A  82      -0.229  67.528  29.997  1.00 25.23           C  
ATOM    609  N   ILE A  83       2.939  65.810  26.880  1.00 20.17           N  
ATOM    610  CA  ILE A  83       3.298  65.031  25.699  1.00 21.34           C  
ATOM    611  C   ILE A  83       2.663  63.657  25.879  1.00 24.12           C  
ATOM    612  O   ILE A  83       3.089  62.879  26.735  1.00 29.83           O  
ATOM    613  CB  ILE A  83       4.820  64.941  25.539  1.00 22.52           C  
ATOM    614  CG1 ILE A  83       5.392  66.340  25.279  1.00 24.37           C  
ATOM    615  CG2 ILE A  83       5.192  63.989  24.392  1.00 20.63           C  
ATOM    616  CD1 ILE A  83       6.897  66.401  25.319  1.00 27.45           C  
ATOM    617  N   TYR A  84       1.612  63.368  25.107  1.00 21.01           N  
ATOM    618  CA  TYR A  84       0.860  62.136  25.327  1.00 23.02           C  
ATOM    619  C   TYR A  84       1.097  61.079  24.262  1.00 21.18           C  
ATOM    620  O   TYR A  84       0.717  59.920  24.471  1.00 20.66           O  
ATOM    621  CB  TYR A  84      -0.646  62.426  25.431  1.00 24.47           C  
ATOM    622  CG  TYR A  84      -1.261  62.951  24.164  1.00 25.77           C  
ATOM    623  CD1 TYR A  84      -1.368  64.316  23.938  1.00 26.80           C  
ATOM    624  CD2 TYR A  84      -1.739  62.084  23.186  1.00 27.65           C  
ATOM    625  CE1 TYR A  84      -1.922  64.805  22.770  1.00 27.89           C  
ATOM    626  CE2 TYR A  84      -2.295  62.562  22.016  1.00 31.71           C  
ATOM    627  CZ  TYR A  84      -2.388  63.926  21.814  1.00 33.56           C  
ATOM    628  OH  TYR A  84      -2.944  64.408  20.651  1.00 36.68           O  
ATOM    629  N   ALA A  85       1.716  61.436  23.134  1.00 21.19           N  
ATOM    630  CA  ALA A  85       1.990  60.437  22.107  1.00 21.78           C  
ATOM    631  C   ALA A  85       2.807  59.281  22.660  1.00 20.94           C  
ATOM    632  O   ALA A  85       2.640  58.136  22.220  1.00 20.30           O  
ATOM    633  CB  ALA A  85       2.709  61.084  20.925  1.00 22.82           C  
ATOM    634  N   ARG A  86       3.690  59.557  23.620  1.00 19.92           N  
ATOM    635  CA  ARG A  86       4.518  58.500  24.182  1.00 18.81           C  
ATOM    636  C   ARG A  86       3.665  57.381  24.770  1.00 19.70           C  
ATOM    637  O   ARG A  86       4.035  56.213  24.666  1.00 18.60           O  
ATOM    638  CB  ARG A  86       5.482  59.065  25.229  1.00 21.29           C  
ATOM    639  CG  ARG A  86       4.805  59.746  26.413  1.00 22.67           C  
ATOM    640  CD  ARG A  86       5.823  60.263  27.428  1.00 22.89           C  
ATOM    641  NE  ARG A  86       6.760  61.227  26.850  1.00 22.50           N  
ATOM    642  CZ  ARG A  86       6.989  62.435  27.355  1.00 21.55           C  
ATOM    643  NH1 ARG A  86       6.337  62.853  28.438  1.00 23.68           N  
ATOM    644  NH2 ARG A  86       7.878  63.227  26.765  1.00 22.94           N  
ATOM    645  N   TYR A  87       2.509  57.710  25.372  1.00 19.90           N  
ATOM    646  CA  TYR A  87       1.672  56.665  25.972  1.00 20.16           C  
ATOM    647  C   TYR A  87       1.007  55.796  24.913  1.00 19.96           C  
ATOM    648  O   TYR A  87       0.778  54.597  25.144  1.00 18.41           O  
ATOM    649  CB  TYR A  87       0.597  57.280  26.882  1.00 18.51           C  
ATOM    650  CG  TYR A  87       1.155  58.101  28.001  1.00 20.89           C  
ATOM    651  CD1 TYR A  87       1.281  59.478  27.878  1.00 21.66           C  
ATOM    652  CD2 TYR A  87       1.527  57.511  29.203  1.00 24.34           C  
ATOM    653  CE1 TYR A  87       1.796  60.246  28.899  1.00 22.81           C  
ATOM    654  CE2 TYR A  87       2.047  58.273  30.236  1.00 26.01           C  
ATOM    655  CZ  TYR A  87       2.180  59.638  30.076  1.00 28.22           C  
ATOM    656  OH  TYR A  87       2.699  60.406  31.087  1.00 27.76           O  
ATOM    657  N   ILE A  88       0.672  56.373  23.757  1.00 20.73           N  
ATOM    658  CA  ILE A  88       0.124  55.564  22.674  1.00 22.21           C  
ATOM    659  C   ILE A  88       1.176  54.582  22.168  1.00 23.74           C  
ATOM    660  O   ILE A  88       0.870  53.414  21.891  1.00 24.94           O  
ATOM    661  CB  ILE A  88      -0.405  56.465  21.545  1.00 23.24           C  
ATOM    662  CG1 ILE A  88      -1.438  57.450  22.102  1.00 27.19           C  
ATOM    663  CG2 ILE A  88      -1.007  55.609  20.445  1.00 26.19           C  
ATOM    664  CD1 ILE A  88      -1.831  58.544  21.116  1.00 28.55           C  
ATOM    665  N   ASP A  89       2.423  55.045  22.019  1.00 19.91           N  
ATOM    666  CA  ASP A  89       3.555  54.155  21.762  1.00 19.58           C  
ATOM    667  C   ASP A  89       3.579  53.027  22.785  1.00 18.62           C  
ATOM    668  O   ASP A  89       3.498  51.843  22.438  1.00 18.25           O  
ATOM    669  CB  ASP A  89       4.843  55.003  21.799  1.00 20.24           C  
ATOM    670  CG  ASP A  89       6.158  54.201  21.794  1.00 27.20           C  
ATOM    671  OD1 ASP A  89       6.234  53.017  22.188  1.00 26.20           O  
ATOM    672  OD2 ASP A  89       7.181  54.826  21.422  1.00 27.85           O  
ATOM    673  N   TRP A  90       3.593  53.395  24.068  1.00 16.78           N  
ATOM    674  CA  TRP A  90       3.855  52.418  25.121  1.00 17.20           C  
ATOM    675  C   TRP A  90       2.766  51.360  25.231  1.00 18.92           C  
ATOM    676  O   TRP A  90       3.071  50.211  25.578  1.00 18.47           O  
ATOM    677  CB  TRP A  90       3.997  53.123  26.475  1.00 17.09           C  
ATOM    678  CG  TRP A  90       5.154  54.057  26.579  1.00 17.23           C  
ATOM    679  CD1 TRP A  90       6.196  54.205  25.694  1.00 15.78           C  
ATOM    680  CD2 TRP A  90       5.371  54.996  27.621  1.00 18.43           C  
ATOM    681  NE1 TRP A  90       7.057  55.169  26.150  1.00 17.82           N  
ATOM    682  CE2 TRP A  90       6.572  55.674  27.331  1.00 18.49           C  
ATOM    683  CE3 TRP A  90       4.669  55.324  28.790  1.00 18.64           C  
ATOM    684  CZ2 TRP A  90       7.084  56.673  28.160  1.00 18.42           C  
ATOM    685  CZ3 TRP A  90       5.177  56.309  29.615  1.00 20.79           C  
ATOM    686  CH2 TRP A  90       6.373  56.976  29.294  1.00 20.76           C  
ATOM    687  N   VAL A  91       1.497  51.714  24.986  1.00 18.25           N  
ATOM    688  CA  VAL A  91       0.439  50.714  25.149  1.00 19.96           C  
ATOM    689  C   VAL A  91       0.585  49.594  24.121  1.00 20.68           C  
ATOM    690  O   VAL A  91       0.156  48.466  24.380  1.00 20.40           O  
ATOM    691  CB  VAL A  91      -0.960  51.373  25.103  1.00 22.03           C  
ATOM    692  CG1 VAL A  91      -1.390  51.699  23.680  1.00 24.25           C  
ATOM    693  CG2 VAL A  91      -2.000  50.482  25.808  1.00 24.57           C  
ATOM    694  N   PHE A  92       1.230  49.862  22.979  1.00 18.68           N  
ATOM    695  CA  PHE A  92       1.509  48.797  22.020  1.00 23.24           C  
ATOM    696  C   PHE A  92       2.898  48.188  22.192  1.00 20.99           C  
ATOM    697  O   PHE A  92       3.054  46.970  22.042  1.00 22.44           O  
ATOM    698  CB  PHE A  92       1.352  49.324  20.590  1.00 23.57           C  
ATOM    699  CG  PHE A  92      -0.050  49.733  20.262  1.00 25.95           C  
ATOM    700  CD1 PHE A  92      -1.016  48.782  19.989  1.00 33.05           C  
ATOM    701  CD2 PHE A  92      -0.410  51.066  20.255  1.00 27.82           C  
ATOM    702  CE1 PHE A  92      -2.313  49.156  19.695  1.00 36.14           C  
ATOM    703  CE2 PHE A  92      -1.705  51.447  19.956  1.00 32.08           C  
ATOM    704  CZ  PHE A  92      -2.656  50.494  19.681  1.00 35.02           C  
ATOM    705  N   THR A  93       3.916  48.993  22.511  1.00 18.50           N  
ATOM    706  CA  THR A  93       5.266  48.445  22.524  1.00 19.78           C  
ATOM    707  C   THR A  93       5.607  47.726  23.819  1.00 19.59           C  
ATOM    708  O   THR A  93       6.374  46.759  23.779  1.00 19.36           O  
ATOM    709  CB  THR A  93       6.323  49.525  22.262  1.00 17.68           C  
ATOM    710  OG1 THR A  93       6.233  50.549  23.265  1.00 18.91           O  
ATOM    711  CG2 THR A  93       6.160  50.118  20.863  1.00 20.53           C  
ATOM    712  N   THR A  94       5.053  48.150  24.968  1.00 17.99           N  
ATOM    713  CA  THR A  94       5.465  47.457  26.188  1.00 18.85           C  
ATOM    714  C   THR A  94       4.929  46.021  26.217  1.00 18.52           C  
ATOM    715  O   THR A  94       5.671  45.124  26.634  1.00 17.78           O  
ATOM    716  CB  THR A  94       5.108  48.241  27.473  1.00 19.07           C  
ATOM    717  OG1 THR A  94       3.722  48.624  27.518  1.00 18.93           O  
ATOM    718  CG2 THR A  94       5.970  49.499  27.570  1.00 20.11           C  
ATOM    719  N   PRO A  95       3.721  45.726  25.714  1.00 16.10           N  
ATOM    720  CA  PRO A  95       3.340  44.303  25.610  1.00 18.20           C  
ATOM    721  C   PRO A  95       4.227  43.521  24.658  1.00 18.00           C  
ATOM    722  O   PRO A  95       4.515  42.344  24.906  1.00 18.07           O  
ATOM    723  CB  PRO A  95       1.887  44.358  25.119  1.00 20.34           C  
ATOM    724  CG  PRO A  95       1.379  45.692  25.623  1.00 22.61           C  
ATOM    725  CD  PRO A  95       2.569  46.617  25.454  1.00 17.75           C  
ATOM    726  N   LEU A  96       4.662  44.148  23.563  1.00 17.16           N  
ATOM    727  CA  LEU A  96       5.551  43.456  22.633  1.00 17.11           C  
ATOM    728  C   LEU A  96       6.930  43.223  23.245  1.00 16.67           C  
ATOM    729  O   LEU A  96       7.550  42.187  23.000  1.00 17.30           O  
ATOM    730  CB  LEU A  96       5.686  44.259  21.336  1.00 18.94           C  
ATOM    731  CG  LEU A  96       4.424  44.295  20.487  1.00 18.30           C  
ATOM    732  CD1 LEU A  96       4.603  45.297  19.359  1.00 21.26           C  
ATOM    733  CD2 LEU A  96       4.135  42.916  19.920  1.00 24.18           C  
ATOM    734  N   LEU A  97       7.438  44.183  24.020  1.00 16.83           N  
ATOM    735  CA  LEU A  97       8.715  43.962  24.691  1.00 15.16           C  
ATOM    736  C   LEU A  97       8.635  42.802  25.677  1.00 16.91           C  
ATOM    737  O   LEU A  97       9.573  42.004  25.776  1.00 17.90           O  
ATOM    738  CB  LEU A  97       9.166  45.243  25.400  1.00 16.32           C  
ATOM    739  CG  LEU A  97       9.585  46.363  24.451  1.00 15.15           C  
ATOM    740  CD1 LEU A  97       9.609  47.699  25.187  1.00 17.72           C  
ATOM    741  CD2 LEU A  97      10.971  46.100  23.881  1.00 18.27           C  
ATOM    742  N   LEU A  98       7.529  42.693  26.424  1.00 17.37           N  
ATOM    743  CA  LEU A  98       7.355  41.527  27.284  1.00 15.89           C  
ATOM    744  C   LEU A  98       7.235  40.247  26.465  1.00 16.51           C  
ATOM    745  O   LEU A  98       7.758  39.197  26.862  1.00 18.77           O  
ATOM    746  CB  LEU A  98       6.123  41.701  28.178  1.00 16.83           C  
ATOM    747  CG  LEU A  98       6.207  42.897  29.123  1.00 17.75           C  
ATOM    748  CD1 LEU A  98       4.901  43.039  29.889  1.00 22.07           C  
ATOM    749  CD2 LEU A  98       7.371  42.728  30.090  1.00 19.90           C  
ATOM    750  N   LEU A  99       6.539  40.311  25.327  1.00 16.92           N  
ATOM    751  CA  LEU A  99       6.389  39.135  24.470  1.00 17.98           C  
ATOM    752  C   LEU A  99       7.741  38.586  24.021  1.00 18.77           C  
ATOM    753  O   LEU A  99       7.907  37.367  23.898  1.00 20.50           O  
ATOM    754  CB  LEU A  99       5.510  39.482  23.268  1.00 21.78           C  
ATOM    755  CG  LEU A  99       5.243  38.350  22.273  1.00 21.18           C  
ATOM    756  CD1 LEU A  99       4.508  37.216  22.965  1.00 21.05           C  
ATOM    757  CD2 LEU A  99       4.430  38.868  21.097  1.00 24.88           C  
ATOM    758  N   ASP A 100       8.725  39.469  23.786  1.00 18.02           N  
ATOM    759  CA  ASP A 100      10.081  39.027  23.448  1.00 18.69           C  
ATOM    760  C   ASP A 100      10.580  37.964  24.417  1.00 20.83           C  
ATOM    761  O   ASP A 100      11.205  36.979  24.005  1.00 23.49           O  
ATOM    762  CB  ASP A 100      11.067  40.200  23.481  1.00 18.28           C  
ATOM    763  CG  ASP A 100      11.267  40.888  22.136  1.00 20.34           C  
ATOM    764  OD1 ASP A 100      11.179  40.240  21.074  1.00 23.20           O  
ATOM    765  OD2 ASP A 100      11.568  42.100  22.166  1.00 20.32           O  
ATOM    766  N   LEU A 101      10.344  38.171  25.717  1.00 19.59           N  
ATOM    767  CA  LEU A 101      10.766  37.220  26.736  1.00 20.98           C  
ATOM    768  C   LEU A 101       9.754  36.095  26.933  1.00 18.85           C  
ATOM    769  O   LEU A 101      10.153  34.950  27.175  1.00 19.89           O  
ATOM    770  CB  LEU A 101      11.017  37.941  28.069  1.00 20.20           C  
ATOM    771  CG  LEU A 101      12.208  38.909  28.016  1.00 22.88           C  
ATOM    772  CD1 LEU A 101      12.460  39.591  29.367  1.00 26.12           C  
ATOM    773  CD2 LEU A 101      13.480  38.243  27.499  1.00 31.02           C  
ATOM    774  N   VAL A 102       8.452  36.399  26.836  1.00 17.86           N  
ATOM    775  CA  VAL A 102       7.430  35.361  27.008  1.00 19.00           C  
ATOM    776  C   VAL A 102       7.630  34.235  26.001  1.00 20.64           C  
ATOM    777  O   VAL A 102       7.400  33.055  26.317  1.00 22.82           O  
ATOM    778  CB  VAL A 102       6.021  35.983  26.893  1.00 21.02           C  
ATOM    779  CG1 VAL A 102       4.956  34.885  26.750  1.00 25.50           C  
ATOM    780  CG2 VAL A 102       5.714  36.840  28.121  1.00 23.58           C  
ATOM    781  N   LEU A 103       8.102  34.568  24.791  1.00 21.37           N  
ATOM    782  CA  LEU A 103       8.327  33.569  23.750  1.00 21.56           C  
ATOM    783  C   LEU A 103       9.437  32.592  24.115  1.00 26.08           C  
ATOM    784  O   LEU A 103       9.542  31.532  23.487  1.00 29.64           O  
ATOM    785  CB  LEU A 103       8.650  34.264  22.419  1.00 22.03           C  
ATOM    786  CG  LEU A 103       7.480  34.988  21.745  1.00 25.04           C  
ATOM    787  CD1 LEU A 103       7.949  35.867  20.572  1.00 24.70           C  
ATOM    788  CD2 LEU A 103       6.412  33.995  21.288  1.00 28.84           C  
ATOM    789  N   LEU A 104      10.267  32.927  25.101  1.00 23.65           N  
ATOM    790  CA  LEU A 104      11.307  32.032  25.589  1.00 24.10           C  
ATOM    791  C   LEU A 104      10.813  31.094  26.685  1.00 26.57           C  
ATOM    792  O   LEU A 104      11.609  30.309  27.207  1.00 32.69           O  
ATOM    793  CB  LEU A 104      12.496  32.835  26.124  1.00 25.37           C  
ATOM    794  CG  LEU A 104      13.112  33.899  25.221  1.00 31.36           C  
ATOM    795  CD1 LEU A 104      14.297  34.555  25.920  1.00 31.30           C  
ATOM    796  CD2 LEU A 104      13.531  33.282  23.901  1.00 39.42           C  
ATOM    797  N   THR A 105       9.537  31.162  27.047  1.00 26.81           N  
ATOM    798  CA  THR A 105       8.979  30.424  28.172  1.00 24.43           C  
ATOM    799  C   THR A 105       7.813  29.567  27.717  1.00 26.78           C  
ATOM    800  O   THR A 105       7.379  29.625  26.567  1.00 28.19           O  
ATOM    801  CB  THR A 105       8.466  31.355  29.271  1.00 23.54           C  
ATOM    802  OG1 THR A 105       7.210  31.919  28.855  1.00 25.31           O  
ATOM    803  CG2 THR A 105       9.450  32.465  29.534  1.00 26.29           C  
ATOM    804  N   ASN A 106       7.289  28.796  28.670  1.00 24.71           N  
ATOM    805  CA  ASN A 106       6.047  28.050  28.516  1.00 26.97           C  
ATOM    806  C   ASN A 106       4.962  28.603  29.435  1.00 26.00           C  
ATOM    807  O   ASN A 106       4.209  27.848  30.048  1.00 29.71           O  
ATOM    808  CB  ASN A 106       6.261  26.561  28.784  1.00 34.02           C  
ATOM    809  CG  ASN A 106       6.967  25.853  27.640  1.00 41.60           C  
ATOM    810  OD1 ASN A 106       6.859  26.252  26.476  1.00 43.38           O  
ATOM    811  ND2 ASN A 106       7.686  24.785  27.965  1.00 45.95           N  
ATOM    812  N   MET A 107       4.884  29.931  29.551  1.00 25.96           N  
ATOM    813  CA  MET A 107       3.816  30.549  30.334  1.00 28.68           C  
ATOM    814  C   MET A 107       2.456  30.157  29.775  1.00 29.35           C  
ATOM    815  O   MET A 107       2.234  30.283  28.564  1.00 31.16           O  
ATOM    816  CB  MET A 107       3.900  32.070  30.303  1.00 31.86           C  
ATOM    817  CG  MET A 107       4.872  32.717  31.224  1.00 37.04           C  
ATOM    818  SD  MET A 107       4.506  34.484  31.131  1.00 32.37           S  
ATOM    819  CE  MET A 107       5.976  35.152  31.908  1.00 34.01           C  
ATOM    820  N   PRO A 108       1.505  29.766  30.616  1.00 29.43           N  
ATOM    821  CA  PRO A 108       0.143  29.533  30.129  1.00 31.56           C  
ATOM    822  C   PRO A 108      -0.558  30.839  29.782  1.00 30.09           C  
ATOM    823  O   PRO A 108      -0.194  31.929  30.239  1.00 26.08           O  
ATOM    824  CB  PRO A 108      -0.542  28.821  31.303  1.00 35.35           C  
ATOM    825  CG  PRO A 108       0.218  29.267  32.504  1.00 38.77           C  
ATOM    826  CD  PRO A 108       1.644  29.478  32.053  1.00 34.46           C  
ATOM    827  N   ALA A 109      -1.582  30.706  28.933  1.00 32.96           N  
ATOM    828  CA  ALA A 109      -2.303  31.870  28.426  1.00 31.81           C  
ATOM    829  C   ALA A 109      -2.917  32.695  29.553  1.00 29.01           C  
ATOM    830  O   ALA A 109      -2.949  33.929  29.475  1.00 29.30           O  
ATOM    831  CB  ALA A 109      -3.384  31.424  27.442  1.00 36.19           C  
ATOM    832  N   THR A 110      -3.424  32.033  30.600  1.00 30.41           N  
ATOM    833  CA  THR A 110      -3.988  32.754  31.741  1.00 33.40           C  
ATOM    834  C   THR A 110      -2.965  33.693  32.367  1.00 32.62           C  
ATOM    835  O   THR A 110      -3.282  34.842  32.706  1.00 31.56           O  
ATOM    836  CB  THR A 110      -4.502  31.762  32.786  1.00 41.97           C  
ATOM    837  OG1 THR A 110      -4.749  32.451  34.018  1.00 49.74           O  
ATOM    838  CG2 THR A 110      -3.473  30.670  33.038  1.00 40.75           C  
ATOM    839  N   MET A 111      -1.721  33.232  32.500  1.00 28.56           N  
ATOM    840  CA  MET A 111      -0.695  34.050  33.127  1.00 26.18           C  
ATOM    841  C   MET A 111      -0.265  35.186  32.214  1.00 25.06           C  
ATOM    842  O   MET A 111      -0.103  36.330  32.665  1.00 24.03           O  
ATOM    843  CB  MET A 111       0.491  33.170  33.496  1.00 26.20           C  
ATOM    844  CG  MET A 111       1.635  33.899  34.137  1.00 30.02           C  
ATOM    845  SD  MET A 111       2.850  32.668  34.641  1.00 33.90           S  
ATOM    846  CE  MET A 111       3.903  33.688  35.665  1.00 35.49           C  
ATOM    847  N   ILE A 112      -0.061  34.885  30.925  1.00 23.12           N  
ATOM    848  CA  ILE A 112       0.235  35.943  29.962  1.00 23.48           C  
ATOM    849  C   ILE A 112      -0.851  37.010  30.012  1.00 25.03           C  
ATOM    850  O   ILE A 112      -0.566  38.209  29.942  1.00 23.57           O  
ATOM    851  CB  ILE A 112       0.394  35.352  28.547  1.00 23.03           C  
ATOM    852  CG1 ILE A 112       1.525  34.327  28.541  1.00 24.30           C  
ATOM    853  CG2 ILE A 112       0.678  36.463  27.540  1.00 24.51           C  
ATOM    854  CD1 ILE A 112       1.602  33.484  27.265  1.00 24.58           C  
ATOM    855  N   ALA A 113      -2.105  36.590  30.183  1.00 25.45           N  
ATOM    856  CA  ALA A 113      -3.222  37.532  30.174  1.00 27.18           C  
ATOM    857  C   ALA A 113      -3.115  38.565  31.297  1.00 26.02           C  
ATOM    858  O   ALA A 113      -3.277  39.766  31.057  1.00 26.62           O  
ATOM    859  CB  ALA A 113      -4.544  36.772  30.262  1.00 28.77           C  
ATOM    860  N   TRP A 114      -2.866  38.130  32.541  1.00 23.23           N  
ATOM    861  CA  TRP A 114      -2.808  39.138  33.598  1.00 21.83           C  
ATOM    862  C   TRP A 114      -1.491  39.910  33.628  1.00 21.95           C  
ATOM    863  O   TRP A 114      -1.474  41.053  34.099  1.00 23.24           O  
ATOM    864  CB  TRP A 114      -3.105  38.539  34.977  1.00 22.71           C  
ATOM    865  CG  TRP A 114      -2.206  37.454  35.538  1.00 22.79           C  
ATOM    866  CD1 TRP A 114      -2.479  36.115  35.574  1.00 28.01           C  
ATOM    867  CD2 TRP A 114      -0.964  37.626  36.244  1.00 21.21           C  
ATOM    868  NE1 TRP A 114      -1.467  35.437  36.210  1.00 27.51           N  
ATOM    869  CE2 TRP A 114      -0.528  36.339  36.635  1.00 23.43           C  
ATOM    870  CE3 TRP A 114      -0.167  38.730  36.559  1.00 22.41           C  
ATOM    871  CZ2 TRP A 114       0.665  36.128  37.330  1.00 24.07           C  
ATOM    872  CZ3 TRP A 114       1.032  38.511  37.253  1.00 21.76           C  
ATOM    873  CH2 TRP A 114       1.426  37.219  37.626  1.00 22.96           C  
ATOM    874  N   ILE A 115      -0.392  39.341  33.122  1.00 22.12           N  
ATOM    875  CA  ILE A 115       0.827  40.134  32.973  1.00 19.83           C  
ATOM    876  C   ILE A 115       0.596  41.255  31.969  1.00 20.06           C  
ATOM    877  O   ILE A 115       0.906  42.426  32.228  1.00 19.38           O  
ATOM    878  CB  ILE A 115       2.009  39.243  32.549  1.00 19.48           C  
ATOM    879  CG1 ILE A 115       2.416  38.330  33.707  1.00 23.29           C  
ATOM    880  CG2 ILE A 115       3.190  40.116  32.078  1.00 19.83           C  
ATOM    881  CD1 ILE A 115       3.470  37.293  33.329  1.00 23.71           C  
ATOM    882  N   MET A 116       0.038  40.909  30.808  1.00 21.89           N  
ATOM    883  CA  MET A 116      -0.224  41.912  29.785  1.00 22.69           C  
ATOM    884  C   MET A 116      -1.299  42.893  30.233  1.00 23.94           C  
ATOM    885  O   MET A 116      -1.218  44.089  29.927  1.00 22.87           O  
ATOM    886  CB  MET A 116      -0.619  41.224  28.481  1.00 24.02           C  
ATOM    887  CG  MET A 116       0.460  40.310  27.978  1.00 21.88           C  
ATOM    888  SD  MET A 116       1.830  41.269  27.320  1.00 25.83           S  
ATOM    889  CE  MET A 116       2.962  39.946  26.900  1.00 27.47           C  
ATOM    890  N   GLY A 117      -2.314  42.408  30.951  1.00 22.79           N  
ATOM    891  CA  GLY A 117      -3.327  43.307  31.484  1.00 25.06           C  
ATOM    892  C   GLY A 117      -2.757  44.318  32.461  1.00 21.62           C  
ATOM    893  O   GLY A 117      -3.090  45.505  32.405  1.00 23.43           O  
ATOM    894  N   ALA A 118      -1.885  43.866  33.365  1.00 20.03           N  
ATOM    895  CA  ALA A 118      -1.251  44.798  34.291  1.00 19.73           C  
ATOM    896  C   ALA A 118      -0.420  45.824  33.540  1.00 20.27           C  
ATOM    897  O   ALA A 118      -0.434  47.009  33.884  1.00 19.59           O  
ATOM    898  CB  ALA A 118      -0.382  44.049  35.303  1.00 21.92           C  
ATOM    899  N   ASP A 119       0.283  45.382  32.497  1.00 19.37           N  
ATOM    900  CA  ASP A 119       1.091  46.292  31.691  1.00 18.83           C  
ATOM    901  C   ASP A 119       0.229  47.377  31.052  1.00 21.09           C  
ATOM    902  O   ASP A 119       0.550  48.573  31.123  1.00 18.11           O  
ATOM    903  CB  ASP A 119       1.840  45.498  30.623  1.00 17.13           C  
ATOM    904  CG  ASP A 119       2.689  46.386  29.756  1.00 20.00           C  
ATOM    905  OD1 ASP A 119       3.886  46.523  30.064  1.00 23.17           O  
ATOM    906  OD2 ASP A 119       2.145  46.975  28.796  1.00 22.31           O  
ATOM    907  N   ILE A 120      -0.880  46.981  30.427  1.00 19.53           N  
ATOM    908  CA  ILE A 120      -1.750  47.957  29.780  1.00 21.09           C  
ATOM    909  C   ILE A 120      -2.373  48.895  30.809  1.00 20.62           C  
ATOM    910  O   ILE A 120      -2.468  50.109  30.581  1.00 21.02           O  
ATOM    911  CB  ILE A 120      -2.815  47.232  28.942  1.00 22.68           C  
ATOM    912  CG1 ILE A 120      -2.138  46.509  27.775  1.00 26.04           C  
ATOM    913  CG2 ILE A 120      -3.875  48.212  28.456  1.00 25.49           C  
ATOM    914  CD1 ILE A 120      -3.022  45.485  27.096  1.00 31.47           C  
ATOM    915  N   ALA A 121      -2.787  48.355  31.962  1.00 20.28           N  
ATOM    916  CA  ALA A 121      -3.337  49.191  33.027  1.00 20.17           C  
ATOM    917  C   ALA A 121      -2.331  50.241  33.482  1.00 18.93           C  
ATOM    918  O   ALA A 121      -2.688  51.410  33.697  1.00 20.14           O  
ATOM    919  CB  ALA A 121      -3.764  48.312  34.207  1.00 20.63           C  
ATOM    920  N   MET A 122      -1.072  49.833  33.644  1.00 19.53           N  
ATOM    921  CA  MET A 122       0.004  50.739  34.031  1.00 18.87           C  
ATOM    922  C   MET A 122       0.063  51.956  33.113  1.00 19.99           C  
ATOM    923  O   MET A 122       0.136  53.100  33.580  1.00 18.78           O  
ATOM    924  CB  MET A 122       1.323  49.963  34.005  1.00 20.18           C  
ATOM    925  CG  MET A 122       2.582  50.768  34.283  1.00 21.07           C  
ATOM    926  SD  MET A 122       4.055  49.727  34.135  1.00 20.12           S  
ATOM    927  CE  MET A 122       4.195  49.465  32.355  1.00 19.63           C  
ATOM    928  N   ILE A 123       0.025  51.720  31.802  1.00 18.49           N  
ATOM    929  CA  ILE A 123       0.092  52.822  30.849  1.00 17.58           C  
ATOM    930  C   ILE A 123      -1.159  53.684  30.946  1.00 19.16           C  
ATOM    931  O   ILE A 123      -1.082  54.922  30.883  1.00 19.70           O  
ATOM    932  CB  ILE A 123       0.302  52.293  29.415  1.00 17.71           C  
ATOM    933  CG1 ILE A 123       1.511  51.347  29.321  1.00 19.09           C  
ATOM    934  CG2 ILE A 123       0.475  53.463  28.435  1.00 18.09           C  
ATOM    935  CD1 ILE A 123       2.810  51.877  29.891  1.00 19.61           C  
ATOM    936  N   ALA A 124      -2.332  53.051  31.074  1.00 20.21           N  
ATOM    937  CA  ALA A 124      -3.575  53.801  31.205  1.00 21.52           C  
ATOM    938  C   ALA A 124      -3.542  54.718  32.419  1.00 23.36           C  
ATOM    939  O   ALA A 124      -3.953  55.877  32.335  1.00 21.17           O  
ATOM    940  CB  ALA A 124      -4.766  52.841  31.300  1.00 20.42           C  
ATOM    941  N   PHE A 125      -3.042  54.221  33.555  1.00 22.30           N  
ATOM    942  CA  PHE A 125      -2.952  55.063  34.745  1.00 21.91           C  
ATOM    943  C   PHE A 125      -1.975  56.209  34.535  1.00 21.01           C  
ATOM    944  O   PHE A 125      -2.203  57.320  35.033  1.00 22.31           O  
ATOM    945  CB  PHE A 125      -2.537  54.222  35.958  1.00 21.88           C  
ATOM    946  CG  PHE A 125      -3.627  53.326  36.477  1.00 26.68           C  
ATOM    947  CD1 PHE A 125      -4.838  53.854  36.883  1.00 35.91           C  
ATOM    948  CD2 PHE A 125      -3.426  51.961  36.586  1.00 27.94           C  
ATOM    949  CE1 PHE A 125      -5.841  53.033  37.374  1.00 40.36           C  
ATOM    950  CE2 PHE A 125      -4.421  51.137  37.072  1.00 29.03           C  
ATOM    951  CZ  PHE A 125      -5.631  51.671  37.462  1.00 37.31           C  
ATOM    952  N   GLY A 126      -0.903  55.973  33.778  1.00 19.96           N  
ATOM    953  CA  GLY A 126       0.056  57.034  33.515  1.00 21.77           C  
ATOM    954  C   GLY A 126      -0.532  58.187  32.723  1.00 21.67           C  
ATOM    955  O   GLY A 126      -0.300  59.351  33.049  1.00 21.39           O  
ATOM    956  N   ILE A 127      -1.298  57.886  31.673  1.00 22.71           N  
ATOM    957  CA  ILE A 127      -1.827  58.971  30.847  1.00 21.71           C  
ATOM    958  C   ILE A 127      -2.977  59.687  31.556  1.00 21.05           C  
ATOM    959  O   ILE A 127      -3.110  60.913  31.460  1.00 22.51           O  
ATOM    960  CB  ILE A 127      -2.239  58.452  29.457  1.00 23.06           C  
ATOM    961  CG1 ILE A 127      -2.690  59.627  28.581  1.00 25.37           C  
ATOM    962  CG2 ILE A 127      -3.337  57.397  29.560  1.00 26.29           C  
ATOM    963  CD1 ILE A 127      -2.833  59.276  27.112  1.00 27.22           C  
ATOM    964  N   ILE A 128      -3.812  58.955  32.297  1.00 20.65           N  
ATOM    965  CA  ILE A 128      -4.845  59.624  33.086  1.00 22.56           C  
ATOM    966  C   ILE A 128      -4.195  60.549  34.106  1.00 22.11           C  
ATOM    967  O   ILE A 128      -4.572  61.717  34.240  1.00 23.46           O  
ATOM    968  CB  ILE A 128      -5.774  58.598  33.756  1.00 24.76           C  
ATOM    969  CG1 ILE A 128      -6.550  57.818  32.696  1.00 25.35           C  
ATOM    970  CG2 ILE A 128      -6.749  59.306  34.697  1.00 29.54           C  
ATOM    971  CD1 ILE A 128      -7.236  56.583  33.252  1.00 28.75           C  
ATOM    972  N   GLY A 129      -3.166  60.050  34.798  1.00 22.10           N  
ATOM    973  CA  GLY A 129      -2.481  60.876  35.775  1.00 20.96           C  
ATOM    974  C   GLY A 129      -1.832  62.094  35.152  1.00 21.43           C  
ATOM    975  O   GLY A 129      -1.815  63.171  35.752  1.00 23.46           O  
ATOM    976  N   ALA A 130      -1.307  61.942  33.930  1.00 22.40           N  
ATOM    977  CA  ALA A 130      -0.608  63.045  33.276  1.00 22.87           C  
ATOM    978  C   ALA A 130      -1.530  64.222  33.006  1.00 25.80           C  
ATOM    979  O   ALA A 130      -1.074  65.371  32.991  1.00 27.56           O  
ATOM    980  CB  ALA A 130       0.019  62.566  31.970  1.00 22.59           C  
ATOM    981  N   PHE A 131      -2.814  63.959  32.778  1.00 22.61           N  
ATOM    982  CA  PHE A 131      -3.808  64.997  32.526  1.00 23.74           C  
ATOM    983  C   PHE A 131      -4.546  65.440  33.787  1.00 24.98           C  
ATOM    984  O   PHE A 131      -5.345  66.385  33.727  1.00 28.19           O  
ATOM    985  CB  PHE A 131      -4.811  64.496  31.477  1.00 24.79           C  
ATOM    986  CG  PHE A 131      -4.302  64.576  30.062  1.00 26.11           C  
ATOM    987  CD1 PHE A 131      -4.275  65.790  29.391  1.00 27.58           C  
ATOM    988  CD2 PHE A 131      -3.861  63.443  29.403  1.00 25.49           C  
ATOM    989  CE1 PHE A 131      -3.804  65.874  28.079  1.00 25.81           C  
ATOM    990  CE2 PHE A 131      -3.390  63.514  28.095  1.00 27.14           C  
ATOM    991  CZ  PHE A 131      -3.369  64.736  27.430  1.00 26.00           C  
ATOM    992  N   THR A 132      -4.297  64.800  34.925  1.00 22.24           N  
ATOM    993  CA  THR A 132      -5.010  65.104  36.159  1.00 24.39           C  
ATOM    994  C   THR A 132      -4.337  66.259  36.886  1.00 28.18           C  
ATOM    995  O   THR A 132      -3.125  66.238  37.117  1.00 31.14           O  
ATOM    996  CB  THR A 132      -5.066  63.863  37.053  1.00 25.48           C  
ATOM    997  OG1 THR A 132      -5.847  62.856  36.403  1.00 26.47           O  
ATOM    998  CG2 THR A 132      -5.730  64.180  38.386  1.00 26.91           C  
ATOM    999  N   VAL A 133      -5.125  67.271  37.233  1.00 29.22           N  
ATOM   1000  CA  VAL A 133      -4.630  68.411  37.988  1.00 31.13           C  
ATOM   1001  C   VAL A 133      -4.863  68.142  39.469  1.00 33.96           C  
ATOM   1002  O   VAL A 133      -5.969  67.771  39.877  1.00 35.67           O  
ATOM   1003  CB  VAL A 133      -5.328  69.708  37.539  1.00 33.18           C  
ATOM   1004  CG1 VAL A 133      -4.883  70.889  38.393  1.00 39.26           C  
ATOM   1005  CG2 VAL A 133      -5.052  69.971  36.059  1.00 35.41           C  
ATOM   1006  N   GLY A 134      -3.825  68.306  40.273  1.00 33.58           N  
ATOM   1007  CA  GLY A 134      -3.979  68.187  41.707  1.00 34.62           C  
ATOM   1008  C   GLY A 134      -3.587  66.823  42.240  1.00 30.21           C  
ATOM   1009  O   GLY A 134      -3.108  65.938  41.524  1.00 29.85           O  
ATOM   1010  N   SER A 135      -3.834  66.659  43.543  1.00 29.51           N  
ATOM   1011  CA  SER A 135      -3.250  65.548  44.289  1.00 30.72           C  
ATOM   1012  C   SER A 135      -3.786  64.184  43.877  1.00 27.68           C  
ATOM   1013  O   SER A 135      -3.096  63.185  44.098  1.00 27.19           O  
ATOM   1014  CB  SER A 135      -3.462  65.759  45.786  1.00 41.35           C  
ATOM   1015  OG  SER A 135      -2.572  66.748  46.272  1.00 47.97           O  
ATOM   1016  N   TYR A 136      -4.977  64.108  43.273  1.00 27.06           N  
ATOM   1017  CA  TYR A 136      -5.475  62.802  42.835  1.00 27.18           C  
ATOM   1018  C   TYR A 136      -4.610  62.170  41.750  1.00 27.85           C  
ATOM   1019  O   TYR A 136      -4.720  60.959  41.525  1.00 30.31           O  
ATOM   1020  CB  TYR A 136      -6.918  62.909  42.340  1.00 32.91           C  
ATOM   1021  CG  TYR A 136      -7.924  63.134  43.447  1.00 34.10           C  
ATOM   1022  CD1 TYR A 136      -8.056  62.229  44.493  1.00 33.43           C  
ATOM   1023  CD2 TYR A 136      -8.746  64.251  43.444  1.00 33.81           C  
ATOM   1024  CE1 TYR A 136      -8.982  62.435  45.502  1.00 33.67           C  
ATOM   1025  CE2 TYR A 136      -9.670  64.465  44.448  1.00 35.26           C  
ATOM   1026  CZ  TYR A 136      -9.781  63.557  45.475  1.00 37.18           C  
ATOM   1027  OH  TYR A 136     -10.703  63.779  46.472  1.00 41.52           O  
ATOM   1028  N   LYS A 137      -3.752  62.946  41.079  1.00 23.82           N  
ATOM   1029  CA  LYS A 137      -2.856  62.349  40.089  1.00 23.87           C  
ATOM   1030  C   LYS A 137      -1.996  61.263  40.720  1.00 26.13           C  
ATOM   1031  O   LYS A 137      -1.625  60.297  40.049  1.00 24.91           O  
ATOM   1032  CB  LYS A 137      -1.961  63.415  39.450  1.00 24.60           C  
ATOM   1033  CG  LYS A 137      -0.847  63.911  40.352  1.00 29.31           C  
ATOM   1034  CD  LYS A 137       0.135  64.785  39.595  1.00 34.21           C  
ATOM   1035  CE  LYS A 137      -0.359  66.215  39.515  1.00 40.69           C  
ATOM   1036  NZ  LYS A 137       0.439  66.998  38.515  1.00 45.85           N  
ATOM   1037  N   TRP A 138      -1.697  61.386  42.011  1.00 23.27           N  
ATOM   1038  CA  TRP A 138      -0.792  60.441  42.651  1.00 22.72           C  
ATOM   1039  C   TRP A 138      -1.455  59.110  42.967  1.00 23.59           C  
ATOM   1040  O   TRP A 138      -0.751  58.106  43.105  1.00 21.63           O  
ATOM   1041  CB  TRP A 138      -0.205  61.068  43.914  1.00 23.36           C  
ATOM   1042  CG  TRP A 138       0.602  62.259  43.577  1.00 25.29           C  
ATOM   1043  CD1 TRP A 138       0.284  63.571  43.810  1.00 26.90           C  
ATOM   1044  CD2 TRP A 138       1.847  62.267  42.868  1.00 24.05           C  
ATOM   1045  NE1 TRP A 138       1.275  64.392  43.313  1.00 27.59           N  
ATOM   1046  CE2 TRP A 138       2.248  63.612  42.739  1.00 26.73           C  
ATOM   1047  CE3 TRP A 138       2.677  61.261  42.361  1.00 24.22           C  
ATOM   1048  CZ2 TRP A 138       3.438  63.979  42.103  1.00 26.32           C  
ATOM   1049  CZ3 TRP A 138       3.855  61.629  41.731  1.00 23.76           C  
ATOM   1050  CH2 TRP A 138       4.222  62.971  41.610  1.00 24.25           C  
ATOM   1051  N   PHE A 139      -2.784  59.075  43.084  1.00 23.65           N  
ATOM   1052  CA  PHE A 139      -3.472  57.794  43.178  1.00 25.15           C  
ATOM   1053  C   PHE A 139      -3.247  56.976  41.916  1.00 24.88           C  
ATOM   1054  O   PHE A 139      -2.873  55.803  41.982  1.00 23.89           O  
ATOM   1055  CB  PHE A 139      -4.964  58.007  43.420  1.00 30.79           C  
ATOM   1056  CG  PHE A 139      -5.341  58.053  44.870  1.00 38.60           C  
ATOM   1057  CD1 PHE A 139      -4.902  57.075  45.750  1.00 42.66           C  
ATOM   1058  CD2 PHE A 139      -6.137  59.067  45.351  1.00 35.39           C  
ATOM   1059  CE1 PHE A 139      -5.253  57.115  47.087  1.00 41.95           C  
ATOM   1060  CE2 PHE A 139      -6.492  59.115  46.699  1.00 34.25           C  
ATOM   1061  CZ  PHE A 139      -6.046  58.138  47.559  1.00 39.65           C  
ATOM   1062  N   TYR A 140      -3.464  57.593  40.753  1.00 22.09           N  
ATOM   1063  CA  TYR A 140      -3.181  56.908  39.496  1.00 21.56           C  
ATOM   1064  C   TYR A 140      -1.729  56.465  39.434  1.00 21.20           C  
ATOM   1065  O   TYR A 140      -1.430  55.341  39.008  1.00 23.12           O  
ATOM   1066  CB  TYR A 140      -3.499  57.822  38.311  1.00 21.64           C  
ATOM   1067  CG  TYR A 140      -4.954  58.210  38.211  1.00 26.50           C  
ATOM   1068  CD1 TYR A 140      -5.931  57.252  37.955  1.00 29.04           C  
ATOM   1069  CD2 TYR A 140      -5.349  59.531  38.355  1.00 26.59           C  
ATOM   1070  CE1 TYR A 140      -7.264  57.600  37.865  1.00 31.76           C  
ATOM   1071  CE2 TYR A 140      -6.677  59.890  38.265  1.00 29.40           C  
ATOM   1072  CZ  TYR A 140      -7.630  58.922  38.017  1.00 32.08           C  
ATOM   1073  OH  TYR A 140      -8.950  59.284  37.920  1.00 37.71           O  
ATOM   1074  N   PHE A 141      -0.812  57.344  39.851  1.00 19.70           N  
ATOM   1075  CA  PHE A 141       0.612  57.022  39.794  1.00 20.42           C  
ATOM   1076  C   PHE A 141       0.937  55.810  40.652  1.00 19.17           C  
ATOM   1077  O   PHE A 141       1.629  54.887  40.204  1.00 19.20           O  
ATOM   1078  CB  PHE A 141       1.454  58.219  40.240  1.00 19.90           C  
ATOM   1079  CG  PHE A 141       2.952  57.946  40.234  1.00 18.24           C  
ATOM   1080  CD1 PHE A 141       3.647  57.846  39.039  1.00 18.39           C  
ATOM   1081  CD2 PHE A 141       3.654  57.823  41.421  1.00 22.46           C  
ATOM   1082  CE1 PHE A 141       5.015  57.615  39.033  1.00 17.21           C  
ATOM   1083  CE2 PHE A 141       5.023  57.583  41.422  1.00 22.07           C  
ATOM   1084  CZ  PHE A 141       5.707  57.481  40.217  1.00 18.12           C  
ATOM   1085  N   VAL A 142       0.441  55.786  41.887  1.00 19.61           N  
ATOM   1086  CA  VAL A 142       0.793  54.694  42.785  1.00 19.99           C  
ATOM   1087  C   VAL A 142       0.194  53.377  42.301  1.00 20.05           C  
ATOM   1088  O   VAL A 142       0.855  52.338  42.337  1.00 20.32           O  
ATOM   1089  CB  VAL A 142       0.358  55.031  44.220  1.00 21.01           C  
ATOM   1090  CG1 VAL A 142       0.507  53.799  45.114  1.00 25.52           C  
ATOM   1091  CG2 VAL A 142       1.205  56.188  44.746  1.00 24.28           C  
ATOM   1092  N   VAL A 143      -1.045  53.400  41.806  1.00 20.20           N  
ATOM   1093  CA  VAL A 143      -1.619  52.164  41.286  1.00 22.62           C  
ATOM   1094  C   VAL A 143      -0.857  51.688  40.049  1.00 20.45           C  
ATOM   1095  O   VAL A 143      -0.627  50.483  39.875  1.00 20.91           O  
ATOM   1096  CB  VAL A 143      -3.119  52.337  41.003  1.00 23.78           C  
ATOM   1097  CG1 VAL A 143      -3.672  51.054  40.416  1.00 29.18           C  
ATOM   1098  CG2 VAL A 143      -3.864  52.671  42.299  1.00 25.01           C  
ATOM   1099  N   GLY A 144      -0.430  52.616  39.184  1.00 18.79           N  
ATOM   1100  CA  GLY A 144       0.403  52.223  38.054  1.00 18.12           C  
ATOM   1101  C   GLY A 144       1.713  51.583  38.489  1.00 18.01           C  
ATOM   1102  O   GLY A 144       2.188  50.628  37.865  1.00 17.81           O  
ATOM   1103  N   CYS A 145       2.318  52.106  39.559  1.00 17.12           N  
ATOM   1104  CA  CYS A 145       3.542  51.504  40.082  1.00 18.41           C  
ATOM   1105  C   CYS A 145       3.283  50.103  40.611  1.00 21.23           C  
ATOM   1106  O   CYS A 145       4.129  49.212  40.473  1.00 21.04           O  
ATOM   1107  CB  CYS A 145       4.137  52.376  41.185  1.00 19.18           C  
ATOM   1108  SG  CYS A 145       4.905  53.908  40.609  1.00 20.81           S  
ATOM   1109  N   ILE A 146       2.138  49.895  41.267  1.00 19.92           N  
ATOM   1110  CA  ILE A 146       1.797  48.552  41.723  1.00 20.21           C  
ATOM   1111  C   ILE A 146       1.633  47.617  40.530  1.00 21.56           C  
ATOM   1112  O   ILE A 146       2.041  46.447  40.582  1.00 20.15           O  
ATOM   1113  CB  ILE A 146       0.534  48.583  42.603  1.00 21.01           C  
ATOM   1114  CG1 ILE A 146       0.828  49.372  43.880  1.00 24.55           C  
ATOM   1115  CG2 ILE A 146       0.087  47.165  42.937  1.00 21.92           C  
ATOM   1116  CD1 ILE A 146      -0.420  49.761  44.676  1.00 24.69           C  
ATOM   1117  N   MET A 147       1.061  48.125  39.427  1.00 20.19           N  
ATOM   1118  CA  MET A 147       0.939  47.328  38.204  1.00 19.25           C  
ATOM   1119  C   MET A 147       2.310  46.915  37.666  1.00 19.50           C  
ATOM   1120  O   MET A 147       2.469  45.802  37.154  1.00 19.24           O  
ATOM   1121  CB  MET A 147       0.163  48.103  37.122  1.00 19.54           C  
ATOM   1122  CG  MET A 147      -1.333  48.320  37.415  1.00 24.91           C  
ATOM   1123  SD  MET A 147      -2.299  46.802  37.614  1.00 26.74           S  
ATOM   1124  CE  MET A 147      -2.357  46.676  39.399  1.00 26.86           C  
ATOM   1125  N   LEU A 148       3.303  47.816  37.732  1.00 18.49           N  
ATOM   1126  CA  LEU A 148       4.660  47.442  37.333  1.00 18.62           C  
ATOM   1127  C   LEU A 148       5.198  46.322  38.219  1.00 19.66           C  
ATOM   1128  O   LEU A 148       5.841  45.384  37.731  1.00 18.28           O  
ATOM   1129  CB  LEU A 148       5.585  48.668  37.379  1.00 17.45           C  
ATOM   1130  CG  LEU A 148       7.041  48.417  36.956  1.00 17.85           C  
ATOM   1131  CD1 LEU A 148       7.100  47.771  35.563  1.00 18.25           C  
ATOM   1132  CD2 LEU A 148       7.837  49.741  36.983  1.00 18.93           C  
ATOM   1133  N   ALA A 149       4.920  46.384  39.527  1.00 17.35           N  
ATOM   1134  CA  ALA A 149       5.363  45.313  40.408  1.00 17.91           C  
ATOM   1135  C   ALA A 149       4.674  44.004  40.056  1.00 19.31           C  
ATOM   1136  O   ALA A 149       5.307  42.942  40.056  1.00 20.75           O  
ATOM   1137  CB  ALA A 149       5.101  45.689  41.864  1.00 20.43           C  
ATOM   1138  N   VAL A 150       3.384  44.069  39.717  1.00 20.06           N  
ATOM   1139  CA  VAL A 150       2.632  42.871  39.343  1.00 21.18           C  
ATOM   1140  C   VAL A 150       3.217  42.238  38.084  1.00 19.96           C  
ATOM   1141  O   VAL A 150       3.485  41.030  38.048  1.00 20.65           O  
ATOM   1142  CB  VAL A 150       1.140  43.210  39.160  1.00 22.02           C  
ATOM   1143  CG1 VAL A 150       0.411  42.046  38.465  1.00 23.47           C  
ATOM   1144  CG2 VAL A 150       0.485  43.521  40.521  1.00 23.42           C  
ATOM   1145  N   LEU A 151       3.414  43.032  37.029  1.00 18.40           N  
ATOM   1146  CA  LEU A 151       3.914  42.427  35.797  1.00 16.98           C  
ATOM   1147  C   LEU A 151       5.331  41.900  35.994  1.00 19.29           C  
ATOM   1148  O   LEU A 151       5.681  40.839  35.465  1.00 20.33           O  
ATOM   1149  CB  LEU A 151       3.831  43.424  34.635  1.00 19.96           C  
ATOM   1150  CG  LEU A 151       4.783  44.606  34.529  1.00 20.84           C  
ATOM   1151  CD1 LEU A 151       6.090  44.217  33.819  1.00 19.97           C  
ATOM   1152  CD2 LEU A 151       4.083  45.740  33.779  1.00 22.28           C  
ATOM   1153  N   ALA A 152       6.150  42.610  36.776  1.00 19.22           N  
ATOM   1154  CA  ALA A 152       7.502  42.129  37.043  1.00 20.16           C  
ATOM   1155  C   ALA A 152       7.475  40.812  37.804  1.00 20.00           C  
ATOM   1156  O   ALA A 152       8.243  39.895  37.495  1.00 20.16           O  
ATOM   1157  CB  ALA A 152       8.311  43.178  37.808  1.00 19.43           C  
ATOM   1158  N   TRP A 153       6.590  40.688  38.794  1.00 19.73           N  
ATOM   1159  CA  TRP A 153       6.482  39.426  39.514  1.00 21.16           C  
ATOM   1160  C   TRP A 153       6.122  38.289  38.568  1.00 20.07           C  
ATOM   1161  O   TRP A 153       6.717  37.204  38.626  1.00 19.75           O  
ATOM   1162  CB  TRP A 153       5.449  39.558  40.630  1.00 22.20           C  
ATOM   1163  CG  TRP A 153       5.193  38.267  41.295  1.00 22.22           C  
ATOM   1164  CD1 TRP A 153       4.041  37.543  41.258  1.00 24.20           C  
ATOM   1165  CD2 TRP A 153       6.133  37.493  42.045  1.00 24.42           C  
ATOM   1166  NE1 TRP A 153       4.191  36.382  41.976  1.00 29.45           N  
ATOM   1167  CE2 TRP A 153       5.465  36.331  42.476  1.00 27.83           C  
ATOM   1168  CE3 TRP A 153       7.466  37.686  42.421  1.00 30.29           C  
ATOM   1169  CZ2 TRP A 153       6.092  35.350  43.241  1.00 31.46           C  
ATOM   1170  CZ3 TRP A 153       8.086  36.712  43.189  1.00 33.19           C  
ATOM   1171  CH2 TRP A 153       7.398  35.560  43.588  1.00 33.41           C  
ATOM   1172  N   GLY A 154       5.149  38.517  37.686  1.00 20.02           N  
ATOM   1173  CA  GLY A 154       4.787  37.480  36.729  1.00 21.00           C  
ATOM   1174  C   GLY A 154       5.949  37.091  35.833  1.00 19.94           C  
ATOM   1175  O   GLY A 154       6.180  35.905  35.582  1.00 21.23           O  
ATOM   1176  N   MET A 155       6.713  38.085  35.362  1.00 18.90           N  
ATOM   1177  CA  MET A 155       7.837  37.795  34.470  1.00 17.99           C  
ATOM   1178  C   MET A 155       8.969  37.082  35.197  1.00 20.08           C  
ATOM   1179  O   MET A 155       9.727  36.327  34.573  1.00 20.03           O  
ATOM   1180  CB  MET A 155       8.365  39.084  33.834  1.00 18.94           C  
ATOM   1181  CG  MET A 155       7.367  39.787  32.908  1.00 19.00           C  
ATOM   1182  SD  MET A 155       6.897  38.787  31.473  1.00 21.47           S  
ATOM   1183  CE  MET A 155       8.458  38.687  30.582  1.00 21.17           C  
ATOM   1184  N   ILE A 156       9.092  37.287  36.506  1.00 20.84           N  
ATOM   1185  CA  ILE A 156      10.170  36.663  37.268  1.00 20.76           C  
ATOM   1186  C   ILE A 156       9.895  35.176  37.484  1.00 23.18           C  
ATOM   1187  O   ILE A 156      10.831  34.371  37.611  1.00 25.28           O  
ATOM   1188  CB  ILE A 156      10.346  37.434  38.599  1.00 26.14           C  
ATOM   1189  CG1 ILE A 156      11.102  38.751  38.352  1.00 27.56           C  
ATOM   1190  CG2 ILE A 156      11.083  36.612  39.629  1.00 34.57           C  
ATOM   1191  CD1 ILE A 156      10.985  39.760  39.521  1.00 29.04           C  
ATOM   1192  N   ASN A 157       8.620  34.776  37.514  1.00 22.57           N  
ATOM   1193  CA  ASN A 157       8.281  33.409  37.906  1.00 25.77           C  
ATOM   1194  C   ASN A 157       8.929  32.325  37.052  1.00 23.81           C  
ATOM   1195  O   ASN A 157       9.386  31.325  37.631  1.00 27.21           O  
ATOM   1196  CB  ASN A 157       6.755  33.249  37.924  1.00 27.84           C  
ATOM   1197  CG  ASN A 157       6.167  33.494  39.298  1.00 31.15           C  
ATOM   1198  OD1 ASN A 157       5.825  32.550  40.012  1.00 38.91           O  
ATOM   1199  ND2 ASN A 157       6.061  34.752  39.685  1.00 30.76           N  
ATOM   1200  N   PRO A 158       9.023  32.443  35.722  1.00 22.57           N  
ATOM   1201  CA  PRO A 158       9.712  31.401  34.941  1.00 24.92           C  
ATOM   1202  C   PRO A 158      11.176  31.227  35.293  1.00 27.42           C  
ATOM   1203  O   PRO A 158      11.778  30.234  34.864  1.00 32.20           O  
ATOM   1204  CB  PRO A 158       9.553  31.881  33.495  1.00 24.26           C  
ATOM   1205  CG  PRO A 158       8.298  32.697  33.519  1.00 24.89           C  
ATOM   1206  CD  PRO A 158       8.302  33.389  34.852  1.00 22.19           C  
ATOM   1207  N   ILE A 159      11.774  32.150  36.044  1.00 24.69           N  
ATOM   1208  CA  ILE A 159      13.174  31.989  36.416  1.00 26.54           C  
ATOM   1209  C   ILE A 159      13.345  30.799  37.352  1.00 29.68           C  
ATOM   1210  O   ILE A 159      14.328  30.052  37.256  1.00 31.60           O  
ATOM   1211  CB  ILE A 159      13.708  33.291  37.044  1.00 22.84           C  
ATOM   1212  CG1 ILE A 159      13.813  34.393  35.986  1.00 23.26           C  
ATOM   1213  CG2 ILE A 159      15.043  33.031  37.720  1.00 24.49           C  
ATOM   1214  CD1 ILE A 159      14.223  35.736  36.525  1.00 23.65           C  
ATOM   1215  N   PHE A 160      12.387  30.581  38.259  1.00 26.63           N  
ATOM   1216  CA  PHE A 160      12.542  29.560  39.287  1.00 28.24           C  
ATOM   1217  C   PHE A 160      11.385  28.567  39.339  1.00 31.91           C  
ATOM   1218  O   PHE A 160      11.355  27.722  40.242  1.00 34.55           O  
ATOM   1219  CB  PHE A 160      12.731  30.214  40.662  1.00 34.04           C  
ATOM   1220  CG  PHE A 160      11.706  31.253  40.983  1.00 38.51           C  
ATOM   1221  CD1 PHE A 160      10.461  30.894  41.466  1.00 42.83           C  
ATOM   1222  CD2 PHE A 160      11.987  32.598  40.797  1.00 41.93           C  
ATOM   1223  CE1 PHE A 160       9.513  31.859  41.758  1.00 48.61           C  
ATOM   1224  CE2 PHE A 160      11.046  33.561  41.093  1.00 44.53           C  
ATOM   1225  CZ  PHE A 160       9.807  33.192  41.570  1.00 47.94           C  
ATOM   1226  N   LYS A 161      10.436  28.646  38.413  1.00 31.40           N  
ATOM   1227  CA  LYS A 161       9.356  27.672  38.282  1.00 31.84           C  
ATOM   1228  C   LYS A 161       9.658  26.847  37.037  1.00 34.81           C  
ATOM   1229  O   LYS A 161       9.439  27.305  35.912  1.00 35.34           O  
ATOM   1230  CB  LYS A 161       7.994  28.350  38.180  1.00 36.55           C  
ATOM   1231  CG  LYS A 161       7.477  28.957  39.473  1.00 43.28           C  
ATOM   1232  CD  LYS A 161       5.987  29.235  39.358  1.00 49.91           C  
ATOM   1233  CE  LYS A 161       5.348  29.467  40.716  1.00 52.21           C  
ATOM   1234  NZ  LYS A 161       5.910  30.656  41.405  1.00 53.30           N  
ATOM   1235  N   GLU A 162      10.182  25.640  37.240  1.00 37.84           N  
ATOM   1236  CA  GLU A 162      10.603  24.831  36.101  1.00 40.16           C  
ATOM   1237  C   GLU A 162       9.443  24.520  35.163  1.00 39.56           C  
ATOM   1238  O   GLU A 162       9.647  24.401  33.949  1.00 39.38           O  
ATOM   1239  CB  GLU A 162      11.264  23.540  36.586  1.00 47.98           C  
ATOM   1240  CG  GLU A 162      10.780  23.052  37.937  1.00 57.12           C  
ATOM   1241  CD  GLU A 162      11.565  21.855  38.430  1.00 66.95           C  
ATOM   1242  OE1 GLU A 162      12.808  21.878  38.314  1.00 69.12           O  
ATOM   1243  OE2 GLU A 162      10.943  20.893  38.930  1.00 72.84           O  
ATOM   1244  N   GLU A 163       8.222  24.393  35.691  1.00 38.16           N  
ATOM   1245  CA  GLU A 163       7.086  24.083  34.828  1.00 38.57           C  
ATOM   1246  C   GLU A 163       6.750  25.219  33.864  1.00 38.71           C  
ATOM   1247  O   GLU A 163       5.992  24.995  32.915  1.00 39.43           O  
ATOM   1248  CB  GLU A 163       5.857  23.739  35.673  1.00 46.02           C  
ATOM   1249  CG  GLU A 163       5.285  24.903  36.466  1.00 48.49           C  
ATOM   1250  CD  GLU A 163       5.926  25.065  37.837  1.00 54.87           C  
ATOM   1251  OE1 GLU A 163       6.951  24.405  38.114  1.00 54.32           O  
ATOM   1252  OE2 GLU A 163       5.389  25.850  38.647  1.00 59.33           O  
ATOM   1253  N   LEU A 164       7.294  26.413  34.079  1.00 33.59           N  
ATOM   1254  CA  LEU A 164       7.088  27.552  33.189  1.00 31.94           C  
ATOM   1255  C   LEU A 164       8.206  27.717  32.167  1.00 31.73           C  
ATOM   1256  O   LEU A 164       8.177  28.675  31.386  1.00 31.98           O  
ATOM   1257  CB  LEU A 164       6.956  28.848  34.001  1.00 30.87           C  
ATOM   1258  CG  LEU A 164       5.842  28.891  35.051  1.00 31.94           C  
ATOM   1259  CD1 LEU A 164       5.791  30.256  35.732  1.00 30.22           C  
ATOM   1260  CD2 LEU A 164       4.503  28.537  34.423  1.00 37.33           C  
ATOM   1261  N   GLN A 165       9.193  26.832  32.168  1.00 33.57           N  
ATOM   1262  CA  GLN A 165      10.381  26.980  31.338  1.00 32.98           C  
ATOM   1263  C   GLN A 165      10.285  26.101  30.096  1.00 34.65           C  
ATOM   1264  O   GLN A 165       9.751  24.990  30.147  1.00 38.26           O  
ATOM   1265  CB  GLN A 165      11.641  26.606  32.125  1.00 36.67           C  
ATOM   1266  CG  GLN A 165      11.890  27.485  33.341  1.00 32.41           C  
ATOM   1267  CD  GLN A 165      13.087  27.042  34.172  1.00 37.10           C  
ATOM   1268  OE1 GLN A 165      13.629  25.950  33.982  1.00 39.00           O  
ATOM   1269  NE2 GLN A 165      13.508  27.899  35.100  1.00 39.61           N  
ATOM   1270  N   LYS A 166      10.819  26.604  28.979  1.00 35.47           N  
ATOM   1271  CA  LYS A 166      11.024  25.756  27.807  1.00 40.21           C  
ATOM   1272  C   LYS A 166      12.235  24.851  28.001  1.00 43.84           C  
ATOM   1273  O   LYS A 166      12.143  23.626  27.869  1.00 46.92           O  
ATOM   1274  CB  LYS A 166      11.209  26.614  26.551  1.00 45.49           C  
ATOM   1275  CG  LYS A 166       9.965  27.324  26.057  1.00 48.88           C  
ATOM   1276  CD  LYS A 166      10.189  27.860  24.644  1.00 50.19           C  
ATOM   1277  CE  LYS A 166       8.888  28.306  24.000  1.00 51.07           C  
ATOM   1278  NZ  LYS A 166       7.906  27.190  23.913  1.00 56.23           N  
ATOM   1279  N   HIS A 167      13.384  25.453  28.297  1.00 45.66           N  
ATOM   1280  CA  HIS A 167      14.618  24.751  28.609  1.00 51.56           C  
ATOM   1281  C   HIS A 167      15.270  25.430  29.799  1.00 50.38           C  
ATOM   1282  O   HIS A 167      15.299  26.661  29.870  1.00 46.25           O  
ATOM   1283  CB  HIS A 167      15.608  24.775  27.437  1.00 57.39           C  
ATOM   1284  CG  HIS A 167      15.228  23.887  26.297  1.00 62.51           C  
ATOM   1285  ND1 HIS A 167      14.353  24.281  25.309  1.00 63.06           N  
ATOM   1286  CD2 HIS A 167      15.621  22.632  25.976  1.00 66.29           C  
ATOM   1287  CE1 HIS A 167      14.213  23.302  24.434  1.00 63.56           C  
ATOM   1288  NE2 HIS A 167      14.973  22.291  24.814  1.00 66.58           N  
ATOM   1289  N   LYS A 168      15.814  24.632  30.723  1.00 53.86           N  
ATOM   1290  CA  LYS A 168      16.701  25.207  31.730  1.00 55.83           C  
ATOM   1291  C   LYS A 168      17.831  25.980  31.065  1.00 54.66           C  
ATOM   1292  O   LYS A 168      18.406  26.896  31.668  1.00 52.01           O  
ATOM   1293  CB  LYS A 168      17.275  24.108  32.627  1.00 61.25           C  
ATOM   1294  CG  LYS A 168      16.340  23.612  33.721  1.00 62.77           C  
ATOM   1295  CD  LYS A 168      17.061  22.665  34.678  1.00 66.46           C  
ATOM   1296  CE  LYS A 168      18.294  22.044  34.034  1.00 70.28           C  
ATOM   1297  NZ  LYS A 168      18.544  20.656  34.504  1.00 75.33           N  
ATOM   1298  N   GLU A 169      18.147  25.615  29.818  1.00 55.30           N  
ATOM   1299  CA  GLU A 169      19.165  26.288  29.020  1.00 59.05           C  
ATOM   1300  C   GLU A 169      18.960  27.796  28.987  1.00 55.13           C  
ATOM   1301  O   GLU A 169      19.896  28.566  29.229  1.00 57.57           O  
ATOM   1302  CB  GLU A 169      19.140  25.712  27.604  1.00 66.55           C  
ATOM   1303  CG  GLU A 169      20.175  26.263  26.645  1.00 72.83           C  
ATOM   1304  CD  GLU A 169      20.062  25.630  25.267  1.00 80.75           C  
ATOM   1305  OE1 GLU A 169      18.991  25.759  24.635  1.00 82.89           O  
ATOM   1306  OE2 GLU A 169      21.039  24.992  24.820  1.00 83.96           O  
ATOM   1307  N   TYR A 170      17.736  28.238  28.681  1.00 49.18           N  
ATOM   1308  CA  TYR A 170      17.488  29.653  28.430  1.00 42.86           C  
ATOM   1309  C   TYR A 170      17.492  30.486  29.694  1.00 34.10           C  
ATOM   1310  O   TYR A 170      17.382  31.713  29.591  1.00 28.38           O  
ATOM   1311  CB  TYR A 170      16.136  29.901  27.740  1.00 43.59           C  
ATOM   1312  CG  TYR A 170      15.816  29.058  26.530  1.00 51.48           C  
ATOM   1313  CD1 TYR A 170      16.737  28.170  26.005  1.00 54.14           C  
ATOM   1314  CD2 TYR A 170      14.591  29.186  25.888  1.00 53.51           C  
ATOM   1315  CE1 TYR A 170      16.438  27.399  24.914  1.00 57.24           C  
ATOM   1316  CE2 TYR A 170      14.289  28.425  24.777  1.00 55.10           C  
ATOM   1317  CZ  TYR A 170      15.221  27.537  24.293  1.00 57.30           C  
ATOM   1318  OH  TYR A 170      14.935  26.770  23.186  1.00 60.28           O  
ATOM   1319  N   THR A 171      17.582  29.862  30.871  1.00 34.78           N  
ATOM   1320  CA  THR A 171      17.310  30.589  32.108  1.00 32.03           C  
ATOM   1321  C   THR A 171      18.298  31.727  32.317  1.00 27.35           C  
ATOM   1322  O   THR A 171      17.905  32.815  32.743  1.00 25.21           O  
ATOM   1323  CB  THR A 171      17.326  29.641  33.309  1.00 37.26           C  
ATOM   1324  OG1 THR A 171      16.360  28.605  33.105  1.00 42.38           O  
ATOM   1325  CG2 THR A 171      16.992  30.399  34.591  1.00 39.44           C  
ATOM   1326  N   GLY A 172      19.581  31.501  32.014  1.00 29.91           N  
ATOM   1327  CA  GLY A 172      20.566  32.556  32.222  1.00 25.04           C  
ATOM   1328  C   GLY A 172      20.282  33.792  31.387  1.00 23.19           C  
ATOM   1329  O   GLY A 172      20.303  34.918  31.887  1.00 22.18           O  
ATOM   1330  N   ALA A 173      19.997  33.592  30.100  1.00 25.41           N  
ATOM   1331  CA  ALA A 173      19.714  34.727  29.227  1.00 22.73           C  
ATOM   1332  C   ALA A 173      18.375  35.369  29.561  1.00 22.86           C  
ATOM   1333  O   ALA A 173      18.255  36.599  29.557  1.00 21.23           O  
ATOM   1334  CB  ALA A 173      19.747  34.273  27.768  1.00 27.59           C  
ATOM   1335  N   TYR A 174      17.352  34.554  29.841  1.00 21.82           N  
ATOM   1336  CA  TYR A 174      16.066  35.106  30.255  1.00 21.56           C  
ATOM   1337  C   TYR A 174      16.232  35.973  31.498  1.00 18.93           C  
ATOM   1338  O   TYR A 174      15.724  37.100  31.563  1.00 17.86           O  
ATOM   1339  CB  TYR A 174      15.069  33.969  30.515  1.00 20.55           C  
ATOM   1340  CG  TYR A 174      13.685  34.442  30.923  1.00 20.53           C  
ATOM   1341  CD1 TYR A 174      12.678  34.569  29.978  1.00 21.43           C  
ATOM   1342  CD2 TYR A 174      13.383  34.730  32.249  1.00 22.40           C  
ATOM   1343  CE1 TYR A 174      11.421  34.991  30.324  1.00 21.29           C  
ATOM   1344  CE2 TYR A 174      12.118  35.159  32.612  1.00 21.55           C  
ATOM   1345  CZ  TYR A 174      11.142  35.284  31.640  1.00 20.71           C  
ATOM   1346  OH  TYR A 174       9.877  35.699  31.983  1.00 21.83           O  
ATOM   1347  N   THR A 175      16.965  35.461  32.492  1.00 20.89           N  
ATOM   1348  CA  THR A 175      17.181  36.200  33.733  1.00 20.57           C  
ATOM   1349  C   THR A 175      17.899  37.518  33.472  1.00 19.82           C  
ATOM   1350  O   THR A 175      17.493  38.575  33.974  1.00 19.77           O  
ATOM   1351  CB  THR A 175      17.987  35.337  34.708  1.00 22.38           C  
ATOM   1352  OG1 THR A 175      17.259  34.142  35.002  1.00 23.33           O  
ATOM   1353  CG2 THR A 175      18.263  36.095  36.007  1.00 25.00           C  
ATOM   1354  N   THR A 176      18.971  37.474  32.679  1.00 18.54           N  
ATOM   1355  CA  THR A 176      19.785  38.663  32.460  1.00 19.29           C  
ATOM   1356  C   THR A 176      19.008  39.712  31.673  1.00 18.89           C  
ATOM   1357  O   THR A 176      19.004  40.892  32.037  1.00 18.49           O  
ATOM   1358  CB  THR A 176      21.075  38.271  31.747  1.00 22.45           C  
ATOM   1359  OG1 THR A 176      21.786  37.322  32.557  1.00 28.98           O  
ATOM   1360  CG2 THR A 176      21.962  39.492  31.502  1.00 24.96           C  
ATOM   1361  N   LEU A 177      18.327  39.288  30.601  1.00 17.67           N  
ATOM   1362  CA  LEU A 177      17.506  40.215  29.823  1.00 17.02           C  
ATOM   1363  C   LEU A 177      16.381  40.801  30.664  1.00 17.61           C  
ATOM   1364  O   LEU A 177      16.064  41.990  30.540  1.00 17.32           O  
ATOM   1365  CB  LEU A 177      16.929  39.507  28.592  1.00 17.90           C  
ATOM   1366  CG  LEU A 177      17.913  39.109  27.495  1.00 21.99           C  
ATOM   1367  CD1 LEU A 177      17.262  38.117  26.528  1.00 25.39           C  
ATOM   1368  CD2 LEU A 177      18.384  40.372  26.768  1.00 25.57           C  
ATOM   1369  N   LEU A 178      15.761  39.983  31.529  1.00 16.27           N  
ATOM   1370  CA  LEU A 178      14.651  40.480  32.333  1.00 16.64           C  
ATOM   1371  C   LEU A 178      15.130  41.482  33.371  1.00 17.01           C  
ATOM   1372  O   LEU A 178      14.461  42.493  33.616  1.00 17.56           O  
ATOM   1373  CB  LEU A 178      13.921  39.319  33.000  1.00 16.87           C  
ATOM   1374  CG  LEU A 178      12.771  39.785  33.894  1.00 18.04           C  
ATOM   1375  CD1 LEU A 178      11.734  40.513  33.054  1.00 19.01           C  
ATOM   1376  CD2 LEU A 178      12.147  38.576  34.557  1.00 21.23           C  
ATOM   1377  N   ILE A 179      16.290  41.235  33.981  1.00 15.63           N  
ATOM   1378  CA  ILE A 179      16.814  42.197  34.954  1.00 17.09           C  
ATOM   1379  C   ILE A 179      17.142  43.516  34.268  1.00 19.81           C  
ATOM   1380  O   ILE A 179      16.831  44.596  34.782  1.00 18.94           O  
ATOM   1381  CB  ILE A 179      18.037  41.608  35.678  1.00 19.31           C  
ATOM   1382  CG1 ILE A 179      17.591  40.427  36.543  1.00 20.91           C  
ATOM   1383  CG2 ILE A 179      18.741  42.697  36.508  1.00 22.67           C  
ATOM   1384  CD1 ILE A 179      18.739  39.714  37.289  1.00 24.96           C  
ATOM   1385  N   TYR A 180      17.761  43.448  33.091  1.00 16.88           N  
ATOM   1386  CA  TYR A 180      17.999  44.651  32.302  1.00 16.72           C  
ATOM   1387  C   TYR A 180      16.691  45.393  32.042  1.00 17.35           C  
ATOM   1388  O   TYR A 180      16.595  46.608  32.269  1.00 16.85           O  
ATOM   1389  CB  TYR A 180      18.701  44.247  31.003  1.00 16.69           C  
ATOM   1390  CG  TYR A 180      18.947  45.353  30.008  1.00 17.81           C  
ATOM   1391  CD1 TYR A 180      20.020  46.211  30.152  1.00 21.37           C  
ATOM   1392  CD2 TYR A 180      18.110  45.517  28.913  1.00 20.14           C  
ATOM   1393  CE1 TYR A 180      20.256  47.220  29.211  1.00 23.03           C  
ATOM   1394  CE2 TYR A 180      18.338  46.512  27.968  1.00 20.46           C  
ATOM   1395  CZ  TYR A 180      19.401  47.359  28.131  1.00 20.73           C  
ATOM   1396  OH  TYR A 180      19.617  48.341  27.193  1.00 20.15           O  
ATOM   1397  N   LEU A 181      15.653  44.665  31.617  1.00 17.20           N  
ATOM   1398  CA  LEU A 181      14.357  45.293  31.357  1.00 16.70           C  
ATOM   1399  C   LEU A 181      13.787  45.954  32.613  1.00 17.87           C  
ATOM   1400  O   LEU A 181      13.330  47.104  32.560  1.00 17.69           O  
ATOM   1401  CB  LEU A 181      13.373  44.255  30.791  1.00 16.91           C  
ATOM   1402  CG  LEU A 181      11.937  44.717  30.463  1.00 17.16           C  
ATOM   1403  CD1 LEU A 181      11.348  43.869  29.348  1.00 20.14           C  
ATOM   1404  CD2 LEU A 181      11.012  44.659  31.669  1.00 17.47           C  
ATOM   1405  N   ILE A 182      13.771  45.232  33.739  1.00 16.60           N  
ATOM   1406  CA  ILE A 182      13.168  45.771  34.965  1.00 16.02           C  
ATOM   1407  C   ILE A 182      13.907  47.020  35.425  1.00 18.20           C  
ATOM   1408  O   ILE A 182      13.283  48.020  35.818  1.00 18.10           O  
ATOM   1409  CB  ILE A 182      13.130  44.710  36.073  1.00 16.85           C  
ATOM   1410  CG1 ILE A 182      12.125  43.626  35.689  1.00 18.85           C  
ATOM   1411  CG2 ILE A 182      12.682  45.350  37.392  1.00 19.30           C  
ATOM   1412  CD1 ILE A 182      12.153  42.398  36.578  1.00 20.27           C  
ATOM   1413  N   VAL A 183      15.239  46.991  35.384  1.00 17.54           N  
ATOM   1414  CA  VAL A 183      16.029  48.168  35.763  1.00 19.09           C  
ATOM   1415  C   VAL A 183      15.617  49.383  34.937  1.00 20.47           C  
ATOM   1416  O   VAL A 183      15.376  50.476  35.473  1.00 20.16           O  
ATOM   1417  CB  VAL A 183      17.533  47.878  35.609  1.00 19.28           C  
ATOM   1418  CG1 VAL A 183      18.332  49.193  35.594  1.00 25.15           C  
ATOM   1419  CG2 VAL A 183      18.017  46.953  36.713  1.00 20.66           C  
ATOM   1420  N   LEU A 184      15.562  49.227  33.616  1.00 15.57           N  
ATOM   1421  CA  LEU A 184      15.188  50.354  32.771  1.00 17.74           C  
ATOM   1422  C   LEU A 184      13.755  50.785  33.020  1.00 19.05           C  
ATOM   1423  O   LEU A 184      13.470  51.986  33.112  1.00 17.29           O  
ATOM   1424  CB  LEU A 184      15.366  50.002  31.296  1.00 17.58           C  
ATOM   1425  CG  LEU A 184      16.778  49.758  30.801  1.00 20.35           C  
ATOM   1426  CD1 LEU A 184      16.703  49.334  29.337  1.00 21.86           C  
ATOM   1427  CD2 LEU A 184      17.622  51.019  30.941  1.00 23.47           C  
ATOM   1428  N   TRP A 185      12.832  49.826  33.132  1.00 16.13           N  
ATOM   1429  CA  TRP A 185      11.430  50.208  33.230  1.00 15.35           C  
ATOM   1430  C   TRP A 185      11.140  50.955  34.525  1.00 16.63           C  
ATOM   1431  O   TRP A 185      10.296  51.856  34.526  1.00 18.61           O  
ATOM   1432  CB  TRP A 185      10.529  48.976  33.114  1.00 16.16           C  
ATOM   1433  CG  TRP A 185      10.408  48.447  31.683  1.00 15.71           C  
ATOM   1434  CD1 TRP A 185      11.338  48.502  30.684  1.00 17.28           C  
ATOM   1435  CD2 TRP A 185       9.267  47.789  31.127  1.00 15.26           C  
ATOM   1436  NE1 TRP A 185      10.851  47.891  29.540  1.00 18.26           N  
ATOM   1437  CE2 TRP A 185       9.579  47.449  29.792  1.00 16.50           C  
ATOM   1438  CE3 TRP A 185       8.013  47.435  31.644  1.00 15.53           C  
ATOM   1439  CZ2 TRP A 185       8.677  46.799  28.956  1.00 16.87           C  
ATOM   1440  CZ3 TRP A 185       7.114  46.773  30.805  1.00 17.18           C  
ATOM   1441  CH2 TRP A 185       7.463  46.447  29.489  1.00 15.96           C  
ATOM   1442  N   VAL A 186      11.846  50.630  35.615  1.00 15.48           N  
ATOM   1443  CA  VAL A 186      11.645  51.361  36.874  1.00 15.26           C  
ATOM   1444  C   VAL A 186      12.022  52.837  36.728  1.00 15.06           C  
ATOM   1445  O   VAL A 186      11.487  53.691  37.455  1.00 17.44           O  
ATOM   1446  CB  VAL A 186      12.425  50.674  38.019  1.00 15.82           C  
ATOM   1447  CG1 VAL A 186      12.447  51.537  39.301  1.00 20.22           C  
ATOM   1448  CG2 VAL A 186      11.766  49.350  38.341  1.00 19.34           C  
ATOM   1449  N   ILE A 187      12.915  53.185  35.793  1.00 15.42           N  
ATOM   1450  CA  ILE A 187      13.295  54.598  35.677  1.00 14.71           C  
ATOM   1451  C   ILE A 187      12.156  55.431  35.098  1.00 14.88           C  
ATOM   1452  O   ILE A 187      12.045  56.634  35.398  1.00 17.76           O  
ATOM   1453  CB  ILE A 187      14.567  54.766  34.826  1.00 16.74           C  
ATOM   1454  CG1 ILE A 187      15.649  53.799  35.278  1.00 23.46           C  
ATOM   1455  CG2 ILE A 187      15.069  56.217  34.914  1.00 18.60           C  
ATOM   1456  CD1 ILE A 187      16.048  53.973  36.662  1.00 24.20           C  
ATOM   1457  N   TYR A 188      11.292  54.829  34.272  1.00 15.94           N  
ATOM   1458  CA  TYR A 188      10.205  55.603  33.673  1.00 17.27           C  
ATOM   1459  C   TYR A 188       9.300  56.245  34.721  1.00 14.29           C  
ATOM   1460  O   TYR A 188       9.050  57.461  34.616  1.00 15.73           O  
ATOM   1461  CB  TYR A 188       9.396  54.733  32.707  1.00 16.55           C  
ATOM   1462  CG  TYR A 188      10.083  54.449  31.391  1.00 16.33           C  
ATOM   1463  CD1 TYR A 188      11.000  53.416  31.283  1.00 16.85           C  
ATOM   1464  CD2 TYR A 188       9.769  55.174  30.257  1.00 16.26           C  
ATOM   1465  CE1 TYR A 188      11.623  53.140  30.060  1.00 15.43           C  
ATOM   1466  CE2 TYR A 188      10.404  54.913  29.023  1.00 17.74           C  
ATOM   1467  CZ  TYR A 188      11.310  53.876  28.953  1.00 17.31           C  
ATOM   1468  OH  TYR A 188      11.915  53.587  27.744  1.00 17.77           O  
ATOM   1469  N   PRO A 189       8.772  55.530  35.723  1.00 14.35           N  
ATOM   1470  CA  PRO A 189       7.969  56.232  36.749  1.00 14.98           C  
ATOM   1471  C   PRO A 189       8.756  57.231  37.572  1.00 16.58           C  
ATOM   1472  O   PRO A 189       8.152  58.177  38.090  1.00 17.12           O  
ATOM   1473  CB  PRO A 189       7.410  55.094  37.622  1.00 16.35           C  
ATOM   1474  CG  PRO A 189       8.330  53.905  37.338  1.00 15.98           C  
ATOM   1475  CD  PRO A 189       8.713  54.061  35.903  1.00 16.19           C  
ATOM   1476  N   ILE A 190      10.077  57.081  37.718  1.00 16.67           N  
ATOM   1477  CA  ILE A 190      10.833  58.133  38.393  1.00 17.08           C  
ATOM   1478  C   ILE A 190      10.793  59.409  37.565  1.00 16.54           C  
ATOM   1479  O   ILE A 190      10.534  60.499  38.083  1.00 17.16           O  
ATOM   1480  CB  ILE A 190      12.283  57.696  38.674  1.00 17.15           C  
ATOM   1481  CG1 ILE A 190      12.291  56.411  39.506  1.00 18.74           C  
ATOM   1482  CG2 ILE A 190      13.039  58.817  39.419  1.00 20.34           C  
ATOM   1483  CD1 ILE A 190      13.696  55.840  39.754  1.00 20.84           C  
ATOM   1484  N   VAL A 191      11.051  59.290  36.258  1.00 17.09           N  
ATOM   1485  CA  VAL A 191      10.978  60.453  35.375  1.00 16.50           C  
ATOM   1486  C   VAL A 191       9.578  61.055  35.393  1.00 18.75           C  
ATOM   1487  O   VAL A 191       9.410  62.281  35.453  1.00 18.69           O  
ATOM   1488  CB  VAL A 191      11.400  60.047  33.950  1.00 18.30           C  
ATOM   1489  CG1 VAL A 191      11.247  61.222  33.006  1.00 19.74           C  
ATOM   1490  CG2 VAL A 191      12.833  59.525  33.973  1.00 20.38           C  
ATOM   1491  N   TRP A 192       8.550  60.202  35.358  1.00 17.25           N  
ATOM   1492  CA  TRP A 192       7.177  60.695  35.387  1.00 17.98           C  
ATOM   1493  C   TRP A 192       6.910  61.441  36.681  1.00 19.32           C  
ATOM   1494  O   TRP A 192       6.367  62.549  36.678  1.00 19.96           O  
ATOM   1495  CB  TRP A 192       6.201  59.527  35.256  1.00 17.36           C  
ATOM   1496  CG  TRP A 192       4.754  59.896  35.000  1.00 18.00           C  
ATOM   1497  CD1 TRP A 192       4.107  59.847  33.798  1.00 19.62           C  
ATOM   1498  CD2 TRP A 192       3.774  60.323  35.965  1.00 20.49           C  
ATOM   1499  NE1 TRP A 192       2.798  60.218  33.947  1.00 22.56           N  
ATOM   1500  CE2 TRP A 192       2.566  60.535  35.262  1.00 21.29           C  
ATOM   1501  CE3 TRP A 192       3.802  60.572  37.341  1.00 20.13           C  
ATOM   1502  CZ2 TRP A 192       1.393  60.956  35.898  1.00 24.97           C  
ATOM   1503  CZ3 TRP A 192       2.637  60.996  37.972  1.00 26.00           C  
ATOM   1504  CH2 TRP A 192       1.450  61.193  37.247  1.00 27.45           C  
ATOM   1505  N   GLY A 193       7.286  60.835  37.806  1.00 18.85           N  
ATOM   1506  CA  GLY A 193       7.029  61.480  39.085  1.00 19.54           C  
ATOM   1507  C   GLY A 193       7.703  62.835  39.195  1.00 20.62           C  
ATOM   1508  O   GLY A 193       7.147  63.774  39.764  1.00 22.14           O  
ATOM   1509  N   LEU A 194       8.900  62.965  38.621  1.00 20.03           N  
ATOM   1510  CA  LEU A 194       9.635  64.221  38.681  1.00 21.18           C  
ATOM   1511  C   LEU A 194       9.102  65.252  37.691  1.00 21.98           C  
ATOM   1512  O   LEU A 194       9.227  66.455  37.932  1.00 23.49           O  
ATOM   1513  CB  LEU A 194      11.118  63.970  38.401  1.00 20.50           C  
ATOM   1514  CG  LEU A 194      11.891  63.151  39.428  1.00 24.03           C  
ATOM   1515  CD1 LEU A 194      13.250  62.792  38.856  1.00 24.18           C  
ATOM   1516  CD2 LEU A 194      12.041  63.970  40.696  1.00 27.11           C  
ATOM   1517  N   GLY A 195       8.538  64.804  36.570  1.00 21.71           N  
ATOM   1518  CA  GLY A 195       8.133  65.731  35.529  1.00 23.32           C  
ATOM   1519  C   GLY A 195       6.629  65.886  35.435  1.00 21.24           C  
ATOM   1520  O   GLY A 195       6.053  66.821  35.998  1.00 22.78           O  
ATOM   1521  N   ALA A 196       5.995  64.960  34.712  1.00 22.52           N  
ATOM   1522  CA  ALA A 196       4.547  64.997  34.525  1.00 21.90           C  
ATOM   1523  C   ALA A 196       3.803  65.107  35.847  1.00 24.10           C  
ATOM   1524  O   ALA A 196       2.793  65.811  35.946  1.00 26.67           O  
ATOM   1525  CB  ALA A 196       4.095  63.743  33.772  1.00 22.56           C  
ATOM   1526  N   GLY A 197       4.289  64.425  36.878  1.00 25.07           N  
ATOM   1527  CA  GLY A 197       3.626  64.475  38.163  1.00 25.51           C  
ATOM   1528  C   GLY A 197       4.025  65.668  39.002  1.00 24.90           C  
ATOM   1529  O   GLY A 197       3.197  66.536  39.292  1.00 28.24           O  
ATOM   1530  N   GLY A 198       5.299  65.734  39.382  1.00 23.67           N  
ATOM   1531  CA  GLY A 198       5.745  66.721  40.346  1.00 23.78           C  
ATOM   1532  C   GLY A 198       6.126  68.096  39.829  1.00 24.30           C  
ATOM   1533  O   GLY A 198       6.262  69.025  40.628  1.00 27.56           O  
ATOM   1534  N   HIS A 199       6.340  68.238  38.516  1.00 23.54           N  
ATOM   1535  CA  HIS A 199       6.783  69.512  37.920  1.00 24.04           C  
ATOM   1536  C   HIS A 199       8.091  69.983  38.548  1.00 25.51           C  
ATOM   1537  O   HIS A 199       8.280  71.176  38.825  1.00 27.70           O  
ATOM   1538  CB  HIS A 199       5.729  70.615  38.046  1.00 25.80           C  
ATOM   1539  CG  HIS A 199       4.407  70.293  37.422  1.00 28.12           C  
ATOM   1540  ND1 HIS A 199       3.406  71.235  37.308  1.00 32.28           N  
ATOM   1541  CD2 HIS A 199       3.912  69.150  36.895  1.00 29.25           C  
ATOM   1542  CE1 HIS A 199       2.355  70.688  36.724  1.00 35.35           C  
ATOM   1543  NE2 HIS A 199       2.632  69.421  36.473  1.00 30.75           N  
ATOM   1544  N   ILE A 200       8.986  69.033  38.793  1.00 23.00           N  
ATOM   1545  CA  ILE A 200      10.285  69.276  39.409  1.00 25.45           C  
ATOM   1546  C   ILE A 200      11.332  69.419  38.307  1.00 25.79           C  
ATOM   1547  O   ILE A 200      12.315  70.154  38.462  1.00 27.53           O  
ATOM   1548  CB  ILE A 200      10.639  68.129  40.378  1.00 30.92           C  
ATOM   1549  CG1 ILE A 200       9.652  68.107  41.548  1.00 38.61           C  
ATOM   1550  CG2 ILE A 200      12.064  68.252  40.882  1.00 37.58           C  
ATOM   1551  CD1 ILE A 200       9.855  66.932  42.492  1.00 43.06           C  
ATOM   1552  N   ILE A 201      11.138  68.710  37.193  1.00 23.32           N  
ATOM   1553  CA  ILE A 201      12.038  68.804  36.050  1.00 22.85           C  
ATOM   1554  C   ILE A 201      11.246  69.269  34.834  1.00 23.05           C  
ATOM   1555  O   ILE A 201      10.040  69.024  34.720  1.00 23.78           O  
ATOM   1556  CB  ILE A 201      12.767  67.472  35.746  1.00 21.85           C  
ATOM   1557  CG1 ILE A 201      11.773  66.385  35.335  1.00 22.33           C  
ATOM   1558  CG2 ILE A 201      13.587  67.029  36.947  1.00 25.65           C  
ATOM   1559  CD1 ILE A 201      12.436  65.050  34.953  1.00 23.60           C  
ATOM   1560  N   GLY A 202      11.942  69.962  33.925  1.00 22.04           N  
ATOM   1561  CA  GLY A 202      11.312  70.521  32.751  1.00 23.98           C  
ATOM   1562  C   GLY A 202      11.013  69.505  31.656  1.00 20.34           C  
ATOM   1563  O   GLY A 202      11.397  68.334  31.689  1.00 20.26           O  
ATOM   1564  N   VAL A 203      10.296  69.996  30.647  1.00 21.54           N  
ATOM   1565  CA  VAL A 203       9.806  69.121  29.588  1.00 20.68           C  
ATOM   1566  C   VAL A 203      10.949  68.638  28.707  1.00 20.30           C  
ATOM   1567  O   VAL A 203      11.005  67.454  28.368  1.00 20.96           O  
ATOM   1568  CB  VAL A 203       8.708  69.840  28.788  1.00 22.26           C  
ATOM   1569  CG1 VAL A 203       8.392  69.107  27.484  1.00 24.81           C  
ATOM   1570  CG2 VAL A 203       7.457  69.984  29.661  1.00 23.26           C  
ATOM   1571  N   ASP A 204      11.887  69.522  28.344  1.00 21.84           N  
ATOM   1572  CA  ASP A 204      13.005  69.057  27.516  1.00 21.05           C  
ATOM   1573  C   ASP A 204      13.834  68.014  28.252  1.00 20.55           C  
ATOM   1574  O   ASP A 204      14.312  67.051  27.645  1.00 20.72           O  
ATOM   1575  CB  ASP A 204      13.910  70.216  27.096  1.00 21.94           C  
ATOM   1576  CG  ASP A 204      13.262  71.157  26.094  1.00 26.84           C  
ATOM   1577  OD1 ASP A 204      12.370  70.730  25.326  1.00 25.93           O  
ATOM   1578  OD2 ASP A 204      13.678  72.341  26.064  1.00 32.93           O  
ATOM   1579  N   VAL A 205      14.029  68.196  29.563  1.00 22.04           N  
ATOM   1580  CA  VAL A 205      14.778  67.211  30.342  1.00 20.78           C  
ATOM   1581  C   VAL A 205      14.066  65.862  30.323  1.00 21.71           C  
ATOM   1582  O   VAL A 205      14.699  64.816  30.140  1.00 20.99           O  
ATOM   1583  CB  VAL A 205      14.994  67.712  31.781  1.00 25.29           C  
ATOM   1584  CG1 VAL A 205      15.466  66.572  32.662  1.00 27.79           C  
ATOM   1585  CG2 VAL A 205      16.003  68.848  31.792  1.00 33.00           C  
ATOM   1586  N  AGLU A 206      12.739  65.855  30.519  0.66 17.95           N  
ATOM   1587  N  BGLU A 206      12.746  65.876  30.528  0.34 21.02           N  
ATOM   1588  CA AGLU A 206      11.996  64.594  30.492  0.66 20.40           C  
ATOM   1589  CA BGLU A 206      11.953  64.652  30.487  0.34 21.01           C  
ATOM   1590  C  AGLU A 206      12.080  63.949  29.114  0.66 19.63           C  
ATOM   1591  C  BGLU A 206      12.066  63.972  29.129  0.34 19.67           C  
ATOM   1592  O  AGLU A 206      12.203  62.721  28.998  0.66 17.90           O  
ATOM   1593  O  BGLU A 206      12.188  62.743  29.044  0.34 18.42           O  
ATOM   1594  CB AGLU A 206      10.530  64.816  30.902  0.66 21.66           C  
ATOM   1595  CB BGLU A 206      10.494  64.989  30.808  0.34 23.40           C  
ATOM   1596  CG AGLU A 206       9.570  65.056  29.731  0.66 27.57           C  
ATOM   1597  CG BGLU A 206       9.709  63.881  31.466  0.34 24.61           C  
ATOM   1598  CD AGLU A 206       8.121  65.284  30.126  0.66 24.69           C  
ATOM   1599  CD BGLU A 206       8.268  64.265  31.759  0.34 24.17           C  
ATOM   1600  OE1AGLU A 206       7.278  65.355  29.200  0.66 24.44           O  
ATOM   1601  OE1BGLU A 206       7.914  65.446  31.562  0.34 22.12           O  
ATOM   1602  OE2AGLU A 206       7.821  65.396  31.336  0.66 21.53           O  
ATOM   1603  OE2BGLU A 206       7.489  63.386  32.182  0.34 31.36           O  
ATOM   1604  N   ILE A 207      12.043  64.763  28.055  1.00 17.79           N  
ATOM   1605  CA  ILE A 207      12.152  64.217  26.706  1.00 17.85           C  
ATOM   1606  C   ILE A 207      13.492  63.522  26.526  1.00 20.95           C  
ATOM   1607  O   ILE A 207      13.578  62.427  25.960  1.00 18.54           O  
ATOM   1608  CB  ILE A 207      11.979  65.336  25.668  1.00 18.97           C  
ATOM   1609  CG1 ILE A 207      10.540  65.862  25.624  1.00 19.67           C  
ATOM   1610  CG2 ILE A 207      12.460  64.849  24.274  1.00 19.25           C  
ATOM   1611  CD1 ILE A 207      10.407  67.184  24.839  1.00 21.60           C  
ATOM   1612  N   ILE A 208      14.568  64.178  26.960  1.00 19.49           N  
ATOM   1613  CA  ILE A 208      15.902  63.605  26.797  1.00 19.37           C  
ATOM   1614  C   ILE A 208      16.058  62.336  27.625  1.00 18.72           C  
ATOM   1615  O   ILE A 208      16.591  61.323  27.145  1.00 18.22           O  
ATOM   1616  CB  ILE A 208      16.959  64.661  27.164  1.00 20.42           C  
ATOM   1617  CG1 ILE A 208      16.961  65.746  26.081  1.00 21.49           C  
ATOM   1618  CG2 ILE A 208      18.328  64.005  27.315  1.00 22.29           C  
ATOM   1619  CD1 ILE A 208      17.673  67.028  26.453  1.00 25.95           C  
ATOM   1620  N   ALA A 209      15.593  62.359  28.871  1.00 17.98           N  
ATOM   1621  CA  ALA A 209      15.714  61.185  29.722  1.00 17.83           C  
ATOM   1622  C   ALA A 209      14.987  59.996  29.111  1.00 17.81           C  
ATOM   1623  O   ALA A 209      15.528  58.890  29.045  1.00 18.65           O  
ATOM   1624  CB  ALA A 209      15.162  61.503  31.111  1.00 18.05           C  
ATOM   1625  N   MET A 210      13.761  60.213  28.638  1.00 16.60           N  
ATOM   1626  CA  MET A 210      13.022  59.096  28.070  1.00 19.40           C  
ATOM   1627  C   MET A 210      13.509  58.734  26.675  1.00 17.84           C  
ATOM   1628  O   MET A 210      13.353  57.580  26.278  1.00 18.91           O  
ATOM   1629  CB  MET A 210      11.524  59.392  28.077  1.00 24.30           C  
ATOM   1630  CG  MET A 210      10.892  59.189  29.477  1.00 25.25           C  
ATOM   1631  SD  MET A 210       9.138  59.478  29.438  1.00 26.53           S  
ATOM   1632  CE  MET A 210       9.144  61.237  29.451  1.00 27.00           C  
ATOM   1633  N   GLY A 211      14.144  59.662  25.953  1.00 17.09           N  
ATOM   1634  CA  GLY A 211      14.798  59.276  24.710  1.00 18.51           C  
ATOM   1635  C   GLY A 211      15.944  58.311  24.947  1.00 18.83           C  
ATOM   1636  O   GLY A 211      16.105  57.326  24.214  1.00 17.78           O  
ATOM   1637  N   ILE A 212      16.748  58.575  25.983  1.00 17.56           N  
ATOM   1638  CA  ILE A 212      17.824  57.656  26.347  1.00 17.73           C  
ATOM   1639  C   ILE A 212      17.244  56.310  26.755  1.00 17.59           C  
ATOM   1640  O   ILE A 212      17.668  55.254  26.265  1.00 17.82           O  
ATOM   1641  CB  ILE A 212      18.687  58.255  27.472  1.00 18.47           C  
ATOM   1642  CG1 ILE A 212      19.448  59.473  26.958  1.00 20.46           C  
ATOM   1643  CG2 ILE A 212      19.667  57.214  28.017  1.00 20.29           C  
ATOM   1644  CD1 ILE A 212      19.953  60.356  28.080  1.00 25.20           C  
ATOM   1645  N   LEU A 213      16.265  56.327  27.666  1.00 16.27           N  
ATOM   1646  CA  LEU A 213      15.651  55.076  28.104  1.00 15.46           C  
ATOM   1647  C   LEU A 213      15.069  54.309  26.926  1.00 17.52           C  
ATOM   1648  O   LEU A 213      15.215  53.083  26.850  1.00 17.15           O  
ATOM   1649  CB  LEU A 213      14.566  55.350  29.142  1.00 17.02           C  
ATOM   1650  CG  LEU A 213      15.035  55.873  30.503  1.00 17.70           C  
ATOM   1651  CD1 LEU A 213      13.843  56.379  31.311  1.00 19.56           C  
ATOM   1652  CD2 LEU A 213      15.743  54.752  31.260  1.00 17.49           C  
ATOM   1653  N   ASP A 214      14.402  55.006  25.999  1.00 17.83           N  
ATOM   1654  CA  ASP A 214      13.758  54.310  24.883  1.00 17.91           C  
ATOM   1655  C   ASP A 214      14.778  53.626  23.986  1.00 16.00           C  
ATOM   1656  O   ASP A 214      14.523  52.524  23.486  1.00 16.59           O  
ATOM   1657  CB  ASP A 214      12.910  55.266  24.042  1.00 16.47           C  
ATOM   1658  CG  ASP A 214      11.593  55.652  24.713  1.00 21.68           C  
ATOM   1659  OD1 ASP A 214      11.131  54.959  25.655  1.00 22.57           O  
ATOM   1660  OD2 ASP A 214      10.983  56.633  24.246  1.00 22.79           O  
ATOM   1661  N   LEU A 215      15.927  54.275  23.747  1.00 17.01           N  
ATOM   1662  CA  LEU A 215      16.970  53.631  22.945  1.00 17.49           C  
ATOM   1663  C   LEU A 215      17.533  52.402  23.650  1.00 16.50           C  
ATOM   1664  O   LEU A 215      17.824  51.392  22.998  1.00 17.32           O  
ATOM   1665  CB  LEU A 215      18.087  54.626  22.640  1.00 17.37           C  
ATOM   1666  CG  LEU A 215      17.634  55.758  21.728  1.00 20.10           C  
ATOM   1667  CD1 LEU A 215      18.753  56.782  21.584  1.00 25.62           C  
ATOM   1668  CD2 LEU A 215      17.233  55.199  20.370  1.00 24.21           C  
ATOM   1669  N   LEU A 216      17.700  52.467  24.974  1.00 14.84           N  
ATOM   1670  CA  LEU A 216      18.175  51.304  25.720  1.00 15.08           C  
ATOM   1671  C   LEU A 216      17.116  50.207  25.772  1.00 15.22           C  
ATOM   1672  O   LEU A 216      17.441  49.012  25.699  1.00 17.01           O  
ATOM   1673  CB  LEU A 216      18.575  51.720  27.139  1.00 16.97           C  
ATOM   1674  CG  LEU A 216      19.737  52.715  27.218  1.00 17.57           C  
ATOM   1675  CD1 LEU A 216      19.870  53.282  28.632  1.00 18.90           C  
ATOM   1676  CD2 LEU A 216      21.050  52.056  26.755  1.00 21.77           C  
ATOM   1677  N   ALA A 217      15.845  50.594  25.919  1.00 15.26           N  
ATOM   1678  CA  ALA A 217      14.770  49.641  26.165  1.00 16.03           C  
ATOM   1679  C   ALA A 217      14.199  49.036  24.894  1.00 16.96           C  
ATOM   1680  O   ALA A 217      13.508  48.003  24.977  1.00 16.41           O  
ATOM   1681  CB  ALA A 217      13.633  50.317  26.949  1.00 16.97           C  
ATOM   1682  N   LYS A 218      14.484  49.635  23.722  1.00 16.63           N  
ATOM   1683  CA  LYS A 218      13.899  49.116  22.486  1.00 14.45           C  
ATOM   1684  C   LYS A 218      14.993  48.584  21.557  1.00 15.87           C  
ATOM   1685  O   LYS A 218      15.200  47.364  21.581  1.00 17.86           O  
ATOM   1686  CB  LYS A 218      12.977  50.147  21.829  1.00 16.52           C  
ATOM   1687  CG  LYS A 218      11.702  50.338  22.642  1.00 18.38           C  
ATOM   1688  CD  LYS A 218      10.735  51.257  21.933  1.00 19.79           C  
ATOM   1689  CE  LYS A 218       9.410  51.289  22.673  1.00 23.69           C  
ATOM   1690  NZ  LYS A 218       9.455  52.209  23.850  1.00 21.53           N  
ATOM   1691  N   PRO A 219      15.739  49.379  20.766  1.00 15.88           N  
ATOM   1692  CA  PRO A 219      16.679  48.717  19.841  1.00 17.62           C  
ATOM   1693  C   PRO A 219      17.818  47.992  20.544  1.00 18.08           C  
ATOM   1694  O   PRO A 219      18.230  46.922  20.070  1.00 18.31           O  
ATOM   1695  CB  PRO A 219      17.178  49.870  18.957  1.00 19.56           C  
ATOM   1696  CG  PRO A 219      17.000  51.090  19.796  1.00 18.63           C  
ATOM   1697  CD  PRO A 219      15.721  50.837  20.534  1.00 15.94           C  
ATOM   1698  N   LEU A 220      18.375  48.527  21.632  1.00 17.00           N  
ATOM   1699  CA  LEU A 220      19.485  47.816  22.267  1.00 18.33           C  
ATOM   1700  C   LEU A 220      18.999  46.523  22.921  1.00 18.11           C  
ATOM   1701  O   LEU A 220      19.599  45.459  22.733  1.00 19.04           O  
ATOM   1702  CB  LEU A 220      20.214  48.714  23.269  1.00 20.82           C  
ATOM   1703  CG  LEU A 220      21.468  48.048  23.858  1.00 22.72           C  
ATOM   1704  CD1 LEU A 220      22.459  47.662  22.757  1.00 24.97           C  
ATOM   1705  CD2 LEU A 220      22.136  48.977  24.870  1.00 22.78           C  
ATOM   1706  N   TYR A 221      17.897  46.593  23.669  1.00 17.10           N  
ATOM   1707  CA  TYR A 221      17.239  45.396  24.188  1.00 17.10           C  
ATOM   1708  C   TYR A 221      16.945  44.391  23.079  1.00 17.65           C  
ATOM   1709  O   TYR A 221      17.193  43.190  23.235  1.00 17.28           O  
ATOM   1710  CB  TYR A 221      15.951  45.817  24.890  1.00 17.47           C  
ATOM   1711  CG  TYR A 221      15.017  44.708  25.336  1.00 16.72           C  
ATOM   1712  CD1 TYR A 221      15.244  44.010  26.512  1.00 20.32           C  
ATOM   1713  CD2 TYR A 221      13.860  44.418  24.617  1.00 15.95           C  
ATOM   1714  CE1 TYR A 221      14.371  43.028  26.944  1.00 20.83           C  
ATOM   1715  CE2 TYR A 221      12.967  43.440  25.045  1.00 18.59           C  
ATOM   1716  CZ  TYR A 221      13.229  42.751  26.211  1.00 19.48           C  
ATOM   1717  OH  TYR A 221      12.356  41.786  26.654  1.00 20.52           O  
ATOM   1718  N   ALA A 222      16.413  44.868  21.949  1.00 16.86           N  
ATOM   1719  CA  ALA A 222      16.104  43.953  20.847  1.00 17.23           C  
ATOM   1720  C   ALA A 222      17.351  43.229  20.364  1.00 17.15           C  
ATOM   1721  O   ALA A 222      17.301  42.026  20.086  1.00 18.83           O  
ATOM   1722  CB  ALA A 222      15.443  44.699  19.686  1.00 20.11           C  
ATOM   1723  N   ILE A 223      18.476  43.936  20.240  1.00 17.90           N  
ATOM   1724  CA  ILE A 223      19.709  43.259  19.831  1.00 18.21           C  
ATOM   1725  C   ILE A 223      20.067  42.150  20.819  1.00 20.53           C  
ATOM   1726  O   ILE A 223      20.483  41.052  20.420  1.00 19.07           O  
ATOM   1727  CB  ILE A 223      20.849  44.277  19.675  1.00 18.80           C  
ATOM   1728  CG1 ILE A 223      20.549  45.175  18.476  1.00 22.87           C  
ATOM   1729  CG2 ILE A 223      22.181  43.557  19.453  1.00 23.09           C  
ATOM   1730  CD1 ILE A 223      21.464  46.374  18.367  1.00 26.37           C  
ATOM   1731  N   GLY A 224      19.878  42.403  22.120  1.00 18.66           N  
ATOM   1732  CA  GLY A 224      20.138  41.367  23.114  1.00 18.03           C  
ATOM   1733  C   GLY A 224      19.226  40.162  22.961  1.00 20.34           C  
ATOM   1734  O   GLY A 224      19.674  39.010  23.049  1.00 19.78           O  
ATOM   1735  N   VAL A 225      17.933  40.409  22.722  1.00 18.06           N  
ATOM   1736  CA  VAL A 225      16.985  39.314  22.516  1.00 17.51           C  
ATOM   1737  C   VAL A 225      17.338  38.532  21.258  1.00 17.68           C  
ATOM   1738  O   VAL A 225      17.273  37.298  21.236  1.00 19.76           O  
ATOM   1739  CB  VAL A 225      15.548  39.861  22.436  1.00 18.96           C  
ATOM   1740  CG1 VAL A 225      14.585  38.758  22.009  1.00 22.56           C  
ATOM   1741  CG2 VAL A 225      15.108  40.474  23.778  1.00 19.43           C  
ATOM   1742  N   LEU A 226      17.650  39.232  20.181  1.00 16.70           N  
ATOM   1743  CA  LEU A 226      17.968  38.603  18.898  1.00 18.55           C  
ATOM   1744  C   LEU A 226      19.232  37.783  18.965  1.00 19.73           C  
ATOM   1745  O   LEU A 226      19.265  36.712  18.428  1.00 19.98           O  
ATOM   1746  CB  LEU A 226      18.010  39.615  17.776  1.00 20.25           C  
ATOM   1747  CG  LEU A 226      16.646  40.180  17.417  1.00 24.71           C  
ATOM   1748  CD1 LEU A 226      16.803  41.420  16.559  1.00 43.93           C  
ATOM   1749  CD2 LEU A 226      15.787  39.134  16.725  1.00 23.93           C  
ATOM   1750  N   ILE A 227      20.248  38.302  19.613  1.00 18.88           N  
ATOM   1751  CA  ILE A 227      21.455  37.505  19.831  1.00 20.27           C  
ATOM   1752  C   ILE A 227      21.123  36.250  20.628  1.00 20.30           C  
ATOM   1753  O   ILE A 227      21.596  35.148  20.308  1.00 21.52           O  
ATOM   1754  CB  ILE A 227      22.533  38.347  20.534  1.00 23.60           C  
ATOM   1755  CG1 ILE A 227      23.074  39.398  19.569  1.00 23.86           C  
ATOM   1756  CG2 ILE A 227      23.663  37.446  21.053  1.00 26.51           C  
ATOM   1757  CD1 ILE A 227      23.984  40.410  20.225  1.00 26.61           C  
ATOM   1758  N   THR A 228      20.300  36.395  21.672  1.00 20.27           N  
ATOM   1759  CA  THR A 228      19.943  35.250  22.506  1.00 21.05           C  
ATOM   1760  C   THR A 228      19.275  34.151  21.693  1.00 19.95           C  
ATOM   1761  O   THR A 228      19.658  32.975  21.786  1.00 21.41           O  
ATOM   1762  CB  THR A 228      19.027  35.704  23.649  1.00 20.60           C  
ATOM   1763  OG1 THR A 228      19.775  36.548  24.524  1.00 23.83           O  
ATOM   1764  CG2 THR A 228      18.504  34.496  24.424  1.00 24.77           C  
ATOM   1765  N   VAL A 229      18.260  34.501  20.901  1.00 20.74           N  
ATOM   1766  CA  VAL A 229      17.545  33.452  20.179  1.00 20.85           C  
ATOM   1767  C   VAL A 229      18.428  32.839  19.097  1.00 19.81           C  
ATOM   1768  O   VAL A 229      18.332  31.639  18.818  1.00 22.52           O  
ATOM   1769  CB  VAL A 229      16.215  33.956  19.587  1.00 21.77           C  
ATOM   1770  CG1 VAL A 229      15.251  34.384  20.703  1.00 23.41           C  
ATOM   1771  CG2 VAL A 229      16.433  35.088  18.601  1.00 26.30           C  
ATOM   1772  N   GLU A 230      19.312  33.631  18.488  1.00 20.38           N  
ATOM   1773  CA  GLU A 230      20.233  33.064  17.506  1.00 20.46           C  
ATOM   1774  C   GLU A 230      21.212  32.097  18.158  1.00 22.35           C  
ATOM   1775  O   GLU A 230      21.482  31.014  17.619  1.00 24.07           O  
ATOM   1776  CB  GLU A 230      20.982  34.191  16.794  1.00 20.72           C  
ATOM   1777  CG  GLU A 230      20.101  35.044  15.902  1.00 22.75           C  
ATOM   1778  CD  GLU A 230      19.922  34.468  14.499  1.00 26.99           C  
ATOM   1779  OE1 GLU A 230      20.472  33.378  14.188  1.00 26.24           O  
ATOM   1780  OE2 GLU A 230      19.219  35.113  13.691  1.00 29.16           O  
ATOM   1781  N   VAL A 231      21.788  32.484  19.298  1.00 22.18           N  
ATOM   1782  CA  VAL A 231      22.757  31.614  19.957  1.00 23.47           C  
ATOM   1783  C   VAL A 231      22.086  30.329  20.414  1.00 22.67           C  
ATOM   1784  O   VAL A 231      22.627  29.229  20.239  1.00 24.67           O  
ATOM   1785  CB  VAL A 231      23.429  32.348  21.130  1.00 25.58           C  
ATOM   1786  CG1 VAL A 231      24.221  31.369  21.987  1.00 30.04           C  
ATOM   1787  CG2 VAL A 231      24.324  33.448  20.598  1.00 25.95           C  
ATOM   1788  N   VAL A 232      20.900  30.447  21.004  1.00 26.04           N  
ATOM   1789  CA  VAL A 232      20.203  29.262  21.490  1.00 29.08           C  
ATOM   1790  C   VAL A 232      19.864  28.330  20.336  1.00 32.36           C  
ATOM   1791  O   VAL A 232      20.071  27.110  20.411  1.00 32.51           O  
ATOM   1792  CB  VAL A 232      18.943  29.674  22.266  1.00 31.11           C  
ATOM   1793  CG1 VAL A 232      18.035  28.488  22.379  1.00 36.37           C  
ATOM   1794  CG2 VAL A 232      19.331  30.233  23.627  1.00 32.64           C  
ATOM   1795  N   TYR A 233      19.338  28.890  19.248  1.00 27.68           N  
ATOM   1796  CA  TYR A 233      18.943  28.058  18.118  1.00 27.45           C  
ATOM   1797  C   TYR A 233      20.150  27.394  17.470  1.00 31.31           C  
ATOM   1798  O   TYR A 233      20.068  26.240  17.031  1.00 34.25           O  
ATOM   1799  CB  TYR A 233      18.165  28.896  17.105  1.00 28.70           C  
ATOM   1800  CG  TYR A 233      17.617  28.081  15.965  1.00 30.29           C  
ATOM   1801  CD1 TYR A 233      16.679  27.079  16.195  1.00 33.35           C  
ATOM   1802  CD2 TYR A 233      18.042  28.294  14.666  1.00 30.08           C  
ATOM   1803  CE1 TYR A 233      16.178  26.323  15.155  1.00 32.99           C  
ATOM   1804  CE2 TYR A 233      17.544  27.546  13.619  1.00 31.87           C  
ATOM   1805  CZ  TYR A 233      16.614  26.558  13.869  1.00 35.00           C  
ATOM   1806  OH  TYR A 233      16.120  25.807  12.825  1.00 38.62           O  
ATOM   1807  N   GLY A 234      21.288  28.089  17.432  1.00 29.59           N  
ATOM   1808  CA  GLY A 234      22.481  27.538  16.813  1.00 31.60           C  
ATOM   1809  C   GLY A 234      23.140  26.429  17.606  1.00 37.26           C  
ATOM   1810  O   GLY A 234      23.930  25.664  17.040  1.00 40.74           O  
ATOM   1811  N   LYS A 235      22.834  26.316  18.894  1.00 35.04           N  
ATOM   1812  CA  LYS A 235      23.435  25.280  19.727  1.00 45.59           C  
ATOM   1813  C   LYS A 235      22.424  24.194  20.075  1.00 52.49           C  
ATOM   1814  O   LYS A 235      22.799  23.051  20.338  1.00 53.59           O  
ATOM   1815  CB  LYS A 235      24.016  25.879  21.009  1.00 48.30           C  
ATOM   1816  CG  LYS A 235      23.013  26.037  22.134  1.00 52.81           C  
ATOM   1817  CD  LYS A 235      23.695  26.459  23.427  1.00 56.48           C  
ATOM   1818  CE  LYS A 235      24.268  27.862  23.324  1.00 57.97           C  
ATOM   1819  NZ  LYS A 235      24.155  28.597  24.616  1.00 61.59           N  
TER    1820      LYS A 235                                                      
HETATM 1821  C1  RET A 301       4.242  55.393  34.036  1.00 16.84           C  
HETATM 1822  C2  RET A 301       3.475  56.268  35.029  1.00 15.21           C  
HETATM 1823  C3  RET A 301       2.569  55.411  35.904  1.00 17.48           C  
HETATM 1824  C4  RET A 301       3.382  54.453  36.743  1.00 19.42           C  
HETATM 1825  C5  RET A 301       4.416  53.727  35.919  1.00 17.73           C  
HETATM 1826  C6  RET A 301       4.700  54.058  34.653  1.00 16.37           C  
HETATM 1827  C7  RET A 301       5.652  53.145  33.900  1.00 17.94           C  
HETATM 1828  C8  RET A 301       5.934  53.240  32.577  1.00 18.68           C  
HETATM 1829  C9  RET A 301       6.868  52.324  31.852  1.00 15.80           C  
HETATM 1830  C10 RET A 301       7.134  52.622  30.562  1.00 17.96           C  
HETATM 1831  C11 RET A 301       8.002  51.858  29.621  1.00 18.57           C  
HETATM 1832  C12 RET A 301       8.202  52.388  28.396  1.00 17.84           C  
HETATM 1833  C13 RET A 301       9.015  51.674  27.363  1.00 16.40           C  
HETATM 1834  C14 RET A 301       8.947  52.180  26.108  1.00 18.30           C  
HETATM 1835  C15 RET A 301       9.658  51.581  24.939  1.00 19.55           C  
HETATM 1836  C16 RET A 301       5.392  56.232  33.507  1.00 15.43           C  
HETATM 1837  C17 RET A 301       3.315  55.151  32.874  1.00 17.87           C  
HETATM 1838  C18 RET A 301       4.998  52.538  36.642  1.00 18.68           C  
HETATM 1839  C19 RET A 301       7.449  51.141  32.578  1.00 15.49           C  
HETATM 1840  C20 RET A 301       9.840  50.470  27.753  1.00 16.97           C  
HETATM 1841  C1  OLB A 302       0.127  64.007  18.702  1.00 62.53           C  
HETATM 1842  C2  OLB A 302      -0.397  63.129  17.588  1.00 60.79           C  
HETATM 1843  C3  OLB A 302      -0.883  61.793  18.102  1.00 58.87           C  
HETATM 1844  C4  OLB A 302      -0.296  60.622  17.346  1.00 56.13           C  
HETATM 1845  C5  OLB A 302       0.599  59.790  18.234  1.00 53.37           C  
HETATM 1846  O19 OLB A 302       0.995  63.637  19.467  1.00 63.93           O  
HETATM 1847  O20 OLB A 302      -0.443  65.212  18.778  1.00 62.65           O  
HETATM 1848  C21 OLB A 302       0.377  66.218  19.326  1.00 62.23           C  
HETATM 1849  C22 OLB A 302      -0.496  67.307  19.916  1.00 61.59           C  
HETATM 1850  O23 OLB A 302       0.066  68.572  19.645  1.00 59.19           O  
HETATM 1851  C24 OLB A 302      -1.891  67.236  19.332  1.00 62.90           C  
HETATM 1852  O25 OLB A 302      -2.824  67.230  20.392  1.00 62.52           O  
HETATM 1853  C6  OLB A 302       1.299  58.680  17.486  1.00 50.58           C  
HETATM 1854  C7  OLB A 302       0.910  57.338  18.048  1.00 50.42           C  
HETATM 1855  C8  OLB A 302       2.086  56.420  18.297  1.00 49.38           C  
HETATM 1856  C9  OLB A 302       2.473  55.652  17.052  1.00 48.37           C  
HETATM 1857  C10 OLB A 302       1.845  54.511  16.706  1.00 49.10           C  
HETATM 1858  C11 OLB A 302       0.734  53.945  17.557  1.00 52.95           C  
HETATM 1859  C12 OLB A 302       0.425  52.513  17.192  1.00 57.42           C  
HETATM 1860  C13 OLB A 302       0.228  52.312  15.707  1.00 60.14           C  
HETATM 1861  C14 OLB A 302      -0.964  51.429  15.406  1.00 62.05           C  
HETATM 1862  C15 OLB A 302      -1.079  50.246  16.346  1.00 63.02           C  
HETATM 1863  C16 OLB A 302      -0.008  49.202  16.117  1.00 63.47           C  
HETATM 1864  C17 OLB A 302      -0.062  48.624  14.721  1.00 63.10           C  
HETATM 1865  C18 OLB A 302      -1.401  47.990  14.415  1.00 62.09           C  
HETATM 1866  C1  OLB A 303      19.568  68.574  29.933  1.00 73.03           C  
HETATM 1867  C2  OLB A 303      19.976  67.658  31.065  1.00 69.19           C  
HETATM 1868  C3  OLB A 303      19.216  66.349  31.030  1.00 65.59           C  
HETATM 1869  C4  OLB A 303      20.099  65.148  31.291  1.00 61.25           C  
HETATM 1870  C5  OLB A 303      19.315  63.853  31.280  1.00 57.01           C  
HETATM 1871  O19 OLB A 303      19.179  68.152  28.867  1.00 73.83           O  
HETATM 1872  O20 OLB A 303      19.657  69.878  30.190  1.00 76.19           O  
HETATM 1873  C21 OLB A 303      18.788  70.658  29.402  1.00 78.18           C  
HETATM 1874  C22 OLB A 303      18.258  71.806  30.232  1.00 79.97           C  
HETATM 1875  O23 OLB A 303      16.870  71.935  30.029  1.00 79.18           O  
HETATM 1876  C24 OLB A 303      18.538  71.541  31.695  1.00 82.11           C  
HETATM 1877  O25 OLB A 303      17.903  72.541  32.458  1.00 82.72           O  
HETATM 1878  C6  OLB A 303      20.208  62.632  31.309  1.00 54.66           C  
HETATM 1879  C7  OLB A 303      20.121  61.884  32.621  1.00 52.44           C  
HETATM 1880  C8  OLB A 303      19.849  60.409  32.425  1.00 50.55           C  
HETATM 1881  C9  OLB A 303      18.456  60.024  32.872  1.00 47.36           C  
HETATM 1882  C10 OLB A 303      17.923  58.821  32.565  1.00 46.52           C  
HETATM 1883  C11 OLB A 303      18.691  57.792  31.762  1.00 44.83           C  
HETATM 1884  C12 OLB A 303      19.479  56.853  32.645  1.00 45.58           C  
HETATM 1885  C13 OLB A 303      19.827  55.547  31.968  1.00 45.82           C  
HETATM 1886  C14 OLB A 303      20.065  54.444  32.977  1.00 44.65           C  
HETATM 1887  C15 OLB A 303      20.680  53.209  32.359  1.00 45.76           C  
HETATM 1888  C16 OLB A 303      20.531  51.972  33.217  1.00 46.22           C  
HETATM 1889  C17 OLB A 303      21.461  50.868  32.762  1.00 48.04           C  
HETATM 1890  C18 OLB A 303      21.012  49.491  33.198  1.00 50.59           C  
HETATM 1891  C1  OLB A 304       3.130  33.056  23.212  1.00 68.49           C  
HETATM 1892  C2  OLB A 304       2.377  34.277  23.688  1.00 66.86           C  
HETATM 1893  C3  OLB A 304       1.026  34.386  23.019  1.00 64.50           C  
HETATM 1894  C4  OLB A 304       0.778  35.772  22.472  1.00 61.66           C  
HETATM 1895  C5  OLB A 304       0.543  36.790  23.565  1.00 59.24           C  
HETATM 1896  O19 OLB A 304       3.031  32.629  22.079  1.00 71.57           O  
HETATM 1897  O20 OLB A 304       3.917  32.495  24.129  1.00 67.10           O  
HETATM 1898  C21 OLB A 304       3.396  31.298  24.652  1.00 68.02           C  
HETATM 1899  C22 OLB A 304       4.514  30.552  25.341  1.00 66.81           C  
HETATM 1900  O23 OLB A 304       3.989  29.843  26.438  1.00 64.58           O  
HETATM 1901  C24 OLB A 304       5.133  29.581  24.360  1.00 67.84           C  
HETATM 1902  O25 OLB A 304       6.030  30.290  23.534  1.00 68.92           O  
HETATM 1903  C6  OLB A 304      -0.086  38.053  23.022  1.00 57.09           C  
HETATM 1904  C7  OLB A 304       0.102  39.236  23.945  1.00 56.69           C  
HETATM 1905  C8  OLB A 304      -0.128  40.552  23.235  1.00 57.69           C  
HETATM 1906  C9  OLB A 304       1.113  41.022  22.504  1.00 57.83           C  
HETATM 1907  C10 OLB A 304       1.084  42.075  21.657  1.00 55.41           C  
HETATM 1908  C11 OLB A 304      -0.190  42.850  21.396  1.00 53.71           C  
HETATM 1909  C12 OLB A 304      -0.392  43.964  22.399  1.00 52.80           C  
HETATM 1910  C13 OLB A 304      -1.337  45.040  21.913  1.00 50.18           C  
HETATM 1911  C14 OLB A 304      -2.094  45.685  23.054  1.00 48.76           C  
HETATM 1912  C15 OLB A 304      -3.032  46.769  22.574  1.00 49.47           C  
HETATM 1913  C16 OLB A 304      -3.789  47.426  23.704  1.00 50.69           C  
HETATM 1914  C17 OLB A 304      -4.741  48.488  23.197  1.00 53.40           C  
HETATM 1915  C18 OLB A 304      -5.378  49.276  24.320  1.00 54.48           C  
HETATM 1916  C1  D12 A 305      15.128  45.930  -2.574  1.00 54.67           C  
HETATM 1917  C2  D12 A 305      15.545  44.823  -1.629  1.00 55.20           C  
HETATM 1918  C3  D12 A 305      16.757  44.105  -2.180  1.00 54.56           C  
HETATM 1919  C4  D12 A 305      17.025  42.866  -1.354  1.00 53.94           C  
HETATM 1920  C5  D12 A 305      17.426  43.263   0.051  1.00 54.01           C  
HETATM 1921  C6  D12 A 305      17.124  42.131   1.011  1.00 54.99           C  
HETATM 1922  C7  D12 A 305      17.760  40.851   0.514  1.00 54.73           C  
HETATM 1923  C8  D12 A 305      16.875  39.676   0.872  1.00 54.62           C  
HETATM 1924  C9  D12 A 305      17.454  38.405   0.291  1.00 52.13           C  
HETATM 1925  C10 D12 A 305      17.298  37.269   1.278  1.00 50.40           C  
HETATM 1926  C11 D12 A 305      17.050  35.977   0.532  1.00 49.42           C  
HETATM 1927  C12 D12 A 305      17.851  34.871   1.181  1.00 49.21           C  
HETATM 1928  C1  D12 A 306       8.078  50.034  41.596  1.00 39.65           C  
HETATM 1929  C2  D12 A 306       8.224  51.379  40.922  1.00 36.07           C  
HETATM 1930  C3  D12 A 306       8.685  52.407  41.928  1.00 35.69           C  
HETATM 1931  C4  D12 A 306       8.715  53.784  41.309  1.00 33.79           C  
HETATM 1932  C5  D12 A 306       8.927  54.818  42.394  1.00 36.42           C  
HETATM 1933  C6  D12 A 306       9.203  56.172  41.784  1.00 35.67           C  
HETATM 1934  C7  D12 A 306       9.279  57.209  42.881  1.00 36.86           C  
HETATM 1935  C8  D12 A 306      10.044  58.431  42.425  1.00 37.54           C  
HETATM 1936  C9  D12 A 306       9.056  59.509  42.033  1.00 39.99           C  
HETATM 1937  C10 D12 A 306       9.492  60.854  42.578  1.00 46.05           C  
HETATM 1938  C11 D12 A 306       8.263  61.714  42.794  1.00 46.96           C  
HETATM 1939  C12 D12 A 306       8.634  63.010  43.484  1.00 47.37           C  
HETATM 1940  C01 C14 A 307      24.895  49.823  27.197  1.00 55.05           C  
HETATM 1941  C02 C14 A 307      24.673  49.419  28.639  1.00 53.80           C  
HETATM 1942  C03 C14 A 307      23.532  50.212  29.242  1.00 52.28           C  
HETATM 1943  C04 C14 A 307      24.054  51.298  30.162  1.00 51.32           C  
HETATM 1944  C05 C14 A 307      24.333  52.556  29.367  1.00 49.41           C  
HETATM 1945  C06 C14 A 307      23.685  53.752  30.030  1.00 46.63           C  
HETATM 1946  C07 C14 A 307      24.025  54.986  29.226  1.00 43.54           C  
HETATM 1947  C08 C14 A 307      23.247  56.181  29.727  1.00 44.38           C  
HETATM 1948  C09 C14 A 307      23.649  57.392  28.916  1.00 43.89           C  
HETATM 1949  C10 C14 A 307      23.364  58.664  29.685  1.00 42.63           C  
HETATM 1950  C11 C14 A 307      24.212  59.772  29.100  1.00 43.83           C  
HETATM 1951  C12 C14 A 307      23.546  61.115  29.307  1.00 45.79           C  
HETATM 1952  C13 C14 A 307      24.509  62.216  28.922  1.00 46.02           C  
HETATM 1953  C14 C14 A 307      23.841  63.563  29.095  1.00 46.60           C  
HETATM 1954  C27 R16 A 308       2.881  64.669  46.847  1.00 51.53           C  
HETATM 1955  C28 R16 A 308       3.814  63.805  46.027  1.00 51.07           C  
HETATM 1956  C29 R16 A 308       3.495  62.345  46.269  1.00 50.58           C  
HETATM 1957  C30 R16 A 308       4.669  61.496  45.828  1.00 47.02           C  
HETATM 1958  C31 R16 A 308       4.178  60.107  45.486  1.00 44.42           C  
HETATM 1959  C32 R16 A 308       5.326  59.239  45.014  1.00 41.71           C  
HETATM 1960  C33 R16 A 308       5.115  57.852  45.580  1.00 41.42           C  
HETATM 1961  C34 R16 A 308       6.080  56.870  44.958  1.00 41.38           C  
HETATM 1962  C35 R16 A 308       5.290  55.672  44.477  1.00 40.05           C  
HETATM 1963  C36 R16 A 308       5.857  54.407  45.076  1.00 40.04           C  
HETATM 1964  C37 R16 A 308       4.917  53.255  44.797  1.00 37.44           C  
HETATM 1965  C38 R16 A 308       5.605  51.965  45.174  1.00 38.21           C  
HETATM 1966  C39 R16 A 308       4.721  50.785  44.852  1.00 41.03           C  
HETATM 1967  C40 R16 A 308       5.476  49.521  45.196  1.00 42.31           C  
HETATM 1968  C41 R16 A 308       4.729  48.323  44.659  1.00 45.12           C  
HETATM 1969  C42 R16 A 308       5.118  47.095  45.452  1.00 47.84           C  
HETATM 1970  C1  D10 A 309       3.156  52.066  12.188  1.00 58.65           C  
HETATM 1971  C2  D10 A 309       2.713  50.768  12.827  1.00 57.36           C  
HETATM 1972  C3  D10 A 309       3.607  49.645  12.351  1.00 56.59           C  
HETATM 1973  C4  D10 A 309       3.066  48.314  12.829  1.00 54.70           C  
HETATM 1974  C5  D10 A 309       4.153  47.264  12.744  1.00 52.79           C  
HETATM 1975  C6  D10 A 309       4.730  47.228  11.346  1.00 51.86           C  
HETATM 1976  C7  D10 A 309       5.903  46.273  11.304  1.00 51.19           C  
HETATM 1977  C8  D10 A 309       5.405  44.847  11.398  1.00 50.97           C  
HETATM 1978  C9  D10 A 309       6.553  43.900  11.128  1.00 52.74           C  
HETATM 1979  C10 D10 A 309       6.020  42.496  10.950  1.00 55.08           C  
HETATM 1980  C1  D10 A 310      20.924  50.459  19.510  1.00 46.34           C  
HETATM 1981  C2  D10 A 310      21.307  51.878  19.868  1.00 47.50           C  
HETATM 1982  C3  D10 A 310      21.391  52.034  21.372  1.00 48.26           C  
HETATM 1983  C4  D10 A 310      21.705  53.478  21.695  1.00 49.85           C  
HETATM 1984  C5  D10 A 310      21.993  53.652  23.171  1.00 51.15           C  
HETATM 1985  C6  D10 A 310      22.104  55.134  23.456  1.00 52.09           C  
HETATM 1986  C7  D10 A 310      22.425  55.372  24.915  1.00 51.54           C  
HETATM 1987  C8  D10 A 310      22.194  56.834  25.238  1.00 51.78           C  
HETATM 1988  C9  D10 A 310      23.282  57.685  24.620  1.00 50.70           C  
HETATM 1989  C10 D10 A 310      22.949  59.151  24.802  1.00 49.95           C  
HETATM 1990  O   HOH A 401       8.489  34.693   7.270  1.00 47.92           O  
HETATM 1991  O   HOH A 402       4.347  62.108  30.551  1.00 40.08           O  
HETATM 1992  O   HOH A 403       6.444  61.242  31.692  1.00 28.55           O  
HETATM 1993  O   HOH A 404      -1.303  76.902  27.239  1.00 39.58           O  
HETATM 1994  O   HOH A 405      15.970  75.335  24.100  1.00 49.35           O  
HETATM 1995  O   HOH A 406       8.574  57.359  24.771  1.00 25.34           O  
HETATM 1996  O   HOH A 407      -4.212  73.706  31.120  1.00 44.98           O  
HETATM 1997  O   HOH A 408      10.655  37.635   6.350  1.00 36.57           O  
HETATM 1998  O   HOH A 409       4.820  66.215  29.196  1.00 30.48           O  
HETATM 1999  O   HOH A 410      14.544  73.677  28.131  1.00 42.72           O  
HETATM 2000  O   HOH A 411      -1.366  67.269  35.487  1.00 46.06           O  
HETATM 2001  O   HOH A 412       0.067  79.537  32.236  1.00 33.77           O  
HETATM 2002  O   HOH A 413       7.939  78.033  35.126  1.00 32.39           O  
HETATM 2003  O   HOH A 414      10.674  73.000  18.664  1.00 33.84           O  
HETATM 2004  O   HOH A 415      -9.559  61.856  37.699  1.00 61.57           O  
HETATM 2005  O   HOH A 416       6.412  66.388  21.556  1.00 24.29           O  
HETATM 2006  O   HOH A 417       9.557  54.574  22.639  1.00 29.39           O  
HETATM 2007  O   HOH A 418       8.101  71.677  34.660  1.00 24.38           O  
HETATM 2008  O   HOH A 419       7.445  57.362  22.184  1.00 27.57           O  
HETATM 2009  O   HOH A 420      -0.428  65.383  36.277  1.00 48.72           O  
HETATM 2010  O   HOH A 421      12.556  28.705  29.118  1.00 33.96           O  
HETATM 2011  O   HOH A 422     -12.491  65.751  46.268  1.00 40.17           O  
HETATM 2012  O   HOH A 423      13.553  26.434  20.921  1.00 59.77           O  
HETATM 2013  O   HOH A 424      -6.047  68.524  32.278  1.00 40.92           O  
HETATM 2014  O   HOH A 425       1.483  66.169  33.324  1.00 36.57           O  
HETATM 2015  O   HOH A 426      14.379  28.845  31.164  1.00 45.87           O  
HETATM 2016  O   HOH A 427       5.576  71.924  15.892  1.00 42.31           O  
HETATM 2017  O  AHOH A 428       7.699  63.325  33.084  0.80 20.62           O  
HETATM 2018  O  BHOH A 428       8.211  66.036  28.534  0.20  9.10           O  
HETATM 2019  O   HOH A 429       9.060  32.389  13.342  1.00 27.12           O  
HETATM 2020  O   HOH A 430       8.201  70.469  17.237  1.00 40.07           O  
HETATM 2021  O   HOH A 431      -6.656  66.136  41.953  1.00 36.67           O  
HETATM 2022  O   HOH A 432      11.335  61.162  24.713  1.00 19.09           O  
HETATM 2023  O   HOH A 433       7.112  21.723  38.631  1.00 64.41           O  
HETATM 2024  O   HOH A 434      20.891  30.761  14.900  1.00 29.61           O  
HETATM 2025  O   HOH A 435       3.818  73.356  39.302  1.00 33.78           O  
HETATM 2026  O   HOH A 436       9.997  69.551  13.980  1.00 31.62           O  
HETATM 2027  O   HOH A 437       8.746  60.046  25.322  1.00 22.83           O  
HETATM 2028  O   HOH A 438       3.648  77.597  32.654  1.00 26.41           O  
HETATM 2029  O   HOH A 439      10.071  75.739  28.503  1.00 26.69           O  
HETATM 2030  O   HOH A 440      20.929  31.140  28.988  1.00 31.66           O  
HETATM 2031  O   HOH A 441       6.076  78.440  37.852  1.00 50.12           O  
HETATM 2032  O   HOH A 442       2.385  68.007  23.579  1.00 22.70           O  
HETATM 2033  O   HOH A 443       8.262  77.146  23.849  1.00 59.66           O  
HETATM 2034  O   HOH A 444       9.840  29.448  16.564  1.00 44.15           O  
HETATM 2035  O   HOH A 445      12.775  76.351  28.561  1.00 40.69           O  
HETATM 2036  O   HOH A 446      11.562  72.297  28.516  1.00 20.99           O  
HETATM 2037  O   HOH A 447       7.783  76.267  20.071  1.00 47.95           O  
HETATM 2038  O   HOH A 448       6.309  70.519  12.173  1.00 49.76           O  
HETATM 2039  O   HOH A 449      -1.008  69.377  38.923  1.00 47.24           O  
HETATM 2040  O   HOH A 450      -5.736  69.202  29.499  1.00 47.02           O  
HETATM 2041  O   HOH A 451      10.927  33.415  16.591  1.00 26.13           O  
HETATM 2042  O   HOH A 452      12.716  46.827  27.415  1.00 18.53           O  
HETATM 2043  O   HOH A 453      25.161  28.962  18.993  1.00 36.42           O  
HETATM 2044  O   HOH A 454       3.106  67.767  32.177  1.00 26.78           O  
HETATM 2045  O   HOH A 455      21.042  29.028  31.952  1.00 40.27           O  
HETATM 2046  O   HOH A 456      -1.803  32.593  36.507  1.00 38.70           O  
HETATM 2047  O   HOH A 457      14.316  71.598  33.937  1.00 29.94           O  
HETATM 2048  O   HOH A 458      11.866  77.887  33.800  1.00 37.28           O  
HETATM 2049  O   HOH A 459      -2.517  28.084  28.142  1.00 48.73           O  
HETATM 2050  O   HOH A 460      15.921  30.255  19.624  1.00 38.05           O  
HETATM 2051  O   HOH A 461       7.931  58.815  32.313  1.00 28.10           O  
HETATM 2052  O   HOH A 462      12.639  25.118  22.543  1.00 61.90           O  
HETATM 2053  O   HOH A 463       5.319  78.726  34.779  1.00 33.13           O  
HETATM 2054  O   HOH A 464      -4.548  72.035  26.541  1.00 40.57           O  
HETATM 2055  O   HOH A 465       1.877  64.228  22.279  1.00 24.79           O  
HETATM 2056  O   HOH A 466      -7.966  67.187  36.496  1.00 41.20           O  
HETATM 2057  O   HOH A 467      -5.753  71.466  33.089  1.00 38.68           O  
HETATM 2058  O   HOH A 468      18.355  66.635  15.771  1.00 50.87           O  
HETATM 2059  O   HOH A 469      14.170  28.486   7.008  1.00 32.17           O  
HETATM 2060  O   HOH A 470      12.092  35.518  21.552  1.00 33.42           O  
HETATM 2061  O   HOH A 471      21.845  30.146  10.021  1.00 54.78           O  
HETATM 2062  O   HOH A 472      12.285  76.700  21.087  1.00 35.70           O  
HETATM 2063  O   HOH A 473       9.242  62.886  24.034  1.00 20.62           O  
HETATM 2064  O   HOH A 474      13.812  71.043  30.630  1.00 27.61           O  
HETATM 2065  O   HOH A 475      -2.913  74.222  38.194  1.00 33.73           O  
HETATM 2066  O   HOH A 476       8.750  24.531  40.582  1.00 56.48           O  
HETATM 2067  O   HOH A 477      -4.099  29.045  30.411  1.00 43.09           O  
HETATM 2068  O   HOH A 478      10.426  36.774   4.268  1.00 60.18           O  
HETATM 2069  O   HOH A 479      -6.112  35.489  33.707  1.00 59.87           O  
HETATM 2070  O   HOH A 480      16.769  32.758   4.370  1.00 39.07           O  
HETATM 2071  O   HOH A 481       2.332  33.939  42.217  1.00 42.91           O  
HETATM 2072  O   HOH A 482      19.345  26.894  34.616  1.00 52.20           O  
HETATM 2073  O   HOH A 483      11.785  72.441  40.497  1.00 53.27           O  
HETATM 2074  O   HOH A 484       2.994  25.743  32.587  1.00 64.70           O  
HETATM 2075  O   HOH A 485      -6.047  72.294  30.283  1.00 58.05           O  
HETATM 2076  O   HOH A 486       9.606  74.767  20.450  1.00 58.85           O  
HETATM 2077  O   HOH A 487      13.340  31.240  32.206  1.00 47.87           O  
HETATM 2078  O   HOH A 488      17.705  31.102   6.212  1.00 38.76           O  
HETATM 2079  O   HOH A 489       1.990  77.567  19.196  1.00 58.41           O  
HETATM 2080  O   HOH A 490      14.587  29.842  21.885  1.00 67.03           O  
HETATM 2081  O   HOH A 491      12.979  30.447   4.196  1.00 49.63           O  
HETATM 2082  O   HOH A 492      16.279  21.725  29.015  1.00 53.10           O  
HETATM 2083  O   HOH A 493      23.069  35.296   7.825  1.00 63.14           O  
HETATM 2084  O   HOH A 494       3.260  64.748  30.631  1.00 44.25           O  
HETATM 2085  O   HOH A 495       3.660  66.215  21.557  1.00 27.75           O  
HETATM 2086  O   HOH A 496       8.577  69.510  11.547  1.00 43.18           O  
HETATM 2087  O   HOH A 497      -1.262  78.316  43.151  1.00 53.70           O  
CONECT 1690 1835                                                                
CONECT 1821 1822 1826 1836 1837                                                 
CONECT 1822 1821 1823                                                           
CONECT 1823 1822 1824                                                           
CONECT 1824 1823 1825                                                           
CONECT 1825 1824 1826 1838                                                      
CONECT 1826 1821 1825 1827                                                      
CONECT 1827 1826 1828                                                           
CONECT 1828 1827 1829                                                           
CONECT 1829 1828 1830 1839                                                      
CONECT 1830 1829 1831                                                           
CONECT 1831 1830 1832                                                           
CONECT 1832 1831 1833                                                           
CONECT 1833 1832 1834 1840                                                      
CONECT 1834 1833 1835                                                           
CONECT 1835 1690 1834                                                           
CONECT 1836 1821                                                                
CONECT 1837 1821                                                                
CONECT 1838 1825                                                                
CONECT 1839 1829                                                                
CONECT 1840 1833                                                                
CONECT 1841 1842 1846 1847                                                      
CONECT 1842 1841 1843                                                           
CONECT 1843 1842 1844                                                           
CONECT 1844 1843 1845                                                           
CONECT 1845 1844 1853                                                           
CONECT 1846 1841                                                                
CONECT 1847 1841 1848                                                           
CONECT 1848 1847 1849                                                           
CONECT 1849 1848 1850 1851                                                      
CONECT 1850 1849                                                                
CONECT 1851 1849 1852                                                           
CONECT 1852 1851                                                                
CONECT 1853 1845 1854                                                           
CONECT 1854 1853 1855                                                           
CONECT 1855 1854 1856                                                           
CONECT 1856 1855 1857                                                           
CONECT 1857 1856 1858                                                           
CONECT 1858 1857 1859                                                           
CONECT 1859 1858 1860                                                           
CONECT 1860 1859 1861                                                           
CONECT 1861 1860 1862                                                           
CONECT 1862 1861 1863                                                           
CONECT 1863 1862 1864                                                           
CONECT 1864 1863 1865                                                           
CONECT 1865 1864                                                                
CONECT 1866 1867 1871 1872                                                      
CONECT 1867 1866 1868                                                           
CONECT 1868 1867 1869                                                           
CONECT 1869 1868 1870                                                           
CONECT 1870 1869 1878                                                           
CONECT 1871 1866                                                                
CONECT 1872 1866 1873                                                           
CONECT 1873 1872 1874                                                           
CONECT 1874 1873 1875 1876                                                      
CONECT 1875 1874                                                                
CONECT 1876 1874 1877                                                           
CONECT 1877 1876                                                                
CONECT 1878 1870 1879                                                           
CONECT 1879 1878 1880                                                           
CONECT 1880 1879 1881                                                           
CONECT 1881 1880 1882                                                           
CONECT 1882 1881 1883                                                           
CONECT 1883 1882 1884                                                           
CONECT 1884 1883 1885                                                           
CONECT 1885 1884 1886                                                           
CONECT 1886 1885 1887                                                           
CONECT 1887 1886 1888                                                           
CONECT 1888 1887 1889                                                           
CONECT 1889 1888 1890                                                           
CONECT 1890 1889                                                                
CONECT 1891 1892 1896 1897                                                      
CONECT 1892 1891 1893                                                           
CONECT 1893 1892 1894                                                           
CONECT 1894 1893 1895                                                           
CONECT 1895 1894 1903                                                           
CONECT 1896 1891                                                                
CONECT 1897 1891 1898                                                           
CONECT 1898 1897 1899                                                           
CONECT 1899 1898 1900 1901                                                      
CONECT 1900 1899                                                                
CONECT 1901 1899 1902                                                           
CONECT 1902 1901                                                                
CONECT 1903 1895 1904                                                           
CONECT 1904 1903 1905                                                           
CONECT 1905 1904 1906                                                           
CONECT 1906 1905 1907                                                           
CONECT 1907 1906 1908                                                           
CONECT 1908 1907 1909                                                           
CONECT 1909 1908 1910                                                           
CONECT 1910 1909 1911                                                           
CONECT 1911 1910 1912                                                           
CONECT 1912 1911 1913                                                           
CONECT 1913 1912 1914                                                           
CONECT 1914 1913 1915                                                           
CONECT 1915 1914                                                                
CONECT 1916 1917                                                                
CONECT 1917 1916 1918                                                           
CONECT 1918 1917 1919                                                           
CONECT 1919 1918 1920                                                           
CONECT 1920 1919 1921                                                           
CONECT 1921 1920 1922                                                           
CONECT 1922 1921 1923                                                           
CONECT 1923 1922 1924                                                           
CONECT 1924 1923 1925                                                           
CONECT 1925 1924 1926                                                           
CONECT 1926 1925 1927                                                           
CONECT 1927 1926                                                                
CONECT 1928 1929                                                                
CONECT 1929 1928 1930                                                           
CONECT 1930 1929 1931                                                           
CONECT 1931 1930 1932                                                           
CONECT 1932 1931 1933                                                           
CONECT 1933 1932 1934                                                           
CONECT 1934 1933 1935                                                           
CONECT 1935 1934 1936                                                           
CONECT 1936 1935 1937                                                           
CONECT 1937 1936 1938                                                           
CONECT 1938 1937 1939                                                           
CONECT 1939 1938                                                                
CONECT 1940 1941                                                                
CONECT 1941 1940 1942                                                           
CONECT 1942 1941 1943                                                           
CONECT 1943 1942 1944                                                           
CONECT 1944 1943 1945                                                           
CONECT 1945 1944 1946                                                           
CONECT 1946 1945 1947                                                           
CONECT 1947 1946 1948                                                           
CONECT 1948 1947 1949                                                           
CONECT 1949 1948 1950                                                           
CONECT 1950 1949 1951                                                           
CONECT 1951 1950 1952                                                           
CONECT 1952 1951 1953                                                           
CONECT 1953 1952                                                                
CONECT 1954 1955                                                                
CONECT 1955 1954 1956                                                           
CONECT 1956 1955 1957                                                           
CONECT 1957 1956 1958                                                           
CONECT 1958 1957 1959                                                           
CONECT 1959 1958 1960                                                           
CONECT 1960 1959 1961                                                           
CONECT 1961 1960 1962                                                           
CONECT 1962 1961 1963                                                           
CONECT 1963 1962 1964                                                           
CONECT 1964 1963 1965                                                           
CONECT 1965 1964 1966                                                           
CONECT 1966 1965 1967                                                           
CONECT 1967 1966 1968                                                           
CONECT 1968 1967 1969                                                           
CONECT 1969 1968                                                                
CONECT 1970 1971                                                                
CONECT 1971 1970 1972                                                           
CONECT 1972 1971 1973                                                           
CONECT 1973 1972 1974                                                           
CONECT 1974 1973 1975                                                           
CONECT 1975 1974 1976                                                           
CONECT 1976 1975 1977                                                           
CONECT 1977 1976 1978                                                           
CONECT 1978 1977 1979                                                           
CONECT 1979 1978                                                                
CONECT 1980 1981                                                                
CONECT 1981 1980 1982                                                           
CONECT 1982 1981 1983                                                           
CONECT 1983 1982 1984                                                           
CONECT 1984 1983 1985                                                           
CONECT 1985 1984 1986                                                           
CONECT 1986 1985 1987                                                           
CONECT 1987 1986 1988                                                           
CONECT 1988 1987 1989                                                           
CONECT 1989 1988                                                                
MASTER      322    0   10   12    2    0   13    6 2076    1  170   19          
END                                                                             
