GenomeNet

Database: PDB
Entry: 9RUB
LinkDB: 9RUB
Original site: 9RUB 
HEADER    LYASE(CARBON-CARBON)                    28-NOV-90   9RUB              
TITLE     CRYSTAL STRUCTURE OF ACTIVATED RIBULOSE-1,5-BISPHOSPHATE              
TITLE    2 CARBOXYLASE COMPLEXED WITH ITS SUBSTRATE, RIBULOSE-1,5-              
TITLE    3 BISPHOSPHATE                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE;                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 4.1.1.39;                                                        
COMPND   5 ENGINEERED: 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    T.LUNDQVIST,G.SCHNEIDER                                               
REVDAT   3   24-FEB-09 9RUB    1       VERSN                                    
REVDAT   2   15-JAN-95 9RUB    1       COMPND                                   
REVDAT   1   15-JAN-93 9RUB    0                                                
JRNL        AUTH   T.LUNDQVIST,G.SCHNEIDER                                      
JRNL        TITL   CRYSTAL STRUCTURE OF ACTIVATED                               
JRNL        TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE COMPLEXED              
JRNL        TITL 3 WITH ITS SUBSTRATE, RIBULOSE-1,5-BISPHOSPHATE.               
JRNL        REF    J.BIOL.CHEM.                  V. 266 12604 1991              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   1905726                                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   G.SCHNEIDER,S.KNIGHT,I.ANDERSSON,Y.LINDQVIST,                
REMARK   1  AUTH 2 T.LUNDQVIST,C.-I.BRANDEN                                     
REMARK   1  TITL   COMPARISON OF THE CRYSTAL STRUCTURES OF L2 AND               
REMARK   1  TITL 2 L8S8 RUBISCO SUGGESTS A FUNCTIONAL ROLE FOR THE              
REMARK   1  TITL 3 SMALL SUBUNIT                                                
REMARK   1  REF    EMBO J.                       V.   9  2045 1990              
REMARK   1  REFN                   ISSN 0261-4189                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   G.SCHNEIDER,Y.LINDQVIST,T.LUNDQVIST                          
REMARK   1  TITL   CRYSTALLOGRAPHIC REFINEMENT AND STRUCTURE OF                 
REMARK   1  TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE FROM                   
REMARK   1  TITL 3 RHODOSPIRILLUM RUBRUM AT 1.7 ANGSTROMS RESOLUTION            
REMARK   1  REF    J.MOL.BIOL.                   V. 211   989 1990              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   T.LUNDQVIST,G.SCHNEIDER                                      
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE COMPLEX OF                          
REMARK   1  TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE AND A                  
REMARK   1  TITL 3 TRANSITION STATE ANALOGUE, 2-CARBOXY-D-ARABINITOL            
REMARK   1  TITL 4 1,5-BISPHOSPHATE                                             
REMARK   1  REF    J.BIOL.CHEM.                  V. 264  7078 1989              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   T.LUNDQVIST,G.SCHNEIDER                                      
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE BINARY COMPLEX OF                   
REMARK   1  TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE AND ITS                
REMARK   1  TITL 3 PRODUCT, 3-PHOSPHO-D-GLYCERATE                               
REMARK   1  REF    J.BIOL.CHEM.                  V. 264  3643 1989              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   G.SCHNEIDER,Y.LINDQVIST,C.-I.BRANDEN,G.LORIMER               
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF                               
REMARK   1  TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE(SLASH)                 
REMARK   1  TITL 3 OXYGENASE FROM RHODOSPIRILLUM RUBRUM AT 2.9                  
REMARK   1  TITL 4 ANGSTROMS RESOLUTION                                         
REMARK   1  REF    EMBO J.                       V.   5  3409 1986              
REMARK   1  REFN                   ISSN 0261-4189                               
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) : 0.199                           
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            : 7000                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 44                                      
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  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.017 ; 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:  RESIDUES A 191 AND B 191 ARE             
REMARK   3  MODIFIED LYSINES WHICH ARE CARBAMYLATED AT THE EPSILON-AMINO        
REMARK   3  GROUP. THE CARBAMYL GROUPS ARE PRESENTED AS HET GROUPS *CBX*        
REMARK   3  AT THE END OF CHAINS *A* AND *B*.                                   
REMARK   4                                                                      
REMARK   4 9RUB 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   (%): 48.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38                     
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       35.30000            
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 300 REMARK:                                                              
REMARK 300 THE TRANSFORMATION GIVEN ON THE *MTRIX* RECORDS BELOW WILL           
REMARK 300 YIELD APPROXIMATE COORDINATES FOR CHAIN *A* WHEN APPLIED TO          
REMARK 300 COORDINATES OF CHAIN *B*.  RESIDUES 422 - 450 WERE OMITTED           
REMARK 300 WHEN GENERATING THIS TRANSFORMATION MATRIX.                          
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: 8750 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33330 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 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     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     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     THR A 460    CB   OG1  CG2                                       
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU A  458   CD    OE1   OE2                                     
REMARK 480     ASP A  459   CG    OD1                                           
REMARK 480     THR A  460   CA    C     O                                       
REMARK 480     VAL B  457   O                                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    SER A   356     N    GLY A   358              2.12            
REMARK 500   OH   TYR B     7     OG1  THR B    51              2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 458   CG    GLU A 458   CD      0.324                       
REMARK 500    ASP A 459   CG    ASP A 459   OD2     0.311                       
REMARK 500    THR A 460   N     THR A 460   CA     -0.205                       
REMARK 500    VAL B 457   C     VAL B 457   O      -0.175                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    SER A   4   N   -  CA  -  CB  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    SER A   4   C   -  N   -  CA  ANGL. DEV. =  21.0 DEGREES          
REMARK 500    ARG A   6   NE  -  CZ  -  NH1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG A   6   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    LEU A  10   N   -  CA  -  C   ANGL. DEV. = -18.5 DEGREES          
REMARK 500    GLU A  22   CA  -  CB  -  CG  ANGL. DEV. =  15.7 DEGREES          
REMARK 500    GLU A  22   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.9 DEGREES          
REMARK 500    LEU A  25   O   -  C   -  N   ANGL. DEV. =  10.7 DEGREES          
REMARK 500    TYR A  38   C   -  N   -  CA  ANGL. DEV. =  17.2 DEGREES          
REMARK 500    ASN A  54   CA  -  CB  -  CG  ANGL. DEV. =  20.6 DEGREES          
REMARK 500    VAL A  55   CA  -  CB  -  CG2 ANGL. DEV. =   9.7 DEGREES          
REMARK 500    GLU A  56   CA  -  C   -  O   ANGL. DEV. =  18.2 DEGREES          
REMARK 500    GLU A  56   O   -  C   -  N   ANGL. DEV. = -12.9 DEGREES          
REMARK 500    VAL A  57   C   -  N   -  CA  ANGL. DEV. =  36.0 DEGREES          
REMARK 500    CYS A  58   N   -  CA  -  CB  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    CYS A  58   CA  -  CB  -  SG  ANGL. DEV. =   8.6 DEGREES          
REMARK 500    THR A  59   N   -  CA  -  C   ANGL. DEV. = -16.9 DEGREES          
REMARK 500    THR A  59   C   -  N   -  CA  ANGL. DEV. =  19.9 DEGREES          
REMARK 500    THR A  60   C   -  N   -  CA  ANGL. DEV. =  18.3 DEGREES          
REMARK 500    ASP A  61   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP A  62   CB  -  CG  -  OD2 ANGL. DEV. =  -9.9 DEGREES          
REMARK 500    ASP A  62   C   -  N   -  CA  ANGL. DEV. =  18.2 DEGREES          
REMARK 500    THR A  64   N   -  CA  -  CB  ANGL. DEV. =  12.3 DEGREES          
REMARK 500    THR A  64   CA  -  C   -  O   ANGL. DEV. =  17.5 DEGREES          
REMARK 500    ARG A  65   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    THR A  64   CA  -  C   -  N   ANGL. DEV. = -13.8 DEGREES          
REMARK 500    ARG A  65   C   -  N   -  CA  ANGL. DEV. =  22.1 DEGREES          
REMARK 500    VAL A  67   C   -  N   -  CA  ANGL. DEV. =  21.6 DEGREES          
REMARK 500    ASP A  68   CB  -  CG  -  OD2 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    VAL A  71   N   -  CA  -  CB  ANGL. DEV. =  20.6 DEGREES          
REMARK 500    TYR A  72   CB  -  CG  -  CD2 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ASP A  75   N   -  CA  -  CB  ANGL. DEV. =  12.9 DEGREES          
REMARK 500    ASP A  75   N   -  CA  -  C   ANGL. DEV. = -16.3 DEGREES          
REMARK 500    ARG A  78   CD  -  NE  -  CZ  ANGL. DEV. =  32.4 DEGREES          
REMARK 500    ARG A  78   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    PHE A  90   CB  -  CG  -  CD2 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ASP A  91   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG A  92   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    THR A  95   CA  -  CB  -  CG2 ANGL. DEV. =   9.0 DEGREES          
REMARK 500    ASP A  96   CB  -  CG  -  OD1 ANGL. DEV. =  18.7 DEGREES          
REMARK 500    ASP A  96   CB  -  CG  -  OD2 ANGL. DEV. = -12.0 DEGREES          
REMARK 500    LYS A  98   O   -  C   -  N   ANGL. DEV. =  10.7 DEGREES          
REMARK 500    PHE A 104   CB  -  CG  -  CD1 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    LEU A 105   CA  -  C   -  O   ANGL. DEV. = -15.6 DEGREES          
REMARK 500    THR A 106   N   -  CA  -  CB  ANGL. DEV. =  21.2 DEGREES          
REMARK 500    LEU A 105   CA  -  C   -  N   ANGL. DEV. =  16.8 DEGREES          
REMARK 500    ASN A 112   CA  -  CB  -  CG  ANGL. DEV. =  13.3 DEGREES          
REMARK 500    MET A 115   CB  -  CA  -  C   ANGL. DEV. =  13.1 DEGREES          
REMARK 500    MET A 115   CA  -  CB  -  CG  ANGL. DEV. =  10.5 DEGREES          
REMARK 500    ASP A 117   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     398 ANGLE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A   3     -155.03     65.79                                   
REMARK 500    SER A   4      -91.70   -149.47                                   
REMARK 500    SER A   5      145.60    -29.90                                   
REMARK 500    ARG A   6      -35.05     79.52                                   
REMARK 500    ASN A   9       61.69   -171.07                                   
REMARK 500    ALA A  11       -8.52    146.95                                   
REMARK 500    TYR A  38      -80.36     21.15                                   
REMARK 500    SER A  50      -97.10   -139.34                                   
REMARK 500    THR A  53       67.31     31.27                                   
REMARK 500    VAL A  55     -119.67     61.27                                   
REMARK 500    ASP A  62      132.14     80.95                                   
REMARK 500    PHE A  63       91.47     78.02                                   
REMARK 500    THR A  64       77.56   -151.31                                   
REMARK 500    VAL A  67       20.12   -151.24                                   
REMARK 500    PRO A  86      159.09    -49.85                                   
REMARK 500    ASP A  96      -16.59   -140.77                                   
REMARK 500    MET A 115      135.99    -37.56                                   
REMARK 500    PRO A 129      169.77    -25.81                                   
REMARK 500    PHE A 136      139.73    156.16                                   
REMARK 500    ASP A 137      -70.86    -50.38                                   
REMARK 500    SER A 144       15.55    -52.39                                   
REMARK 500    LYS A 148       -7.32    -59.15                                   
REMARK 500    ASP A 156       19.41     24.52                                   
REMARK 500    LEU A 169      143.85   -170.75                                   
REMARK 500    LEU A 171      100.04      8.50                                   
REMARK 500    ARG A 172     -179.07    -54.05                                   
REMARK 500    TRP A 184       16.40    -65.05                                   
REMARK 500    PRO A 195       42.33    -84.01                                   
REMARK 500    ALA A 202       75.91   -151.52                                   
REMARK 500    LEU A 204      -60.53    -13.99                                   
REMARK 500    ASP A 220      -77.71   -106.74                                   
REMARK 500    GLU A 221       -2.55    -51.15                                   
REMARK 500    ASP A 263       14.86    -67.10                                   
REMARK 500    TYR A 265      -63.17    -97.65                                   
REMARK 500    VAL A 266       40.11    -60.43                                   
REMARK 500    ALA A 267        4.58    176.80                                   
REMARK 500    ARG A 288       40.43    -57.43                                   
REMARK 500    ALA A 289      151.06    -44.70                                   
REMARK 500    VAL A 294      -72.29   -105.67                                   
REMARK 500    PRO A 297        8.55    -58.32                                   
REMARK 500    HIS A 321       78.92    -69.72                                   
REMARK 500    THR A 324      148.16    176.41                                   
REMARK 500    PHE A 327     -143.85   -130.60                                   
REMARK 500    LYS A 329     -108.01     62.56                                   
REMARK 500    GLU A 333       54.66      2.21                                   
REMARK 500    SER A 334       72.69     75.12                                   
REMARK 500    ALA A 338      -56.20    -28.63                                   
REMARK 500    GLU A 347       60.70   -174.20                                   
REMARK 500    PRO A 351        2.20    -56.60                                   
REMARK 500    PHE A 352      -48.37   -157.36                                   
REMARK 500    SER A 356       47.49   -102.74                                   
REMARK 500    TRP A 357       12.37    -19.45                                   
REMARK 500    MET A 360     -123.97    -60.26                                   
REMARK 500    LYS A 361     -156.87   -164.38                                   
REMARK 500    ASN A 372     -177.56    -49.59                                   
REMARK 500    ALA A 373      -62.01    -18.64                                   
REMARK 500    PHE A 380      -17.74    -48.35                                   
REMARK 500    LEU A 383      -89.68    -83.65                                   
REMARK 500    ASN A 385     -168.92   -170.92                                   
REMARK 500    ALA A 386       19.10   -149.75                                   
REMARK 500    PRO A 403       11.93    -56.21                                   
REMARK 500    ARG A 418      -76.83    -44.45                                   
REMARK 500    PRO A 422      125.89     40.46                                   
REMARK 500    PHE A 440       66.60   -118.65                                   
REMARK 500    ASP A 443      -57.44   -123.57                                   
REMARK 500    ALA A 444       74.19    -65.90                                   
REMARK 500    ASP A 445      -84.89    171.48                                   
REMARK 500    PRO A 449      -80.38     16.51                                   
REMARK 500    TRP A 451      -33.92    -17.87                                   
REMARK 500    ARG A 452      -70.44    -48.73                                   
REMARK 500    VAL A 457     -157.64    118.72                                   
REMARK 500    ASP A 459      155.46    127.79                                   
REMARK 500    GLN B   3      -25.44     53.19                                   
REMARK 500    SER B   4      170.94    131.96                                   
REMARK 500    SER B   5       17.17   -155.76                                   
REMARK 500    ASN B   9       83.68   -168.05                                   
REMARK 500    SER B  50      -89.98   -108.21                                   
REMARK 500    THR B  53       72.51     63.12                                   
REMARK 500    ASN B  54      -87.80    -17.64                                   
REMARK 500    GLU B  56     -103.39     87.92                                   
REMARK 500    CYS B  58      -34.01    -28.13                                   
REMARK 500    THR B  59     -157.69     51.28                                   
REMARK 500    ASP B  61      168.05     66.14                                   
REMARK 500    ASP B  62       87.42     84.24                                   
REMARK 500    PHE B  63      -22.69    110.00                                   
REMARK 500    GLU B  73      141.88   -170.94                                   
REMARK 500    GLU B  79       65.16     70.23                                   
REMARK 500    PRO B  86      147.72    -37.49                                   
REMARK 500    ASP B  91      110.93     71.83                                   
REMARK 500    ALA B  99      176.81    -54.76                                   
REMARK 500    LEU B 107      -73.22    -72.23                                   
REMARK 500    MET B 109       59.81   -158.04                                   
REMARK 500    ASN B 111       23.91    -74.94                                   
REMARK 500    MET B 115      123.24   -170.59                                   
REMARK 500    TYR B 120      131.24     65.43                                   
REMARK 500    ASP B 125      138.70    150.32                                   
REMARK 500    ASP B 137      -75.70    -66.70                                   
REMARK 500    GLU B 154        0.37    -56.71                                   
REMARK 500    LYS B 191      -88.71    -88.23                                   
REMARK 500    ASN B 192      121.29    124.03                                   
REMARK 500    GLU B 194      -56.77    -28.29                                   
REMARK 500    ALA B 202       62.10    167.84                                   
REMARK 500    ASP B 213      -70.84    -66.98                                   
REMARK 500    ALA B 214        9.18    -52.84                                   
REMARK 500    ASP B 235      -60.36   -103.38                                   
REMARK 500    ARG B 243      -76.04    -86.98                                   
REMARK 500    TYR B 246      -79.64    -63.16                                   
REMARK 500    ALA B 267      -17.09   -140.92                                   
REMARK 500    ALA B 269      -10.35    -39.29                                   
REMARK 500    ARG B 276     -130.04    -72.30                                   
REMARK 500    ARG B 277      -49.33     11.55                                   
REMARK 500    PHE B 279       77.74   -115.67                                   
REMARK 500    ARG B 288      -87.47    -73.53                                   
REMARK 500    ALA B 289     -122.24    106.05                                   
REMARK 500    THR B 322     -145.66   -153.73                                   
REMARK 500    PHE B 327      175.86    143.99                                   
REMARK 500    MET B 330       14.72    160.70                                   
REMARK 500    GLU B 333     -168.81   -106.62                                   
REMARK 500    SER B 335       18.85      7.93                                   
REMARK 500    ALA B 338        2.00    -65.33                                   
REMARK 500    PHE B 352      -33.18   -137.50                                   
REMARK 500    ALA B 373       -4.29    -50.54                                   
REMARK 500    ASN B 385     -169.56   -127.60                                   
REMARK 500    PRO B 403      -84.64    -37.14                                   
REMARK 500    PRO B 422       52.80    -63.94                                   
REMARK 500    VAL B 423      -55.76     44.05                                   
REMARK 500    ARG B 428       94.43    -68.75                                   
REMARK 500    GLU B 429      -46.83    143.48                                   
REMARK 500    LEU B 433      -70.24    -59.45                                   
REMARK 500    PHE B 440       78.61   -112.57                                   
REMARK 500    ALA B 444      -76.13    -68.31                                   
REMARK 500    ASP B 445       26.39    -46.91                                   
REMARK 500    GLN B 446      -18.87   -159.53                                   
REMARK 500    GLU B 458      158.97      8.55                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    VAL B 457         16.99                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 500  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 RUB A 600   O2                                                     
REMARK 620 2 RUB A 600   O3   73.1                                              
REMARK 620 3 ASP A 193   OD1 102.9 154.1                                        
REMARK 620 4 FMT A 601   O1  144.2  74.4  99.8                                  
REMARK 620 5 FMT A 601   O2  124.5 105.9  54.5  52.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 500  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 FMT B 701   O1                                                     
REMARK 620 2 ASP B 193   OD1  66.6                                              
REMARK 620 3 RUB B 700   O3   74.4 137.9                                        
REMARK 620 4 RUB B 700   O2  145.0 147.0  74.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 SHEETS *ACT* AND *BCT* PRESENTED BELOW ARE ACTUALLY                  
REMARK 700 EIGHT-STRANDED BETA/ALPHA BARRELS.  THESE ARE REPRESENTED            
REMARK 700 AS NINE-STRANDED SHEETS IN WHICH THE FIRST AND LAST STRANDS          
REMARK 700 ARE IDENTICAL.                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: ACT                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE CHAIN A                                
REMARK 800 SITE_IDENTIFIER: BCT                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE CHAIN B                                
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RUB A 600                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RUB B 700                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 500                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 500                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 601                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 701                 
DBREF  9RUB A    1   466  UNP    P04718   RBL2_RHORU       1    466             
DBREF  9RUB B    1   466  UNP    P04718   RBL2_RHORU       1    466             
SEQADV 9RUB ASP A   91  UNP  P04718    HIS    91 CONFLICT                       
SEQADV 9RUB ASP B   91  UNP  P04718    HIS    91 CONFLICT                       
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 ASP 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 ASP 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                  
HET    RUB  A 600      18                                                       
HET    RUB  B 700      18                                                       
HET     MG  A 500       1                                                       
HET     MG  B 500       1                                                       
HET    FMT  A 601       3                                                       
HET    FMT  B 701       3                                                       
HETNAM     RUB RIBULOSE-1,5-DIPHOSPHATE                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     FMT FORMIC ACID                                                      
FORMUL   3  RUB    2(C5 H12 O11 P2)                                             
FORMUL   5   MG    2(MG 2+)                                                     
FORMUL   7  FMT    2(C H2 O2)                                                   
HELIX    1  AA GLU A   14  GLY A   20  1                                   7    
HELIX    2  AB TYR A   38  SER A   49  1                                  12    
HELIX    3  AC ILE A  101  MET A  109  1                                   9    
HELIX    4  AD GLU A  130  ARG A  133  1                                   4    
HELIX    5  AE SER A  144  LEU A  150  1                                   7    
HELIX    6  A1 PRO A  173  TRP A  184  1                                  12    
HELIX    7  A2 LEU A  204  THR A  222  1                                  19    
HELIX    8  A3 ASP A  235  PHE A  251  1                                  17    
HELIX    9  A4 ALA A  269  ARG A  278  1                                  10    
HELIX   10  AF GLY A  292  THR A  295  1                                   4    
HELIX   11  A5 ALA A  305  GLN A  315  1                                  11    
HELIX   12  A6 ARG A  337  THR A  344  1                                   8    
HELIX   13  A7 ARG A  375  GLY A  378  5                                   4    
HELIX   14  A8 PRO A  403  ASP A  419  1                                  17    
HELIX   15  AG VAL A  423  GLU A  429  1                                   7    
HELIX   16  AH LYS A  431  PHE A  440  1                                  10    
HELIX   17  AI GLY A  442  TYR A  448  1                                   7    
HELIX   18  AJ TRP A  451  LEU A  455  1                                   5    
HELIX   19  BA GLU B   14  GLY B   20  1                                   7    
HELIX   20  BB TYR B   38  SER B   49  1                                  12    
HELIX   21  BC ILE B  101  MET B  109  1                                   9    
HELIX   22  BD GLU B  130  ARG B  133  1                                   4    
HELIX   23  BE SER B  144  LEU B  150  1                                   7    
HELIX   24  B1 PRO B  173  TRP B  184  1                                  12    
HELIX   25  B2 LEU B  204  THR B  222  1                                  19    
HELIX   26  B3 ASP B  235  PHE B  251  1                                  17    
HELIX   27  B4 ALA B  269  ARG B  278  1                                  10    
HELIX   28  BF GLY B  292  THR B  295  1                                   4    
HELIX   29  B5 ALA B  305  GLN B  315  1                                  11    
HELIX   30  B6 ARG B  337  THR B  344  1                                   8    
HELIX   31  B6 ARG B  375  LEU B  383  1                                   9    
HELIX   32  B8 PRO B  403  ASP B  419  1                                  17    
HELIX   33  BG VAL B  423  GLU B  429  1                                   7    
HELIX   34  BH LYS B  431  PHE B  440  1                                  10    
HELIX   35  BI GLY B  442  TYR B  448  1                                   7    
HELIX   36  BJ TRP B  451  LEU B  455  1                                   5    
SHEET    1 ANT 5 VAL A   8  LEU A  10  0                                        
SHEET    2 ANT 5 ALA A  69  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 CTA 9 VAL A 160  ILE A 164  0                                        
SHEET    2 CTA 9 PHE A 189  LYS A 191  1                                        
SHEET    3 CTA 9 LEU A 227  ASN A 231  1                                        
SHEET    4 CTA 9 VAL A 258  ASP A 263  1                                        
SHEET    5 CTA 9 LEU A 284  HIS A 287  1                                        
SHEET    6 CTA 9 GLY A 319  HIS A 321  1                                        
SHEET    7 CTA 9 THR A 364  GLY A 369  1                                        
SHEET    8 CTA 9 ILE A 389  ALA A 392  1                                        
SHEET    9 CTA 9 VAL A 160  ILE A 164  1                                        
SHEET    1 BNT 5 VAL B   8  LEU B  10  0                                        
SHEET    2 BNT 5 ALA B  69  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 CTB 9 VAL B 160  ILE B 164  0                                        
SHEET    2 CTB 9 PHE B 189  LYS B 191  1                                        
SHEET    3 CTB 9 LEU B 227  ASN B 231  1                                        
SHEET    4 CTB 9 VAL B 258  ASP B 263  1                                        
SHEET    5 CTB 9 LEU B 284  HIS B 287  1                                        
SHEET    6 CTB 9 GLY B 319  HIS B 321  1                                        
SHEET    7 CTB 9 THR B 364  GLY B 369  1                                        
SHEET    8 CTB 9 ILE A 389  ALA A 392  1                                        
SHEET    9 CTB 9 VAL B 160  ILE B 164  1                                        
LINK         NZ  LYS A 191                 C   FMT A 601     1555   1555  1.45  
LINK         NZ  LYS B 191                 C   FMT B 701     1555   1555  1.51  
LINK        MG    MG A 500                 O2  RUB A 600     1555   1555  2.47  
LINK        MG    MG A 500                 O3  RUB A 600     1555   1555  2.62  
LINK        MG    MG A 500                 OD1 ASP A 193     1555   1555  2.55  
LINK        MG    MG A 500                 O1  FMT A 601     1555   1555  2.39  
LINK        MG    MG A 500                 O2  FMT A 601     1555   1555  2.45  
LINK        MG    MG B 500                 O1  FMT B 701     1555   1555  2.46  
LINK        MG    MG B 500                 OD1 ASP B 193     1555   1555  2.53  
LINK        MG    MG B 500                 O3  RUB B 700     1555   1555  2.17  
LINK        MG    MG B 500                 O2  RUB B 700     1555   1555  2.42  
LINK         O3  RUB B 700                 O2  FMT B 701     1555   1555  2.03  
CISPEP   1 LYS A  166    PRO A  167          0         5.20                     
CISPEP   2 LYS B  166    PRO B  167          0         3.51                     
SITE     1 ACT  5 FMT A 601  LYS A 191  ASP A 193  GLU A 194                    
SITE     2 ACT  5  MG A 500                                                     
SITE     1 BCT  5 FMT B 701  LYS B 191  ASP B 193  GLU B 194                    
SITE     2 BCT  5  MG B 500                                                     
SITE     1 AC1 10 ILE A 164  ASP A 193  HIS A 321  ILE A 366                    
SITE     2 AC1 10 SER A 368  ALA A 392  GLY A 393   MG A 500                    
SITE     3 AC1 10 FMT A 601  ASN B 111                                          
SITE     1 AC2 11 ILE B 164  HIS B 287  HIS B 321  THR B 322                    
SITE     2 AC2 11 SER B 368  GLY B 369  THR B 391  ALA B 392                    
SITE     3 AC2 11 GLY B 393   MG B 500  FMT B 701                               
SITE     1 AC3  3 ASP A 193  RUB A 600  FMT A 601                               
SITE     1 AC4  4 ASP B 193  GLU B 194  RUB B 700  FMT B 701                    
SITE     1 AC5  6 ILE A 164  LYS A 191  ASN A 192  ASP A 193                    
SITE     2 AC5  6  MG A 500  RUB A 600                                          
SITE     1 AC6  7 LYS B 191  ASP B 193  GLU B 194  HIS B 287                    
SITE     2 AC6  7 HIS B 321   MG B 500  RUB B 700                               
CRYST1   65.500   70.600  104.100  90.00  92.10  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.036668        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000672        0.00000                         
SCALE1      0.015267  0.000000  0.000560        0.00000                         
SCALE2      0.000000  0.014164  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009613        0.00000                         
MTRIX1   1  0.373740 -0.056007  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                                                                             
DBGET integrated database retrieval system