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