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Database: PDB
Entry: 3AXK
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Original site: 3AXK 
HEADER    LYASE                                   11-APR-11   3AXK              
TITLE     STRUCTURE OF RICE RUBISCO IN COMPLEX WITH NADP(H)                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN;             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: RUBISCO LARGE SUBUNIT, D-RIBULOSE 1,5-BISPHOSPHATE          
COMPND   5 CARBOXYLASE/OXYGENASE LARGE SUBUNIT;                                 
COMPND   6 EC: 4.1.1.39;                                                        
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN,             
COMPND   9 CHLOROPLASTIC;                                                       
COMPND  10 CHAIN: S, T;                                                         
COMPND  11 SYNONYM: RUBISCO SMALL SUBUNIT, D-RIBULOSE 1,5-BISPHOSPHATE          
COMPND  12 CARBOXYLASE/OXYGENASE SMALL SUBUNIT;                                 
COMPND  13 EC: 4.1.1.39                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ORYZA SATIVA JAPONICA GROUP;                    
SOURCE   3 ORGANISM_COMMON: JAPANESE RICE;                                      
SOURCE   4 ORGANISM_TAXID: 39947;                                               
SOURCE   5 TISSUE: LEAVES;                                                      
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: ORYZA SATIVA JAPONICA GROUP;                    
SOURCE   8 ORGANISM_COMMON: JAPANESE RICE;                                      
SOURCE   9 ORGANISM_TAXID: 39947;                                               
SOURCE  10 TISSUE: LEAVES                                                       
KEYWDS    ALPHA/BETA BARREL, PHOTOSYNTHETIC CARBON REDUCTION, LYASE             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.MATSUMURA,E.MIZOHATA,H.ISHIDA,A.KOGAMI,T.UENO,A.MAKINO,T.INOUE,     
AUTHOR   2 A.YOKOTA,T.MAE,Y.KAI                                                 
REVDAT   3   05-JUN-13 3AXK    1       JRNL                                     
REVDAT   2   13-JUN-12 3AXK    1       JRNL                                     
REVDAT   1   11-APR-12 3AXK    0                                                
JRNL        AUTH   H.MATSUMURA,E.MIZOHATA,H.ISHIDA,A.KOGAMI,T.UENO,A.MAKINO,    
JRNL        AUTH 2 T.INOUE,A.YOKOTA,T.MAE,Y.KAI                                 
JRNL        TITL   CRYSTAL STRUCTURE OF RICE RUBISCO AND IMPLICATIONS FOR       
JRNL        TITL 2 ACTIVATION INDUCED BY POSITIVE EFFECTORS NADPH AND           
JRNL        TITL 3 6-PHOSPHOGLUCONATE                                           
JRNL        REF    J.MOL.BIOL.                   V. 422    75 2012              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   22609438                                                     
JRNL        DOI    10.1016/J.JMB.2012.05.014                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.63                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 369893.340                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 88564                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.189                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3848                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.02                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 13812                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1970                       
REMARK   3   BIN FREE R VALUE                    : 0.2130                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 0.70                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 103                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.021                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8745                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 122                                     
REMARK   3   SOLVENT ATOMS            : 1125                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 13.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.53000                                              
REMARK   3    B22 (A**2) : 0.53000                                              
REMARK   3    B33 (A**2) : -1.07000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.17                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.13                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.20                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.14                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.79                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.240 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.850 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.890 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.630 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.37                                                 
REMARK   3   BSOL        : 67.03                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : RUB.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : RUB.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3AXK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-APR-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB029820.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-NOV-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU ULTRAX 18                   
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : YALE MIRRORS                       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 89311                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.630                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 10.500                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.07000                            
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: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 75MM HEPES-KOH (PH 7.75), 9% PEG4000,    
REMARK 280  25% GLYCEROL, VAPOR DIFFUSION, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       8555   Y+1/2,-X+1/2,Z+1/2                                      
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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       55.12300            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       55.12300            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       99.88400            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       55.12300            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       55.12300            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       99.88400            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       55.12300            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       55.12300            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       99.88400            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000       55.12300            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       55.12300            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       99.88400            
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: HEXADECAMERIC                     
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC              
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 91580 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 118410 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -356.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, T, S                            
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 350   BIOMT1   2 -1.000000  0.000000  0.000000      110.24600            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      110.24600            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000      110.24600            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000      110.24600            
REMARK 350   BIOMT3   4  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     SER A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     LYS A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     VAL A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     PHE A    13                                                      
REMARK 465     LYS A    14                                                      
REMARK 465     ALA A    15                                                      
REMARK 465     GLY A    16                                                      
REMARK 465     VAL A    17                                                      
REMARK 465     LYS A    18                                                      
REMARK 465     ASP A    19                                                      
REMARK 465     GLY A    64                                                      
REMARK 465     THR A    65                                                      
REMARK 465     TRP A    66                                                      
REMARK 465     THR A    67                                                      
REMARK 465     GLY A   333                                                      
REMARK 465     LYS A   334                                                      
REMARK 465     LEU A   335                                                      
REMARK 465     GLU A   336                                                      
REMARK 465     GLY A   337                                                      
REMARK 465     LYS A   463                                                      
REMARK 465     ALA A   464                                                      
REMARK 465     ILE A   465                                                      
REMARK 465     LYS A   466                                                      
REMARK 465     PHE A   467                                                      
REMARK 465     GLU A   468                                                      
REMARK 465     PHE A   469                                                      
REMARK 465     GLU A   470                                                      
REMARK 465     PRO A   471                                                      
REMARK 465     VAL A   472                                                      
REMARK 465     ASP A   473                                                      
REMARK 465     LYS A   474                                                      
REMARK 465     LEU A   475                                                      
REMARK 465     ASP A   476                                                      
REMARK 465     SER A   477                                                      
REMARK 465     GLY S   122                                                      
REMARK 465     CYS S   123                                                      
REMARK 465     GLU S   124                                                      
REMARK 465     GLU S   125                                                      
REMARK 465     SER S   126                                                      
REMARK 465     GLY S   127                                                      
REMARK 465     GLY S   128                                                      
REMARK 465     ASN S   129                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     PRO B     3                                                      
REMARK 465     GLN B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     THR B     7                                                      
REMARK 465     LYS B     8                                                      
REMARK 465     ALA B     9                                                      
REMARK 465     SER B    10                                                      
REMARK 465     VAL B    11                                                      
REMARK 465     GLY B    12                                                      
REMARK 465     PHE B    13                                                      
REMARK 465     LYS B    14                                                      
REMARK 465     ALA B    15                                                      
REMARK 465     GLY B    16                                                      
REMARK 465     VAL B    17                                                      
REMARK 465     LYS B    18                                                      
REMARK 465     ASP B    19                                                      
REMARK 465     TYR B    20                                                      
REMARK 465     GLY B    64                                                      
REMARK 465     THR B    65                                                      
REMARK 465     TRP B    66                                                      
REMARK 465     THR B    67                                                      
REMARK 465     THR B    68                                                      
REMARK 465     VAL B    69                                                      
REMARK 465     VAL B   331                                                      
REMARK 465     VAL B   332                                                      
REMARK 465     GLY B   333                                                      
REMARK 465     LYS B   334                                                      
REMARK 465     LEU B   335                                                      
REMARK 465     GLU B   336                                                      
REMARK 465     GLY B   337                                                      
REMARK 465     ALA B   464                                                      
REMARK 465     ILE B   465                                                      
REMARK 465     LYS B   466                                                      
REMARK 465     PHE B   467                                                      
REMARK 465     GLU B   468                                                      
REMARK 465     PHE B   469                                                      
REMARK 465     GLU B   470                                                      
REMARK 465     PRO B   471                                                      
REMARK 465     VAL B   472                                                      
REMARK 465     ASP B   473                                                      
REMARK 465     LYS B   474                                                      
REMARK 465     LEU B   475                                                      
REMARK 465     ASP B   476                                                      
REMARK 465     SER B   477                                                      
REMARK 465     PRO T   121                                                      
REMARK 465     GLY T   122                                                      
REMARK 465     CYS T   123                                                      
REMARK 465     GLU T   124                                                      
REMARK 465     GLU T   125                                                      
REMARK 465     SER T   126                                                      
REMARK 465     GLY T   127                                                      
REMARK 465     GLY T   128                                                      
REMARK 465     ASN T   129                                                      
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     TYR A  20    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A  21    CG   CD   CE   NZ                                   
REMARK 470     GLU A  93    CG   CD   OE1  OE2                                  
REMARK 470     NME S   0    N                                                   
REMARK 470     LYS B  21    CG   CD   CE   NZ                                   
REMARK 470     GLU B 338    CG   CD   OE1  OE2                                  
REMARK 470     NME T   0    N                                                   
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   OD1  ASP B   203     O    HOH B  1112              2.05            
REMARK 500   N    ILE B   382     O    HOH B  1125              2.12            
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    LEU A  22   CA  -  CB  -  CG  ANGL. DEV. = -23.0 DEGREES          
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    SER A  62     -114.32   -151.81                                   
REMARK 500    HIS A  86      138.42   -171.12                                   
REMARK 500    ASP A  94      102.77     -7.33                                   
REMARK 500    ASN A 123      -38.02   -130.67                                   
REMARK 500    HIS A 153      -53.66   -135.87                                   
REMARK 500    ASN A 207      -86.07   -121.96                                   
REMARK 500    MET A 212      101.30   -161.01                                   
REMARK 500    TYR A 239       99.96    -67.72                                   
REMARK 500    MET A 297       -0.60     80.52                                   
REMARK 500    ASP A 357       83.46   -160.96                                   
REMARK 500    VAL A 369       55.17     36.60                                   
REMARK 500    GLU S  13     -149.77     60.93                                   
REMARK 500    LEU S  15       -9.36     88.62                                   
REMARK 500    LYS S  71     -126.13     56.64                                   
REMARK 500    SER S 114      112.93   -172.19                                   
REMARK 500    LEU B  22     -138.01   -164.69                                   
REMARK 500    SER B  62      -86.24   -145.23                                   
REMARK 500    THR B  75     -169.19   -160.08                                   
REMARK 500    HIS B 153      -53.15   -135.59                                   
REMARK 500    ASN B 207      -85.67   -121.45                                   
REMARK 500    TYR B 239       98.20    -67.90                                   
REMARK 500    MET B 297       -1.61     79.59                                   
REMARK 500    ASP B 357       95.29   -161.19                                   
REMARK 500    VAL B 369       55.81     35.19                                   
REMARK 500    THR B 406      -54.47   -125.32                                   
REMARK 500    GLU T  13     -145.84     62.56                                   
REMARK 500    LEU T  15       -5.60     84.07                                   
REMARK 500    LYS T  71     -129.56     58.61                                   
REMARK 500    SER T 114      112.13   -174.36                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 912        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH A 993        DISTANCE =  5.75 ANGSTROMS                       
REMARK 525    HOH S 763        DISTANCE =  7.91 ANGSTROMS                       
REMARK 525    HOH S1013        DISTANCE =  5.39 ANGSTROMS                       
REMARK 525    HOH T 595        DISTANCE =  5.51 ANGSTROMS                       
REMARK 525    HOH T 960        DISTANCE =  5.65 ANGSTROMS                       
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 478  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 204   OE1                                                    
REMARK 620 2 KCX A 201   OQ1  84.7                                              
REMARK 620 3 ASP A 203   OD2  87.0  94.9                                        
REMARK 620 4 KCX A 201   OQ2 104.7  45.4 135.4                                  
REMARK 620 5 HOH A 616   O   160.1 105.2  75.2  94.2                            
REMARK 620 6 HOH A 693   O    95.5 102.5 162.5  60.6  98.9                      
REMARK 620 7 HOH A 901   O    88.0 172.3  87.1 135.2  82.5  75.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 478  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 204   OE1                                                    
REMARK 620 2 KCX B 201   OQ1  78.0                                              
REMARK 620 3 ASP B 203   OD2  97.5  96.5                                        
REMARK 620 4 HOH B 855   O   169.4 111.7  77.6                                  
REMARK 620 5 HOH B 787   O    93.5  83.6 168.7  91.9                            
REMARK 620 6 HOH B 734   O    93.1 171.1  84.3  77.1  97.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 478                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP A 479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP A 480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 478                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1WDD   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF RICE RUBISCO IN COMPLEX WITH CABP                       
REMARK 900 RELATED ID: 3AXM   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF RICE RUBISCO IN COMPLEX WITH 6PG                        
DBREF  3AXK A    1   477  UNP    P0C512   RBL_ORYSJ        1    477             
DBREF  3AXK S    1   129  UNP    Q0INY7   RBS1_ORYSJ      48    175             
DBREF  3AXK B    1   477  UNP    P0C512   RBL_ORYSJ        1    477             
DBREF  3AXK T    1   129  UNP    Q0INY7   RBS1_ORYSJ      48    175             
SEQADV 3AXK NME S    0  UNP  Q0INY7              AMIDATION                      
SEQADV 3AXK CYS S  112  UNP  Q0INY7    LEU   158 CONFLICT                       
SEQADV 3AXK NME T    0  UNP  Q0INY7              AMIDATION                      
SEQADV 3AXK CYS T  112  UNP  Q0INY7    LEU   158 CONFLICT                       
SEQRES   1 A  477  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLY PHE          
SEQRES   2 A  477  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR          
SEQRES   3 A  477  PRO GLU TYR GLU THR LYS ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 A  477  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 A  477  ALA GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 A  477  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 A  477  ARG TYR LYS GLY ARG CYS TYR HIS ILE GLU PRO VAL VAL          
SEQRES   8 A  477  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR PRO          
SEQRES   9 A  477  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 A  477  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 A  477  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO THR          
SEQRES  12 A  477  TYR SER LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN          
SEQRES  13 A  477  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU          
SEQRES  14 A  477  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 A  477  LYS ASN TYR GLY ARG ALA CYS TYR GLU CYS LEU ARG GLY          
SEQRES  16 A  477  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 A  477  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE VAL PHE CYS          
SEQRES  18 A  477  ALA GLU ALA ILE TYR LYS SER GLN ALA GLU THR GLY GLU          
SEQRES  19 A  477  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 A  477  GLU GLU MET ILE LYS ARG ALA VAL PHE ALA ARG GLU LEU          
SEQRES  21 A  477  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 A  477  PHE THR ALA ASN THR SER LEU ALA HIS TYR CYS ARG ASP          
SEQRES  23 A  477  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 A  477  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG          
SEQRES  25 A  477  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 A  477  ILE HIS ALA GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 A  477  ARG GLU MET THR LEU GLY PHE VAL ASP LEU LEU ARG ASP          
SEQRES  28 A  477  ASP PHE ILE GLU LYS ASP ARG ALA ARG GLY ILE PHE PHE          
SEQRES  29 A  477  THR GLN ASP TRP VAL SER MET PRO GLY VAL ILE PRO VAL          
SEQRES  30 A  477  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 A  477  THR GLU ILE PHE GLY ASP ASP SER VAL LEU GLN PHE GLY          
SEQRES  32 A  477  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 A  477  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN          
SEQRES  34 A  477  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN          
SEQRES  35 A  477  GLU ILE ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 A  477  ALA ALA ALA CYS GLU ILE TRP LYS ALA ILE LYS PHE GLU          
SEQRES  37 A  477  PHE GLU PRO VAL ASP LYS LEU ASP SER                          
SEQRES   1 S  129  NME MET GLN VAL TRP PRO ILE GLU GLY ILE LYS LYS PHE          
SEQRES   2 S  129  GLU THR LEU SER TYR LEU PRO PRO LEU THR VAL GLU ASP          
SEQRES   3 S  129  LEU LEU LYS GLN ILE GLU TYR LEU LEU ARG SER LYS TRP          
SEQRES   4 S  129  VAL PRO CYS LEU GLU PHE SER LYS VAL GLY PHE VAL TYR          
SEQRES   5 S  129  ARG GLU ASN HIS ARG SER PRO GLY TYR TYR ASP GLY ARG          
SEQRES   6 S  129  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR          
SEQRES   7 S  129  ASP ALA THR GLN VAL LEU LYS GLU LEU GLU GLU ALA LYS          
SEQRES   8 S  129  LYS ALA TYR PRO ASP ALA PHE VAL ARG ILE ILE GLY PHE          
SEQRES   9 S  129  ASP ASN VAL ARG GLN VAL GLN CYS ILE SER PHE ILE ALA          
SEQRES  10 S  129  TYR LYS PRO PRO GLY CYS GLU GLU SER GLY GLY ASN              
SEQRES   1 B  477  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLY PHE          
SEQRES   2 B  477  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR          
SEQRES   3 B  477  PRO GLU TYR GLU THR LYS ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 B  477  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 B  477  ALA GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 B  477  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 B  477  ARG TYR LYS GLY ARG CYS TYR HIS ILE GLU PRO VAL VAL          
SEQRES   8 B  477  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR PRO          
SEQRES   9 B  477  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 B  477  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 B  477  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO THR          
SEQRES  12 B  477  TYR SER LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN          
SEQRES  13 B  477  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU          
SEQRES  14 B  477  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 B  477  LYS ASN TYR GLY ARG ALA CYS TYR GLU CYS LEU ARG GLY          
SEQRES  16 B  477  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 B  477  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE VAL PHE CYS          
SEQRES  18 B  477  ALA GLU ALA ILE TYR LYS SER GLN ALA GLU THR GLY GLU          
SEQRES  19 B  477  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 B  477  GLU GLU MET ILE LYS ARG ALA VAL PHE ALA ARG GLU LEU          
SEQRES  21 B  477  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 B  477  PHE THR ALA ASN THR SER LEU ALA HIS TYR CYS ARG ASP          
SEQRES  23 B  477  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 B  477  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG          
SEQRES  25 B  477  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 B  477  ILE HIS ALA GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 B  477  ARG GLU MET THR LEU GLY PHE VAL ASP LEU LEU ARG ASP          
SEQRES  28 B  477  ASP PHE ILE GLU LYS ASP ARG ALA ARG GLY ILE PHE PHE          
SEQRES  29 B  477  THR GLN ASP TRP VAL SER MET PRO GLY VAL ILE PRO VAL          
SEQRES  30 B  477  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 B  477  THR GLU ILE PHE GLY ASP ASP SER VAL LEU GLN PHE GLY          
SEQRES  32 B  477  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 B  477  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN          
SEQRES  34 B  477  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN          
SEQRES  35 B  477  GLU ILE ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 B  477  ALA ALA ALA CYS GLU ILE TRP LYS ALA ILE LYS PHE GLU          
SEQRES  37 B  477  PHE GLU PRO VAL ASP LYS LEU ASP SER                          
SEQRES   1 T  129  NME MET GLN VAL TRP PRO ILE GLU GLY ILE LYS LYS PHE          
SEQRES   2 T  129  GLU THR LEU SER TYR LEU PRO PRO LEU THR VAL GLU ASP          
SEQRES   3 T  129  LEU LEU LYS GLN ILE GLU TYR LEU LEU ARG SER LYS TRP          
SEQRES   4 T  129  VAL PRO CYS LEU GLU PHE SER LYS VAL GLY PHE VAL TYR          
SEQRES   5 T  129  ARG GLU ASN HIS ARG SER PRO GLY TYR TYR ASP GLY ARG          
SEQRES   6 T  129  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR          
SEQRES   7 T  129  ASP ALA THR GLN VAL LEU LYS GLU LEU GLU GLU ALA LYS          
SEQRES   8 T  129  LYS ALA TYR PRO ASP ALA PHE VAL ARG ILE ILE GLY PHE          
SEQRES   9 T  129  ASP ASN VAL ARG GLN VAL GLN CYS ILE SER PHE ILE ALA          
SEQRES  10 T  129  TYR LYS PRO PRO GLY CYS GLU GLU SER GLY GLY ASN              
MODRES 3AXK KCX A  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3AXK KCX B  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
HET    KCX  A 201      12                                                       
HET    NME  S   0       1                                                       
HET    KCX  B 201      12                                                       
HET    NME  T   0       1                                                       
HET    GOL  A 501       6                                                       
HET    GOL  A 502       6                                                       
HET     MG  A 478       1                                                       
HET    NDP  A 479      48                                                       
HET    NDP  A 480      48                                                       
HET    GOL  B 503       6                                                       
HET    GOL  B 504       6                                                       
HET     MG  B 478       1                                                       
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID                                        
HETNAM     NME METHYLAMINE                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE                  
HETNAM   2 NDP  PHOSPHATE                                                       
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  KCX    2(C7 H14 N2 O4)                                              
FORMUL   2  NME    2(C H5 N)                                                    
FORMUL   5  GOL    4(C3 H8 O3)                                                  
FORMUL   7   MG    2(MG 2+)                                                     
FORMUL   8  NDP    2(C21 H30 N7 O17 P3)                                         
FORMUL  13  HOH   *1125(H2 O)                                                   
HELIX    1   1 TYR A   20  TYR A   25  1                                   6    
HELIX    2   2 PRO A   49  SER A   61  1                                  13    
HELIX    3   3 VAL A   69  THR A   75  5                                   7    
HELIX    4   4 SER A   76  TYR A   80  5                                   5    
HELIX    5   5 PRO A  104  PHE A  108  5                                   5    
HELIX    6   6 SER A  112  GLY A  122  1                                  11    
HELIX    7   7 ASN A  123  PHE A  127  5                                   5    
HELIX    8   8 PRO A  141  LYS A  146  1                                   6    
HELIX    9   9 GLY A  154  ASN A  163  1                                  10    
HELIX   10  10 SER A  181  GLY A  195  1                                  15    
HELIX   11  11 ARG A  213  GLY A  233  1                                  21    
HELIX   12  12 THR A  246  GLY A  261  1                                  16    
HELIX   13  13 TYR A  269  GLY A  273  1                                   5    
HELIX   14  14 GLY A  273  GLY A  288  1                                  16    
HELIX   15  15 MET A  297  ARG A  303  1                                   7    
HELIX   16  16 HIS A  310  GLY A  322  1                                  13    
HELIX   17  17 GLU A  338  ASP A  351  1                                  14    
HELIX   18  18 ASP A  357  GLY A  361  5                                   5    
HELIX   19  19 HIS A  383  TRP A  385  5                                   3    
HELIX   20  20 HIS A  386  GLY A  395  1                                  10    
HELIX   21  21 GLY A  403  GLY A  408  1                                   6    
HELIX   22  22 GLY A  412  GLU A  433  1                                  22    
HELIX   23  23 ASP A  436  LYS A  450  1                                  15    
HELIX   24  24 SER A  452  TRP A  462  1                                  11    
HELIX   25  25 THR S   22  SER S   36  1                                  15    
HELIX   26  26 ASP S   79  TYR S   94  1                                  16    
HELIX   27  27 PRO B   49  SER B   61  1                                  13    
HELIX   28  28 TRP B   70  THR B   75  5                                   6    
HELIX   29  29 SER B   76  LYS B   81  1                                   6    
HELIX   30  30 PRO B  104  PHE B  108  5                                   5    
HELIX   31  31 SER B  112  GLY B  122  1                                  11    
HELIX   32  32 ASN B  123  PHE B  127  5                                   5    
HELIX   33  33 PRO B  141  LYS B  146  1                                   6    
HELIX   34  34 GLY B  154  ASN B  163  1                                  10    
HELIX   35  35 SER B  181  GLY B  195  1                                  15    
HELIX   36  36 ARG B  213  GLY B  233  1                                  21    
HELIX   37  37 THR B  246  GLY B  261  1                                  16    
HELIX   38  38 TYR B  269  GLY B  273  1                                   5    
HELIX   39  39 GLY B  273  GLY B  288  1                                  16    
HELIX   40  40 MET B  297  ARG B  303  1                                   7    
HELIX   41  41 HIS B  310  GLY B  322  1                                  13    
HELIX   42  42 GLU B  338  ASP B  351  1                                  14    
HELIX   43  43 ASP B  357  GLY B  361  5                                   5    
HELIX   44  44 HIS B  383  TRP B  385  5                                   3    
HELIX   45  45 HIS B  386  GLY B  395  1                                  10    
HELIX   46  46 GLY B  403  GLY B  408  1                                   6    
HELIX   47  47 GLY B  412  GLU B  433  1                                  22    
HELIX   48  48 ASP B  436  CYS B  449  1                                  14    
HELIX   49  49 SER B  452  LYS B  463  1                                  12    
HELIX   50  50 THR T   22  SER T   36  1                                  15    
HELIX   51  51 ASP T   79  TYR T   94  1                                  16    
SHEET    1   A 5 ARG A  83  PRO A  89  0                                        
SHEET    2   A 5 TYR A  97  TYR A 103 -1  O  TYR A 100   N  HIS A  86           
SHEET    3   A 5 ILE A  36  PRO A  44 -1  N  VAL A  42   O  TYR A  97           
SHEET    4   A 5 LEU A 130  ARG A 139 -1  O  ARG A 134   N  ARG A  41           
SHEET    5   A 5 GLY A 308  MET A 309  1  O  GLY A 308   N  LEU A 135           
SHEET    1   B 9 LEU A 169  THR A 173  0                                        
SHEET    2   B 9 PHE A 199  KCX A 201  1  O  PHE A 199   N  LEU A 170           
SHEET    3   B 9 GLY A 237  ASN A 241  1  O  TYR A 239   N  THR A 200           
SHEET    4   B 9 ILE A 264  ASP A 268  1  O  MET A 266   N  LEU A 240           
SHEET    5   B 9 LEU A 290  HIS A 294  1  O  HIS A 292   N  VAL A 265           
SHEET    6   B 9 HIS A 325  GLY A 329  1  N  HIS A 325   O  LEU A 291           
SHEET    7   B 9 ILE A 375  SER A 379  1  O  VAL A 377   N  ALA A 328           
SHEET    8   B 9 VAL A 399  PHE A 402  1  O  GLN A 401   N  ALA A 378           
SHEET    9   B 9 LEU A 169  THR A 173  1  N  GLY A 171   O  PHE A 402           
SHEET    1   C 2 PHE A 353  ILE A 354  0                                        
SHEET    2   C 2 GLN A 366  ASP A 367 -1  O  GLN A 366   N  ILE A 354           
SHEET    1   D 4 THR S  68  TRP S  70  0                                        
SHEET    2   D 4 VAL S  39  SER S  45 -1  N  LEU S  42   O  TRP S  70           
SHEET    3   D 4 PHE S  98  ASP S 105 -1  O  PHE S  98   N  SER S  45           
SHEET    4   D 4 VAL S 110  TYR S 118 -1  O  PHE S 115   N  ILE S 101           
SHEET    1   E 5 ARG B  83  PRO B  89  0                                        
SHEET    2   E 5 TYR B  97  TYR B 103 -1  O  ILE B  98   N  GLU B  88           
SHEET    3   E 5 ILE B  36  PRO B  44 -1  N  PHE B  40   O  ALA B  99           
SHEET    4   E 5 LEU B 130  ARG B 139 -1  O  ARG B 134   N  ARG B  41           
SHEET    5   E 5 GLY B 308  MET B 309  1  O  GLY B 308   N  LEU B 135           
SHEET    1   F 9 LEU B 169  THR B 173  0                                        
SHEET    2   F 9 PHE B 199  KCX B 201  1  O  PHE B 199   N  LEU B 170           
SHEET    3   F 9 GLY B 237  ASN B 241  1  O  TYR B 239   N  THR B 200           
SHEET    4   F 9 ILE B 264  ASP B 268  1  O  MET B 266   N  LEU B 240           
SHEET    5   F 9 LEU B 290  HIS B 294  1  O  HIS B 292   N  VAL B 265           
SHEET    6   F 9 HIS B 325  GLY B 329  1  N  HIS B 325   O  LEU B 291           
SHEET    7   F 9 ILE B 375  SER B 379  1  O  VAL B 377   N  ALA B 328           
SHEET    8   F 9 VAL B 399  GLN B 401  1  O  VAL B 399   N  ALA B 378           
SHEET    9   F 9 LEU B 169  THR B 173  1  N  LEU B 169   O  LEU B 400           
SHEET    1   G 2 PHE B 353  ILE B 354  0                                        
SHEET    2   G 2 GLN B 366  ASP B 367 -1  O  GLN B 366   N  ILE B 354           
SHEET    1   H 4 THR T  68  TRP T  70  0                                        
SHEET    2   H 4 VAL T  39  SER T  45 -1  N  LEU T  42   O  TRP T  70           
SHEET    3   H 4 PHE T  98  ASP T 105 -1  O  ILE T 102   N  CYS T  41           
SHEET    4   H 4 VAL T 110  TYR T 118 -1  O  ALA T 117   N  VAL T  99           
SSBOND   1 CYS A  247    CYS B  247                          1555   1555  2.67  
LINK         C   THR A 200                 N   KCX A 201     1555   1555  1.33  
LINK         C   KCX A 201                 N   ASP A 202     1555   1555  1.34  
LINK         C   THR B 200                 N   KCX B 201     1555   1555  1.33  
LINK         C   KCX B 201                 N   ASP B 202     1555   1555  1.33  
LINK         OE1 GLU A 204                MG    MG A 478     1555   1555  1.99  
LINK         OE1 GLU B 204                MG    MG B 478     1555   1555  2.08  
LINK         OQ1 KCX A 201                MG    MG A 478     1555   1555  2.10  
LINK         OQ1 KCX B 201                MG    MG B 478     1555   1555  2.15  
LINK         OD2 ASP B 203                MG    MG B 478     1555   1555  2.16  
LINK         OD2 ASP A 203                MG    MG A 478     1555   1555  2.43  
LINK         OQ2 KCX A 201                MG    MG A 478     1555   1555  2.99  
LINK        MG    MG A 478                 O   HOH A 616     1555   1555  1.98  
LINK        MG    MG B 478                 O   HOH B 855     1555   1555  1.99  
LINK        MG    MG A 478                 O   HOH A 693     1555   1555  2.04  
LINK        MG    MG B 478                 O   HOH B 787     1555   1555  2.24  
LINK        MG    MG B 478                 O   HOH B 734     1555   1555  2.27  
LINK        MG    MG A 478                 O   HOH A 901     1555   1555  2.59  
LINK         C   NME T   0                 N   MET T   1     1555   1555  1.33  
LINK         C   NME S   0                 N   MET S   1     1555   1555  1.33  
CISPEP   1 LYS A  175    PRO A  176          0        -0.92                     
CISPEP   2 LYS B  175    PRO B  176          0         0.37                     
SITE     1 AC1  9 LEU A 270  GLY A 273  MET A 297  ILE A 301                    
SITE     2 AC1  9 HOH A 627  HOH A 628  HOH A 629  LEU B 270                    
SITE     3 AC1  9 ILE B 301                                                     
SITE     1 AC2  5 HIS A  86  GLU A  88  LYS A 356  ARG A 358                    
SITE     2 AC2  5 HOH B 976                                                     
SITE     1 AC3  6 KCX A 201  ASP A 203  GLU A 204  HOH A 616                    
SITE     2 AC3  6 HOH A 693  HOH A 901                                          
SITE     1 AC4 28 LYS A 175  HIS A 294  ARG A 295  HIS A 298                    
SITE     2 AC4 28 SER A 379  GLY A 380  GLY A 381  GLY A 403                    
SITE     3 AC4 28 GLY A 404  GLY A 405  HOH A 580  HOH A 595                    
SITE     4 AC4 28 HOH A 614  HOH A 616  HOH A 693  HOH A 758                    
SITE     5 AC4 28 HOH A1073  HOH A1080  HOH A1081  HOH A1083                    
SITE     6 AC4 28 HOH A1085  HOH A1086  HOH A1115  GLU B  60                    
SITE     7 AC4 28 ASN B 123  GLY B 126  PHE B 127  HOH B 733                    
SITE     1 AC5 32 GLU A  60  THR A  68  ASN A 123  GLY A 126                    
SITE     2 AC5 32 PHE A 127  HOH A 534  HOH A 594  HOH A 854                    
SITE     3 AC5 32 HOH A1074  HOH A1076  HOH A1090  HOH A1091                    
SITE     4 AC5 32 HOH A1092  HOH A1093  HOH A1096  LYS B 175                    
SITE     5 AC5 32 HIS B 294  ARG B 295  HIS B 298  SER B 379                    
SITE     6 AC5 32 GLY B 380  GLY B 381  ILE B 382  GLY B 404                    
SITE     7 AC5 32 GLY B 405  HOH B 696  HOH B 787  HOH B 855                    
SITE     8 AC5 32 HOH B1078  HOH B1079  HOH B1087  HOH B1125                    
SITE     1 AC6  9 SER A 145  LYS A 146  PHE A 148  ARG A 213                    
SITE     2 AC6  9 HOH A 497  HOH A 539  HOH A1109  GLU B 110                    
SITE     3 AC6  9 GOL B 504                                                     
SITE     1 AC7  6 LYS A 146  THR A 147  HOH A 894  HOH A 895                    
SITE     2 AC7  6 GOL B 503  HOH B 654                                          
SITE     1 AC8  6 KCX B 201  ASP B 203  GLU B 204  HOH B 734                    
SITE     2 AC8  6 HOH B 787  HOH B 855                                          
CRYST1  110.246  110.246  199.768  90.00  90.00  90.00 I 4          16          
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      0.009071  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009071  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005006        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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