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Database: PDB
Entry: 1RBA
LinkDB: 1RBA
Original site: 1RBA 
HEADER    LYASE(CARBON-CARBON)                    18-NOV-91   1RBA              
TITLE     SUBSTITUTION OF ASP193 TO ASN AT THE ACTIVE SITE OF RIBULOSE-1,5-     
TITLE    2 BISPHOSPHATE CARBOXYLASE RESULTS IN CONFORMATIONAL CHANGES           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RUBISCO;                                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 4.1.1.39;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RHODOSPIRILLUM RUBRUM;                          
SOURCE   3 ORGANISM_TAXID: 1085                                                 
KEYWDS    LYASE(CARBON-CARBON)                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.SCHNEIDER,E.SODERLIND                                               
REVDAT   3   07-SEP-11 1RBA    1       SEQADV REMARK                            
REVDAT   2   24-FEB-09 1RBA    1       VERSN                                    
REVDAT   1   31-JAN-94 1RBA    0                                                
JRNL        AUTH   E.SODERLIND,G.SCHNEIDER,S.GUTTERIDGE                         
JRNL        TITL   SUBSTITUTION OF ASP193 TO ASN AT THE ACTIVE SITE OF          
JRNL        TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE RESULTS IN             
JRNL        TITL 3 CONFORMATIONAL CHANGES.                                      
JRNL        REF    EUR.J.BIOCHEM.                V. 206   729 1992              
JRNL        REFN                   ISSN 0014-2956                               
JRNL        PMID   1606957                                                      
JRNL        DOI    10.1111/J.1432-1033.1992.TB16979.X                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROLSQ                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 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 + TEST SET) : 0.207                           
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                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6585                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 110                                     
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  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.019 ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1RBA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       34.65000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6710 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL                        
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     GLU A    56                                                      
REMARK 465     VAL A    57                                                      
REMARK 465     CYS A    58                                                      
REMARK 465     THR A    59                                                      
REMARK 465     THR A    60                                                      
REMARK 465     ASP A    61                                                      
REMARK 465     ASP A    62                                                      
REMARK 465     PHE A    63                                                      
REMARK 465     MET A   325                                                      
REMARK 465     GLY A   326                                                      
REMARK 465     PHE A   327                                                      
REMARK 465     GLY A   328                                                      
REMARK 465     LYS A   329                                                      
REMARK 465     MET A   330                                                      
REMARK 465     GLU A   331                                                      
REMARK 465     GLY A   332                                                      
REMARK 465     GLU A   333                                                      
REMARK 465     SER A   334                                                      
REMARK 465     GLY A   442                                                      
REMARK 465     ASP A   443                                                      
REMARK 465     ALA A   444                                                      
REMARK 465     ASP A   445                                                      
REMARK 465     GLN A   446                                                      
REMARK 465     ILE A   447                                                      
REMARK 465     TYR A   448                                                      
REMARK 465     PRO A   449                                                      
REMARK 465     GLY A   450                                                      
REMARK 465     TRP A   451                                                      
REMARK 465     ARG A   452                                                      
REMARK 465     LYS A   453                                                      
REMARK 465     ALA A   454                                                      
REMARK 465     LEU A   455                                                      
REMARK 465     GLY A   456                                                      
REMARK 465     VAL A   457                                                      
REMARK 465     GLU A   458                                                      
REMARK 465     ASP A   459                                                      
REMARK 465     THR A   460                                                      
REMARK 465     ARG A   461                                                      
REMARK 465     SER A   462                                                      
REMARK 465     ALA A   463                                                      
REMARK 465     LEU A   464                                                      
REMARK 465     PRO A   465                                                      
REMARK 465     ALA A   466                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     GLN B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     MET B   325                                                      
REMARK 465     GLY B   326                                                      
REMARK 465     PHE B   327                                                      
REMARK 465     GLY B   328                                                      
REMARK 465     LYS B   329                                                      
REMARK 465     MET B   330                                                      
REMARK 465     GLU B   331                                                      
REMARK 465     GLY B   332                                                      
REMARK 465     GLU B   333                                                      
REMARK 465     SER B   334                                                      
REMARK 465     GLU B   458                                                      
REMARK 465     ASP B   459                                                      
REMARK 465     THR B   460                                                      
REMARK 465     ARG B   461                                                      
REMARK 465     SER B   462                                                      
REMARK 465     ALA B   463                                                      
REMARK 465     LEU B   464                                                      
REMARK 465     PRO B   465                                                      
REMARK 465     ALA B   466                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER B 296    OG                                                  
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 475        DISTANCE =  6.75 ANGSTROMS                       
REMARK 525    HOH A 476        DISTANCE =  5.13 ANGSTROMS                       
REMARK 525    HOH A 477        DISTANCE =  5.40 ANGSTROMS                       
REMARK 525    HOH A 480        DISTANCE = 15.07 ANGSTROMS                       
REMARK 525    HOH A 481        DISTANCE =  9.77 ANGSTROMS                       
REMARK 525    HOH A 482        DISTANCE =  6.27 ANGSTROMS                       
REMARK 525    HOH A 483        DISTANCE =  6.39 ANGSTROMS                       
REMARK 525    HOH A 488        DISTANCE =  7.34 ANGSTROMS                       
REMARK 525    HOH A 490        DISTANCE =  7.45 ANGSTROMS                       
REMARK 525    HOH A 508        DISTANCE =  6.66 ANGSTROMS                       
REMARK 525    HOH A 510        DISTANCE =  5.55 ANGSTROMS                       
REMARK 525    HOH A 519        DISTANCE =  5.18 ANGSTROMS                       
REMARK 525    HOH A 527        DISTANCE =  7.15 ANGSTROMS                       
REMARK 525    HOH A 528        DISTANCE =  7.36 ANGSTROMS                       
REMARK 525    HOH A 529        DISTANCE =  6.15 ANGSTROMS                       
REMARK 525    HOH A 530        DISTANCE =  9.11 ANGSTROMS                       
REMARK 525    HOH A 531        DISTANCE =  5.73 ANGSTROMS                       
REMARK 525    HOH A 533        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH B 474        DISTANCE =  5.18 ANGSTROMS                       
REMARK 525    HOH B 486        DISTANCE =  5.13 ANGSTROMS                       
REMARK 525    HOH B 505        DISTANCE =  5.46 ANGSTROMS                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEETS PRESENTED AS *ACT* AND *BCT* ON SHEET RECORDS             
REMARK 700 BELOW ARE ACTUALLY EIGHT-STRANDED BETA-BARRELS.  THIS IS             
REMARK 700 REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST AND          
REMARK 700 LAST STRANDS ARE IDENTICAL.                                          
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 SEQUENCE ADVISORY NOTICE:                                            
REMARK 999      DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE.                 
REMARK 999                                                                      
REMARK 999      SWISS-PROT ENTRY NAME: RBL2_RHORU                               
REMARK 999                                                                      
REMARK 999      SWISS-PROT RESIDUE      PDB SEQRES                              
REMARK 999        NAME   NUMBER         NAME  CHAIN  SEQ/INSERT CODE            
REMARK 999        HIS     91            ASP     A     91                        
REMARK 999        HIS     91            ASP     B     91                        
DBREF  1RBA A    1   466  UNP    P04718   RBL2_RHORU       1    466             
DBREF  1RBA B    1   466  UNP    P04718   RBL2_RHORU       1    466             
SEQADV 1RBA ASP A   91  UNP  P04718    HIS    91 CONFLICT                       
SEQADV 1RBA ASN A  193  UNP  P04718    ASP   193 ENGINEERED MUTATION            
SEQADV 1RBA ASP B   91  UNP  P04718    HIS    91 CONFLICT                       
SEQADV 1RBA ASN B  193  UNP  P04718    ASP   193 ENGINEERED MUTATION            
SEQRES   1 A  466  MET ASP GLN SER SER ARG TYR VAL ASN LEU ALA LEU LYS          
SEQRES   2 A  466  GLU GLU ASP LEU ILE ALA GLY GLY GLU HIS VAL LEU CYS          
SEQRES   3 A  466  ALA TYR ILE MET LYS PRO LYS ALA GLY TYR GLY TYR VAL          
SEQRES   4 A  466  ALA THR ALA ALA HIS PHE ALA ALA GLU SER SER THR GLY          
SEQRES   5 A  466  THR ASN VAL GLU VAL CYS THR THR ASP ASP PHE THR ARG          
SEQRES   6 A  466  GLY VAL ASP ALA LEU VAL TYR GLU VAL ASP GLU ALA ARG          
SEQRES   7 A  466  GLU LEU THR LYS ILE ALA TYR PRO VAL ALA LEU PHE ASP          
SEQRES   8 A  466  ARG ASN ILE THR ASP GLY LYS ALA MET ILE ALA SER PHE          
SEQRES   9 A  466  LEU THR LEU THR MET GLY ASN ASN GLN GLY MET GLY ASP          
SEQRES  10 A  466  VAL GLU TYR ALA LYS MET HIS ASP PHE TYR VAL PRO GLU          
SEQRES  11 A  466  ALA TYR ARG ALA LEU PHE ASP GLY PRO SER VAL ASN ILE          
SEQRES  12 A  466  SER ALA LEU TRP LYS VAL LEU GLY ARG PRO GLU VAL ASP          
SEQRES  13 A  466  GLY GLY LEU VAL VAL GLY THR ILE ILE LYS PRO LYS LEU          
SEQRES  14 A  466  GLY LEU ARG PRO LYS PRO PHE ALA GLU ALA CYS HIS ALA          
SEQRES  15 A  466  PHE TRP LEU GLY GLY ASP PHE ILE LYS ASN ASN GLU PRO          
SEQRES  16 A  466  GLN GLY ASN GLN PRO PHE ALA PRO LEU ARG ASP THR ILE          
SEQRES  17 A  466  ALA LEU VAL ALA ASP ALA MET ARG ARG ALA GLN ASP GLU          
SEQRES  18 A  466  THR GLY GLU ALA LYS LEU PHE SER ALA ASN ILE THR ALA          
SEQRES  19 A  466  ASP ASP PRO PHE GLU ILE ILE ALA ARG GLY GLU TYR VAL          
SEQRES  20 A  466  LEU GLU THR PHE GLY GLU ASN ALA SER HIS VAL ALA LEU          
SEQRES  21 A  466  LEU VAL ASP GLY TYR VAL ALA GLY ALA ALA ALA ILE THR          
SEQRES  22 A  466  THR ALA ARG ARG ARG PHE PRO ASP ASN PHE LEU HIS TYR          
SEQRES  23 A  466  HIS ARG ALA GLY HIS GLY ALA VAL THR SER PRO GLN SER          
SEQRES  24 A  466  LYS ARG GLY TYR THR ALA PHE VAL HIS CYS LYS MET ALA          
SEQRES  25 A  466  ARG LEU GLN GLY ALA SER GLY ILE HIS THR GLY THR MET          
SEQRES  26 A  466  GLY PHE GLY LYS MET GLU GLY GLU SER SER ASP ARG ALA          
SEQRES  27 A  466  ILE ALA TYR MET LEU THR GLN ASP GLU ALA GLN GLY PRO          
SEQRES  28 A  466  PHE TYR ARG GLN SER TRP GLY GLY MET LYS ALA CYS THR          
SEQRES  29 A  466  PRO ILE ILE SER GLY GLY MET ASN ALA LEU ARG MET PRO          
SEQRES  30 A  466  GLY PHE PHE GLU ASN LEU GLY ASN ALA ASN VAL ILE LEU          
SEQRES  31 A  466  THR ALA GLY GLY GLY ALA PHE GLY HIS ILE ASP GLY PRO          
SEQRES  32 A  466  VAL ALA GLY ALA ARG SER LEU ARG GLN ALA TRP GLN ALA          
SEQRES  33 A  466  TRP ARG ASP GLY VAL PRO VAL LEU ASP TYR ALA ARG GLU          
SEQRES  34 A  466  HIS LYS GLU LEU ALA ARG ALA PHE GLU SER PHE PRO GLY          
SEQRES  35 A  466  ASP ALA ASP GLN ILE TYR PRO GLY TRP ARG LYS ALA LEU          
SEQRES  36 A  466  GLY VAL GLU ASP THR ARG SER ALA LEU PRO ALA                  
SEQRES   1 B  466  MET ASP GLN SER SER ARG TYR VAL ASN LEU ALA LEU LYS          
SEQRES   2 B  466  GLU GLU ASP LEU ILE ALA GLY GLY GLU HIS VAL LEU CYS          
SEQRES   3 B  466  ALA TYR ILE MET LYS PRO LYS ALA GLY TYR GLY TYR VAL          
SEQRES   4 B  466  ALA THR ALA ALA HIS PHE ALA ALA GLU SER SER THR GLY          
SEQRES   5 B  466  THR ASN VAL GLU VAL CYS THR THR ASP ASP PHE THR ARG          
SEQRES   6 B  466  GLY VAL ASP ALA LEU VAL TYR GLU VAL ASP GLU ALA ARG          
SEQRES   7 B  466  GLU LEU THR LYS ILE ALA TYR PRO VAL ALA LEU PHE ASP          
SEQRES   8 B  466  ARG ASN ILE THR ASP GLY LYS ALA MET ILE ALA SER PHE          
SEQRES   9 B  466  LEU THR LEU THR MET GLY ASN ASN GLN GLY MET GLY ASP          
SEQRES  10 B  466  VAL GLU TYR ALA LYS MET HIS ASP PHE TYR VAL PRO GLU          
SEQRES  11 B  466  ALA TYR ARG ALA LEU PHE ASP GLY PRO SER VAL ASN ILE          
SEQRES  12 B  466  SER ALA LEU TRP LYS VAL LEU GLY ARG PRO GLU VAL ASP          
SEQRES  13 B  466  GLY GLY LEU VAL VAL GLY THR ILE ILE LYS PRO LYS LEU          
SEQRES  14 B  466  GLY LEU ARG PRO LYS PRO PHE ALA GLU ALA CYS HIS ALA          
SEQRES  15 B  466  PHE TRP LEU GLY GLY ASP PHE ILE LYS ASN ASN GLU PRO          
SEQRES  16 B  466  GLN GLY ASN GLN PRO PHE ALA PRO LEU ARG ASP THR ILE          
SEQRES  17 B  466  ALA LEU VAL ALA ASP ALA MET ARG ARG ALA GLN ASP GLU          
SEQRES  18 B  466  THR GLY GLU ALA LYS LEU PHE SER ALA ASN ILE THR ALA          
SEQRES  19 B  466  ASP ASP PRO PHE GLU ILE ILE ALA ARG GLY GLU TYR VAL          
SEQRES  20 B  466  LEU GLU THR PHE GLY GLU ASN ALA SER HIS VAL ALA LEU          
SEQRES  21 B  466  LEU VAL ASP GLY TYR VAL ALA GLY ALA ALA ALA ILE THR          
SEQRES  22 B  466  THR ALA ARG ARG ARG PHE PRO ASP ASN PHE LEU HIS TYR          
SEQRES  23 B  466  HIS ARG ALA GLY HIS GLY ALA VAL THR SER PRO GLN SER          
SEQRES  24 B  466  LYS ARG GLY TYR THR ALA PHE VAL HIS CYS LYS MET ALA          
SEQRES  25 B  466  ARG LEU GLN GLY ALA SER GLY ILE HIS THR GLY THR MET          
SEQRES  26 B  466  GLY PHE GLY LYS MET GLU GLY GLU SER SER ASP ARG ALA          
SEQRES  27 B  466  ILE ALA TYR MET LEU THR GLN ASP GLU ALA GLN GLY PRO          
SEQRES  28 B  466  PHE TYR ARG GLN SER TRP GLY GLY MET LYS ALA CYS THR          
SEQRES  29 B  466  PRO ILE ILE SER GLY GLY MET ASN ALA LEU ARG MET PRO          
SEQRES  30 B  466  GLY PHE PHE GLU ASN LEU GLY ASN ALA ASN VAL ILE LEU          
SEQRES  31 B  466  THR ALA GLY GLY GLY ALA PHE GLY HIS ILE ASP GLY PRO          
SEQRES  32 B  466  VAL ALA GLY ALA ARG SER LEU ARG GLN ALA TRP GLN ALA          
SEQRES  33 B  466  TRP ARG ASP GLY VAL PRO VAL LEU ASP TYR ALA ARG GLU          
SEQRES  34 B  466  HIS LYS GLU LEU ALA ARG ALA PHE GLU SER PHE PRO GLY          
SEQRES  35 B  466  ASP ALA ASP GLN ILE TYR PRO GLY TRP ARG LYS ALA LEU          
SEQRES  36 B  466  GLY VAL GLU ASP THR ARG SER ALA LEU PRO ALA                  
FORMUL   3  HOH   *110(H2 O)                                                    
HELIX    1 AHA GLU A   14  GLY A   20  1                                   7    
HELIX    2 AHB TYR A   38  SER A   49  1                                  12    
HELIX    3 AHC ILE A  101  MET A  109  1                                   9    
HELIX    4 AHD GLU A  130  ARG A  133  1                                   4    
HELIX    5 AHE SER A  144  LEU A  150  1                                   7    
HELIX    6 AH1 PRO A  173  TRP A  184  1                                  12    
HELIX    7 AH2 LEU A  204  THR A  222  1                                  19    
HELIX    8 AH3 ASP A  235  PHE A  251  1                                  17    
HELIX    9 AH4 ALA A  269  ARG A  278  1                                  10    
HELIX   10 AHF GLY A  292  THR A  295  1                                   4    
HELIX   11 AH5 ALA A  305  GLN A  315  1                                  11    
HELIX   12 AH6 ARG A  337  THR A  344  1                                   8    
HELIX   13 AH7 MET A  376  LEU A  383  1                                   8    
HELIX   14 AH8 PRO A  403  ASP A  419  1                                  17    
HELIX   15 AHG VAL A  423  GLU A  429  1                                   7    
HELIX   16 AHH LYS A  431  PHE A  440  1                                  10    
HELIX   17 BHA GLU B   14  GLY B   20  1                                   7    
HELIX   18 BHB TYR B   38  SER B   49  1                                  12    
HELIX   19 BHC ILE B  101  MET B  109  1                                   9    
HELIX   20 BHD GLU B  130  ARG B  133  1                                   4    
HELIX   21 BHE SER B  144  LEU B  150  1                                   7    
HELIX   22 BH1 PRO B  173  TRP B  184  1                                  12    
HELIX   23 BH2 LEU B  204  THR B  222  1                                  19    
HELIX   24 BH3 ASP B  235  PHE B  251  1                                  17    
HELIX   25 BH4 ALA B  269  ARG B  278  1                                  10    
HELIX   26 BHF GLY B  292  THR B  295  1                                   4    
HELIX   27 BH5 ALA B  305  GLN B  315  1                                  11    
HELIX   28 BH6 ARG B  337  THR B  344  1                                   8    
HELIX   29 BH7 MET B  376  LEU B  383  1                                   8    
HELIX   30 BH8 PRO B  403  ASP B  419  1                                  17    
HELIX   31 BHG VAL B  423  GLU B  429  1                                   7    
HELIX   32 BHH LYS B  431  PHE B  440  1                                  10    
HELIX   33 BHI GLY B  442  TYR B  448  1                                   7    
HELIX   34 BHJ TRP B  451  LEU B  455  1                                   5    
SHEET    1 ANT 5 VAL A   8  LEU A  10  0                                        
SHEET    2 ANT 5 LEU A  70  ASP A  75  1                                        
SHEET    3 ANT 5 GLU A  79  PRO A  86 -1                                        
SHEET    4 ANT 5 HIS A  23  PRO A  32 -1                                        
SHEET    5 ANT 5 ASP A 117  TYR A 127 -1                                        
SHEET    1 ACT 9 VAL A 160  ILE A 164  0                                        
SHEET    2 ACT 9 PHE A 189  LYS A 191  1                                        
SHEET    3 ACT 9 LEU A 227  ASN A 231  1                                        
SHEET    4 ACT 9 VAL A 258  ASP A 263  1                                        
SHEET    5 ACT 9 LEU A 284  HIS A 287  1                                        
SHEET    6 ACT 9 GLY A 319  HIS A 321  1                                        
SHEET    7 ACT 9 THR A 364  GLY A 369  1                                        
SHEET    8 ACT 9 ILE A 389  ALA A 392  1                                        
SHEET    9 ACT 9 VAL A 160  ILE A 164  1                                        
SHEET    1 BNT 5 VAL B   8  LEU B  10  0                                        
SHEET    2 BNT 5 LEU B  70  ASP B  75  1                                        
SHEET    3 BNT 5 GLU B  79  PRO B  86 -1                                        
SHEET    4 BNT 5 HIS B  23  PRO B  32 -1                                        
SHEET    5 BNT 5 ASP B 117  TYR B 127 -1                                        
SHEET    1 BCT 9 VAL B 160  ILE B 164  0                                        
SHEET    2 BCT 9 PHE B 189  LYS B 191  1                                        
SHEET    3 BCT 9 LEU B 227  ASN B 231  1                                        
SHEET    4 BCT 9 VAL B 258  ASP B 263  1                                        
SHEET    5 BCT 9 LEU B 284  HIS B 287  1                                        
SHEET    6 BCT 9 GLY B 319  HIS B 321  1                                        
SHEET    7 BCT 9 THR B 364  GLY B 369  1                                        
SHEET    8 BCT 9 ILE B 389  ALA B 392  1                                        
SHEET    9 BCT 9 VAL B 160  ILE B 164  1                                        
CISPEP   1 LYS A  166    PRO A  167          0        -2.27                     
CISPEP   2 LYS B  166    PRO B  167          0         0.74                     
CRYST1   65.500   69.300  103.100  90.00  92.10  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015267  0.000000  0.000560        0.00000                         
SCALE2      0.000000  0.014430  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009706        0.00000                         
MTRIX1   1  0.373740 -0.056207  0.940855        6.14161    1                    
MTRIX2   1 -0.073400 -0.996800 -0.033512       17.87800    1                    
MTRIX3   1  0.909789 -0.054363 -0.376740       -7.57091    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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