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Database: PDB
Entry: 2DBZ
LinkDB: 2DBZ
Original site: 2DBZ 
HEADER    OXIDOREDUCTASE                          16-DEC-05   2DBZ              
TITLE     CRYSTAL STRUCTURE OF GLYOXYLATE REDUCTASE (PH0597) FROM PYROCOCCUS    
TITLE    2 HORIKOSHII OT3, COMPLEXED WITH NADP (P61)                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLYOXYLATE REDUCTASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: GLYCOLATE REDUCTASE, PH0597;                                
COMPND   5 EC: 1.1.1.26;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PYROCOCCUS HORIKOSHII;                          
SOURCE   3 ORGANISM_TAXID: 70601;                                               
SOURCE   4 STRAIN: OT3;                                                         
SOURCE   5 GENE: PH0597;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIL;                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET11A                                    
KEYWDS    GLYOXYLATE REDUCTASE, D-3-PHOSPHOGLYCERATE DEHYDROGENASE, STRUCTURAL  
KEYWDS   2 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND         
KEYWDS   3 FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS            
KEYWDS   4 INITIATIVE, RSGI, OXIDOREDUCTASE                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.YOSHIKAWA,R.ARAI,Y.KINOSHITA,T.UCHIKUBO-KAMO,R.AKASAKA,T.TERADA,    
AUTHOR   2 M.SHIROUZU,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS           
AUTHOR   3 INITIATIVE (RSGI)                                                    
REVDAT   5   13-JUL-11 2DBZ    1       VERSN                                    
REVDAT   4   09-JUN-09 2DBZ    1       REVDAT                                   
REVDAT   3   24-FEB-09 2DBZ    1       VERSN                                    
REVDAT   2   02-DEC-08 2DBZ    1       JRNL                                     
REVDAT   1   16-JUN-06 2DBZ    0                                                
JRNL        AUTH   S.YOSHIKAWA,R.ARAI,Y.KINOSHITA,T.UCHIKUBO-KAMO,T.WAKAMATSU,  
JRNL        AUTH 2 R.AKASAKA,R.MASUI,T.TERADA,S.KURAMITSU,M.SHIROUZU,S.YOKOYAMA 
JRNL        TITL   STRUCTURE OF ARCHAEAL GLYOXYLATE REDUCTASE FROM PYROCOCCUS   
JRNL        TITL 2 HORIKOSHII OT3 COMPLEXED WITH NICOTINAMIDE ADENINE           
JRNL        TITL 3 DINUCLEOTIDE PHOSPHATE.                                      
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  63   357 2007              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   17327673                                                     
JRNL        DOI    10.1107/S0907444906055442                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.45 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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.31                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 848916.650                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 90.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 37243                          
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) : 0.239                           
REMARK   3   FREE R VALUE                     : 0.276                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 3747                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
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) : 2.45                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.60                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 82.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5100                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3340                       
REMARK   3   BIN FREE R VALUE                    : 0.3880                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.10                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 573                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.016                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5346                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 116                                     
REMARK   3   SOLVENT ATOMS            : 73                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 55.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 62.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -7.18000                                             
REMARK   3    B22 (A**2) : -7.18000                                             
REMARK   3    B33 (A**2) : 14.37000                                             
REMARK   3    B12 (A**2) : 4.12000                                              
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) : 0.35                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.33                            
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) : 0.42                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.37                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.90                            
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) : 3.930 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 5.320 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 6.600 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 8.360 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.36                                                 
REMARK   3   BSOL        : 47.19                                                
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  : SO4.PARAM                                      
REMARK   3  PARAMETER FILE  4  : NAP.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   : SO4.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NAP.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2DBZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-DEC-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB025233.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-MAY-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL26B1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : SI DOUBLE CRYSTAL                  
REMARK 200  OPTICS                         : TWO DIMENSIONAL FOCUSING MIRROR    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU JUPITER 210                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41156                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 7.236                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.7890                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.90                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.46500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.502                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2DBQ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.77                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M POTASSIUM SODIUM TARTRATE PH 5.6,   
REMARK 280  0.1M SODIUM CITRATE, 2.0M AMMONIUM SULFATE, VAPOR DIFFUSION,        
REMARK 280  SITTING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.69300            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      121.38600            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       91.03950            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      151.73250            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       30.34650            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10990 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 26000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -120.0 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     GLU A   334                                                      
REMARK 465     GLU B   334                                                      
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    ASN A  64       11.57    -61.39                                   
REMARK 500    LEU A  68      107.92    -49.59                                   
REMARK 500    TYR A  78       26.58   -148.28                                   
REMARK 500    ASP A  98      -38.02     68.66                                   
REMARK 500    LEU A 158       56.86    -93.73                                   
REMARK 500    ALA A 211       46.27   -149.51                                   
REMARK 500    ALA A 240      -91.50    -91.18                                   
REMARK 500    ASN A 274      103.88   -161.90                                   
REMARK 500    ARG A 329      148.50   -178.30                                   
REMARK 500    ASP B  58     -159.40    -87.54                                   
REMARK 500    TYR B  74       57.05    -98.27                                   
REMARK 500    TYR B  78       27.50   -151.91                                   
REMARK 500    ASP B  98      -40.13     69.93                                   
REMARK 500    ALA B 211       44.63   -156.45                                   
REMARK 500    ALA B 240      -88.93    -89.86                                   
REMARK 500    ARG B 313       20.16    -71.47                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 402                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2DBQ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE SAME PROTEIN (SPACE GROUP I41)              
REMARK 900 RELATED ID: 2DBR   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE SAME PROTEIN (SPACE GROUP P1)               
REMARK 900 RELATED ID: PHO001000597.2   RELATED DB: TARGETDB                    
DBREF  2DBZ A    1   334  UNP    O58320   GYAR_PYRHO       1    334             
DBREF  2DBZ B    1   334  UNP    O58320   GYAR_PYRHO       1    334             
SEQRES   1 A  334  MET LYS PRO LYS VAL PHE ILE THR ARG GLU ILE PRO GLU          
SEQRES   2 A  334  VAL GLY ILE LYS MET LEU GLU ASP GLU PHE GLU VAL GLU          
SEQRES   3 A  334  VAL TRP GLY ASP GLU LYS GLU ILE PRO ARG GLU ILE LEU          
SEQRES   4 A  334  LEU LYS LYS VAL LYS GLU VAL ASP ALA LEU VAL THR MET          
SEQRES   5 A  334  LEU SER GLU ARG ILE ASP LYS GLU VAL PHE GLU ASN ALA          
SEQRES   6 A  334  PRO LYS LEU ARG ILE VAL ALA ASN TYR ALA VAL GLY TYR          
SEQRES   7 A  334  ASP ASN ILE ASP ILE GLU GLU ALA THR LYS ARG GLY ILE          
SEQRES   8 A  334  TYR VAL THR ASN THR PRO ASP VAL LEU THR ASP ALA THR          
SEQRES   9 A  334  ALA ASP LEU ALA PHE ALA LEU LEU LEU ALA THR ALA ARG          
SEQRES  10 A  334  HIS VAL VAL LYS GLY ASP ARG PHE VAL ARG SER GLY GLU          
SEQRES  11 A  334  TRP LYS LYS ARG GLY VAL ALA TRP HIS PRO LYS TRP PHE          
SEQRES  12 A  334  LEU GLY TYR ASP VAL TYR GLY LYS THR ILE GLY ILE ILE          
SEQRES  13 A  334  GLY LEU GLY ARG ILE GLY GLN ALA ILE ALA LYS ARG ALA          
SEQRES  14 A  334  LYS GLY PHE ASN MET ARG ILE LEU TYR TYR SER ARG THR          
SEQRES  15 A  334  ARG LYS GLU GLU VAL GLU ARG GLU LEU ASN ALA GLU PHE          
SEQRES  16 A  334  LYS PRO LEU GLU ASP LEU LEU ARG GLU SER ASP PHE VAL          
SEQRES  17 A  334  VAL LEU ALA VAL PRO LEU THR ARG GLU THR TYR HIS LEU          
SEQRES  18 A  334  ILE ASN GLU GLU ARG LEU LYS LEU MET LYS LYS THR ALA          
SEQRES  19 A  334  ILE LEU ILE ASN ILE ALA ARG GLY LYS VAL VAL ASP THR          
SEQRES  20 A  334  ASN ALA LEU VAL LYS ALA LEU LYS GLU GLY TRP ILE ALA          
SEQRES  21 A  334  GLY ALA GLY LEU ASP VAL PHE GLU GLU GLU PRO TYR TYR          
SEQRES  22 A  334  ASN GLU GLU LEU PHE LYS LEU ASP ASN VAL VAL LEU THR          
SEQRES  23 A  334  PRO HIS ILE GLY SER ALA SER PHE GLY ALA ARG GLU GLY          
SEQRES  24 A  334  MET ALA GLU LEU VAL ALA LYS ASN LEU ILE ALA PHE LYS          
SEQRES  25 A  334  ARG GLY GLU ILE PRO PRO THR LEU VAL ASN ARG GLU VAL          
SEQRES  26 A  334  ILE LYS ILE ARG LYS PRO GLY PHE GLU                          
SEQRES   1 B  334  MET LYS PRO LYS VAL PHE ILE THR ARG GLU ILE PRO GLU          
SEQRES   2 B  334  VAL GLY ILE LYS MET LEU GLU ASP GLU PHE GLU VAL GLU          
SEQRES   3 B  334  VAL TRP GLY ASP GLU LYS GLU ILE PRO ARG GLU ILE LEU          
SEQRES   4 B  334  LEU LYS LYS VAL LYS GLU VAL ASP ALA LEU VAL THR MET          
SEQRES   5 B  334  LEU SER GLU ARG ILE ASP LYS GLU VAL PHE GLU ASN ALA          
SEQRES   6 B  334  PRO LYS LEU ARG ILE VAL ALA ASN TYR ALA VAL GLY TYR          
SEQRES   7 B  334  ASP ASN ILE ASP ILE GLU GLU ALA THR LYS ARG GLY ILE          
SEQRES   8 B  334  TYR VAL THR ASN THR PRO ASP VAL LEU THR ASP ALA THR          
SEQRES   9 B  334  ALA ASP LEU ALA PHE ALA LEU LEU LEU ALA THR ALA ARG          
SEQRES  10 B  334  HIS VAL VAL LYS GLY ASP ARG PHE VAL ARG SER GLY GLU          
SEQRES  11 B  334  TRP LYS LYS ARG GLY VAL ALA TRP HIS PRO LYS TRP PHE          
SEQRES  12 B  334  LEU GLY TYR ASP VAL TYR GLY LYS THR ILE GLY ILE ILE          
SEQRES  13 B  334  GLY LEU GLY ARG ILE GLY GLN ALA ILE ALA LYS ARG ALA          
SEQRES  14 B  334  LYS GLY PHE ASN MET ARG ILE LEU TYR TYR SER ARG THR          
SEQRES  15 B  334  ARG LYS GLU GLU VAL GLU ARG GLU LEU ASN ALA GLU PHE          
SEQRES  16 B  334  LYS PRO LEU GLU ASP LEU LEU ARG GLU SER ASP PHE VAL          
SEQRES  17 B  334  VAL LEU ALA VAL PRO LEU THR ARG GLU THR TYR HIS LEU          
SEQRES  18 B  334  ILE ASN GLU GLU ARG LEU LYS LEU MET LYS LYS THR ALA          
SEQRES  19 B  334  ILE LEU ILE ASN ILE ALA ARG GLY LYS VAL VAL ASP THR          
SEQRES  20 B  334  ASN ALA LEU VAL LYS ALA LEU LYS GLU GLY TRP ILE ALA          
SEQRES  21 B  334  GLY ALA GLY LEU ASP VAL PHE GLU GLU GLU PRO TYR TYR          
SEQRES  22 B  334  ASN GLU GLU LEU PHE LYS LEU ASP ASN VAL VAL LEU THR          
SEQRES  23 B  334  PRO HIS ILE GLY SER ALA SER PHE GLY ALA ARG GLU GLY          
SEQRES  24 B  334  MET ALA GLU LEU VAL ALA LYS ASN LEU ILE ALA PHE LYS          
SEQRES  25 B  334  ARG GLY GLU ILE PRO PRO THR LEU VAL ASN ARG GLU VAL          
SEQRES  26 B  334  ILE LYS ILE ARG LYS PRO GLY PHE GLU                          
HET    SO4  B 501       5                                                       
HET    SO4  A 502       5                                                       
HET    SO4  B 503       5                                                       
HET    SO4  A 504       5                                                       
HET    NAP  A 401      48                                                       
HET    NAP  B 402      48                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE                 
HETSYN     NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE                       
FORMUL   3  SO4    4(O4 S 2-)                                                   
FORMUL   7  NAP    2(C21 H28 N7 O17 P3)                                         
FORMUL   9  HOH   *73(H2 O)                                                     
HELIX    1   1 PRO A   12  ASP A   21  1                                  10    
HELIX    2   2 PRO A   35  VAL A   43  1                                   9    
HELIX    3   3 ASP A   58  ASN A   64  1                                   7    
HELIX    4   4 ASP A   82  ARG A   89  1                                   8    
HELIX    5   5 LEU A  100  HIS A  118  1                                  19    
HELIX    6   6 HIS A  118  SER A  128  1                                  11    
HELIX    7   7 GLY A  129  GLY A  135  1                                   7    
HELIX    8   8 GLY A  159  PHE A  172  1                                  14    
HELIX    9   9 LYS A  184  ASN A  192  1                                   9    
HELIX   10  10 PRO A  197  SER A  205  1                                   9    
HELIX   11  11 ASN A  223  MET A  230  1                                   8    
HELIX   12  12 ARG A  241  VAL A  245  5                                   5    
HELIX   13  13 ASP A  246  GLY A  257  1                                  12    
HELIX   14  14 ASN A  274  LEU A  280  1                                   7    
HELIX   15  15 SER A  293  ARG A  313  1                                  21    
HELIX   16  16 GLU A  324  ARG A  329  1                                   6    
HELIX   17  17 PRO B   12  ASP B   21  1                                  10    
HELIX   18  18 PRO B   35  VAL B   43  1                                   9    
HELIX   19  19 ASP B   58  ASN B   64  1                                   7    
HELIX   20  20 ASP B   82  ARG B   89  1                                   8    
HELIX   21  21 LEU B  100  HIS B  118  1                                  19    
HELIX   22  22 HIS B  118  SER B  128  1                                  11    
HELIX   23  23 GLY B  129  ARG B  134  1                                   6    
HELIX   24  24 GLY B  159  GLY B  171  1                                  13    
HELIX   25  25 LYS B  184  ASN B  192  1                                   9    
HELIX   26  26 PRO B  197  SER B  205  1                                   9    
HELIX   27  27 GLU B  225  MET B  230  1                                   6    
HELIX   28  28 ARG B  241  VAL B  245  5                                   5    
HELIX   29  29 ASP B  246  GLU B  256  1                                  11    
HELIX   30  30 ASN B  274  LEU B  280  1                                   7    
HELIX   31  31 SER B  293  ARG B  313  1                                  21    
HELIX   32  32 GLU B  324  ARG B  329  1                                   6    
SHEET    1   A 5 GLU A  24  VAL A  27  0                                        
SHEET    2   A 5 LYS A   4  ILE A   7  1  N  ILE A   7   O  GLU A  26           
SHEET    3   A 5 ALA A  48  THR A  51  1  O  ALA A  48   N  LYS A   4           
SHEET    4   A 5 ILE A  70  ASN A  73  1  O  ALA A  72   N  LEU A  49           
SHEET    5   A 5 TYR A  92  THR A  94  1  O  TYR A  92   N  VAL A  71           
SHEET    1   B 7 ALA A 193  PHE A 195  0                                        
SHEET    2   B 7 ARG A 175  TYR A 179  1  N  ILE A 176   O  GLU A 194           
SHEET    3   B 7 THR A 152  ILE A 156  1  N  ILE A 153   O  LEU A 177           
SHEET    4   B 7 PHE A 207  LEU A 210  1  O  PHE A 207   N  GLY A 154           
SHEET    5   B 7 ILE A 235  ASN A 238  1  O  ILE A 237   N  VAL A 208           
SHEET    6   B 7 GLY A 261  LEU A 264  1  O  GLY A 263   N  LEU A 236           
SHEET    7   B 7 VAL A 283  LEU A 285  1  O  VAL A 284   N  LEU A 264           
SHEET    1   C 5 GLU B  24  VAL B  27  0                                        
SHEET    2   C 5 LYS B   4  ILE B   7  1  N  ILE B   7   O  GLU B  26           
SHEET    3   C 5 ALA B  48  THR B  51  1  O  ALA B  48   N  LYS B   4           
SHEET    4   C 5 ILE B  70  ASN B  73  1  O  ALA B  72   N  LEU B  49           
SHEET    5   C 5 TYR B  92  THR B  94  1  O  TYR B  92   N  VAL B  71           
SHEET    1   D 7 ALA B 193  PHE B 195  0                                        
SHEET    2   D 7 ARG B 175  TYR B 179  1  N  ILE B 176   O  GLU B 194           
SHEET    3   D 7 THR B 152  ILE B 156  1  N  ILE B 153   O  LEU B 177           
SHEET    4   D 7 PHE B 207  LEU B 210  1  O  PHE B 207   N  GLY B 154           
SHEET    5   D 7 ILE B 235  ASN B 238  1  O  ILE B 237   N  VAL B 208           
SHEET    6   D 7 GLY B 261  LEU B 264  1  O  GLY B 263   N  LEU B 236           
SHEET    7   D 7 VAL B 283  LEU B 285  1  O  VAL B 284   N  LEU B 264           
CISPEP   1 GLU A  270    PRO A  271          0        -0.07                     
CISPEP   2 GLU B  270    PRO B  271          0        -0.12                     
SITE     1 AC1  4 TYR B  78  ASN B  95  ARG B 160  HOH B 530                    
SITE     1 AC2  3 TYR A  78  ASN A  95  ARG A 160                               
SITE     1 AC3  8 LEU B  53  ALA B  75  VAL B  76  GLY B  77                    
SITE     2 AC3  8 ARG B 241  HIS B 288  SER B 291  NAP B 402                    
SITE     1 AC4  9 LEU A  53  ALA A  75  VAL A  76  GLY A  77                    
SITE     2 AC4  9 LEU A 100  ARG A 241  HIS A 288  SER A 291                    
SITE     3 AC4  9 NAP A 401                                                     
SITE     1 AC5 24 LYS A  42  VAL A  76  GLY A  77  THR A 104                    
SITE     2 AC5 24 LEU A 158  GLY A 159  ARG A 160  ILE A 161                    
SITE     3 AC5 24 SER A 180  ARG A 181  THR A 182  ALA A 211                    
SITE     4 AC5 24 PRO A 213  GLU A 217  THR A 218  ILE A 239                    
SITE     5 AC5 24 ALA A 240  ARG A 241  ASP A 265  HIS A 288                    
SITE     6 AC5 24 GLY A 290  SER A 291  SO4 A 504  HOH A 512                    
SITE     1 AC6 27 LYS B  42  VAL B  76  GLY B  77  THR B 104                    
SITE     2 AC6 27 GLY B 157  LEU B 158  GLY B 159  ARG B 160                    
SITE     3 AC6 27 ILE B 161  SER B 180  ARG B 181  THR B 182                    
SITE     4 AC6 27 ALA B 211  VAL B 212  PRO B 213  GLU B 217                    
SITE     5 AC6 27 THR B 218  ILE B 239  ALA B 240  ARG B 241                    
SITE     6 AC6 27 ASP B 265  HIS B 288  GLY B 290  SER B 291                    
SITE     7 AC6 27 SO4 B 503  HOH B 510  HOH B 530                               
CRYST1  104.472  104.472  182.079  90.00  90.00 120.00 P 61         12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009572  0.005526  0.000000        0.00000                         
SCALE2      0.000000  0.011053  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005492        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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