GenomeNet

Database: PDB
Entry: 2P9G
LinkDB: 2P9G
Original site: 2P9G 
HEADER    OXIDOREDUCTASE                          25-MAR-07   2P9G              
TITLE     CRYSTAL STRUCTURE OF SERINE BOUND G336V,G337V DOUBLE MUTANT OF E.COLI 
TITLE    2 PHOSPHOGLYCERATE DEHYDROGENASE                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-3-PHOSPHOGLYCERATE DEHYDROGENASE;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PGDH;                                                       
COMPND   5 EC: 1.1.1.95;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: SERA;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;                                  
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PTRC99                                    
KEYWDS    OXIDOREDUCTASE, SERINE BIOSYNTHESIS, D-3-PHOSPHOGLYCERATE             
KEYWDS   2 DEHYDROGENASE, DOUBLE MUTATION                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.DEY,J.C.SACCHETTINI                                                 
REVDAT   4   13-JUL-11 2P9G    1       VERSN                                    
REVDAT   3   24-FEB-09 2P9G    1       VERSN                                    
REVDAT   2   17-JUL-07 2P9G    1       JRNL                                     
REVDAT   1   24-APR-07 2P9G    0                                                
JRNL        AUTH   S.DEY,Z.HU,X.L.XU,J.C.SACCHETTINI,G.A.GRANT                  
JRNL        TITL   THE EFFECT OF HINGE MUTATIONS ON EFFECTOR BINDING AND DOMAIN 
JRNL        TITL 2 ROTATION IN ESCHERICHIA COLI D-3-PHOSPHOGLYCERATE            
JRNL        TITL 3 DEHYDROGENASE.                                               
JRNL        REF    J.BIOL.CHEM.                  V. 282 18418 2007              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   17459882                                                     
JRNL        DOI    10.1074/JBC.M701174200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 23997                          
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) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1285                            
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) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1732                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2940                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 107                          
REMARK   3   BIN FREE R VALUE                    : 0.3680                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6130                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 102                                     
REMARK   3   SOLVENT ATOMS            : 49                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.72                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.14000                                             
REMARK   3    B22 (A**2) : -3.00000                                             
REMARK   3    B33 (A**2) : 6.14000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.366         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.269         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.366        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.936                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.911                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6344 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8618 ; 1.869 ; 1.990       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   806 ; 6.421 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   262 ;36.971 ;24.962       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1072 ;18.899 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    30 ;23.879 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1008 ; 0.112 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4710 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2887 ; 0.274 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4346 ; 0.344 ; 0.500       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   406 ; 0.216 ; 0.500       
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):   126 ; 0.187 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    24 ; 0.261 ; 0.500       
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):  4096 ; 4.074 ; 5.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6440 ; 6.244 ; 7.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2434 ; 8.101 ; 9.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED 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   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2P9G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-APR-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB042133.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-MAY-06                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 4.5                                
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          : OTHER                              
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.541                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MONOCHROMATOR                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25289                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.320                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.05200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.20700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1PSD                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 400, 0.1M ACETATE, 0.2M          
REMARK 280  CALCIUM ACETATE, PH 4.5, VAPOR DIFFUSION, HANGING DROP,             
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
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   -X+1/2,Y+1/2,-Z                                         
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        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 -1.000000  0.000000  0.000000       72.03600            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       66.11950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       72.03600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       66.11950            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 19500 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 62520 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.0 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 350   BIOMT1   2 -1.000000  0.000000  0.000000      144.07200            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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     ALA A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     LYS B     3                                                      
REMARK 465     VAL B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     LEU B     6                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLY A 377   N     GLY A 377   CA      0.090                       
REMARK 500    LYS B 218   CD    LYS B 218   CE      0.179                       
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    TYR A 378   CG  -  CD2 -  CE2 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500    TYR A 378   CZ  -  CE2 -  CD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ARG B 338   CB  -  CA  -  C   ANGL. DEV. = -14.5 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    GLU A  17       10.95     59.25                                   
REMARK 500    ASP A  44        1.10    -44.33                                   
REMARK 500    GLU A  45      -38.28   -151.97                                   
REMARK 500    LEU A  47      -74.62    -42.02                                   
REMARK 500    ARG A  60     -144.83   -123.19                                   
REMARK 500    TYR A 159       52.83   -100.67                                   
REMARK 500    ASN A 214      164.75    172.09                                   
REMARK 500    SER A 239      -95.07    -90.84                                   
REMARK 500    ASN A 286       30.44    -94.13                                   
REMARK 500    SER A 296       73.31   -102.64                                   
REMARK 500    SER A 323       -4.31     88.50                                   
REMARK 500    HIS A 335       22.89   -149.84                                   
REMARK 500    VAL A 336      131.70    167.91                                   
REMARK 500    ARG A 338      113.51     79.00                                   
REMARK 500    GLU A 360       10.43    -65.11                                   
REMARK 500    GLN A 361       24.40   -146.18                                   
REMARK 500    LYS B   8      100.30     10.43                                   
REMARK 500    ASP B   9       42.28    -56.95                                   
REMARK 500    ARG B  60     -135.72   -119.17                                   
REMARK 500    ALA B  83      145.96    174.62                                   
REMARK 500    ASN B 108       49.58   -140.67                                   
REMARK 500    SER B 172       12.51    -65.69                                   
REMARK 500    PRO B 215      -38.23    -31.95                                   
REMARK 500    SER B 233     -169.92    -72.17                                   
REMARK 500    SER B 239      -77.40    -99.31                                   
REMARK 500    ASP B 245       97.23    -62.81                                   
REMARK 500    LYS B 256       16.13     56.96                                   
REMARK 500    HIS B 292       65.77     63.57                                   
REMARK 500    SER B 323        5.29     82.63                                   
REMARK 500    HIS B 335      -62.35   -128.81                                   
REMARK 500    VAL B 337      118.92    -13.07                                   
REMARK 500    GLU B 360        1.88    -64.48                                   
REMARK 500    ALA B 374      -87.45     -2.57                                   
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 NAI A 450                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI B 550                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SER A 451                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SER A 551                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2P9C   RELATED DB: PDB                                   
REMARK 900 SERINE BOUND G336V SINGLE MUTANT OF D-3- PHOSPHOGLYCERATE            
REMARK 900 DEHYDROGENASE                                                        
REMARK 900 RELATED ID: 2P9E   RELATED DB: PDB                                   
REMARK 900 G336V MUTANT OF D-3-PHOSPHOGLYCERATE DEHYDROGENASE                   
REMARK 900 RELATED ID: 1YBA   RELATED DB: PDB                                   
REMARK 900 D-3 PHOSPHOGLYCERATE DEHYDROGENASE                                   
REMARK 900 RELATED ID: 1PSD   RELATED DB: PDB                                   
REMARK 900 SERINE BOUND D-3 PHOSPHOGLYCERATE DEHYDROGENASE                      
DBREF  2P9G A    1   410  UNP    P0A9T0   SERA_ECOLI       1    410             
DBREF  2P9G B    1   410  UNP    P0A9T0   SERA_ECOLI       1    410             
SEQADV 2P9G ALA A   81  UNP  P0A9T0    CYS    81 ENGINEERED                     
SEQADV 2P9G ALA A   83  UNP  P0A9T0    CYS    83 ENGINEERED                     
SEQADV 2P9G ALA A  250  UNP  P0A9T0    CYS   250 ENGINEERED                     
SEQADV 2P9G ALA A  282  UNP  P0A9T0    CYS   282 ENGINEERED                     
SEQADV 2P9G VAL A  336  UNP  P0A9T0    GLY   336 ENGINEERED                     
SEQADV 2P9G VAL A  337  UNP  P0A9T0    GLY   337 ENGINEERED                     
SEQADV 2P9G ALA B   81  UNP  P0A9T0    CYS    81 ENGINEERED                     
SEQADV 2P9G ALA B   83  UNP  P0A9T0    CYS    83 ENGINEERED                     
SEQADV 2P9G ALA B  250  UNP  P0A9T0    CYS   250 ENGINEERED                     
SEQADV 2P9G ALA B  282  UNP  P0A9T0    CYS   282 ENGINEERED                     
SEQADV 2P9G VAL B  336  UNP  P0A9T0    GLY   336 ENGINEERED                     
SEQADV 2P9G VAL B  337  UNP  P0A9T0    GLY   337 ENGINEERED                     
SEQRES   1 A  410  MET ALA LYS VAL SER LEU GLU LYS ASP LYS ILE LYS PHE          
SEQRES   2 A  410  LEU LEU VAL GLU GLY VAL HIS GLN LYS ALA LEU GLU SER          
SEQRES   3 A  410  LEU ARG ALA ALA GLY TYR THR ASN ILE GLU PHE HIS LYS          
SEQRES   4 A  410  GLY ALA LEU ASP ASP GLU GLN LEU LYS GLU SER ILE ARG          
SEQRES   5 A  410  ASP ALA HIS PHE ILE GLY LEU ARG SER ARG THR HIS LEU          
SEQRES   6 A  410  THR GLU ASP VAL ILE ASN ALA ALA GLU LYS LEU VAL ALA          
SEQRES   7 A  410  ILE GLY ALA PHE ALA ILE GLY THR ASN GLN VAL ASP LEU          
SEQRES   8 A  410  ASP ALA ALA ALA LYS ARG GLY ILE PRO VAL PHE ASN ALA          
SEQRES   9 A  410  PRO PHE SER ASN THR ARG SER VAL ALA GLU LEU VAL ILE          
SEQRES  10 A  410  GLY GLU LEU LEU LEU LEU LEU ARG GLY VAL PRO GLU ALA          
SEQRES  11 A  410  ASN ALA LYS ALA HIS ARG GLY VAL TRP ASN LYS LEU ALA          
SEQRES  12 A  410  ALA GLY SER PHE GLU ALA ARG GLY LYS LYS LEU GLY ILE          
SEQRES  13 A  410  ILE GLY TYR GLY HIS ILE GLY THR GLN LEU GLY ILE LEU          
SEQRES  14 A  410  ALA GLU SER LEU GLY MET TYR VAL TYR PHE TYR ASP ILE          
SEQRES  15 A  410  GLU ASN LYS LEU PRO LEU GLY ASN ALA THR GLN VAL GLN          
SEQRES  16 A  410  HIS LEU SER ASP LEU LEU ASN MET SER ASP VAL VAL SER          
SEQRES  17 A  410  LEU HIS VAL PRO GLU ASN PRO SER THR LYS ASN MET MET          
SEQRES  18 A  410  GLY ALA LYS GLU ILE SER LEU MET LYS PRO GLY SER LEU          
SEQRES  19 A  410  LEU ILE ASN ALA SER ARG GLY THR VAL VAL ASP ILE PRO          
SEQRES  20 A  410  ALA LEU ALA ASP ALA LEU ALA SER LYS HIS LEU ALA GLY          
SEQRES  21 A  410  ALA ALA ILE ASP VAL PHE PRO THR GLU PRO ALA THR ASN          
SEQRES  22 A  410  SER ASP PRO PHE THR SER PRO LEU ALA GLU PHE ASP ASN          
SEQRES  23 A  410  VAL LEU LEU THR PRO HIS ILE GLY GLY SER THR GLN GLU          
SEQRES  24 A  410  ALA GLN GLU ASN ILE GLY LEU GLU VAL ALA GLY LYS LEU          
SEQRES  25 A  410  ILE LYS TYR SER ASP ASN GLY SER THR LEU SER ALA VAL          
SEQRES  26 A  410  ASN PHE PRO GLU VAL SER LEU PRO LEU HIS VAL VAL ARG          
SEQRES  27 A  410  ARG LEU MET HIS ILE HIS GLU ASN ARG PRO GLY VAL LEU          
SEQRES  28 A  410  THR ALA LEU ASN LYS ILE PHE ALA GLU GLN GLY VAL ASN          
SEQRES  29 A  410  ILE ALA ALA GLN TYR LEU GLN THR SER ALA GLN MET GLY          
SEQRES  30 A  410  TYR VAL VAL ILE ASP ILE GLU ALA ASP GLU ASP VAL ALA          
SEQRES  31 A  410  GLU LYS ALA LEU GLN ALA MET LYS ALA ILE PRO GLY THR          
SEQRES  32 A  410  ILE ARG ALA ARG LEU LEU TYR                                  
SEQRES   1 B  410  MET ALA LYS VAL SER LEU GLU LYS ASP LYS ILE LYS PHE          
SEQRES   2 B  410  LEU LEU VAL GLU GLY VAL HIS GLN LYS ALA LEU GLU SER          
SEQRES   3 B  410  LEU ARG ALA ALA GLY TYR THR ASN ILE GLU PHE HIS LYS          
SEQRES   4 B  410  GLY ALA LEU ASP ASP GLU GLN LEU LYS GLU SER ILE ARG          
SEQRES   5 B  410  ASP ALA HIS PHE ILE GLY LEU ARG SER ARG THR HIS LEU          
SEQRES   6 B  410  THR GLU ASP VAL ILE ASN ALA ALA GLU LYS LEU VAL ALA          
SEQRES   7 B  410  ILE GLY ALA PHE ALA ILE GLY THR ASN GLN VAL ASP LEU          
SEQRES   8 B  410  ASP ALA ALA ALA LYS ARG GLY ILE PRO VAL PHE ASN ALA          
SEQRES   9 B  410  PRO PHE SER ASN THR ARG SER VAL ALA GLU LEU VAL ILE          
SEQRES  10 B  410  GLY GLU LEU LEU LEU LEU LEU ARG GLY VAL PRO GLU ALA          
SEQRES  11 B  410  ASN ALA LYS ALA HIS ARG GLY VAL TRP ASN LYS LEU ALA          
SEQRES  12 B  410  ALA GLY SER PHE GLU ALA ARG GLY LYS LYS LEU GLY ILE          
SEQRES  13 B  410  ILE GLY TYR GLY HIS ILE GLY THR GLN LEU GLY ILE LEU          
SEQRES  14 B  410  ALA GLU SER LEU GLY MET TYR VAL TYR PHE TYR ASP ILE          
SEQRES  15 B  410  GLU ASN LYS LEU PRO LEU GLY ASN ALA THR GLN VAL GLN          
SEQRES  16 B  410  HIS LEU SER ASP LEU LEU ASN MET SER ASP VAL VAL SER          
SEQRES  17 B  410  LEU HIS VAL PRO GLU ASN PRO SER THR LYS ASN MET MET          
SEQRES  18 B  410  GLY ALA LYS GLU ILE SER LEU MET LYS PRO GLY SER LEU          
SEQRES  19 B  410  LEU ILE ASN ALA SER ARG GLY THR VAL VAL ASP ILE PRO          
SEQRES  20 B  410  ALA LEU ALA ASP ALA LEU ALA SER LYS HIS LEU ALA GLY          
SEQRES  21 B  410  ALA ALA ILE ASP VAL PHE PRO THR GLU PRO ALA THR ASN          
SEQRES  22 B  410  SER ASP PRO PHE THR SER PRO LEU ALA GLU PHE ASP ASN          
SEQRES  23 B  410  VAL LEU LEU THR PRO HIS ILE GLY GLY SER THR GLN GLU          
SEQRES  24 B  410  ALA GLN GLU ASN ILE GLY LEU GLU VAL ALA GLY LYS LEU          
SEQRES  25 B  410  ILE LYS TYR SER ASP ASN GLY SER THR LEU SER ALA VAL          
SEQRES  26 B  410  ASN PHE PRO GLU VAL SER LEU PRO LEU HIS VAL VAL ARG          
SEQRES  27 B  410  ARG LEU MET HIS ILE HIS GLU ASN ARG PRO GLY VAL LEU          
SEQRES  28 B  410  THR ALA LEU ASN LYS ILE PHE ALA GLU GLN GLY VAL ASN          
SEQRES  29 B  410  ILE ALA ALA GLN TYR LEU GLN THR SER ALA GLN MET GLY          
SEQRES  30 B  410  TYR VAL VAL ILE ASP ILE GLU ALA ASP GLU ASP VAL ALA          
SEQRES  31 B  410  GLU LYS ALA LEU GLN ALA MET LYS ALA ILE PRO GLY THR          
SEQRES  32 B  410  ILE ARG ALA ARG LEU LEU TYR                                  
HET    NAI  A 450      44                                                       
HET    NAI  B 550      44                                                       
HET    SER  A 451       7                                                       
HET    SER  A 551       7                                                       
HETNAM     NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE                     
HETNAM     SER SERINE                                                           
HETSYN     NAI NADH                                                             
FORMUL   3  NAI    2(C21 H29 N7 O14 P2)                                         
FORMUL   5  SER    2(C3 H7 N O3)                                                
FORMUL   6  HOH   *49(H2 O)                                                     
HELIX    1   1 GLU A    7  LYS A   10  5                                   4    
HELIX    2   2 HIS A   20  ALA A   29  1                                  10    
HELIX    3   3 GLU A   45  ARG A   52  1                                   8    
HELIX    4   4 THR A   66  ALA A   73  1                                   8    
HELIX    5   5 ASP A   90  ARG A   97  1                                   8    
HELIX    6   6 ASN A  108  GLY A  126  1                                  19    
HELIX    7   7 GLY A  126  HIS A  135  1                                  10    
HELIX    8   8 GLY A  160  LEU A  173  1                                  14    
HELIX    9   9 HIS A  196  SER A  204  1                                   9    
HELIX   10  10 GLY A  222  MET A  229  1                                   8    
HELIX   11  11 ASP A  245  SER A  255  1                                  11    
HELIX   12  12 SER A  279  PHE A  284  5                                   6    
HELIX   13  13 THR A  297  GLY A  319  1                                  23    
HELIX   14  14 GLY A  349  GLU A  360  1                                  12    
HELIX   15  15 ASP A  386  ALA A  399  1                                  14    
HELIX   16  16 HIS B   20  ALA B   29  1                                  10    
HELIX   17  17 ASP B   43  ARG B   52  1                                  10    
HELIX   18  18 THR B   66  ASN B   71  1                                   6    
HELIX   19  19 ASP B   90  ARG B   97  1                                   8    
HELIX   20  20 ASN B  108  ARG B  125  1                                  18    
HELIX   21  21 GLY B  126  HIS B  135  1                                  10    
HELIX   22  22 GLY B  160  SER B  172  1                                  13    
HELIX   23  23 HIS B  196  SER B  204  1                                   9    
HELIX   24  24 GLY B  222  LEU B  228  1                                   7    
HELIX   25  25 ARG B  240  VAL B  244  5                                   5    
HELIX   26  26 ASP B  245  SER B  255  1                                  11    
HELIX   27  27 SER B  279  PHE B  284  5                                   6    
HELIX   28  28 THR B  297  ASN B  318  1                                  22    
HELIX   29  29 GLY B  349  GLU B  360  1                                  12    
HELIX   30  30 ASP B  386  ALA B  399  1                                  14    
SHEET    1   A 5 ASN A  34  PHE A  37  0                                        
SHEET    2   A 5 LYS A  12  LEU A  15  1  N  LEU A  15   O  GLU A  36           
SHEET    3   A 5 PHE A  56  LEU A  59  1  O  GLY A  58   N  LEU A  14           
SHEET    4   A 5 ALA A  78  ALA A  81  1  O  GLY A  80   N  ILE A  57           
SHEET    5   A 5 VAL A 101  PHE A 102  1  O  PHE A 102   N  ALA A  81           
SHEET    1   B 6 TYR A 176  TYR A 180  0                                        
SHEET    2   B 6 LYS A 153  ILE A 157  1  N  ILE A 156   O  TYR A 178           
SHEET    3   B 6 VAL A 206  LEU A 209  1  O  VAL A 206   N  GLY A 155           
SHEET    4   B 6 SER A 233  ASN A 237  1  O  ILE A 236   N  VAL A 207           
SHEET    5   B 6 LEU A 258  ILE A 263  1  O  ALA A 259   N  SER A 233           
SHEET    6   B 6 VAL A 287  LEU A 289  1  O  LEU A 288   N  ALA A 261           
SHEET    1   C 8 THR A 403  TYR A 410  0                                        
SHEET    2   C 8 ARG A 339  GLU A 345 -1  N  ILE A 343   O  ILE A 404           
SHEET    3   C 8 MET A 376  GLU A 384 -1  O  ILE A 381   N  LEU A 340           
SHEET    4   C 8 ASN A 364  THR A 372 -1  N  ALA A 367   O  ASP A 382           
SHEET    5   C 8 ASN B 364  SER B 373 -1  O  GLN B 368   N  LEU A 370           
SHEET    6   C 8 MET B 376  GLU B 384 -1  O  MET B 376   N  SER B 373           
SHEET    7   C 8 ARG B 339  GLU B 345 -1  N  LEU B 340   O  ILE B 381           
SHEET    8   C 8 THR B 403  TYR B 410 -1  O  ARG B 405   N  ILE B 343           
SHEET    1   D 5 ILE B  35  PHE B  37  0                                        
SHEET    2   D 5 PHE B  13  LEU B  15  1  N  LEU B  15   O  GLU B  36           
SHEET    3   D 5 PHE B  56  LEU B  59  1  O  GLY B  58   N  LEU B  14           
SHEET    4   D 5 ALA B  78  ALA B  81  1  O  GLY B  80   N  ILE B  57           
SHEET    5   D 5 VAL B 101  PHE B 102  1  O  PHE B 102   N  ALA B  81           
SHEET    1   E 7 THR B 192  GLN B 193  0                                        
SHEET    2   E 7 TYR B 176  TYR B 180  1  N  PHE B 179   O  THR B 192           
SHEET    3   E 7 LYS B 153  ILE B 157  1  N  ILE B 156   O  TYR B 178           
SHEET    4   E 7 VAL B 206  LEU B 209  1  O  VAL B 206   N  GLY B 155           
SHEET    5   E 7 LEU B 234  ASN B 237  1  O  ILE B 236   N  VAL B 207           
SHEET    6   E 7 GLY B 260  ILE B 263  1  O  ALA B 262   N  ASN B 237           
SHEET    7   E 7 VAL B 287  LEU B 289  1  O  LEU B 288   N  ALA B 261           
CISPEP   1 VAL B  337    ARG B  338          0         8.44                     
SITE     1 AC1 21 ILE A  84  PHE A 106  TYR A 159  GLY A 160                    
SITE     2 AC1 21 HIS A 161  ILE A 162  TYR A 180  ASP A 181                    
SITE     3 AC1 21 ILE A 182  LYS A 185  HIS A 210  VAL A 211                    
SITE     4 AC1 21 PRO A 212  SER A 216  ALA A 238  SER A 239                    
SITE     5 AC1 21 ARG A 240  ASP A 264  HIS A 292  GLY A 294                    
SITE     6 AC1 21 GLY A 295                                                     
SITE     1 AC2 20 PHE B 106  ASN B 108  GLY B 160  HIS B 161                    
SITE     2 AC2 20 ILE B 162  ASP B 181  ILE B 182  LYS B 185                    
SITE     3 AC2 20 HIS B 210  VAL B 211  PRO B 212  SER B 216                    
SITE     4 AC2 20 THR B 217  MET B 220  ALA B 238  SER B 239                    
SITE     5 AC2 20 ARG B 240  ASP B 264  HIS B 292  GLY B 295                    
SITE     1 AC3 10 HIS A 344  ASN A 346  ARG A 347  GLY A 349                    
SITE     2 AC3 10 VAL A 350  LEU A 351  LEU A 370  HOH A 546                    
SITE     3 AC3 10 ASN B 364  ILE B 365                                          
SITE     1 AC4 11 ASN A 364  ILE A 365  HOH A 517  HIS B 344                    
SITE     2 AC4 11 ASN B 346  ARG B 347  PRO B 348  GLY B 349                    
SITE     3 AC4 11 VAL B 350  LEU B 370  THR B 372                               
CRYST1  144.072  132.239   52.370  90.00  90.00  90.00 P 21 21 2     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      0.006941  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007562  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019095        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system