HEADER OXIDOREDUCTASE 16-DEC-14 4XB1
TITLE HYPERTHERMOPHILIC ARCHAEAL HOMOSERINE DEHYDROGENASE IN COMPLEX WITH
TITLE 2 NADPH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 319AA LONG HYPOTHETICAL HOMOSERINE DEHYDROGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS HORIKOSHII OT3;
SOURCE 3 ORGANISM_TAXID: 70601;
SOURCE 4 STRAIN: OT3;
SOURCE 5 GENE: PH1075;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCOLDI
KEYWDS ROSSMANN FOLD, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.SAKURABA,S.INOUE,K.YONEDA,T.OHSHIMA
REVDAT 3 08-NOV-23 4XB1 1 REMARK
REVDAT 2 25-DEC-19 4XB1 1 SOURCE JRNL REMARK
REVDAT 1 15-JUL-15 4XB1 0
JRNL AUTH J.HAYASHI,S.INOUE,K.KIM,K.YONEDA,Y.KAWARABAYASI,T.OHSHIMA,
JRNL AUTH 2 H.SAKURABA
JRNL TITL CRYSTAL STRUCTURES OF A HYPERTHERMOPHILIC ARCHAEAL
JRNL TITL 2 HOMOSERINE DEHYDROGENASE SUGGEST A NOVEL COFACTOR BINDING
JRNL TITL 3 MODE FOR OXIDOREDUCTASES.
JRNL REF SCI REP V. 5 11674 2015
JRNL REFN ESSN 2045-2322
JRNL PMID 26154028
JRNL DOI 10.1038/SREP11674
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 50089
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) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2685
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3668
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.74
REMARK 3 BIN R VALUE (WORKING SET) : 0.2310
REMARK 3 BIN FREE R VALUE SET COUNT : 172
REMARK 3 BIN FREE R VALUE : 0.2930
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4916
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 138
REMARK 3 SOLVENT ATOMS : 212
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.35000
REMARK 3 B22 (A**2) : 0.35000
REMARK 3 B33 (A**2) : -0.70000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.169
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.156
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.107
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.395
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5129 ; 0.020 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5017 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6960 ; 2.133 ; 2.010
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11565 ; 0.956 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 636 ; 6.843 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 214 ;41.403 ;25.234
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 908 ;18.106 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;20.562 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 808 ; 0.135 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5678 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1054 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 2550 ; 4.166 ; 4.300
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2549 ; 4.165 ; 4.300
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3184 ; 5.721 ; 6.442
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4XB1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-DEC-14.
REMARK 100 THE DEPOSITION ID IS D_1000205369.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NE3A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53097
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 7.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.28500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 9.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 3DO5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2-METHYL-2,4-PENTANDIOL, POTASSIUM
REMARK 280 PHOSPHATE, PH 6.2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
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 47.94250
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 23.97125
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 71.91375
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -15
REMARK 465 ASN A -14
REMARK 465 HIS A -13
REMARK 465 LYS A -12
REMARK 465 VAL A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 ILE A -4
REMARK 465 GLU A -3
REMARK 465 GLY A -2
REMARK 465 ARG A -1
REMARK 465 HIS A 0
REMARK 465 MET B -15
REMARK 465 ASN B -14
REMARK 465 HIS B -13
REMARK 465 LYS B -12
REMARK 465 VAL B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 ILE B -4
REMARK 465 GLU B -3
REMARK 465 GLY B -2
REMARK 465 ARG B -1
REMARK 465 HIS B 0
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 PHE A 10 57.34 -147.83
REMARK 500 PHE A 139 37.92 -144.66
REMARK 500 ALA A 145 -126.58 53.07
REMARK 500 ASN A 317 76.32 -119.51
REMARK 500 PHE B 10 55.06 -146.73
REMARK 500 PHE B 139 37.58 -141.24
REMARK 500 ALA B 145 -126.06 51.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1002 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 140 O
REMARK 620 2 GLU A 140 OE1 79.8
REMARK 620 3 VAL A 143 O 86.2 134.1
REMARK 620 4 ALA A 145 O 86.3 115.5 106.8
REMARK 620 5 THR A 147 O 158.3 80.0 113.9 95.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B1002 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 140 O
REMARK 620 2 GLU B 140 OE1 77.8
REMARK 620 3 VAL B 143 O 85.0 128.1
REMARK 620 4 ALA B 145 O 84.1 118.8 107.3
REMARK 620 5 THR B 147 O 160.1 84.9 113.7 95.9
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 1005
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4XB2 RELATED DB: PDB
DBREF 4XB1 A 1 319 UNP O58802 O58802_PYRHO 1 319
DBREF 4XB1 B 1 319 UNP O58802 O58802_PYRHO 1 319
SEQADV 4XB1 MET A -15 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 ASN A -14 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 HIS A -13 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 LYS A -12 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 VAL A -11 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 HIS A -10 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 HIS A -9 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 HIS A -8 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 HIS A -7 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 HIS A -6 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 HIS A -5 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 ILE A -4 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 GLU A -3 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 GLY A -2 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 ARG A -1 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 HIS A 0 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 MET B -15 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 ASN B -14 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 HIS B -13 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 LYS B -12 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 VAL B -11 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 HIS B -10 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 HIS B -9 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 HIS B -8 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 HIS B -7 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 HIS B -6 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 HIS B -5 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 ILE B -4 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 GLU B -3 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 GLY B -2 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 ARG B -1 UNP O58802 EXPRESSION TAG
SEQADV 4XB1 HIS B 0 UNP O58802 EXPRESSION TAG
SEQRES 1 A 335 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS ILE GLU
SEQRES 2 A 335 GLY ARG HIS MET LYS VAL ASN ILE SER ILE PHE GLY PHE
SEQRES 3 A 335 GLY THR VAL GLY ARG ALA LEU ALA GLU ILE ILE ALA GLU
SEQRES 4 A 335 LYS SER ARG ILE PHE GLY VAL GLU LEU ASN VAL ILE SER
SEQRES 5 A 335 ILE THR ASP ARG SER GLY THR ILE TRP GLY ASP PHE ASP
SEQRES 6 A 335 LEU LEU GLU ALA LYS GLU VAL LYS GLU SER THR GLY LYS
SEQRES 7 A 335 LEU SER ASN ILE GLY ASP TYR GLU VAL TYR ASN PHE SER
SEQRES 8 A 335 PRO GLN GLU LEU VAL GLU GLU VAL LYS PRO ASN ILE LEU
SEQRES 9 A 335 VAL ASP VAL SER SER TRP ASP GLU ALA HIS GLU MET TYR
SEQRES 10 A 335 LYS VAL ALA LEU GLY GLU GLY ILE SER VAL VAL THR SER
SEQRES 11 A 335 ASN LYS PRO PRO ILE ALA ASN TYR TYR ASP GLU LEU MET
SEQRES 12 A 335 ASN LEU ALA LYS GLU ASN ASN ALA GLY ILE PHE PHE GLU
SEQRES 13 A 335 SER THR VAL MET ALA GLY THR PRO ILE ILE GLY VAL LEU
SEQRES 14 A 335 ARG GLU ASN LEU LEU GLY GLU ASN ILE LYS ARG ILE ASP
SEQRES 15 A 335 ALA VAL VAL ASN ALA SER THR THR PHE ILE LEU THR LYS
SEQRES 16 A 335 MET SER GLU GLY LYS THR LEU ASP ASP ALA ILE GLU GLU
SEQRES 17 A 335 ALA LYS SER LEU GLY ILE LEU GLU GLU ASP PRO SER LYS
SEQRES 18 A 335 ASP ILE ASP GLY ILE ASP ALA TYR TYR LYS ALA LYS ILE
SEQRES 19 A 335 LEU HIS TRP VAL SER TYR GLY GLU PRO PRO GLU GLU GLU
SEQRES 20 A 335 GLU ARG LEU GLY ILE ARG GLU VAL ARG ASP ALA ARG ASN
SEQRES 21 A 335 VAL ARG LEU VAL ALA GLN VAL SER LYS GLY LYS ILE SER
SEQRES 22 A 335 VAL LYS PRO ARG LYS LEU SER SER ASP ASN PRO LEU LEU
SEQRES 23 A 335 VAL GLU GLY VAL GLN ASN ALA ALA VAL ILE ARG THR ASN
SEQRES 24 A 335 ASN LEU GLY GLU VAL ILE LEU LYS GLY PRO GLY GLY GLY
SEQRES 25 A 335 GLY ARG VAL THR ALA SER GLY VAL PHE THR ASP ILE ILE
SEQRES 26 A 335 LYS ALA THR LEU LYS PHE PRO ASN LEU ARG
SEQRES 1 B 335 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS ILE GLU
SEQRES 2 B 335 GLY ARG HIS MET LYS VAL ASN ILE SER ILE PHE GLY PHE
SEQRES 3 B 335 GLY THR VAL GLY ARG ALA LEU ALA GLU ILE ILE ALA GLU
SEQRES 4 B 335 LYS SER ARG ILE PHE GLY VAL GLU LEU ASN VAL ILE SER
SEQRES 5 B 335 ILE THR ASP ARG SER GLY THR ILE TRP GLY ASP PHE ASP
SEQRES 6 B 335 LEU LEU GLU ALA LYS GLU VAL LYS GLU SER THR GLY LYS
SEQRES 7 B 335 LEU SER ASN ILE GLY ASP TYR GLU VAL TYR ASN PHE SER
SEQRES 8 B 335 PRO GLN GLU LEU VAL GLU GLU VAL LYS PRO ASN ILE LEU
SEQRES 9 B 335 VAL ASP VAL SER SER TRP ASP GLU ALA HIS GLU MET TYR
SEQRES 10 B 335 LYS VAL ALA LEU GLY GLU GLY ILE SER VAL VAL THR SER
SEQRES 11 B 335 ASN LYS PRO PRO ILE ALA ASN TYR TYR ASP GLU LEU MET
SEQRES 12 B 335 ASN LEU ALA LYS GLU ASN ASN ALA GLY ILE PHE PHE GLU
SEQRES 13 B 335 SER THR VAL MET ALA GLY THR PRO ILE ILE GLY VAL LEU
SEQRES 14 B 335 ARG GLU ASN LEU LEU GLY GLU ASN ILE LYS ARG ILE ASP
SEQRES 15 B 335 ALA VAL VAL ASN ALA SER THR THR PHE ILE LEU THR LYS
SEQRES 16 B 335 MET SER GLU GLY LYS THR LEU ASP ASP ALA ILE GLU GLU
SEQRES 17 B 335 ALA LYS SER LEU GLY ILE LEU GLU GLU ASP PRO SER LYS
SEQRES 18 B 335 ASP ILE ASP GLY ILE ASP ALA TYR TYR LYS ALA LYS ILE
SEQRES 19 B 335 LEU HIS TRP VAL SER TYR GLY GLU PRO PRO GLU GLU GLU
SEQRES 20 B 335 GLU ARG LEU GLY ILE ARG GLU VAL ARG ASP ALA ARG ASN
SEQRES 21 B 335 VAL ARG LEU VAL ALA GLN VAL SER LYS GLY LYS ILE SER
SEQRES 22 B 335 VAL LYS PRO ARG LYS LEU SER SER ASP ASN PRO LEU LEU
SEQRES 23 B 335 VAL GLU GLY VAL GLN ASN ALA ALA VAL ILE ARG THR ASN
SEQRES 24 B 335 ASN LEU GLY GLU VAL ILE LEU LYS GLY PRO GLY GLY GLY
SEQRES 25 B 335 GLY ARG VAL THR ALA SER GLY VAL PHE THR ASP ILE ILE
SEQRES 26 B 335 LYS ALA THR LEU LYS PHE PRO ASN LEU ARG
HET NDP A1001 48
HET NA A1002 1
HET MPD A1003 8
HET MPD A1004 8
HET NDP B1001 48
HET NA B1002 1
HET MPD B1003 8
HET MPD B1004 8
HET MPD B1005 8
HETNAM NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 2 NDP PHOSPHATE
HETNAM NA SODIUM ION
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
FORMUL 3 NDP 2(C21 H30 N7 O17 P3)
FORMUL 4 NA 2(NA 1+)
FORMUL 5 MPD 5(C6 H14 O2)
FORMUL 12 HOH *212(H2 O)
HELIX 1 AA1 GLY A 11 SER A 25 1 15
HELIX 2 AA2 ASP A 49 GLY A 61 1 13
HELIX 3 AA3 LYS A 62 ILE A 66 5 5
HELIX 4 AA4 SER A 75 LYS A 84 1 10
HELIX 5 AA5 ALA A 97 GLU A 107 1 11
HELIX 6 AA6 ASN A 115 ASN A 133 1 19
HELIX 7 AA7 PHE A 139 VAL A 143 5 5
HELIX 8 AA8 PRO A 148 ASN A 156 1 9
HELIX 9 AA9 ASN A 170 GLU A 182 1 13
HELIX 10 AB1 THR A 185 LEU A 196 1 12
HELIX 11 AB2 PRO A 203 ASP A 208 1 6
HELIX 12 AB3 GLY A 209 GLY A 225 1 17
HELIX 13 AB4 GLY A 296 LEU A 313 1 18
HELIX 14 AB5 GLY B 11 SER B 25 1 15
HELIX 15 AB6 ASP B 49 GLY B 61 1 13
HELIX 16 AB7 SER B 75 LYS B 84 1 10
HELIX 17 AB8 ALA B 97 GLU B 107 1 11
HELIX 18 AB9 ASN B 115 ASN B 133 1 19
HELIX 19 AC1 PHE B 139 VAL B 143 5 5
HELIX 20 AC2 PRO B 148 ASN B 156 1 9
HELIX 21 AC3 ASN B 170 GLU B 182 1 13
HELIX 22 AC4 THR B 185 LEU B 196 1 12
HELIX 23 AC5 PRO B 203 ASP B 208 1 6
HELIX 24 AC6 GLY B 209 GLY B 225 1 17
HELIX 25 AC7 GLY B 296 LEU B 313 1 18
SHEET 1 AA1 3 ARG A 26 ILE A 27 0
SHEET 2 AA1 3 VAL A 30 ASP A 39 -1 O VAL A 30 N ILE A 27
SHEET 3 AA1 3 GLY A 42 TRP A 45 -1 O ILE A 44 N ILE A 37
SHEET 1 AA2 6 ARG A 26 ILE A 27 0
SHEET 2 AA2 6 VAL A 30 ASP A 39 -1 O VAL A 30 N ILE A 27
SHEET 3 AA2 6 LYS A 2 PHE A 8 1 N VAL A 3 O GLU A 31
SHEET 4 AA2 6 ILE A 87 ASP A 90 1 O VAL A 89 N PHE A 8
SHEET 5 AA2 6 SER A 110 THR A 113 1 O VAL A 112 N ASP A 90
SHEET 6 AA2 6 ILE A 137 PHE A 138 1 O PHE A 138 N VAL A 111
SHEET 1 AA312 GLU A 230 ARG A 233 0
SHEET 2 AA312 LYS A 255 LYS A 262 1 O VAL A 258 N GLU A 232
SHEET 3 AA312 VAL A 245 SER A 252 -1 N GLN A 250 O SER A 257
SHEET 4 AA312 ILE A 162 VAL A 168 -1 N ALA A 167 O ALA A 249
SHEET 5 AA312 GLN A 275 THR A 282 -1 O VAL A 279 N ASP A 166
SHEET 6 AA312 GLY A 286 PRO A 293 -1 O VAL A 288 N ILE A 280
SHEET 7 AA312 GLY B 286 PRO B 293 -1 O ILE B 289 N LYS A 291
SHEET 8 AA312 GLN B 275 THR B 282 -1 N ILE B 280 O VAL B 288
SHEET 9 AA312 ILE B 162 VAL B 168 -1 N ARG B 164 O ARG B 281
SHEET 10 AA312 VAL B 245 SER B 252 -1 O VAL B 251 N ILE B 165
SHEET 11 AA312 LYS B 255 LYS B 262 -1 O LYS B 255 N SER B 252
SHEET 12 AA312 GLU B 230 ARG B 233 1 N GLU B 232 O VAL B 258
SHEET 1 AA4 7 VAL B 71 TYR B 72 0
SHEET 2 AA4 7 GLY B 42 TRP B 45 -1 N THR B 43 O TYR B 72
SHEET 3 AA4 7 GLU B 31 ASP B 39 -1 N ILE B 37 O ILE B 44
SHEET 4 AA4 7 LYS B 2 PHE B 8 1 N ILE B 5 O ASN B 33
SHEET 5 AA4 7 ILE B 87 ASP B 90 1 O VAL B 89 N PHE B 8
SHEET 6 AA4 7 SER B 110 THR B 113 1 O SER B 110 N LEU B 88
SHEET 7 AA4 7 ILE B 137 PHE B 138 1 O PHE B 138 N VAL B 111
LINK O GLU A 140 NA NA A1002 1555 1555 2.59
LINK OE1 GLU A 140 NA NA A1002 1555 1555 2.47
LINK O VAL A 143 NA NA A1002 1555 1555 2.32
LINK O ALA A 145 NA NA A1002 1555 1555 2.38
LINK O THR A 147 NA NA A1002 1555 1555 2.40
LINK O GLU B 140 NA NA B1002 1555 1555 2.58
LINK OE1 GLU B 140 NA NA B1002 1555 1555 2.50
LINK O VAL B 143 NA NA B1002 1555 1555 2.23
LINK O ALA B 145 NA NA B1002 1555 1555 2.41
LINK O THR B 147 NA NA B1002 1555 1555 2.47
SITE 1 AC1 27 PHE A 8 PHE A 10 GLY A 11 THR A 12
SITE 2 AC1 27 VAL A 13 ASP A 39 ARG A 40 LYS A 57
SITE 3 AC1 27 VAL A 91 SER A 92 SER A 93 SER A 114
SITE 4 AC1 27 ASN A 115 LYS A 116 SER A 141 GLY A 295
SITE 5 AC1 27 GLY A 296 THR A 300 MPD A1003 HOH A1143
SITE 6 AC1 27 HOH A1161 HOH A1170 HOH A1201 HOH A1205
SITE 7 AC1 27 HOH A1211 HOH A1213 HOH A1219
SITE 1 AC2 5 GLU A 140 VAL A 143 MET A 144 ALA A 145
SITE 2 AC2 5 THR A 147
SITE 1 AC3 7 LYS A 116 LYS A 215 GLY A 294 NDP A1001
SITE 2 AC3 7 HOH A1144 HOH A1188 HOH A1201
SITE 1 AC4 3 LYS A 131 GLY A 225 LEU A 318
SITE 1 AC5 23 PHE B 8 PHE B 10 GLY B 11 THR B 12
SITE 2 AC5 23 VAL B 13 ASP B 39 ARG B 40 LYS B 57
SITE 3 AC5 23 VAL B 91 SER B 92 SER B 93 SER B 114
SITE 4 AC5 23 ASN B 115 LYS B 116 SER B 141 GLY B 295
SITE 5 AC5 23 GLY B 296 THR B 300 MPD B1003 HOH B1125
SITE 6 AC5 23 HOH B1163 HOH B1174 HOH B1188
SITE 1 AC6 5 GLU B 140 VAL B 143 MET B 144 ALA B 145
SITE 2 AC6 5 THR B 147
SITE 1 AC7 6 LYS B 116 LYS B 215 GLY B 294 NDP B1001
SITE 2 AC7 6 HOH B1163 HOH B1178
SITE 1 AC8 5 ASN A 73 GLU A 78 ASN B 267 HOH B1103
SITE 2 AC8 5 HOH B1109
SITE 1 AC9 2 MET B 127 GLY B 225
CRYST1 112.560 112.560 95.885 90.00 90.00 90.00 P 41 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 0.008884 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008884 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010429 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
