HEADER    TRANSLATION, RIBOSOME                   22-AUG-02   1MI6              
TITLE     DOCKING OF THE MODIFIED RF2 X-RAY STRUCTURE INTO THE LOW RESOLUTION   
TITLE    2 CRYO-EM MAP OF RF2 E.COLI 70S RIBOSOME                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PEPTIDE CHAIN RELEASE FACTOR RF-2;                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: RELEASE FACTOR 2; RF2                                       
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12                                                          
KEYWDS    RF2, RELEASE COMPLEX, CONFORMATIONAL CHANGES, TRANSLATION, RIBOSOME   
EXPDTA    ELECTRON MICROSCOPY                                                   
MDLTYP    CA ATOMS ONLY, CHAIN A                                                
AUTHOR    U.B.S.RAWAT,A.V.ZAVIALOV,J.SENGUPTA,M.VALLE,R.A.GRASSUCCI,J.LINDE,    
AUTHOR   2 B.VESTERGAARD,M.EHRENBERG,J.FRANK                                    
REVDAT   6   14-FEB-24 1MI6    1       REMARK SEQADV                            
REVDAT   5   18-JUL-18 1MI6    1       REMARK                                   
REVDAT   4   01-FEB-17 1MI6    1       AUTHOR                                   
REVDAT   3   13-JUL-11 1MI6    1       VERSN                                    
REVDAT   2   24-FEB-09 1MI6    1       VERSN                                    
REVDAT   1   14-JAN-03 1MI6    0                                                
JRNL        AUTH   U.B.S.RAWAT,A.V.ZAVIALOV,J.SENGUPTA,M.VALLE,R.A.GRASSUCCI,   
JRNL        AUTH 2 J.LINDE,B.VESTERGAARD,M.EHRENBERG,J.FRANK                    
JRNL        TITL   A CRYO-ELECTRON MICROSCOPIC STUDY OF RIBOSOME-BOUND          
JRNL        TITL 2 TERMINATION FACTOR RF2                                       
JRNL        REF    NATURE                        V. 421    87 2003              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   12511960                                                     
JRNL        DOI    10.1038/NATURE01224                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  TITL   THE CRYSTAL STRUCTURE OF HUMAN EUKARYOTIC RELEASE FACTOR     
REMARK   1  TITL 2 ERF1-MECHANISM OF STOP CODON RECOGNITION AND PEPTIDYL-TRNA   
REMARK   1  TITL 3 HYDROLYSIS                                                   
REMARK   1  REF    CELL(CAMBRIDGE,MASS.)         V. 100   311 2000              
REMARK   1  REFN                   ISSN 0092-8674                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  TITL   BACTERIAL POLYPEPTIDE RELEASE FACTOR RF2 IS STRUCTURALLY     
REMARK   1  TITL 2 DISTINCT FROM EUKARYOTIC ERF1                                
REMARK   1  REF    MOL.CELL                      V.   8  1375 2001              
REMARK   1  REFN                   ISSN 1097-2765                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.   12.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : O, SPIDER                                 
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 1GQE                                
REMARK   3   REFINEMENT SPACE             : REAL                                
REMARK   3   REFINEMENT PROTOCOL          : OTHER                               
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : METHOD--MANUAL                                   
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 12.80                          
REMARK   3   NUMBER OF PARTICLES               : 18199                          
REMARK   3   CTF CORRECTION METHOD             : NULL                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: TMV                     
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: SPIDER PACKAGE                                        
REMARK   4                                                                      
REMARK   4 1MI6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-AUG-02.                  
REMARK 100 THE DEPOSITION ID IS D_1000016929.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : VITREOUS ICE (CRYO EM)            
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : E.COLI 70S RIBOSOME - RF2(WT)     
REMARK 245                                    COMPLEX                           
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 32.00                             
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : RAPID-FREEZING IN LIQUID ETHANE   
REMARK 245   SAMPLE BUFFER                  : POLYMIX BUFFER                    
REMARK 245   PH                             : 7.50                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : 08-NOV-01                      
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : 93.00                          
REMARK 245   MICROSCOPE MODEL                  : FEI TECNAI F20                 
REMARK 245   DETECTOR TYPE                     : KODAK SO-163 FILM              
REMARK 245   MINIMUM DEFOCUS (NM)              : 2500.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 4000.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : 0.00                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : 0.00                           
REMARK 245   NOMINAL CS                        : 2.00                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 2000.00                        
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 50000                          
REMARK 245   CALIBRATED MAGNIFICATION          : 49696                          
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 200                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
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 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     PHE A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1GQE   RELATED DB: PDB                                   
REMARK 900 POLYPEPTIDE CHAIN RELEASE FACTOR 2 (RF2) FROM E. COLI                
REMARK 900 RELATED ID: 1DT9   RELATED DB: PDB                                   
REMARK 900 THE CRYSTAL STRUCTURE OF HUMAN EUKARYOTIC RELEASE FACTOR ERF1        
REMARK 900 RELATED ID: EMD-1006   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-1007   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-1008   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-1009   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-1010   RELATED DB: EMDB                              
DBREF  1MI6 A    1   365  UNP    P07012   RF2_ECOLI        1    365             
SEQADV 1MI6 ALA A  246  UNP  P07012    THR   246 CONFLICT                       
SEQADV 1MI6 VAL A  298  UNP  P07012    LEU   298 CONFLICT                       
SEQRES   1 A  365  MET PHE GLU ILE ASN PRO VAL ASN ASN ARG ILE GLN ASP          
SEQRES   2 A  365  LEU THR GLU ARG SER ASP VAL LEU ARG GLY TYR LEU ASP          
SEQRES   3 A  365  TYR ASP ALA LYS LYS GLU ARG LEU GLU GLU VAL ASN ALA          
SEQRES   4 A  365  GLU LEU GLU GLN PRO ASP VAL TRP ASN GLU PRO GLU ARG          
SEQRES   5 A  365  ALA GLN ALA LEU GLY LYS GLU ARG SER SER LEU GLU ALA          
SEQRES   6 A  365  VAL VAL ASP THR LEU ASP GLN MET LYS GLN GLY LEU GLU          
SEQRES   7 A  365  ASP VAL SER GLY LEU LEU GLU LEU ALA VAL GLU ALA ASP          
SEQRES   8 A  365  ASP GLU GLU THR PHE ASN GLU ALA VAL ALA GLU LEU ASP          
SEQRES   9 A  365  ALA LEU GLU GLU LYS LEU ALA GLN LEU GLU PHE ARG ARG          
SEQRES  10 A  365  MET PHE SER GLY GLU TYR ASP SER ALA ASP CYS TYR LEU          
SEQRES  11 A  365  ASP ILE GLN ALA GLY SER GLY GLY THR GLU ALA GLN ASP          
SEQRES  12 A  365  TRP ALA SER MET LEU GLU ARG MET TYR LEU ARG TRP ALA          
SEQRES  13 A  365  GLU SER ARG GLY PHE LYS THR GLU ILE ILE GLU GLU SER          
SEQRES  14 A  365  GLU GLY GLU VAL ALA GLY ILE LYS SER VAL THR ILE LYS          
SEQRES  15 A  365  ILE SER GLY ASP TYR ALA TYR GLY TRP LEU ARG THR GLU          
SEQRES  16 A  365  THR GLY VAL HIS ARG LEU VAL ARG LYS SER PRO PHE ASP          
SEQRES  17 A  365  SER GLY GLY ARG ARG HIS THR SER PHE SER SER ALA PHE          
SEQRES  18 A  365  VAL TYR PRO GLU VAL ASP ASP ASP ILE ASP ILE GLU ILE          
SEQRES  19 A  365  ASN PRO ALA ASP LEU ARG ILE ASP VAL TYR ARG ALA SER          
SEQRES  20 A  365  GLY ALA GLY GLY GLN HIS VAL ASN ARG THR GLU SER ALA          
SEQRES  21 A  365  VAL ARG ILE THR HIS ILE PRO THR GLY ILE VAL THR GLN          
SEQRES  22 A  365  CYS GLN ASN ASP ARG SER GLN HIS LYS ASN LYS ASP GLN          
SEQRES  23 A  365  ALA MET LYS GLN MET LYS ALA LYS LEU TYR GLU VAL GLU          
SEQRES  24 A  365  MET GLN LYS LYS ASN ALA GLU LYS GLN ALA MET GLU ASP          
SEQRES  25 A  365  ASN LYS SER ASP ILE GLY TRP GLY SER GLN ILE ARG SER          
SEQRES  26 A  365  TYR VAL LEU ASP ASP SER ARG ILE LYS ASP LEU ARG THR          
SEQRES  27 A  365  GLY VAL GLU THR ARG ASN THR GLN ALA VAL LEU ASP GLY          
SEQRES  28 A  365  SER LEU ASP GLN PHE ILE GLU ALA SER LEU LYS ALA GLY          
SEQRES  29 A  365  LEU                                                          
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
ATOM      1  CA  ILE A   4     -83.196  19.808 -53.044  1.00 43.76           C  
ATOM      2  CA  ASN A   5     -81.846  16.200 -52.676  1.00 35.92           C  
ATOM      3  CA  PRO A   6     -79.348  15.005 -49.972  1.00 28.31           C  
ATOM      4  CA  VAL A   7     -76.697  14.469 -52.676  1.00 22.58           C  
ATOM      5  CA  ASN A   8     -77.070  18.104 -53.829  1.00 24.27           C  
ATOM      6  CA  ASN A   9     -76.867  19.121 -50.152  1.00 23.77           C  
ATOM      7  CA  ARG A  10     -73.604  17.105 -50.074  1.00 19.92           C  
ATOM      8  CA  ILE A  11     -72.401  18.981 -53.212  1.00 16.28           C  
ATOM      9  CA  GLN A  12     -73.262  22.308 -51.530  1.00 20.05           C  
ATOM     10  CA  ASP A  13     -71.393  21.295 -48.332  1.00 20.07           C  
ATOM     11  CA  LEU A  14     -68.286  20.084 -50.238  1.00 16.21           C  
ATOM     12  CA  THR A  15     -68.398  23.193 -52.484  1.00 21.05           C  
ATOM     13  CA  GLU A  16     -68.568  25.677 -49.550  1.00 20.20           C  
ATOM     14  CA  ARG A  17     -65.808  23.779 -47.683  1.00 17.57           C  
ATOM     15  CA  SER A  18     -63.564  23.724 -50.772  1.00 20.18           C  
ATOM     16  CA  ASP A  19     -64.194  27.475 -51.384  1.00 22.35           C  
ATOM     17  CA  VAL A  20     -62.931  28.350 -47.879  1.00 22.34           C  
ATOM     18  CA  LEU A  21     -60.114  25.790 -48.305  1.00 22.29           C  
ATOM     19  CA  ARG A  22     -58.952  27.554 -51.519  1.00 22.42           C  
ATOM     20  CA  GLY A  23     -58.682  30.770 -49.462  1.00 22.82           C  
ATOM     21  CA  TYR A  24     -56.973  29.161 -46.446  1.00 20.84           C  
ATOM     22  CA  LEU A  25     -54.427  27.251 -48.562  1.00 20.03           C  
ATOM     23  CA  ASP A  26     -54.005  30.376 -50.799  1.00 24.29           C  
ATOM     24  CA  TYR A  27     -54.927  28.654 -54.091  1.00 19.79           C  
ATOM     25  CA  ASP A  28     -54.157  31.650 -56.360  1.00 19.83           C  
ATOM     26  CA  ALA A  29     -50.670  32.274 -54.879  1.00 19.32           C  
ATOM     27  CA  LYS A  30     -49.803  28.563 -55.096  1.00 19.26           C  
ATOM     28  CA  LYS A  31     -51.033  28.478 -58.728  1.00 21.43           C  
ATOM     29  CA  GLU A  32     -48.791  31.522 -59.392  1.00 25.03           C  
ATOM     30  CA  ARG A  33     -45.719  29.965 -57.712  1.00 22.38           C  
ATOM     31  CA  LEU A  34     -46.458  26.646 -59.484  1.00 20.84           C  
ATOM     32  CA  GLU A  35     -46.266  28.523 -62.830  1.00 27.73           C  
ATOM     33  CA  GLU A  36     -42.914  30.157 -61.865  1.00 27.70           C  
ATOM     34  CA  VAL A  37     -41.368  26.853 -60.666  1.00 24.20           C  
ATOM     35  CA  ASN A  38     -42.766  24.897 -63.639  1.00 28.00           C  
ATOM     36  CA  ALA A  39     -41.329  27.486 -66.068  1.00 31.96           C  
ATOM     37  CA  GLU A  40     -37.883  27.084 -64.445  1.00 37.67           C  
ATOM     38  CA  LEU A  41     -38.297  23.273 -64.704  1.00 44.47           C  
ATOM     39  CA  GLU A  42     -39.084  23.728 -68.439  1.00 56.40           C  
ATOM     40  CA  GLN A  43     -36.088  26.104 -68.954  1.00 65.22           C  
ATOM     41  CA  PRO A  44     -33.274  23.628 -69.971  1.00 69.30           C  
ATOM     42  CA  ASP A  45     -30.603  25.563 -67.986  1.00 68.24           C  
ATOM     43  CA  VAL A  46     -31.991  24.183 -64.683  1.00 62.75           C  
ATOM     44  CA  TRP A  47     -31.135  20.548 -65.573  1.00 58.86           C  
ATOM     45  CA  ASN A  48     -27.419  21.385 -65.901  1.00 61.82           C  
ATOM     46  CA  GLU A  49     -27.773  21.416 -62.059  1.00 59.08           C  
ATOM     47  CA  PRO A  50     -29.578  18.114 -61.157  1.00 49.25           C  
ATOM     48  CA  GLU A  51     -29.904  19.140 -57.468  1.00 39.57           C  
ATOM     49  CA  ARG A  52     -31.580  22.469 -58.406  1.00 29.31           C  
ATOM     50  CA  ALA A  53     -33.992  20.750 -60.819  1.00 19.96           C  
ATOM     51  CA  GLN A  54     -34.834  17.986 -58.296  1.00 16.95           C  
ATOM     52  CA  ALA A  55     -35.521  20.542 -55.532  1.00 16.51           C  
ATOM     53  CA  LEU A  56     -37.739  22.580 -57.877  1.00 14.62           C  
ATOM     54  CA  GLY A  57     -39.429  19.296 -58.946  1.00 14.76           C  
ATOM     55  CA  LYS A  58     -40.241  18.598 -55.285  1.00 18.77           C  
ATOM     56  CA  GLU A  59     -41.584  22.182 -54.902  1.00 16.69           C  
ATOM     57  CA  ARG A  60     -43.720  21.746 -58.061  1.00 17.63           C  
ATOM     58  CA  SER A  61     -45.110  18.377 -56.860  1.00 18.15           C  
ATOM     59  CA  SER A  62     -45.864  19.834 -53.400  1.00 18.82           C  
ATOM     60  CA  LEU A  63     -47.978  22.599 -55.058  1.00 15.23           C  
ATOM     61  CA  GLU A  64     -49.602  20.337 -57.712  1.00 18.85           C  
ATOM     62  CA  ALA A  65     -50.844  18.354 -54.676  1.00 18.16           C  
ATOM     63  CA  VAL A  66     -52.843  21.515 -53.764  1.00 17.19           C  
ATOM     64  CA  VAL A  67     -53.557  23.496 -56.963  1.00 18.04           C  
ATOM     65  CA  ASP A  68     -54.483  20.574 -59.254  1.00 20.97           C  
ATOM     66  CA  THR A  69     -56.342  18.890 -56.344  1.00 18.52           C  
ATOM     67  CA  LEU A  70     -58.541  22.007 -55.949  1.00 15.78           C  
ATOM     68  CA  ASP A  71     -59.013  22.028 -59.773  1.00 18.25           C  
ATOM     69  CA  GLN A  72     -60.075  18.338 -59.697  1.00 22.74           C  
ATOM     70  CA  MET A  73     -62.496  19.327 -56.918  1.00 23.09           C  
ATOM     71  CA  LYS A  74     -63.960  22.271 -58.904  1.00 20.11           C  
ATOM     72  CA  GLN A  75     -64.242  20.309 -62.176  1.00 18.83           C  
ATOM     73  CA  GLY A  76     -65.583  17.198 -60.412  1.00 17.92           C  
ATOM     74  CA  LEU A  77     -68.342  19.078 -58.539  1.00 16.07           C  
ATOM     75  CA  GLU A  78     -69.613  20.513 -61.872  1.00 19.38           C  
ATOM     76  CA  ASP A  79     -69.460  17.051 -63.534  1.00 18.65           C  
ATOM     77  CA  VAL A  80     -71.427  15.484 -60.636  1.00 15.29           C  
ATOM     78  CA  SER A  81     -74.089  18.256 -60.716  1.00 15.21           C  
ATOM     79  CA  GLY A  82     -74.595  17.617 -64.458  1.00 15.26           C  
ATOM     80  CA  LEU A  83     -74.753  13.828 -63.988  1.00 14.08           C  
ATOM     81  CA  LEU A  84     -77.390  14.234 -61.235  1.00 18.01           C  
ATOM     82  CA  GLU A  85     -79.363  16.722 -63.395  1.00 23.01           C  
ATOM     83  CA  LEU A  86     -79.329  14.187 -66.268  1.00 21.58           C  
ATOM     84  CA  ALA A  87     -80.028  11.209 -63.950  1.00 19.19           C  
ATOM     85  CA  VAL A  88     -83.070  12.736 -62.204  1.00 22.97           C  
ATOM     86  CA  GLU A  89     -84.718  14.046 -65.416  1.00 29.68           C  
ATOM     87  CA  ALA A  90     -84.019  10.842 -67.405  1.00 29.52           C  
ATOM     88  CA  ASP A  91     -84.869   8.737 -64.294  1.00 31.41           C  
ATOM     89  CA  ASP A  92     -81.584   6.890 -65.020  1.00 29.26           C  
ATOM     90  CA  GLU A  93     -80.441   6.214 -61.445  1.00 25.62           C  
ATOM     91  CA  GLU A  94     -77.372   4.288 -62.675  1.00 24.19           C  
ATOM     92  CA  THR A  95     -75.934   7.743 -63.518  1.00 19.96           C  
ATOM     93  CA  PHE A  96     -77.163   8.951 -60.091  1.00 15.47           C  
ATOM     94  CA  ASN A  97     -75.118   6.243 -58.320  1.00 16.00           C  
ATOM     95  CA  GLU A  98     -72.095   7.042 -60.543  1.00 20.13           C  
ATOM     96  CA  ALA A  99     -72.448  10.748 -59.600  1.00 16.27           C  
ATOM     97  CA  VAL A 100     -72.795   9.856 -55.874  1.00 14.69           C  
ATOM     98  CA  ALA A 101     -69.649   7.655 -56.077  1.00 15.28           C  
ATOM     99  CA  GLU A 102     -67.681  10.339 -57.970  1.00 19.19           C  
ATOM    100  CA  LEU A 103     -68.805  12.792 -55.250  1.00 15.36           C  
ATOM    101  CA  ASP A 104     -67.502  10.250 -52.656  1.00 15.86           C  
ATOM    102  CA  ALA A 105     -64.076  10.215 -54.388  1.00 17.83           C  
ATOM    103  CA  LEU A 106     -64.184  14.049 -54.335  1.00 18.77           C  
ATOM    104  CA  GLU A 107     -65.057  13.916 -50.594  1.00 19.28           C  
ATOM    105  CA  GLU A 108     -62.047  11.587 -50.033  1.00 22.14           C  
ATOM    106  CA  LYS A 109     -59.725  13.909 -52.037  1.00 22.09           C  
ATOM    107  CA  LEU A 110     -61.100  16.921 -50.110  1.00 17.57           C  
ATOM    108  CA  ALA A 111     -60.497  15.156 -46.763  1.00 17.36           C  
ATOM    109  CA  GLN A 112     -56.943  14.156 -47.764  1.00 19.35           C  
ATOM    110  CA  LEU A 113     -56.210  17.762 -48.787  1.00 15.37           C  
ATOM    111  CA  GLU A 114     -57.795  19.215 -45.582  1.00 16.32           C  
ATOM    112  CA  PHE A 115     -55.540  16.794 -43.632  1.00 17.56           C  
ATOM    113  CA  ARG A 116     -52.611  19.116 -44.642  1.00 19.10           C  
ATOM    114  CA  ARG A 117     -53.729  21.352 -41.746  1.00 25.45           C  
ATOM    115  CA  MET A 118     -54.419  18.490 -39.309  1.00 30.05           C  
ATOM    116  CA  PHE A 119     -50.879  17.121 -39.819  1.00 26.10           C  
ATOM    117  CA  SER A 120     -49.712  19.994 -37.502  1.00 33.33           C  
ATOM    118  CA  GLY A 121     -47.208  17.548 -35.921  1.00 31.97           C  
ATOM    119  CA  GLU A 122     -44.534  14.888 -36.539  1.00 31.33           C  
ATOM    120  CA  TYR A 123     -45.691  11.226 -36.391  1.00 24.76           C  
ATOM    121  CA  ASP A 124     -49.387  12.169 -36.698  1.00 18.05           C  
ATOM    122  CA  SER A 125     -50.702   8.770 -37.922  1.00 16.40           C  
ATOM    123  CA  ALA A 126     -48.768   6.773 -35.295  1.00 15.26           C  
ATOM    124  CA  ASP A 127     -49.399   5.249 -31.886  1.00 14.59           C  
ATOM    125  CA  CYS A 128     -47.683   7.158 -29.034  1.00 12.68           C  
ATOM    126  CA  TYR A 129     -46.125   6.930 -25.571  1.00 12.65           C  
ATOM    127  CA  LEU A 130     -47.528   9.150 -22.799  1.00 12.80           C  
ATOM    128  CA  ASP A 131     -45.898  10.145 -19.480  1.00 11.86           C  
ATOM    129  CA  ILE A 132     -48.560  11.360 -17.034  1.00  9.86           C  
ATOM    130  CA  GLN A 133     -46.631  13.023 -14.174  1.00 14.47           C  
ATOM    131  CA  ALA A 134     -47.690  14.969 -11.053  1.00 14.30           C  
ATOM    132  CA  GLY A 135     -46.394  18.459 -10.296  1.00 17.37           C  
ATOM    133  CA  SER A 136     -44.208  18.817  -7.179  1.00 20.46           C  
ATOM    134  CA  GLY A 137     -47.197  19.182  -4.800  1.00 18.72           C  
ATOM    135  CA  GLY A 138     -47.299  15.798  -3.014  1.00 18.02           C  
ATOM    136  CA  THR A 139     -50.661  14.037  -2.510  1.00 14.51           C  
ATOM    137  CA  GLU A 140     -52.544  17.124  -3.829  1.00 12.43           C  
ATOM    138  CA  ALA A 141     -50.685  17.065  -7.179  1.00 10.33           C  
ATOM    139  CA  GLN A 142     -50.795  13.237  -7.267  1.00 11.57           C  
ATOM    140  CA  ASP A 143     -54.612  13.450  -6.857  1.00 11.47           C  
ATOM    141  CA  TRP A 144     -54.788  15.617 -10.045  1.00 12.10           C  
ATOM    142  CA  ALA A 145     -52.332  13.384 -11.958  1.00 10.87           C  
ATOM    143  CA  SER A 146     -54.808  10.528 -11.320  1.00 10.63           C  
ATOM    144  CA  MET A 147     -57.739  12.617 -12.646  1.00  9.84           C  
ATOM    145  CA  LEU A 148     -55.635  13.207 -15.775  1.00  9.48           C  
ATOM    146  CA  GLU A 149     -55.101   9.401 -15.773  1.00 10.84           C  
ATOM    147  CA  ARG A 150     -58.909   8.868 -15.623  1.00 12.36           C  
ATOM    148  CA  MET A 151     -59.432  11.515 -18.347  1.00  9.92           C  
ATOM    149  CA  TYR A 152     -56.812  10.312 -20.866  1.00 11.27           C  
ATOM    150  CA  LEU A 153     -57.582   6.619 -20.154  1.00  9.79           C  
ATOM    151  CA  ARG A 154     -61.324   7.016 -20.776  1.00 10.10           C  
ATOM    152  CA  TRP A 155     -60.645   9.202 -23.829  1.00 11.86           C  
ATOM    153  CA  ALA A 156     -58.201   6.637 -25.309  1.00 11.87           C  
ATOM    154  CA  GLU A 157     -60.572   3.738 -24.432  1.00 13.37           C  
ATOM    155  CA  SER A 158     -63.583   5.495 -26.046  1.00 12.13           C  
ATOM    156  CA  ARG A 159     -61.445   6.202 -29.144  1.00 15.85           C  
ATOM    157  CA  GLY A 160     -60.446   2.491 -28.932  1.00 15.47           C  
ATOM    158  CA  PHE A 161     -56.721   3.293 -28.553  1.00 12.40           C  
ATOM    159  CA  LYS A 162     -55.509   0.521 -26.252  1.00 11.18           C  
ATOM    160  CA  THR A 163     -54.079   1.915 -22.993  1.00 12.63           C  
ATOM    161  CA  GLU A 164     -51.037  -0.356 -22.611  1.00 16.31           C  
ATOM    162  CA  ILE A 165     -49.848   0.641 -19.102  1.00 14.06           C  
ATOM    163  CA  ILE A 166     -46.027   0.361 -19.117  1.00 12.80           C  
ATOM    164  CA  GLU A 167     -45.334   1.422 -15.498  1.00 16.18           C  
ATOM    165  CA  GLU A 168     -47.642   3.031 -12.875  1.00 15.58           C  
ATOM    166  CA  SER A 169     -45.975   5.058 -10.084  1.00 13.66           C  
ATOM    167  CA  GLU A 170     -48.596   5.364  -7.286  1.00 14.65           C  
ATOM    168  CA  GLY A 171     -48.998   8.517  -5.127  1.00 13.56           C  
ATOM    169  CA  GLU A 172     -48.801   8.493  -1.283  1.00 16.21           C  
ATOM    170  CA  VAL A 173     -52.226   8.122   0.408  1.00 15.55           C  
ATOM    171  CA  ALA A 174     -53.913   8.054  -3.025  1.00 15.30           C  
ATOM    172  CA  GLY A 175     -53.315   9.415  -6.541  1.00 13.89           C  
ATOM    173  CA  ILE A 176     -50.227   8.778  -8.724  1.00 12.60           C  
ATOM    174  CA  LYS A 177     -46.715  10.211  -8.873  1.00 10.21           C  
ATOM    175  CA  SER A 178     -46.880   9.193 -12.553  1.00 13.07           C  
ATOM    176  CA  VAL A 179     -47.912   6.598 -15.134  1.00 10.96           C  
ATOM    177  CA  THR A 180     -46.281   5.664 -18.465  1.00 11.67           C  
ATOM    178  CA  ILE A 181     -48.737   4.389 -21.133  1.00 12.18           C  
ATOM    179  CA  LYS A 182     -48.378   3.370 -24.792  1.00 12.65           C  
ATOM    180  CA  ILE A 183     -51.580   4.882 -26.239  1.00 11.93           C  
ATOM    181  CA  SER A 184     -51.776   2.099 -28.805  1.00 12.32           C  
ATOM    182  CA  GLY A 185     -54.135   3.325 -31.543  1.00 14.06           C  
ATOM    183  CA  ASP A 186     -54.272   4.851 -35.036  1.00 14.41           C  
ATOM    184  CA  TYR A 187     -53.477   8.589 -35.065  1.00 12.54           C  
ATOM    185  CA  ALA A 188     -53.093   8.519 -31.224  1.00 12.31           C  
ATOM    186  CA  TYR A 189     -50.022  10.759 -31.633  1.00 11.80           C  
ATOM    187  CA  GLY A 190     -51.806  13.114 -34.072  1.00 10.45           C  
ATOM    188  CA  TRP A 191     -54.820  13.528 -31.788  1.00 12.30           C  
ATOM    189  CA  LEU A 192     -53.213  13.493 -28.335  1.00 13.58           C  
ATOM    190  CA  ARG A 193     -50.294  15.842 -29.189  1.00 14.53           C  
ATOM    191  CA  THR A 194     -52.870  18.676 -29.126  1.00 13.52           C  
ATOM    192  CA  GLU A 195     -53.879  17.880 -25.504  1.00 10.90           C  
ATOM    193  CA  THR A 196     -50.311  17.641 -24.136  1.00 10.64           C  
ATOM    194  CA  GLY A 197     -48.148  19.890 -21.874  1.00 13.75           C  
ATOM    195  CA  VAL A 198     -48.750  20.930 -18.229  1.00 11.94           C  
ATOM    196  CA  HIS A 199     -52.262  21.258 -16.747  1.00 12.06           C  
ATOM    197  CA  ARG A 200     -53.421  23.416 -13.796  1.00 12.74           C  
ATOM    198  CA  LEU A 201     -56.253  22.206 -11.513  1.00 10.67           C  
ATOM    199  CA  VAL A 202     -57.227  25.089  -9.184  1.00 13.72           C  
ATOM    200  CA  ARG A 203     -59.253  23.877  -6.153  1.00 13.42           C  
ATOM    201  CA  LYS A 204     -58.945  23.413  -2.374  1.00 19.46           C  
ATOM    202  CA  SER A 205     -56.588  20.717  -1.058  1.00 21.09           C  
ATOM    203  CA  PRO A 206     -58.196  18.257   1.409  1.00 23.72           C  
ATOM    204  CA  PHE A 207     -54.650  17.065   2.274  1.00 28.22           C  
ATOM    205  CA  ASP A 208     -53.729  20.550   3.615  1.00 41.79           C  
ATOM    206  CA  SER A 209     -54.355  21.266   7.345  1.00 51.61           C  
ATOM    207  CA  GLY A 210     -57.297  23.556   6.431  1.00 55.52           C  
ATOM    208  CA  GLY A 211     -59.464  24.254   3.346  1.00 57.24           C  
ATOM    209  CA  ARG A 212     -56.585  26.124   1.637  1.00 54.69           C  
ATOM    210  CA  ARG A 213     -57.111  27.126  -2.011  1.00 41.52           C  
ATOM    211  CA  HIS A 214     -54.358  25.250  -3.908  1.00 26.59           C  
ATOM    212  CA  THR A 215     -53.077  24.548  -7.413  1.00 18.11           C  
ATOM    213  CA  SER A 216     -52.565  20.936  -8.360  1.00 15.52           C  
ATOM    214  CA  PHE A 217     -50.210  21.071 -11.371  1.00 15.66           C  
ATOM    215  CA  SER A 218     -49.741  17.855 -13.384  1.00 13.03           C  
ATOM    216  CA  SER A 219     -48.053  17.010 -16.689  1.00 14.58           C  
ATOM    217  CA  ALA A 220     -48.913  14.933 -19.792  1.00 10.36           C  
ATOM    218  CA  PHE A 221     -46.018  14.462 -22.268  1.00 11.37           C  
ATOM    219  CA  VAL A 222     -46.473  12.646 -25.619  1.00 11.76           C  
ATOM    220  CA  TYR A 223     -43.470  11.033 -27.382  1.00 14.35           C  
ATOM    221  CA  PRO A 224     -42.874   8.404 -30.136  1.00 14.72           C  
ATOM    222  CA  GLU A 225     -39.685   6.917 -28.641  1.00 24.28           C  
ATOM    223  CA  VAL A 226     -38.729   3.899 -26.464  1.00 34.82           C  
ATOM    224  CA  ASP A 227     -34.885   4.211 -26.482  1.00 47.00           C  
ATOM    225  CA  ASP A 228     -32.880   6.428 -24.064  1.00 56.39           C  
ATOM    226  CA  ASP A 229     -33.892   4.403 -21.000  1.00 61.70           C  
ATOM    227  CA  ILE A 230     -31.485   1.412 -20.957  1.00 64.66           C  
ATOM    228  CA  ASP A 231     -29.331   2.491 -23.995  1.00 67.17           C  
ATOM    229  CA  ILE A 232     -26.005   0.583 -24.330  1.00 65.32           C  
ATOM    230  CA  GLU A 233     -23.269   1.531 -26.831  1.00 60.06           C  
ATOM    231  CA  ILE A 234     -22.797  -0.607 -29.973  1.00 52.12           C  
ATOM    232  CA  ASN A 235     -19.077   0.211 -29.684  1.00 43.75           C  
ATOM    233  CA  PRO A 236     -17.408   0.278 -33.170  1.00 39.52           C  
ATOM    234  CA  ALA A 237     -13.935  -0.326 -31.541  1.00 34.84           C  
ATOM    235  CA  ASP A 238     -11.915   0.200 -33.858  1.00 30.42           C  
ATOM    236  CA  LEU A 239      -8.938   0.761 -31.452  1.00 29.87           C  
ATOM    237  CA  ARG A 240      -5.744   2.579 -32.522  1.00 30.03           C  
ATOM    238  CA  ILE A 241      -2.937   0.767 -30.651  1.00 28.89           C  
ATOM    239  CA  ASP A 242      -0.607   3.793 -30.199  1.00 29.27           C  
ATOM    240  CA  VAL A 243       1.882   1.692 -28.188  1.00 27.77           C  
ATOM    241  CA  TYR A 244       3.747   0.700 -30.471  1.00 24.24           C  
ATOM    242  CA  ARG A 245       4.447  -3.044 -30.131  1.00 27.27           C  
ATOM    243  CA  ALA A 246       4.989  -5.973 -32.486  1.00 43.98           C  
ATOM    244  CA  SER A 247       2.747  -8.771 -31.133  1.00 52.89           C  
ATOM    245  CA  GLY A 248       0.711  -6.195 -29.161  1.00 57.55           C  
ATOM    246  CA  ALA A 249      -2.181  -8.700 -29.003  1.00 67.79           C  
ATOM    247  CA  GLY A 250      -0.100 -11.238 -27.022  1.00 80.75           C  
ATOM    248  CA  GLY A 251       3.695 -11.751 -26.992  1.00 86.78           C  
ATOM    249  CA  GLN A 252       3.210 -12.816 -23.353  1.00 91.60           C  
ATOM    250  CA  HIS A 253       6.094 -13.157 -20.843  1.00 93.11           C  
ATOM    251  CA  VAL A 254       8.857 -11.784 -23.178  1.00 90.31           C  
ATOM    252  CA  ASN A 255       9.285  -8.038 -22.263  1.00 84.06           C  
ATOM    253  CA  ARG A 256       8.912  -4.692 -24.132  1.00 70.03           C  
ATOM    254  CA  THR A 257       5.290  -3.616 -23.574  1.00 60.52           C  
ATOM    255  CA  GLU A 258       6.577  -0.935 -24.852  1.00 51.37           C  
ATOM    256  CA  SER A 259       7.544   1.517 -23.131  1.00 34.22           C  
ATOM    257  CA  ALA A 260       3.945   1.655 -21.748  1.00 20.95           C  
ATOM    258  CA  VAL A 261       0.624   0.675 -23.358  1.00 17.06           C  
ATOM    259  CA  ARG A 262      -1.469   3.523 -24.802  1.00 15.97           C  
ATOM    260  CA  ILE A 263      -4.603   2.702 -26.865  1.00 16.28           C  
ATOM    261  CA  THR A 264      -7.059   5.240 -28.355  1.00 18.20           C  
ATOM    262  CA  HIS A 265     -10.664   4.815 -29.575  1.00 23.04           C  
ATOM    263  CA  ILE A 266     -10.713   5.715 -33.299  1.00 26.66           C  
ATOM    264  CA  PRO A 267     -14.256   7.289 -33.268  1.00 29.27           C  
ATOM    265  CA  THR A 268     -14.214   9.259 -29.978  1.00 30.02           C  
ATOM    266  CA  GLY A 269     -10.443   9.742 -29.610  1.00 26.44           C  
ATOM    267  CA  ILE A 270     -10.713   8.688 -25.926  1.00 23.75           C  
ATOM    268  CA  VAL A 271      -7.324   7.436 -24.636  1.00 18.98           C  
ATOM    269  CA  THR A 272      -6.501   4.498 -22.319  1.00 15.49           C  
ATOM    270  CA  GLN A 273      -3.071   3.711 -20.789  1.00 14.97           C  
ATOM    271  CA  CYS A 274      -1.393   0.945 -18.729  1.00 12.25           C  
ATOM    272  CA  GLN A 275       2.084  -0.400 -17.757  1.00 16.61           C  
ATOM    273  CA  ASN A 276       1.304  -3.024 -15.059  1.00 21.22           C  
ATOM    274  CA  ASP A 277       3.078  -5.865 -16.952  1.00 19.93           C  
ATOM    275  CA  ARG A 278       6.284  -6.711 -18.886  1.00 26.03           C  
ATOM    276  CA  SER A 279       4.213  -7.324 -22.060  1.00 25.69           C  
ATOM    277  CA  GLN A 280       1.138  -5.811 -23.661  1.00 26.18           C  
ATOM    278  CA  HIS A 281      -0.540  -9.234 -23.157  1.00 25.60           C  
ATOM    279  CA  LYS A 282      -1.858  -8.446 -19.635  1.00 21.21           C  
ATOM    280  CA  ASN A 283      -1.856  -4.613 -19.977  1.00 18.49           C  
ATOM    281  CA  LYS A 284      -4.350  -5.090 -22.854  1.00 19.40           C  
ATOM    282  CA  ASP A 285      -6.943  -6.370 -20.331  1.00 21.30           C  
ATOM    283  CA  GLN A 286      -6.689  -3.237 -18.139  1.00 17.23           C  
ATOM    284  CA  ALA A 287      -6.651  -0.931 -21.202  1.00 17.26           C  
ATOM    285  CA  MET A 288      -9.769  -2.719 -22.546  1.00 19.15           C  
ATOM    286  CA  LYS A 289     -11.537  -2.272 -19.178  1.00 17.72           C  
ATOM    287  CA  GLN A 290     -10.708   1.466 -19.230  1.00 13.96           C  
ATOM    288  CA  MET A 291     -11.899   1.645 -22.853  1.00 19.38           C  
ATOM    289  CA  LYS A 292     -15.235  -0.109 -22.272  1.00 22.40           C  
ATOM    290  CA  ALA A 293     -15.793   1.793 -18.994  1.00 20.83           C  
ATOM    291  CA  LYS A 294     -15.093   5.256 -20.472  1.00 22.90           C  
ATOM    292  CA  LEU A 295     -17.109   4.629 -23.647  1.00 27.26           C  
ATOM    293  CA  TYR A 296     -20.064   3.042 -21.810  1.00 32.78           C  
ATOM    294  CA  GLU A 297     -20.064   5.999 -19.351  1.00 33.79           C  
ATOM    295  CA  VAL A 298     -21.285   8.225 -22.244  1.00 38.08           C  
ATOM    296  CA  GLU A 299     -24.577   6.222 -22.340  1.00 45.28           C  
ATOM    297  CA  MET A 300     -24.613   5.273 -18.601  1.00 53.63           C  
ATOM    298  CA  GLN A 301     -25.461   8.980 -18.152  1.00 55.20           C  
ATOM    299  CA  LYS A 302     -28.434   8.821 -20.508  1.00 56.60           C  
ATOM    300  CA  LYS A 303     -30.454   6.246 -18.519  1.00 57.94           C  
ATOM    301  CA  ASN A 304     -32.727   9.178 -17.563  1.00 59.25           C  
ATOM    302  CA  ALA A 305     -33.877  11.082 -20.724  1.00 61.97           C  
ATOM    303  CA  GLU A 306     -37.438   9.638 -21.000  1.00 66.57           C  
ATOM    304  CA  LYS A 307     -37.250   9.801 -17.154  1.00 70.91           C  
ATOM    305  CA  GLN A 308     -37.053  13.626 -17.538  1.00 78.07           C  
ATOM    306  CA  ALA A 309     -40.732  13.774 -18.630  1.00 85.05           C  
ATOM    307  CA  MET A 310     -41.935  11.423 -16.081  1.00 92.19           C  
ATOM    308  CA  GLU A 311     -39.578  13.557 -13.964  1.00 96.50           C  
ATOM    309  CA  ASP A 312     -36.587  13.111 -11.636  1.00100.72           C  
ATOM    310  CA  ASN A 313     -35.996  15.813  -8.943  1.00106.20           C  
ATOM    311  CA  LYS A 314     -38.871  18.009 -10.174  1.00111.86           C  
ATOM    312  CA  SER A 315     -38.484  21.581  -8.798  1.00114.01           C  
ATOM    313  CA  ASP A 316     -41.150  22.929  -6.371  1.00113.53           C  
ATOM    314  CA  ILE A 317     -44.515  24.439  -7.445  1.00106.61           C  
ATOM    315  CA  GLY A 318     -44.530  28.198  -7.921  1.00 90.49           C  
ATOM    316  CA  TRP A 319     -48.259  28.482  -8.758  1.00 71.48           C  
ATOM    317  CA  GLY A 320     -47.774  31.107 -11.538  1.00 44.23           C  
ATOM    318  CA  SER A 321     -48.948  29.816 -14.948  1.00 23.66           C  
ATOM    319  CA  GLN A 322     -52.224  29.938 -16.942  1.00 14.89           C  
ATOM    320  CA  ILE A 323     -51.772  26.991 -19.390  1.00 11.20           C  
ATOM    321  CA  ARG A 324     -54.549  24.319 -19.658  1.00 10.67           C  
ATOM    322  CA  SER A 325     -56.515  25.634 -16.667  1.00 14.95           C  
ATOM    323  CA  TYR A 326     -59.236  23.764 -14.731  1.00 12.64           C  
ATOM    324  CA  VAL A 327     -61.115  26.028 -12.304  1.00 14.73           C  
ATOM    325  CA  LEU A 328     -63.430  23.168 -11.274  1.00 17.83           C  
ATOM    326  CA  ASP A 329     -64.577  25.198  -8.216  1.00 24.33           C  
ATOM    327  CA  ASP A 330     -66.346  27.576 -10.692  1.00 19.16           C  
ATOM    328  CA  SER A 331     -66.883  24.722 -13.245  1.00 15.49           C  
ATOM    329  CA  ARG A 332     -64.713  26.560 -15.811  1.00 12.92           C  
ATOM    330  CA  ILE A 333     -61.924  24.933 -17.904  1.00 12.34           C  
ATOM    331  CA  LYS A 334     -59.853  26.806 -20.556  1.00 13.89           C  
ATOM    332  CA  ASP A 335     -57.076  26.121 -23.101  1.00 12.51           C  
ATOM    333  CA  LEU A 336     -55.136  29.107 -24.519  1.00 13.43           C  
ATOM    334  CA  ARG A 337     -54.245  27.919 -28.070  1.00 16.35           C  
ATOM    335  CA  THR A 338     -57.823  27.383 -29.261  1.00 16.44           C  
ATOM    336  CA  GLY A 339     -59.415  30.182 -27.167  1.00 17.73           C  
ATOM    337  CA  VAL A 340     -62.026  27.558 -26.042  1.00 15.89           C  
ATOM    338  CA  GLU A 341     -63.401  28.021 -22.549  1.00 18.53           C  
ATOM    339  CA  THR A 342     -65.763  25.166 -21.549  1.00 14.86           C  
ATOM    340  CA  ARG A 343     -68.197  24.686 -18.646  1.00 13.81           C  
ATOM    341  CA  ASN A 344     -68.903  20.933 -18.854  1.00 14.95           C  
ATOM    342  CA  THR A 345     -66.252  19.718 -16.413  1.00 15.31           C  
ATOM    343  CA  GLN A 346     -68.037  16.356 -16.127  1.00 17.92           C  
ATOM    344  CA  ALA A 347     -67.957  15.595 -19.880  1.00 14.82           C  
ATOM    345  CA  VAL A 348     -64.310  16.550 -20.442  1.00 13.42           C  
ATOM    346  CA  LEU A 349     -63.230  14.711 -17.239  1.00 10.57           C  
ATOM    347  CA  ASP A 350     -65.223  11.687 -18.567  1.00 14.21           C  
ATOM    348  CA  GLY A 351     -63.770  11.825 -22.106  1.00 13.77           C  
ATOM    349  CA  SER A 352     -64.506  15.003 -24.114  1.00 14.72           C  
ATOM    350  CA  LEU A 353     -60.912  16.281 -24.572  1.00 14.46           C  
ATOM    351  CA  ASP A 354     -62.318  15.853 -28.113  1.00 13.54           C  
ATOM    352  CA  GLN A 355     -63.611  19.475 -28.049  1.00 15.41           C  
ATOM    353  CA  PHE A 356     -60.084  20.867 -27.522  1.00 12.94           C  
ATOM    354  CA  ILE A 357     -58.511  18.270 -29.846  1.00 12.14           C  
ATOM    355  CA  GLU A 358     -60.985  19.004 -32.680  1.00 15.48           C  
ATOM    356  CA  ALA A 359     -60.616  22.781 -32.104  1.00 15.84           C  
ATOM    357  CA  SER A 360     -56.796  22.443 -32.180  1.00 14.52           C  
ATOM    358  CA  LEU A 361     -56.892  20.469 -35.454  1.00 15.07           C  
ATOM    359  CA  LYS A 362     -59.423  22.939 -36.968  1.00 19.46           C  
ATOM    360  CA  ALA A 363     -57.009  25.783 -36.133  1.00 19.87           C  
ATOM    361  CA  GLY A 364     -53.988  23.655 -37.171  1.00 21.89           C  
ATOM    362  CA  LEU A 365     -52.284  23.417 -33.743  1.00 22.14           C  
TER     363      LEU A 365                                                      
MASTER      126    0    0    0    0    0    0    6  362    1    0   29          
END                                                                             
