HEADER ISOMERASE 31-MAR-09 3GW8
TITLE CRYSTAL STRUCTURE OF PHOSPHOGLYCEROMUTASE FROM BURKHOLDERIA
TITLE 2 PSEUDOMALLEI WITH VANADATE AND GLYCEROL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2,3-BISPHOSPHOGLYCERATE-DEPENDENT PHOSPHOGLYCERATE MUTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PHOSPHOGLYCEROMUTASE, PGAM, BPG-DEPENDENT PGAM, DPGM;
COMPND 5 EC: 5.4.2.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA PSEUDOMALLEI;
SOURCE 3 ORGANISM_COMMON: PSEUDOMONAS PSEUDOMALLEI;
SOURCE 4 ORGANISM_TAXID: 28450;
SOURCE 5 STRAIN: 1710B;
SOURCE 6 GENE: GPMA, BPSL0443;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: BG1861
KEYWDS SSGCID, NIAID, DECODE, UWPPG, SBRI, GLYCOLYSIS, ISOMERASE, STRUCTURAL
KEYWDS 2 GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 3 05-OCT-11 3GW8 1 JRNL
REVDAT 2 13-JUL-11 3GW8 1 VERSN
REVDAT 1 07-APR-09 3GW8 0
JRNL AUTH D.R.DAVIES,B.L.STAKER,J.A.ABENDROTH,T.E.EDWARDS,R.HARTLEY,
JRNL AUTH 2 J.LEONARD,H.KIM,A.L.RYCHEL,S.N.HEWITT,P.J.MYLER,L.J.STEWART
JRNL TITL AN ENSEMBLE OF STRUCTURES OF BURKHOLDERIA PSEUDOMALLEI
JRNL TITL 2 2,3-BISPHOSPHOGLYCERATE-DEPENDENT PHOSPHOGLYCERATE MUTASE.
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 67 1044 2011
JRNL REFN ESSN 1744-3091
JRNL PMID 21904048
JRNL DOI 10.1107/S1744309111030405
REMARK 2
REMARK 2 RESOLUTION. 1.93 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0088
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) : 1.93
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.6
REMARK 3 NUMBER OF REFLECTIONS : 34057
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1696
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) : 1.93
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2017
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.28
REMARK 3 BIN R VALUE (WORKING SET) : 0.2600
REMARK 3 BIN FREE R VALUE SET COUNT : 92
REMARK 3 BIN FREE R VALUE : 0.3080
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3666
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 82
REMARK 3 SOLVENT ATOMS : 315
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.58000
REMARK 3 B22 (A**2) : -0.38000
REMARK 3 B33 (A**2) : 0.07000
REMARK 3 B12 (A**2) : 0.31000
REMARK 3 B13 (A**2) : -0.28000
REMARK 3 B23 (A**2) : 0.17000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.192
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.163
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.102
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.495
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3879 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2664 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5265 ; 1.200 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6461 ; 0.838 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 466 ; 6.004 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 181 ;34.778 ;23.370
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 617 ;12.783 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 33 ;18.038 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 567 ; 0.069 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4259 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 778 ; 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): 2320 ; 0.550 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 928 ; 0.115 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3742 ; 1.019 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1559 ; 1.511 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1523 ; 2.505 ; 4.500
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:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3GW8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-APR-09.
REMARK 100 THE RCSB ID CODE IS RCSB052384.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
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 FR-E+ SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL2000
REMARK 200 DATA SCALING SOFTWARE : HKL2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34058
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.930
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 (%) : 92.8
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.9750
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.30100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.890
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: 3EZN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: EMERALD CRYO SCREEN B-4, 100 MM MES PH
REMARK 280 6.0, 5% PEG 1000, 10% GLYCEROL, 30% PEG 600, 11.7 MG/ML PROTEIN,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 -7
REMARK 465 ALA A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 GLN A 231
REMARK 465 GLU A 232
REMARK 465 ALA A 233
REMARK 465 ILE A 234
REMARK 465 ALA A 235
REMARK 465 LYS A 236
REMARK 465 ALA A 237
REMARK 465 GLN A 238
REMARK 465 ALA A 239
REMARK 465 ALA A 240
REMARK 465 VAL A 241
REMARK 465 ALA A 242
REMARK 465 GLN A 243
REMARK 465 GLN A 244
REMARK 465 GLY A 245
REMARK 465 LYS A 246
REMARK 465 SER A 247
REMARK 465 ALA A 248
REMARK 465 ALA A 249
REMARK 465 MET B -7
REMARK 465 ALA B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 GLN B 231
REMARK 465 GLU B 232
REMARK 465 ALA B 233
REMARK 465 ILE B 234
REMARK 465 ALA B 235
REMARK 465 LYS B 236
REMARK 465 ALA B 237
REMARK 465 GLN B 238
REMARK 465 ALA B 239
REMARK 465 ALA B 240
REMARK 465 VAL B 241
REMARK 465 ALA B 242
REMARK 465 GLN B 243
REMARK 465 GLN B 244
REMARK 465 GLY B 245
REMARK 465 LYS B 246
REMARK 465 SER B 247
REMARK 465 ALA B 248
REMARK 465 ALA B 249
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 129 CG CD OE1 OE2
REMARK 470 VAL A 202 CG1 CG2
REMARK 470 LYS B 44 CG CD CE NZ
REMARK 470 LYS B 140 CG CD CE NZ
REMARK 470 GLU B 218 CG CD OE1 OE2
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 SER A 166 -52.63 -132.96
REMARK 500 ALA A 181 -139.69 -144.48
REMARK 500 ARG B 115 13.47 -147.04
REMARK 500 SER B 166 -52.94 -134.91
REMARK 500 ALA B 181 -133.51 -145.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 VO4 A 401
REMARK 610 VO4 B 401
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 VO4 B 401 V
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GOL B 402 O2
REMARK 620 2 VO4 B 401 O1 89.3
REMARK 620 3 VO4 B 401 O2 97.8 115.6
REMARK 620 4 VO4 B 401 O3 91.8 124.0 119.7
REMARK 620 5 HIS B 9 NE2 174.9 89.1 87.2 85.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 VO4 A 401 V
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GOL A 402 O2
REMARK 620 2 VO4 A 401 O1 110.8
REMARK 620 3 VO4 A 401 O2 99.6 114.1
REMARK 620 4 VO4 A 401 O3 83.9 124.4 115.5
REMARK 620 5 HIS A 9 NE2 160.2 84.0 85.4 76.7
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 VO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VO4 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VO4 B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3EZN RELATED DB: PDB
REMARK 900 APO CRYSTAL STRUCTURE
REMARK 900 RELATED ID: 3FDZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE WITH 2,3-DIPHOSPHOGLYCERIC ACID IN ONE
REMARK 900 MONOMER AND 3-PHOSPHOGLYCERIC ACID IN THE OTHER
REMARK 900 RELATED ID: 3GP3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE WITH 2-PHOSPHOSERINE
REMARK 900 RELATED ID: 3GP5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE WITH VANADATE AND 3-PHOSPHOGLYCERIC ACID
REMARK 900 RELATED ID: BUPSA.00114.A RELATED DB: TARGETDB
DBREF 3GW8 A 1 249 UNP Q63XU7 GPMA_BURPS 1 249
DBREF 3GW8 B 1 249 UNP Q63XU7 GPMA_BURPS 1 249
SEQADV 3GW8 MET A -7 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GW8 ALA A -6 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GW8 HIS A -5 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GW8 HIS A -4 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GW8 HIS A -3 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GW8 HIS A -2 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GW8 HIS A -1 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GW8 HIS A 0 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GW8 MET B -7 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GW8 ALA B -6 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GW8 HIS B -5 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GW8 HIS B -4 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GW8 HIS B -3 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GW8 HIS B -2 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GW8 HIS B -1 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GW8 HIS B 0 UNP Q63XU7 EXPRESSION TAG
SEQRES 1 A 257 MET ALA HIS HIS HIS HIS HIS HIS MET TYR LYS LEU VAL
SEQRES 2 A 257 LEU ILE ARG HIS GLY GLU SER THR TRP ASN LYS GLU ASN
SEQRES 3 A 257 ARG PHE THR GLY TRP VAL ASP VAL ASP LEU THR GLU GLN
SEQRES 4 A 257 GLY ASN ARG GLU ALA ARG GLN ALA GLY GLN LEU LEU LYS
SEQRES 5 A 257 GLU ALA GLY TYR THR PHE ASP ILE ALA TYR THR SER VAL
SEQRES 6 A 257 LEU LYS ARG ALA ILE ARG THR LEU TRP HIS VAL GLN ASP
SEQRES 7 A 257 GLN MET ASP LEU MET TYR VAL PRO VAL VAL HIS SER TRP
SEQRES 8 A 257 ARG LEU ASN GLU ARG HIS TYR GLY ALA LEU SER GLY LEU
SEQRES 9 A 257 ASN LYS ALA GLU THR ALA ALA LYS TYR GLY ASP GLU GLN
SEQRES 10 A 257 VAL LEU VAL TRP ARG ARG SER TYR ASP THR PRO PRO PRO
SEQRES 11 A 257 ALA LEU GLU PRO GLY ASP GLU ARG ALA PRO TYR ALA ASP
SEQRES 12 A 257 PRO ARG TYR ALA LYS VAL PRO ARG GLU GLN LEU PRO LEU
SEQRES 13 A 257 THR GLU CYS LEU LYS ASP THR VAL ALA ARG VAL LEU PRO
SEQRES 14 A 257 LEU TRP ASN GLU SER ILE ALA PRO ALA VAL LYS ALA GLY
SEQRES 15 A 257 LYS GLN VAL LEU ILE ALA ALA HIS GLY ASN SER LEU ARG
SEQRES 16 A 257 ALA LEU ILE LYS TYR LEU ASP GLY ILE SER ASP ALA ASP
SEQRES 17 A 257 ILE VAL GLY LEU ASN ILE PRO ASN GLY VAL PRO LEU VAL
SEQRES 18 A 257 TYR GLU LEU ASP GLU SER LEU THR PRO ILE ARG HIS TYR
SEQRES 19 A 257 TYR LEU GLY ASP GLN GLU ALA ILE ALA LYS ALA GLN ALA
SEQRES 20 A 257 ALA VAL ALA GLN GLN GLY LYS SER ALA ALA
SEQRES 1 B 257 MET ALA HIS HIS HIS HIS HIS HIS MET TYR LYS LEU VAL
SEQRES 2 B 257 LEU ILE ARG HIS GLY GLU SER THR TRP ASN LYS GLU ASN
SEQRES 3 B 257 ARG PHE THR GLY TRP VAL ASP VAL ASP LEU THR GLU GLN
SEQRES 4 B 257 GLY ASN ARG GLU ALA ARG GLN ALA GLY GLN LEU LEU LYS
SEQRES 5 B 257 GLU ALA GLY TYR THR PHE ASP ILE ALA TYR THR SER VAL
SEQRES 6 B 257 LEU LYS ARG ALA ILE ARG THR LEU TRP HIS VAL GLN ASP
SEQRES 7 B 257 GLN MET ASP LEU MET TYR VAL PRO VAL VAL HIS SER TRP
SEQRES 8 B 257 ARG LEU ASN GLU ARG HIS TYR GLY ALA LEU SER GLY LEU
SEQRES 9 B 257 ASN LYS ALA GLU THR ALA ALA LYS TYR GLY ASP GLU GLN
SEQRES 10 B 257 VAL LEU VAL TRP ARG ARG SER TYR ASP THR PRO PRO PRO
SEQRES 11 B 257 ALA LEU GLU PRO GLY ASP GLU ARG ALA PRO TYR ALA ASP
SEQRES 12 B 257 PRO ARG TYR ALA LYS VAL PRO ARG GLU GLN LEU PRO LEU
SEQRES 13 B 257 THR GLU CYS LEU LYS ASP THR VAL ALA ARG VAL LEU PRO
SEQRES 14 B 257 LEU TRP ASN GLU SER ILE ALA PRO ALA VAL LYS ALA GLY
SEQRES 15 B 257 LYS GLN VAL LEU ILE ALA ALA HIS GLY ASN SER LEU ARG
SEQRES 16 B 257 ALA LEU ILE LYS TYR LEU ASP GLY ILE SER ASP ALA ASP
SEQRES 17 B 257 ILE VAL GLY LEU ASN ILE PRO ASN GLY VAL PRO LEU VAL
SEQRES 18 B 257 TYR GLU LEU ASP GLU SER LEU THR PRO ILE ARG HIS TYR
SEQRES 19 B 257 TYR LEU GLY ASP GLN GLU ALA ILE ALA LYS ALA GLN ALA
SEQRES 20 B 257 ALA VAL ALA GLN GLN GLY LYS SER ALA ALA
HET VO4 A 401 4
HET GOL A 402 12
HET VO4 A 403 5
HET PG4 A 501 13
HET PG4 A 502 13
HET PG4 A 250 13
HET VO4 B 401 4
HET GOL B 402 12
HET VO4 B 403 5
HET PG4 B 501 13
HETNAM VO4 VANADATE ION
HETNAM GOL GLYCEROL
HETNAM PG4 TETRAETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 VO4 4(O4 V 3-)
FORMUL 4 GOL 2(C3 H8 O3)
FORMUL 6 PG4 4(C8 H18 O5)
FORMUL 13 HOH *315(H2 O)
HELIX 1 1 SER A 12 GLU A 17 1 6
HELIX 2 2 THR A 29 ALA A 46 1 18
HELIX 3 3 LEU A 58 ASP A 73 1 16
HELIX 4 4 TRP A 83 ASN A 86 5 4
HELIX 5 5 TYR A 90 SER A 94 5 5
HELIX 6 6 ASN A 97 GLY A 106 1 10
HELIX 7 7 GLY A 106 SER A 116 1 11
HELIX 8 8 ASP A 135 ALA A 139 5 5
HELIX 9 9 PRO A 142 LEU A 146 5 5
HELIX 10 10 CYS A 151 SER A 166 1 16
HELIX 11 11 SER A 166 ALA A 173 1 8
HELIX 12 12 HIS A 182 GLY A 195 1 14
HELIX 13 13 SER A 197 VAL A 202 1 6
HELIX 14 14 SER B 12 GLU B 17 1 6
HELIX 15 15 THR B 29 ALA B 46 1 18
HELIX 16 16 LEU B 58 ASP B 73 1 16
HELIX 17 17 TRP B 83 ASN B 86 5 4
HELIX 18 18 TYR B 90 SER B 94 5 5
HELIX 19 19 ASN B 97 GLY B 106 1 10
HELIX 20 20 GLY B 106 SER B 116 1 11
HELIX 21 21 ASP B 135 ALA B 139 5 5
HELIX 22 22 PRO B 142 LEU B 146 5 5
HELIX 23 23 CYS B 151 SER B 166 1 16
HELIX 24 24 SER B 166 ALA B 173 1 8
HELIX 25 25 HIS B 182 ASP B 194 1 13
HELIX 26 26 SER B 197 VAL B 202 1 6
SHEET 1 A 6 VAL A 79 HIS A 81 0
SHEET 2 A 6 ILE A 52 THR A 55 1 N THR A 55 O VAL A 80
SHEET 3 A 6 VAL A 177 ALA A 181 1 O ALA A 180 N TYR A 54
SHEET 4 A 6 TYR A 2 ARG A 8 1 N ILE A 7 O ALA A 181
SHEET 5 A 6 LEU A 212 LEU A 216 -1 O LEU A 212 N LEU A 6
SHEET 6 A 6 PRO A 222 TYR A 227 -1 O ILE A 223 N GLU A 215
SHEET 1 B 6 VAL B 79 HIS B 81 0
SHEET 2 B 6 ILE B 52 THR B 55 1 N ALA B 53 O VAL B 80
SHEET 3 B 6 VAL B 177 ALA B 181 1 O ALA B 180 N TYR B 54
SHEET 4 B 6 TYR B 2 ARG B 8 1 N VAL B 5 O ILE B 179
SHEET 5 B 6 LEU B 212 LEU B 216 -1 O TYR B 214 N LEU B 4
SHEET 6 B 6 PRO B 222 TYR B 227 -1 O ILE B 223 N GLU B 215
LINK V VO4 B 401 O2 BGOL B 402 1555 1555 1.92
LINK V VO4 A 401 O2 AGOL A 402 1555 1555 1.94
LINK V VO4 A 401 O2 BGOL A 402 1555 1555 1.98
LINK V VO4 B 401 O2 AGOL B 402 1555 1555 2.01
LINK NE2 HIS B 9 V VO4 B 401 1555 1555 2.23
LINK NE2 HIS A 9 V VO4 A 401 1555 1555 2.30
SITE 1 AC1 9 ARG A 8 HIS A 9 ASN A 15 ARG A 60
SITE 2 AC1 9 GLU A 87 HIS A 182 GLY A 183 HOH A 313
SITE 3 AC1 9 GOL A 402
SITE 1 AC2 12 ARG A 8 ASN A 15 ARG A 19 PHE A 20
SITE 2 AC2 12 THR A 21 GLY A 22 GLU A 87 TYR A 90
SITE 3 AC2 12 HOH A 255 HOH A 383 VO4 A 401 VO4 A 403
SITE 1 AC3 6 PHE A 20 TYR A 90 LYS A 98 ASN A 184
SITE 2 AC3 6 HOH A 255 GOL A 402
SITE 1 AC4 4 ILE A 196 LEU A 204 HIS A 225 HOH A 414
SITE 1 AC5 2 ALA A 173 LYS A 175
SITE 1 AC6 4 LYS A 140 HOH A 317 ASP B 51 LYS B 175
SITE 1 AC7 9 ARG B 8 HIS B 9 ASN B 15 ARG B 60
SITE 2 AC7 9 GLU B 87 HIS B 182 GLY B 183 HOH B 277
SITE 3 AC7 9 GOL B 402
SITE 1 AC8 11 ARG B 8 ASN B 15 ARG B 19 PHE B 20
SITE 2 AC8 11 THR B 21 GLY B 22 GLU B 87 TYR B 90
SITE 3 AC8 11 HOH B 342 VO4 B 401 VO4 B 403
SITE 1 AC9 6 TYR B 90 LYS B 98 ARG B 114 ARG B 115
SITE 2 AC9 6 ASN B 184 GOL B 402
SITE 1 BC1 7 ASP B 194 ILE B 196 LEU B 204 TYR B 214
SITE 2 BC1 7 HIS B 225 TYR B 227 HOH B 282
CRYST1 45.175 49.112 62.590 106.42 91.18 107.61 P 1 2
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 0.022136 0.007026 0.002711 0.00000
SCALE2 0.000000 0.021363 0.006794 0.00000
SCALE3 0.000000 0.000000 0.016769 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
