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Database: PDB
Entry: 1H94
LinkDB: 1H94
Original site: 1H94 
HEADER    OXIDOREDUCTASE                          23-FEB-01   1H94              
TITLE     COMPLEX OF ACTIVE MUTANT (S215->C) OF GLUCOSE 6-PHOSPHATE             
TITLE    2 DEHYDROGENASE FROM L.MESENTEROIDES WITH COENZYME NAD                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUCOSE 6-PHOSPHATE 1-DEHYDROGENASE;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: G6PD;                                                       
COMPND   5 EC: 1.1.1.49;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: LEUCONOSTOC MESENTEROIDES;                      
SOURCE   3 ORGANISM_TAXID: 1245;                                                
SOURCE   4 STRAIN: SU294;                                                       
SOURCE   5 GENE: G6PD;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PLMZ;                                     
SOURCE   9 EXPRESSION_SYSTEM_GENE: G6PD;                                        
SOURCE  10 OTHER_DETAILS: SITE DIRECTED MUTAGENESIS                             
KEYWDS    OXIDOREDUCTASE, GLUCOSE METABOLISM                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.J.ADAMS,C.E.NAYLOR,S.GOVER                                          
REVDAT   6   13-DEC-23 1H94    1       REMARK                                   
REVDAT   5   22-MAY-19 1H94    1       REMARK                                   
REVDAT   4   08-MAY-19 1H94    1       REMARK                                   
REVDAT   3   24-FEB-09 1H94    1       VERSN                                    
REVDAT   2   15-MAR-08 1H94    1       VERSN                                    
REVDAT   1   03-MAY-01 1H94    0                                                
JRNL        AUTH   C.E.NAYLOR,S.GOVER,A.K.BASAK,M.S.COSGROVE,H.R.LEVY,M.J.ADAMS 
JRNL        TITL   NADP+ AND NAD+ BINDING TO THE DUAL COENZYME SPECIFIC ENZYME  
JRNL        TITL 2 LEUCONOSTOC MESENTEROIDES GLUCOSE 6-PHOSPHATE DEHYDROGENASE: 
JRNL        TITL 3 DIFFERENT INTERDOMAIN HINGE ANGLES ARE SEEN IN DIFFERENT     
JRNL        TITL 4 BINARY AND TERNARY COMPLEXES                                 
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  57   635 2001              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   11320304                                                     
JRNL        DOI    10.1107/S0907444901003420                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.S.COSGROVE,S.GOVER,C.E.NAYLOR,L.VANDEPUTTE-RUTTEN,         
REMARK   1  AUTH 2 M.J.ADAMS,H.R.LEVY                                           
REMARK   1  TITL   AN EXAMINATION OF THE ROLE OF ASP-177 IN THE HIS-ASP         
REMARK   1  TITL 2 CATALYTIC DYAD OF LEUCONOSTOC MESENTEROIDES GLUCOSE          
REMARK   1  TITL 3 6-PHOSPHATE DEHYDROGENASE: X-RAY STRUCTURE AND PH DEPENDENCE 
REMARK   1  TITL 4 OF KINETIC PARAMETERS OF THE D177N MUTANT ENZYME             
REMARK   1  REF    BIOCHEMISTRY                  V.  39 15002 2000              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  PMID   11106478                                                     
REMARK   1  DOI    10.1021/BI0014608                                            
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   P.ROWLAND,A.K.BASAK,S.GOVER,H.R.LEVY,M.J.ADAMS               
REMARK   1  TITL   THE THREE-DIMENSIONAL STRUCTURE OF GLUCOSE 6-PHOSPHATE       
REMARK   1  TITL 2 DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES REFINED AT 2    
REMARK   1  TITL 3 ANGSTROMS RESOLUTION                                         
REMARK   1  REF    STRUCTURE                     V.   2  1073 1994              
REMARK   1  REFN                   ISSN 0969-2126                               
REMARK   1  PMID   7881907                                                      
REMARK   1  DOI    10.1016/S0969-2126(94)00110-3                                
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   M.J.ADAMS,A.K.BASAK,S.GOVER,P.ROWLAND,H.R.LEVY               
REMARK   1  TITL   SITE-DIRECTED MUTAGENESIS TO FACILITATE X-RAY STRUCTURAL     
REMARK   1  TITL 2 STUDIES OF LEUCONOSTOC MESENTEROIDES GLUCOSE 6-PHOSPHATE     
REMARK   1  TITL 3 DEHYDROGENASE                                                
REMARK   1  REF    PROTEIN SCI.                  V.   2   859 1993              
REMARK   1  REFN                   ISSN 0961-8368                               
REMARK   1  PMID   8495203                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 100000.000                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 89.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 16513                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : FREE R-VALUE                    
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM, USING XPLOR             
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.292                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 810                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 904                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3220                       
REMARK   3   BIN FREE R VALUE                    : 0.3660                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 46                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3840                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 44                                      
REMARK   3   SOLVENT ATOMS            : 61                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.38                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 20.0                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.257                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.93                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.070                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 3.770 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 5.450 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.770 ; 1.500                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 5.450 ; 2.000                
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  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARAM19.SOL                                    
REMARK   3  PARAMETER FILE  3  : NAD.PAR                                        
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH19.SOL                                     
REMARK   3  TOPOLOGY FILE  3   : NAD.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT WAS MODELLED WITH DENSITY    
REMARK   3  0.311 E/A**3 AND TEMPERATURE FACTOR 31.7 A**2. THE OCCUPANCY OF     
REMARK   3  COENZYME NAD HAS BEEN REDUCED TO 0.6 IN ORDER TO MATCH ITS          
REMARK   3  TEMPERATURE FACTORS TO THOSE OF ATOMS IN THE NEIGHBOURING           
REMARK   3  PROTEIN RESIDUES.                                                   
REMARK   4                                                                      
REMARK   4 1H94 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-FEB-01.                  
REMARK 100 THE DEPOSITION ID IS D_1290005807.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-MAY-95                          
REMARK 200  TEMPERATURE           (KELVIN) : 293.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.542                              
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16682                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.9                               
REMARK 200  DATA REDUNDANCY                : 2.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.48000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE, TFFC                                           
REMARK 200 STARTING MODEL: SUBUNIT 'A' OF 1DPG                                  
REMARK 200                                                                      
REMARK 200 REMARK: RIGID-BODY MINIMISATION USED X-PLOR 3.1                      
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROP VAPOUR DIFFUSION, 2+2       
REMARK 280  MICROLITER DROPS. THE WELL BUFFER: 20% V/V PEG 400 IN 0.1M HEPES-   
REMARK 280  NAOH, PH 7.5 WITH 0.2M CALCIUM CHLORIDE. THE PROTEIN AT 10MG/ML     
REMARK 280  IN 100MM TRIS-HCL WITH 12.5MM NAD+., PH 7.50, VAPOR DIFFUSION,      
REMARK 280  HANGING DROP                                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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       65.95000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       22.60000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       65.95000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       22.60000            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 5350 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 46310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.5 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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      131.90000            
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 CHAIN A ENGINEERED MUTATION SER215CYS                                
REMARK 400  BETA-D-GLUCOSE 6-PHOSPHATE + NADP(+) = D-GLUCONO-DELTA-LACTONE      
REMARK 400  6-PHOSPHATE + NADPH.                                                
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    LYS A  21      -46.16   -137.71                                   
REMARK 500    LYS A  37      -56.83   -127.45                                   
REMARK 500    ALA A  45     -165.30   -178.32                                   
REMARK 500    ALA A  48       41.51    -95.41                                   
REMARK 500    LYS A  63      -71.55    -64.63                                   
REMARK 500    PHE A  65       59.17   -110.89                                   
REMARK 500    ASP A  67      -46.26   -130.17                                   
REMARK 500    HIS A  84      129.52   -171.56                                   
REMARK 500    ASN A 111       70.66     55.91                                   
REMARK 500    SER A 117       47.88   -105.00                                   
REMARK 500    ASN A 203     -178.55   -170.31                                   
REMARK 500    ASN A 209      143.58   -173.46                                   
REMARK 500    GLU A 221     -137.20     58.90                                   
REMARK 500    ASN A 239      -78.48    -92.89                                   
REMARK 500    PHE A 256       45.05   -102.93                                   
REMARK 500    LEU A 301        5.59    -65.00                                   
REMARK 500    ASP A 309       20.02   -142.67                                   
REMARK 500    GLU A 328      103.00    -48.81                                   
REMARK 500    GLN A 344      144.66   -170.16                                   
REMARK 500    LYS A 454       46.05   -104.23                                   
REMARK 500    LYS A 484       35.74   -155.01                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: PROCHECK, WITH IDENTIFICATION                  
REMARK 650 CORRESPONDING TO 2.0A L. MESENTEROIDES STRUCTURE, 1DPG.              
REMARK 650 HELIX_ID: A,BEND AT K21 IS CONSEQUENCE OF CONSERVED P24.             
REMARK 650 HELIX_ID: D,THE FIRST TURN IS 3_10 (CLASS 5).                        
REMARK 650 HELIX_ID: F,THE FIRST 2 TURNS ARE 3_10 (CLASS 5).                    
REMARK 650 HELIX_ID: H,G231 BRIDGES H & I' SO IS NOT HELICAL.                   
REMARK 650 HELIX_ID: I',PART OF HELIX I IN 1DPG. RESIDUES 235-239               
REMARK 650  DISTORTED BY SIDECHAIN INTERACTION OF N239 WITH D235.               
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DETERMINATION METHOD: INITIAL AND              
REMARK 700 TERMINAL RESIDUES ARE AS DEFINED BY PROCHECK.                        
REMARK 700 REGISTRATION IS AS GIVEN BY HYDROGEN BONDS AND IN THE                
REMARK 700 CASE OF SHEET COE INVOLVES RESIDUES THAT IMMEDIATELY                 
REMARK 700 PRECEDE EACH SHEET ELEMENT. THIS IS DONE TO PRESERVE                 
REMARK 700 OBSERVED CONSISTENCY WITH NATIVE STRUCTURE 1DPG.                     
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 799                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1DPG   RELATED DB: PDB                                   
REMARK 900 GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES     
REMARK 900 RELATED ID: 1E77   RELATED DB: PDB                                   
REMARK 900 COMPLEX OF ACTIVE MUTANT (Q365->C) OF GLUCOSE 6-PHOSPHATE            
REMARK 900 DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH SUBSTRATE          
REMARK 900 RELATED ID: 1E7M   RELATED DB: PDB                                   
REMARK 900 ACTIVE SITE MUTANT (D177->N) OF GLUCOSE 6 -PHOSPHATE DEHYDROGENASE   
REMARK 900 FROM LEUCONOSTOC MESENTEROIDES                                       
REMARK 900 RELATED ID: 1E7Y   RELATED DB: PDB                                   
REMARK 900 ACTIVE SITE MUTANT (D177->N) OF GLUCOSE 6 -PHOSPHATE DEHYDROGENASE   
REMARK 900 FROM LEUCONOSTOC MESENTEROIDES COMPLEXED WITH SUBSTRATE AND NADPH    
REMARK 900 RELATED ID: 1H93   RELATED DB: PDB                                   
REMARK 900 ACTIVE MUTANT (S215->C) OF GLUCOSE 6- PHOSPHATE DEHYDROGENASE FROM   
REMARK 900 LEUCONOSTOC MESENTEROIDES                                            
REMARK 900 RELATED ID: 2DPG   RELATED DB: PDB                                   
REMARK 900 COMPLEX OF INACTIVE MUTANT (H240->N) OF GLUCOSE 6-PHOSPHATE          
REMARK 900 DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH NADP+              
DBREF  1H94 A    1   485  UNP    P11411   G6PD_LEUME       1    485             
SEQADV 1H94 CYS A  215  UNP  P11411    SER   215 ENGINEERED MUTATION            
SEQRES   1 A  485  VAL SER GLU ILE LYS THR LEU VAL THR PHE PHE GLY GLY          
SEQRES   2 A  485  THR GLY ASP LEU ALA LYS ARG LYS LEU TYR PRO SER VAL          
SEQRES   3 A  485  PHE ASN LEU TYR LYS LYS GLY TYR LEU GLN LYS HIS PHE          
SEQRES   4 A  485  ALA ILE VAL GLY THR ALA ARG GLN ALA LEU ASN ASP ASP          
SEQRES   5 A  485  GLU PHE LYS GLN LEU VAL ARG ASP SER ILE LYS ASP PHE          
SEQRES   6 A  485  THR ASP ASP GLN ALA GLN ALA GLU ALA PHE ILE GLU HIS          
SEQRES   7 A  485  PHE SER TYR ARG ALA HIS ASP VAL THR ASP ALA ALA SER          
SEQRES   8 A  485  TYR ALA VAL LEU LYS GLU ALA ILE GLU GLU ALA ALA ASP          
SEQRES   9 A  485  LYS PHE ASP ILE ASP GLY ASN ARG ILE PHE TYR MET SER          
SEQRES  10 A  485  VAL ALA PRO ARG PHE PHE GLY THR ILE ALA LYS TYR LEU          
SEQRES  11 A  485  LYS SER GLU GLY LEU LEU ALA ASP THR GLY TYR ASN ARG          
SEQRES  12 A  485  LEU MET ILE GLU LYS PRO PHE GLY THR SER TYR ASP THR          
SEQRES  13 A  485  ALA ALA GLU LEU GLN ASN ASP LEU GLU ASN ALA PHE ASP          
SEQRES  14 A  485  ASP ASN GLN LEU PHE ARG ILE ASP HIS TYR LEU GLY LYS          
SEQRES  15 A  485  GLU MET VAL GLN ASN ILE ALA ALA LEU ARG PHE GLY ASN          
SEQRES  16 A  485  PRO ILE PHE ASP ALA ALA TRP ASN LYS ASP TYR ILE LYS          
SEQRES  17 A  485  ASN VAL GLN VAL THR LEU CYS GLU VAL LEU GLY VAL GLU          
SEQRES  18 A  485  GLU ARG ALA GLY TYR TYR ASP THR ALA GLY ALA LEU LEU          
SEQRES  19 A  485  ASP MET ILE GLN ASN HIS THR MET GLN ILE VAL GLY TRP          
SEQRES  20 A  485  LEU ALA MET GLU LYS PRO GLU SER PHE THR ASP LYS ASP          
SEQRES  21 A  485  ILE ARG ALA ALA LYS ASN ALA ALA PHE ASN ALA LEU LYS          
SEQRES  22 A  485  ILE TYR ASP GLU ALA GLU VAL ASN LYS TYR PHE VAL ARG          
SEQRES  23 A  485  ALA GLN TYR GLY ALA GLY ASP SER ALA ASP PHE LYS PRO          
SEQRES  24 A  485  TYR LEU GLU GLU LEU ASP VAL PRO ALA ASP SER LYS ASN          
SEQRES  25 A  485  ASN THR PHE ILE ALA GLY GLU LEU GLN PHE ASP LEU PRO          
SEQRES  26 A  485  ARG TRP GLU GLY VAL PRO PHE TYR VAL ARG SER GLY LYS          
SEQRES  27 A  485  ARG LEU ALA ALA LYS GLN THR ARG VAL ASP ILE VAL PHE          
SEQRES  28 A  485  LYS ALA GLY THR PHE ASN PHE GLY SER GLU GLN GLU ALA          
SEQRES  29 A  485  GLN GLU ALA VAL LEU SER ILE ILE ILE ASP PRO LYS GLY          
SEQRES  30 A  485  ALA ILE GLU LEU LYS LEU ASN ALA LYS SER VAL GLU ASP          
SEQRES  31 A  485  ALA PHE ASN THR ARG THR ILE ASP LEU GLY TRP THR VAL          
SEQRES  32 A  485  SER ASP GLU ASP LYS LYS ASN THR PRO GLU PRO TYR GLU          
SEQRES  33 A  485  ARG MET ILE HIS ASP THR MET ASN GLY ASP GLY SER ASN          
SEQRES  34 A  485  PHE ALA ASP TRP ASN GLY VAL SER ILE ALA TRP LYS PHE          
SEQRES  35 A  485  VAL ASP ALA ILE SER ALA VAL TYR THR ALA ASP LYS ALA          
SEQRES  36 A  485  PRO LEU GLU THR TYR LYS SER GLY SER MET GLY PRO GLU          
SEQRES  37 A  485  ALA SER ASP LYS LEU LEU ALA ALA ASN GLY ASP ALA TRP          
SEQRES  38 A  485  VAL PHE LYS GLY                                              
HET    NAD  A 799      44                                                       
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
FORMUL   2  NAD    C21 H27 N7 O14 P2                                            
FORMUL   3  HOH   *61(H2 O)                                                     
HELIX    1   A ASP A   16  LYS A   31  1SEE REMARK 650                    16    
HELIX    2   B ASP A   51  SER A   61  1                                  11    
HELIX    3  B' GLN A   69  ILE A   76  1                                   8    
HELIX    4   C SER A   91  LYS A  105  1                                  15    
HELIX    5   D PRO A  120  SER A  132  1SEE REMARK 650                    13    
HELIX    6   E TYR A  154  GLU A  165  1                                  12    
HELIX    7  F' HIS A  178  GLY A  181  5                                   4    
HELIX    8   F GLU A  183  GLY A  194  1SEE REMARK 650                    12    
HELIX    9   G PRO A  196  ASP A  199  1                                   4    
HELIX   10   H ALA A  224  ALA A  230  1SEE REMARK 650                     7    
HELIX   11  I' ALA A  232  ASP A  235  1SEE REMARK 650                     4    
HELIX   12   I HIS A  240  ALA A  249  1                                  10    
HELIX   13   J ASP A  258  PHE A  269  1                                  12    
HELIX   14   K GLU A  277  TYR A  283  1                                   7    
HELIX   15   L ASP A  405  ASN A  410  1                                   6    
HELIX   16   M PRO A  414  ASN A  424  1                                  11    
HELIX   17   N TRP A  433  THR A  451  1                                  19    
HELIX   18   O GLU A  468  ALA A  475  1                                   8    
SHEET    1 COE 6 PHE A  79  ALA A  83  0                                        
SHEET    2 COE 6 ALA A  40  ALA A  45  1  N  ILE A  41   O  HIS A  78           
SHEET    3 COE 6 LEU A   7  PHE A  11  1  N  THR A   6   O  HIS A  38           
SHEET    4 COE 6 ARG A 112  MET A 116  1  O  ASN A 111   N  LEU A   7           
SHEET    5 COE 6 ASN A 142  ILE A 146  1  O  TYR A 141   N  ARG A 112           
SHEET    6 COE 6 LEU A 173  ARG A 175  1  O  GLN A 172   N  LEU A 144           
SHEET    1 DIM 9 THR A 394  THR A 402  0                                        
SHEET    2 DIM 9 ALA A 378  LYS A 386 -1  N  ILE A 379   O  TRP A 401           
SHEET    3 DIM 9 VAL A 368  ASP A 374 -1  N  VAL A 368   O  LYS A 382           
SHEET    4 DIM 9 GLN A 344  PHE A 351 -1  O  THR A 345   N  ILE A 373           
SHEET    5 DIM 9 ILE A 207  CYS A 215 -1  O  ASN A 209   N  VAL A 350           
SHEET    6 DIM 9 PHE A 332  GLY A 337  1  N  TYR A 333   O  VAL A 210           
SHEET    7 DIM 9 PHE A 315  LEU A 320 -1  N  ILE A 316   O  SER A 336           
SHEET    8 DIM 9 PHE A 284  TYR A 289 -1  N  VAL A 285   O  ALA A 317           
SHEET    9 DIM 9 GLU A 458  TYR A 460  1  O  GLU A 458   N  GLN A 288           
CISPEP   1 LYS A  148    PRO A  149          0        -0.78                     
CISPEP   2 ASP A  374    PRO A  375          0        -0.33                     
SITE     1 AC1 17 GLY A  12  THR A  14  GLY A  15  ASP A  16                    
SITE     2 AC1 17 LEU A  17  ALA A  18  ALA A  45  ARG A  46                    
SITE     3 AC1 17 GLN A  47  HIS A  84  ASP A  85  VAL A  86                    
SITE     4 AC1 17 SER A 117  GLU A 147  LYS A 148  ARG A 223                    
SITE     5 AC1 17 HOH A2061                                                     
CRYST1  131.900   45.200   93.500  90.00 107.10  90.00 C 1 2 1       4          
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      0.007581  0.000000  0.002332        0.00000                         
SCALE2      0.000000  0.022124  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011190        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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