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Database: PDB
Entry: 2O4C
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Original site: 2O4C 
HEADER    OXIDOREDUCTASE                          04-DEC-06   2O4C              
TITLE     CRYSTAL STRUCTURE OF D-ERYTHRONATE-4-PHOSPHATE DEHYDROGENASE COMPLEXED
TITLE    2 WITH NAD                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ERYTHRONATE-4-PHOSPHATE DEHYDROGENASE;                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.1.1.290;                                                       
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 287;                                                 
SOURCE   4 STRAIN: PAO1;                                                        
SOURCE   5 GENE: PA1375, PDXB;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: C41(DE3);                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLAMID;                               
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET21A(+)                                 
KEYWDS    ERYTHRONATE-4-PHSPHATE, DEHYDROGENASE, NAD, TARTRATE, PHOSPHATE ION,  
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.Y.HA,J.H.LEE,K.H.KIM,D.J.KIM,H.H.LEE,H.K.KIM,H.J.YOON,S.W.SUH       
REVDAT   4   18-OCT-17 2O4C    1       REMARK                                   
REVDAT   3   13-JUL-11 2O4C    1       VERSN                                    
REVDAT   2   24-FEB-09 2O4C    1       VERSN                                    
REVDAT   1   20-FEB-07 2O4C    0                                                
JRNL        AUTH   J.Y.HA,J.H.LEE,K.H.KIM,D.J.KIM,H.H.LEE,H.K.KIM,H.J.YOON,     
JRNL        AUTH 2 S.W.SUH                                                      
JRNL        TITL   CRYSTAL STRUCTURE OF D-ERYTHRONATE-4-PHOSPHATE DEHYDROGENASE 
JRNL        TITL 2 COMPLEXED WITH NAD                                           
JRNL        REF    J.MOL.BIOL.                   V. 366  1294 2007              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   17217963                                                     
JRNL        DOI    10.1016/J.JMB.2006.12.038                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.77                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 55468                          
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 + TEST SET) : 0.229                           
REMARK   3   R VALUE            (WORKING SET) : 0.225                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 5563                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3627                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.98                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2910                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 374                          
REMARK   3   BIN FREE R VALUE                    : 0.3650                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5772                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 109                                     
REMARK   3   SOLVENT ATOMS            : 167                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.48                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.260         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.215         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.155         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.335         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.940                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.919                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5996 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8181 ; 1.173 ; 1.992       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   758 ; 5.229 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   268 ;33.975 ;22.090       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   914 ;15.720 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    78 ;18.437 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   934 ; 0.070 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4610 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2742 ; 0.190 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4032 ; 0.297 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   322 ; 0.137 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    44 ; 0.170 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    12 ; 0.112 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3863 ; 0.589 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6000 ; 0.990 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2418 ; 1.283 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2181 ; 2.073 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2O4C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-DEC-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000040670.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-JUN-04; 25-JUN-04               
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY; PHOTON FACTORY     
REMARK 200  BEAMLINE                       : AR-NW12A; AR-NW12A                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97930, 0.97946, 0.95000;         
REMARK 200                                   1.00000                            
REMARK 200  MONOCHROMATOR                  : SI(111) DOUBLE CRYSTAL             
REMARK 200                                   MONOCHROMATOR; SI(111) DOUBLE      
REMARK 200                                   CRYSTAL MONOCHROMATOR              
REMARK 200  OPTICS                         : MIRRORS; MIRRORS                   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210; ADSC QUANTUM     
REMARK 200                                   210                                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63477                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.04900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD; SINGLE WAVELENGTH                         
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE 2.03, RESOLVE 2.03                              
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.76                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.7M AMMONIUM DIHYDROGEN PHOSPHATE,      
REMARK 280  0.4M AMMONIUM TARTRATE, 0.1M SODIUM CITRATE (PH 5.6), 10MM          
REMARK 280  CUPRIC CHLORIDE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 297K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       42.45700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       71.49700            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       50.81500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       71.49700            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       42.45700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       50.81500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5480 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31160 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 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 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    VAL A  49       66.38   -103.37                                   
REMARK 500    THR A  66     -155.91   -163.85                                   
REMARK 500    ALA A  87       64.40     39.92                                   
REMARK 500    ASP A 146       81.62   -160.37                                   
REMARK 500    HIS A 174       38.34   -140.64                                   
REMARK 500    SER A 207      -95.29    -89.71                                   
REMARK 500    TYR A 258       34.67    -95.51                                   
REMARK 500    ARG B  44     -164.11   -112.80                                   
REMARK 500    SER B  86       77.89   -109.47                                   
REMARK 500    ASP B 146       84.15   -159.10                                   
REMARK 500    HIS B 174       42.05   -142.68                                   
REMARK 500    ASP B 180     -153.85   -121.92                                   
REMARK 500    SER B 207      -97.84    -91.57                                   
REMARK 500    ALA B 210        7.42    -67.13                                   
REMARK 500    GLN B 239       79.03   -105.58                                   
REMARK 500    TYR B 258       31.86    -77.16                                   
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 PO4 A 900                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TLA B 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 2647                
DBREF  2O4C A    1   380  UNP    Q9I3W9   PDXB_PSEAE       1    380             
DBREF  2O4C B    1   380  UNP    Q9I3W9   PDXB_PSEAE       1    380             
SEQRES   1 A  380  MET ARG ILE LEU ALA ASP GLU ASN ILE PRO VAL VAL ASP          
SEQRES   2 A  380  ALA PHE PHE ALA ASP GLN GLY SER ILE ARG ARG LEU PRO          
SEQRES   3 A  380  GLY ARG ALA ILE ASP ARG ALA ALA LEU ALA GLU VAL ASP          
SEQRES   4 A  380  VAL LEU LEU VAL ARG SER VAL THR GLU VAL SER ARG ALA          
SEQRES   5 A  380  ALA LEU ALA GLY SER PRO VAL ARG PHE VAL GLY THR CYS          
SEQRES   6 A  380  THR ILE GLY THR ASP HIS LEU ASP LEU ASP TYR PHE ALA          
SEQRES   7 A  380  GLU ALA GLY ILE ALA TRP SER SER ALA PRO GLY CYS ASN          
SEQRES   8 A  380  ALA ARG GLY VAL VAL ASP TYR VAL LEU GLY CYS LEU LEU          
SEQRES   9 A  380  ALA MET ALA GLU VAL ARG GLY ALA ASP LEU ALA GLU ARG          
SEQRES  10 A  380  THR TYR GLY VAL VAL GLY ALA GLY GLN VAL GLY GLY ARG          
SEQRES  11 A  380  LEU VAL GLU VAL LEU ARG GLY LEU GLY TRP LYS VAL LEU          
SEQRES  12 A  380  VAL CYS ASP PRO PRO ARG GLN ALA ARG GLU PRO ASP GLY          
SEQRES  13 A  380  GLU PHE VAL SER LEU GLU ARG LEU LEU ALA GLU ALA ASP          
SEQRES  14 A  380  VAL ILE SER LEU HIS THR PRO LEU ASN ARG ASP GLY GLU          
SEQRES  15 A  380  HIS PRO THR ARG HIS LEU LEU ASP GLU PRO ARG LEU ALA          
SEQRES  16 A  380  ALA LEU ARG PRO GLY THR TRP LEU VAL ASN ALA SER ARG          
SEQRES  17 A  380  GLY ALA VAL VAL ASP ASN GLN ALA LEU ARG ARG LEU LEU          
SEQRES  18 A  380  GLU GLY GLY ALA ASP LEU GLU VAL ALA LEU ASP VAL TRP          
SEQRES  19 A  380  GLU GLY GLU PRO GLN ALA ASP PRO GLU LEU ALA ALA ARG          
SEQRES  20 A  380  CYS LEU ILE ALA THR PRO HIS ILE ALA GLY TYR SER LEU          
SEQRES  21 A  380  GLU GLY LYS LEU ARG GLY THR ALA GLN ILE TYR GLN ALA          
SEQRES  22 A  380  TYR CYS ALA TRP ARG GLY ILE ALA GLU ARG VAL SER LEU          
SEQRES  23 A  380  GLN ASP VAL LEU PRO GLU THR TRP LEU ALA GLY LEU GLN          
SEQRES  24 A  380  LEU ASN PRO GLY CYS ASP PRO ALA TRP ALA LEU ALA THR          
SEQRES  25 A  380  LEU CYS ARG ALA VAL TYR ASP PRO ARG SER ASP ASP ALA          
SEQRES  26 A  380  ALA PHE ARG ARG SER LEU THR GLY ASP SER ALA THR ARG          
SEQRES  27 A  380  ARG ALA ALA PHE ASP ALA LEU ARG LYS HIS TYR PRO PRO          
SEQRES  28 A  380  ARG ARG GLU ILE THR GLY LEU ARG VAL ALA THR GLY GLY          
SEQRES  29 A  380  GLN ALA GLU LEU GLN ARG VAL VAL ARG ALA LEU GLY ALA          
SEQRES  30 A  380  GLN LEU VAL                                                  
SEQRES   1 B  380  MET ARG ILE LEU ALA ASP GLU ASN ILE PRO VAL VAL ASP          
SEQRES   2 B  380  ALA PHE PHE ALA ASP GLN GLY SER ILE ARG ARG LEU PRO          
SEQRES   3 B  380  GLY ARG ALA ILE ASP ARG ALA ALA LEU ALA GLU VAL ASP          
SEQRES   4 B  380  VAL LEU LEU VAL ARG SER VAL THR GLU VAL SER ARG ALA          
SEQRES   5 B  380  ALA LEU ALA GLY SER PRO VAL ARG PHE VAL GLY THR CYS          
SEQRES   6 B  380  THR ILE GLY THR ASP HIS LEU ASP LEU ASP TYR PHE ALA          
SEQRES   7 B  380  GLU ALA GLY ILE ALA TRP SER SER ALA PRO GLY CYS ASN          
SEQRES   8 B  380  ALA ARG GLY VAL VAL ASP TYR VAL LEU GLY CYS LEU LEU          
SEQRES   9 B  380  ALA MET ALA GLU VAL ARG GLY ALA ASP LEU ALA GLU ARG          
SEQRES  10 B  380  THR TYR GLY VAL VAL GLY ALA GLY GLN VAL GLY GLY ARG          
SEQRES  11 B  380  LEU VAL GLU VAL LEU ARG GLY LEU GLY TRP LYS VAL LEU          
SEQRES  12 B  380  VAL CYS ASP PRO PRO ARG GLN ALA ARG GLU PRO ASP GLY          
SEQRES  13 B  380  GLU PHE VAL SER LEU GLU ARG LEU LEU ALA GLU ALA ASP          
SEQRES  14 B  380  VAL ILE SER LEU HIS THR PRO LEU ASN ARG ASP GLY GLU          
SEQRES  15 B  380  HIS PRO THR ARG HIS LEU LEU ASP GLU PRO ARG LEU ALA          
SEQRES  16 B  380  ALA LEU ARG PRO GLY THR TRP LEU VAL ASN ALA SER ARG          
SEQRES  17 B  380  GLY ALA VAL VAL ASP ASN GLN ALA LEU ARG ARG LEU LEU          
SEQRES  18 B  380  GLU GLY GLY ALA ASP LEU GLU VAL ALA LEU ASP VAL TRP          
SEQRES  19 B  380  GLU GLY GLU PRO GLN ALA ASP PRO GLU LEU ALA ALA ARG          
SEQRES  20 B  380  CYS LEU ILE ALA THR PRO HIS ILE ALA GLY TYR SER LEU          
SEQRES  21 B  380  GLU GLY LYS LEU ARG GLY THR ALA GLN ILE TYR GLN ALA          
SEQRES  22 B  380  TYR CYS ALA TRP ARG GLY ILE ALA GLU ARG VAL SER LEU          
SEQRES  23 B  380  GLN ASP VAL LEU PRO GLU THR TRP LEU ALA GLY LEU GLN          
SEQRES  24 B  380  LEU ASN PRO GLY CYS ASP PRO ALA TRP ALA LEU ALA THR          
SEQRES  25 B  380  LEU CYS ARG ALA VAL TYR ASP PRO ARG SER ASP ASP ALA          
SEQRES  26 B  380  ALA PHE ARG ARG SER LEU THR GLY ASP SER ALA THR ARG          
SEQRES  27 B  380  ARG ALA ALA PHE ASP ALA LEU ARG LYS HIS TYR PRO PRO          
SEQRES  28 B  380  ARG ARG GLU ILE THR GLY LEU ARG VAL ALA THR GLY GLY          
SEQRES  29 B  380  GLN ALA GLU LEU GLN ARG VAL VAL ARG ALA LEU GLY ALA          
SEQRES  30 B  380  GLN LEU VAL                                                  
HET    PO4  A 900       5                                                       
HET    NAD  A1002      44                                                       
HET    NAD  B1001      44                                                       
HET    TLA  B 500      10                                                       
HET    GOL  B2647       6                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
HETNAM     TLA L(+)-TARTARIC ACID                                               
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  PO4    O4 P 3-                                                      
FORMUL   4  NAD    2(C21 H27 N7 O14 P2)                                         
FORMUL   6  TLA    C4 H6 O6                                                     
FORMUL   7  GOL    C3 H8 O3                                                     
FORMUL   8  HOH   *167(H2 O)                                                    
HELIX    1   1 VAL A   11  ALA A   17  1                                   7    
HELIX    2   2 ASP A   18  GLY A   20  5                                   3    
HELIX    3   3 PRO A   26  ILE A   30  5                                   5    
HELIX    4   4 SER A   50  ALA A   55  1                                   6    
HELIX    5   5 ASP A   73  GLY A   81  1                                   9    
HELIX    6   6 ASN A   91  GLY A  111  1                                  21    
HELIX    7   7 ASP A  113  GLU A  116  5                                   4    
HELIX    8   8 GLY A  125  LEU A  138  1                                  14    
HELIX    9   9 ASP A  146  GLU A  153  1                                   8    
HELIX   10  10 SER A  160  ALA A  168  1                                   9    
HELIX   11  11 ASP A  190  ALA A  196  1                                   7    
HELIX   12  12 ARG A  208  VAL A  212  5                                   5    
HELIX   13  13 ASP A  213  GLY A  223  1                                  11    
HELIX   14  14 ASP A  241  ALA A  246  1                                   6    
HELIX   15  15 SER A  259  GLY A  279  1                                  21    
HELIX   16  16 SER A  285  VAL A  289  5                                   5    
HELIX   17  17 ASP A  305  TYR A  318  1                                  14    
HELIX   18  18 PRO A  320  SER A  330  1                                  11    
HELIX   19  19 ASP A  334  HIS A  348  1                                  15    
HELIX   20  20 GLU A  354  GLY A  357  5                                   4    
HELIX   21  21 GLN A  365  GLY A  376  1                                  12    
HELIX   22  22 VAL B   11  ALA B   17  1                                   7    
HELIX   23  23 ASP B   18  GLY B   20  5                                   3    
HELIX   24  24 ALA B   33  VAL B   38  5                                   6    
HELIX   25  25 SER B   50  ALA B   55  1                                   6    
HELIX   26  26 GLY B   68  LEU B   72  5                                   5    
HELIX   27  27 ASP B   73  GLY B   81  1                                   9    
HELIX   28  28 ASN B   91  GLY B  111  1                                  21    
HELIX   29  29 ASP B  113  GLU B  116  5                                   4    
HELIX   30  30 GLY B  125  LEU B  138  1                                  14    
HELIX   31  31 ASP B  146  GLU B  153  1                                   8    
HELIX   32  32 SER B  160  ALA B  168  1                                   9    
HELIX   33  33 ASP B  190  ALA B  196  1                                   7    
HELIX   34  34 ARG B  208  VAL B  212  5                                   5    
HELIX   35  35 ASP B  213  GLY B  223  1                                  11    
HELIX   36  36 ASP B  241  ALA B  246  1                                   6    
HELIX   37  37 SER B  259  GLY B  279  1                                  21    
HELIX   38  38 SER B  285  LEU B  290  1                                   6    
HELIX   39  39 ASP B  305  TYR B  318  1                                  14    
HELIX   40  40 PRO B  320  SER B  330  1                                  11    
HELIX   41  41 ASP B  334  HIS B  348  1                                  15    
HELIX   42  42 GLU B  354  GLY B  357  5                                   4    
HELIX   43  43 GLN B  365  GLY B  376  1                                  12    
SHEET    1   A 5 SER A  21  LEU A  25  0                                        
SHEET    2   A 5 ARG A   2  ASP A   6  1  N  ILE A   3   O  ARG A  23           
SHEET    3   A 5 VAL A  40  VAL A  43  1  O  LEU A  42   N  LEU A   4           
SHEET    4   A 5 PHE A  61  THR A  64  1  O  GLY A  63   N  VAL A  43           
SHEET    5   A 5 ALA A  83  SER A  85  1  O  SER A  85   N  THR A  64           
SHEET    1   B 6 LYS A 141  CYS A 145  0                                        
SHEET    2   B 6 THR A 118  VAL A 122  1  N  TYR A 119   O  LEU A 143           
SHEET    3   B 6 VAL A 170  LEU A 173  1  O  VAL A 170   N  GLY A 120           
SHEET    4   B 6 THR A 201  ASN A 205  1  O  TRP A 202   N  ILE A 171           
SHEET    5   B 6 LEU A 227  LEU A 231  1  O  GLU A 228   N  LEU A 203           
SHEET    6   B 6 ILE A 250  ALA A 251  1  O  ILE A 250   N  LEU A 231           
SHEET    1   C 6 GLN A 378  VAL A 380  0                                        
SHEET    2   C 6 ARG A 359  ALA A 361  1  N  VAL A 360   O  GLN A 378           
SHEET    3   C 6 LEU A 295  LEU A 300  1  N  LEU A 300   O  ALA A 361           
SHEET    4   C 6 LEU B 295  LEU B 300 -1  O  GLY B 297   N  GLN A 299           
SHEET    5   C 6 ARG B 359  ALA B 361  1  O  ALA B 361   N  LEU B 300           
SHEET    6   C 6 GLN B 378  LEU B 379  1  O  GLN B 378   N  VAL B 360           
SHEET    1   D 5 SER B  21  LEU B  25  0                                        
SHEET    2   D 5 ARG B   2  ASP B   6  1  N  ILE B   3   O  SER B  21           
SHEET    3   D 5 VAL B  40  LEU B  42  1  O  LEU B  42   N  LEU B   4           
SHEET    4   D 5 PHE B  61  THR B  64  1  O  PHE B  61   N  LEU B  41           
SHEET    5   D 5 ALA B  83  SER B  86  1  O  SER B  85   N  VAL B  62           
SHEET    1   E 6 LYS B 141  CYS B 145  0                                        
SHEET    2   E 6 THR B 118  VAL B 122  1  N  TYR B 119   O  LEU B 143           
SHEET    3   E 6 VAL B 170  LEU B 173  1  O  VAL B 170   N  GLY B 120           
SHEET    4   E 6 THR B 201  ASN B 205  1  O  VAL B 204   N  ILE B 171           
SHEET    5   E 6 LEU B 227  LEU B 231  1  O  ALA B 230   N  LEU B 203           
SHEET    6   E 6 ILE B 250  ALA B 251  1  O  ILE B 250   N  LEU B 231           
SSBOND   1 CYS A   65    CYS A   90                          1555   1555  2.03  
SSBOND   2 CYS B   65    CYS B   90                          1555   1555  2.05  
CISPEP   1 GLU A  237    PRO A  238          0        -0.20                     
CISPEP   2 GLU B  237    PRO B  238          0         3.65                     
SITE     1 AC1  5 ARG A  44  SER A  45  THR A  66  TYR A 258                    
SITE     2 AC1  5 ARG A 346                                                     
SITE     1 AC2 26 ASN B  91  VAL B  95  VAL B 122  GLY B 123                    
SITE     2 AC2 26 GLY B 125  GLN B 126  VAL B 127  CYS B 145                    
SITE     3 AC2 26 ASP B 146  PRO B 147  PRO B 148  HIS B 174                    
SITE     4 AC2 26 THR B 175  PRO B 176  HIS B 183  THR B 185                    
SITE     5 AC2 26 ALA B 206  SER B 207  ARG B 208  ASP B 232                    
SITE     6 AC2 26 HIS B 254  ALA B 256  GLY B 257  HOH B2652                    
SITE     7 AC2 26 HOH B2661  HOH B2702                                          
SITE     1 AC3 28 ASN A  91  VAL A  95  GLY A 123  GLY A 125                    
SITE     2 AC3 28 GLN A 126  VAL A 127  CYS A 145  ASP A 146                    
SITE     3 AC3 28 PRO A 147  PRO A 148  HIS A 174  THR A 175                    
SITE     4 AC3 28 PRO A 176  HIS A 183  THR A 185  ALA A 206                    
SITE     5 AC3 28 SER A 207  ARG A 208  ASP A 232  HIS A 254                    
SITE     6 AC3 28 ALA A 256  GLY A 257  HOH A1003  HOH A1004                    
SITE     7 AC3 28 HOH A1008  HOH A1038  HOH A1060  HOH A1084                    
SITE     1 AC4  4 ARG B 208  HIS B 254  TYR B 258  ARG B 346                    
SITE     1 AC5  4 LEU B 138  TRP B 140  ALA B 307  HOH B2676                    
CRYST1   84.914  101.630  142.994  90.00  90.00  90.00 P 21 21 21    8          
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      0.011777  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009840  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006993        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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