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Database: PDB
Entry: 1MHS
LinkDB: 1MHS
Original site: 1MHS 
HEADER    MEMBRANE PROTEIN, PROTON TRANSPORT      21-AUG-02   1MHS              
TITLE     MODEL OF NEUROSPORA CRASSA PROTON ATPASE                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PLASMA MEMBRANE ATPASE;                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PROTON PUMP;                                                
COMPND   5 EC: 3.6.3.6                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: NEUROSPORA CRASSA;                              
SOURCE   3 ORGANISM_TAXID: 5141;                                                
SOURCE   4 STRAIN: FGSC 4761;                                                   
SOURCE   5 OTHER_DETAILS: ISOLATED FROM PLASMA MEMBRANE OF CULTURED NEUROSPORA  
SOURCE   6 CELLS                                                                
KEYWDS    ION TRANSPORT, PROTON PUMP, MEMBRANE PROTEIN, P-TYPE ATPASE, ACTIVE   
KEYWDS   2 TRANSPORT, PROTON TRANSPORT                                          
EXPDTA    ELECTRON CRYSTALLOGRAPHY                                              
AUTHOR    W.KUHLBRANDT                                                          
REVDAT   3   18-JUL-18 1MHS    1       REMARK                                   
REVDAT   2   24-FEB-09 1MHS    1       VERSN                                    
REVDAT   1   18-SEP-02 1MHS    0                                                
JRNL        AUTH   W.KUHLBRANDT,J.ZEELEN,J.DIETRICH                             
JRNL        TITL   STRUCTURE, MECHANISM AND REGULATION OF THE NEUROSPORA PLASMA 
JRNL        TITL 2 MEMBRANE H+-ATPASE                                           
JRNL        REF    SCIENCE                       V. 297  1692 2002              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   12169656                                                     
JRNL        DOI    10.1126/SCIENCE.1072574                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.AUER,G.A.SCARBOROUGH,W.KUHLBRANDT                          
REMARK   1  TITL   THREE-DIMENSIONAL MAP OF THE PLASMA MEMBRANE H+-ATPASE IN    
REMARK   1  TITL 2 THE OPEN CONFORMATION                                        
REMARK   1  REF    NATURE                        V. 392   840 1998              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    8.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : NULL                                                 
REMARK   3   AUTHORS     : NULL                                                 
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 8.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : NULL                            
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 14082                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1MHS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-AUG-02.                  
REMARK 100 THE DEPOSITION ID IS D_1000016920.                                   
REMARK 240                                                                      
REMARK 240 EXPERIMENTAL DETAILS                                                 
REMARK 240   RECONSTRUCTION METHOD          : CRYSTALLOGRAPHY                   
REMARK 240   SAMPLE TYPE                    : 2D ARRAY                          
REMARK 240   SPECIMEN TYPE                  : VITREOUS ICE (CRYO EM)            
REMARK 240 DATA ACQUISITION                                                     
REMARK 240   DATE OF DATA COLLECTION        : NULL                              
REMARK 240   TEMPERATURE           (KELVIN) : NULL                              
REMARK 240   PH                             : NULL                              
REMARK 240   NUMBER OF CRYSTALS USED        : NULL                              
REMARK 240   MICROSCOPE MODEL               : JEOL 3000SFF                      
REMARK 240   DETECTOR TYPE                  : KODAK SO-163 FILM                 
REMARK 240   ACCELERATION VOLTAGE (KV)      : 300                               
REMARK 240   NUMBER OF UNIQUE REFLECTIONS   : NULL                              
REMARK 240   RESOLUTION RANGE HIGH      (A) : NULL                              
REMARK 240   RESOLUTION RANGE LOW       (A) : NULL                              
REMARK 240   DATA SCALING SOFTWARE          : NULL                              
REMARK 240   COMPLETENESS FOR RANGE     (%) : NULL                              
REMARK 240   DATA REDUNDANCY                : NULL                              
REMARK 240 IN THE HIGHEST RESOLUTION SHELL                                      
REMARK 240   HIGHEST RESOLUTION SHELL, RANGE HIGH (A) :NULL                     
REMARK 240   HIGHEST RESOLUTION SHELL, RANGE LOW  (A) :NULL                     
REMARK 240   COMPLETENESS FOR SHELL     (%) : NULL                              
REMARK 240   DATA REDUNDANCY IN SHELL       : NULL                              
REMARK 240   R MERGE FOR SHELL          (I) : NULL                              
REMARK 240   METHOD USED TO DETERMINE THE STRUCTURE: NULL                       
REMARK 240   SOFTWARE USED                  : NULL                              
REMARK 240   STARTING MODEL                 : NULL                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-Z                                              
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 295                                                                      
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY                                        
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW             
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS              
REMARK 295 IN THIS ENTRY.  APPLYING THE APPROPRIATE MTRIX                       
REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD               
REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.              
REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH             
REMARK 295 ATOMS ARE NOT FOUND IN THE ENTRY.                                    
REMARK 295               APPLIED TO          TRANSFORMED TO                     
REMARK 295   TRANSFORM CHAIN  RESIDUES       CHAIN  RESIDUES     RMSD           
REMARK 295     SSS                                                              
REMARK 295    M  1       A    1 .. 920         B    1 .. 920       ?            
REMARK 295    WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS                        
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 THIS ENTRY CONTAINS A PORTION OF THE BIOLOGICALLY                    
REMARK 300 SIGNIFICANT MULTIMER.  SEE REMARK 350 FOR INFORMATION                
REMARK 300 ON GENERATING THE BIOLOGICAL MOLECULE(S)                             
REMARK 300 ASSEMBLY COMPONENTS                                                  
REMARK 300 COM_ID: 1                                                            
REMARK 300 NAME:PLASMA MEMBRANE PROTON ATPASE HEXAMERIC ASSEMBLY                
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1EUL   RELATED DB: PDB                                   
REMARK 900 2.6 A X-RAY STRUCTURE OF SARCOPLASMIC CALCIUM ATPASE IN E1 STATE     
REMARK 900 RELATED ID: 1IWO   RELATED DB: PDB                                   
REMARK 900 3.1 A X-RAY STRUCTURE OF SARCOPLASMIC CALCIUM ATPASE IN E2 STATE     
DBREF  1MHS A    1   920  UNP    P07038   PMA1_NEUCR       1    920             
DBREF  1MHS B    1   920  UNP    P07038   PMA1_NEUCR       1    920             
SEQRES   1 A  920  MET ALA ASP HIS SER ALA SER GLY ALA PRO ALA LEU SER          
SEQRES   2 A  920  THR ASN ILE GLU SER GLY LYS PHE ASP GLU LYS ALA ALA          
SEQRES   3 A  920  GLU ALA ALA ALA TYR GLN PRO LYS PRO LYS VAL GLU ASP          
SEQRES   4 A  920  ASP GLU ASP GLU ASP ILE ASP ALA LEU ILE GLU ASP LEU          
SEQRES   5 A  920  GLU SER HIS ASP GLY HIS ASP ALA GLU GLU GLU GLU GLU          
SEQRES   6 A  920  GLU ALA THR PRO GLY GLY GLY ARG VAL VAL PRO GLU ASP          
SEQRES   7 A  920  MET LEU GLN THR ASP THR ARG VAL GLY LEU THR SER GLU          
SEQRES   8 A  920  GLU VAL VAL GLN ARG ARG ARG LYS TYR GLY LEU ASN GLN          
SEQRES   9 A  920  MET LYS GLU GLU LYS GLU ASN HIS PHE LEU LYS PHE LEU          
SEQRES  10 A  920  GLY PHE PHE VAL GLY PRO ILE GLN PHE VAL MET GLU GLY          
SEQRES  11 A  920  ALA ALA VAL LEU ALA ALA GLY LEU GLU ASP TRP VAL ASP          
SEQRES  12 A  920  PHE GLY VAL ILE CYS GLY LEU LEU LEU LEU ASN ALA VAL          
SEQRES  13 A  920  VAL GLY PHE VAL GLN GLU PHE GLN ALA GLY SER ILE VAL          
SEQRES  14 A  920  ASP GLU LEU LYS LYS THR LEU ALA LEU LYS ALA VAL VAL          
SEQRES  15 A  920  LEU ARG ASP GLY THR LEU LYS GLU ILE GLU ALA PRO GLU          
SEQRES  16 A  920  VAL VAL PRO GLY ASP ILE LEU GLN VAL GLU GLU GLY THR          
SEQRES  17 A  920  ILE ILE PRO ALA ASP GLY ARG ILE VAL THR ASP ASP ALA          
SEQRES  18 A  920  PHE LEU GLN VAL ASP GLN SER ALA LEU THR GLY GLU SER          
SEQRES  19 A  920  LEU ALA VAL ASP LYS HIS LYS GLY ASP GLN VAL PHE ALA          
SEQRES  20 A  920  SER SER ALA VAL LYS ARG GLY GLU ALA PHE VAL VAL ILE          
SEQRES  21 A  920  THR ALA THR GLY ASP ASN THR PHE VAL GLY ARG ALA ALA          
SEQRES  22 A  920  ALA LEU VAL ASN ALA ALA SER GLY GLY SER GLY HIS PHE          
SEQRES  23 A  920  THR GLU VAL LEU ASN GLY ILE GLY THR ILE LEU LEU ILE          
SEQRES  24 A  920  LEU VAL ILE PHE THR LEU LEU ILE VAL TRP VAL SER SER          
SEQRES  25 A  920  PHE TYR ARG SER ASN PRO ILE VAL GLN ILE LEU GLU PHE          
SEQRES  26 A  920  THR LEU ALA ILE THR ILE ILE GLY VAL PRO VAL GLY LEU          
SEQRES  27 A  920  PRO ALA VAL VAL THR THR THR MET ALA VAL GLY ALA ALA          
SEQRES  28 A  920  TYR LEU ALA LYS LYS LYS ALA ILE VAL GLN LYS LEU SER          
SEQRES  29 A  920  ALA ILE GLU SER LEU ALA GLY VAL GLU ILE LEU CYS SER          
SEQRES  30 A  920  ASP LYS THR GLY THR LEU THR LYS ASN LYS LEU SER LEU          
SEQRES  31 A  920  HIS ASP PRO TYR THR VAL ALA GLY VAL ASP PRO GLU ASP          
SEQRES  32 A  920  LEU MET LEU THR ALA CYS LEU ALA ALA SER ARG LYS LYS          
SEQRES  33 A  920  LYS GLY ILE ASP ALA ILE ASP LYS ALA PHE LEU LYS SER          
SEQRES  34 A  920  LEU LYS TYR TYR PRO ARG ALA LYS SER VAL LEU SER LYS          
SEQRES  35 A  920  TYR LYS VAL LEU GLN PHE HIS PRO PHE ASP PRO VAL SER          
SEQRES  36 A  920  LYS LYS VAL VAL ALA VAL VAL GLU SER PRO GLN GLY GLU          
SEQRES  37 A  920  ARG ILE THR CYS VAL LYS GLY ALA PRO LEU PHE VAL LEU          
SEQRES  38 A  920  LYS THR VAL GLU GLU ASP HIS PRO ILE PRO GLU GLU VAL          
SEQRES  39 A  920  ASP GLN ALA TYR LYS ASN LYS VAL ALA GLU PHE ALA THR          
SEQRES  40 A  920  ARG GLY PHE ARG SER LEU GLY VAL ALA ARG LYS ARG GLY          
SEQRES  41 A  920  GLU GLY SER TRP GLU ILE LEU GLY ILE MET PRO CYS MET          
SEQRES  42 A  920  ASP PRO PRO ARG HIS ASP THR TYR LYS THR VAL CYS GLU          
SEQRES  43 A  920  ALA LYS THR LEU GLY LEU SER ILE LYS MET LEU THR GLY          
SEQRES  44 A  920  ASP ALA VAL GLY ILE ALA ARG GLU THR SER ARG GLN LEU          
SEQRES  45 A  920  GLY LEU GLY THR ASN ILE TYR ASN ALA GLU ARG LEU GLY          
SEQRES  46 A  920  LEU GLY GLY GLY GLY ASP MET PRO GLY SER GLU VAL TYR          
SEQRES  47 A  920  ASP PHE VAL GLU ALA ALA ASP GLY PHE ALA GLU VAL PHE          
SEQRES  48 A  920  PRO GLN HIS LYS TYR ASN VAL VAL GLU ILE LEU GLN GLN          
SEQRES  49 A  920  ARG GLY TYR LEU VAL ALA MET THR GLY ASP GLY VAL ASN          
SEQRES  50 A  920  ASP ALA PRO SER LEU LYS LYS ALA ASP THR GLY ILE ALA          
SEQRES  51 A  920  VAL GLU GLY SER SER ASP ALA ALA ARG SER ALA ALA ASP          
SEQRES  52 A  920  ILE VAL PHE LEU ALA PRO GLY LEU GLY ALA ILE ILE ASP          
SEQRES  53 A  920  ALA LEU LYS THR SER ARG GLN ILE PHE HIS ARG MET TYR          
SEQRES  54 A  920  ALA TYR VAL VAL TYR ARG ILE ALA LEU SER ILE HIS LEU          
SEQRES  55 A  920  GLU ILE PHE LEU GLY LEU TRP ILE ALA ILE LEU ASN ARG          
SEQRES  56 A  920  SER LEU ASN ILE GLU LEU VAL VAL PHE ILE ALA ILE PHE          
SEQRES  57 A  920  ALA ASP VAL ALA THR LEU ALA ILE ALA TYR ASP ASN ALA          
SEQRES  58 A  920  PRO TYR SER GLN THR PRO VAL LYS TRP ASN LEU PRO LYS          
SEQRES  59 A  920  LEU TRP GLY MET SER VAL LEU LEU GLY VAL VAL LEU ALA          
SEQRES  60 A  920  VAL GLY THR TRP ILE THR VAL THR THR MET TYR ALA GLN          
SEQRES  61 A  920  GLY GLU ASN GLY GLY ILE VAL GLN ASN PHE GLY ASN MET          
SEQRES  62 A  920  ASP GLU VAL LEU PHE LEU GLN ILE SER LEU THR GLU ASN          
SEQRES  63 A  920  TRP LEU ILE PHE ILE THR ARG ALA ASN GLY PRO PHE TRP          
SEQRES  64 A  920  SER SER ILE PRO SER TRP GLN LEU SER GLY ALA ILE PHE          
SEQRES  65 A  920  LEU VAL ASP ILE LEU ALA THR CYS PHE THR ILE TRP GLY          
SEQRES  66 A  920  TRP PHE GLU HIS SER ASP THR SER ILE VAL ALA VAL VAL          
SEQRES  67 A  920  ARG ILE TRP ILE PHE SER PHE GLY ILE PHE CYS ILE MET          
SEQRES  68 A  920  GLY GLY VAL TYR TYR ILE LEU GLN ASP SER VAL GLY PHE          
SEQRES  69 A  920  ASP ASN LEU MET HIS GLY LYS SER PRO LYS GLY ASN GLN          
SEQRES  70 A  920  LYS GLN ARG SER LEU GLU ASP PHE VAL VAL SER LEU GLN          
SEQRES  71 A  920  ARG VAL SER THR GLN HIS GLU LYS SER GLN                      
SEQRES   1 B  920  MET ALA ASP HIS SER ALA SER GLY ALA PRO ALA LEU SER          
SEQRES   2 B  920  THR ASN ILE GLU SER GLY LYS PHE ASP GLU LYS ALA ALA          
SEQRES   3 B  920  GLU ALA ALA ALA TYR GLN PRO LYS PRO LYS VAL GLU ASP          
SEQRES   4 B  920  ASP GLU ASP GLU ASP ILE ASP ALA LEU ILE GLU ASP LEU          
SEQRES   5 B  920  GLU SER HIS ASP GLY HIS ASP ALA GLU GLU GLU GLU GLU          
SEQRES   6 B  920  GLU ALA THR PRO GLY GLY GLY ARG VAL VAL PRO GLU ASP          
SEQRES   7 B  920  MET LEU GLN THR ASP THR ARG VAL GLY LEU THR SER GLU          
SEQRES   8 B  920  GLU VAL VAL GLN ARG ARG ARG LYS TYR GLY LEU ASN GLN          
SEQRES   9 B  920  MET LYS GLU GLU LYS GLU ASN HIS PHE LEU LYS PHE LEU          
SEQRES  10 B  920  GLY PHE PHE VAL GLY PRO ILE GLN PHE VAL MET GLU GLY          
SEQRES  11 B  920  ALA ALA VAL LEU ALA ALA GLY LEU GLU ASP TRP VAL ASP          
SEQRES  12 B  920  PHE GLY VAL ILE CYS GLY LEU LEU LEU LEU ASN ALA VAL          
SEQRES  13 B  920  VAL GLY PHE VAL GLN GLU PHE GLN ALA GLY SER ILE VAL          
SEQRES  14 B  920  ASP GLU LEU LYS LYS THR LEU ALA LEU LYS ALA VAL VAL          
SEQRES  15 B  920  LEU ARG ASP GLY THR LEU LYS GLU ILE GLU ALA PRO GLU          
SEQRES  16 B  920  VAL VAL PRO GLY ASP ILE LEU GLN VAL GLU GLU GLY THR          
SEQRES  17 B  920  ILE ILE PRO ALA ASP GLY ARG ILE VAL THR ASP ASP ALA          
SEQRES  18 B  920  PHE LEU GLN VAL ASP GLN SER ALA LEU THR GLY GLU SER          
SEQRES  19 B  920  LEU ALA VAL ASP LYS HIS LYS GLY ASP GLN VAL PHE ALA          
SEQRES  20 B  920  SER SER ALA VAL LYS ARG GLY GLU ALA PHE VAL VAL ILE          
SEQRES  21 B  920  THR ALA THR GLY ASP ASN THR PHE VAL GLY ARG ALA ALA          
SEQRES  22 B  920  ALA LEU VAL ASN ALA ALA SER GLY GLY SER GLY HIS PHE          
SEQRES  23 B  920  THR GLU VAL LEU ASN GLY ILE GLY THR ILE LEU LEU ILE          
SEQRES  24 B  920  LEU VAL ILE PHE THR LEU LEU ILE VAL TRP VAL SER SER          
SEQRES  25 B  920  PHE TYR ARG SER ASN PRO ILE VAL GLN ILE LEU GLU PHE          
SEQRES  26 B  920  THR LEU ALA ILE THR ILE ILE GLY VAL PRO VAL GLY LEU          
SEQRES  27 B  920  PRO ALA VAL VAL THR THR THR MET ALA VAL GLY ALA ALA          
SEQRES  28 B  920  TYR LEU ALA LYS LYS LYS ALA ILE VAL GLN LYS LEU SER          
SEQRES  29 B  920  ALA ILE GLU SER LEU ALA GLY VAL GLU ILE LEU CYS SER          
SEQRES  30 B  920  ASP LYS THR GLY THR LEU THR LYS ASN LYS LEU SER LEU          
SEQRES  31 B  920  HIS ASP PRO TYR THR VAL ALA GLY VAL ASP PRO GLU ASP          
SEQRES  32 B  920  LEU MET LEU THR ALA CYS LEU ALA ALA SER ARG LYS LYS          
SEQRES  33 B  920  LYS GLY ILE ASP ALA ILE ASP LYS ALA PHE LEU LYS SER          
SEQRES  34 B  920  LEU LYS TYR TYR PRO ARG ALA LYS SER VAL LEU SER LYS          
SEQRES  35 B  920  TYR LYS VAL LEU GLN PHE HIS PRO PHE ASP PRO VAL SER          
SEQRES  36 B  920  LYS LYS VAL VAL ALA VAL VAL GLU SER PRO GLN GLY GLU          
SEQRES  37 B  920  ARG ILE THR CYS VAL LYS GLY ALA PRO LEU PHE VAL LEU          
SEQRES  38 B  920  LYS THR VAL GLU GLU ASP HIS PRO ILE PRO GLU GLU VAL          
SEQRES  39 B  920  ASP GLN ALA TYR LYS ASN LYS VAL ALA GLU PHE ALA THR          
SEQRES  40 B  920  ARG GLY PHE ARG SER LEU GLY VAL ALA ARG LYS ARG GLY          
SEQRES  41 B  920  GLU GLY SER TRP GLU ILE LEU GLY ILE MET PRO CYS MET          
SEQRES  42 B  920  ASP PRO PRO ARG HIS ASP THR TYR LYS THR VAL CYS GLU          
SEQRES  43 B  920  ALA LYS THR LEU GLY LEU SER ILE LYS MET LEU THR GLY          
SEQRES  44 B  920  ASP ALA VAL GLY ILE ALA ARG GLU THR SER ARG GLN LEU          
SEQRES  45 B  920  GLY LEU GLY THR ASN ILE TYR ASN ALA GLU ARG LEU GLY          
SEQRES  46 B  920  LEU GLY GLY GLY GLY ASP MET PRO GLY SER GLU VAL TYR          
SEQRES  47 B  920  ASP PHE VAL GLU ALA ALA ASP GLY PHE ALA GLU VAL PHE          
SEQRES  48 B  920  PRO GLN HIS LYS TYR ASN VAL VAL GLU ILE LEU GLN GLN          
SEQRES  49 B  920  ARG GLY TYR LEU VAL ALA MET THR GLY ASP GLY VAL ASN          
SEQRES  50 B  920  ASP ALA PRO SER LEU LYS LYS ALA ASP THR GLY ILE ALA          
SEQRES  51 B  920  VAL GLU GLY SER SER ASP ALA ALA ARG SER ALA ALA ASP          
SEQRES  52 B  920  ILE VAL PHE LEU ALA PRO GLY LEU GLY ALA ILE ILE ASP          
SEQRES  53 B  920  ALA LEU LYS THR SER ARG GLN ILE PHE HIS ARG MET TYR          
SEQRES  54 B  920  ALA TYR VAL VAL TYR ARG ILE ALA LEU SER ILE HIS LEU          
SEQRES  55 B  920  GLU ILE PHE LEU GLY LEU TRP ILE ALA ILE LEU ASN ARG          
SEQRES  56 B  920  SER LEU ASN ILE GLU LEU VAL VAL PHE ILE ALA ILE PHE          
SEQRES  57 B  920  ALA ASP VAL ALA THR LEU ALA ILE ALA TYR ASP ASN ALA          
SEQRES  58 B  920  PRO TYR SER GLN THR PRO VAL LYS TRP ASN LEU PRO LYS          
SEQRES  59 B  920  LEU TRP GLY MET SER VAL LEU LEU GLY VAL VAL LEU ALA          
SEQRES  60 B  920  VAL GLY THR TRP ILE THR VAL THR THR MET TYR ALA GLN          
SEQRES  61 B  920  GLY GLU ASN GLY GLY ILE VAL GLN ASN PHE GLY ASN MET          
SEQRES  62 B  920  ASP GLU VAL LEU PHE LEU GLN ILE SER LEU THR GLU ASN          
SEQRES  63 B  920  TRP LEU ILE PHE ILE THR ARG ALA ASN GLY PRO PHE TRP          
SEQRES  64 B  920  SER SER ILE PRO SER TRP GLN LEU SER GLY ALA ILE PHE          
SEQRES  65 B  920  LEU VAL ASP ILE LEU ALA THR CYS PHE THR ILE TRP GLY          
SEQRES  66 B  920  TRP PHE GLU HIS SER ASP THR SER ILE VAL ALA VAL VAL          
SEQRES  67 B  920  ARG ILE TRP ILE PHE SER PHE GLY ILE PHE CYS ILE MET          
SEQRES  68 B  920  GLY GLY VAL TYR TYR ILE LEU GLN ASP SER VAL GLY PHE          
SEQRES  69 B  920  ASP ASN LEU MET HIS GLY LYS SER PRO LYS GLY ASN GLN          
SEQRES  70 B  920  LYS GLN ARG SER LEU GLU ASP PHE VAL VAL SER LEU GLN          
SEQRES  71 B  920  ARG VAL SER THR GLN HIS GLU LYS SER GLN                      
HELIX    1   1 HIS A    4  ALA A    9  1                                   6    
HELIX    2   2 ASP A   22  ALA A   29  1                                   8    
HELIX    3   3 GLU A   41  GLU A   53  1                                  13    
HELIX    4   4 ALA A   67  ARG A   73  1                                   7    
HELIX    5   5 SER A   90  TYR A  100  1                                  11    
HELIX    6   6 HIS A  112  LEU A  117  1                                   6    
HELIX    7   7 LEU A  117  ALA A  135  1                                  19    
HELIX    8   8 VAL A  142  GLU A  171  1                                  30    
HELIX    9   9 GLY A  284  SER A  311  1                                  28    
HELIX   10  10 PRO A  318  VAL A  334  1                                  17    
HELIX   11  11 GLY A  337  LYS A  356  1                                  20    
HELIX   12  12 ALA A  365  GLY A  371  1                                   7    
HELIX   13  13 GLU A  402  ALA A  411  1                                  10    
HELIX   14  14 ALA A  421  TYR A  433  1                                  13    
HELIX   15  15 LYS A  437  SER A  441  5                                   5    
HELIX   16  16 ALA A  476  VAL A  484  1                                   9    
HELIX   17  17 PRO A  491  THR A  507  1                                  17    
HELIX   18  18 ARG A  537  GLY A  551  1                                  15    
HELIX   19  19 ALA A  561  GLY A  573  1                                  13    
HELIX   20  20 ASP A  591  ASP A  599  5                                   9    
HELIX   21  21 GLN A  613  GLN A  624  1                                  12    
HELIX   22  22 GLY A  635  ASN A  637  5                                   3    
HELIX   23  23 ASP A  638  ALA A  645  1                                   8    
HELIX   24  24 SER A  655  ALA A  661  1                                   7    
HELIX   25  25 LEU A  671  ILE A  712  1                                  42    
HELIX   26  26 ASN A  718  ASP A  730  1                                  13    
HELIX   27  27 VAL A  731  ILE A  736  1                                   6    
HELIX   28  28 ALA A  741  THR A  746  5                                   6    
HELIX   29  29 MET A  758  TYR A  778  1                                  21    
HELIX   30  30 ASN A  792  ILE A  809  1                                  18    
HELIX   31  31 SER A  824  ILE A  843  1                                  20    
HELIX   32  32 ALA A  856  SER A  864  1                                   9    
HELIX   33  33 PHE A  865  ILE A  877  1                                  13    
HELIX   34  34 PHE A  884  SER A  892  1                                   9    
HELIX   35  35 GLY A  895  GLN A  910  1                                  16    
HELIX   36  36 VAL A  912  GLN A  920  1                                   9    
HELIX   37  37 HIS B    4  ALA B    9  1                                   6    
HELIX   38  38 ASP B   22  ALA B   29  1                                   8    
HELIX   39  39 GLU B   41  GLU B   53  1                                  13    
HELIX   40  40 ALA B   67  ARG B   73  1                                   7    
HELIX   41  41 SER B   90  TYR B  100  1                                  11    
HELIX   42  42 HIS B  112  LEU B  117  1                                   6    
HELIX   43  43 LEU B  117  ALA B  135  1                                  19    
HELIX   44  44 VAL B  142  GLU B  171  1                                  30    
HELIX   45  45 GLY B  284  SER B  311  1                                  28    
HELIX   46  46 PRO B  318  VAL B  334  1                                  17    
HELIX   47  47 GLY B  337  LYS B  356  1                                  20    
HELIX   48  48 ALA B  365  GLY B  371  1                                   7    
HELIX   49  49 GLU B  402  ALA B  411  1                                  10    
HELIX   50  50 ALA B  421  TYR B  433  1                                  13    
HELIX   51  51 LYS B  437  SER B  441  5                                   5    
HELIX   52  52 ALA B  476  VAL B  484  1                                   9    
HELIX   53  53 PRO B  491  THR B  507  1                                  17    
HELIX   54  54 ARG B  537  GLY B  551  1                                  15    
HELIX   55  55 ALA B  561  GLY B  573  1                                  13    
HELIX   56  56 ASP B  591  ASP B  599  5                                   9    
HELIX   57  57 GLN B  613  GLN B  624  1                                  12    
HELIX   58  58 GLY B  635  ASN B  637  5                                   3    
HELIX   59  59 ASP B  638  ALA B  645  1                                   8    
HELIX   60  60 SER B  655  ALA B  661  1                                   7    
HELIX   61  61 LEU B  671  ILE B  712  1                                  42    
HELIX   62  62 ASN B  718  ASP B  730  1                                  13    
HELIX   63  63 VAL B  731  ILE B  736  1                                   6    
HELIX   64  64 ALA B  741  THR B  746  5                                   6    
HELIX   65  65 MET B  758  TYR B  778  1                                  21    
HELIX   66  66 ASN B  792  ILE B  809  1                                  18    
HELIX   67  67 SER B  824  ILE B  843  1                                  20    
HELIX   68  68 ALA B  856  SER B  864  1                                   9    
HELIX   69  69 PHE B  865  ILE B  877  1                                  13    
HELIX   70  70 PHE B  884  SER B  892  1                                   9    
HELIX   71  71 GLY B  895  GLN B  910  1                                  16    
HELIX   72  72 VAL B  912  GLN B  920  1                                   9    
SHEET    1   A 6 LEU A 188  GLU A 190  0                                        
SHEET    2   A 6 VAL A 181  LEU A 183 -1  N  VAL A 182   O  LYS A 189           
SHEET    3   A 6 ILE A 201  VAL A 204 -1  O  ILE A 201   N  LEU A 183           
SHEET    4   A 6 ALA A 256  ALA A 262 -1  O  ALA A 256   N  VAL A 204           
SHEET    5   A 6 ASP A 213  ASP A 219 -1  N  THR A 218   O  PHE A 257           
SHEET    6   A 6 GLN A 244  VAL A 245 -1  O  VAL A 245   N  GLY A 214           
SHEET    1   B 2 GLN A 224  VAL A 225  0                                        
SHEET    2   B 2 VAL A 237  ASP A 238 -1  O  VAL A 237   N  VAL A 225           
SHEET    1   C 3 ILE A 374  ASP A 378  0                                        
SHEET    2   C 3 SER A 553  THR A 558  1  O  SER A 553   N  LEU A 375           
SHEET    3   C 3 PHE A 607  ALA A 608  1  O  PHE A 607   N  THR A 558           
SHEET    1   D 4 VAL A 445  ASP A 452  0                                        
SHEET    2   D 4 LYS A 457  VAL A 462 -1  O  VAL A 459   N  HIS A 449           
SHEET    3   D 4 ILE A 470  GLY A 475 -1  O  LYS A 474   N  VAL A 458           
SHEET    4   D 4 GLY A 514  VAL A 515 -1  O  GLY A 514   N  GLY A 475           
SHEET    1   E 3 ALA A 630  MET A 631  0                                        
SHEET    2   E 3 THR A 647  VAL A 651  1  O  ILE A 649   N  MET A 631           
SHEET    3   E 3 ILE A 664  PHE A 666  1  O  PHE A 666   N  ALA A 650           
SHEET    1   F 6 LEU B 188  GLU B 190  0                                        
SHEET    2   F 6 VAL B 181  LEU B 183 -1  N  VAL B 182   O  LYS B 189           
SHEET    3   F 6 ILE B 201  VAL B 204 -1  O  ILE B 201   N  LEU B 183           
SHEET    4   F 6 ALA B 256  ALA B 262 -1  O  ALA B 256   N  VAL B 204           
SHEET    5   F 6 ASP B 213  ASP B 219 -1  N  THR B 218   O  PHE B 257           
SHEET    6   F 6 GLN B 244  VAL B 245 -1  O  VAL B 245   N  GLY B 214           
SHEET    1   G 2 GLN B 224  VAL B 225  0                                        
SHEET    2   G 2 VAL B 237  ASP B 238 -1  O  VAL B 237   N  VAL B 225           
SHEET    1   H 3 ILE B 374  ASP B 378  0                                        
SHEET    2   H 3 SER B 553  THR B 558  1  O  SER B 553   N  LEU B 375           
SHEET    3   H 3 PHE B 607  ALA B 608  1  O  PHE B 607   N  THR B 558           
SHEET    1   I 4 VAL B 445  ASP B 452  0                                        
SHEET    2   I 4 LYS B 457  VAL B 462 -1  O  VAL B 459   N  HIS B 449           
SHEET    3   I 4 ILE B 470  GLY B 475 -1  O  LYS B 474   N  VAL B 458           
SHEET    4   I 4 GLY B 514  VAL B 515 -1  O  GLY B 514   N  GLY B 475           
SHEET    1   J 3 ALA B 630  MET B 631  0                                        
SHEET    2   J 3 THR B 647  VAL B 651  1  O  ILE B 649   N  MET B 631           
SHEET    3   J 3 ILE B 664  PHE B 666  1  O  PHE B 666   N  ALA B 650           
CRYST1  167.000  167.000  250.000  90.00  90.00 120.00 P 3 2 1      12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.005988  0.003457  0.000000        0.00000                         
SCALE2      0.000000  0.006914  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004000        0.00000                         
MTRIX1   1  0.500000  0.866000  0.000000       84.50000    1                    
MTRIX2   1 -0.866000  0.500000  0.000000       48.20000    1                    
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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