HEADER    PROTON TRANSPORT                        10-JUL-15   5AX1              
TITLE     CRYSTAL STRUCTURE OF THE CELL-FREE SYNTHESIZED MEMBRANE PROTEIN,      
TITLE    2 ACETABULARIA RHODOPSIN I, AT 1.80 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 5AX1    1       REMARK                                   
REVDAT   3   26-FEB-20 5AX1    1       REMARK                                   
REVDAT   2   18-NOV-15 5AX1    1       JRNL                                     
REVDAT   1   26-AUG-15 5AX1    0                                                
SPRSDE     26-AUG-15 5AX1      3WTA                                             
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.    1.80 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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.83                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 26595                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.204                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.170                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1108                            
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 34.8328 -  3.6043    1.00     3236   143  0.1845 0.2146        
REMARK   3     2  3.6043 -  2.8613    1.00     3206   138  0.1713 0.1714        
REMARK   3     3  2.8613 -  2.4997    1.00     3200   139  0.1460 0.1617        
REMARK   3     4  2.4997 -  2.2712    1.00     3196   139  0.1479 0.1955        
REMARK   3     5  2.2712 -  2.1085    1.00     3192   139  0.1534 0.2036        
REMARK   3     6  2.1085 -  1.9842    1.00     3179   137  0.1827 0.2403        
REMARK   3     7  1.9842 -  1.8848    1.00     3182   139  0.2091 0.2638        
REMARK   3     8  1.8848 -  1.8028    0.97     3096   134  0.2637 0.3052        
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)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.360           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.62                          
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      :  0.007           2004                                  
REMARK   3   ANGLE     :  1.073           2698                                  
REMARK   3   CHIRALITY :  0.041            310                                  
REMARK   3   PLANARITY :  0.005            315                                  
REMARK   3   DIHEDRAL  : 14.996            737                                  
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):    6.165   50.283   25.743              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1792 T22:   0.1625                                     
REMARK   3      T33:   0.1452 T12:  -0.0031                                     
REMARK   3      T13:   0.0287 T23:   0.0127                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7099 L22:   2.1862                                     
REMARK   3      L33:   1.5633 L12:  -0.3383                                     
REMARK   3      L13:  -0.4114 L23:   0.2723                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0352 S12:   0.0603 S13:   0.0151                       
REMARK   3      S21:  -0.0241 S22:  -0.0114 S23:   0.0885                       
REMARK   3      S31:  -0.1293 S32:  -0.1787 S33:  -0.0211                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 168 THROUGH 201 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   13.141   48.539   33.797              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2936 T22:   0.1605                                     
REMARK   3      T33:   0.1284 T12:  -0.0105                                     
REMARK   3      T13:   0.0616 T23:   0.0001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8559 L22:   1.5982                                     
REMARK   3      L33:   1.5677 L12:  -0.1864                                     
REMARK   3      L13:   0.1903 L23:  -0.9720                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0041 S12:   0.1387 S13:  -0.3296                       
REMARK   3      S21:   0.0661 S22:  -0.0857 S23:  -0.0640                       
REMARK   3      S31:   0.3396 S32:   0.0239 S33:   0.0462                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 202 THROUGH 236 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   16.849   47.435   23.592              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1533 T22:   0.1409                                     
REMARK   3      T33:   0.1157 T12:  -0.0132                                     
REMARK   3      T13:   0.0312 T23:   0.0226                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6357 L22:   6.9298                                     
REMARK   3      L33:   3.0057 L12:  -1.8501                                     
REMARK   3      L13:  -1.1335 L23:   3.0471                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0246 S12:   0.0059 S13:  -0.0072                       
REMARK   3      S21:   0.0656 S22:   0.1232 S23:  -0.0549                       
REMARK   3      S31:  -0.0141 S32:   0.0351 S33:  -0.1049                       
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 5AX1 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_1300000113.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-OCT-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
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 MX325HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26610                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 34.830                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08568                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.5500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.87                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.910                              
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   (%): 57.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG400, 0.1M TRIS, 0.1M NACL, 20MM   
REMARK 280  MGCL2, PH 8.0, LIPIDIC CUBIC PHASE, 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: 1770 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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     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    ASN A 106       43.08   -107.67                                   
REMARK 500    LYS A 218      -79.81   -115.88                                   
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 C14 A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue D10 A 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue R16 A 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue D12 A 308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue D12 A 309                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5AWZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5AX0   RELATED DB: PDB                                   
DBREF  5AX1 A    1   237  UNP    G3CEP6   G3CEP6_ACEAT     1    237             
SEQADV 5AX1 GLY A   -6  UNP  G3CEP6              EXPRESSION TAG                 
SEQADV 5AX1 SER A   -5  UNP  G3CEP6              EXPRESSION TAG                 
SEQADV 5AX1 SER A   -4  UNP  G3CEP6              EXPRESSION TAG                 
SEQADV 5AX1 GLY A   -3  UNP  G3CEP6              EXPRESSION TAG                 
SEQADV 5AX1 SER A   -2  UNP  G3CEP6              EXPRESSION TAG                 
SEQADV 5AX1 SER A   -1  UNP  G3CEP6              EXPRESSION TAG                 
SEQADV 5AX1 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    C14  A 304      14                                                       
HET    D10  A 305      10                                                       
HET    D10  A 306      10                                                       
HET    R16  A 307      16                                                       
HET    D12  A 308      12                                                       
HET    D12  A 309      12                                                       
HETNAM     RET RETINAL                                                          
HETNAM     OLB (2S)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE                   
HETNAM     C14 TETRADECANE                                                      
HETNAM     D10 DECANE                                                           
HETNAM     R16 HEXADECANE                                                       
HETNAM     D12 DODECANE                                                         
FORMUL   2  RET    C20 H28 O                                                    
FORMUL   3  OLB    2(C21 H40 O4)                                                
FORMUL   5  C14    C14 H30                                                      
FORMUL   6  D10    2(C10 H22)                                                   
FORMUL   8  R16    C16 H34                                                      
FORMUL   9  D12    2(C12 H26)                                                   
FORMUL  11  HOH   *86(H2 O)                                                     
HELIX    1 AA1 THR A    9  VAL A   34  1                                  26    
HELIX    2 AA2 GLN A   35  ARG A   37  5                                   3    
HELIX    3 AA3 PRO A   38  GLY A   66  1                                  29    
HELIX    4 AA4 GLY A   67  ASN A   69  5                                   3    
HELIX    5 AA5 THR A   75  GLU A   79  5                                   5    
HELIX    6 AA6 TYR A   84  LEU A  103  1                                  20    
HELIX    7 AA7 PRO A  108  THR A  132  1                                  25    
HELIX    8 AA8 TYR A  136  LYS A  161  1                                  26    
HELIX    9 AA9 GLU A  162  GLN A  165  5                                   4    
HELIX   10 AB1 HIS A  167  GLU A  169  5                                   3    
HELIX   11 AB2 TYR A  170  GLY A  195  1                                  26    
HELIX   12 AB3 GLY A  202  LYS A  218  1                                  17    
HELIX   13 AB4 LYS A  218  LEU A  236  1                                  19    
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        -6.01                     
SITE     1 AC1  6 TRP A  90  GLY A 144  TRP A 185  TYR A 188                    
SITE     2 AC1  6 ASP A 214  LYS A 218                                          
SITE     1 AC2  8 THR A  57  ALA A  58  ASN A  65  LYS A  70                    
SITE     2 AC2  8 TYR A  84  ALA A  85  ILE A  88  HOH A 469                    
SITE     1 AC3  4 LEU A  11  VAL A 205  ILE A 208  D12 A 308                    
SITE     1 AC4  2 TRP A 138  PHE A 141                                          
SITE     1 AC5  2 LEU A 216  D12 A 308                                          
SITE     1 AC6  2 CYS A 145  GLY A 193                                          
SITE     1 AC7  2 OLB A 303  D10 A 306                                          
SITE     1 AC8  2 VAL A  91  ILE A 120                                          
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      10.111  76.361  40.806  1.00 45.68           N  
ATOM      2  CA  SER A   2       8.976  75.461  40.624  1.00 43.74           C  
ATOM      3  C   SER A   2       8.495  75.448  39.176  1.00 36.55           C  
ATOM      4  O   SER A   2       8.515  76.473  38.504  1.00 37.88           O  
ATOM      5  CB  SER A   2       7.827  75.866  41.541  1.00 46.11           C  
ATOM      6  OG  SER A   2       7.394  77.179  41.225  1.00 48.10           O  
ATOM      7  N   ASN A   3       8.043  74.285  38.720  1.00 33.84           N  
ATOM      8  CA  ASN A   3       7.578  74.098  37.348  1.00 31.47           C  
ATOM      9  C   ASN A   3       8.531  74.689  36.299  1.00 30.71           C  
ATOM     10  O   ASN A   3       8.102  75.446  35.419  1.00 27.67           O  
ATOM     11  CB  ASN A   3       6.184  74.710  37.177  1.00 31.06           C  
ATOM     12  CG  ASN A   3       5.485  74.213  35.927  1.00 30.03           C  
ATOM     13  OD1 ASN A   3       5.752  73.103  35.463  1.00 27.25           O  
ATOM     14  ND2 ASN A   3       4.602  75.039  35.363  1.00 29.71           N  
ATOM     15  N   PRO A   4       9.830  74.350  36.389  1.00 31.09           N  
ATOM     16  CA  PRO A   4      10.795  74.964  35.467  1.00 29.20           C  
ATOM     17  C   PRO A   4      10.579  74.510  34.024  1.00 27.66           C  
ATOM     18  O   PRO A   4      10.170  73.373  33.816  1.00 26.97           O  
ATOM     19  CB  PRO A   4      12.140  74.467  35.994  1.00 29.88           C  
ATOM     20  CG  PRO A   4      11.810  73.105  36.568  1.00 30.66           C  
ATOM     21  CD  PRO A   4      10.447  73.274  37.195  1.00 30.78           C  
ATOM     22  N   ASN A   5      10.836  75.394  33.063  1.00 29.18           N  
ATOM     23  CA  ASN A   5      10.828  75.021  31.643  1.00 28.36           C  
ATOM     24  C   ASN A   5       9.661  74.110  31.256  1.00 24.66           C  
ATOM     25  O   ASN A   5       9.877  72.982  30.794  1.00 25.54           O  
ATOM     26  CB  ASN A   5      12.159  74.348  31.306  1.00 29.07           C  
ATOM     27  CG  ASN A   5      13.349  75.208  31.700  1.00 35.10           C  
ATOM     28  OD1 ASN A   5      13.430  76.371  31.320  1.00 34.60           O  
ATOM     29  ND2 ASN A   5      14.261  74.647  32.485  1.00 37.59           N  
ATOM     30  N   PRO A   6       8.419  74.586  31.462  1.00 24.27           N  
ATOM     31  CA  PRO A   6       7.260  73.685  31.366  1.00 23.43           C  
ATOM     32  C   PRO A   6       6.729  73.482  29.944  1.00 25.57           C  
ATOM     33  O   PRO A   6       5.645  72.912  29.780  1.00 23.77           O  
ATOM     34  CB  PRO A   6       6.219  74.384  32.248  1.00 24.20           C  
ATOM     35  CG  PRO A   6       6.532  75.861  32.062  1.00 26.75           C  
ATOM     36  CD  PRO A   6       8.030  75.949  31.889  1.00 28.02           C  
ATOM     37  N   PHE A   7       7.490  73.918  28.940  1.00 23.51           N  
ATOM     38  CA  PHE A   7       7.132  73.709  27.538  1.00 24.61           C  
ATOM     39  C   PHE A   7       8.312  73.220  26.714  1.00 26.14           C  
ATOM     40  O   PHE A   7       9.447  73.642  26.924  1.00 26.17           O  
ATOM     41  CB  PHE A   7       6.587  75.001  26.914  1.00 24.69           C  
ATOM     42  CG  PHE A   7       5.311  75.461  27.525  1.00 25.83           C  
ATOM     43  CD1 PHE A   7       4.098  74.977  27.068  1.00 25.80           C  
ATOM     44  CD2 PHE A   7       5.318  76.372  28.581  1.00 27.26           C  
ATOM     45  CE1 PHE A   7       2.907  75.390  27.651  1.00 27.68           C  
ATOM     46  CE2 PHE A   7       4.128  76.788  29.168  1.00 29.07           C  
ATOM     47  CZ  PHE A   7       2.923  76.297  28.703  1.00 28.00           C  
ATOM     48  N   GLN A   8       8.024  72.340  25.763  1.00 22.36           N  
ATOM     49  CA  GLN A   8       9.043  71.833  24.842  1.00 22.19           C  
ATOM     50  C   GLN A   8       9.679  72.972  24.031  1.00 24.07           C  
ATOM     51  O   GLN A   8       8.985  73.872  23.552  1.00 26.06           O  
ATOM     52  CB  GLN A   8       8.422  70.781  23.924  1.00 23.26           C  
ATOM     53  CG  GLN A   8       9.381  70.172  22.906  1.00 22.62           C  
ATOM     54  CD  GLN A   8       8.758  69.014  22.161  1.00 21.60           C  
ATOM     55  OE1 GLN A   8       7.855  68.346  22.673  1.00 22.87           O  
ATOM     56  NE2 GLN A   8       9.222  68.780  20.931  1.00 20.65           N  
ATOM     57  N   THR A   9      11.002  72.960  23.916  1.00 25.10           N  
ATOM     58  CA  THR A   9      11.705  73.907  23.052  1.00 26.91           C  
ATOM     59  C   THR A   9      12.432  73.137  21.966  1.00 25.84           C  
ATOM     60  O   THR A   9      12.307  71.917  21.880  1.00 23.25           O  
ATOM     61  CB  THR A   9      12.745  74.749  23.804  1.00 29.03           C  
ATOM     62  OG1 THR A   9      13.878  73.917  24.108  1.00 26.75           O  
ATOM     63  CG2 THR A   9      12.158  75.346  25.091  1.00 29.54           C  
ATOM     64  N   THR A  10      13.228  73.845  21.169  1.00 27.82           N  
ATOM     65  CA  THR A  10      13.987  73.195  20.105  1.00 28.64           C  
ATOM     66  C   THR A  10      14.979  72.164  20.650  1.00 27.61           C  
ATOM     67  O   THR A  10      15.353  71.240  19.938  1.00 26.56           O  
ATOM     68  CB  THR A  10      14.743  74.219  19.246  1.00 32.83           C  
ATOM     69  OG1 THR A  10      15.678  74.933  20.062  1.00 36.80           O  
ATOM     70  CG2 THR A  10      13.767  75.200  18.642  1.00 34.61           C  
ATOM     71  N   LEU A  11      15.396  72.309  21.909  1.00 28.11           N  
ATOM     72  CA  LEU A  11      16.214  71.267  22.548  1.00 29.18           C  
ATOM     73  C   LEU A  11      15.500  69.910  22.571  1.00 27.48           C  
ATOM     74  O   LEU A  11      16.070  68.882  22.178  1.00 24.68           O  
ATOM     75  CB  LEU A  11      16.591  71.667  23.977  1.00 31.40           C  
ATOM     76  CG  LEU A  11      17.367  70.593  24.747  1.00 36.84           C  
ATOM     77  CD1 LEU A  11      18.725  70.342  24.098  1.00 39.17           C  
ATOM     78  CD2 LEU A  11      17.529  70.967  26.214  1.00 40.46           C  
ATOM     79  N   GLY A  12      14.254  69.904  23.038  1.00 24.74           N  
ATOM     80  CA  GLY A  12      13.478  68.680  23.092  1.00 21.99           C  
ATOM     81  C   GLY A  12      13.188  68.138  21.704  1.00 23.56           C  
ATOM     82  O   GLY A  12      13.277  66.932  21.463  1.00 21.09           O  
ATOM     83  N   THR A  13      12.854  69.041  20.790  1.00 25.48           N  
ATOM     84  CA  THR A  13      12.540  68.677  19.411  1.00 25.27           C  
ATOM     85  C   THR A  13      13.729  67.999  18.733  1.00 23.74           C  
ATOM     86  O   THR A  13      13.571  66.962  18.089  1.00 24.20           O  
ATOM     87  CB  THR A  13      12.114  69.916  18.596  1.00 26.21           C  
ATOM     88  OG1 THR A  13      10.945  70.489  19.193  1.00 24.40           O  
ATOM     89  CG2 THR A  13      11.815  69.537  17.130  1.00 23.05           C  
ATOM     90  N   ASP A  14      14.915  68.583  18.890  1.00 25.19           N  
ATOM     91  CA  ASP A  14      16.132  68.003  18.321  1.00 28.01           C  
ATOM     92  C   ASP A  14      16.395  66.610  18.876  1.00 25.25           C  
ATOM     93  O   ASP A  14      16.806  65.712  18.140  1.00 22.85           O  
ATOM     94  CB  ASP A  14      17.341  68.895  18.593  1.00 31.67           C  
ATOM     95  CG  ASP A  14      17.289  70.200  17.830  1.00 36.41           C  
ATOM     96  OD1 ASP A  14      16.503  70.303  16.863  1.00 36.94           O  
ATOM     97  OD2 ASP A  14      18.045  71.115  18.200  1.00 37.22           O  
ATOM     98  N   ALA A  15      16.151  66.427  20.172  1.00 22.00           N  
ATOM     99  CA  ALA A  15      16.345  65.120  20.797  1.00 20.84           C  
ATOM    100  C   ALA A  15      15.400  64.081  20.205  1.00 21.66           C  
ATOM    101  O   ALA A  15      15.784  62.924  19.981  1.00 20.73           O  
ATOM    102  CB  ALA A  15      16.154  65.217  22.320  1.00 19.69           C  
ATOM    103  N   GLN A  16      14.161  64.489  19.943  1.00 21.37           N  
ATOM    104  CA  GLN A  16      13.168  63.565  19.390  1.00 21.52           C  
ATOM    105  C   GLN A  16      13.540  63.151  17.961  1.00 20.58           C  
ATOM    106  O   GLN A  16      13.374  61.988  17.576  1.00 20.62           O  
ATOM    107  CB  GLN A  16      11.767  64.193  19.424  1.00 20.41           C  
ATOM    108  CG  GLN A  16      11.183  64.283  20.843  1.00 17.69           C  
ATOM    109  CD  GLN A  16      10.012  65.262  20.961  1.00 20.21           C  
ATOM    110  OE1 GLN A  16       9.737  66.042  20.049  1.00 21.61           O  
ATOM    111  NE2 GLN A  16       9.327  65.224  22.108  1.00 18.51           N  
ATOM    112  N   TRP A  17      14.044  64.096  17.180  1.00 19.50           N  
ATOM    113  CA  TRP A  17      14.489  63.770  15.822  1.00 20.08           C  
ATOM    114  C   TRP A  17      15.641  62.769  15.846  1.00 24.16           C  
ATOM    115  O   TRP A  17      15.715  61.888  14.994  1.00 24.44           O  
ATOM    116  CB  TRP A  17      14.906  65.029  15.046  1.00 24.40           C  
ATOM    117  CG  TRP A  17      13.738  65.800  14.471  1.00 26.50           C  
ATOM    118  CD1 TRP A  17      13.426  67.106  14.708  1.00 27.19           C  
ATOM    119  CD2 TRP A  17      12.727  65.306  13.574  1.00 28.72           C  
ATOM    120  NE1 TRP A  17      12.290  67.459  14.018  1.00 26.82           N  
ATOM    121  CE2 TRP A  17      11.839  66.373  13.318  1.00 29.54           C  
ATOM    122  CE3 TRP A  17      12.487  64.068  12.967  1.00 31.20           C  
ATOM    123  CZ2 TRP A  17      10.731  66.240  12.480  1.00 32.25           C  
ATOM    124  CZ3 TRP A  17      11.386  63.936  12.137  1.00 32.77           C  
ATOM    125  CH2 TRP A  17      10.524  65.017  11.897  1.00 33.18           C  
ATOM    126  N   VAL A  18      16.543  62.912  16.812  1.00 23.04           N  
ATOM    127  CA  VAL A  18      17.667  61.990  16.929  1.00 23.03           C  
ATOM    128  C   VAL A  18      17.160  60.579  17.240  1.00 21.40           C  
ATOM    129  O   VAL A  18      17.572  59.605  16.593  1.00 20.56           O  
ATOM    130  CB  VAL A  18      18.668  62.458  18.009  1.00 23.96           C  
ATOM    131  CG1 VAL A  18      19.673  61.355  18.328  1.00 24.92           C  
ATOM    132  CG2 VAL A  18      19.390  63.724  17.544  1.00 26.69           C  
ATOM    133  N   VAL A  19      16.239  60.468  18.199  1.00 17.65           N  
ATOM    134  CA  VAL A  19      15.695  59.166  18.563  1.00 17.50           C  
ATOM    135  C   VAL A  19      14.880  58.589  17.416  1.00 18.57           C  
ATOM    136  O   VAL A  19      14.965  57.388  17.134  1.00 18.34           O  
ATOM    137  CB  VAL A  19      14.826  59.239  19.838  1.00 18.44           C  
ATOM    138  CG1 VAL A  19      14.210  57.861  20.152  1.00 16.98           C  
ATOM    139  CG2 VAL A  19      15.663  59.755  21.010  1.00 19.17           C  
ATOM    140  N   PHE A  20      14.104  59.438  16.745  1.00 19.67           N  
ATOM    141  CA  PHE A  20      13.404  59.028  15.522  1.00 20.81           C  
ATOM    142  C   PHE A  20      14.335  58.317  14.537  1.00 20.00           C  
ATOM    143  O   PHE A  20      14.029  57.219  14.059  1.00 19.61           O  
ATOM    144  CB  PHE A  20      12.771  60.240  14.820  1.00 20.85           C  
ATOM    145  CG  PHE A  20      12.372  59.971  13.384  1.00 22.65           C  
ATOM    146  CD1 PHE A  20      11.302  59.137  13.090  1.00 22.59           C  
ATOM    147  CD2 PHE A  20      13.062  60.563  12.333  1.00 23.55           C  
ATOM    148  CE1 PHE A  20      10.930  58.897  11.769  1.00 24.24           C  
ATOM    149  CE2 PHE A  20      12.696  60.325  11.010  1.00 26.86           C  
ATOM    150  CZ  PHE A  20      11.632  59.486  10.730  1.00 26.31           C  
ATOM    151  N   ALA A  21      15.464  58.955  14.233  1.00 21.26           N  
ATOM    152  CA  ALA A  21      16.422  58.420  13.262  1.00 23.49           C  
ATOM    153  C   ALA A  21      16.959  57.050  13.681  1.00 22.81           C  
ATOM    154  O   ALA A  21      17.064  56.129  12.858  1.00 20.38           O  
ATOM    155  CB  ALA A  21      17.573  59.398  13.067  1.00 24.71           C  
ATOM    156  N   VAL A  22      17.298  56.911  14.959  1.00 20.89           N  
ATOM    157  CA  VAL A  22      17.833  55.643  15.438  1.00 20.51           C  
ATOM    158  C   VAL A  22      16.770  54.539  15.365  1.00 20.66           C  
ATOM    159  O   VAL A  22      17.059  53.418  14.918  1.00 18.23           O  
ATOM    160  CB  VAL A  22      18.374  55.760  16.883  1.00 21.95           C  
ATOM    161  CG1 VAL A  22      18.888  54.401  17.369  1.00 22.09           C  
ATOM    162  CG2 VAL A  22      19.494  56.812  16.947  1.00 20.86           C  
ATOM    163  N   MET A  23      15.547  54.845  15.803  1.00 17.23           N  
ATOM    164  CA  MET A  23      14.465  53.849  15.781  1.00 17.42           C  
ATOM    165  C   MET A  23      14.172  53.392  14.352  1.00 18.72           C  
ATOM    166  O   MET A  23      13.936  52.201  14.099  1.00 17.81           O  
ATOM    167  CB  MET A  23      13.182  54.406  16.404  1.00 18.98           C  
ATOM    168  CG  MET A  23      13.277  54.754  17.892  1.00 16.69           C  
ATOM    169  SD  MET A  23      13.609  53.287  18.892  1.00 18.90           S  
ATOM    170  CE  MET A  23      13.458  53.993  20.546  1.00 15.29           C  
ATOM    171  N   ALA A  24      14.169  54.346  13.423  1.00 19.84           N  
ATOM    172  CA  ALA A  24      13.879  54.039  12.023  1.00 19.53           C  
ATOM    173  C   ALA A  24      14.970  53.154  11.445  1.00 21.21           C  
ATOM    174  O   ALA A  24      14.684  52.149  10.789  1.00 21.74           O  
ATOM    175  CB  ALA A  24      13.733  55.332  11.198  1.00 22.42           C  
ATOM    176  N   LEU A  25      16.221  53.531  11.693  1.00 19.73           N  
ATOM    177  CA  LEU A  25      17.372  52.748  11.248  1.00 21.50           C  
ATOM    178  C   LEU A  25      17.329  51.310  11.793  1.00 19.34           C  
ATOM    179  O   LEU A  25      17.597  50.354  11.070  1.00 18.45           O  
ATOM    180  CB  LEU A  25      18.663  53.429  11.692  1.00 23.96           C  
ATOM    181  CG  LEU A  25      19.986  52.674  11.569  1.00 31.39           C  
ATOM    182  CD1 LEU A  25      20.416  52.541  10.105  1.00 32.42           C  
ATOM    183  CD2 LEU A  25      21.066  53.371  12.395  1.00 37.33           C  
ATOM    184  N   ALA A  26      17.015  51.161  13.074  1.00 17.74           N  
ATOM    185  CA  ALA A  26      16.932  49.819  13.651  1.00 16.97           C  
ATOM    186  C   ALA A  26      15.871  48.975  12.954  1.00 16.57           C  
ATOM    187  O   ALA A  26      16.099  47.805  12.657  1.00 17.21           O  
ATOM    188  CB  ALA A  26      16.640  49.886  15.166  1.00 17.63           C  
ATOM    189  N   ALA A  27      14.709  49.566  12.703  1.00 18.34           N  
ATOM    190  CA  ALA A  27      13.620  48.853  12.035  1.00 19.61           C  
ATOM    191  C   ALA A  27      14.057  48.369  10.654  1.00 19.65           C  
ATOM    192  O   ALA A  27      13.779  47.229  10.253  1.00 21.26           O  
ATOM    193  CB  ALA A  27      12.402  49.750  11.914  1.00 21.53           C  
ATOM    194  N   ILE A  28      14.746  49.245   9.938  1.00 18.88           N  
ATOM    195  CA  ILE A  28      15.235  48.926   8.594  1.00 20.62           C  
ATOM    196  C   ILE A  28      16.275  47.814   8.641  1.00 21.17           C  
ATOM    197  O   ILE A  28      16.216  46.859   7.868  1.00 20.87           O  
ATOM    198  CB  ILE A  28      15.837  50.173   7.913  1.00 23.65           C  
ATOM    199  CG1 ILE A  28      14.749  51.236   7.711  1.00 26.29           C  
ATOM    200  CG2 ILE A  28      16.502  49.797   6.592  1.00 24.52           C  
ATOM    201  CD1 ILE A  28      15.276  52.586   7.220  1.00 28.39           C  
ATOM    202  N   VAL A  29      17.236  47.941   9.546  1.00 19.93           N  
ATOM    203  CA  VAL A  29      18.288  46.939   9.660  1.00 21.08           C  
ATOM    204  C   VAL A  29      17.720  45.554  10.010  1.00 20.79           C  
ATOM    205  O   VAL A  29      18.095  44.552   9.391  1.00 20.69           O  
ATOM    206  CB  VAL A  29      19.340  47.370  10.709  1.00 25.33           C  
ATOM    207  CG1 VAL A  29      20.208  46.195  11.120  1.00 27.53           C  
ATOM    208  CG2 VAL A  29      20.206  48.531  10.147  1.00 21.57           C  
ATOM    209  N   PHE A  30      16.811  45.504  10.979  1.00 19.93           N  
ATOM    210  CA  PHE A  30      16.174  44.243  11.358  1.00 17.69           C  
ATOM    211  C   PHE A  30      15.345  43.686  10.206  1.00 19.87           C  
ATOM    212  O   PHE A  30      15.303  42.474   9.989  1.00 19.87           O  
ATOM    213  CB  PHE A  30      15.267  44.409  12.590  1.00 16.87           C  
ATOM    214  CG  PHE A  30      15.984  44.821  13.844  1.00 19.96           C  
ATOM    215  CD1 PHE A  30      17.320  44.525  14.037  1.00 21.79           C  
ATOM    216  CD2 PHE A  30      15.299  45.496  14.844  1.00 19.07           C  
ATOM    217  CE1 PHE A  30      17.970  44.909  15.202  1.00 20.54           C  
ATOM    218  CE2 PHE A  30      15.940  45.883  16.016  1.00 19.54           C  
ATOM    219  CZ  PHE A  30      17.279  45.587  16.192  1.00 20.29           C  
ATOM    220  N   SER A  31      14.669  44.570   9.478  1.00 19.42           N  
ATOM    221  CA  SER A  31      13.850  44.138   8.344  1.00 23.65           C  
ATOM    222  C   SER A  31      14.674  43.513   7.224  1.00 23.25           C  
ATOM    223  O   SER A  31      14.211  42.608   6.528  1.00 21.94           O  
ATOM    224  CB  SER A  31      13.041  45.310   7.789  1.00 24.73           C  
ATOM    225  OG  SER A  31      12.013  45.654   8.699  1.00 25.26           O  
ATOM    226  N   ILE A  32      15.895  43.993   7.034  1.00 22.94           N  
ATOM    227  CA  ILE A  32      16.750  43.408   6.005  1.00 23.46           C  
ATOM    228  C   ILE A  32      17.381  42.110   6.536  1.00 25.01           C  
ATOM    229  O   ILE A  32      17.447  41.099   5.828  1.00 25.82           O  
ATOM    230  CB  ILE A  32      17.817  44.422   5.540  1.00 26.49           C  
ATOM    231  CG1 ILE A  32      17.119  45.589   4.832  1.00 27.91           C  
ATOM    232  CG2 ILE A  32      18.819  43.774   4.577  1.00 29.50           C  
ATOM    233  CD1 ILE A  32      17.972  46.838   4.658  1.00 31.10           C  
ATOM    234  N   ALA A  33      17.786  42.129   7.803  1.00 23.61           N  
ATOM    235  CA  ALA A  33      18.462  40.984   8.417  1.00 25.47           C  
ATOM    236  C   ALA A  33      17.596  39.717   8.437  1.00 22.77           C  
ATOM    237  O   ALA A  33      18.075  38.621   8.141  1.00 21.02           O  
ATOM    238  CB  ALA A  33      18.898  41.338   9.834  1.00 24.61           C  
ATOM    239  N   VAL A  34      16.318  39.879   8.765  1.00 21.20           N  
ATOM    240  CA  VAL A  34      15.420  38.736   8.944  1.00 21.36           C  
ATOM    241  C   VAL A  34      15.259  37.920   7.658  1.00 22.80           C  
ATOM    242  O   VAL A  34      14.995  36.718   7.715  1.00 22.93           O  
ATOM    243  CB  VAL A  34      14.023  39.191   9.458  1.00 23.97           C  
ATOM    244  CG1 VAL A  34      13.299  40.024   8.403  1.00 24.03           C  
ATOM    245  CG2 VAL A  34      13.167  37.978   9.872  1.00 22.86           C  
ATOM    246  N   GLN A  35      15.461  38.561   6.502  1.00 23.01           N  
ATOM    247  CA  GLN A  35      15.393  37.875   5.217  1.00 24.68           C  
ATOM    248  C   GLN A  35      16.433  36.762   5.093  1.00 26.77           C  
ATOM    249  O   GLN A  35      16.255  35.831   4.309  1.00 28.23           O  
ATOM    250  CB  GLN A  35      15.576  38.865   4.058  1.00 27.67           C  
ATOM    251  CG  GLN A  35      14.685  40.099   4.128  1.00 30.82           C  
ATOM    252  CD  GLN A  35      13.209  39.756   4.233  1.00 35.93           C  
ATOM    253  OE1 GLN A  35      12.749  38.744   3.698  1.00 39.86           O  
ATOM    254  NE2 GLN A  35      12.462  40.597   4.932  1.00 35.09           N  
ATOM    255  N   PHE A  36      17.518  36.867   5.858  1.00 23.17           N  
ATOM    256  CA  PHE A  36      18.623  35.909   5.774  1.00 23.82           C  
ATOM    257  C   PHE A  36      18.587  34.835   6.856  1.00 25.20           C  
ATOM    258  O   PHE A  36      19.503  34.017   6.952  1.00 27.11           O  
ATOM    259  CB  PHE A  36      19.959  36.645   5.863  1.00 23.96           C  
ATOM    260  CG  PHE A  36      20.226  37.537   4.698  1.00 29.91           C  
ATOM    261  CD1 PHE A  36      20.946  37.073   3.608  1.00 31.86           C  
ATOM    262  CD2 PHE A  36      19.746  38.833   4.682  1.00 29.41           C  
ATOM    263  CE1 PHE A  36      21.195  37.900   2.514  1.00 31.31           C  
ATOM    264  CE2 PHE A  36      19.984  39.661   3.596  1.00 29.71           C  
ATOM    265  CZ  PHE A  36      20.711  39.193   2.512  1.00 31.11           C  
ATOM    266  N   ARG A  37      17.546  34.851   7.679  1.00 22.79           N  
ATOM    267  CA  ARG A  37      17.498  33.976   8.852  1.00 21.86           C  
ATOM    268  C   ARG A  37      16.461  32.861   8.690  1.00 23.89           C  
ATOM    269  O   ARG A  37      15.433  33.054   8.052  1.00 23.14           O  
ATOM    270  CB  ARG A  37      17.204  34.809  10.104  1.00 20.61           C  
ATOM    271  CG  ARG A  37      18.129  36.016  10.280  1.00 26.40           C  
ATOM    272  CD  ARG A  37      19.608  35.625  10.238  1.00 27.57           C  
ATOM    273  NE  ARG A  37      19.932  34.502  11.120  1.00 28.08           N  
ATOM    274  CZ  ARG A  37      20.690  33.465  10.769  1.00 32.06           C  
ATOM    275  NH1 ARG A  37      21.207  33.391   9.545  1.00 35.24           N  
ATOM    276  NH2 ARG A  37      20.931  32.494  11.638  1.00 30.65           N  
ATOM    277  N   PRO A  38      16.728  31.680   9.270  1.00 29.81           N  
ATOM    278  CA  PRO A  38      15.777  30.566   9.126  1.00 29.85           C  
ATOM    279  C   PRO A  38      14.433  30.873   9.784  1.00 27.06           C  
ATOM    280  O   PRO A  38      14.378  31.661  10.726  1.00 26.05           O  
ATOM    281  CB  PRO A  38      16.487  29.399   9.827  1.00 30.48           C  
ATOM    282  CG  PRO A  38      17.403  30.056  10.807  1.00 32.54           C  
ATOM    283  CD  PRO A  38      17.883  31.315  10.107  1.00 32.19           C  
ATOM    284  N   LEU A  39      13.367  30.267   9.272  1.00 27.75           N  
ATOM    285  CA  LEU A  39      12.002  30.571   9.709  1.00 26.34           C  
ATOM    286  C   LEU A  39      11.749  30.570  11.227  1.00 25.52           C  
ATOM    287  O   LEU A  39      11.057  31.464  11.720  1.00 26.11           O  
ATOM    288  CB  LEU A  39      11.020  29.601   9.033  1.00 28.48           C  
ATOM    289  CG  LEU A  39      11.013  29.688   7.504  1.00 35.40           C  
ATOM    290  CD1 LEU A  39       9.918  28.822   6.887  1.00 37.05           C  
ATOM    291  CD2 LEU A  39      10.884  31.141   7.040  1.00 36.24           C  
ATOM    292  N   PRO A  40      12.300  29.590  11.979  1.00 25.33           N  
ATOM    293  CA  PRO A  40      11.994  29.600  13.421  1.00 23.63           C  
ATOM    294  C   PRO A  40      12.413  30.878  14.169  1.00 22.20           C  
ATOM    295  O   PRO A  40      11.909  31.124  15.264  1.00 20.19           O  
ATOM    296  CB  PRO A  40      12.786  28.402  13.955  1.00 26.01           C  
ATOM    297  CG  PRO A  40      12.906  27.476  12.789  1.00 25.69           C  
ATOM    298  CD  PRO A  40      13.101  28.407  11.608  1.00 25.68           C  
ATOM    299  N   LEU A  41      13.318  31.665  13.596  1.00 22.17           N  
ATOM    300  CA  LEU A  41      13.791  32.884  14.250  1.00 22.15           C  
ATOM    301  C   LEU A  41      13.008  34.128  13.844  1.00 21.53           C  
ATOM    302  O   LEU A  41      13.122  35.173  14.483  1.00 18.45           O  
ATOM    303  CB  LEU A  41      15.285  33.105  13.951  1.00 23.99           C  
ATOM    304  CG  LEU A  41      16.270  32.089  14.547  1.00 26.61           C  
ATOM    305  CD1 LEU A  41      17.645  32.215  13.913  1.00 30.28           C  
ATOM    306  CD2 LEU A  41      16.360  32.250  16.058  1.00 32.06           C  
ATOM    307  N   ARG A  42      12.212  34.025  12.786  1.00 23.62           N  
ATOM    308  CA  ARG A  42      11.682  35.237  12.165  1.00 22.62           C  
ATOM    309  C   ARG A  42      10.637  35.962  13.016  1.00 21.77           C  
ATOM    310  O   ARG A  42      10.588  37.190  13.003  1.00 19.92           O  
ATOM    311  CB  ARG A  42      11.131  34.914  10.772  1.00 21.08           C  
ATOM    312  CG  ARG A  42      12.230  34.405   9.843  1.00 20.59           C  
ATOM    313  CD  ARG A  42      11.894  34.565   8.356  1.00 25.77           C  
ATOM    314  NE  ARG A  42      13.004  34.106   7.515  1.00 29.71           N  
ATOM    315  CZ  ARG A  42      13.061  34.266   6.193  1.00 36.47           C  
ATOM    316  NH1 ARG A  42      14.108  33.817   5.506  1.00 37.12           N  
ATOM    317  NH2 ARG A  42      12.073  34.880   5.555  1.00 38.05           N  
ATOM    318  N   LEU A  43       9.819  35.228  13.767  1.00 20.31           N  
ATOM    319  CA  LEU A  43       8.854  35.885  14.658  1.00 21.10           C  
ATOM    320  C   LEU A  43       9.535  36.875  15.606  1.00 20.10           C  
ATOM    321  O   LEU A  43       9.070  38.008  15.784  1.00 19.33           O  
ATOM    322  CB  LEU A  43       8.063  34.846  15.473  1.00 22.73           C  
ATOM    323  CG  LEU A  43       7.104  35.472  16.496  1.00 22.84           C  
ATOM    324  CD1 LEU A  43       6.116  36.408  15.808  1.00 25.30           C  
ATOM    325  CD2 LEU A  43       6.367  34.405  17.329  1.00 24.12           C  
ATOM    326  N   THR A  44      10.646  36.468  16.204  1.00 18.34           N  
ATOM    327  CA  THR A  44      11.342  37.353  17.137  1.00 17.96           C  
ATOM    328  C   THR A  44      11.843  38.626  16.427  1.00 18.78           C  
ATOM    329  O   THR A  44      11.723  39.732  16.962  1.00 16.61           O  
ATOM    330  CB  THR A  44      12.500  36.619  17.825  1.00 19.64           C  
ATOM    331  OG1 THR A  44      11.977  35.457  18.495  1.00 23.63           O  
ATOM    332  CG2 THR A  44      13.176  37.513  18.855  1.00 18.65           C  
ATOM    333  N   TYR A  45      12.373  38.480  15.215  1.00 18.69           N  
ATOM    334  CA  TYR A  45      12.742  39.658  14.432  1.00 17.59           C  
ATOM    335  C   TYR A  45      11.524  40.540  14.167  1.00 17.76           C  
ATOM    336  O   TYR A  45      11.600  41.755  14.318  1.00 17.90           O  
ATOM    337  CB  TYR A  45      13.399  39.255  13.096  1.00 16.87           C  
ATOM    338  CG  TYR A  45      14.865  38.861  13.204  1.00 18.63           C  
ATOM    339  CD1 TYR A  45      15.239  37.563  13.546  1.00 17.99           C  
ATOM    340  CD2 TYR A  45      15.875  39.791  12.951  1.00 18.98           C  
ATOM    341  CE1 TYR A  45      16.585  37.202  13.647  1.00 18.57           C  
ATOM    342  CE2 TYR A  45      17.220  39.442  13.041  1.00 17.45           C  
ATOM    343  CZ  TYR A  45      17.568  38.148  13.391  1.00 20.22           C  
ATOM    344  OH  TYR A  45      18.900  37.801  13.498  1.00 20.50           O  
ATOM    345  N   TYR A  46      10.401  39.945  13.773  1.00 16.46           N  
ATOM    346  CA  TYR A  46       9.208  40.746  13.439  1.00 19.30           C  
ATOM    347  C   TYR A  46       8.695  41.545  14.641  1.00 18.29           C  
ATOM    348  O   TYR A  46       8.227  42.685  14.505  1.00 18.42           O  
ATOM    349  CB  TYR A  46       8.076  39.855  12.920  1.00 19.61           C  
ATOM    350  CG  TYR A  46       8.383  39.140  11.618  1.00 29.27           C  
ATOM    351  CD1 TYR A  46       9.201  39.716  10.661  1.00 31.99           C  
ATOM    352  CD2 TYR A  46       7.851  37.885  11.360  1.00 33.48           C  
ATOM    353  CE1 TYR A  46       9.479  39.051   9.458  1.00 35.57           C  
ATOM    354  CE2 TYR A  46       8.120  37.220  10.182  1.00 37.45           C  
ATOM    355  CZ  TYR A  46       8.932  37.807   9.235  1.00 39.01           C  
ATOM    356  OH  TYR A  46       9.190  37.132   8.065  1.00 45.85           O  
ATOM    357  N   VAL A  47       8.773  40.938  15.815  1.00 16.44           N  
ATOM    358  CA  VAL A  47       8.338  41.615  17.037  1.00 16.47           C  
ATOM    359  C   VAL A  47       9.164  42.886  17.248  1.00 17.89           C  
ATOM    360  O   VAL A  47       8.633  43.964  17.551  1.00 15.65           O  
ATOM    361  CB  VAL A  47       8.459  40.678  18.260  1.00 17.53           C  
ATOM    362  CG1 VAL A  47       8.215  41.459  19.564  1.00 19.64           C  
ATOM    363  CG2 VAL A  47       7.460  39.558  18.125  1.00 18.91           C  
ATOM    364  N   ASN A  48      10.468  42.774  17.040  1.00 17.00           N  
ATOM    365  CA  ASN A  48      11.350  43.906  17.261  1.00 15.60           C  
ATOM    366  C   ASN A  48      11.286  44.931  16.130  1.00 18.49           C  
ATOM    367  O   ASN A  48      11.452  46.139  16.365  1.00 17.85           O  
ATOM    368  CB  ASN A  48      12.769  43.392  17.494  1.00 17.31           C  
ATOM    369  CG  ASN A  48      12.867  42.598  18.790  1.00 19.97           C  
ATOM    370  OD1 ASN A  48      13.120  41.380  18.793  1.00 23.56           O  
ATOM    371  ND2 ASN A  48      12.604  43.273  19.893  1.00 13.25           N  
ATOM    372  N   ILE A  49      11.003  44.465  14.916  1.00 18.24           N  
ATOM    373  CA  ILE A  49      10.761  45.385  13.803  1.00 16.59           C  
ATOM    374  C   ILE A  49       9.531  46.242  14.091  1.00 19.14           C  
ATOM    375  O   ILE A  49       9.562  47.462  13.905  1.00 18.37           O  
ATOM    376  CB  ILE A  49      10.564  44.648  12.476  1.00 17.90           C  
ATOM    377  CG1 ILE A  49      11.872  43.994  12.036  1.00 19.48           C  
ATOM    378  CG2 ILE A  49      10.098  45.633  11.406  1.00 18.93           C  
ATOM    379  CD1 ILE A  49      11.682  42.893  11.012  1.00 17.70           C  
ATOM    380  N   ALA A  50       8.465  45.605  14.582  1.00 21.00           N  
ATOM    381  CA  ALA A  50       7.244  46.318  14.967  1.00 19.57           C  
ATOM    382  C   ALA A  50       7.495  47.333  16.090  1.00 18.73           C  
ATOM    383  O   ALA A  50       7.034  48.470  16.014  1.00 20.25           O  
ATOM    384  CB  ALA A  50       6.152  45.322  15.393  1.00 18.93           C  
ATOM    385  N   ILE A  51       8.210  46.911  17.132  1.00 16.00           N  
ATOM    386  CA  ILE A  51       8.534  47.790  18.263  1.00 17.06           C  
ATOM    387  C   ILE A  51       9.222  49.060  17.789  1.00 18.28           C  
ATOM    388  O   ILE A  51       8.829  50.167  18.162  1.00 16.25           O  
ATOM    389  CB  ILE A  51       9.443  47.085  19.288  1.00 14.17           C  
ATOM    390  CG1 ILE A  51       8.654  46.009  20.047  1.00 15.93           C  
ATOM    391  CG2 ILE A  51      10.007  48.085  20.293  1.00 15.39           C  
ATOM    392  CD1 ILE A  51       9.542  44.992  20.781  1.00 15.10           C  
ATOM    393  N   CYS A  52      10.239  48.895  16.949  1.00 14.52           N  
ATOM    394  CA  CYS A  52      11.038  50.039  16.505  1.00 17.33           C  
ATOM    395  C   CYS A  52      10.280  50.917  15.506  1.00 17.82           C  
ATOM    396  O   CYS A  52      10.445  52.147  15.484  1.00 17.49           O  
ATOM    397  CB  CYS A  52      12.368  49.544  15.924  1.00 18.44           C  
ATOM    398  SG  CYS A  52      13.485  48.937  17.250  1.00 20.07           S  
ATOM    399  N   THR A  53       9.422  50.294  14.707  1.00 19.52           N  
ATOM    400  CA  THR A  53       8.604  51.036  13.752  1.00 19.06           C  
ATOM    401  C   THR A  53       7.555  51.902  14.467  1.00 19.65           C  
ATOM    402  O   THR A  53       7.347  53.071  14.111  1.00 20.13           O  
ATOM    403  CB  THR A  53       7.920  50.073  12.763  1.00 21.39           C  
ATOM    404  OG1 THR A  53       8.931  49.344  12.039  1.00 19.71           O  
ATOM    405  CG2 THR A  53       7.046  50.834  11.769  1.00 23.54           C  
ATOM    406  N   ILE A  54       6.891  51.325  15.465  1.00 16.54           N  
ATOM    407  CA  ILE A  54       5.935  52.077  16.277  1.00 18.31           C  
ATOM    408  C   ILE A  54       6.635  53.225  17.011  1.00 17.87           C  
ATOM    409  O   ILE A  54       6.134  54.357  17.040  1.00 20.32           O  
ATOM    410  CB  ILE A  54       5.217  51.157  17.293  1.00 16.86           C  
ATOM    411  CG1 ILE A  54       4.287  50.192  16.555  1.00 17.56           C  
ATOM    412  CG2 ILE A  54       4.419  51.982  18.313  1.00 16.21           C  
ATOM    413  CD1 ILE A  54       3.912  48.957  17.376  1.00 16.70           C  
ATOM    414  N   ALA A  55       7.803  52.951  17.590  1.00 18.16           N  
ATOM    415  CA  ALA A  55       8.541  54.011  18.289  1.00 19.70           C  
ATOM    416  C   ALA A  55       8.996  55.115  17.329  1.00 18.53           C  
ATOM    417  O   ALA A  55       8.935  56.301  17.671  1.00 18.54           O  
ATOM    418  CB  ALA A  55       9.742  53.433  19.045  1.00 19.22           C  
ATOM    419  N   ALA A  56       9.445  54.747  16.128  1.00 15.88           N  
ATOM    420  CA  ALA A  56       9.843  55.756  15.150  1.00 18.50           C  
ATOM    421  C   ALA A  56       8.657  56.649  14.782  1.00 18.49           C  
ATOM    422  O   ALA A  56       8.784  57.873  14.683  1.00 18.07           O  
ATOM    423  CB  ALA A  56      10.427  55.096  13.894  1.00 18.07           C  
ATOM    424  N   THR A  57       7.499  56.031  14.604  1.00 18.16           N  
ATOM    425  CA  THR A  57       6.277  56.754  14.265  1.00 20.92           C  
ATOM    426  C   THR A  57       5.893  57.753  15.370  1.00 21.15           C  
ATOM    427  O   THR A  57       5.545  58.901  15.099  1.00 19.71           O  
ATOM    428  CB  THR A  57       5.120  55.778  14.031  1.00 25.23           C  
ATOM    429  OG1 THR A  57       5.467  54.874  12.963  1.00 27.57           O  
ATOM    430  CG2 THR A  57       3.852  56.531  13.661  1.00 26.65           C  
ATOM    431  N   ALA A  58       5.970  57.301  16.613  1.00 19.81           N  
ATOM    432  CA  ALA A  58       5.659  58.149  17.764  1.00 19.35           C  
ATOM    433  C   ALA A  58       6.630  59.323  17.904  1.00 19.88           C  
ATOM    434  O   ALA A  58       6.223  60.449  18.224  1.00 18.99           O  
ATOM    435  CB  ALA A  58       5.658  57.312  19.038  1.00 16.57           C  
ATOM    436  N   TYR A  59       7.917  59.071  17.686  1.00 17.95           N  
ATOM    437  CA  TYR A  59       8.893  60.152  17.793  1.00 19.17           C  
ATOM    438  C   TYR A  59       8.760  61.146  16.636  1.00 20.98           C  
ATOM    439  O   TYR A  59       8.952  62.350  16.820  1.00 20.21           O  
ATOM    440  CB  TYR A  59      10.320  59.598  17.885  1.00 19.50           C  
ATOM    441  CG  TYR A  59      10.732  59.382  19.329  1.00 18.94           C  
ATOM    442  CD1 TYR A  59      10.515  58.156  19.965  1.00 17.58           C  
ATOM    443  CD2 TYR A  59      11.314  60.411  20.065  1.00 18.89           C  
ATOM    444  CE1 TYR A  59      10.875  57.966  21.300  1.00 16.52           C  
ATOM    445  CE2 TYR A  59      11.671  60.230  21.394  1.00 16.18           C  
ATOM    446  CZ  TYR A  59      11.447  59.002  22.003  1.00 18.00           C  
ATOM    447  OH  TYR A  59      11.807  58.821  23.316  1.00 17.03           O  
ATOM    448  N   TYR A  60       8.421  60.652  15.451  1.00 20.19           N  
ATOM    449  CA  TYR A  60       8.114  61.549  14.342  1.00 23.48           C  
ATOM    450  C   TYR A  60       6.993  62.514  14.756  1.00 24.00           C  
ATOM    451  O   TYR A  60       7.107  63.734  14.594  1.00 22.94           O  
ATOM    452  CB  TYR A  60       7.719  60.752  13.101  1.00 22.07           C  
ATOM    453  CG  TYR A  60       7.356  61.627  11.925  1.00 24.32           C  
ATOM    454  CD1 TYR A  60       8.336  62.106  11.062  1.00 28.71           C  
ATOM    455  CD2 TYR A  60       6.038  61.996  11.692  1.00 25.62           C  
ATOM    456  CE1 TYR A  60       8.008  62.916   9.993  1.00 30.37           C  
ATOM    457  CE2 TYR A  60       5.702  62.813  10.627  1.00 31.12           C  
ATOM    458  CZ  TYR A  60       6.689  63.265   9.783  1.00 32.48           C  
ATOM    459  OH  TYR A  60       6.350  64.070   8.724  1.00 36.87           O  
ATOM    460  N   ALA A  61       5.931  61.955  15.331  1.00 24.68           N  
ATOM    461  CA  ALA A  61       4.773  62.743  15.740  1.00 24.50           C  
ATOM    462  C   ALA A  61       5.148  63.782  16.797  1.00 23.05           C  
ATOM    463  O   ALA A  61       4.753  64.949  16.707  1.00 24.61           O  
ATOM    464  CB  ALA A  61       3.667  61.825  16.265  1.00 24.70           C  
ATOM    465  N   MET A  62       5.912  63.358  17.795  1.00 21.50           N  
ATOM    466  CA  MET A  62       6.338  64.270  18.850  1.00 22.71           C  
ATOM    467  C   MET A  62       7.247  65.392  18.329  1.00 24.71           C  
ATOM    468  O   MET A  62       7.130  66.547  18.755  1.00 22.40           O  
ATOM    469  CB  MET A  62       7.029  63.482  19.961  1.00 21.30           C  
ATOM    470  CG  MET A  62       6.029  62.646  20.772  1.00 20.88           C  
ATOM    471  SD  MET A  62       6.703  61.792  22.207  1.00 20.78           S  
ATOM    472  CE  MET A  62       7.756  60.558  21.430  1.00 21.16           C  
ATOM    473  N   ALA A  63       8.134  65.064  17.394  1.00 19.62           N  
ATOM    474  CA  ALA A  63       9.081  66.055  16.868  1.00 21.15           C  
ATOM    475  C   ALA A  63       8.400  67.085  15.976  1.00 25.37           C  
ATOM    476  O   ALA A  63       8.751  68.275  15.983  1.00 26.21           O  
ATOM    477  CB  ALA A  63      10.204  65.358  16.104  1.00 23.17           C  
ATOM    478  N   VAL A  64       7.424  66.628  15.203  1.00 25.33           N  
ATOM    479  CA  VAL A  64       6.693  67.511  14.295  1.00 27.05           C  
ATOM    480  C   VAL A  64       5.714  68.422  15.039  1.00 29.82           C  
ATOM    481  O   VAL A  64       5.525  69.590  14.661  1.00 29.86           O  
ATOM    482  CB  VAL A  64       5.931  66.691  13.225  1.00 29.66           C  
ATOM    483  CG1 VAL A  64       4.966  67.575  12.433  1.00 35.16           C  
ATOM    484  CG2 VAL A  64       6.921  66.011  12.285  1.00 28.92           C  
ATOM    485  N   ASN A  65       5.116  67.906  16.110  1.00 28.93           N  
ATOM    486  CA  ASN A  65       4.042  68.617  16.812  1.00 30.53           C  
ATOM    487  C   ASN A  65       4.422  69.255  18.153  1.00 29.84           C  
ATOM    488  O   ASN A  65       3.687  70.103  18.657  1.00 28.89           O  
ATOM    489  CB  ASN A  65       2.867  67.665  17.060  1.00 33.27           C  
ATOM    490  CG  ASN A  65       2.188  67.228  15.782  1.00 40.05           C  
ATOM    491  OD1 ASN A  65       1.861  68.049  14.924  1.00 43.51           O  
ATOM    492  ND2 ASN A  65       1.989  65.921  15.637  1.00 40.57           N  
ATOM    493  N   GLY A  66       5.547  68.844  18.731  1.00 28.37           N  
ATOM    494  CA  GLY A  66       5.912  69.269  20.080  1.00 28.74           C  
ATOM    495  C   GLY A  66       6.026  70.775  20.271  1.00 28.90           C  
ATOM    496  O   GLY A  66       5.709  71.310  21.342  1.00 27.32           O  
ATOM    497  N   GLY A  67       6.471  71.460  19.223  1.00 28.05           N  
ATOM    498  CA  GLY A  67       6.615  72.905  19.246  1.00 30.64           C  
ATOM    499  C   GLY A  67       5.299  73.664  19.311  1.00 31.31           C  
ATOM    500  O   GLY A  67       5.286  74.875  19.561  1.00 31.81           O  
ATOM    501  N   ASP A  68       4.186  72.970  19.084  1.00 28.63           N  
ATOM    502  CA  ASP A  68       2.874  73.605  19.223  1.00 29.40           C  
ATOM    503  C   ASP A  68       2.596  74.009  20.679  1.00 26.35           C  
ATOM    504  O   ASP A  68       1.757  74.878  20.930  1.00 27.64           O  
ATOM    505  CB  ASP A  68       1.762  72.681  18.727  1.00 33.38           C  
ATOM    506  CG  ASP A  68       1.799  72.464  17.221  1.00 38.62           C  
ATOM    507  OD1 ASP A  68       2.606  73.123  16.529  1.00 38.11           O  
ATOM    508  OD2 ASP A  68       1.005  71.631  16.732  1.00 41.68           O  
ATOM    509  N   ASN A  69       3.301  73.374  21.618  1.00 25.16           N  
ATOM    510  CA  ASN A  69       3.183  73.661  23.057  1.00 24.96           C  
ATOM    511  C   ASN A  69       1.751  73.466  23.568  1.00 27.36           C  
ATOM    512  O   ASN A  69       1.250  74.220  24.407  1.00 28.44           O  
ATOM    513  CB  ASN A  69       3.702  75.074  23.366  1.00 26.01           C  
ATOM    514  CG  ASN A  69       5.216  75.176  23.232  1.00 31.22           C  
ATOM    515  OD1 ASN A  69       5.933  74.166  23.308  1.00 32.30           O  
ATOM    516  ND2 ASN A  69       5.709  76.383  23.017  1.00 26.96           N  
ATOM    517  N   LYS A  70       1.121  72.412  23.054  1.00 25.86           N  
ATOM    518  CA  LYS A  70      -0.231  72.000  23.406  1.00 26.26           C  
ATOM    519  C   LYS A  70      -0.249  70.480  23.301  1.00 24.18           C  
ATOM    520  O   LYS A  70       0.551  69.913  22.567  1.00 26.63           O  
ATOM    521  CB  LYS A  70      -1.282  72.612  22.463  1.00 30.25           C  
ATOM    522  CG  LYS A  70      -1.406  74.132  22.488  1.00 33.27           C  
ATOM    523  CD  LYS A  70      -2.062  74.617  23.788  1.00 36.02           C  
ATOM    524  CE  LYS A  70      -2.876  75.882  23.532  1.00 37.68           C  
ATOM    525  NZ  LYS A  70      -3.545  76.412  24.753  1.00 39.86           N  
ATOM    526  N   PRO A  71      -1.137  69.805  24.043  1.00 25.10           N  
ATOM    527  CA  PRO A  71      -2.046  70.336  25.063  1.00 26.48           C  
ATOM    528  C   PRO A  71      -1.303  70.616  26.359  1.00 24.87           C  
ATOM    529  O   PRO A  71      -0.125  70.291  26.453  1.00 24.50           O  
ATOM    530  CB  PRO A  71      -3.050  69.198  25.256  1.00 28.43           C  
ATOM    531  CG  PRO A  71      -2.246  67.979  25.010  1.00 26.26           C  
ATOM    532  CD  PRO A  71      -1.302  68.348  23.877  1.00 23.86           C  
ATOM    533  N   THR A  72      -1.989  71.188  27.342  1.00 26.25           N  
ATOM    534  CA  THR A  72      -1.391  71.439  28.649  1.00 27.47           C  
ATOM    535  C   THR A  72      -2.306  70.974  29.778  1.00 29.25           C  
ATOM    536  O   THR A  72      -3.513  70.811  29.582  1.00 31.32           O  
ATOM    537  CB  THR A  72      -1.093  72.942  28.866  1.00 26.55           C  
ATOM    538  OG1 THR A  72      -2.326  73.670  28.983  1.00 29.83           O  
ATOM    539  CG2 THR A  72      -0.270  73.512  27.712  1.00 25.26           C  
ATOM    540  N   ALA A  73      -1.727  70.773  30.957  1.00 23.76           N  
ATOM    541  CA  ALA A  73      -2.523  70.545  32.168  1.00 26.42           C  
ATOM    542  C   ALA A  73      -2.155  71.571  33.222  1.00 29.23           C  
ATOM    543  O   ALA A  73      -0.982  71.918  33.369  1.00 31.95           O  
ATOM    544  CB  ALA A  73      -2.309  69.138  32.703  1.00 25.69           C  
ATOM    545  N   GLY A  74      -3.153  72.043  33.962  1.00 28.83           N  
ATOM    546  CA  GLY A  74      -2.928  73.014  35.017  1.00 29.85           C  
ATOM    547  C   GLY A  74      -3.092  74.431  34.502  1.00 33.93           C  
ATOM    548  O   GLY A  74      -3.192  74.656  33.299  1.00 37.22           O  
ATOM    549  N   THR A  75      -3.128  75.393  35.414  1.00 37.34           N  
ATOM    550  CA  THR A  75      -3.329  76.784  35.024  1.00 39.93           C  
ATOM    551  C   THR A  75      -2.303  77.693  35.683  1.00 37.20           C  
ATOM    552  O   THR A  75      -1.628  77.298  36.637  1.00 34.98           O  
ATOM    553  CB  THR A  75      -4.741  77.282  35.402  1.00 45.92           C  
ATOM    554  OG1 THR A  75      -4.951  77.094  36.807  1.00 45.10           O  
ATOM    555  CG2 THR A  75      -5.811  76.524  34.623  1.00 47.58           C  
ATOM    556  N   GLY A  76      -2.206  78.919  35.179  1.00 37.94           N  
ATOM    557  CA  GLY A  76      -1.295  79.895  35.745  1.00 38.11           C  
ATOM    558  C   GLY A  76       0.126  79.371  35.770  1.00 33.14           C  
ATOM    559  O   GLY A  76       0.574  78.741  34.819  1.00 32.79           O  
ATOM    560  N   ALA A  77       0.811  79.600  36.885  1.00 33.62           N  
ATOM    561  CA  ALA A  77       2.225  79.281  37.017  1.00 34.42           C  
ATOM    562  C   ALA A  77       2.503  77.779  37.027  1.00 31.76           C  
ATOM    563  O   ALA A  77       3.651  77.371  36.910  1.00 32.48           O  
ATOM    564  CB  ALA A  77       2.782  79.913  38.283  1.00 38.38           C  
ATOM    565  N   ASP A  78       1.453  76.974  37.176  1.00 29.72           N  
ATOM    566  CA  ASP A  78       1.583  75.521  37.268  1.00 31.88           C  
ATOM    567  C   ASP A  78       1.261  74.814  35.956  1.00 29.72           C  
ATOM    568  O   ASP A  78       1.309  73.583  35.891  1.00 28.82           O  
ATOM    569  CB  ASP A  78       0.670  74.972  38.361  1.00 35.56           C  
ATOM    570  CG  ASP A  78       1.084  75.426  39.741  1.00 41.98           C  
ATOM    571  OD1 ASP A  78       2.304  75.415  40.020  1.00 41.74           O  
ATOM    572  OD2 ASP A  78       0.194  75.802  40.537  1.00 45.32           O  
ATOM    573  N   GLU A  79       0.920  75.589  34.927  1.00 29.26           N  
ATOM    574  CA  GLU A  79       0.596  75.025  33.618  1.00 27.44           C  
ATOM    575  C   GLU A  79       1.833  74.372  32.994  1.00 26.23           C  
ATOM    576  O   GLU A  79       2.922  74.949  33.005  1.00 26.60           O  
ATOM    577  CB  GLU A  79       0.026  76.099  32.678  1.00 27.44           C  
ATOM    578  CG  GLU A  79      -0.492  75.533  31.355  1.00 28.24           C  
ATOM    579  CD  GLU A  79      -1.262  76.546  30.528  1.00 32.93           C  
ATOM    580  OE1 GLU A  79      -1.264  77.741  30.890  1.00 33.55           O  
ATOM    581  OE2 GLU A  79      -1.873  76.143  29.517  1.00 34.14           O  
ATOM    582  N   ARG A  80       1.657  73.165  32.465  1.00 24.16           N  
ATOM    583  CA  ARG A  80       2.762  72.388  31.907  1.00 23.10           C  
ATOM    584  C   ARG A  80       2.280  71.617  30.686  1.00 23.41           C  
ATOM    585  O   ARG A  80       1.191  71.046  30.694  1.00 25.78           O  
ATOM    586  CB  ARG A  80       3.344  71.431  32.964  1.00 22.37           C  
ATOM    587  CG  ARG A  80       4.729  70.855  32.620  1.00 21.87           C  
ATOM    588  CD  ARG A  80       5.239  69.936  33.736  1.00 25.17           C  
ATOM    589  NE  ARG A  80       6.616  69.469  33.550  1.00 23.86           N  
ATOM    590  CZ  ARG A  80       6.948  68.344  32.920  1.00 21.61           C  
ATOM    591  NH1 ARG A  80       6.003  67.583  32.383  1.00 20.16           N  
ATOM    592  NH2 ARG A  80       8.223  67.985  32.814  1.00 19.67           N  
ATOM    593  N   GLN A  81       3.093  71.605  29.634  1.00 22.88           N  
ATOM    594  CA  GLN A  81       2.756  70.876  28.423  1.00 23.00           C  
ATOM    595  C   GLN A  81       2.614  69.385  28.710  1.00 21.96           C  
ATOM    596  O   GLN A  81       3.412  68.818  29.457  1.00 22.00           O  
ATOM    597  CB  GLN A  81       3.825  71.111  27.352  1.00 23.17           C  
ATOM    598  CG  GLN A  81       3.636  70.320  26.070  1.00 22.43           C  
ATOM    599  CD  GLN A  81       4.537  70.819  24.953  1.00 23.43           C  
ATOM    600  OE1 GLN A  81       5.246  71.820  25.104  1.00 24.11           O  
ATOM    601  NE2 GLN A  81       4.508  70.128  23.822  1.00 24.31           N  
ATOM    602  N   VAL A  82       1.589  68.764  28.136  1.00 20.73           N  
ATOM    603  CA  VAL A  82       1.451  67.311  28.207  1.00 21.25           C  
ATOM    604  C   VAL A  82       1.774  66.659  26.864  1.00 20.16           C  
ATOM    605  O   VAL A  82       1.062  66.839  25.884  1.00 21.86           O  
ATOM    606  CB  VAL A  82       0.032  66.880  28.634  1.00 22.56           C  
ATOM    607  CG1 VAL A  82      -0.056  65.351  28.710  1.00 21.16           C  
ATOM    608  CG2 VAL A  82      -0.335  67.509  29.974  1.00 22.07           C  
ATOM    609  N   ILE A  83       2.855  65.896  26.840  1.00 20.95           N  
ATOM    610  CA  ILE A  83       3.207  65.086  25.684  1.00 19.98           C  
ATOM    611  C   ILE A  83       2.605  63.691  25.853  1.00 23.17           C  
ATOM    612  O   ILE A  83       3.052  62.917  26.705  1.00 26.60           O  
ATOM    613  CB  ILE A  83       4.730  64.998  25.522  1.00 20.05           C  
ATOM    614  CG1 ILE A  83       5.294  66.393  25.195  1.00 22.17           C  
ATOM    615  CG2 ILE A  83       5.099  63.997  24.415  1.00 19.87           C  
ATOM    616  CD1 ILE A  83       6.801  66.483  25.345  1.00 22.64           C  
ATOM    617  N   TYR A  84       1.572  63.376  25.079  1.00 22.92           N  
ATOM    618  CA  TYR A  84       0.848  62.122  25.310  1.00 25.07           C  
ATOM    619  C   TYR A  84       1.094  61.050  24.241  1.00 22.68           C  
ATOM    620  O   TYR A  84       0.665  59.908  24.401  1.00 20.33           O  
ATOM    621  CB  TYR A  84      -0.654  62.397  25.425  1.00 25.36           C  
ATOM    622  CG  TYR A  84      -1.279  62.949  24.165  1.00 27.91           C  
ATOM    623  CD1 TYR A  84      -1.375  64.322  23.952  1.00 27.28           C  
ATOM    624  CD2 TYR A  84      -1.777  62.095  23.184  1.00 28.75           C  
ATOM    625  CE1 TYR A  84      -1.947  64.827  22.795  1.00 29.67           C  
ATOM    626  CE2 TYR A  84      -2.345  62.589  22.031  1.00 30.94           C  
ATOM    627  CZ  TYR A  84      -2.432  63.952  21.839  1.00 32.22           C  
ATOM    628  OH  TYR A  84      -3.002  64.432  20.683  1.00 35.31           O  
ATOM    629  N   ALA A  85       1.775  61.404  23.153  1.00 22.86           N  
ATOM    630  CA  ALA A  85       2.053  60.413  22.109  1.00 21.43           C  
ATOM    631  C   ALA A  85       2.866  59.248  22.653  1.00 19.57           C  
ATOM    632  O   ALA A  85       2.688  58.102  22.227  1.00 19.55           O  
ATOM    633  CB  ALA A  85       2.778  61.057  20.934  1.00 20.56           C  
ATOM    634  N   ARG A  86       3.759  59.541  23.593  1.00 17.96           N  
ATOM    635  CA  ARG A  86       4.576  58.499  24.205  1.00 18.21           C  
ATOM    636  C   ARG A  86       3.724  57.349  24.782  1.00 19.57           C  
ATOM    637  O   ARG A  86       4.111  56.185  24.669  1.00 18.36           O  
ATOM    638  CB  ARG A  86       5.489  59.103  25.282  1.00 19.67           C  
ATOM    639  CG  ARG A  86       4.770  59.808  26.432  1.00 19.95           C  
ATOM    640  CD  ARG A  86       5.772  60.297  27.478  1.00 20.72           C  
ATOM    641  NE  ARG A  86       6.728  61.256  26.911  1.00 18.23           N  
ATOM    642  CZ  ARG A  86       6.921  62.488  27.375  1.00 19.99           C  
ATOM    643  NH1 ARG A  86       6.231  62.920  28.429  1.00 20.08           N  
ATOM    644  NH2 ARG A  86       7.819  63.287  26.802  1.00 20.88           N  
ATOM    645  N   TYR A  87       2.561  57.658  25.364  1.00 21.17           N  
ATOM    646  CA  TYR A  87       1.698  56.613  25.946  1.00 18.86           C  
ATOM    647  C   TYR A  87       1.055  55.740  24.871  1.00 19.71           C  
ATOM    648  O   TYR A  87       0.814  54.545  25.088  1.00 18.53           O  
ATOM    649  CB  TYR A  87       0.600  57.229  26.827  1.00 19.10           C  
ATOM    650  CG  TYR A  87       1.142  58.070  27.954  1.00 19.28           C  
ATOM    651  CD1 TYR A  87       1.213  59.454  27.837  1.00 19.95           C  
ATOM    652  CD2 TYR A  87       1.602  57.484  29.133  1.00 21.94           C  
ATOM    653  CE1 TYR A  87       1.719  60.231  28.854  1.00 20.70           C  
ATOM    654  CE2 TYR A  87       2.115  58.259  30.162  1.00 23.13           C  
ATOM    655  CZ  TYR A  87       2.174  59.632  30.011  1.00 24.72           C  
ATOM    656  OH  TYR A  87       2.674  60.417  31.019  1.00 26.42           O  
ATOM    657  N   ILE A  88       0.774  56.331  23.714  1.00 20.87           N  
ATOM    658  CA  ILE A  88       0.202  55.573  22.606  1.00 22.85           C  
ATOM    659  C   ILE A  88       1.251  54.593  22.062  1.00 22.35           C  
ATOM    660  O   ILE A  88       0.940  53.440  21.762  1.00 22.73           O  
ATOM    661  CB  ILE A  88      -0.313  56.507  21.494  1.00 25.20           C  
ATOM    662  CG1 ILE A  88      -1.293  57.525  22.090  1.00 25.93           C  
ATOM    663  CG2 ILE A  88      -0.993  55.706  20.405  1.00 27.08           C  
ATOM    664  CD1 ILE A  88      -1.772  58.588  21.110  1.00 27.34           C  
ATOM    665  N   ASP A  89       2.491  55.062  21.948  1.00 19.07           N  
ATOM    666  CA  ASP A  89       3.648  54.197  21.709  1.00 20.63           C  
ATOM    667  C   ASP A  89       3.634  53.030  22.713  1.00 20.92           C  
ATOM    668  O   ASP A  89       3.541  51.860  22.333  1.00 19.44           O  
ATOM    669  CB  ASP A  89       4.932  55.047  21.820  1.00 22.56           C  
ATOM    670  CG  ASP A  89       6.239  54.243  21.737  1.00 23.72           C  
ATOM    671  OD1 ASP A  89       6.312  53.062  22.146  1.00 21.23           O  
ATOM    672  OD2 ASP A  89       7.244  54.851  21.297  1.00 22.32           O  
ATOM    673  N   TRP A  90       3.698  53.362  23.995  1.00 17.32           N  
ATOM    674  CA  TRP A  90       3.917  52.354  25.041  1.00 15.85           C  
ATOM    675  C   TRP A  90       2.817  51.299  25.138  1.00 17.80           C  
ATOM    676  O   TRP A  90       3.097  50.144  25.480  1.00 16.61           O  
ATOM    677  CB  TRP A  90       4.070  53.028  26.410  1.00 15.02           C  
ATOM    678  CG  TRP A  90       5.188  54.031  26.517  1.00 16.93           C  
ATOM    679  CD1 TRP A  90       6.218  54.238  25.631  1.00 16.98           C  
ATOM    680  CD2 TRP A  90       5.379  54.970  27.578  1.00 17.18           C  
ATOM    681  NE1 TRP A  90       7.032  55.246  26.083  1.00 16.88           N  
ATOM    682  CE2 TRP A  90       6.543  55.709  27.279  1.00 18.95           C  
ATOM    683  CE3 TRP A  90       4.684  55.248  28.761  1.00 17.03           C  
ATOM    684  CZ2 TRP A  90       7.024  56.715  28.116  1.00 20.43           C  
ATOM    685  CZ3 TRP A  90       5.156  56.261  29.590  1.00 19.19           C  
ATOM    686  CH2 TRP A  90       6.318  56.974  29.267  1.00 20.47           C  
ATOM    687  N   VAL A  91       1.571  51.669  24.855  1.00 19.95           N  
ATOM    688  CA  VAL A  91       0.487  50.697  25.027  1.00 19.31           C  
ATOM    689  C   VAL A  91       0.629  49.563  24.000  1.00 21.24           C  
ATOM    690  O   VAL A  91       0.187  48.435  24.247  1.00 19.54           O  
ATOM    691  CB  VAL A  91      -0.911  51.362  24.944  1.00 20.80           C  
ATOM    692  CG1 VAL A  91      -1.333  51.612  23.499  1.00 24.51           C  
ATOM    693  CG2 VAL A  91      -1.953  50.512  25.696  1.00 24.20           C  
ATOM    694  N   PHE A  92       1.293  49.841  22.877  1.00 19.13           N  
ATOM    695  CA  PHE A  92       1.582  48.789  21.910  1.00 20.77           C  
ATOM    696  C   PHE A  92       2.972  48.175  22.088  1.00 20.69           C  
ATOM    697  O   PHE A  92       3.138  46.967  21.924  1.00 22.01           O  
ATOM    698  CB  PHE A  92       1.436  49.322  20.480  1.00 20.12           C  
ATOM    699  CG  PHE A  92       0.041  49.734  20.141  1.00 24.66           C  
ATOM    700  CD1 PHE A  92      -0.933  48.782  19.903  1.00 28.80           C  
ATOM    701  CD2 PHE A  92      -0.306  51.075  20.076  1.00 26.04           C  
ATOM    702  CE1 PHE A  92      -2.232  49.157  19.597  1.00 31.45           C  
ATOM    703  CE2 PHE A  92      -1.597  51.455  19.773  1.00 27.47           C  
ATOM    704  CZ  PHE A  92      -2.562  50.497  19.532  1.00 31.76           C  
ATOM    705  N   THR A  93       3.975  48.986  22.414  1.00 19.53           N  
ATOM    706  CA  THR A  93       5.331  48.448  22.417  1.00 19.17           C  
ATOM    707  C   THR A  93       5.680  47.690  23.697  1.00 17.97           C  
ATOM    708  O   THR A  93       6.428  46.712  23.640  1.00 19.13           O  
ATOM    709  CB  THR A  93       6.391  49.549  22.171  1.00 16.36           C  
ATOM    710  OG1 THR A  93       6.284  50.576  23.162  1.00 15.88           O  
ATOM    711  CG2 THR A  93       6.222  50.155  20.778  1.00 16.58           C  
ATOM    712  N   THR A  94       5.163  48.109  24.852  1.00 16.77           N  
ATOM    713  CA  THR A  94       5.561  47.410  26.073  1.00 14.90           C  
ATOM    714  C   THR A  94       5.013  45.962  26.104  1.00 14.84           C  
ATOM    715  O   THR A  94       5.725  45.063  26.547  1.00 17.00           O  
ATOM    716  CB  THR A  94       5.192  48.217  27.390  1.00 17.90           C  
ATOM    717  OG1 THR A  94       3.803  48.556  27.444  1.00 18.07           O  
ATOM    718  CG2 THR A  94       5.998  49.506  27.444  1.00 17.65           C  
ATOM    719  N   PRO A  95       3.787  45.706  25.596  1.00 15.89           N  
ATOM    720  CA  PRO A  95       3.455  44.276  25.508  1.00 17.37           C  
ATOM    721  C   PRO A  95       4.344  43.502  24.529  1.00 17.76           C  
ATOM    722  O   PRO A  95       4.614  42.320  24.756  1.00 18.13           O  
ATOM    723  CB  PRO A  95       1.999  44.277  25.024  1.00 18.04           C  
ATOM    724  CG  PRO A  95       1.457  45.588  25.524  1.00 20.10           C  
ATOM    725  CD  PRO A  95       2.600  46.554  25.373  1.00 18.41           C  
ATOM    726  N   LEU A  96       4.784  44.146  23.451  1.00 17.03           N  
ATOM    727  CA  LEU A  96       5.664  43.463  22.508  1.00 18.86           C  
ATOM    728  C   LEU A  96       7.031  43.209  23.137  1.00 17.64           C  
ATOM    729  O   LEU A  96       7.644  42.178  22.891  1.00 16.96           O  
ATOM    730  CB  LEU A  96       5.820  44.271  21.213  1.00 18.60           C  
ATOM    731  CG  LEU A  96       4.571  44.381  20.340  1.00 21.58           C  
ATOM    732  CD1 LEU A  96       4.820  45.357  19.193  1.00 19.30           C  
ATOM    733  CD2 LEU A  96       4.175  43.011  19.794  1.00 23.87           C  
ATOM    734  N   LEU A  97       7.503  44.147  23.953  1.00 16.09           N  
ATOM    735  CA  LEU A  97       8.793  43.978  24.628  1.00 14.30           C  
ATOM    736  C   LEU A  97       8.734  42.806  25.601  1.00 15.28           C  
ATOM    737  O   LEU A  97       9.693  42.036  25.712  1.00 16.84           O  
ATOM    738  CB  LEU A  97       9.209  45.271  25.349  1.00 14.37           C  
ATOM    739  CG  LEU A  97       9.658  46.402  24.401  1.00 15.40           C  
ATOM    740  CD1 LEU A  97       9.642  47.760  25.111  1.00 16.80           C  
ATOM    741  CD2 LEU A  97      11.047  46.125  23.847  1.00 17.49           C  
ATOM    742  N   LEU A  98       7.605  42.648  26.286  1.00 15.32           N  
ATOM    743  CA  LEU A  98       7.425  41.489  27.156  1.00 14.90           C  
ATOM    744  C   LEU A  98       7.330  40.217  26.322  1.00 17.42           C  
ATOM    745  O   LEU A  98       7.846  39.166  26.715  1.00 15.34           O  
ATOM    746  CB  LEU A  98       6.166  41.634  28.026  1.00 17.68           C  
ATOM    747  CG  LEU A  98       6.198  42.788  29.038  1.00 18.25           C  
ATOM    748  CD1 LEU A  98       4.908  42.831  29.837  1.00 18.67           C  
ATOM    749  CD2 LEU A  98       7.397  42.644  29.972  1.00 18.26           C  
ATOM    750  N   LEU A  99       6.672  40.321  25.173  1.00 18.51           N  
ATOM    751  CA  LEU A  99       6.471  39.153  24.318  1.00 20.43           C  
ATOM    752  C   LEU A  99       7.819  38.585  23.880  1.00 19.25           C  
ATOM    753  O   LEU A  99       7.960  37.375  23.763  1.00 17.99           O  
ATOM    754  CB  LEU A  99       5.609  39.505  23.101  1.00 22.17           C  
ATOM    755  CG  LEU A  99       5.352  38.352  22.123  1.00 22.71           C  
ATOM    756  CD1 LEU A  99       4.605  37.205  22.814  1.00 22.05           C  
ATOM    757  CD2 LEU A  99       4.581  38.850  20.908  1.00 21.44           C  
ATOM    758  N   ASP A 100       8.805  39.460  23.657  1.00 17.92           N  
ATOM    759  CA  ASP A 100      10.173  39.032  23.320  1.00 19.03           C  
ATOM    760  C   ASP A 100      10.658  37.918  24.257  1.00 19.16           C  
ATOM    761  O   ASP A 100      11.236  36.923  23.814  1.00 20.78           O  
ATOM    762  CB  ASP A 100      11.155  40.212  23.396  1.00 17.13           C  
ATOM    763  CG  ASP A 100      11.361  40.912  22.052  1.00 20.32           C  
ATOM    764  OD1 ASP A 100      11.256  40.239  21.004  1.00 20.17           O  
ATOM    765  OD2 ASP A 100      11.666  42.134  22.053  1.00 19.03           O  
ATOM    766  N   LEU A 101      10.419  38.108  25.551  1.00 17.46           N  
ATOM    767  CA  LEU A 101      10.869  37.172  26.581  1.00 19.91           C  
ATOM    768  C   LEU A 101       9.861  36.045  26.819  1.00 18.01           C  
ATOM    769  O   LEU A 101      10.252  34.899  27.097  1.00 19.27           O  
ATOM    770  CB  LEU A 101      11.144  37.921  27.897  1.00 21.17           C  
ATOM    771  CG  LEU A 101      12.337  38.884  27.885  1.00 21.65           C  
ATOM    772  CD1 LEU A 101      12.536  39.570  29.248  1.00 20.71           C  
ATOM    773  CD2 LEU A 101      13.620  38.189  27.435  1.00 23.76           C  
ATOM    774  N   VAL A 102       8.571  36.364  26.729  1.00 15.86           N  
ATOM    775  CA  VAL A 102       7.519  35.348  26.908  1.00 18.37           C  
ATOM    776  C   VAL A 102       7.691  34.210  25.884  1.00 20.96           C  
ATOM    777  O   VAL A 102       7.421  33.031  26.179  1.00 22.31           O  
ATOM    778  CB  VAL A 102       6.103  35.973  26.774  1.00 20.98           C  
ATOM    779  CG1 VAL A 102       5.030  34.898  26.659  1.00 24.74           C  
ATOM    780  CG2 VAL A 102       5.799  36.908  27.959  1.00 21.86           C  
ATOM    781  N   LEU A 103       8.164  34.565  24.686  1.00 20.16           N  
ATOM    782  CA  LEU A 103       8.404  33.586  23.625  1.00 22.35           C  
ATOM    783  C   LEU A 103       9.484  32.573  24.015  1.00 24.27           C  
ATOM    784  O   LEU A 103       9.567  31.494  23.433  1.00 25.57           O  
ATOM    785  CB  LEU A 103       8.791  34.301  22.311  1.00 20.17           C  
ATOM    786  CG  LEU A 103       7.628  35.023  21.619  1.00 21.68           C  
ATOM    787  CD1 LEU A 103       8.116  35.890  20.458  1.00 20.80           C  
ATOM    788  CD2 LEU A 103       6.569  34.029  21.138  1.00 25.20           C  
ATOM    789  N   LEU A 104      10.304  32.918  25.004  1.00 23.20           N  
ATOM    790  CA  LEU A 104      11.332  32.001  25.495  1.00 23.67           C  
ATOM    791  C   LEU A 104      10.828  31.098  26.627  1.00 25.95           C  
ATOM    792  O   LEU A 104      11.610  30.377  27.236  1.00 27.66           O  
ATOM    793  CB  LEU A 104      12.552  32.784  25.982  1.00 25.14           C  
ATOM    794  CG  LEU A 104      13.239  33.670  24.945  1.00 29.25           C  
ATOM    795  CD1 LEU A 104      14.381  34.446  25.593  1.00 29.76           C  
ATOM    796  CD2 LEU A 104      13.742  32.802  23.800  1.00 30.68           C  
ATOM    797  N   THR A 105       9.531  31.152  26.913  1.00 24.05           N  
ATOM    798  CA  THR A 105       8.960  30.401  28.031  1.00 23.17           C  
ATOM    799  C   THR A 105       7.803  29.509  27.610  1.00 26.03           C  
ATOM    800  O   THR A 105       7.297  29.621  26.493  1.00 27.53           O  
ATOM    801  CB  THR A 105       8.421  31.336  29.135  1.00 22.74           C  
ATOM    802  OG1 THR A 105       7.149  31.856  28.726  1.00 22.63           O  
ATOM    803  CG2 THR A 105       9.368  32.491  29.381  1.00 21.59           C  
ATOM    804  N   ASN A 106       7.376  28.641  28.528  1.00 25.01           N  
ATOM    805  CA  ASN A 106       6.122  27.921  28.374  1.00 29.43           C  
ATOM    806  C   ASN A 106       5.034  28.428  29.326  1.00 28.03           C  
ATOM    807  O   ASN A 106       4.309  27.629  29.921  1.00 29.48           O  
ATOM    808  CB  ASN A 106       6.330  26.417  28.587  1.00 33.50           C  
ATOM    809  CG  ASN A 106       7.091  25.761  27.446  1.00 39.07           C  
ATOM    810  OD1 ASN A 106       6.976  26.167  26.289  1.00 37.44           O  
ATOM    811  ND2 ASN A 106       7.869  24.732  27.769  1.00 41.89           N  
ATOM    812  N   MET A 107       4.907  29.746  29.476  1.00 26.51           N  
ATOM    813  CA  MET A 107       3.796  30.292  30.255  1.00 27.35           C  
ATOM    814  C   MET A 107       2.466  29.967  29.590  1.00 28.41           C  
ATOM    815  O   MET A 107       2.320  30.145  28.378  1.00 30.61           O  
ATOM    816  CB  MET A 107       3.899  31.814  30.406  1.00 28.30           C  
ATOM    817  CG  MET A 107       4.991  32.338  31.306  1.00 30.88           C  
ATOM    818  SD  MET A 107       4.753  34.138  31.427  1.00 39.43           S  
ATOM    819  CE  MET A 107       6.431  34.752  31.375  1.00 39.27           C  
ATOM    820  N   PRO A 108       1.481  29.524  30.378  1.00 29.50           N  
ATOM    821  CA  PRO A 108       0.136  29.286  29.843  1.00 30.88           C  
ATOM    822  C   PRO A 108      -0.564  30.599  29.483  1.00 31.40           C  
ATOM    823  O   PRO A 108      -0.195  31.663  30.008  1.00 26.92           O  
ATOM    824  CB  PRO A 108      -0.578  28.563  30.992  1.00 33.18           C  
ATOM    825  CG  PRO A 108       0.140  29.014  32.215  1.00 35.04           C  
ATOM    826  CD  PRO A 108       1.576  29.202  31.813  1.00 32.97           C  
ATOM    827  N   ALA A 109      -1.561  30.520  28.604  1.00 30.72           N  
ATOM    828  CA  ALA A 109      -2.230  31.716  28.086  1.00 30.24           C  
ATOM    829  C   ALA A 109      -2.851  32.562  29.197  1.00 30.28           C  
ATOM    830  O   ALA A 109      -2.808  33.791  29.141  1.00 28.16           O  
ATOM    831  CB  ALA A 109      -3.292  31.326  27.074  1.00 31.83           C  
ATOM    832  N   THR A 110      -3.425  31.902  30.201  1.00 29.33           N  
ATOM    833  CA  THR A 110      -4.016  32.608  31.335  1.00 31.12           C  
ATOM    834  C   THR A 110      -3.014  33.527  32.039  1.00 30.22           C  
ATOM    835  O   THR A 110      -3.356  34.646  32.440  1.00 30.75           O  
ATOM    836  CB  THR A 110      -4.598  31.625  32.372  1.00 35.63           C  
ATOM    837  OG1 THR A 110      -4.894  32.341  33.574  1.00 43.54           O  
ATOM    838  CG2 THR A 110      -3.602  30.528  32.694  1.00 32.16           C  
ATOM    839  N   MET A 111      -1.774  33.062  32.174  1.00 27.10           N  
ATOM    840  CA  MET A 111      -0.733  33.837  32.848  1.00 25.19           C  
ATOM    841  C   MET A 111      -0.236  35.009  31.990  1.00 26.05           C  
ATOM    842  O   MET A 111      -0.084  36.131  32.478  1.00 23.86           O  
ATOM    843  CB  MET A 111       0.433  32.921  33.224  1.00 26.53           C  
ATOM    844  CG  MET A 111       1.578  33.637  33.936  1.00 27.62           C  
ATOM    845  SD  MET A 111       2.790  32.459  34.590  1.00 34.34           S  
ATOM    846  CE  MET A 111       3.895  33.580  35.448  1.00 30.58           C  
ATOM    847  N   ILE A 112       0.022  34.744  30.710  1.00 22.94           N  
ATOM    848  CA  ILE A 112       0.387  35.808  29.779  1.00 21.56           C  
ATOM    849  C   ILE A 112      -0.686  36.907  29.805  1.00 21.50           C  
ATOM    850  O   ILE A 112      -0.375  38.101  29.817  1.00 21.39           O  
ATOM    851  CB  ILE A 112       0.575  35.261  28.342  1.00 19.81           C  
ATOM    852  CG1 ILE A 112       1.675  34.192  28.336  1.00 18.89           C  
ATOM    853  CG2 ILE A 112       0.917  36.409  27.368  1.00 20.26           C  
ATOM    854  CD1 ILE A 112       1.700  33.322  27.057  1.00 22.04           C  
ATOM    855  N   ALA A 113      -1.945  36.487  29.866  1.00 25.07           N  
ATOM    856  CA  ALA A 113      -3.085  37.404  29.901  1.00 26.17           C  
ATOM    857  C   ALA A 113      -3.033  38.425  31.047  1.00 25.01           C  
ATOM    858  O   ALA A 113      -3.228  39.622  30.820  1.00 23.77           O  
ATOM    859  CB  ALA A 113      -4.386  36.606  29.981  1.00 26.67           C  
ATOM    860  N   TRP A 114      -2.791  37.979  32.277  1.00 22.00           N  
ATOM    861  CA  TRP A 114      -2.802  38.959  33.364  1.00 21.25           C  
ATOM    862  C   TRP A 114      -1.506  39.776  33.416  1.00 20.83           C  
ATOM    863  O   TRP A 114      -1.512  40.926  33.880  1.00 21.68           O  
ATOM    864  CB  TRP A 114      -3.115  38.311  34.728  1.00 24.23           C  
ATOM    865  CG  TRP A 114      -2.188  37.260  35.317  1.00 25.14           C  
ATOM    866  CD1 TRP A 114      -2.408  35.910  35.357  1.00 26.10           C  
ATOM    867  CD2 TRP A 114      -0.958  37.483  36.033  1.00 23.54           C  
ATOM    868  NE1 TRP A 114      -1.380  35.278  36.017  1.00 27.40           N  
ATOM    869  CE2 TRP A 114      -0.478  36.220  36.443  1.00 25.17           C  
ATOM    870  CE3 TRP A 114      -0.209  38.622  36.349  1.00 24.86           C  
ATOM    871  CZ2 TRP A 114       0.714  36.066  37.155  1.00 23.94           C  
ATOM    872  CZ3 TRP A 114       0.984  38.467  37.050  1.00 22.73           C  
ATOM    873  CH2 TRP A 114       1.430  37.197  37.445  1.00 23.24           C  
ATOM    874  N   ILE A 115      -0.411  39.220  32.903  1.00 18.91           N  
ATOM    875  CA  ILE A 115       0.831  39.985  32.816  1.00 17.93           C  
ATOM    876  C   ILE A 115       0.643  41.122  31.815  1.00 21.08           C  
ATOM    877  O   ILE A 115       0.993  42.275  32.083  1.00 19.83           O  
ATOM    878  CB  ILE A 115       2.036  39.105  32.394  1.00 18.97           C  
ATOM    879  CG1 ILE A 115       2.470  38.203  33.554  1.00 23.19           C  
ATOM    880  CG2 ILE A 115       3.204  39.976  31.936  1.00 17.28           C  
ATOM    881  CD1 ILE A 115       3.472  37.131  33.154  1.00 23.59           C  
ATOM    882  N   MET A 116       0.069  40.798  30.662  1.00 23.65           N  
ATOM    883  CA  MET A 116      -0.154  41.803  29.629  1.00 23.21           C  
ATOM    884  C   MET A 116      -1.214  42.808  30.078  1.00 23.35           C  
ATOM    885  O   MET A 116      -1.146  43.991  29.742  1.00 22.63           O  
ATOM    886  CB  MET A 116      -0.570  41.139  28.313  1.00 24.26           C  
ATOM    887  CG  MET A 116       0.498  40.231  27.731  1.00 25.03           C  
ATOM    888  SD  MET A 116       1.928  41.153  27.153  1.00 29.75           S  
ATOM    889  CE  MET A 116       3.002  39.812  26.634  1.00 30.41           C  
ATOM    890  N   GLY A 117      -2.192  42.328  30.839  1.00 23.79           N  
ATOM    891  CA  GLY A 117      -3.251  43.175  31.354  1.00 25.20           C  
ATOM    892  C   GLY A 117      -2.728  44.211  32.334  1.00 24.44           C  
ATOM    893  O   GLY A 117      -3.113  45.386  32.273  1.00 23.57           O  
ATOM    894  N   ALA A 118      -1.844  43.781  33.232  1.00 21.99           N  
ATOM    895  CA  ALA A 118      -1.206  44.698  34.179  1.00 22.60           C  
ATOM    896  C   ALA A 118      -0.409  45.758  33.418  1.00 19.28           C  
ATOM    897  O   ALA A 118      -0.434  46.947  33.762  1.00 18.36           O  
ATOM    898  CB  ALA A 118      -0.299  43.937  35.144  1.00 22.70           C  
ATOM    899  N   ASP A 119       0.287  45.308  32.379  1.00 18.01           N  
ATOM    900  CA  ASP A 119       1.113  46.191  31.560  1.00 18.96           C  
ATOM    901  C   ASP A 119       0.264  47.270  30.904  1.00 18.35           C  
ATOM    902  O   ASP A 119       0.602  48.443  30.944  1.00 17.04           O  
ATOM    903  CB  ASP A 119       1.860  45.402  30.486  1.00 19.14           C  
ATOM    904  CG  ASP A 119       2.746  46.298  29.620  1.00 20.57           C  
ATOM    905  OD1 ASP A 119       3.959  46.364  29.899  1.00 20.09           O  
ATOM    906  OD2 ASP A 119       2.225  46.945  28.682  1.00 20.67           O  
ATOM    907  N   ILE A 120      -0.841  46.872  30.293  1.00 19.05           N  
ATOM    908  CA  ILE A 120      -1.709  47.845  29.638  1.00 20.74           C  
ATOM    909  C   ILE A 120      -2.345  48.805  30.663  1.00 22.31           C  
ATOM    910  O   ILE A 120      -2.431  50.016  30.427  1.00 21.88           O  
ATOM    911  CB  ILE A 120      -2.796  47.130  28.809  1.00 22.82           C  
ATOM    912  CG1 ILE A 120      -2.147  46.436  27.600  1.00 25.24           C  
ATOM    913  CG2 ILE A 120      -3.872  48.112  28.356  1.00 22.76           C  
ATOM    914  CD1 ILE A 120      -3.010  45.345  26.978  1.00 27.32           C  
ATOM    915  N   ALA A 121      -2.761  48.270  31.809  1.00 20.81           N  
ATOM    916  CA  ALA A 121      -3.301  49.094  32.891  1.00 20.96           C  
ATOM    917  C   ALA A 121      -2.304  50.158  33.338  1.00 17.87           C  
ATOM    918  O   ALA A 121      -2.669  51.314  33.560  1.00 19.76           O  
ATOM    919  CB  ALA A 121      -3.699  48.215  34.077  1.00 19.32           C  
ATOM    920  N   MET A 122      -1.048  49.752  33.475  1.00 17.81           N  
ATOM    921  CA  MET A 122       0.031  50.644  33.890  1.00 18.75           C  
ATOM    922  C   MET A 122       0.110  51.875  32.975  1.00 19.60           C  
ATOM    923  O   MET A 122       0.188  53.017  33.429  1.00 19.85           O  
ATOM    924  CB  MET A 122       1.357  49.875  33.880  1.00 18.80           C  
ATOM    925  CG  MET A 122       2.599  50.695  34.174  1.00 19.39           C  
ATOM    926  SD  MET A 122       4.095  49.685  34.084  1.00 19.00           S  
ATOM    927  CE  MET A 122       4.305  49.517  32.299  1.00 18.12           C  
ATOM    928  N   ILE A 123       0.073  51.632  31.673  1.00 17.96           N  
ATOM    929  CA  ILE A 123       0.157  52.731  30.725  1.00 17.23           C  
ATOM    930  C   ILE A 123      -1.090  53.612  30.821  1.00 19.04           C  
ATOM    931  O   ILE A 123      -0.999  54.841  30.770  1.00 18.35           O  
ATOM    932  CB  ILE A 123       0.329  52.205  29.284  1.00 16.57           C  
ATOM    933  CG1 ILE A 123       1.528  51.254  29.219  1.00 17.71           C  
ATOM    934  CG2 ILE A 123       0.504  53.369  28.310  1.00 19.72           C  
ATOM    935  CD1 ILE A 123       2.840  51.890  29.674  1.00 16.15           C  
ATOM    936  N   ALA A 124      -2.248  52.974  30.976  1.00 20.52           N  
ATOM    937  CA  ALA A 124      -3.516  53.689  31.103  1.00 22.42           C  
ATOM    938  C   ALA A 124      -3.527  54.627  32.307  1.00 21.57           C  
ATOM    939  O   ALA A 124      -3.967  55.764  32.211  1.00 22.21           O  
ATOM    940  CB  ALA A 124      -4.673  52.703  31.204  1.00 21.72           C  
ATOM    941  N   PHE A 125      -3.056  54.144  33.452  1.00 20.73           N  
ATOM    942  CA  PHE A 125      -2.988  54.990  34.639  1.00 22.61           C  
ATOM    943  C   PHE A 125      -2.000  56.137  34.439  1.00 22.65           C  
ATOM    944  O   PHE A 125      -2.199  57.243  34.952  1.00 22.61           O  
ATOM    945  CB  PHE A 125      -2.606  54.163  35.865  1.00 23.49           C  
ATOM    946  CG  PHE A 125      -3.724  53.306  36.386  1.00 26.36           C  
ATOM    947  CD1 PHE A 125      -4.846  53.884  36.956  1.00 30.61           C  
ATOM    948  CD2 PHE A 125      -3.639  51.926  36.337  1.00 27.39           C  
ATOM    949  CE1 PHE A 125      -5.877  53.099  37.449  1.00 33.62           C  
ATOM    950  CE2 PHE A 125      -4.667  51.137  36.816  1.00 29.48           C  
ATOM    951  CZ  PHE A 125      -5.786  51.722  37.372  1.00 33.54           C  
ATOM    952  N   GLY A 126      -0.933  55.874  33.693  1.00 19.09           N  
ATOM    953  CA  GLY A 126       0.031  56.913  33.366  1.00 21.41           C  
ATOM    954  C   GLY A 126      -0.549  58.089  32.589  1.00 24.07           C  
ATOM    955  O   GLY A 126      -0.323  59.250  32.950  1.00 22.32           O  
ATOM    956  N   ILE A 127      -1.295  57.805  31.522  1.00 24.54           N  
ATOM    957  CA  ILE A 127      -1.836  58.887  30.698  1.00 21.89           C  
ATOM    958  C   ILE A 127      -2.974  59.617  31.417  1.00 22.22           C  
ATOM    959  O   ILE A 127      -3.101  60.834  31.296  1.00 22.70           O  
ATOM    960  CB  ILE A 127      -2.317  58.380  29.308  1.00 21.12           C  
ATOM    961  CG1 ILE A 127      -2.713  59.570  28.420  1.00 21.05           C  
ATOM    962  CG2 ILE A 127      -3.480  57.390  29.438  1.00 23.48           C  
ATOM    963  CD1 ILE A 127      -2.821  59.230  26.940  1.00 21.91           C  
ATOM    964  N   ILE A 128      -3.780  58.896  32.194  1.00 22.56           N  
ATOM    965  CA  ILE A 128      -4.829  59.547  32.977  1.00 23.80           C  
ATOM    966  C   ILE A 128      -4.195  60.475  34.013  1.00 23.37           C  
ATOM    967  O   ILE A 128      -4.615  61.625  34.175  1.00 23.82           O  
ATOM    968  CB  ILE A 128      -5.749  58.524  33.684  1.00 25.46           C  
ATOM    969  CG1 ILE A 128      -6.494  57.678  32.648  1.00 26.75           C  
ATOM    970  CG2 ILE A 128      -6.753  59.240  34.584  1.00 28.08           C  
ATOM    971  CD1 ILE A 128      -7.315  56.552  33.241  1.00 28.30           C  
ATOM    972  N   GLY A 129      -3.168  59.975  34.696  1.00 21.96           N  
ATOM    973  CA  GLY A 129      -2.454  60.771  35.675  1.00 22.13           C  
ATOM    974  C   GLY A 129      -1.816  61.987  35.029  1.00 23.76           C  
ATOM    975  O   GLY A 129      -1.793  63.067  35.621  1.00 25.29           O  
ATOM    976  N   ALA A 130      -1.308  61.817  33.805  1.00 21.80           N  
ATOM    977  CA  ALA A 130      -0.636  62.911  33.108  1.00 22.79           C  
ATOM    978  C   ALA A 130      -1.565  64.101  32.862  1.00 25.07           C  
ATOM    979  O   ALA A 130      -1.120  65.249  32.867  1.00 26.01           O  
ATOM    980  CB  ALA A 130      -0.051  62.421  31.793  1.00 22.46           C  
ATOM    981  N   PHE A 131      -2.853  63.832  32.661  1.00 23.96           N  
ATOM    982  CA  PHE A 131      -3.823  64.906  32.430  1.00 22.41           C  
ATOM    983  C   PHE A 131      -4.564  65.375  33.690  1.00 26.00           C  
ATOM    984  O   PHE A 131      -5.338  66.330  33.645  1.00 28.98           O  
ATOM    985  CB  PHE A 131      -4.841  64.462  31.380  1.00 23.22           C  
ATOM    986  CG  PHE A 131      -4.310  64.502  29.965  1.00 24.65           C  
ATOM    987  CD1 PHE A 131      -4.219  65.708  29.280  1.00 27.89           C  
ATOM    988  CD2 PHE A 131      -3.919  63.340  29.323  1.00 24.11           C  
ATOM    989  CE1 PHE A 131      -3.733  65.752  27.974  1.00 27.11           C  
ATOM    990  CE2 PHE A 131      -3.434  63.371  28.014  1.00 25.10           C  
ATOM    991  CZ  PHE A 131      -3.342  64.580  27.343  1.00 25.39           C  
ATOM    992  N   THR A 132      -4.322  64.708  34.810  1.00 22.77           N  
ATOM    993  CA  THR A 132      -5.015  65.021  36.064  1.00 24.92           C  
ATOM    994  C   THR A 132      -4.337  66.169  36.796  1.00 26.63           C  
ATOM    995  O   THR A 132      -3.134  66.135  37.052  1.00 28.99           O  
ATOM    996  CB  THR A 132      -5.073  63.780  36.985  1.00 24.49           C  
ATOM    997  OG1 THR A 132      -5.831  62.752  36.340  1.00 29.01           O  
ATOM    998  CG2 THR A 132      -5.726  64.111  38.334  1.00 24.43           C  
ATOM    999  N   VAL A 133      -5.112  67.195  37.120  1.00 28.66           N  
ATOM   1000  CA  VAL A 133      -4.601  68.314  37.886  1.00 29.43           C  
ATOM   1001  C   VAL A 133      -4.815  68.078  39.376  1.00 32.04           C  
ATOM   1002  O   VAL A 133      -5.908  67.727  39.811  1.00 34.36           O  
ATOM   1003  CB  VAL A 133      -5.280  69.631  37.457  1.00 31.69           C  
ATOM   1004  CG1 VAL A 133      -4.833  70.781  38.339  1.00 33.22           C  
ATOM   1005  CG2 VAL A 133      -4.979  69.919  35.986  1.00 33.46           C  
ATOM   1006  N   GLY A 134      -3.762  68.253  40.160  1.00 32.41           N  
ATOM   1007  CA  GLY A 134      -3.895  68.152  41.599  1.00 33.52           C  
ATOM   1008  C   GLY A 134      -3.569  66.779  42.153  1.00 32.23           C  
ATOM   1009  O   GLY A 134      -3.170  65.870  41.420  1.00 29.90           O  
ATOM   1010  N   SER A 135      -3.775  66.639  43.457  1.00 32.87           N  
ATOM   1011  CA  SER A 135      -3.280  65.499  44.229  1.00 33.71           C  
ATOM   1012  C   SER A 135      -3.793  64.122  43.827  1.00 30.86           C  
ATOM   1013  O   SER A 135      -3.129  63.122  44.100  1.00 31.39           O  
ATOM   1014  CB  SER A 135      -3.599  65.715  45.711  1.00 38.44           C  
ATOM   1015  OG  SER A 135      -2.943  66.867  46.195  1.00 44.38           O  
ATOM   1016  N   TYR A 136      -4.962  64.051  43.198  1.00 29.90           N  
ATOM   1017  CA  TYR A 136      -5.513  62.746  42.808  1.00 32.07           C  
ATOM   1018  C   TYR A 136      -4.665  62.042  41.754  1.00 30.75           C  
ATOM   1019  O   TYR A 136      -4.787  60.831  41.557  1.00 32.73           O  
ATOM   1020  CB  TYR A 136      -6.955  62.895  42.309  1.00 33.89           C  
ATOM   1021  CG  TYR A 136      -7.935  63.143  43.432  1.00 36.83           C  
ATOM   1022  CD1 TYR A 136      -7.950  62.331  44.559  1.00 36.94           C  
ATOM   1023  CD2 TYR A 136      -8.825  64.208  43.383  1.00 38.92           C  
ATOM   1024  CE1 TYR A 136      -8.839  62.564  45.598  1.00 37.61           C  
ATOM   1025  CE2 TYR A 136      -9.711  64.450  44.412  1.00 39.74           C  
ATOM   1026  CZ  TYR A 136      -9.717  63.625  45.516  1.00 40.16           C  
ATOM   1027  OH  TYR A 136     -10.603  63.877  46.538  1.00 42.46           O  
ATOM   1028  N   LYS A 137      -3.793  62.793  41.090  1.00 25.96           N  
ATOM   1029  CA  LYS A 137      -2.913  62.214  40.082  1.00 28.50           C  
ATOM   1030  C   LYS A 137      -2.042  61.114  40.690  1.00 26.52           C  
ATOM   1031  O   LYS A 137      -1.667  60.165  40.013  1.00 25.84           O  
ATOM   1032  CB  LYS A 137      -2.036  63.299  39.448  1.00 26.58           C  
ATOM   1033  CG  LYS A 137      -0.950  63.841  40.364  1.00 26.00           C  
ATOM   1034  CD  LYS A 137       0.046  64.710  39.593  1.00 29.37           C  
ATOM   1035  CE  LYS A 137      -0.521  66.089  39.285  1.00 33.58           C  
ATOM   1036  NZ  LYS A 137       0.287  66.814  38.233  1.00 34.24           N  
ATOM   1037  N   TRP A 138      -1.746  61.233  41.980  1.00 24.39           N  
ATOM   1038  CA  TRP A 138      -0.810  60.310  42.615  1.00 24.88           C  
ATOM   1039  C   TRP A 138      -1.455  58.962  42.918  1.00 25.62           C  
ATOM   1040  O   TRP A 138      -0.765  57.956  43.099  1.00 24.81           O  
ATOM   1041  CB  TRP A 138      -0.232  60.958  43.879  1.00 24.15           C  
ATOM   1042  CG  TRP A 138       0.585  62.163  43.531  1.00 23.35           C  
ATOM   1043  CD1 TRP A 138       0.276  63.470  43.786  1.00 26.41           C  
ATOM   1044  CD2 TRP A 138       1.825  62.178  42.801  1.00 23.91           C  
ATOM   1045  NE1 TRP A 138       1.259  64.299  43.276  1.00 25.03           N  
ATOM   1046  CE2 TRP A 138       2.220  63.527  42.672  1.00 24.20           C  
ATOM   1047  CE3 TRP A 138       2.648  61.181  42.263  1.00 20.99           C  
ATOM   1048  CZ2 TRP A 138       3.402  63.901  42.032  1.00 23.83           C  
ATOM   1049  CZ3 TRP A 138       3.819  61.556  41.628  1.00 22.69           C  
ATOM   1050  CH2 TRP A 138       4.181  62.905  41.507  1.00 21.77           C  
ATOM   1051  N   PHE A 139      -2.783  58.929  42.950  1.00 26.33           N  
ATOM   1052  CA  PHE A 139      -3.480  57.658  43.079  1.00 29.66           C  
ATOM   1053  C   PHE A 139      -3.259  56.831  41.812  1.00 25.17           C  
ATOM   1054  O   PHE A 139      -2.956  55.642  41.881  1.00 25.71           O  
ATOM   1055  CB  PHE A 139      -4.974  57.870  43.343  1.00 32.29           C  
ATOM   1056  CG  PHE A 139      -5.325  58.011  44.806  1.00 38.24           C  
ATOM   1057  CD1 PHE A 139      -4.904  57.066  45.736  1.00 39.71           C  
ATOM   1058  CD2 PHE A 139      -6.085  59.079  45.248  1.00 39.19           C  
ATOM   1059  CE1 PHE A 139      -5.228  57.190  47.071  1.00 40.21           C  
ATOM   1060  CE2 PHE A 139      -6.414  59.209  46.590  1.00 41.17           C  
ATOM   1061  CZ  PHE A 139      -5.982  58.264  47.502  1.00 41.80           C  
ATOM   1062  N   TYR A 140      -3.408  57.470  40.656  1.00 24.02           N  
ATOM   1063  CA  TYR A 140      -3.147  56.813  39.376  1.00 24.36           C  
ATOM   1064  C   TYR A 140      -1.705  56.347  39.295  1.00 22.97           C  
ATOM   1065  O   TYR A 140      -1.415  55.232  38.847  1.00 24.33           O  
ATOM   1066  CB  TYR A 140      -3.452  57.756  38.205  1.00 26.74           C  
ATOM   1067  CG  TYR A 140      -4.909  58.148  38.117  1.00 30.28           C  
ATOM   1068  CD1 TYR A 140      -5.877  57.207  37.798  1.00 32.68           C  
ATOM   1069  CD2 TYR A 140      -5.315  59.456  38.350  1.00 31.50           C  
ATOM   1070  CE1 TYR A 140      -7.208  57.549  37.721  1.00 35.48           C  
ATOM   1071  CE2 TYR A 140      -6.649  59.811  38.273  1.00 34.46           C  
ATOM   1072  CZ  TYR A 140      -7.590  58.851  37.959  1.00 37.28           C  
ATOM   1073  OH  TYR A 140      -8.917  59.188  37.875  1.00 40.28           O  
ATOM   1074  N   PHE A 141      -0.801  57.214  39.726  1.00 22.23           N  
ATOM   1075  CA  PHE A 141       0.622  56.913  39.695  1.00 21.32           C  
ATOM   1076  C   PHE A 141       0.942  55.681  40.526  1.00 19.96           C  
ATOM   1077  O   PHE A 141       1.620  54.763  40.060  1.00 20.30           O  
ATOM   1078  CB  PHE A 141       1.434  58.102  40.214  1.00 22.80           C  
ATOM   1079  CG  PHE A 141       2.917  57.867  40.211  1.00 21.99           C  
ATOM   1080  CD1 PHE A 141       3.616  57.794  39.006  1.00 20.75           C  
ATOM   1081  CD2 PHE A 141       3.617  57.719  41.400  1.00 21.80           C  
ATOM   1082  CE1 PHE A 141       4.980  57.593  38.984  1.00 20.54           C  
ATOM   1083  CE2 PHE A 141       4.992  57.511  41.389  1.00 23.23           C  
ATOM   1084  CZ  PHE A 141       5.675  57.440  40.171  1.00 20.02           C  
ATOM   1085  N   VAL A 142       0.467  55.671  41.767  1.00 21.17           N  
ATOM   1086  CA  VAL A 142       0.788  54.568  42.659  1.00 22.69           C  
ATOM   1087  C   VAL A 142       0.191  53.249  42.154  1.00 22.58           C  
ATOM   1088  O   VAL A 142       0.846  52.205  42.205  1.00 24.40           O  
ATOM   1089  CB  VAL A 142       0.318  54.874  44.091  1.00 26.03           C  
ATOM   1090  CG1 VAL A 142       0.442  53.647  44.972  1.00 28.13           C  
ATOM   1091  CG2 VAL A 142       1.148  56.024  44.651  1.00 26.26           C  
ATOM   1092  N   VAL A 143      -1.034  53.283  41.640  1.00 22.19           N  
ATOM   1093  CA  VAL A 143      -1.626  52.049  41.140  1.00 23.04           C  
ATOM   1094  C   VAL A 143      -0.843  51.568  39.908  1.00 21.82           C  
ATOM   1095  O   VAL A 143      -0.625  50.369  39.734  1.00 21.79           O  
ATOM   1096  CB  VAL A 143      -3.124  52.215  40.816  1.00 24.30           C  
ATOM   1097  CG1 VAL A 143      -3.670  50.951  40.176  1.00 28.36           C  
ATOM   1098  CG2 VAL A 143      -3.918  52.539  42.097  1.00 23.76           C  
ATOM   1099  N   GLY A 144      -0.374  52.501  39.080  1.00 19.44           N  
ATOM   1100  CA  GLY A 144       0.455  52.129  37.949  1.00 18.71           C  
ATOM   1101  C   GLY A 144       1.757  51.473  38.377  1.00 18.12           C  
ATOM   1102  O   GLY A 144       2.206  50.499  37.763  1.00 18.55           O  
ATOM   1103  N   CYS A 145       2.370  52.004  39.432  1.00 19.40           N  
ATOM   1104  CA  CYS A 145       3.584  51.409  39.993  1.00 19.46           C  
ATOM   1105  C   CYS A 145       3.359  49.993  40.517  1.00 21.37           C  
ATOM   1106  O   CYS A 145       4.224  49.128  40.357  1.00 18.64           O  
ATOM   1107  CB  CYS A 145       4.143  52.280  41.118  1.00 21.71           C  
ATOM   1108  SG  CYS A 145       4.854  53.852  40.547  1.00 21.54           S  
ATOM   1109  N   ILE A 146       2.219  49.762  41.172  1.00 20.57           N  
ATOM   1110  CA  ILE A 146       1.854  48.414  41.597  1.00 20.93           C  
ATOM   1111  C   ILE A 146       1.667  47.493  40.371  1.00 21.94           C  
ATOM   1112  O   ILE A 146       2.093  46.332  40.388  1.00 20.02           O  
ATOM   1113  CB  ILE A 146       0.587  48.442  42.488  1.00 21.60           C  
ATOM   1114  CG1 ILE A 146       0.857  49.293  43.738  1.00 22.25           C  
ATOM   1115  CG2 ILE A 146       0.172  47.021  42.893  1.00 23.11           C  
ATOM   1116  CD1 ILE A 146      -0.390  49.618  44.586  1.00 22.13           C  
ATOM   1117  N   MET A 147       1.083  48.012  39.289  1.00 20.94           N  
ATOM   1118  CA  MET A 147       0.962  47.221  38.056  1.00 21.39           C  
ATOM   1119  C   MET A 147       2.339  46.835  37.492  1.00 22.62           C  
ATOM   1120  O   MET A 147       2.509  45.750  36.948  1.00 16.31           O  
ATOM   1121  CB  MET A 147       0.164  47.976  36.976  1.00 21.93           C  
ATOM   1122  CG  MET A 147      -1.323  48.161  37.262  1.00 23.12           C  
ATOM   1123  SD  MET A 147      -2.228  46.615  37.522  1.00 26.17           S  
ATOM   1124  CE  MET A 147      -2.346  46.580  39.311  1.00 23.09           C  
ATOM   1125  N   LEU A 148       3.321  47.725  37.608  1.00 20.81           N  
ATOM   1126  CA  LEU A 148       4.684  47.383  37.177  1.00 18.30           C  
ATOM   1127  C   LEU A 148       5.239  46.245  38.048  1.00 20.44           C  
ATOM   1128  O   LEU A 148       5.899  45.322  37.553  1.00 19.09           O  
ATOM   1129  CB  LEU A 148       5.604  48.611  37.242  1.00 18.19           C  
ATOM   1130  CG  LEU A 148       7.079  48.434  36.868  1.00 18.05           C  
ATOM   1131  CD1 LEU A 148       7.223  47.742  35.511  1.00 18.55           C  
ATOM   1132  CD2 LEU A 148       7.810  49.802  36.863  1.00 21.19           C  
ATOM   1133  N   ALA A 149       4.963  46.305  39.349  1.00 18.49           N  
ATOM   1134  CA  ALA A 149       5.401  45.245  40.245  1.00 19.12           C  
ATOM   1135  C   ALA A 149       4.719  43.927  39.867  1.00 20.09           C  
ATOM   1136  O   ALA A 149       5.359  42.873  39.854  1.00 20.12           O  
ATOM   1137  CB  ALA A 149       5.108  45.612  41.720  1.00 18.46           C  
ATOM   1138  N   VAL A 150       3.428  43.993  39.539  1.00 19.52           N  
ATOM   1139  CA  VAL A 150       2.673  42.789  39.164  1.00 21.90           C  
ATOM   1140  C   VAL A 150       3.222  42.137  37.888  1.00 22.72           C  
ATOM   1141  O   VAL A 150       3.487  40.922  37.858  1.00 21.74           O  
ATOM   1142  CB  VAL A 150       1.167  43.101  38.963  1.00 22.02           C  
ATOM   1143  CG1 VAL A 150       0.465  41.953  38.226  1.00 23.19           C  
ATOM   1144  CG2 VAL A 150       0.487  43.381  40.322  1.00 22.92           C  
ATOM   1145  N   LEU A 151       3.399  42.934  36.835  1.00 20.02           N  
ATOM   1146  CA  LEU A 151       3.892  42.367  35.581  1.00 19.21           C  
ATOM   1147  C   LEU A 151       5.306  41.824  35.778  1.00 19.60           C  
ATOM   1148  O   LEU A 151       5.636  40.771  35.249  1.00 19.68           O  
ATOM   1149  CB  LEU A 151       3.840  43.395  34.442  1.00 18.25           C  
ATOM   1150  CG  LEU A 151       4.785  44.597  34.402  1.00 19.68           C  
ATOM   1151  CD1 LEU A 151       6.111  44.243  33.711  1.00 21.20           C  
ATOM   1152  CD2 LEU A 151       4.092  45.773  33.703  1.00 19.07           C  
ATOM   1153  N   ALA A 152       6.129  42.522  36.565  1.00 18.19           N  
ATOM   1154  CA  ALA A 152       7.495  42.059  36.837  1.00 19.65           C  
ATOM   1155  C   ALA A 152       7.494  40.720  37.572  1.00 19.57           C  
ATOM   1156  O   ALA A 152       8.253  39.811  37.229  1.00 20.51           O  
ATOM   1157  CB  ALA A 152       8.273  43.098  37.640  1.00 20.38           C  
ATOM   1158  N   TRP A 153       6.642  40.601  38.584  1.00 19.86           N  
ATOM   1159  CA  TRP A 153       6.507  39.345  39.309  1.00 21.16           C  
ATOM   1160  C   TRP A 153       6.174  38.189  38.369  1.00 21.68           C  
ATOM   1161  O   TRP A 153       6.785  37.120  38.438  1.00 21.00           O  
ATOM   1162  CB  TRP A 153       5.435  39.472  40.391  1.00 22.10           C  
ATOM   1163  CG  TRP A 153       5.124  38.176  41.063  1.00 25.07           C  
ATOM   1164  CD1 TRP A 153       3.931  37.516  41.056  1.00 26.51           C  
ATOM   1165  CD2 TRP A 153       6.029  37.363  41.820  1.00 26.33           C  
ATOM   1166  NE1 TRP A 153       4.027  36.352  41.783  1.00 26.73           N  
ATOM   1167  CE2 TRP A 153       5.306  36.234  42.263  1.00 27.74           C  
ATOM   1168  CE3 TRP A 153       7.376  37.485  42.176  1.00 26.98           C  
ATOM   1169  CZ2 TRP A 153       5.885  35.230  43.038  1.00 31.10           C  
ATOM   1170  CZ3 TRP A 153       7.950  36.482  42.961  1.00 29.06           C  
ATOM   1171  CH2 TRP A 153       7.203  35.372  43.376  1.00 31.66           C  
ATOM   1172  N   GLY A 154       5.209  38.402  37.479  1.00 20.08           N  
ATOM   1173  CA  GLY A 154       4.840  37.359  36.533  1.00 20.70           C  
ATOM   1174  C   GLY A 154       5.997  36.961  35.628  1.00 21.20           C  
ATOM   1175  O   GLY A 154       6.233  35.775  35.396  1.00 22.30           O  
ATOM   1176  N   MET A 155       6.730  37.954  35.131  1.00 18.23           N  
ATOM   1177  CA  MET A 155       7.849  37.706  34.216  1.00 17.90           C  
ATOM   1178  C   MET A 155       8.988  36.997  34.944  1.00 19.33           C  
ATOM   1179  O   MET A 155       9.761  36.243  34.354  1.00 19.82           O  
ATOM   1180  CB  MET A 155       8.344  39.025  33.601  1.00 16.06           C  
ATOM   1181  CG  MET A 155       7.329  39.687  32.667  1.00 17.36           C  
ATOM   1182  SD  MET A 155       6.883  38.670  31.238  1.00 20.93           S  
ATOM   1183  CE  MET A 155       8.449  38.655  30.349  1.00 23.64           C  
ATOM   1184  N   ILE A 156       9.064  37.218  36.247  1.00 17.88           N  
ATOM   1185  CA  ILE A 156      10.114  36.627  37.061  1.00 19.67           C  
ATOM   1186  C   ILE A 156       9.913  35.122  37.274  1.00 21.45           C  
ATOM   1187  O   ILE A 156      10.877  34.354  37.395  1.00 22.03           O  
ATOM   1188  CB  ILE A 156      10.185  37.367  38.429  1.00 33.88           C  
ATOM   1189  CG1 ILE A 156      10.941  38.674  38.250  1.00 34.83           C  
ATOM   1190  CG2 ILE A 156      10.903  36.572  39.468  1.00 35.50           C  
ATOM   1191  CD1 ILE A 156      12.209  38.467  37.550  1.00 36.67           C  
ATOM   1192  N   ASN A 157       8.659  34.690  37.307  1.00 22.48           N  
ATOM   1193  CA  ASN A 157       8.365  33.312  37.707  1.00 23.85           C  
ATOM   1194  C   ASN A 157       9.004  32.191  36.863  1.00 23.99           C  
ATOM   1195  O   ASN A 157       9.424  31.177  37.433  1.00 25.79           O  
ATOM   1196  CB  ASN A 157       6.846  33.109  37.776  1.00 24.00           C  
ATOM   1197  CG  ASN A 157       6.302  33.324  39.179  1.00 28.24           C  
ATOM   1198  OD1 ASN A 157       5.932  32.374  39.866  1.00 31.30           O  
ATOM   1199  ND2 ASN A 157       6.277  34.573  39.620  1.00 27.07           N  
ATOM   1200  N   PRO A 158       9.091  32.350  35.523  1.00 22.75           N  
ATOM   1201  CA  PRO A 158       9.769  31.283  34.766  1.00 24.96           C  
ATOM   1202  C   PRO A 158      11.228  31.066  35.158  1.00 26.19           C  
ATOM   1203  O   PRO A 158      11.789  30.029  34.829  1.00 30.85           O  
ATOM   1204  CB  PRO A 158       9.686  31.778  33.318  1.00 24.44           C  
ATOM   1205  CG  PRO A 158       8.465  32.600  33.283  1.00 25.73           C  
ATOM   1206  CD  PRO A 158       8.403  33.293  34.625  1.00 24.00           C  
ATOM   1207  N   ILE A 159      11.841  32.037  35.830  1.00 23.14           N  
ATOM   1208  CA  ILE A 159      13.226  31.883  36.249  1.00 25.33           C  
ATOM   1209  C   ILE A 159      13.396  30.721  37.224  1.00 28.47           C  
ATOM   1210  O   ILE A 159      14.364  29.961  37.130  1.00 30.15           O  
ATOM   1211  CB  ILE A 159      13.759  33.193  36.883  1.00 24.07           C  
ATOM   1212  CG1 ILE A 159      13.882  34.277  35.811  1.00 23.97           C  
ATOM   1213  CG2 ILE A 159      15.084  32.951  37.566  1.00 23.34           C  
ATOM   1214  CD1 ILE A 159      14.324  35.629  36.339  1.00 21.73           C  
ATOM   1215  N   PHE A 160      12.444  30.557  38.144  1.00 29.15           N  
ATOM   1216  CA  PHE A 160      12.568  29.522  39.169  1.00 29.19           C  
ATOM   1217  C   PHE A 160      11.419  28.510  39.179  1.00 29.75           C  
ATOM   1218  O   PHE A 160      11.367  27.637  40.047  1.00 32.60           O  
ATOM   1219  CB  PHE A 160      12.693  30.166  40.556  1.00 32.13           C  
ATOM   1220  CG  PHE A 160      11.645  31.199  40.835  1.00 34.01           C  
ATOM   1221  CD1 PHE A 160      10.407  30.833  41.330  1.00 36.76           C  
ATOM   1222  CD2 PHE A 160      11.898  32.540  40.589  1.00 34.93           C  
ATOM   1223  CE1 PHE A 160       9.440  31.787  41.583  1.00 38.69           C  
ATOM   1224  CE2 PHE A 160      10.936  33.494  40.842  1.00 35.42           C  
ATOM   1225  CZ  PHE A 160       9.706  33.119  41.335  1.00 37.05           C  
ATOM   1226  N   LYS A 161      10.502  28.619  38.223  1.00 31.77           N  
ATOM   1227  CA  LYS A 161       9.447  27.623  38.080  1.00 33.56           C  
ATOM   1228  C   LYS A 161       9.664  26.804  36.814  1.00 34.67           C  
ATOM   1229  O   LYS A 161       9.386  27.252  35.698  1.00 32.75           O  
ATOM   1230  CB  LYS A 161       8.072  28.281  38.077  1.00 37.21           C  
ATOM   1231  CG  LYS A 161       7.726  28.911  39.417  1.00 41.78           C  
ATOM   1232  CD  LYS A 161       6.235  29.110  39.577  1.00 45.44           C  
ATOM   1233  CE  LYS A 161       5.891  29.488  41.009  1.00 47.14           C  
ATOM   1234  NZ  LYS A 161       6.324  28.442  41.985  1.00 51.42           N  
ATOM   1235  N   GLU A 162      10.177  25.598  37.016  1.00 35.76           N  
ATOM   1236  CA  GLU A 162      10.583  24.711  35.939  1.00 39.94           C  
ATOM   1237  C   GLU A 162       9.435  24.383  34.984  1.00 38.64           C  
ATOM   1238  O   GLU A 162       9.658  24.190  33.790  1.00 39.61           O  
ATOM   1239  CB  GLU A 162      11.184  23.421  36.519  1.00 46.85           C  
ATOM   1240  CG  GLU A 162      10.542  22.917  37.819  1.00 54.13           C  
ATOM   1241  CD  GLU A 162      10.848  23.803  39.030  1.00 58.51           C  
ATOM   1242  OE1 GLU A 162      12.016  24.223  39.184  1.00 60.44           O  
ATOM   1243  OE2 GLU A 162       9.914  24.102  39.809  1.00 58.57           O  
ATOM   1244  N   GLU A 163       8.209  24.339  35.498  1.00 37.49           N  
ATOM   1245  CA  GLU A 163       7.056  24.007  34.661  1.00 40.56           C  
ATOM   1246  C   GLU A 163       6.745  25.116  33.647  1.00 38.44           C  
ATOM   1247  O   GLU A 163       6.055  24.877  32.652  1.00 40.15           O  
ATOM   1248  CB  GLU A 163       5.819  23.725  35.522  1.00 44.15           C  
ATOM   1249  CG  GLU A 163       5.288  24.926  36.292  1.00 45.46           C  
ATOM   1250  CD  GLU A 163       5.888  25.053  37.683  1.00 48.87           C  
ATOM   1251  OE1 GLU A 163       6.940  24.432  37.953  1.00 48.82           O  
ATOM   1252  OE2 GLU A 163       5.289  25.766  38.514  1.00 51.76           O  
ATOM   1253  N   LEU A 164       7.267  26.314  33.901  1.00 32.10           N  
ATOM   1254  CA  LEU A 164       7.082  27.468  33.009  1.00 32.76           C  
ATOM   1255  C   LEU A 164       8.234  27.628  32.021  1.00 33.62           C  
ATOM   1256  O   LEU A 164       8.238  28.552  31.207  1.00 32.16           O  
ATOM   1257  CB  LEU A 164       6.942  28.766  33.819  1.00 30.63           C  
ATOM   1258  CG  LEU A 164       5.788  28.848  34.819  1.00 32.81           C  
ATOM   1259  CD1 LEU A 164       5.715  30.235  35.455  1.00 30.45           C  
ATOM   1260  CD2 LEU A 164       4.469  28.473  34.144  1.00 33.87           C  
ATOM   1261  N   GLN A 165       9.217  26.740  32.105  1.00 35.37           N  
ATOM   1262  CA  GLN A 165      10.437  26.881  31.318  1.00 34.97           C  
ATOM   1263  C   GLN A 165      10.345  26.138  29.993  1.00 36.98           C  
ATOM   1264  O   GLN A 165       9.735  25.076  29.910  1.00 35.18           O  
ATOM   1265  CB  GLN A 165      11.643  26.388  32.122  1.00 36.04           C  
ATOM   1266  CG  GLN A 165      11.982  27.301  33.298  1.00 34.20           C  
ATOM   1267  CD  GLN A 165      13.171  26.830  34.121  1.00 37.09           C  
ATOM   1268  OE1 GLN A 165      13.641  25.701  33.973  1.00 40.24           O  
ATOM   1269  NE2 GLN A 165      13.672  27.709  34.987  1.00 37.62           N  
ATOM   1270  N   LYS A 166      10.957  26.710  28.958  1.00 36.68           N  
ATOM   1271  CA  LYS A 166      10.986  26.085  27.637  1.00 43.78           C  
ATOM   1272  C   LYS A 166      12.276  25.296  27.450  1.00 47.19           C  
ATOM   1273  O   LYS A 166      12.246  24.098  27.174  1.00 49.47           O  
ATOM   1274  CB  LYS A 166      10.840  27.145  26.542  1.00 44.90           C  
ATOM   1275  CG  LYS A 166      10.912  26.605  25.128  1.00 52.05           C  
ATOM   1276  CD  LYS A 166      10.335  27.612  24.139  1.00 55.42           C  
ATOM   1277  CE  LYS A 166       8.831  27.740  24.314  1.00 58.01           C  
ATOM   1278  NZ  LYS A 166       8.210  28.658  23.325  1.00 59.24           N  
ATOM   1279  N   HIS A 167      13.408  25.978  27.594  1.00 48.50           N  
ATOM   1280  CA  HIS A 167      14.715  25.326  27.591  1.00 54.02           C  
ATOM   1281  C   HIS A 167      15.500  25.769  28.824  1.00 53.94           C  
ATOM   1282  O   HIS A 167      15.999  26.895  28.888  1.00 50.14           O  
ATOM   1283  CB  HIS A 167      15.483  25.655  26.311  1.00 57.85           C  
ATOM   1284  CG  HIS A 167      14.776  25.238  25.054  1.00 63.08           C  
ATOM   1285  ND1 HIS A 167      14.520  26.119  24.027  1.00 63.97           N  
ATOM   1286  CD2 HIS A 167      14.286  24.040  24.659  1.00 66.54           C  
ATOM   1287  CE1 HIS A 167      13.890  25.483  23.053  1.00 65.98           C  
ATOM   1288  NE2 HIS A 167      13.737  24.223  23.409  1.00 68.18           N  
ATOM   1289  N   LYS A 168      15.597  24.871  29.800  1.00 56.57           N  
ATOM   1290  CA  LYS A 168      16.095  25.224  31.127  1.00 58.63           C  
ATOM   1291  C   LYS A 168      17.578  25.595  31.114  1.00 57.99           C  
ATOM   1292  O   LYS A 168      18.020  26.457  31.887  1.00 56.51           O  
ATOM   1293  CB  LYS A 168      15.837  24.075  32.102  1.00 63.20           C  
ATOM   1294  CG  LYS A 168      16.867  23.928  33.212  1.00 64.97           C  
ATOM   1295  CD  LYS A 168      16.739  22.592  33.915  1.00 68.94           C  
ATOM   1296  CE  LYS A 168      18.079  21.901  34.058  1.00 71.53           C  
ATOM   1297  NZ  LYS A 168      17.899  20.473  34.434  1.00 75.65           N  
ATOM   1298  N   GLU A 169      18.336  24.985  30.207  1.00 58.47           N  
ATOM   1299  CA  GLU A 169      19.779  25.198  30.158  1.00 56.00           C  
ATOM   1300  C   GLU A 169      20.150  26.642  29.841  1.00 49.41           C  
ATOM   1301  O   GLU A 169      21.312  27.023  29.959  1.00 48.93           O  
ATOM   1302  CB  GLU A 169      20.423  24.264  29.129  1.00 60.69           C  
ATOM   1303  CG  GLU A 169      20.330  22.782  29.473  1.00 66.86           C  
ATOM   1304  CD  GLU A 169      19.014  22.164  29.043  1.00 70.93           C  
ATOM   1305  OE1 GLU A 169      18.082  22.924  28.698  1.00 70.13           O  
ATOM   1306  OE2 GLU A 169      18.918  20.918  29.034  1.00 74.67           O  
ATOM   1307  N   TYR A 170      19.164  27.444  29.444  1.00 44.82           N  
ATOM   1308  CA  TYR A 170      19.424  28.827  29.067  1.00 44.51           C  
ATOM   1309  C   TYR A 170      18.600  29.832  29.888  1.00 39.96           C  
ATOM   1310  O   TYR A 170      18.274  30.933  29.436  1.00 39.95           O  
ATOM   1311  CB  TYR A 170      19.175  29.001  27.572  1.00 46.66           C  
ATOM   1312  CG  TYR A 170      20.133  28.170  26.753  1.00 51.97           C  
ATOM   1313  CD1 TYR A 170      21.386  28.661  26.400  1.00 53.93           C  
ATOM   1314  CD2 TYR A 170      19.800  26.878  26.362  1.00 55.91           C  
ATOM   1315  CE1 TYR A 170      22.274  27.893  25.662  1.00 57.41           C  
ATOM   1316  CE2 TYR A 170      20.679  26.105  25.624  1.00 59.64           C  
ATOM   1317  CZ  TYR A 170      21.912  26.616  25.277  1.00 60.66           C  
ATOM   1318  OH  TYR A 170      22.779  25.837  24.546  1.00 65.46           O  
ATOM   1319  N   THR A 171      18.293  29.442  31.118  1.00 37.76           N  
ATOM   1320  CA  THR A 171      17.650  30.324  32.085  1.00 35.24           C  
ATOM   1321  C   THR A 171      18.477  31.582  32.328  1.00 25.09           C  
ATOM   1322  O   THR A 171      17.937  32.657  32.614  1.00 23.54           O  
ATOM   1323  CB  THR A 171      17.432  29.574  33.414  1.00 33.92           C  
ATOM   1324  OG1 THR A 171      16.677  28.387  33.149  1.00 34.18           O  
ATOM   1325  CG2 THR A 171      16.699  30.444  34.420  1.00 33.49           C  
ATOM   1326  N   GLY A 172      19.794  31.445  32.201  1.00 25.77           N  
ATOM   1327  CA  GLY A 172      20.703  32.563  32.399  1.00 26.58           C  
ATOM   1328  C   GLY A 172      20.457  33.735  31.460  1.00 24.91           C  
ATOM   1329  O   GLY A 172      20.442  34.891  31.890  1.00 22.48           O  
ATOM   1330  N   ALA A 173      20.264  33.444  30.175  1.00 24.23           N  
ATOM   1331  CA  ALA A 173      20.014  34.502  29.202  1.00 23.82           C  
ATOM   1332  C   ALA A 173      18.688  35.199  29.490  1.00 25.31           C  
ATOM   1333  O   ALA A 173      18.603  36.432  29.472  1.00 25.27           O  
ATOM   1334  CB  ALA A 173      20.033  33.936  27.776  1.00 25.61           C  
ATOM   1335  N   TYR A 174      17.655  34.411  29.787  1.00 22.37           N  
ATOM   1336  CA  TYR A 174      16.352  34.971  30.155  1.00 23.14           C  
ATOM   1337  C   TYR A 174      16.469  35.887  31.381  1.00 22.81           C  
ATOM   1338  O   TYR A 174      15.960  37.018  31.393  1.00 20.03           O  
ATOM   1339  CB  TYR A 174      15.345  33.835  30.422  1.00 22.23           C  
ATOM   1340  CG  TYR A 174      13.945  34.302  30.782  1.00 21.39           C  
ATOM   1341  CD1 TYR A 174      12.955  34.414  29.810  1.00 23.14           C  
ATOM   1342  CD2 TYR A 174      13.606  34.610  32.098  1.00 21.10           C  
ATOM   1343  CE1 TYR A 174      11.668  34.837  30.135  1.00 20.93           C  
ATOM   1344  CE2 TYR A 174      12.326  35.040  32.433  1.00 21.65           C  
ATOM   1345  CZ  TYR A 174      11.355  35.142  31.448  1.00 21.08           C  
ATOM   1346  OH  TYR A 174      10.080  35.556  31.785  1.00 20.83           O  
ATOM   1347  N   THR A 175      17.148  35.393  32.410  1.00 21.58           N  
ATOM   1348  CA  THR A 175      17.320  36.141  33.655  1.00 20.94           C  
ATOM   1349  C   THR A 175      18.026  37.478  33.415  1.00 22.50           C  
ATOM   1350  O   THR A 175      17.580  38.531  33.877  1.00 22.41           O  
ATOM   1351  CB  THR A 175      18.111  35.299  34.684  1.00 22.27           C  
ATOM   1352  OG1 THR A 175      17.395  34.090  34.943  1.00 21.47           O  
ATOM   1353  CG2 THR A 175      18.305  36.057  36.000  1.00 22.82           C  
ATOM   1354  N   THR A 176      19.130  37.430  32.686  1.00 21.40           N  
ATOM   1355  CA  THR A 176      19.923  38.621  32.411  1.00 22.22           C  
ATOM   1356  C   THR A 176      19.134  39.685  31.627  1.00 20.96           C  
ATOM   1357  O   THR A 176      19.113  40.852  32.017  1.00 19.52           O  
ATOM   1358  CB  THR A 176      21.201  38.235  31.647  1.00 26.64           C  
ATOM   1359  OG1 THR A 176      21.959  37.321  32.456  1.00 30.53           O  
ATOM   1360  CG2 THR A 176      22.037  39.471  31.335  1.00 29.50           C  
ATOM   1361  N   LEU A 177      18.485  39.279  30.536  1.00 19.42           N  
ATOM   1362  CA  LEU A 177      17.636  40.192  29.750  1.00 18.41           C  
ATOM   1363  C   LEU A 177      16.492  40.791  30.560  1.00 18.23           C  
ATOM   1364  O   LEU A 177      16.150  41.961  30.410  1.00 19.73           O  
ATOM   1365  CB  LEU A 177      17.052  39.458  28.533  1.00 18.47           C  
ATOM   1366  CG  LEU A 177      18.056  39.165  27.421  1.00 22.15           C  
ATOM   1367  CD1 LEU A 177      17.483  38.115  26.469  1.00 24.01           C  
ATOM   1368  CD2 LEU A 177      18.410  40.450  26.665  1.00 22.46           C  
ATOM   1369  N   LEU A 178      15.884  39.976  31.414  1.00 18.74           N  
ATOM   1370  CA  LEU A 178      14.741  40.439  32.186  1.00 17.12           C  
ATOM   1371  C   LEU A 178      15.168  41.442  33.250  1.00 18.25           C  
ATOM   1372  O   LEU A 178      14.473  42.426  33.501  1.00 18.17           O  
ATOM   1373  CB  LEU A 178      14.017  39.260  32.839  1.00 17.43           C  
ATOM   1374  CG  LEU A 178      12.825  39.622  33.735  1.00 19.85           C  
ATOM   1375  CD1 LEU A 178      11.849  40.503  32.972  1.00 21.14           C  
ATOM   1376  CD2 LEU A 178      12.142  38.320  34.159  1.00 20.57           C  
ATOM   1377  N   ILE A 179      16.309  41.197  33.882  1.00 18.69           N  
ATOM   1378  CA  ILE A 179      16.782  42.132  34.909  1.00 19.02           C  
ATOM   1379  C   ILE A 179      17.133  43.464  34.264  1.00 17.68           C  
ATOM   1380  O   ILE A 179      16.798  44.525  34.790  1.00 18.84           O  
ATOM   1381  CB  ILE A 179      17.976  41.555  35.664  1.00 22.35           C  
ATOM   1382  CG1 ILE A 179      17.484  40.353  36.468  1.00 21.21           C  
ATOM   1383  CG2 ILE A 179      18.614  42.601  36.573  1.00 24.65           C  
ATOM   1384  CD1 ILE A 179      18.521  39.689  37.289  1.00 22.95           C  
ATOM   1385  N   TYR A 180      17.783  43.399  33.104  1.00 16.70           N  
ATOM   1386  CA  TYR A 180      18.059  44.588  32.307  1.00 18.28           C  
ATOM   1387  C   TYR A 180      16.768  45.353  32.004  1.00 19.39           C  
ATOM   1388  O   TYR A 180      16.701  46.571  32.186  1.00 17.75           O  
ATOM   1389  CB  TYR A 180      18.784  44.181  31.017  1.00 19.40           C  
ATOM   1390  CG  TYR A 180      19.038  45.304  30.027  1.00 17.64           C  
ATOM   1391  CD1 TYR A 180      20.149  46.134  30.144  1.00 19.74           C  
ATOM   1392  CD2 TYR A 180      18.184  45.503  28.949  1.00 17.08           C  
ATOM   1393  CE1 TYR A 180      20.381  47.169  29.199  1.00 20.10           C  
ATOM   1394  CE2 TYR A 180      18.409  46.515  28.018  1.00 19.24           C  
ATOM   1395  CZ  TYR A 180      19.500  47.343  28.152  1.00 19.85           C  
ATOM   1396  OH  TYR A 180      19.688  48.338  27.206  1.00 22.45           O  
ATOM   1397  N   LEU A 181      15.733  44.641  31.565  1.00 17.33           N  
ATOM   1398  CA  LEU A 181      14.440  45.272  31.286  1.00 17.55           C  
ATOM   1399  C   LEU A 181      13.828  45.934  32.540  1.00 17.93           C  
ATOM   1400  O   LEU A 181      13.360  47.072  32.492  1.00 16.35           O  
ATOM   1401  CB  LEU A 181      13.465  44.233  30.706  1.00 18.17           C  
ATOM   1402  CG  LEU A 181      12.043  44.677  30.331  1.00 18.99           C  
ATOM   1403  CD1 LEU A 181      11.527  43.816  29.162  1.00 21.93           C  
ATOM   1404  CD2 LEU A 181      11.060  44.619  31.505  1.00 17.89           C  
ATOM   1405  N   ILE A 182      13.808  45.212  33.649  1.00 18.44           N  
ATOM   1406  CA  ILE A 182      13.191  45.743  34.865  1.00 17.64           C  
ATOM   1407  C   ILE A 182      13.913  46.994  35.364  1.00 19.56           C  
ATOM   1408  O   ILE A 182      13.270  47.974  35.780  1.00 18.31           O  
ATOM   1409  CB  ILE A 182      13.160  44.680  35.971  1.00 18.09           C  
ATOM   1410  CG1 ILE A 182      12.179  43.570  35.581  1.00 19.52           C  
ATOM   1411  CG2 ILE A 182      12.751  45.308  37.310  1.00 17.23           C  
ATOM   1412  CD1 ILE A 182      12.205  42.365  36.513  1.00 20.48           C  
ATOM   1413  N   VAL A 183      15.243  46.962  35.336  1.00 18.57           N  
ATOM   1414  CA  VAL A 183      16.038  48.115  35.766  1.00 19.92           C  
ATOM   1415  C   VAL A 183      15.645  49.341  34.946  1.00 19.03           C  
ATOM   1416  O   VAL A 183      15.383  50.417  35.495  1.00 18.83           O  
ATOM   1417  CB  VAL A 183      17.558  47.857  35.616  1.00 22.87           C  
ATOM   1418  CG1 VAL A 183      18.347  49.172  35.667  1.00 26.82           C  
ATOM   1419  CG2 VAL A 183      18.052  46.875  36.667  1.00 22.33           C  
ATOM   1420  N   LEU A 184      15.589  49.179  33.627  1.00 18.10           N  
ATOM   1421  CA  LEU A 184      15.241  50.299  32.758  1.00 17.72           C  
ATOM   1422  C   LEU A 184      13.810  50.761  32.990  1.00 19.51           C  
ATOM   1423  O   LEU A 184      13.544  51.961  33.076  1.00 20.81           O  
ATOM   1424  CB  LEU A 184      15.425  49.931  31.280  1.00 16.70           C  
ATOM   1425  CG  LEU A 184      16.858  49.763  30.777  1.00 20.93           C  
ATOM   1426  CD1 LEU A 184      16.870  49.358  29.297  1.00 17.82           C  
ATOM   1427  CD2 LEU A 184      17.642  51.052  30.986  1.00 22.99           C  
ATOM   1428  N   TRP A 185      12.883  49.813  33.088  1.00 16.47           N  
ATOM   1429  CA  TRP A 185      11.471  50.177  33.191  1.00 14.81           C  
ATOM   1430  C   TRP A 185      11.154  50.912  34.488  1.00 17.94           C  
ATOM   1431  O   TRP A 185      10.269  51.754  34.504  1.00 18.96           O  
ATOM   1432  CB  TRP A 185      10.571  48.941  33.070  1.00 15.78           C  
ATOM   1433  CG  TRP A 185      10.453  48.410  31.627  1.00 15.53           C  
ATOM   1434  CD1 TRP A 185      11.390  48.481  30.642  1.00 17.55           C  
ATOM   1435  CD2 TRP A 185       9.312  47.755  31.053  1.00 17.53           C  
ATOM   1436  NE1 TRP A 185      10.915  47.892  29.485  1.00 18.50           N  
ATOM   1437  CE2 TRP A 185       9.643  47.428  29.721  1.00 16.30           C  
ATOM   1438  CE3 TRP A 185       8.054  47.378  31.555  1.00 17.78           C  
ATOM   1439  CZ2 TRP A 185       8.744  46.782  28.859  1.00 15.87           C  
ATOM   1440  CZ3 TRP A 185       7.160  46.730  30.703  1.00 16.06           C  
ATOM   1441  CH2 TRP A 185       7.519  46.424  29.373  1.00 16.98           C  
ATOM   1442  N   VAL A 186      11.868  50.601  35.566  1.00 15.03           N  
ATOM   1443  CA  VAL A 186      11.644  51.300  36.841  1.00 15.28           C  
ATOM   1444  C   VAL A 186      12.033  52.785  36.738  1.00 17.06           C  
ATOM   1445  O   VAL A 186      11.512  53.638  37.481  1.00 18.35           O  
ATOM   1446  CB  VAL A 186      12.425  50.629  38.003  1.00 20.49           C  
ATOM   1447  CG1 VAL A 186      12.463  51.525  39.255  1.00 20.88           C  
ATOM   1448  CG2 VAL A 186      11.798  49.286  38.345  1.00 19.59           C  
ATOM   1449  N   ILE A 187      12.928  53.116  35.811  1.00 17.61           N  
ATOM   1450  CA  ILE A 187      13.329  54.519  35.678  1.00 17.98           C  
ATOM   1451  C   ILE A 187      12.185  55.375  35.123  1.00 18.98           C  
ATOM   1452  O   ILE A 187      12.081  56.566  35.451  1.00 19.53           O  
ATOM   1453  CB  ILE A 187      14.571  54.700  34.776  1.00 21.35           C  
ATOM   1454  CG1 ILE A 187      15.683  53.728  35.179  1.00 24.13           C  
ATOM   1455  CG2 ILE A 187      15.082  56.151  34.838  1.00 19.54           C  
ATOM   1456  CD1 ILE A 187      16.129  53.892  36.582  1.00 24.69           C  
ATOM   1457  N   TYR A 188      11.323  54.783  34.296  1.00 15.18           N  
ATOM   1458  CA  TYR A 188      10.243  55.565  33.671  1.00 17.98           C  
ATOM   1459  C   TYR A 188       9.320  56.250  34.696  1.00 18.77           C  
ATOM   1460  O   TYR A 188       9.074  57.453  34.551  1.00 17.02           O  
ATOM   1461  CB  TYR A 188       9.409  54.711  32.711  1.00 16.03           C  
ATOM   1462  CG  TYR A 188      10.097  54.410  31.393  1.00 15.21           C  
ATOM   1463  CD1 TYR A 188      11.023  53.376  31.290  1.00 16.41           C  
ATOM   1464  CD2 TYR A 188       9.824  55.164  30.251  1.00 16.52           C  
ATOM   1465  CE1 TYR A 188      11.662  53.091  30.072  1.00 14.33           C  
ATOM   1466  CE2 TYR A 188      10.462  54.887  29.036  1.00 16.23           C  
ATOM   1467  CZ  TYR A 188      11.373  53.842  28.961  1.00 16.25           C  
ATOM   1468  OH  TYR A 188      11.997  53.560  27.759  1.00 16.52           O  
ATOM   1469  N   PRO A 189       8.811  55.514  35.718  1.00 17.53           N  
ATOM   1470  CA  PRO A 189       7.994  56.218  36.729  1.00 17.37           C  
ATOM   1471  C   PRO A 189       8.758  57.269  37.541  1.00 19.03           C  
ATOM   1472  O   PRO A 189       8.150  58.228  38.028  1.00 19.98           O  
ATOM   1473  CB  PRO A 189       7.496  55.083  37.653  1.00 17.37           C  
ATOM   1474  CG  PRO A 189       8.412  53.909  37.373  1.00 17.90           C  
ATOM   1475  CD  PRO A 189       8.777  54.049  35.921  1.00 16.15           C  
ATOM   1476  N   ILE A 190      10.066  57.098  37.702  1.00 19.25           N  
ATOM   1477  CA  ILE A 190      10.851  58.119  38.375  1.00 19.17           C  
ATOM   1478  C   ILE A 190      10.825  59.405  37.551  1.00 18.15           C  
ATOM   1479  O   ILE A 190      10.574  60.483  38.079  1.00 18.99           O  
ATOM   1480  CB  ILE A 190      12.304  57.675  38.613  1.00 19.35           C  
ATOM   1481  CG1 ILE A 190      12.331  56.378  39.436  1.00 20.91           C  
ATOM   1482  CG2 ILE A 190      13.078  58.797  39.317  1.00 22.61           C  
ATOM   1483  CD1 ILE A 190      13.733  55.839  39.730  1.00 21.21           C  
ATOM   1484  N   VAL A 191      11.069  59.283  36.248  1.00 17.05           N  
ATOM   1485  CA  VAL A 191      11.009  60.453  35.375  1.00 17.57           C  
ATOM   1486  C   VAL A 191       9.614  61.079  35.379  1.00 19.14           C  
ATOM   1487  O   VAL A 191       9.473  62.302  35.464  1.00 19.98           O  
ATOM   1488  CB  VAL A 191      11.408  60.087  33.929  1.00 18.74           C  
ATOM   1489  CG1 VAL A 191      11.289  61.309  33.019  1.00 19.12           C  
ATOM   1490  CG2 VAL A 191      12.826  59.545  33.917  1.00 18.50           C  
ATOM   1491  N   TRP A 192       8.586  60.242  35.284  1.00 19.31           N  
ATOM   1492  CA  TRP A 192       7.201  60.728  35.299  1.00 19.25           C  
ATOM   1493  C   TRP A 192       6.905  61.472  36.608  1.00 20.98           C  
ATOM   1494  O   TRP A 192       6.320  62.556  36.608  1.00 20.52           O  
ATOM   1495  CB  TRP A 192       6.230  59.552  35.124  1.00 17.33           C  
ATOM   1496  CG  TRP A 192       4.762  59.911  34.883  1.00 19.74           C  
ATOM   1497  CD1 TRP A 192       4.107  59.880  33.682  1.00 20.19           C  
ATOM   1498  CD2 TRP A 192       3.783  60.319  35.858  1.00 22.58           C  
ATOM   1499  NE1 TRP A 192       2.790  60.236  33.848  1.00 18.75           N  
ATOM   1500  CE2 TRP A 192       2.566  60.517  35.171  1.00 19.21           C  
ATOM   1501  CE3 TRP A 192       3.815  60.535  37.243  1.00 22.47           C  
ATOM   1502  CZ2 TRP A 192       1.398  60.923  35.817  1.00 20.58           C  
ATOM   1503  CZ3 TRP A 192       2.657  60.940  37.883  1.00 25.27           C  
ATOM   1504  CH2 TRP A 192       1.461  61.126  37.173  1.00 25.49           C  
ATOM   1505  N   GLY A 193       7.312  60.880  37.726  1.00 19.89           N  
ATOM   1506  CA  GLY A 193       7.083  61.500  39.022  1.00 20.87           C  
ATOM   1507  C   GLY A 193       7.719  62.875  39.141  1.00 22.20           C  
ATOM   1508  O   GLY A 193       7.138  63.793  39.722  1.00 23.72           O  
ATOM   1509  N   LEU A 194       8.918  63.019  38.584  1.00 21.80           N  
ATOM   1510  CA  LEU A 194       9.639  64.282  38.649  1.00 23.16           C  
ATOM   1511  C   LEU A 194       9.072  65.306  37.662  1.00 23.71           C  
ATOM   1512  O   LEU A 194       9.129  66.510  37.910  1.00 25.35           O  
ATOM   1513  CB  LEU A 194      11.132  64.061  38.383  1.00 22.71           C  
ATOM   1514  CG  LEU A 194      11.885  63.211  39.412  1.00 24.11           C  
ATOM   1515  CD1 LEU A 194      13.251  62.773  38.883  1.00 23.69           C  
ATOM   1516  CD2 LEU A 194      12.035  63.963  40.731  1.00 28.32           C  
ATOM   1517  N   GLY A 195       8.523  64.821  36.550  1.00 23.85           N  
ATOM   1518  CA  GLY A 195       8.093  65.697  35.467  1.00 22.84           C  
ATOM   1519  C   GLY A 195       6.588  65.869  35.389  1.00 22.70           C  
ATOM   1520  O   GLY A 195       6.021  66.774  36.011  1.00 22.85           O  
ATOM   1521  N   ALA A 196       5.947  65.001  34.609  1.00 21.67           N  
ATOM   1522  CA  ALA A 196       4.486  64.978  34.464  1.00 20.60           C  
ATOM   1523  C   ALA A 196       3.754  65.081  35.804  1.00 23.47           C  
ATOM   1524  O   ALA A 196       2.742  65.778  35.921  1.00 26.06           O  
ATOM   1525  CB  ALA A 196       4.058  63.696  33.725  1.00 20.45           C  
ATOM   1526  N   GLY A 197       4.271  64.395  36.820  1.00 24.20           N  
ATOM   1527  CA  GLY A 197       3.645  64.413  38.132  1.00 24.62           C  
ATOM   1528  C   GLY A 197       3.981  65.632  38.974  1.00 26.22           C  
ATOM   1529  O   GLY A 197       3.103  66.450  39.279  1.00 27.98           O  
ATOM   1530  N   GLY A 198       5.252  65.763  39.347  1.00 26.68           N  
ATOM   1531  CA  GLY A 198       5.658  66.763  40.324  1.00 27.22           C  
ATOM   1532  C   GLY A 198       6.028  68.154  39.820  1.00 27.06           C  
ATOM   1533  O   GLY A 198       6.130  69.076  40.617  1.00 27.44           O  
ATOM   1534  N   HIS A 199       6.246  68.294  38.516  1.00 25.85           N  
ATOM   1535  CA  HIS A 199       6.673  69.565  37.909  1.00 27.33           C  
ATOM   1536  C   HIS A 199       8.009  70.012  38.525  1.00 27.61           C  
ATOM   1537  O   HIS A 199       8.221  71.207  38.799  1.00 27.20           O  
ATOM   1538  CB  HIS A 199       5.655  70.692  38.120  1.00 29.63           C  
ATOM   1539  CG  HIS A 199       4.323  70.462  37.486  1.00 34.73           C  
ATOM   1540  ND1 HIS A 199       3.269  71.345  37.593  1.00 37.90           N  
ATOM   1541  CD2 HIS A 199       3.881  69.448  36.701  1.00 40.78           C  
ATOM   1542  CE1 HIS A 199       2.237  70.881  36.917  1.00 40.23           C  
ATOM   1543  NE2 HIS A 199       2.574  69.723  36.380  1.00 41.25           N  
ATOM   1544  N   ILE A 200       8.892  69.049  38.756  1.00 27.16           N  
ATOM   1545  CA  ILE A 200      10.206  69.275  39.352  1.00 29.64           C  
ATOM   1546  C   ILE A 200      11.290  69.398  38.268  1.00 28.13           C  
ATOM   1547  O   ILE A 200      12.298  70.084  38.443  1.00 27.16           O  
ATOM   1548  CB  ILE A 200      10.555  68.120  40.324  1.00 35.71           C  
ATOM   1549  CG1 ILE A 200       9.491  68.040  41.415  1.00 40.81           C  
ATOM   1550  CG2 ILE A 200      11.935  68.288  40.913  1.00 39.69           C  
ATOM   1551  CD1 ILE A 200       9.258  69.356  42.108  1.00 42.38           C  
ATOM   1552  N   ILE A 201      11.079  68.707  37.155  1.00 23.10           N  
ATOM   1553  CA  ILE A 201      11.968  68.821  36.006  1.00 23.15           C  
ATOM   1554  C   ILE A 201      11.160  69.285  34.801  1.00 23.41           C  
ATOM   1555  O   ILE A 201       9.949  69.027  34.712  1.00 21.26           O  
ATOM   1556  CB  ILE A 201      12.689  67.493  35.688  1.00 22.29           C  
ATOM   1557  CG1 ILE A 201      11.676  66.406  35.316  1.00 22.40           C  
ATOM   1558  CG2 ILE A 201      13.532  67.059  36.879  1.00 24.14           C  
ATOM   1559  CD1 ILE A 201      12.308  65.103  34.837  1.00 22.38           C  
ATOM   1560  N   GLY A 202      11.839  69.992  33.902  1.00 22.09           N  
ATOM   1561  CA  GLY A 202      11.230  70.558  32.715  1.00 24.52           C  
ATOM   1562  C   GLY A 202      10.915  69.550  31.625  1.00 23.42           C  
ATOM   1563  O   GLY A 202      11.330  68.383  31.663  1.00 20.51           O  
ATOM   1564  N   VAL A 203      10.158  70.015  30.642  1.00 24.72           N  
ATOM   1565  CA  VAL A 203       9.679  69.146  29.587  1.00 22.62           C  
ATOM   1566  C   VAL A 203      10.839  68.658  28.711  1.00 20.25           C  
ATOM   1567  O   VAL A 203      10.899  67.471  28.406  1.00 23.22           O  
ATOM   1568  CB  VAL A 203       8.596  69.854  28.749  1.00 24.39           C  
ATOM   1569  CG1 VAL A 203       8.309  69.084  27.456  1.00 26.14           C  
ATOM   1570  CG2 VAL A 203       7.327  70.012  29.585  1.00 25.61           C  
ATOM   1571  N   ASP A 204      11.770  69.541  28.339  1.00 23.08           N  
ATOM   1572  CA  ASP A 204      12.927  69.119  27.518  1.00 23.19           C  
ATOM   1573  C   ASP A 204      13.757  68.062  28.242  1.00 23.57           C  
ATOM   1574  O   ASP A 204      14.202  67.089  27.635  1.00 19.40           O  
ATOM   1575  CB  ASP A 204      13.830  70.308  27.158  1.00 24.36           C  
ATOM   1576  CG  ASP A 204      13.196  71.252  26.170  1.00 27.60           C  
ATOM   1577  OD1 ASP A 204      12.336  70.812  25.374  1.00 27.58           O  
ATOM   1578  OD2 ASP A 204      13.569  72.448  26.184  1.00 32.14           O  
ATOM   1579  N   VAL A 205      13.954  68.250  29.548  1.00 21.35           N  
ATOM   1580  CA  VAL A 205      14.701  67.273  30.344  1.00 21.62           C  
ATOM   1581  C   VAL A 205      14.002  65.905  30.375  1.00 20.47           C  
ATOM   1582  O   VAL A 205      14.645  64.864  30.223  1.00 19.62           O  
ATOM   1583  CB  VAL A 205      14.915  67.774  31.794  1.00 25.79           C  
ATOM   1584  CG1 VAL A 205      15.500  66.674  32.655  1.00 27.29           C  
ATOM   1585  CG2 VAL A 205      15.833  68.985  31.805  1.00 30.13           C  
ATOM   1586  N   GLU A 206      12.686  65.903  30.578  1.00 17.62           N  
ATOM   1587  CA  GLU A 206      11.936  64.653  30.572  1.00 19.65           C  
ATOM   1588  C   GLU A 206      12.037  63.997  29.195  1.00 18.72           C  
ATOM   1589  O   GLU A 206      12.122  62.775  29.093  1.00 16.84           O  
ATOM   1590  CB  GLU A 206      10.468  64.887  30.955  1.00 24.23           C  
ATOM   1591  CG  GLU A 206       9.528  64.971  29.761  1.00 29.21           C  
ATOM   1592  CD  GLU A 206       8.120  65.376  30.118  1.00 29.84           C  
ATOM   1593  OE1 GLU A 206       7.800  65.433  31.329  1.00 22.14           O  
ATOM   1594  OE2 GLU A 206       7.339  65.628  29.172  1.00 33.24           O  
ATOM   1595  N   ILE A 207      12.062  64.811  28.141  1.00 17.91           N  
ATOM   1596  CA  ILE A 207      12.134  64.280  26.775  1.00 17.77           C  
ATOM   1597  C   ILE A 207      13.450  63.555  26.564  1.00 20.48           C  
ATOM   1598  O   ILE A 207      13.492  62.431  26.034  1.00 19.76           O  
ATOM   1599  CB  ILE A 207      11.992  65.386  25.729  1.00 18.62           C  
ATOM   1600  CG1 ILE A 207      10.555  65.915  25.685  1.00 19.09           C  
ATOM   1601  CG2 ILE A 207      12.435  64.883  24.343  1.00 19.67           C  
ATOM   1602  CD1 ILE A 207      10.392  67.166  24.828  1.00 21.23           C  
ATOM   1603  N   ILE A 208      14.526  64.209  26.980  1.00 18.91           N  
ATOM   1604  CA  ILE A 208      15.865  63.655  26.830  1.00 20.03           C  
ATOM   1605  C   ILE A 208      16.024  62.379  27.661  1.00 19.50           C  
ATOM   1606  O   ILE A 208      16.557  61.378  27.176  1.00 18.44           O  
ATOM   1607  CB  ILE A 208      16.925  64.703  27.226  1.00 21.65           C  
ATOM   1608  CG1 ILE A 208      16.988  65.803  26.155  1.00 20.81           C  
ATOM   1609  CG2 ILE A 208      18.293  64.070  27.397  1.00 20.39           C  
ATOM   1610  CD1 ILE A 208      17.693  67.082  26.618  1.00 25.43           C  
ATOM   1611  N   ALA A 209      15.548  62.405  28.901  1.00 19.44           N  
ATOM   1612  CA  ALA A 209      15.651  61.233  29.775  1.00 17.95           C  
ATOM   1613  C   ALA A 209      14.949  60.016  29.175  1.00 19.51           C  
ATOM   1614  O   ALA A 209      15.497  58.914  29.154  1.00 18.28           O  
ATOM   1615  CB  ALA A 209      15.075  61.543  31.158  1.00 14.73           C  
ATOM   1616  N   MET A 210      13.733  60.212  28.681  1.00 17.22           N  
ATOM   1617  CA  MET A 210      12.989  59.091  28.128  1.00 17.68           C  
ATOM   1618  C   MET A 210      13.507  58.713  26.745  1.00 17.94           C  
ATOM   1619  O   MET A 210      13.363  57.563  26.335  1.00 21.15           O  
ATOM   1620  CB  MET A 210      11.497  59.400  28.084  1.00 16.89           C  
ATOM   1621  CG  MET A 210      10.845  59.286  29.477  1.00 17.71           C  
ATOM   1622  SD  MET A 210       9.101  59.642  29.408  1.00 26.44           S  
ATOM   1623  CE  MET A 210       9.170  61.419  29.542  1.00 34.34           C  
ATOM   1624  N   GLY A 211      14.136  59.656  26.047  1.00 16.73           N  
ATOM   1625  CA  GLY A 211      14.807  59.335  24.794  1.00 19.52           C  
ATOM   1626  C   GLY A 211      15.932  58.338  25.024  1.00 19.00           C  
ATOM   1627  O   GLY A 211      16.074  57.348  24.298  1.00 19.55           O  
ATOM   1628  N   ILE A 212      16.744  58.608  26.039  1.00 17.21           N  
ATOM   1629  CA  ILE A 212      17.839  57.719  26.407  1.00 18.24           C  
ATOM   1630  C   ILE A 212      17.291  56.342  26.823  1.00 18.02           C  
ATOM   1631  O   ILE A 212      17.750  55.297  26.334  1.00 17.29           O  
ATOM   1632  CB  ILE A 212      18.689  58.335  27.542  1.00 18.32           C  
ATOM   1633  CG1 ILE A 212      19.453  59.568  27.022  1.00 19.71           C  
ATOM   1634  CG2 ILE A 212      19.678  57.319  28.108  1.00 19.95           C  
ATOM   1635  CD1 ILE A 212      19.987  60.457  28.145  1.00 23.62           C  
ATOM   1636  N   LEU A 213      16.302  56.342  27.708  1.00 16.53           N  
ATOM   1637  CA  LEU A 213      15.673  55.090  28.141  1.00 16.37           C  
ATOM   1638  C   LEU A 213      15.123  54.296  26.958  1.00 17.77           C  
ATOM   1639  O   LEU A 213      15.305  53.080  26.895  1.00 16.33           O  
ATOM   1640  CB  LEU A 213      14.555  55.364  29.143  1.00 15.78           C  
ATOM   1641  CG  LEU A 213      15.018  55.851  30.523  1.00 18.44           C  
ATOM   1642  CD1 LEU A 213      13.833  56.366  31.346  1.00 18.03           C  
ATOM   1643  CD2 LEU A 213      15.731  54.719  31.275  1.00 18.77           C  
ATOM   1644  N   ASP A 214      14.465  54.984  26.025  1.00 16.56           N  
ATOM   1645  CA  ASP A 214      13.816  54.316  24.899  1.00 18.69           C  
ATOM   1646  C   ASP A 214      14.850  53.636  24.001  1.00 18.77           C  
ATOM   1647  O   ASP A 214      14.604  52.544  23.489  1.00 16.02           O  
ATOM   1648  CB  ASP A 214      12.978  55.301  24.058  1.00 17.83           C  
ATOM   1649  CG  ASP A 214      11.618  55.640  24.691  1.00 18.53           C  
ATOM   1650  OD1 ASP A 214      11.163  54.943  25.633  1.00 18.02           O  
ATOM   1651  OD2 ASP A 214      10.983  56.617  24.217  1.00 18.58           O  
ATOM   1652  N   LEU A 215      15.992  54.293  23.798  1.00 17.57           N  
ATOM   1653  CA  LEU A 215      17.066  53.714  22.986  1.00 18.76           C  
ATOM   1654  C   LEU A 215      17.623  52.453  23.657  1.00 17.82           C  
ATOM   1655  O   LEU A 215      17.902  51.451  22.991  1.00 17.88           O  
ATOM   1656  CB  LEU A 215      18.184  54.737  22.754  1.00 17.52           C  
ATOM   1657  CG  LEU A 215      17.811  55.929  21.862  1.00 20.54           C  
ATOM   1658  CD1 LEU A 215      18.947  56.949  21.821  1.00 23.84           C  
ATOM   1659  CD2 LEU A 215      17.459  55.445  20.453  1.00 22.13           C  
ATOM   1660  N   LEU A 216      17.778  52.507  24.976  1.00 16.63           N  
ATOM   1661  CA  LEU A 216      18.254  51.353  25.743  1.00 17.62           C  
ATOM   1662  C   LEU A 216      17.208  50.236  25.780  1.00 16.15           C  
ATOM   1663  O   LEU A 216      17.546  49.047  25.671  1.00 16.84           O  
ATOM   1664  CB  LEU A 216      18.633  51.787  27.177  1.00 15.67           C  
ATOM   1665  CG  LEU A 216      19.825  52.747  27.269  1.00 18.56           C  
ATOM   1666  CD1 LEU A 216      19.973  53.310  28.686  1.00 17.36           C  
ATOM   1667  CD2 LEU A 216      21.130  52.074  26.827  1.00 21.27           C  
ATOM   1668  N   ALA A 217      15.939  50.622  25.893  1.00 12.15           N  
ATOM   1669  CA  ALA A 217      14.871  49.652  26.133  1.00 16.67           C  
ATOM   1670  C   ALA A 217      14.301  49.044  24.860  1.00 16.70           C  
ATOM   1671  O   ALA A 217      13.580  48.046  24.938  1.00 15.95           O  
ATOM   1672  CB  ALA A 217      13.741  50.291  26.937  1.00 16.96           C  
ATOM   1673  N   LYS A 218      14.591  49.643  23.702  1.00 16.78           N  
ATOM   1674  CA  LYS A 218      14.028  49.124  22.455  1.00 17.21           C  
ATOM   1675  C   LYS A 218      15.133  48.601  21.507  1.00 18.71           C  
ATOM   1676  O   LYS A 218      15.360  47.384  21.495  1.00 17.15           O  
ATOM   1677  CB  LYS A 218      13.112  50.174  21.793  1.00 16.78           C  
ATOM   1678  CG  LYS A 218      11.817  50.434  22.570  1.00 19.37           C  
ATOM   1679  CD  LYS A 218      10.882  51.374  21.828  1.00 20.23           C  
ATOM   1680  CE  LYS A 218       9.515  51.445  22.499  1.00 23.13           C  
ATOM   1681  NZ  LYS A 218       9.550  52.167  23.812  1.00 23.90           N  
ATOM   1682  N   PRO A 219      15.852  49.474  20.753  1.00 17.29           N  
ATOM   1683  CA  PRO A 219      16.779  48.792  19.831  1.00 20.36           C  
ATOM   1684  C   PRO A 219      17.967  48.099  20.514  1.00 21.27           C  
ATOM   1685  O   PRO A 219      18.393  47.065  20.005  1.00 20.20           O  
ATOM   1686  CB  PRO A 219      17.271  49.926  18.917  1.00 20.60           C  
ATOM   1687  CG  PRO A 219      17.124  51.169  19.737  1.00 20.53           C  
ATOM   1688  CD  PRO A 219      15.917  50.946  20.601  1.00 15.52           C  
ATOM   1689  N   LEU A 220      18.495  48.622  21.622  1.00 18.48           N  
ATOM   1690  CA  LEU A 220      19.615  47.920  22.269  1.00 20.23           C  
ATOM   1691  C   LEU A 220      19.133  46.612  22.912  1.00 18.92           C  
ATOM   1692  O   LEU A 220      19.764  45.561  22.753  1.00 18.28           O  
ATOM   1693  CB  LEU A 220      20.315  48.803  23.309  1.00 18.80           C  
ATOM   1694  CG  LEU A 220      21.611  48.169  23.837  1.00 21.98           C  
ATOM   1695  CD1 LEU A 220      22.618  47.867  22.715  1.00 24.97           C  
ATOM   1696  CD2 LEU A 220      22.255  49.046  24.893  1.00 21.13           C  
ATOM   1697  N   TYR A 221      18.017  46.682  23.633  1.00 17.92           N  
ATOM   1698  CA  TYR A 221      17.348  45.489  24.152  1.00 19.00           C  
ATOM   1699  C   TYR A 221      17.070  44.467  23.039  1.00 17.97           C  
ATOM   1700  O   TYR A 221      17.347  43.281  23.198  1.00 18.03           O  
ATOM   1701  CB  TYR A 221      16.041  45.888  24.842  1.00 16.86           C  
ATOM   1702  CG  TYR A 221      15.113  44.760  25.282  1.00 17.02           C  
ATOM   1703  CD1 TYR A 221      15.365  44.030  26.436  1.00 18.67           C  
ATOM   1704  CD2 TYR A 221      13.941  44.484  24.578  1.00 16.77           C  
ATOM   1705  CE1 TYR A 221      14.494  43.034  26.853  1.00 17.94           C  
ATOM   1706  CE2 TYR A 221      13.062  43.498  24.990  1.00 16.63           C  
ATOM   1707  CZ  TYR A 221      13.344  42.773  26.128  1.00 16.82           C  
ATOM   1708  OH  TYR A 221      12.474  41.781  26.541  1.00 18.95           O  
ATOM   1709  N   ALA A 222      16.525  44.932  21.919  1.00 15.56           N  
ATOM   1710  CA  ALA A 222      16.215  44.037  20.796  1.00 18.35           C  
ATOM   1711  C   ALA A 222      17.457  43.289  20.305  1.00 18.96           C  
ATOM   1712  O   ALA A 222      17.394  42.094  20.002  1.00 19.58           O  
ATOM   1713  CB  ALA A 222      15.586  44.823  19.640  1.00 18.35           C  
ATOM   1714  N   ILE A 223      18.574  44.002  20.201  1.00 18.37           N  
ATOM   1715  CA  ILE A 223      19.835  43.389  19.789  1.00 18.61           C  
ATOM   1716  C   ILE A 223      20.228  42.287  20.773  1.00 19.65           C  
ATOM   1717  O   ILE A 223      20.680  41.209  20.374  1.00 17.17           O  
ATOM   1718  CB  ILE A 223      20.955  44.434  19.673  1.00 20.44           C  
ATOM   1719  CG1 ILE A 223      20.693  45.342  18.463  1.00 22.83           C  
ATOM   1720  CG2 ILE A 223      22.325  43.759  19.520  1.00 22.82           C  
ATOM   1721  CD1 ILE A 223      21.594  46.561  18.398  1.00 27.02           C  
ATOM   1722  N   GLY A 224      20.030  42.542  22.060  1.00 17.87           N  
ATOM   1723  CA  GLY A 224      20.313  41.528  23.064  1.00 18.54           C  
ATOM   1724  C   GLY A 224      19.407  40.311  22.939  1.00 18.46           C  
ATOM   1725  O   GLY A 224      19.864  39.171  23.074  1.00 16.88           O  
ATOM   1726  N   VAL A 225      18.121  40.543  22.695  1.00 16.37           N  
ATOM   1727  CA  VAL A 225      17.180  39.443  22.494  1.00 16.73           C  
ATOM   1728  C   VAL A 225      17.524  38.640  21.241  1.00 18.54           C  
ATOM   1729  O   VAL A 225      17.524  37.406  21.257  1.00 17.89           O  
ATOM   1730  CB  VAL A 225      15.737  39.950  22.377  1.00 16.72           C  
ATOM   1731  CG1 VAL A 225      14.790  38.813  21.941  1.00 16.56           C  
ATOM   1732  CG2 VAL A 225      15.277  40.555  23.705  1.00 15.28           C  
ATOM   1733  N   LEU A 226      17.813  39.351  20.157  1.00 17.72           N  
ATOM   1734  CA  LEU A 226      18.095  38.689  18.882  1.00 16.17           C  
ATOM   1735  C   LEU A 226      19.377  37.864  18.961  1.00 19.25           C  
ATOM   1736  O   LEU A 226      19.427  36.738  18.462  1.00 19.70           O  
ATOM   1737  CB  LEU A 226      18.171  39.726  17.757  1.00 15.76           C  
ATOM   1738  CG  LEU A 226      16.793  40.301  17.412  1.00 16.84           C  
ATOM   1739  CD1 LEU A 226      16.906  41.589  16.591  1.00 18.81           C  
ATOM   1740  CD2 LEU A 226      15.926  39.270  16.678  1.00 16.67           C  
ATOM   1741  N   ILE A 227      20.413  38.419  19.584  1.00 17.89           N  
ATOM   1742  CA  ILE A 227      21.646  37.666  19.797  1.00 19.09           C  
ATOM   1743  C   ILE A 227      21.381  36.409  20.626  1.00 19.98           C  
ATOM   1744  O   ILE A 227      21.877  35.319  20.309  1.00 19.54           O  
ATOM   1745  CB  ILE A 227      22.716  38.525  20.492  1.00 22.04           C  
ATOM   1746  CG1 ILE A 227      23.261  39.570  19.519  1.00 22.08           C  
ATOM   1747  CG2 ILE A 227      23.856  37.654  21.021  1.00 24.12           C  
ATOM   1748  CD1 ILE A 227      24.251  40.531  20.149  1.00 24.32           C  
ATOM   1749  N   THR A 228      20.596  36.560  21.688  1.00 18.72           N  
ATOM   1750  CA  THR A 228      20.236  35.417  22.527  1.00 21.35           C  
ATOM   1751  C   THR A 228      19.527  34.308  21.757  1.00 18.52           C  
ATOM   1752  O   THR A 228      19.907  33.140  21.869  1.00 19.53           O  
ATOM   1753  CB  THR A 228      19.347  35.863  23.700  1.00 23.25           C  
ATOM   1754  OG1 THR A 228      20.104  36.735  24.543  1.00 23.70           O  
ATOM   1755  CG2 THR A 228      18.876  34.663  24.506  1.00 28.27           C  
ATOM   1756  N   VAL A 229      18.503  34.642  20.973  1.00 18.82           N  
ATOM   1757  CA  VAL A 229      17.764  33.574  20.296  1.00 19.36           C  
ATOM   1758  C   VAL A 229      18.626  32.938  19.204  1.00 20.46           C  
ATOM   1759  O   VAL A 229      18.520  31.739  18.941  1.00 20.56           O  
ATOM   1760  CB  VAL A 229      16.415  34.061  19.692  1.00 22.52           C  
ATOM   1761  CG1 VAL A 229      15.451  34.526  20.806  1.00 20.58           C  
ATOM   1762  CG2 VAL A 229      16.628  35.159  18.649  1.00 25.11           C  
ATOM   1763  N   GLU A 230      19.503  33.722  18.584  1.00 19.24           N  
ATOM   1764  CA  GLU A 230      20.393  33.159  17.571  1.00 20.32           C  
ATOM   1765  C   GLU A 230      21.367  32.158  18.192  1.00 20.29           C  
ATOM   1766  O   GLU A 230      21.554  31.047  17.680  1.00 22.80           O  
ATOM   1767  CB  GLU A 230      21.151  34.281  16.845  1.00 19.94           C  
ATOM   1768  CG  GLU A 230      20.262  35.115  15.913  1.00 18.13           C  
ATOM   1769  CD  GLU A 230      20.140  34.520  14.508  1.00 23.08           C  
ATOM   1770  OE1 GLU A 230      20.697  33.421  14.253  1.00 22.15           O  
ATOM   1771  OE2 GLU A 230      19.479  35.159  13.656  1.00 23.42           O  
ATOM   1772  N   VAL A 231      21.975  32.541  19.305  1.00 20.20           N  
ATOM   1773  CA  VAL A 231      22.957  31.681  19.942  1.00 23.88           C  
ATOM   1774  C   VAL A 231      22.293  30.413  20.471  1.00 25.82           C  
ATOM   1775  O   VAL A 231      22.804  29.311  20.274  1.00 27.38           O  
ATOM   1776  CB  VAL A 231      23.688  32.408  21.081  1.00 24.57           C  
ATOM   1777  CG1 VAL A 231      24.563  31.432  21.853  1.00 27.59           C  
ATOM   1778  CG2 VAL A 231      24.529  33.551  20.515  1.00 24.68           C  
ATOM   1779  N   VAL A 232      21.146  30.571  21.125  1.00 27.12           N  
ATOM   1780  CA  VAL A 232      20.434  29.420  21.680  1.00 29.69           C  
ATOM   1781  C   VAL A 232      19.983  28.473  20.573  1.00 29.14           C  
ATOM   1782  O   VAL A 232      20.207  27.259  20.657  1.00 31.37           O  
ATOM   1783  CB  VAL A 232      19.211  29.850  22.523  1.00 28.13           C  
ATOM   1784  CG1 VAL A 232      18.388  28.632  22.918  1.00 29.75           C  
ATOM   1785  CG2 VAL A 232      19.664  30.598  23.760  1.00 29.84           C  
ATOM   1786  N   TYR A 233      19.377  29.017  19.518  1.00 26.64           N  
ATOM   1787  CA  TYR A 233      18.934  28.171  18.408  1.00 26.50           C  
ATOM   1788  C   TYR A 233      20.109  27.418  17.791  1.00 30.03           C  
ATOM   1789  O   TYR A 233      20.002  26.222  17.503  1.00 31.55           O  
ATOM   1790  CB  TYR A 233      18.212  29.001  17.340  1.00 25.99           C  
ATOM   1791  CG  TYR A 233      17.645  28.185  16.197  1.00 27.24           C  
ATOM   1792  CD1 TYR A 233      16.773  27.121  16.433  1.00 26.46           C  
ATOM   1793  CD2 TYR A 233      17.968  28.484  14.884  1.00 25.24           C  
ATOM   1794  CE1 TYR A 233      16.250  26.383  15.390  1.00 28.67           C  
ATOM   1795  CE2 TYR A 233      17.453  27.749  13.833  1.00 25.45           C  
ATOM   1796  CZ  TYR A 233      16.591  26.703  14.088  1.00 28.35           C  
ATOM   1797  OH  TYR A 233      16.081  25.963  13.042  1.00 29.00           O  
ATOM   1798  N   GLY A 234      21.232  28.108  17.612  1.00 29.12           N  
ATOM   1799  CA  GLY A 234      22.432  27.490  17.073  1.00 31.28           C  
ATOM   1800  C   GLY A 234      22.963  26.329  17.903  1.00 34.82           C  
ATOM   1801  O   GLY A 234      23.592  25.413  17.369  1.00 37.53           O  
ATOM   1802  N   LYS A 235      22.706  26.352  19.207  1.00 36.64           N  
ATOM   1803  CA  LYS A 235      23.213  25.308  20.102  1.00 40.44           C  
ATOM   1804  C   LYS A 235      22.240  24.143  20.313  1.00 41.11           C  
ATOM   1805  O   LYS A 235      22.626  23.103  20.845  1.00 40.46           O  
ATOM   1806  CB  LYS A 235      23.576  25.910  21.463  1.00 42.15           C  
ATOM   1807  CG  LYS A 235      24.772  26.853  21.443  1.00 44.79           C  
ATOM   1808  CD  LYS A 235      24.991  27.478  22.819  1.00 46.73           C  
ATOM   1809  CE  LYS A 235      26.228  28.368  22.853  1.00 48.07           C  
ATOM   1810  NZ  LYS A 235      27.491  27.603  22.638  1.00 51.25           N  
ATOM   1811  N   LEU A 236      20.987  24.314  19.898  1.00 42.04           N  
ATOM   1812  CA  LEU A 236      19.953  23.308  20.144  1.00 46.20           C  
ATOM   1813  C   LEU A 236      20.180  22.037  19.331  1.00 50.48           C  
ATOM   1814  O   LEU A 236      19.856  20.934  19.779  1.00 54.73           O  
ATOM   1815  CB  LEU A 236      18.566  23.882  19.839  1.00 44.58           C  
ATOM   1816  CG  LEU A 236      17.994  24.879  20.853  1.00 42.45           C  
ATOM   1817  CD1 LEU A 236      16.599  25.336  20.443  1.00 41.71           C  
ATOM   1818  CD2 LEU A 236      17.980  24.295  22.268  1.00 43.96           C  
TER    1819      LEU A 236                                                      
HETATM 1820  C1  RET A 301       4.263  55.352  33.971  1.00 16.39           C  
HETATM 1821  C2  RET A 301       3.510  56.228  34.997  1.00 18.31           C  
HETATM 1822  C3  RET A 301       2.580  55.428  35.883  1.00 19.40           C  
HETATM 1823  C4  RET A 301       3.372  54.430  36.689  1.00 17.54           C  
HETATM 1824  C5  RET A 301       4.465  53.747  35.893  1.00 17.24           C  
HETATM 1825  C6  RET A 301       4.754  54.040  34.606  1.00 15.38           C  
HETATM 1826  C7  RET A 301       5.723  53.220  33.870  1.00 15.96           C  
HETATM 1827  C8  RET A 301       5.963  53.178  32.521  1.00 15.66           C  
HETATM 1828  C9  RET A 301       6.917  52.347  31.824  1.00 16.64           C  
HETATM 1829  C10 RET A 301       7.178  52.630  30.521  1.00 17.99           C  
HETATM 1830  C11 RET A 301       8.044  51.942  29.617  1.00 18.75           C  
HETATM 1831  C12 RET A 301       8.162  52.397  28.319  1.00 18.56           C  
HETATM 1832  C13 RET A 301       8.975  51.741  27.315  1.00 18.43           C  
HETATM 1833  C14 RET A 301       8.920  52.215  26.070  1.00 17.91           C  
HETATM 1834  C15 RET A 301       9.699  51.603  24.937  1.00 18.72           C  
HETATM 1835  C16 RET A 301       5.424  56.158  33.428  1.00 12.64           C  
HETATM 1836  C17 RET A 301       3.346  55.116  32.799  1.00 15.06           C  
HETATM 1837  C18 RET A 301       4.924  52.489  36.600  1.00 16.05           C  
HETATM 1838  C19 RET A 301       7.600  51.195  32.518  1.00 15.25           C  
HETATM 1839  C20 RET A 301       9.847  50.556  27.691  1.00 16.38           C  
HETATM 1840  C1  OLB A 302       0.377  63.999  18.856  1.00 53.80           C  
HETATM 1841  C2  OLB A 302      -0.440  62.890  18.231  1.00 51.50           C  
HETATM 1842  C3  OLB A 302       0.053  61.525  18.657  1.00 50.11           C  
HETATM 1843  C4  OLB A 302       0.049  60.512  17.532  1.00 49.30           C  
HETATM 1844  C5  OLB A 302       0.274  59.107  18.043  1.00 47.85           C  
HETATM 1845  O19 OLB A 302       1.575  63.891  19.037  1.00 55.24           O  
HETATM 1846  O20 OLB A 302      -0.315  65.093  19.190  1.00 54.31           O  
HETATM 1847  C21 OLB A 302       0.447  66.279  19.211  1.00 53.83           C  
HETATM 1848  C22 OLB A 302      -0.372  67.382  19.847  1.00 54.73           C  
HETATM 1849  O23 OLB A 302       0.241  68.633  19.630  1.00 53.98           O  
HETATM 1850  C24 OLB A 302      -1.764  67.393  19.254  1.00 55.97           C  
HETATM 1851  O25 OLB A 302      -2.699  67.322  20.309  1.00 56.51           O  
HETATM 1852  C6  OLB A 302       1.478  58.450  17.412  1.00 46.45           C  
HETATM 1853  C7  OLB A 302       2.107  57.417  18.318  1.00 46.39           C  
HETATM 1854  C8  OLB A 302       1.624  56.014  18.029  1.00 47.85           C  
HETATM 1855  C9  OLB A 302       2.234  55.427  16.780  1.00 48.20           C  
HETATM 1856  C10 OLB A 302       1.697  54.325  16.220  1.00 50.32           C  
HETATM 1857  C11 OLB A 302       0.488  53.661  16.837  1.00 52.12           C  
HETATM 1858  C12 OLB A 302       0.395  52.199  16.457  1.00 54.04           C  
HETATM 1859  C13 OLB A 302      -0.748  51.930  15.503  1.00 56.45           C  
HETATM 1860  C14 OLB A 302      -1.387  50.577  15.729  1.00 57.88           C  
HETATM 1861  C15 OLB A 302      -0.385  49.446  15.671  1.00 58.98           C  
HETATM 1862  C16 OLB A 302      -0.332  48.797  14.306  1.00 60.64           C  
HETATM 1863  C17 OLB A 302      -1.556  47.956  14.009  1.00 61.37           C  
HETATM 1864  C18 OLB A 302      -1.430  47.196  12.705  1.00 61.07           C  
HETATM 1865  C1  OLB A 303      19.646  67.778  30.587  1.00 66.95           C  
HETATM 1866  C2  OLB A 303      19.416  66.283  30.534  1.00 64.55           C  
HETATM 1867  C3  OLB A 303      20.136  65.572  31.660  1.00 61.78           C  
HETATM 1868  C4  OLB A 303      20.587  64.178  31.284  1.00 59.06           C  
HETATM 1869  C5  OLB A 303      19.477  63.161  31.426  1.00 56.58           C  
HETATM 1870  O19 OLB A 303      20.504  68.272  31.292  1.00 68.35           O  
HETATM 1871  O20 OLB A 303      18.840  68.501  29.803  1.00 67.88           O  
HETATM 1872  C21 OLB A 303      19.385  69.722  29.352  1.00 68.73           C  
HETATM 1873  C22 OLB A 303      19.005  70.827  30.315  1.00 69.96           C  
HETATM 1874  O23 OLB A 303      20.129  71.161  31.098  1.00 71.31           O  
HETATM 1875  C24 OLB A 303      18.532  72.045  29.550  1.00 69.40           C  
HETATM 1876  O25 OLB A 303      17.162  72.256  29.822  1.00 68.75           O  
HETATM 1877  C6  OLB A 303      20.004  61.781  31.745  1.00 55.08           C  
HETATM 1878  C7  OLB A 303      19.582  61.306  33.116  1.00 53.72           C  
HETATM 1879  C8  OLB A 303      19.450  59.800  33.187  1.00 52.35           C  
HETATM 1880  C9  OLB A 303      18.138  59.313  32.612  1.00 50.25           C  
HETATM 1881  C10 OLB A 303      18.055  58.111  32.002  1.00 47.36           C  
HETATM 1882  C11 OLB A 303      19.265  57.213  31.876  1.00 44.71           C  
HETATM 1883  C12 OLB A 303      19.088  55.920  32.637  1.00 44.36           C  
HETATM 1884  C13 OLB A 303      20.254  54.972  32.476  1.00 43.20           C  
HETATM 1885  C14 OLB A 303      19.962  53.629  33.100  1.00 43.94           C  
HETATM 1886  C15 OLB A 303      21.018  52.589  32.796  1.00 45.38           C  
HETATM 1887  C16 OLB A 303      20.588  51.207  33.238  1.00 46.41           C  
HETATM 1888  C17 OLB A 303      21.567  50.133  32.818  1.00 48.25           C  
HETATM 1889  C18 OLB A 303      21.057  48.737  33.102  1.00 48.61           C  
HETATM 1890  C01 C14 A 304       5.135  48.339  44.337  1.00 42.11           C  
HETATM 1891  C02 C14 A 304       5.486  49.536  45.193  1.00 41.35           C  
HETATM 1892  C03 C14 A 304       4.730  50.765  44.734  1.00 40.42           C  
HETATM 1893  C04 C14 A 304       5.566  51.980  45.066  1.00 39.42           C  
HETATM 1894  C05 C14 A 304       4.866  53.250  44.642  1.00 40.42           C  
HETATM 1895  C06 C14 A 304       5.795  54.424  44.877  1.00 41.16           C  
HETATM 1896  C07 C14 A 304       5.072  55.723  44.611  1.00 40.25           C  
HETATM 1897  C08 C14 A 304       5.991  56.892  44.903  1.00 40.72           C  
HETATM 1898  C09 C14 A 304       5.200  57.953  45.631  1.00 40.69           C  
HETATM 1899  C10 C14 A 304       5.258  59.272  44.892  1.00 41.18           C  
HETATM 1900  C11 C14 A 304       4.198  60.183  45.473  1.00 41.72           C  
HETATM 1901  C12 C14 A 304       4.736  61.590  45.634  1.00 42.72           C  
HETATM 1902  C13 C14 A 304       3.582  62.522  45.937  1.00 43.83           C  
HETATM 1903  C14 C14 A 304       4.068  63.956  45.969  1.00 44.05           C  
HETATM 1904  C1  D10 A 305       6.575  37.293  46.494  1.00 48.96           C  
HETATM 1905  C2  D10 A 305       7.184  38.658  46.262  1.00 48.23           C  
HETATM 1906  C3  D10 A 305       6.382  39.407  45.221  1.00 47.72           C  
HETATM 1907  C4  D10 A 305       7.043  40.746  44.978  1.00 46.36           C  
HETATM 1908  C5  D10 A 305       6.611  41.319  43.644  1.00 45.01           C  
HETATM 1909  C6  D10 A 305       7.651  42.315  43.174  1.00 44.42           C  
HETATM 1910  C7  D10 A 305       8.528  41.689  42.108  1.00 45.89           C  
HETATM 1911  C8  D10 A 305       9.948  42.207  42.228  1.00 47.28           C  
HETATM 1912  C9  D10 A 305      10.093  43.523  41.496  1.00 49.06           C  
HETATM 1913  C10 D10 A 305      11.482  44.078  41.736  1.00 49.45           C  
HETATM 1914  C1  D10 A 306      21.215  51.144  18.566  1.00 52.73           C  
HETATM 1915  C2  D10 A 306      21.422  51.110  20.063  1.00 51.98           C  
HETATM 1916  C3  D10 A 306      21.503  52.529  20.583  1.00 51.93           C  
HETATM 1917  C4  D10 A 306      21.775  52.519  22.071  1.00 50.61           C  
HETATM 1918  C5  D10 A 306      22.108  53.924  22.520  1.00 50.64           C  
HETATM 1919  C6  D10 A 306      22.455  53.917  23.992  1.00 50.66           C  
HETATM 1920  C7  D10 A 306      23.102  55.231  24.370  1.00 50.20           C  
HETATM 1921  C8  D10 A 306      22.050  56.203  24.854  1.00 50.03           C  
HETATM 1922  C9  D10 A 306      22.735  57.424  25.429  1.00 50.18           C  
HETATM 1923  C10 D10 A 306      23.431  58.202  24.334  1.00 49.12           C  
HETATM 1924  C27 R16 A 307       7.142  65.395  43.632  1.00 50.76           C  
HETATM 1925  C28 R16 A 307       8.253  64.381  43.449  1.00 49.44           C  
HETATM 1926  C29 R16 A 307       7.660  62.999  43.273  1.00 47.16           C  
HETATM 1927  C30 R16 A 307       8.743  61.949  43.396  1.00 46.90           C  
HETATM 1928  C31 R16 A 307       9.291  61.591  42.032  1.00 46.15           C  
HETATM 1929  C32 R16 A 307      10.063  60.289  42.103  1.00 44.75           C  
HETATM 1930  C33 R16 A 307       9.102  59.129  42.259  1.00 42.94           C  
HETATM 1931  C34 R16 A 307       9.862  57.821  42.386  1.00 40.87           C  
HETATM 1932  C35 R16 A 307       8.877  56.677  42.254  1.00 39.61           C  
HETATM 1933  C36 R16 A 307       9.587  55.355  42.054  1.00 37.36           C  
HETATM 1934  C37 R16 A 307       8.574  54.316  41.616  1.00 37.74           C  
HETATM 1935  C38 R16 A 307       9.207  52.941  41.558  1.00 36.51           C  
HETATM 1936  C39 R16 A 307       8.131  51.907  41.315  1.00 36.98           C  
HETATM 1937  C40 R16 A 307       8.708  50.517  41.452  1.00 37.55           C  
HETATM 1938  C41 R16 A 307       7.617  49.497  41.211  1.00 37.40           C  
HETATM 1939  C42 R16 A 307       8.236  48.157  40.877  1.00 37.22           C  
HETATM 1940  C1  D12 A 308      23.921  50.661  30.120  1.00 50.05           C  
HETATM 1941  C2  D12 A 308      24.467  51.903  29.450  1.00 48.80           C  
HETATM 1942  C3  D12 A 308      23.889  53.138  30.107  1.00 47.86           C  
HETATM 1943  C4  D12 A 308      24.327  54.362  29.332  1.00 46.39           C  
HETATM 1944  C5  D12 A 308      23.435  55.533  29.671  1.00 44.55           C  
HETATM 1945  C6  D12 A 308      23.882  56.739  28.877  1.00 45.10           C  
HETATM 1946  C7  D12 A 308      23.602  57.998  29.667  1.00 44.64           C  
HETATM 1947  C8  D12 A 308      24.319  59.158  29.014  1.00 45.11           C  
HETATM 1948  C9  D12 A 308      23.833  60.460  29.611  1.00 44.80           C  
HETATM 1949  C10 D12 A 308      24.395  61.623  28.822  1.00 44.67           C  
HETATM 1950  C11 D12 A 308      23.867  62.925  29.384  1.00 44.98           C  
HETATM 1951  C12 D12 A 308      24.102  64.042  28.391  1.00 45.35           C  
HETATM 1952  C1  D12 A 309      -4.249  48.117  23.535  1.00 47.22           C  
HETATM 1953  C2  D12 A 309      -3.575  46.768  23.658  1.00 48.03           C  
HETATM 1954  C3  D12 A 309      -2.457  46.674  22.644  1.00 48.39           C  
HETATM 1955  C4  D12 A 309      -1.748  45.343  22.766  1.00 49.27           C  
HETATM 1956  C5  D12 A 309      -1.086  45.022  21.443  1.00 50.15           C  
HETATM 1957  C6  D12 A 309       0.167  44.203  21.668  1.00 51.46           C  
HETATM 1958  C7  D12 A 309      -0.186  42.739  21.816  1.00 51.69           C  
HETATM 1959  C8  D12 A 309       1.081  41.937  22.036  1.00 51.60           C  
HETATM 1960  C9  D12 A 309       0.761  40.456  22.052  1.00 51.74           C  
HETATM 1961  C10 D12 A 309       0.636  39.969  23.479  1.00 50.71           C  
HETATM 1962  C11 D12 A 309       0.788  38.463  23.521  1.00 50.70           C  
HETATM 1963  C12 D12 A 309      -0.483  37.805  23.028  1.00 51.14           C  
HETATM 1964  O   HOH A 401       4.099  62.175  30.351  1.00 42.84           O  
HETATM 1965  O   HOH A 402       3.612  73.544  39.111  1.00 34.11           O  
HETATM 1966  O   HOH A 403       9.409  54.609  22.456  1.00 24.49           O  
HETATM 1967  O   HOH A 404     -12.067  65.881  46.569  1.00 51.26           O  
HETATM 1968  O   HOH A 405       8.876  34.918   6.947  1.00 53.58           O  
HETATM 1969  O   HOH A 406      15.757  75.553  24.483  1.00 49.26           O  
HETATM 1970  O   HOH A 407       5.750  78.468  37.823  1.00 53.79           O  
HETATM 1971  O   HOH A 408       7.663  63.403  32.882  1.00 26.01           O  
HETATM 1972  O   HOH A 409       6.386  71.030  12.727  1.00 65.09           O  
HETATM 1973  O   HOH A 410       7.455  57.295  22.100  1.00 23.02           O  
HETATM 1974  O   HOH A 411      19.326  71.012  20.446  1.00 56.70           O  
HETATM 1975  O   HOH A 412      -1.486  76.992  27.088  1.00 29.25           O  
HETATM 1976  O   HOH A 413      10.657  73.063  18.747  1.00 29.76           O  
HETATM 1977  O   HOH A 414      -4.568  73.838  31.201  1.00 36.37           O  
HETATM 1978  O   HOH A 415      14.674  73.613  28.282  1.00 44.08           O  
HETATM 1979  O   HOH A 416       8.520  57.422  24.744  1.00 21.02           O  
HETATM 1980  O   HOH A 417       0.046  79.589  32.359  1.00 29.85           O  
HETATM 1981  O   HOH A 418       9.185  32.387  13.374  1.00 25.76           O  
HETATM 1982  O   HOH A 419      -6.734  66.137  41.788  1.00 41.55           O  
HETATM 1983  O   HOH A 420       4.758  66.363  29.082  1.00 25.87           O  
HETATM 1984  O   HOH A 421       7.891  78.099  35.026  1.00 37.00           O  
HETATM 1985  O   HOH A 422      11.372  61.250  24.840  1.00 18.33           O  
HETATM 1986  O   HOH A 423      12.439  29.083  29.480  1.00 35.43           O  
HETATM 1987  O   HOH A 424       3.489  77.613  32.780  1.00 29.47           O  
HETATM 1988  O   HOH A 425      10.074  29.607  16.620  1.00 48.22           O  
HETATM 1989  O   HOH A 426      10.131  75.782  28.497  1.00 28.28           O  
HETATM 1990  O   HOH A 427       2.317  68.051  23.542  1.00 18.00           O  
HETATM 1991  O   HOH A 428      -6.083  68.302  31.885  1.00 61.13           O  
HETATM 1992  O   HOH A 429      20.970  30.787  14.985  1.00 22.39           O  
HETATM 1993  O   HOH A 430       8.440  70.530  17.526  1.00 36.38           O  
HETATM 1994  O   HOH A 431       7.998  71.628  34.594  1.00 20.60           O  
HETATM 1995  O   HOH A 432       5.531  72.019  16.016  1.00 41.28           O  
HETATM 1996  O   HOH A 433       1.484  66.183  33.471  1.00 39.61           O  
HETATM 1997  O   HOH A 434       6.332  66.338  21.490  1.00 21.91           O  
HETATM 1998  O   HOH A 435      12.740  46.836  27.307  1.00 17.25           O  
HETATM 1999  O   HOH A 436       8.708  60.075  25.317  1.00 18.91           O  
HETATM 2000  O   HOH A 437      10.998  33.505  16.720  1.00 23.41           O  
HETATM 2001  O   HOH A 438      25.147  29.001  18.724  1.00 31.20           O  
HETATM 2002  O   HOH A 439       4.590  32.083  42.347  1.00 55.70           O  
HETATM 2003  O   HOH A 440      11.447  72.365  28.487  1.00 23.37           O  
HETATM 2004  O   HOH A 441      21.516  28.993  32.008  1.00 36.42           O  
HETATM 2005  O   HOH A 442      10.076  69.695  13.883  1.00 33.50           O  
HETATM 2006  O   HOH A 443      12.822  76.625  28.536  1.00 42.55           O  
HETATM 2007  O   HOH A 444      -5.701  68.981  29.154  1.00 47.49           O  
HETATM 2008  O   HOH A 445       5.396  78.697  35.020  1.00 37.52           O  
HETATM 2009  O   HOH A 446      12.204  72.195  40.438  1.00 48.15           O  
HETATM 2010  O   HOH A 447       3.102  67.760  32.149  1.00 23.59           O  
HETATM 2011  O   HOH A 448      -0.850  69.451  38.704  1.00 31.34           O  
HETATM 2012  O   HOH A 449      12.076  35.516  21.403  1.00 32.93           O  
HETATM 2013  O   HOH A 450      -2.072  27.804  27.640  1.00 37.12           O  
HETATM 2014  O   HOH A 451      11.704  78.051  33.938  1.00 36.58           O  
HETATM 2015  O   HOH A 452      14.265  71.640  33.915  1.00 27.63           O  
HETATM 2016  O   HOH A 453      21.545  33.036   5.037  1.00 53.54           O  
HETATM 2017  O   HOH A 454       2.171  34.037  41.838  1.00 37.93           O  
HETATM 2018  O   HOH A 455      -4.668  72.027  26.376  1.00 33.47           O  
HETATM 2019  O   HOH A 456      -3.061  74.137  38.107  1.00 30.06           O  
HETATM 2020  O   HOH A 457       1.864  64.250  22.249  1.00 20.87           O  
HETATM 2021  O   HOH A 458      -5.915  35.804  33.434  1.00 56.40           O  
HETATM 2022  O   HOH A 459       9.250  62.929  24.012  1.00 17.62           O  
HETATM 2023  O   HOH A 460      21.704  30.943  29.408  1.00 34.02           O  
HETATM 2024  O   HOH A 461      -4.011  28.972  30.019  1.00 39.38           O  
HETATM 2025  O   HOH A 462      -1.159  32.332  36.563  1.00 40.78           O  
HETATM 2026  O   HOH A 463      -8.761  62.236  36.895  1.00 64.16           O  
HETATM 2027  O   HOH A 464      14.241  28.556   6.926  1.00 29.54           O  
HETATM 2028  O   HOH A 465      13.736  71.081  30.625  1.00 27.17           O  
HETATM 2029  O   HOH A 466      -0.857  67.697  35.561  1.00 50.93           O  
HETATM 2030  O   HOH A 467       7.755  76.467  20.468  1.00 55.77           O  
HETATM 2031  O   HOH A 468      -6.054  71.351  33.157  1.00 32.56           O  
HETATM 2032  O   HOH A 469      -4.924  68.461  22.135  1.00 49.71           O  
HETATM 2033  O   HOH A 470      16.902  32.760   4.384  1.00 33.75           O  
HETATM 2034  O   HOH A 471      12.491  76.913  21.160  1.00 29.61           O  
HETATM 2035  O   HOH A 472       4.327  30.500  25.767  1.00 53.00           O  
HETATM 2036  O   HOH A 473       7.873  59.057  32.072  1.00 39.19           O  
HETATM 2037  O   HOH A 474      14.360  28.928  30.759  1.00 46.52           O  
HETATM 2038  O   HOH A 475      22.714  30.488   9.590  1.00 61.87           O  
HETATM 2039  O   HOH A 476      -8.234  67.061  36.136  1.00 61.15           O  
HETATM 2040  O   HOH A 477      -6.245  72.372  30.577  1.00 57.86           O  
HETATM 2041  O   HOH A 478      17.881  31.126   6.173  1.00 35.89           O  
HETATM 2042  O   HOH A 479      15.463  70.983  37.617  1.00 54.56           O  
HETATM 2043  O   HOH A 480       6.276  61.371  31.461  1.00 29.70           O  
HETATM 2044  O   HOH A 481       9.747  74.961  20.354  1.00 54.41           O  
HETATM 2045  O   HOH A 482      13.137  30.964  31.650  1.00 42.84           O  
HETATM 2046  O   HOH A 483       3.578  66.300  21.574  1.00 28.75           O  
HETATM 2047  O   HOH A 484       3.326  64.888  30.797  1.00 35.51           O  
HETATM 2048  O   HOH A 485      -1.504  78.181  43.460  1.00 52.24           O  
HETATM 2049  O   HOH A 486       8.752  69.599  11.583  1.00 45.63           O  
CONECT 1681 1834                                                                
CONECT 1820 1821 1825 1835 1836                                                 
CONECT 1821 1820 1822                                                           
CONECT 1822 1821 1823                                                           
CONECT 1823 1822 1824                                                           
CONECT 1824 1823 1825 1837                                                      
CONECT 1825 1820 1824 1826                                                      
CONECT 1826 1825 1827                                                           
CONECT 1827 1826 1828                                                           
CONECT 1828 1827 1829 1838                                                      
CONECT 1829 1828 1830                                                           
CONECT 1830 1829 1831                                                           
CONECT 1831 1830 1832                                                           
CONECT 1832 1831 1833 1839                                                      
CONECT 1833 1832 1834                                                           
CONECT 1834 1681 1833                                                           
CONECT 1835 1820                                                                
CONECT 1836 1820                                                                
CONECT 1837 1824                                                                
CONECT 1838 1828                                                                
CONECT 1839 1832                                                                
CONECT 1840 1841 1845 1846                                                      
CONECT 1841 1840 1842                                                           
CONECT 1842 1841 1843                                                           
CONECT 1843 1842 1844                                                           
CONECT 1844 1843 1852                                                           
CONECT 1845 1840                                                                
CONECT 1846 1840 1847                                                           
CONECT 1847 1846 1848                                                           
CONECT 1848 1847 1849 1850                                                      
CONECT 1849 1848                                                                
CONECT 1850 1848 1851                                                           
CONECT 1851 1850                                                                
CONECT 1852 1844 1853                                                           
CONECT 1853 1852 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                                                                
CONECT 1865 1866 1870 1871                                                      
CONECT 1866 1865 1867                                                           
CONECT 1867 1866 1868                                                           
CONECT 1868 1867 1869                                                           
CONECT 1869 1868 1877                                                           
CONECT 1870 1865                                                                
CONECT 1871 1865 1872                                                           
CONECT 1872 1871 1873                                                           
CONECT 1873 1872 1874 1875                                                      
CONECT 1874 1873                                                                
CONECT 1875 1873 1876                                                           
CONECT 1876 1875                                                                
CONECT 1877 1869 1878                                                           
CONECT 1878 1877 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                                                                
CONECT 1890 1891                                                                
CONECT 1891 1890 1892                                                           
CONECT 1892 1891 1893                                                           
CONECT 1893 1892 1894                                                           
CONECT 1894 1893 1895                                                           
CONECT 1895 1894 1896                                                           
CONECT 1896 1895 1897                                                           
CONECT 1897 1896 1898                                                           
CONECT 1898 1897 1899                                                           
CONECT 1899 1898 1900                                                           
CONECT 1900 1899 1901                                                           
CONECT 1901 1900 1902                                                           
CONECT 1902 1901 1903                                                           
CONECT 1903 1902                                                                
CONECT 1904 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                                                                
CONECT 1914 1915                                                                
CONECT 1915 1914 1916                                                           
CONECT 1916 1915 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                                                                
CONECT 1924 1925                                                                
CONECT 1925 1924 1926                                                           
CONECT 1926 1925 1927                                                           
CONECT 1927 1926 1928                                                           
CONECT 1928 1927 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                                                                
CONECT 1952 1953                                                                
CONECT 1953 1952 1954                                                           
CONECT 1954 1953 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                                                                
MASTER      316    0    9   13    2    0   10    6 2048    1  145   19          
END                                                                             
