HEADER ISOMERASE 26-NOV-08 3FDZ
TITLE CRYSTAL STRUCTURE OF PHOSPHOGLYCEROMUTASE FROM BURKHOLDERIA
TITLE 2 PSEUDOMALLEI 1710B WITH BOUND 2,3-DIPHOSPHOGLYCERIC ACID AND 3-
TITLE 3 PHOSPHOGLYCERIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2,3-BISPHOSPHOGLYCERATE-DEPENDENT PHOSPHOGLYCERATE MUTASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PHOSPHOGLYCEROMUTASE, PGAM, BPG-DEPENDENT PGAM, DPGM;
COMPND 5 EC: 5.4.2.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: 2,3-BISPHOSPHOGLYCERATE-DEPENDENT PHOSPHOGLYCERATE MUTASE;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: PHOSPHOGLYCEROMUTASE, PGAM, BPG-DEPENDENT PGAM, DPGM;
COMPND 11 EC: 5.4.2.1;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA PSEUDOMALLEI 1710B;
SOURCE 3 ORGANISM_TAXID: 320372;
SOURCE 4 STRAIN: 1719B;
SOURCE 5 GENE: BURPS1710B_0662, GPMA;
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: AVA0421;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: BURKHOLDERIA PSEUDOMALLEI 1710B;
SOURCE 13 ORGANISM_TAXID: 320372;
SOURCE 14 STRAIN: 1719B;
SOURCE 15 GENE: BURPS1710B_0662, GPMA;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: AVA0421
KEYWDS ISOMERASE, SSGCID, PHOSPHOGLYCEROMUTASE, BURKHOLDERIA PSEUDOMALLEI,
KEYWDS 2 GLYCOLYSIS, STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER
KEYWDS 3 FOR INFECTIOUS DISEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 4 05-OCT-11 3FDZ 1 JRNL VERSN
REVDAT 3 07-APR-09 3FDZ 1 REMARK
REVDAT 2 31-MAR-09 3FDZ 1 REMARK
REVDAT 1 13-JAN-09 3FDZ 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. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0053
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.75
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 20934
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) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1066
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) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.31
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1440
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.87
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE SET COUNT : 82
REMARK 3 BIN FREE R VALUE : 0.3310
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3668
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 223
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.18
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.60000
REMARK 3 B22 (A**2) : -0.45000
REMARK 3 B33 (A**2) : -0.17000
REMARK 3 B12 (A**2) : 0.12000
REMARK 3 B13 (A**2) : -1.14000
REMARK 3 B23 (A**2) : -0.05000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.418
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.266
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.174
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.030
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.891
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3796 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5175 ; 1.526 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 457 ; 6.698 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 177 ;38.445 ;23.390
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 610 ;14.593 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;13.904 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 563 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2905 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 2291 ; 0.585 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3693 ; 1.059 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1505 ; 1.923 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1482 ; 3.013 ; 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 : 1.20
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
REMARK 4
REMARK 4 3FDZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-DEC-08.
REMARK 100 THE RCSB ID CODE IS RCSB050471.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-SEP-08
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.00
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : SATURN
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20934
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.4300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.34500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 600, 5% PEG 1000, 10%
REMARK 280 GLYCEROL, 100 MM MES PH 6.0, CRYSTALS SOAKED OVERNIGHT WITH 20 MM
REMARK 280 3-PHOSPHOGLYCERIC ACID, VAPOR DIFFUSION, VAPOR DIFFUSION, SITTING
REMARK 280 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, 3
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 300 REMARK: THE ASYMMETRIC UNIT CONTAINS TWO BIOLOGICAL UNITS
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: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 4.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 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 ASP B 230
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 LYS A 140 CG CD CE NZ
REMARK 470 LYS B 140 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NE2 GLN A 41 OE1 GLN A 71 2.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 25 52.32 -95.95
REMARK 500 SER A 166 -60.56 -138.38
REMARK 500 ALA A 181 -137.08 -143.90
REMARK 500 ASP B 25 56.83 -93.88
REMARK 500 SER B 166 -59.07 -127.36
REMARK 500 ALA B 181 -141.56 -141.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 323 DISTANCE = 5.14 ANGSTROMS
REMARK 525 HOH B 345 DISTANCE = 5.69 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DG2 A1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3PG B1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1002
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3EZN RELATED DB: PDB
REMARK 900 SAME STRUCTURE WITHOUT LIGANDS
REMARK 900 RELATED ID: BUPSA.00114.A RELATED DB: TARGETDB
REMARK 900 RELATED ID: 3GP3 RELATED DB: PDB
REMARK 900 RELATED ID: 3GP5 RELATED DB: PDB
REMARK 900 RELATED ID: 3GW8 RELATED DB: PDB
DBREF 3FDZ A 1 249 UNP Q3JWH7 GPMA_BURP1 1 249
DBREF 3FDZ B 1 249 UNP Q3JWH7 GPMA_BURP1 1 249
SEQADV 3FDZ MET A -7 UNP Q3JWH7 EXPRESSION TAG
SEQADV 3FDZ ALA A -6 UNP Q3JWH7 EXPRESSION TAG
SEQADV 3FDZ HIS A -5 UNP Q3JWH7 EXPRESSION TAG
SEQADV 3FDZ HIS A -4 UNP Q3JWH7 EXPRESSION TAG
SEQADV 3FDZ HIS A -3 UNP Q3JWH7 EXPRESSION TAG
SEQADV 3FDZ HIS A -2 UNP Q3JWH7 EXPRESSION TAG
SEQADV 3FDZ HIS A -1 UNP Q3JWH7 EXPRESSION TAG
SEQADV 3FDZ HIS A 0 UNP Q3JWH7 EXPRESSION TAG
SEQADV 3FDZ MET B -7 UNP Q3JWH7 EXPRESSION TAG
SEQADV 3FDZ ALA B -6 UNP Q3JWH7 EXPRESSION TAG
SEQADV 3FDZ HIS B -5 UNP Q3JWH7 EXPRESSION TAG
SEQADV 3FDZ HIS B -4 UNP Q3JWH7 EXPRESSION TAG
SEQADV 3FDZ HIS B -3 UNP Q3JWH7 EXPRESSION TAG
SEQADV 3FDZ HIS B -2 UNP Q3JWH7 EXPRESSION TAG
SEQADV 3FDZ HIS B -1 UNP Q3JWH7 EXPRESSION TAG
SEQADV 3FDZ HIS B 0 UNP Q3JWH7 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 NEP 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
MODRES 3FDZ NEP B 9 HIS N1-PHOSPHONOHISTIDINE
HET NEP B 9 14
HET DG2 A1001 15
HET PEG A1002 7
HET 3PG B1001 11
HET PEG B1002 7
HETNAM NEP N1-PHOSPHONOHISTIDINE
HETNAM DG2 2,3-DIPHOSPHOGLYCERIC ACID
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM 3PG 3-PHOSPHOGLYCERIC ACID
FORMUL 2 NEP C6 H10 N3 O5 P
FORMUL 3 DG2 C3 H8 O10 P2
FORMUL 4 PEG 2(C4 H10 O3)
FORMUL 5 3PG C3 H7 O7 P
FORMUL 7 HOH *223(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 GLY A 174 1 9
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 GLY B 47 1 19
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
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 LEU A 178 N TYR A 54
SHEET 4 A 6 TYR A 2 ARG A 8 1 N VAL A 5 O ILE A 179
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 THR B 55 O VAL B 80
SHEET 3 B 6 VAL B 177 ALA B 181 1 O LEU B 178 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 PRO B 211 LEU B 216 -1 O LEU B 216 N TYR B 2
SHEET 6 B 6 PRO B 222 TYR B 227 -1 O TYR B 226 N VAL B 213
LINK C ARG B 8 N NEP B 9 1555 1555 1.34
LINK C NEP B 9 N GLY B 10 1555 1555 1.32
SITE 1 AC1 17 ARG A 8 HIS A 9 ASN A 15 THR A 21
SITE 2 AC1 17 GLY A 22 ARG A 60 GLU A 87 TYR A 90
SITE 3 AC1 17 LYS A 98 ARG A 114 ARG A 115 HIS A 182
SITE 4 AC1 17 GLY A 183 ASN A 184 HOH A 349 HOH A 350
SITE 5 AC1 17 HOH A 355
SITE 1 AC2 6 ASP A 194 LEU A 204 TYR A 214 HIS A 225
SITE 2 AC2 6 TYR A 227 HOH A 259
SITE 1 AC3 12 NEP B 9 ARG B 19 PHE B 20 THR B 21
SITE 2 AC3 12 GLY B 22 GLU B 87 TYR B 90 LYS B 98
SITE 3 AC3 12 ARG B 114 ARG B 115 ASN B 184 HOH B 330
SITE 1 AC4 6 ILE B 190 LEU B 204 TYR B 214 HIS B 225
SITE 2 AC4 6 TYR B 227 HOH B 366
CRYST1 44.390 48.480 62.090 106.03 91.54 107.50 P 1 1
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 0.022528 0.007103 0.002853 0.00000
SCALE2 0.000000 0.021628 0.006755 0.00000
SCALE3 0.000000 0.000000 0.016879 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
