HEADER    RIBOSOME                                07-APR-08   2VRH              
TITLE     STRUCTURE OF THE E. COLI TRIGGER FACTOR BOUND TO A TRANSLATING        
TITLE    2 RIBOSOME                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRIGGER FACTOR;                                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 OTHER_DETAILS: BASED ON PDB 1W26_A. RESIDUES 22-62 WERE REPLACED WITH
COMPND   6 THE CORRESPONDING RESIDUES OF PDB 1OMS_B;                            
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: 50S RIBOSOMAL PROTEIN L23;                                 
COMPND   9 CHAIN: B;                                                            
COMPND  10 OTHER_DETAILS: BASED ON PDB 2AW4_T;                                  
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: 50S RIBOSOMAL PROTEIN L24;                                 
COMPND  13 CHAIN: C;                                                            
COMPND  14 FRAGMENT: RESIDUES 2-104;                                            
COMPND  15 OTHER_DETAILS: BASED ON PDB 2AW4_U;                                  
COMPND  16 MOL_ID: 4;                                                           
COMPND  17 MOLECULE: 50S RIBOSOMAL PROTEIN L29;                                 
COMPND  18 CHAIN: D;                                                            
COMPND  19 OTHER_DETAILS: BASED ON PDB 2AW4_X                                   
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 OTHER_DETAILS: BASED ON PDB 1W26_A;                                  
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   9 ORGANISM_TAXID: 562;                                                 
SOURCE  10 OTHER_DETAILS: BASED ON PDB 2AW4_T;                                  
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  13 ORGANISM_TAXID: 562;                                                 
SOURCE  14 OTHER_DETAILS: BASED ON PDB 2AW4_U;                                  
SOURCE  15 MOL_ID: 4;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  17 ORGANISM_TAXID: 562;                                                 
SOURCE  18 OTHER_DETAILS: BASED ON PDB 2AW4_X                                   
KEYWDS    RIBOSOME, TRIGGER FACTOR, RIBOSOMAL PROTEIN, RIBONUCLEOPROTEIN, CO-   
KEYWDS   2 TRANSLATIONAL PROTEIN FOLDING, ROTAMASE, CHAPERONE, ISOMERASE, CELL  
KEYWDS   3 CYCLE, RNA-BINDING, RRNA-BINDING, CELL DIVISION, RIBOSOME-NASCENT    
KEYWDS   4 CHAIN COMPLEX                                                        
EXPDTA    ELECTRON MICROSCOPY                                                   
MDLTYP    CA ATOMS ONLY, CHAIN A, B, C, D                                       
AUTHOR    F.MERZ,D.BOEHRINGER,C.SCHAFFITZEL,S.PREISSLER,A.HOFFMANN,T.MAIER,     
AUTHOR   2 A.RUTKOWSKA,J.LOZZA,N.BAN,B.BUKAU,E.DEUERLING                        
REVDAT   5   23-AUG-17 2VRH    1       REMARK                                   
REVDAT   4   07-AUG-13 2VRH    1       REMARK CRYST1 SCALE1 SCALE2              
REVDAT   4 2                   1       SCALE3                                   
REVDAT   3   14-DEC-11 2VRH    1       REMARK VERSN                             
REVDAT   2   24-FEB-09 2VRH    1       VERSN                                    
REVDAT   1   17-JUN-08 2VRH    0                                                
JRNL        AUTH   F.MERZ,D.BOEHRINGER,C.SCHAFFITZEL,S.PREISSLER,A.HOFFMANN,    
JRNL        AUTH 2 T.MAIER,A.RUTKOWSKA,J.LOZZA,N.BAN,B.BUKAU,E.DEUERLING        
JRNL        TITL   MOLECULAR MECHANISM AND STRUCTURE OF TRIGGER FACTOR BOUND TO 
JRNL        TITL 2 THE TRANSLATING RIBOSOME.                                    
JRNL        REF    EMBO J.                       V.  27  1622 2008              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   18497744                                                     
JRNL        DOI    10.1038/EMBOJ.2008.89                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.   19.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : MOLREP, IMAGIC, SPIDER                    
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 2AW4                                
REMARK   3   REFINEMENT SPACE             : REAL                                
REMARK   3   REFINEMENT PROTOCOL          : RIGID BODY FIT                      
REMARK   3   REFINEMENT TARGET            : CROSS-CORRELATION COEFFICIENT       
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : REFINEMENT PROTOCOL--RIGID BODY                  
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : 4.233                          
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 19.00                          
REMARK   3   NUMBER OF PARTICLES               : NULL                           
REMARK   3   CTF CORRECTION METHOD             : NULL                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: FITTING OF CRYSTAL STRUCTURES INTO MAP EMD-1499       
REMARK   4                                                                      
REMARK   4 2VRH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE.                               
REMARK 100 THE DEPOSITION ID IS D_1290035874.                                   
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                 : STRUCTURE OF THE E. COLI          
REMARK 245                                    TRIGGER FACTOR BOUND TO A         
REMARK 245                                    TRANSLATING RIBOSOME              
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : HOLEY CARBON                      
REMARK 245   SAMPLE VITRIFICATION DETAILS   : LIQUID ETHANE                     
REMARK 245   SAMPLE BUFFER                  : 50 MM HEPES-KOH PH 7.5, 100 MM    
REMARK 245                                    KCL, 25 MM MGCL2, 0.5 MG/ML       
REMARK 245                                    CHLORAMPHENICOL                   
REMARK 245   PH                             : 7.50                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : 88.00                          
REMARK 245   MICROSCOPE MODEL                  : FEI TECNAI 20                  
REMARK 245   DETECTOR TYPE                     : KODAK SO-163 FILM              
REMARK 245   MINIMUM DEFOCUS (NM)              : 1500.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 3500.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : NULL                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : NULL                           
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 50000                          
REMARK 245   CALIBRATED MAGNIFICATION          : 50000                          
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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     ALA A   432                                                      
REMARK 465     GLU B   100                                                      
REMARK 465     LYS C   103                                                      
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1P9Y   RELATED DB: PDB                                   
REMARK 900 RIBOSOME BINDING OF E. COLI TRIGGER FACTOR MUTANT F44L.              
REMARK 900 RELATED ID: 2J28   RELATED DB: PDB                                   
REMARK 900 MODEL OF E. COLI SRP BOUND TO 70S RNCS                               
REMARK 900 RELATED ID: 2VHM   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF PDF BINDING HELIX IN COMPLEX WITH THE RIBOSOME          
REMARK 900 RELATED ID: 2WWQ   RELATED DB: PDB                                   
REMARK 900 E.COLI 70S RIBOSOME STALLED DURING TRANSLATION OF TNAC LEADER        
REMARK 900 PEPTIDE                                                              
REMARK 900 RELATED ID: 1P86   RELATED DB: PDB                                   
REMARK 900 REAL SPACE REFINED COORDINATES OF THE 50S SUBUNIT FITTEDINTO THE     
REMARK 900 LOW RESOLUTION CRYO-EM MAP OF THE INITIATION-LIKESTATE OF E. COLI    
REMARK 900 70S RIBOSOME                                                         
REMARK 900 RELATED ID: 2AW4   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE BACTERIAL RIBOSOME FROMESCHERICHIA COLI AT  
REMARK 900 3.5 A RESOLUTION. THIS FILE CONTAINSTHE 50S SUBUNIT OF ONE 70S       
REMARK 900 RIBOSOME. THE ENTIRE CRYSTALSTRUCTURE CONTAINS TWO 70S RIBOSOMES     
REMARK 900 AND IS DESCRIBED INREMARK 400.                                       
REMARK 900 RELATED ID: 1W26   RELATED DB: PDB                                   
REMARK 900 TRIGGER FACTOR IN COMPLEX WITH THE RIBOSOME FORMS A MOLECULAR        
REMARK 900 CRADLE FOR NASCENT PROTEINS                                          
REMARK 900 RELATED ID: 1W2B   RELATED DB: PDB                                   
REMARK 900 TRIGGER FACTOR RIBOSOME BINDING DOMAIN IN COMPLEX WITH 50S           
REMARK 900 RELATED ID: 1P85   RELATED DB: PDB                                   
REMARK 900 REAL SPACE REFINED COORDINATES OF THE 50S SUBUNIT FITTEDINTO THE     
REMARK 900 LOW RESOLUTION CRYO-EM MAP OF THE EF -G.GTP STATEOF E. COLI 70S      
REMARK 900 RIBOSOME                                                             
REMARK 900 RELATED ID: 2VHN   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF PDF BINDING HELIX IN COMPLEX WITH THE RIBOSOME          
REMARK 900 RELATED ID: 1OMS   RELATED DB: PDB                                   
REMARK 900 STRUCTURE DETERMINATION BY MAD: E.COLI TRIGGER FACTORBINDING AT THE  
REMARK 900 RIBOSOMAL EXIT TUNNEL.                                               
REMARK 900 RELATED ID: 2AWB   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE BACTERIAL RIBOSOME FROMESCHERICHIA COLI AT  
REMARK 900 3.5 A RESOLUTION. THIS FILE CONTAINSTHE 50S SUBUNIT OF THE SECOND    
REMARK 900 70S RIBOSOME. THE ENTIRECRYSTAL STRUCTURE CONTAINS TWO 70S           
REMARK 900 RIBOSOMES AND ISDESCRIBED IN REMARK 400.                             
REMARK 900 RELATED ID: 1L1P   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF THE PPIASE DOMAIN FROM E. COLITRIGGER FACTOR   
REMARK 900 RELATED ID: EMD-1499   RELATED DB: EMDB                              
REMARK 900 STRUCTURE OF THE E. COLI TRIGGER FACTOR BOUND TO A TRANSLATING       
REMARK 900 RIBOSOME                                                             
DBREF  2VRH A    1   432  UNP    P0A850   TIG_ECOLI        1    432             
DBREF  2VRH B    1   100  UNP    Q0TCE3   RL23_ECOL5       1    100             
DBREF  2VRH C    1   103  UNP    P60624   RL24_ECOLI       2    104             
DBREF  2VRH D    1    63  UNP    P0A7M6   RL29_ECOLI       1     63             
SEQRES   1 A  432  MSE GLN VAL SER VAL GLU THR THR GLN GLY LEU GLY ARG          
SEQRES   2 A  432  ARG VAL THR ILE THR ILE ALA ALA ASP SER ILE GLU THR          
SEQRES   3 A  432  ALA VAL LYS SER GLU LEU VAL ASN VAL ALA LYS LYS VAL          
SEQRES   4 A  432  ARG ILE ASP GLY PHE ARG LYS GLY LYS VAL PRO MSE ASN          
SEQRES   5 A  432  ILE VAL ALA GLN ARG TYR GLY ALA SER VAL ARG GLN ASP          
SEQRES   6 A  432  VAL LEU GLY ASP LEU MSE SER ARG ASN PHE ILE ASP ALA          
SEQRES   7 A  432  ILE ILE LYS GLU LYS ILE ASN PRO ALA GLY ALA PRO THR          
SEQRES   8 A  432  TYR VAL PRO GLY GLU TYR LYS LEU GLY GLU ASP PHE THR          
SEQRES   9 A  432  TYR SER VAL GLU PHE GLU VAL TYR PRO GLU VAL GLU LEU          
SEQRES  10 A  432  GLN GLY LEU GLU ALA ILE GLU VAL GLU LYS PRO ILE VAL          
SEQRES  11 A  432  GLU VAL THR ASP ALA ASP VAL ASP GLY MSE LEU ASP THR          
SEQRES  12 A  432  LEU ARG LYS GLN GLN ALA THR TRP LYS GLU LYS ASP GLY          
SEQRES  13 A  432  ALA VAL GLU ALA GLU ASP ARG VAL THR ILE ASP PHE THR          
SEQRES  14 A  432  GLY SER VAL ASP GLY GLU GLU PHE GLU GLY GLY LYS ALA          
SEQRES  15 A  432  SER ASP PHE VAL LEU ALA MSE GLY GLN GLY ARG MSE ILE          
SEQRES  16 A  432  PRO GLY PHE GLU ASP GLY ILE LYS GLY HIS LYS ALA GLY          
SEQRES  17 A  432  GLU GLU PHE THR ILE ASP VAL THR PHE PRO GLU GLU TYR          
SEQRES  18 A  432  HIS ALA GLU ASN LEU LYS GLY LYS ALA ALA LYS PHE ALA          
SEQRES  19 A  432  ILE ASN LEU LYS LYS VAL GLU GLU ARG GLU LEU PRO GLU          
SEQRES  20 A  432  LEU THR ALA GLU PHE ILE LYS ARG PHE GLY VAL GLU ASP          
SEQRES  21 A  432  GLY SER VAL GLU GLY LEU ARG ALA GLU VAL ARG LYS ASN          
SEQRES  22 A  432  MSE GLU ARG GLU LEU LYS SER ALA ILE ARG ASN ARG VAL          
SEQRES  23 A  432  LYS SER GLN ALA ILE GLU GLY LEU VAL LYS ALA ASN ASP          
SEQRES  24 A  432  ILE ASP VAL PRO ALA ALA LEU ILE ASP SER GLU ILE ASP          
SEQRES  25 A  432  VAL LEU ARG ARG GLN ALA ALA GLN ARG PHE GLY GLY ASN          
SEQRES  26 A  432  GLU LYS GLN ALA LEU GLU LEU PRO ARG GLU LEU PHE GLU          
SEQRES  27 A  432  GLU GLN ALA LYS ARG ARG VAL VAL VAL GLY LEU LEU LEU          
SEQRES  28 A  432  GLY GLU VAL ILE ARG THR ASN GLU LEU LYS ALA ASP GLU          
SEQRES  29 A  432  GLU ARG VAL LYS GLY LEU ILE GLU GLU MSE ALA SER ALA          
SEQRES  30 A  432  TYR GLU ASP PRO LYS GLU VAL ILE GLU PHE TYR SER LYS          
SEQRES  31 A  432  ASN LYS GLU LEU MSE ASP ASN MSE ARG ASN VAL ALA LEU          
SEQRES  32 A  432  GLU GLU GLN ALA VAL GLU ALA VAL LEU ALA LYS ALA LYS          
SEQRES  33 A  432  VAL THR GLU LYS GLU THR THR PHE ASN GLU LEU MSE ASN          
SEQRES  34 A  432  GLN GLN ALA                                                  
SEQRES   1 B  100  MET ILE ARG GLU GLU ARG LEU LEU LYS VAL LEU ARG ALA          
SEQRES   2 B  100  PRO HIS VAL SER GLU LYS ALA SER THR ALA MET GLU LYS          
SEQRES   3 B  100  SER ASN THR ILE VAL LEU LYS VAL ALA LYS ASP ALA THR          
SEQRES   4 B  100  LYS ALA GLU ILE LYS ALA ALA VAL GLN LYS LEU PHE GLU          
SEQRES   5 B  100  VAL GLU VAL GLU VAL VAL ASN THR LEU VAL VAL LYS GLY          
SEQRES   6 B  100  LYS VAL LYS ARG HIS GLY GLN ARG ILE GLY ARG ARG SER          
SEQRES   7 B  100  ASP TRP LYS LYS ALA TYR VAL THR LEU LYS GLU GLY GLN          
SEQRES   8 B  100  ASN LEU ASP PHE VAL GLY GLY ALA GLU                          
SEQRES   1 C  103  ALA ALA LYS ILE ARG ARG ASP ASP GLU VAL ILE VAL LEU          
SEQRES   2 C  103  THR GLY LYS ASP LYS GLY LYS ARG GLY LYS VAL LYS ASN          
SEQRES   3 C  103  VAL LEU SER SER GLY LYS VAL ILE VAL GLU GLY ILE ASN          
SEQRES   4 C  103  LEU VAL LYS LYS HIS GLN LYS PRO VAL PRO ALA LEU ASN          
SEQRES   5 C  103  GLN PRO GLY GLY ILE VAL GLU LYS GLU ALA ALA ILE GLN          
SEQRES   6 C  103  VAL SER ASN VAL ALA ILE PHE ASN ALA ALA THR GLY LYS          
SEQRES   7 C  103  ALA ASP ARG VAL GLY PHE ARG PHE GLU ASP GLY LYS LYS          
SEQRES   8 C  103  VAL ARG PHE PHE LYS SER ASN SER GLU THR ILE LYS              
SEQRES   1 D   63  MET LYS ALA LYS GLU LEU ARG GLU LYS SER VAL GLU GLU          
SEQRES   2 D   63  LEU ASN THR GLU LEU LEU ASN LEU LEU ARG GLU GLN PHE          
SEQRES   3 D   63  ASN LEU ARG MET GLN ALA ALA SER GLY GLN LEU GLN GLN          
SEQRES   4 D   63  SER HIS LEU LEU LYS GLN VAL ARG ARG ASP VAL ALA ARG          
SEQRES   5 D   63  VAL LYS THR LEU LEU ASN GLU LYS ALA GLY ALA                  
MODRES 2VRH MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 2VRH MSE A   51  MET  SELENOMETHIONINE                                   
MODRES 2VRH MSE A   71  MET  SELENOMETHIONINE                                   
MODRES 2VRH MSE A  140  MET  SELENOMETHIONINE                                   
MODRES 2VRH MSE A  189  MET  SELENOMETHIONINE                                   
MODRES 2VRH MSE A  194  MET  SELENOMETHIONINE                                   
MODRES 2VRH MSE A  274  MET  SELENOMETHIONINE                                   
MODRES 2VRH MSE A  374  MET  SELENOMETHIONINE                                   
MODRES 2VRH MSE A  395  MET  SELENOMETHIONINE                                   
MODRES 2VRH MSE A  398  MET  SELENOMETHIONINE                                   
MODRES 2VRH MSE A  428  MET  SELENOMETHIONINE                                   
HET    MSE  A   1       1                                                       
HET    MSE  A  51       1                                                       
HET    MSE  A  71       1                                                       
HET    MSE  A 140       1                                                       
HET    MSE  A 189       1                                                       
HET    MSE  A 194       1                                                       
HET    MSE  A 274       1                                                       
HET    MSE  A 374       1                                                       
HET    MSE  A 395       1                                                       
HET    MSE  A 398       1                                                       
HET    MSE  A 428       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    11(C5 H11 N O2 SE)                                           
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                         
HETATM    1  CA  MSE A   1     537.518 425.216 415.313  1.00117.02           C  
ATOM      2  CA  GLN A   2     541.018 424.229 416.425  1.00 90.49           C  
ATOM      3  CA  VAL A   3     542.662 421.790 413.990  1.00 73.07           C  
ATOM      4  CA  SER A   4     546.015 419.965 414.095  1.00 63.53           C  
ATOM      5  CA  VAL A   5     547.461 417.503 411.607  1.00 57.62           C  
ATOM      6  CA  GLU A   6     549.795 414.519 412.135  1.00 49.63           C  
ATOM      7  CA  THR A   7     551.773 412.370 409.750  1.00 56.74           C  
ATOM      8  CA  THR A   8     551.691 408.726 410.687  1.00 50.99           C  
ATOM      9  CA  GLN A   9     553.205 406.317 408.154  1.00 70.05           C  
ATOM     10  CA  GLY A  10     553.720 406.871 404.433  1.00 62.53           C  
ATOM     11  CA  LEU A  11     550.428 408.264 403.164  1.00 52.80           C  
ATOM     12  CA  GLY A  12     548.910 407.939 406.623  1.00 43.03           C  
ATOM     13  CA  ARG A  13     547.678 410.982 408.493  1.00 45.16           C  
ATOM     14  CA  ARG A  14     545.694 411.934 411.563  1.00 53.29           C  
ATOM     15  CA  VAL A  15     543.631 415.110 411.603  1.00 45.26           C  
ATOM     16  CA  THR A  16     542.637 416.245 415.072  1.00 59.12           C  
ATOM     17  CA  ILE A  17     539.781 418.633 415.717  1.00 39.39           C  
ATOM     18  CA  THR A  18     538.067 420.349 418.606  1.00 58.49           C  
ATOM     19  CA  ILE A  19     534.459 421.568 418.458  1.00 29.60           C  
ATOM     20  CA  ALA A  20     533.455 424.247 420.983  1.00 47.41           C  
ATOM     21  CA  ALA A  21     530.984 423.410 423.763  1.00 47.25           C  
ATOM     22  CA  ASP A  22     528.703 426.157 422.478  1.00 43.71           C  
ATOM     23  CA  SER A  23     528.642 424.987 419.050  1.00 27.04           C  
ATOM     24  CA  ILE A  24     527.378 421.670 420.280  1.00 22.22           C  
ATOM     25  CA  GLU A  25     524.790 423.134 422.667  1.00 21.54           C  
ATOM     26  CA  THR A  26     523.410 425.504 420.071  1.00 22.44           C  
ATOM     27  CA  ALA A  27     523.049 422.689 417.551  1.00 20.31           C  
ATOM     28  CA  VAL A  28     521.465 420.416 420.158  1.00 22.07           C  
ATOM     29  CA  LYS A  29     518.953 423.069 421.163  1.00 25.58           C  
ATOM     30  CA  SER A  30     518.044 423.783 417.539  1.00 26.22           C  
ATOM     31  CA  GLU A  31     517.476 420.152 416.680  1.00 23.66           C  
ATOM     32  CA  LEU A  32     515.456 419.610 419.856  1.00 22.67           C  
ATOM     33  CA  VAL A  33     513.211 422.487 418.737  1.00 26.65           C  
ATOM     34  CA  ASN A  34     512.714 420.755 415.372  1.00 29.63           C  
ATOM     35  CA  VAL A  35     512.112 417.356 416.970  1.00 23.52           C  
ATOM     36  CA  ALA A  36     509.430 418.894 419.175  1.00 24.61           C  
ATOM     37  CA  LYS A  37     507.670 420.128 416.040  1.00 26.42           C  
ATOM     38  CA  LYS A  38     507.416 416.535 414.799  1.00 24.87           C  
ATOM     39  CA  VAL A  39     506.365 414.838 418.045  1.00 21.25           C  
ATOM     40  CA  ARG A  40     502.797 414.001 419.057  1.00 18.28           C  
ATOM     41  CA  ILE A  41     503.023 412.029 422.276  1.00 21.14           C  
ATOM     42  CA  ASP A  42     501.918 411.667 425.881  1.00 19.89           C  
ATOM     43  CA  GLY A  43     498.469 413.158 425.307  1.00 17.00           C  
ATOM     44  CA  PHE A  44     499.686 416.330 423.583  1.00 14.22           C  
ATOM     45  CA  ARG A  45     498.794 417.594 420.087  1.00 14.93           C  
ATOM     46  CA  LYS A  46     501.636 417.442 417.544  1.00 17.12           C  
ATOM     47  CA  GLY A  47     504.293 420.043 418.311  1.00 17.02           C  
ATOM     48  CA  LYS A  48     502.837 420.846 421.740  1.00 18.74           C  
ATOM     49  CA  VAL A  49     504.749 418.336 423.828  1.00 17.61           C  
ATOM     50  CA  PRO A  50     506.541 420.107 426.719  1.00 17.98           C  
HETATM   51  CA  MSE A  51     510.197 420.578 425.994  1.00 20.15           C  
ATOM     52  CA  ASN A  52     511.136 418.941 429.276  1.00 20.13           C  
ATOM     53  CA  ILE A  53     509.458 415.778 427.988  1.00 18.99           C  
ATOM     54  CA  VAL A  54     511.012 416.090 424.511  1.00 17.49           C  
ATOM     55  CA  ALA A  55     514.434 416.504 426.151  1.00 19.62           C  
ATOM     56  CA  GLN A  56     513.926 413.720 428.666  1.00 24.06           C  
ATOM     57  CA  ARG A  57     512.892 411.324 425.859  1.00 24.08           C  
ATOM     58  CA  TYR A  58     515.041 412.386 422.917  1.00 21.86           C  
ATOM     59  CA  GLY A  59     517.812 414.524 424.379  1.00 21.33           C  
ATOM     60  CA  ALA A  60     520.379 411.714 424.372  1.00 21.53           C  
ATOM     61  CA  SER A  61     519.599 410.623 420.806  1.00 22.29           C  
ATOM     62  CA  VAL A  62     519.690 414.231 419.632  1.00 21.64           C  
ATOM     63  CA  ARG A  63     523.115 414.671 420.864  1.00 33.93           C  
ATOM     64  CA  GLN A  64     524.719 411.655 419.261  1.00 40.70           C  
ATOM     65  CA  ASP A  65     523.390 412.314 415.765  1.00 45.00           C  
ATOM     66  CA  VAL A  66     524.399 415.963 416.267  1.00 29.51           C  
ATOM     67  CA  LEU A  67     527.936 415.209 417.503  1.00 35.85           C  
ATOM     68  CA  GLY A  68     528.243 412.829 414.599  1.00 21.21           C  
ATOM     69  CA  ASP A  69     527.054 415.361 412.087  1.00 40.12           C  
ATOM     70  CA  LEU A  70     529.488 417.910 413.514  1.00 26.01           C  
HETATM   71  CA  MSE A  71     532.491 415.572 413.392  1.00 38.88           C  
ATOM     72  CA  SER A  72     531.760 415.122 409.735  1.00 42.50           C  
ATOM     73  CA  ARG A  73     530.899 418.736 408.819  1.00 42.69           C  
ATOM     74  CA  ASN A  74     533.964 419.944 410.708  1.00 36.97           C  
ATOM     75  CA  PHE A  75     536.266 417.325 409.157  1.00 44.24           C  
ATOM     76  CA  ILE A  76     535.260 418.269 405.631  1.00 39.89           C  
ATOM     77  CA  ASP A  77     535.840 421.965 406.344  1.00 45.58           C  
ATOM     78  CA  ALA A  78     539.280 421.226 407.796  1.00 41.85           C  
ATOM     79  CA  ILE A  79     540.463 419.260 404.740  1.00 48.52           C  
ATOM     80  CA  ILE A  80     539.015 421.929 402.509  1.00 52.03           C  
ATOM     81  CA  LYS A  81     541.027 424.766 403.992  1.00 57.54           C  
ATOM     82  CA  GLU A  82     544.196 422.744 404.568  1.00 48.79           C  
ATOM     83  CA  LYS A  83     543.625 421.368 401.082  1.00 54.85           C  
ATOM     84  CA  ILE A  84     544.021 417.792 402.360  1.00 47.66           C  
ATOM     85  CA  ASN A  85     542.808 415.109 399.960  1.00 54.47           C  
ATOM     86  CA  PRO A  86     541.969 411.727 401.589  1.00 49.15           C  
ATOM     87  CA  ALA A  87     542.046 408.533 399.515  1.00 42.29           C  
ATOM     88  CA  GLY A  88     539.252 406.122 400.362  1.00 43.11           C  
ATOM     89  CA  ALA A  89     536.888 406.630 403.282  1.00 48.07           C  
ATOM     90  CA  PRO A  90     538.341 408.297 406.382  1.00 44.32           C  
ATOM     91  CA  THR A  91     538.085 406.823 409.865  1.00 41.73           C  
ATOM     92  CA  TYR A  92     536.625 408.831 412.709  1.00 38.07           C  
ATOM     93  CA  VAL A  93     537.974 408.281 416.174  1.00 31.39           C  
ATOM     94  CA  PRO A  94     536.270 410.188 418.972  1.00 45.14           C  
ATOM     95  CA  GLY A  95     537.828 410.990 422.297  1.00 59.40           C  
ATOM     96  CA  GLU A  96     535.455 410.813 425.255  1.00 77.33           C  
ATOM     97  CA  TYR A  97     532.576 413.241 425.577  1.00 68.15           C  
ATOM     98  CA  LYS A  98     532.026 415.319 428.685  1.00 66.53           C  
ATOM     99  CA  LEU A  99     528.480 416.697 428.774  1.00 56.85           C  
ATOM    100  CA  GLY A 100     528.609 420.451 428.469  1.00 61.07           C  
ATOM    101  CA  GLU A 101     532.265 420.722 427.548  1.00 56.29           C  
ATOM    102  CA  ASP A 102     534.281 420.851 424.368  1.00 60.61           C  
ATOM    103  CA  PHE A 103     534.865 417.759 422.277  1.00 49.69           C  
ATOM    104  CA  THR A 104     537.937 416.561 420.472  1.00 49.55           C  
ATOM    105  CA  TYR A 105     538.133 413.732 417.995  1.00 39.56           C  
ATOM    106  CA  SER A 106     540.456 412.453 415.293  1.00 38.72           C  
ATOM    107  CA  VAL A 107     540.051 411.212 411.763  1.00 38.27           C  
ATOM    108  CA  GLU A 108     542.639 408.799 410.380  1.00 37.92           C  
ATOM    109  CA  PHE A 109     543.192 408.319 406.684  1.00 21.57           C  
ATOM    110  CA  GLU A 110     545.711 408.125 403.858  1.00 37.08           C  
ATOM    111  CA  VAL A 111     546.254 410.808 401.229  1.00 32.18           C  
ATOM    112  CA  TYR A 112     546.643 410.279 397.500  1.00 35.57           C  
ATOM    113  CA  PRO A 113     550.319 410.229 396.585  1.00 37.31           C  
ATOM    114  CA  GLU A 114     552.319 412.917 394.757  1.00 52.72           C  
ATOM    115  CA  VAL A 115     553.322 411.768 391.286  1.00 46.59           C  
ATOM    116  CA  GLU A 116     556.340 412.902 389.296  1.00 39.26           C  
ATOM    117  CA  LEU A 117     555.862 411.166 385.970  1.00 45.23           C  
ATOM    118  CA  GLN A 118     559.330 410.050 384.870  1.00 32.45           C  
ATOM    119  CA  GLY A 119     560.748 408.078 381.946  1.00 20.30           C  
ATOM    120  CA  LEU A 120     557.848 408.853 379.612  1.00 44.95           C  
ATOM    121  CA  GLU A 121     560.251 409.430 376.722  1.00 46.50           C  
ATOM    122  CA  ALA A 122     562.180 406.293 377.652  1.00 46.40           C  
ATOM    123  CA  ILE A 123     559.139 404.003 377.227  1.00 45.79           C  
ATOM    124  CA  GLU A 124     559.264 402.137 373.910  1.00 50.06           C  
ATOM    125  CA  VAL A 125     556.167 401.045 372.014  1.00 34.47           C  
ATOM    126  CA  GLU A 126     556.234 398.709 369.063  1.00 37.79           C  
ATOM    127  CA  LYS A 127     553.227 399.185 366.792  1.00 58.96           C  
ATOM    128  CA  PRO A 128     552.405 396.171 364.626  1.00 38.83           C  
ATOM    129  CA  ILE A 129     551.477 396.689 360.984  1.00 54.29           C  
ATOM    130  CA  VAL A 130     549.179 393.715 360.380  1.00 49.59           C  
ATOM    131  CA  GLU A 131     546.314 392.680 358.162  1.00 50.89           C  
ATOM    132  CA  VAL A 132     544.097 389.646 357.753  1.00 56.42           C  
ATOM    133  CA  THR A 133     545.170 388.042 354.484  1.00 66.68           C  
ATOM    134  CA  ASP A 134     543.361 385.652 352.163  1.00 79.17           C  
ATOM    135  CA  ALA A 135     545.823 383.059 353.478  1.00 77.53           C  
ATOM    136  CA  ASP A 136     544.325 383.579 356.921  1.00 74.17           C  
ATOM    137  CA  VAL A 137     540.643 383.373 355.959  1.00 62.03           C  
ATOM    138  CA  ASP A 138     541.404 380.147 354.119  1.00 77.71           C  
ATOM    139  CA  GLY A 139     543.067 378.774 357.211  1.00 76.74           C  
HETATM  140  CA  MSE A 140     540.178 379.658 359.487  1.00 72.78           C  
ATOM    141  CA  LEU A 141     537.547 378.023 357.279  1.00 78.00           C  
ATOM    142  CA  ASP A 142     539.781 374.978 357.210  1.00 92.92           C  
ATOM    143  CA  THR A 143     539.664 375.160 361.002  1.00 86.74           C  
ATOM    144  CA  LEU A 144     535.874 375.506 361.108  1.00 79.08           C  
ATOM    145  CA  ARG A 145     535.391 372.445 358.925  1.00 80.44           C  
ATOM    146  CA  LYS A 146     537.933 370.640 361.077  1.00 82.06           C  
ATOM    147  CA  GLN A 147     536.102 371.727 364.224  1.00 89.60           C  
ATOM    148  CA  GLN A 148     532.822 370.038 363.225  1.00 92.70           C  
ATOM    149  CA  ALA A 149     534.405 367.594 361.168  1.00 95.18           C  
ATOM    150  CA  THR A 150     532.382 364.797 361.078  1.00 95.15           C  
ATOM    151  CA  TRP A 151     534.415 362.441 363.147  1.00108.87           C  
ATOM    152  CA  LYS A 152     535.033 359.289 361.078  1.00109.90           C  
ATOM    153  CA  GLU A 153     537.296 356.398 362.167  1.00110.47           C  
ATOM    154  CA  LYS A 154     540.265 354.325 361.054  1.00121.60           C  
ATOM    155  CA  ASP A 155     542.929 352.083 362.558  1.00147.00           C  
ATOM    156  CA  GLY A 156     546.715 352.244 362.643  1.00145.23           C  
ATOM    157  CA  ALA A 157     547.891 355.836 362.293  1.00124.58           C  
ATOM    158  CA  VAL A 158     547.265 358.232 365.164  1.00112.45           C  
ATOM    159  CA  GLU A 159     548.107 361.323 363.101  1.00103.88           C  
ATOM    160  CA  ALA A 160     548.973 364.743 364.516  1.00 89.64           C  
ATOM    161  CA  GLU A 161     545.355 365.964 364.515  1.00103.95           C  
ATOM    162  CA  ASP A 162     543.194 362.894 365.162  1.00 80.60           C  
ATOM    163  CA  ARG A 163     540.869 362.484 368.140  1.00 84.45           C  
ATOM    164  CA  VAL A 164     541.519 359.549 370.453  1.00 99.77           C  
ATOM    165  CA  THR A 165     539.991 357.782 373.464  1.00113.73           C  
ATOM    166  CA  ILE A 166     542.487 356.633 376.120  1.00115.74           C  
ATOM    167  CA  ASP A 167     543.110 355.319 379.652  1.00118.90           C  
ATOM    168  CA  PHE A 168     546.358 356.483 381.277  1.00109.03           C  
ATOM    169  CA  THR A 169     548.547 356.507 384.395  1.00 97.89           C  
ATOM    170  CA  GLY A 170     551.628 358.566 385.191  1.00101.41           C  
ATOM    171  CA  SER A 171     554.815 357.243 386.756  1.00117.67           C  
ATOM    172  CA  VAL A 172     557.366 359.851 387.836  1.00144.99           C  
ATOM    173  CA  ASP A 173     560.013 357.129 388.255  1.00162.92           C  
ATOM    174  CA  GLY A 174     558.000 354.363 389.881  1.00170.58           C  
ATOM    175  CA  GLU A 175     555.148 356.249 391.535  1.00164.63           C  
ATOM    176  CA  GLU A 176     551.649 357.319 390.531  1.00159.46           C  
ATOM    177  CA  PHE A 177     550.817 360.948 391.306  1.00151.28           C  
ATOM    178  CA  GLU A 178     547.875 363.095 392.398  1.00143.70           C  
ATOM    179  CA  GLY A 179     546.574 363.101 388.831  1.00128.29           C  
ATOM    180  CA  GLY A 180     547.140 360.673 385.980  1.00123.90           C  
ATOM    181  CA  LYS A 181     543.780 359.023 386.636  1.00127.80           C  
ATOM    182  CA  ALA A 182     542.351 358.307 383.179  1.00137.40           C  
ATOM    183  CA  SER A 183     539.184 356.303 382.613  1.00138.90           C  
ATOM    184  CA  ASP A 184     538.283 356.277 378.912  1.00141.38           C  
ATOM    185  CA  PHE A 185     539.246 359.891 378.173  1.00123.76           C  
ATOM    186  CA  VAL A 186     538.765 361.635 374.815  1.00105.06           C  
ATOM    187  CA  LEU A 187     541.480 363.855 373.337  1.00 83.48           C  
ATOM    188  CA  ALA A 188     541.356 365.954 370.182  1.00 97.37           C  
HETATM  189  CA  MSE A 189     545.076 366.414 369.621  1.00 98.50           C  
ATOM    190  CA  GLY A 190     546.681 369.216 367.673  1.00106.75           C  
ATOM    191  CA  GLN A 191     545.005 371.677 370.010  1.00 84.27           C  
ATOM    192  CA  GLY A 192     547.691 371.515 372.668  1.00 66.79           C  
ATOM    193  CA  ARG A 193     545.224 370.432 375.326  1.00 72.07           C  
HETATM  194  CA  MSE A 194     547.918 368.144 376.790  1.00 78.34           C  
ATOM    195  CA  ILE A 195     551.454 368.696 378.145  1.00 59.44           C  
ATOM    196  CA  PRO A 196     553.839 369.374 375.265  1.00 65.48           C  
ATOM    197  CA  GLY A 197     555.432 366.128 374.147  1.00 74.09           C  
ATOM    198  CA  PHE A 198     552.688 363.963 375.661  1.00 70.76           C  
ATOM    199  CA  GLU A 199     550.547 363.510 372.565  1.00 86.60           C  
ATOM    200  CA  ASP A 200     553.565 363.583 370.259  1.00 95.96           C  
ATOM    201  CA  GLY A 201     554.503 360.114 371.450  1.00100.58           C  
ATOM    202  CA  ILE A 202     551.038 358.692 370.845  1.00109.86           C  
ATOM    203  CA  LYS A 203     551.383 359.770 367.201  1.00130.08           C  
ATOM    204  CA  GLY A 204     552.200 356.193 366.212  1.00134.57           C  
ATOM    205  CA  HIS A 205     550.395 353.531 368.225  1.00142.29           C  
ATOM    206  CA  LYS A 206     547.698 351.462 366.494  1.00149.84           C  
ATOM    207  CA  ALA A 207     543.979 351.866 367.207  1.00151.17           C  
ATOM    208  CA  GLY A 208     544.196 349.169 369.879  1.00152.72           C  
ATOM    209  CA  GLU A 209     547.741 348.483 371.080  1.00153.36           C  
ATOM    210  CA  GLU A 210     549.085 349.553 374.479  1.00145.78           C  
ATOM    211  CA  PHE A 211     552.463 351.130 375.240  1.00148.60           C  
ATOM    212  CA  THR A 212     554.368 353.453 377.594  1.00134.28           C  
ATOM    213  CA  ILE A 213     555.804 356.886 376.738  1.00117.98           C  
ATOM    214  CA  ASP A 214     558.262 359.345 378.300  1.00108.11           C  
ATOM    215  CA  VAL A 215     557.165 362.924 379.004  1.00 71.93           C  
ATOM    216  CA  THR A 216     558.355 365.920 381.019  1.00 66.72           C  
ATOM    217  CA  PHE A 217     556.388 368.613 382.792  1.00 68.13           C  
ATOM    218  CA  PRO A 218     556.952 372.226 381.758  1.00 68.23           C  
ATOM    219  CA  GLU A 219     559.107 374.001 384.321  1.00 61.75           C  
ATOM    220  CA  GLU A 220     556.246 376.280 385.388  1.00 67.31           C  
ATOM    221  CA  TYR A 221     553.570 373.579 385.805  1.00 45.14           C  
ATOM    222  CA  HIS A 222     551.153 374.545 388.620  1.00 68.48           C  
ATOM    223  CA  ALA A 223     551.888 371.310 390.523  1.00 70.28           C  
ATOM    224  CA  GLU A 224     555.106 372.249 392.309  1.00 77.82           C  
ATOM    225  CA  ASN A 225     555.588 368.508 392.834  1.00 88.56           C  
ATOM    226  CA  LEU A 226     555.639 367.819 389.084  1.00 76.89           C  
ATOM    227  CA  LYS A 227     557.056 370.917 387.409  1.00 72.55           C  
ATOM    228  CA  GLY A 228     560.329 370.083 385.700  1.00 67.56           C  
ATOM    229  CA  LYS A 229     560.245 366.396 386.636  1.00 70.91           C  
ATOM    230  CA  ALA A 230     560.234 363.609 384.049  1.00 70.82           C  
ATOM    231  CA  ALA A 231     557.498 360.991 383.988  1.00 78.81           C  
ATOM    232  CA  LYS A 232     556.217 358.005 382.041  1.00 86.68           C  
ATOM    233  CA  PHE A 233     552.709 357.242 380.830  1.00 85.80           C  
ATOM    234  CA  ALA A 234     550.690 354.041 380.488  1.00 99.51           C  
ATOM    235  CA  ILE A 235     548.515 354.789 377.461  1.00108.94           C  
ATOM    236  CA  ASN A 236     545.483 352.655 376.571  1.00123.19           C  
ATOM    237  CA  LEU A 237     544.765 353.357 372.911  1.00112.44           C  
ATOM    238  CA  LYS A 238     541.308 351.988 372.148  1.00124.60           C  
ATOM    239  CA  LYS A 239     540.035 354.460 369.533  1.00127.68           C  
ATOM    240  CA  VAL A 240     541.382 356.463 366.605  1.00125.89           C  
ATOM    241  CA  GLU A 241     539.214 358.843 364.591  1.00122.94           C  
ATOM    242  CA  GLU A 242     540.000 361.157 361.689  1.00128.13           C  
ATOM    243  CA  ARG A 243     538.135 364.413 361.063  1.00139.14           C  
ATOM    244  CA  GLU A 244     536.736 364.195 357.516  1.00140.37           C  
ATOM    245  CA  LEU A 245     535.892 367.832 356.460  1.00153.91           C  
ATOM    246  CA  PRO A 246     532.093 367.446 356.169  1.00159.74           C  
ATOM    247  CA  GLU A 247     529.184 369.635 355.076  1.00153.38           C  
ATOM    248  CA  LEU A 248     529.415 372.848 353.081  1.00129.53           C  
ATOM    249  CA  THR A 249     525.659 372.736 352.584  1.00132.89           C  
ATOM    250  CA  ALA A 250     523.011 375.198 353.718  1.00133.51           C  
ATOM    251  CA  GLU A 251     522.603 373.503 357.079  1.00131.63           C  
ATOM    252  CA  PHE A 252     526.311 374.224 357.376  1.00111.23           C  
ATOM    253  CA  ILE A 253     527.476 377.600 356.074  1.00 98.08           C  
ATOM    254  CA  LYS A 254     524.256 379.258 357.229  1.00 93.09           C  
ATOM    255  CA  ARG A 255     524.666 377.526 360.575  1.00 90.43           C  
ATOM    256  CA  PHE A 256     527.370 380.144 361.069  1.00 66.62           C  
ATOM    257  CA  GLY A 257     524.851 382.937 360.693  1.00 50.90           C  
ATOM    258  CA  VAL A 258     525.351 383.387 356.966  1.00 55.42           C  
ATOM    259  CA  GLU A 259     521.757 383.717 355.787  1.00 75.31           C  
ATOM    260  CA  ASP A 260     522.226 383.626 351.995  1.00 96.40           C  
ATOM    261  CA  GLY A 261     524.536 380.650 352.606  1.00 83.89           C  
ATOM    262  CA  SER A 262     526.809 381.493 349.657  1.00 78.00           C  
ATOM    263  CA  VAL A 263     530.356 380.170 350.205  1.00 80.95           C  
ATOM    264  CA  GLU A 264     531.429 383.654 349.060  1.00 85.25           C  
ATOM    265  CA  GLY A 265     529.581 384.821 352.168  1.00 83.71           C  
ATOM    266  CA  LEU A 266     531.048 382.528 354.794  1.00 69.20           C  
ATOM    267  CA  ARG A 267     534.408 383.989 353.855  1.00 60.26           C  
ATOM    268  CA  ALA A 268     533.151 387.533 354.527  1.00 53.12           C  
ATOM    269  CA  GLU A 269     531.658 386.403 357.806  1.00 47.65           C  
ATOM    270  CA  VAL A 270     534.938 384.845 358.952  1.00 61.33           C  
ATOM    271  CA  ARG A 271     536.848 387.657 357.264  1.00 62.20           C  
ATOM    272  CA  LYS A 272     534.969 390.382 359.086  1.00 66.68           C  
ATOM    273  CA  ASN A 273     535.172 388.604 362.388  1.00 43.15           C  
HETATM  274  CA  MSE A 274     538.904 388.012 362.141  1.00 44.06           C  
ATOM    275  CA  GLU A 275     539.520 391.661 361.296  1.00 42.45           C  
ATOM    276  CA  ARG A 276     537.482 392.570 364.368  1.00 57.30           C  
ATOM    277  CA  GLU A 277     539.642 390.275 366.481  1.00 49.19           C  
ATOM    278  CA  LEU A 278     542.824 391.799 365.036  1.00 41.34           C  
ATOM    279  CA  LYS A 279     541.641 395.348 365.699  1.00 39.61           C  
ATOM    280  CA  SER A 280     541.309 394.404 369.362  1.00 45.50           C  
ATOM    281  CA  ALA A 281     544.633 392.566 369.596  1.00 34.55           C  
ATOM    282  CA  ILE A 282     546.409 395.610 368.192  1.00 40.46           C  
ATOM    283  CA  ARG A 283     544.760 398.004 370.625  1.00 35.37           C  
ATOM    284  CA  ASN A 284     545.999 395.687 373.388  1.00 48.80           C  
ATOM    285  CA  ARG A 285     549.538 395.261 372.097  1.00 27.90           C  
ATOM    286  CA  VAL A 286     549.923 399.004 371.853  1.00 31.47           C  
ATOM    287  CA  LYS A 287     548.071 399.809 375.053  1.00 36.04           C  
ATOM    288  CA  SER A 288     549.718 397.120 377.221  1.00 43.04           C  
ATOM    289  CA  GLN A 289     553.222 398.190 376.020  1.00 41.45           C  
ATOM    290  CA  ALA A 290     552.602 401.844 376.793  1.00 28.79           C  
ATOM    291  CA  ILE A 291     551.220 400.979 380.213  1.00 32.13           C  
ATOM    292  CA  GLU A 292     554.010 398.604 381.136  1.00 46.00           C  
ATOM    293  CA  GLY A 293     556.471 401.344 380.225  1.00 25.81           C  
ATOM    294  CA  LEU A 294     554.561 403.765 382.380  1.00 39.12           C  
ATOM    295  CA  VAL A 295     554.330 401.497 385.434  1.00 37.51           C  
ATOM    296  CA  LYS A 296     557.903 400.223 385.274  1.00 25.48           C  
ATOM    297  CA  ALA A 297     559.336 403.752 385.227  1.00 38.86           C  
ATOM    298  CA  ASN A 298     557.105 405.083 388.007  1.00 42.20           C  
ATOM    299  CA  ASP A 299     557.067 403.164 391.267  1.00 67.70           C  
ATOM    300  CA  ILE A 300     554.730 404.945 393.651  1.00 52.89           C  
ATOM    301  CA  ASP A 301     553.250 404.596 397.155  1.00 61.11           C  
ATOM    302  CA  VAL A 302     549.741 403.156 396.872  1.00 53.72           C  
ATOM    303  CA  PRO A 303     547.221 403.990 399.641  1.00 36.58           C  
ATOM    304  CA  ALA A 304     545.694 400.870 401.241  1.00 42.66           C  
ATOM    305  CA  ALA A 305     542.032 401.896 401.228  1.00 38.93           C  
ATOM    306  CA  LEU A 306     542.179 402.068 397.426  1.00 45.58           C  
ATOM    307  CA  ILE A 307     543.696 398.594 397.015  1.00 42.02           C  
ATOM    308  CA  ASP A 308     541.081 397.105 399.336  1.00 39.21           C  
ATOM    309  CA  SER A 309     538.134 398.437 397.301  1.00 36.77           C  
ATOM    310  CA  GLU A 310     539.649 397.099 394.120  1.00 38.23           C  
ATOM    311  CA  ILE A 311     539.907 393.694 395.712  1.00 43.00           C  
ATOM    312  CA  ASP A 312     536.198 393.841 396.563  1.00 48.35           C  
ATOM    313  CA  VAL A 313     535.473 394.962 393.023  1.00 42.66           C  
ATOM    314  CA  LEU A 314     537.566 392.047 391.764  1.00 45.29           C  
ATOM    315  CA  ARG A 315     535.917 389.527 394.070  1.00 53.80           C  
ATOM    316  CA  ARG A 316     532.391 390.578 393.094  1.00 45.53           C  
ATOM    317  CA  GLN A 317     533.344 390.310 389.409  1.00 45.87           C  
ATOM    318  CA  ALA A 318     534.666 386.821 390.225  1.00 62.07           C  
ATOM    319  CA  ALA A 319     531.527 385.752 392.059  1.00 59.52           C  
ATOM    320  CA  GLN A 320     529.327 387.039 389.240  1.00 65.71           C  
ATOM    321  CA  ARG A 321     531.062 384.448 387.017  1.00 78.75           C  
ATOM    322  CA  PHE A 322     531.168 381.865 389.801  1.00102.14           C  
ATOM    323  CA  GLY A 323     527.479 381.436 389.070  1.00 95.26           C  
ATOM    324  CA  GLY A 324     527.081 384.700 390.926  1.00 94.31           C  
ATOM    325  CA  ASN A 325     526.967 384.632 394.720  1.00 83.13           C  
ATOM    326  CA  GLU A 326     526.338 388.162 396.029  1.00101.96           C  
ATOM    327  CA  LYS A 327     528.478 388.720 399.136  1.00 94.16           C  
ATOM    328  CA  GLN A 328     529.917 385.208 398.969  1.00 85.82           C  
ATOM    329  CA  ALA A 329     532.612 387.077 397.074  1.00 76.98           C  
ATOM    330  CA  LEU A 330     533.625 388.808 400.298  1.00 81.11           C  
ATOM    331  CA  GLU A 331     534.468 385.190 401.090  1.00 86.51           C  
ATOM    332  CA  LEU A 332     537.079 384.545 398.341  1.00 61.87           C  
ATOM    333  CA  PRO A 333     540.581 384.798 399.857  1.00 44.59           C  
ATOM    334  CA  ARG A 334     542.107 388.279 399.633  1.00 51.69           C  
ATOM    335  CA  GLU A 335     545.558 387.302 398.348  1.00 53.60           C  
ATOM    336  CA  LEU A 336     543.771 385.928 395.297  1.00 52.83           C  
ATOM    337  CA  PHE A 337     543.383 389.459 393.904  1.00 45.39           C  
ATOM    338  CA  GLU A 338     545.769 391.498 396.085  1.00 55.93           C  
ATOM    339  CA  GLU A 339     548.404 391.693 393.331  1.00 45.48           C  
ATOM    340  CA  GLN A 340     546.362 392.643 390.273  1.00 38.22           C  
ATOM    341  CA  ALA A 341     544.335 394.882 392.577  1.00 35.90           C  
ATOM    342  CA  LYS A 342     547.351 396.959 393.521  1.00 49.86           C  
ATOM    343  CA  ARG A 343     548.153 397.015 389.825  1.00 51.25           C  
ATOM    344  CA  ARG A 344     544.911 398.651 388.750  1.00 44.84           C  
ATOM    345  CA  VAL A 345     545.148 401.147 391.540  1.00 33.40           C  
ATOM    346  CA  VAL A 346     548.652 402.084 390.268  1.00 30.01           C  
ATOM    347  CA  VAL A 347     547.799 402.273 386.570  1.00 27.66           C  
ATOM    348  CA  GLY A 348     544.991 404.552 387.654  1.00 28.02           C  
ATOM    349  CA  LEU A 349     546.972 406.937 389.755  1.00 35.26           C  
ATOM    350  CA  LEU A 350     549.556 407.177 386.961  1.00 36.53           C  
ATOM    351  CA  LEU A 351     547.210 407.575 384.020  1.00 39.26           C  
ATOM    352  CA  GLY A 352     545.568 410.125 386.282  1.00 52.46           C  
ATOM    353  CA  GLU A 353     548.670 412.240 386.721  1.00 54.97           C  
ATOM    354  CA  VAL A 354     548.939 411.944 382.953  1.00 27.03           C  
ATOM    355  CA  ILE A 355     545.465 413.396 382.670  1.00 48.38           C  
ATOM    356  CA  ARG A 356     546.262 416.238 385.068  1.00 45.65           C  
ATOM    357  CA  THR A 357     549.559 417.243 383.474  1.00 72.19           C  
ATOM    358  CA  ASN A 358     547.914 417.452 380.038  1.00 53.20           C  
ATOM    359  CA  GLU A 359     544.637 418.783 381.487  1.00 63.44           C  
ATOM    360  CA  LEU A 360     542.623 416.306 379.432  1.00 53.72           C  
ATOM    361  CA  LYS A 361     538.844 416.125 379.033  1.00 51.76           C  
ATOM    362  CA  ALA A 362     536.607 413.266 378.006  1.00 40.91           C  
ATOM    363  CA  ASP A 363     536.307 413.760 374.247  1.00 26.51           C  
ATOM    364  CA  GLU A 364     532.535 413.538 373.706  1.00 46.26           C  
ATOM    365  CA  GLU A 365     532.852 412.868 369.995  1.00 54.97           C  
ATOM    366  CA  ARG A 366     534.802 409.760 370.981  1.00 48.01           C  
ATOM    367  CA  VAL A 367     532.317 408.854 373.693  1.00 39.46           C  
ATOM    368  CA  LYS A 368     529.546 408.946 371.081  1.00 51.36           C  
ATOM    369  CA  GLY A 369     531.569 406.612 368.891  1.00 40.02           C  
ATOM    370  CA  LEU A 370     532.202 404.176 371.713  1.00 44.42           C  
ATOM    371  CA  ILE A 371     528.481 404.078 372.385  1.00 33.95           C  
ATOM    372  CA  GLU A 372     527.841 403.294 368.738  1.00 47.52           C  
ATOM    373  CA  GLU A 373     530.376 400.465 368.545  1.00 58.77           C  
HETATM  374  CA  MSE A 374     528.664 399.134 371.633  1.00 44.45           C  
ATOM    375  CA  ALA A 375     525.109 399.587 370.286  1.00 60.01           C  
ATOM    376  CA  SER A 376     526.209 398.241 366.900  1.00 70.50           C  
ATOM    377  CA  ALA A 377     525.748 394.675 368.127  1.00 62.97           C  
ATOM    378  CA  TYR A 378     522.038 394.859 368.941  1.00 55.34           C  
ATOM    379  CA  GLU A 379     518.969 394.391 366.734  1.00 62.65           C  
ATOM    380  CA  ASP A 380     518.238 398.092 367.000  1.00 52.50           C  
ATOM    381  CA  PRO A 381     521.283 400.259 367.809  1.00 48.19           C  
ATOM    382  CA  LYS A 382     519.231 403.458 367.889  1.00 47.39           C  
ATOM    383  CA  GLU A 383     517.259 402.336 370.945  1.00 64.08           C  
ATOM    384  CA  VAL A 384     520.416 401.483 372.912  1.00 55.38           C  
ATOM    385  CA  ILE A 385     521.765 404.944 372.099  1.00 47.88           C  
ATOM    386  CA  GLU A 386     518.467 406.644 372.934  1.00 52.49           C  
ATOM    387  CA  PHE A 387     518.612 404.755 376.209  1.00 54.56           C  
ATOM    388  CA  TYR A 388     522.255 405.330 376.949  1.00 55.00           C  
ATOM    389  CA  SER A 389     521.988 409.058 376.210  1.00 53.43           C  
ATOM    390  CA  LYS A 390     519.243 409.843 378.763  1.00 45.73           C  
ATOM    391  CA  ASN A 391     521.092 408.017 381.594  1.00 68.50           C  
ATOM    392  CA  LYS A 392     523.877 410.286 382.946  1.00 76.61           C  
ATOM    393  CA  GLU A 393     525.191 407.372 385.044  1.00 76.30           C  
ATOM    394  CA  LEU A 394     526.231 405.110 382.169  1.00 70.42           C  
HETATM  395  CA  MSE A 395     527.350 408.258 380.341  1.00 55.21           C  
ATOM    396  CA  ASP A 396     529.982 409.363 382.836  1.00 63.76           C  
ATOM    397  CA  ASN A 397     531.475 405.862 382.898  1.00 47.54           C  
HETATM  398  CA  MSE A 398     531.693 405.906 379.125  1.00 30.48           C  
ATOM    399  CA  ARG A 399     533.453 409.243 379.460  1.00 43.90           C  
ATOM    400  CA  ASN A 400     535.987 407.625 381.828  1.00 38.58           C  
ATOM    401  CA  VAL A 401     536.566 404.914 379.240  1.00 35.58           C  
ATOM    402  CA  ALA A 402     537.285 407.547 376.591  1.00 46.76           C  
ATOM    403  CA  LEU A 403     539.361 409.545 379.040  1.00 49.71           C  
ATOM    404  CA  GLU A 404     541.428 406.482 379.742  1.00 53.81           C  
ATOM    405  CA  GLU A 405     542.195 405.826 376.062  1.00 49.08           C  
ATOM    406  CA  GLN A 406     543.149 409.489 375.830  1.00 44.51           C  
ATOM    407  CA  ALA A 407     545.535 409.247 378.782  1.00 25.44           C  
ATOM    408  CA  VAL A 408     547.135 406.302 377.016  1.00 47.47           C  
ATOM    409  CA  GLU A 409     547.687 408.156 373.743  1.00 46.83           C  
ATOM    410  CA  ALA A 410     549.286 410.983 375.759  1.00 35.17           C  
ATOM    411  CA  VAL A 411     551.975 408.451 376.666  1.00 45.65           C  
ATOM    412  CA  LEU A 412     552.193 406.854 373.235  1.00 53.25           C  
ATOM    413  CA  ALA A 413     552.946 410.375 372.035  1.00 54.54           C  
ATOM    414  CA  LYS A 414     555.862 411.249 374.314  1.00 43.59           C  
ATOM    415  CA  ALA A 415     557.287 407.764 373.691  1.00 42.35           C  
ATOM    416  CA  LYS A 416     559.706 405.923 371.405  1.00 56.92           C  
ATOM    417  CA  VAL A 417     557.138 404.305 369.176  1.00 41.56           C  
ATOM    418  CA  THR A 418     558.933 401.922 366.847  1.00 52.89           C  
ATOM    419  CA  GLU A 419     556.737 400.141 364.258  1.00 43.16           C  
ATOM    420  CA  LYS A 420     556.899 396.867 362.357  1.00 58.47           C  
ATOM    421  CA  GLU A 421     555.113 394.442 360.074  1.00 59.92           C  
ATOM    422  CA  THR A 422     554.013 391.015 361.271  1.00 66.78           C  
ATOM    423  CA  THR A 423     551.337 388.320 360.989  1.00 58.79           C  
ATOM    424  CA  PHE A 424     547.750 388.017 362.145  1.00 56.25           C  
ATOM    425  CA  ASN A 425     548.798 385.005 364.198  1.00 53.55           C  
ATOM    426  CA  GLU A 426     551.500 386.949 366.003  1.00 70.41           C  
ATOM    427  CA  LEU A 427     548.862 389.357 367.237  1.00 58.31           C  
HETATM  428  CA  MSE A 428     546.437 386.558 367.898  1.00 60.13           C  
ATOM    429  CA  ASN A 429     548.582 385.950 370.934  1.00 58.49           C  
ATOM    430  CA  GLN A 430     546.187 387.912 373.150  1.00 61.93           C  
ATOM    431  CA  GLN A 431     547.927 386.571 376.260  1.00 87.77           C  
TER     432      GLN A 431                                                      
ATOM    433  CA  MET B   1     494.212 404.213 460.642  1.00 20.00           C  
ATOM    434  CA  ILE B   2     491.009 403.466 459.371  1.00 20.00           C  
ATOM    435  CA  ARG B   3     493.140 402.124 456.443  1.00 20.00           C  
ATOM    436  CA  GLU B   4     490.633 399.315 456.658  1.00 20.00           C  
ATOM    437  CA  GLU B   5     489.072 399.513 453.241  1.00 20.00           C  
ATOM    438  CA  ARG B   6     490.988 399.085 450.012  1.00 20.00           C  
ATOM    439  CA  LEU B   7     493.685 401.753 450.302  1.00 20.00           C  
ATOM    440  CA  LEU B   8     495.785 398.966 448.808  1.00 20.00           C  
ATOM    441  CA  LYS B   9     495.040 399.863 445.181  1.00 20.00           C  
ATOM    442  CA  VAL B  10     492.608 402.764 444.875  1.00 20.00           C  
ATOM    443  CA  LEU B  11     495.084 404.665 442.699  1.00 20.00           C  
ATOM    444  CA  ARG B  12     497.113 403.603 439.635  1.00 20.00           C  
ATOM    445  CA  ALA B  13     498.600 404.909 436.379  1.00 20.00           C  
ATOM    446  CA  PRO B  14     499.205 408.613 435.596  1.00 20.00           C  
ATOM    447  CA  HIS B  15     497.786 410.109 432.404  1.00 20.00           C  
ATOM    448  CA  VAL B  16     500.442 412.276 430.771  1.00 20.00           C  
ATOM    449  CA  SER B  17     497.595 413.885 428.858  1.00 20.00           C  
ATOM    450  CA  GLU B  18     497.502 417.356 427.338  1.00 20.00           C  
ATOM    451  CA  LYS B  19     496.109 418.502 430.680  1.00 20.00           C  
ATOM    452  CA  ALA B  20     499.436 417.365 432.129  1.00 20.00           C  
ATOM    453  CA  SER B  21     501.950 420.118 432.913  1.00 20.00           C  
ATOM    454  CA  THR B  22     499.380 422.560 431.541  1.00 20.00           C  
ATOM    455  CA  ALA B  23     497.381 422.163 434.744  1.00 20.00           C  
ATOM    456  CA  MET B  24     500.026 423.505 437.155  1.00 20.00           C  
ATOM    457  CA  GLU B  25     499.568 426.875 438.851  1.00 20.00           C  
ATOM    458  CA  LYS B  26     499.842 427.328 442.608  1.00 20.00           C  
ATOM    459  CA  SER B  27     499.421 423.567 442.926  1.00 20.00           C  
ATOM    460  CA  ASN B  28     500.368 420.649 440.751  1.00 20.00           C  
ATOM    461  CA  THR B  29     497.482 418.217 440.878  1.00 20.00           C  
ATOM    462  CA  ILE B  30     497.273 414.858 439.232  1.00 20.00           C  
ATOM    463  CA  VAL B  31     495.144 412.487 437.201  1.00 20.00           C  
ATOM    464  CA  LEU B  32     495.637 408.830 438.036  1.00 20.00           C  
ATOM    465  CA  LYS B  33     493.591 406.220 436.212  1.00 20.00           C  
ATOM    466  CA  VAL B  34     491.961 405.567 439.602  1.00 20.00           C  
ATOM    467  CA  ALA B  35     489.770 402.472 439.919  1.00 20.00           C  
ATOM    468  CA  LYS B  36     486.147 402.800 438.791  1.00 20.00           C  
ATOM    469  CA  ASP B  37     485.111 402.892 442.456  1.00 20.00           C  
ATOM    470  CA  ALA B  38     487.658 404.512 444.756  1.00 20.00           C  
ATOM    471  CA  THR B  39     485.562 407.464 445.924  1.00 20.00           C  
ATOM    472  CA  LYS B  40     487.176 410.780 446.844  1.00 20.00           C  
ATOM    473  CA  ALA B  41     488.105 410.252 450.498  1.00 20.00           C  
ATOM    474  CA  GLU B  42     489.887 406.958 449.796  1.00 20.00           C  
ATOM    475  CA  ILE B  43     491.755 408.709 446.984  1.00 20.00           C  
ATOM    476  CA  LYS B  44     492.759 411.576 449.270  1.00 20.00           C  
ATOM    477  CA  ALA B  45     494.226 409.005 451.660  1.00 20.00           C  
ATOM    478  CA  ALA B  46     495.743 406.821 448.946  1.00 20.00           C  
ATOM    479  CA  VAL B  47     498.181 409.573 448.058  1.00 20.00           C  
ATOM    480  CA  GLN B  48     498.745 410.092 451.784  1.00 20.00           C  
ATOM    481  CA  LYS B  49     500.527 406.869 452.757  1.00 20.00           C  
ATOM    482  CA  LEU B  50     502.050 406.628 449.284  1.00 20.00           C  
ATOM    483  CA  PHE B  51     503.644 409.404 447.202  1.00 20.00           C  
ATOM    484  CA  GLU B  52     504.065 411.107 450.598  1.00 20.00           C  
ATOM    485  CA  VAL B  53     502.508 414.334 449.306  1.00 20.00           C  
ATOM    486  CA  GLU B  54     499.890 416.636 450.873  1.00 20.00           C  
ATOM    487  CA  VAL B  55     496.524 416.503 449.106  1.00 20.00           C  
ATOM    488  CA  GLU B  56     494.193 419.500 449.400  1.00 20.00           C  
ATOM    489  CA  VAL B  57     491.160 418.144 447.572  1.00 20.00           C  
ATOM    490  CA  VAL B  58     489.989 415.506 445.074  1.00 20.00           C  
ATOM    491  CA  ASN B  59     487.430 415.647 442.236  1.00 20.00           C  
ATOM    492  CA  THR B  60     487.316 412.678 439.834  1.00 20.00           C  
ATOM    493  CA  LEU B  61     484.670 411.623 437.297  1.00 20.00           C  
ATOM    494  CA  VAL B  62     484.259 408.803 434.743  1.00 20.00           C  
ATOM    495  CA  VAL B  63     484.985 409.074 430.982  1.00 20.00           C  
ATOM    496  CA  LYS B  64     483.668 406.189 428.831  1.00 20.00           C  
ATOM    497  CA  GLY B  65     485.330 404.298 425.974  1.00 20.00           C  
ATOM    498  CA  LYS B  66     483.169 403.069 423.079  1.00 20.00           C  
ATOM    499  CA  VAL B  67     484.201 401.517 419.775  1.00 20.00           C  
ATOM    500  CA  LYS B  68     483.181 398.908 417.246  1.00 20.00           C  
ATOM    501  CA  ARG B  69     485.607 396.031 416.787  1.00 20.00           C  
ATOM    502  CA  HIS B  70     484.786 392.406 416.021  1.00 20.00           C  
ATOM    503  CA  GLY B  71     485.153 389.394 413.765  1.00 20.00           C  
ATOM    504  CA  GLN B  72     482.465 391.200 411.792  1.00 20.00           C  
ATOM    505  CA  ARG B  73     480.627 394.044 413.525  1.00 20.00           C  
ATOM    506  CA  ILE B  74     480.116 394.396 417.285  1.00 20.00           C  
ATOM    507  CA  GLY B  75     482.731 396.013 419.519  1.00 20.00           C  
ATOM    508  CA  ARG B  76     482.010 397.937 422.706  1.00 20.00           C  
ATOM    509  CA  ARG B  77     482.946 400.468 425.387  1.00 20.00           C  
ATOM    510  CA  SER B  78     485.731 400.317 427.994  1.00 20.00           C  
ATOM    511  CA  ASP B  79     485.151 402.679 430.989  1.00 20.00           C  
ATOM    512  CA  TRP B  80     487.528 404.517 433.381  1.00 20.00           C  
ATOM    513  CA  LYS B  81     487.650 407.098 436.187  1.00 20.00           C  
ATOM    514  CA  LYS B  82     489.815 410.222 436.049  1.00 20.00           C  
ATOM    515  CA  ALA B  83     490.867 412.015 439.241  1.00 20.00           C  
ATOM    516  CA  TYR B  84     492.555 415.417 439.375  1.00 20.00           C  
ATOM    517  CA  VAL B  85     493.199 415.771 443.105  1.00 20.00           C  
ATOM    518  CA  THR B  86     495.194 418.834 444.131  1.00 20.00           C  
ATOM    519  CA  LEU B  87     498.257 418.840 446.375  1.00 20.00           C  
ATOM    520  CA  LYS B  88     499.975 422.027 447.558  1.00 20.00           C  
ATOM    521  CA  GLU B  89     502.887 424.327 446.697  1.00 20.00           C  
ATOM    522  CA  GLY B  90     505.697 424.082 449.244  1.00 20.00           C  
ATOM    523  CA  GLN B  91     506.273 420.483 448.160  1.00 20.00           C  
ATOM    524  CA  ASN B  92     507.367 419.631 444.619  1.00 20.00           C  
ATOM    525  CA  LEU B  93     507.900 416.233 443.010  1.00 20.00           C  
ATOM    526  CA  ASP B  94     511.116 415.934 445.035  1.00 20.00           C  
ATOM    527  CA  PHE B  95     513.052 412.678 444.826  1.00 20.00           C  
ATOM    528  CA  VAL B  96     510.967 410.693 442.352  1.00 20.00           C  
ATOM    529  CA  GLY B  97     510.737 409.603 438.736  1.00 20.00           C  
ATOM    530  CA  GLY B  98     508.439 411.647 436.540  1.00 20.00           C  
ATOM    531  CA  ALA B  99     506.945 410.084 433.420  1.00 20.00           C  
TER     532      ALA B  99                                                      
ATOM    533  CA  ALA C   1     503.581 361.657 420.535  1.00 20.00           C  
ATOM    534  CA  ALA C   2     506.631 362.894 418.630  1.00 20.00           C  
ATOM    535  CA  LYS C   3     509.169 362.337 421.412  1.00 20.00           C  
ATOM    536  CA  ILE C   4     511.776 363.609 418.960  1.00 20.00           C  
ATOM    537  CA  ARG C   5     513.341 366.269 421.183  1.00 20.00           C  
ATOM    538  CA  ARG C   6     515.835 368.992 420.271  1.00 20.00           C  
ATOM    539  CA  ASP C   7     519.329 368.186 418.987  1.00 20.00           C  
ATOM    540  CA  ASP C   8     517.685 364.967 417.827  1.00 20.00           C  
ATOM    541  CA  GLU C   9     519.648 364.352 414.629  1.00 20.00           C  
ATOM    542  CA  VAL C  10     517.208 363.009 412.044  1.00 20.00           C  
ATOM    543  CA  ILE C  11     517.270 362.604 408.273  1.00 20.00           C  
ATOM    544  CA  VAL C  12     514.944 363.850 405.540  1.00 20.00           C  
ATOM    545  CA  LEU C  13     512.229 361.468 404.306  1.00 20.00           C  
ATOM    546  CA  THR C  14     509.061 361.621 402.209  1.00 20.00           C  
ATOM    547  CA  GLY C  15     510.431 363.898 399.501  1.00 20.00           C  
ATOM    548  CA  LYS C  16     512.003 367.107 398.225  1.00 20.00           C  
ATOM    549  CA  ASP C  17     515.476 367.286 399.766  1.00 20.00           C  
ATOM    550  CA  LYS C  18     515.509 363.684 401.009  1.00 20.00           C  
ATOM    551  CA  GLY C  19     518.600 361.743 402.006  1.00 20.00           C  
ATOM    552  CA  LYS C  20     519.811 364.887 403.739  1.00 20.00           C  
ATOM    553  CA  ARG C  21     521.465 365.192 407.147  1.00 20.00           C  
ATOM    554  CA  GLY C  22     519.889 367.778 409.458  1.00 20.00           C  
ATOM    555  CA  LYS C  23     519.720 367.581 413.255  1.00 20.00           C  
ATOM    556  CA  VAL C  24     518.448 369.462 416.310  1.00 20.00           C  
ATOM    557  CA  LYS C  25     515.259 370.771 414.699  1.00 20.00           C  
ATOM    558  CA  ASN C  26     512.715 372.792 416.666  1.00 20.00           C  
ATOM    559  CA  VAL C  27     509.716 370.485 416.744  1.00 20.00           C  
ATOM    560  CA  LEU C  28     507.311 370.890 419.598  1.00 20.00           C  
ATOM    561  CA  SER C  29     504.399 368.974 421.100  1.00 20.00           C  
ATOM    562  CA  SER C  30     501.876 369.542 418.304  1.00 20.00           C  
ATOM    563  CA  GLY C  31     504.443 371.999 416.909  1.00 20.00           C  
ATOM    564  CA  LYS C  32     506.939 372.272 413.998  1.00 20.00           C  
ATOM    565  CA  VAL C  33     510.099 370.429 412.807  1.00 20.00           C  
ATOM    566  CA  ILE C  34     512.552 372.960 411.375  1.00 20.00           C  
ATOM    567  CA  VAL C  35     515.426 370.445 411.330  1.00 20.00           C  
ATOM    568  CA  GLU C  36     518.134 371.829 409.023  1.00 20.00           C  
ATOM    569  CA  GLY C  37     517.599 370.150 405.675  1.00 20.00           C  
ATOM    570  CA  ILE C  38     514.308 371.809 404.727  1.00 20.00           C  
ATOM    571  CA  ASN C  39     514.367 375.396 403.493  1.00 20.00           C  
ATOM    572  CA  LEU C  40     514.381 377.121 400.141  1.00 20.00           C  
ATOM    573  CA  VAL C  41     515.599 380.741 399.852  1.00 20.00           C  
ATOM    574  CA  LYS C  42     512.574 382.986 400.586  1.00 20.00           C  
ATOM    575  CA  LYS C  43     511.977 386.686 401.440  1.00 20.00           C  
ATOM    576  CA  HIS C  44     510.806 389.455 403.806  1.00 20.00           C  
ATOM    577  CA  GLN C  45     509.420 392.921 402.936  1.00 20.00           C  
ATOM    578  CA  LYS C  46     510.187 395.971 405.059  1.00 20.00           C  
ATOM    579  CA  PRO C  47     507.458 395.280 407.587  1.00 20.00           C  
ATOM    580  CA  VAL C  48     508.891 397.617 410.186  1.00 20.00           C  
ATOM    581  CA  PRO C  49     508.029 401.058 408.933  1.00 20.00           C  
ATOM    582  CA  ALA C  50     511.026 402.539 410.737  1.00 20.00           C  
ATOM    583  CA  LEU C  51     514.635 403.359 410.074  1.00 20.00           C  
ATOM    584  CA  ASN C  52     515.485 399.684 410.103  1.00 20.00           C  
ATOM    585  CA  GLN C  53     513.457 398.597 407.101  1.00 20.00           C  
ATOM    586  CA  PRO C  54     515.223 395.260 406.785  1.00 20.00           C  
ATOM    587  CA  GLY C  55     514.259 392.114 404.961  1.00 20.00           C  
ATOM    588  CA  GLY C  56     515.151 388.506 405.672  1.00 20.00           C  
ATOM    589  CA  ILE C  57     515.409 386.894 402.272  1.00 20.00           C  
ATOM    590  CA  VAL C  58     517.856 384.365 403.755  1.00 20.00           C  
ATOM    591  CA  GLU C  59     517.130 381.334 405.919  1.00 20.00           C  
ATOM    592  CA  LYS C  60     513.749 380.309 407.252  1.00 20.00           C  
ATOM    593  CA  GLU C  61     511.936 377.076 407.936  1.00 20.00           C  
ATOM    594  CA  ALA C  62     510.160 374.401 405.946  1.00 20.00           C  
ATOM    595  CA  ALA C  63     507.785 372.766 408.429  1.00 20.00           C  
ATOM    596  CA  ILE C  64     507.167 369.358 406.859  1.00 20.00           C  
ATOM    597  CA  GLN C  65     505.513 366.595 408.822  1.00 20.00           C  
ATOM    598  CA  VAL C  66     507.220 364.974 411.775  1.00 20.00           C  
ATOM    599  CA  SER C  67     507.270 361.993 409.412  1.00 20.00           C  
ATOM    600  CA  ASN C  68     510.996 362.286 408.680  1.00 20.00           C  
ATOM    601  CA  VAL C  69     513.718 359.631 408.701  1.00 20.00           C  
ATOM    602  CA  ALA C  70     513.449 358.375 412.271  1.00 20.00           C  
ATOM    603  CA  ILE C  71     516.554 359.387 414.255  1.00 20.00           C  
ATOM    604  CA  PHE C  72     518.649 356.721 412.438  1.00 20.00           C  
ATOM    605  CA  ASN C  73     521.913 355.317 413.819  1.00 20.00           C  
ATOM    606  CA  ALA C  74     523.456 352.957 411.272  1.00 20.00           C  
ATOM    607  CA  ALA C  75     521.499 353.222 408.018  1.00 20.00           C  
ATOM    608  CA  THR C  76     518.239 355.199 408.115  1.00 20.00           C  
ATOM    609  CA  GLY C  77     514.772 355.260 409.666  1.00 20.00           C  
ATOM    610  CA  LYS C  78     514.783 352.463 412.231  1.00 20.00           C  
ATOM    611  CA  ALA C  79     511.514 353.170 414.036  1.00 20.00           C  
ATOM    612  CA  ASP C  80     511.865 354.029 417.718  1.00 20.00           C  
ATOM    613  CA  ARG C  81     508.538 352.345 418.493  1.00 20.00           C  
ATOM    614  CA  VAL C  82     509.628 350.527 421.637  1.00 20.00           C  
ATOM    615  CA  GLY C  83     509.557 351.533 425.280  1.00 20.00           C  
ATOM    616  CA  PHE C  84     512.396 351.124 427.737  1.00 20.00           C  
ATOM    617  CA  ARG C  85     511.746 350.462 431.414  1.00 20.00           C  
ATOM    618  CA  PHE C  86     512.772 351.154 435.011  1.00 20.00           C  
ATOM    619  CA  GLU C  87     514.900 354.085 433.867  1.00 20.00           C  
ATOM    620  CA  ASP C  88     514.108 357.705 434.724  1.00 20.00           C  
ATOM    621  CA  GLY C  89     510.809 358.361 436.498  1.00 20.00           C  
ATOM    622  CA  LYS C  90     509.330 360.824 434.066  1.00 20.00           C  
ATOM    623  CA  LYS C  91     510.199 359.054 430.840  1.00 20.00           C  
ATOM    624  CA  VAL C  92     511.978 356.005 429.618  1.00 20.00           C  
ATOM    625  CA  ARG C  93     512.562 356.611 425.909  1.00 20.00           C  
ATOM    626  CA  PHE C  94     513.733 353.508 424.065  1.00 20.00           C  
ATOM    627  CA  PHE C  95     514.989 353.409 420.482  1.00 20.00           C  
ATOM    628  CA  LYS C  96     515.188 351.735 417.067  1.00 20.00           C  
ATOM    629  CA  SER C  97     514.274 348.057 416.885  1.00 20.00           C  
ATOM    630  CA  ASN C  98     517.961 347.273 416.367  1.00 20.00           C  
ATOM    631  CA  SER C  99     519.418 347.392 419.908  1.00 20.00           C  
ATOM    632  CA  GLU C 100     518.015 348.913 423.094  1.00 20.00           C  
ATOM    633  CA  THR C 101     517.806 352.421 424.539  1.00 20.00           C  
ATOM    634  CA  ILE C 102     520.178 354.904 422.898  1.00 20.00           C  
TER     635      ILE C 102                                                      
ATOM    636  CA  MET D   1     512.393 383.637 447.058  1.00 20.00           C  
ATOM    637  CA  LYS D   2     508.857 383.760 445.690  1.00 20.00           C  
ATOM    638  CA  ALA D   3     506.832 380.886 444.191  1.00 20.00           C  
ATOM    639  CA  LYS D   4     505.689 377.899 446.234  1.00 20.00           C  
ATOM    640  CA  GLU D   5     508.167 378.232 449.108  1.00 20.00           C  
ATOM    641  CA  LEU D   6     507.479 378.424 452.871  1.00 20.00           C  
ATOM    642  CA  ARG D   7     504.105 376.635 452.742  1.00 20.00           C  
ATOM    643  CA  GLU D   8     503.932 376.008 456.505  1.00 20.00           C  
ATOM    644  CA  LYS D   9     504.767 379.462 457.861  1.00 20.00           C  
ATOM    645  CA  SER D  10     501.964 379.517 460.444  1.00 20.00           C  
ATOM    646  CA  VAL D  11     503.811 382.564 461.708  1.00 20.00           C  
ATOM    647  CA  GLU D  12     502.581 384.087 458.487  1.00 20.00           C  
ATOM    648  CA  GLU D  13     503.158 387.621 457.277  1.00 20.00           C  
ATOM    649  CA  LEU D  14     501.247 387.880 453.999  1.00 20.00           C  
ATOM    650  CA  ASN D  15     500.328 391.514 454.710  1.00 20.00           C  
ATOM    651  CA  THR D  16     501.578 394.404 452.573  1.00 20.00           C  
ATOM    652  CA  GLU D  17     503.144 391.737 450.358  1.00 20.00           C  
ATOM    653  CA  LEU D  18     501.120 393.305 447.566  1.00 20.00           C  
ATOM    654  CA  LEU D  19     501.533 397.079 447.924  1.00 20.00           C  
ATOM    655  CA  ASN D  20     505.227 396.919 448.789  1.00 20.00           C  
ATOM    656  CA  LEU D  21     505.588 395.037 445.510  1.00 20.00           C  
ATOM    657  CA  LEU D  22     503.204 397.441 443.775  1.00 20.00           C  
ATOM    658  CA  ARG D  23     506.298 399.208 442.440  1.00 20.00           C  
ATOM    659  CA  GLU D  24     505.257 398.095 438.961  1.00 20.00           C  
ATOM    660  CA  GLN D  25     501.488 398.553 438.714  1.00 20.00           C  
ATOM    661  CA  PHE D  26     501.758 401.362 441.245  1.00 20.00           C  
ATOM    662  CA  ASN D  27     504.877 403.136 439.970  1.00 20.00           C  
ATOM    663  CA  LEU D  28     506.930 401.548 437.195  1.00 20.00           C  
ATOM    664  CA  ARG D  29     503.891 400.639 435.055  1.00 20.00           C  
ATOM    665  CA  MET D  30     503.099 404.304 434.553  1.00 20.00           C  
ATOM    666  CA  GLN D  31     505.208 404.995 431.509  1.00 20.00           C  
ATOM    667  CA  ALA D  32     508.449 403.509 430.198  1.00 20.00           C  
ATOM    668  CA  ALA D  33     510.223 401.972 433.199  1.00 20.00           C  
ATOM    669  CA  SER D  34     508.285 398.918 434.443  1.00 20.00           C  
ATOM    670  CA  GLY D  35     511.334 396.992 433.350  1.00 20.00           C  
ATOM    671  CA  GLN D  36     511.774 397.921 429.701  1.00 20.00           C  
ATOM    672  CA  LEU D  37     514.589 395.564 428.722  1.00 20.00           C  
ATOM    673  CA  GLN D  38     516.637 393.877 431.476  1.00 20.00           C  
ATOM    674  CA  GLN D  39     513.614 392.457 433.336  1.00 20.00           C  
ATOM    675  CA  SER D  40     510.194 393.646 432.160  1.00 20.00           C  
ATOM    676  CA  HIS D  41     506.910 391.998 433.109  1.00 20.00           C  
ATOM    677  CA  LEU D  42     507.047 390.288 436.494  1.00 20.00           C  
ATOM    678  CA  LEU D  43     503.460 390.336 437.781  1.00 20.00           C  
ATOM    679  CA  LYS D  44     501.943 387.429 435.836  1.00 20.00           C  
ATOM    680  CA  GLN D  45     505.397 385.921 435.370  1.00 20.00           C  
ATOM    681  CA  VAL D  46     505.959 385.521 439.100  1.00 20.00           C  
ATOM    682  CA  ARG D  47     504.295 388.068 441.410  1.00 20.00           C  
ATOM    683  CA  ARG D  48     501.014 386.393 440.498  1.00 20.00           C  
ATOM    684  CA  ASP D  49     501.678 384.069 443.436  1.00 20.00           C  
ATOM    685  CA  VAL D  50     499.552 386.404 445.565  1.00 20.00           C  
ATOM    686  CA  ALA D  51     496.946 383.652 445.314  1.00 20.00           C  
ATOM    687  CA  ARG D  52     499.221 380.946 446.700  1.00 20.00           C  
ATOM    688  CA  VAL D  53     499.733 383.051 449.843  1.00 20.00           C  
ATOM    689  CA  LYS D  54     496.180 384.273 450.449  1.00 20.00           C  
ATOM    690  CA  THR D  55     495.029 380.795 449.469  1.00 20.00           C  
ATOM    691  CA  LEU D  56     497.222 379.241 452.160  1.00 20.00           C  
ATOM    692  CA  LEU D  57     496.072 381.730 454.789  1.00 20.00           C  
ATOM    693  CA  ASN D  58     492.564 380.806 453.656  1.00 20.00           C  
ATOM    694  CA  GLU D  59     493.457 377.150 454.186  1.00 20.00           C  
ATOM    695  CA  LYS D  60     495.159 377.626 457.560  1.00 20.00           C  
ATOM    696  CA  ALA D  61     491.720 378.683 458.753  1.00 20.00           C  
ATOM    697  CA  GLY D  62     491.118 375.609 460.887  1.00 20.00           C  
ATOM    698  CA  ALA D  63     493.854 376.570 463.315  1.00 20.00           C  
TER     699      ALA D  63                                                      
MASTER      150    0   11    0    0    0    0    6  695    4    0   55          
END                                                                             
