HEADER ISOMERASE 20-MAR-09 3GP3
TITLE CRYSTAL STRUCTURE OF PHOSPHOGLYCEROMUTASE FROM BURKHOLDERIA
TITLE 2 PSEUDOMALLEI WITH 2-PHOSPHOSERINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2,3-BISPHOSPHOGLYCERATE-DEPENDENT PHOSPHOGLYCERATE MUTASE;
COMPND 3 CHAIN: A, B, C, D;
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 PHOSPHOGLYCEROMUTASE, DECODE, SBRI, NIAID, UWPPG, GLYCOLYSIS,
KEYWDS 2 ISOMERASE, STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER
KEYWDS 3 FOR INFECTIOUS DISEASE, SSGCID
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 3 05-OCT-11 3GP3 1 JRNL VERSN
REVDAT 2 07-APR-09 3GP3 1 REMARK
REVDAT 1 31-MAR-09 3GP3 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. 1.50 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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 3 NUMBER OF REFLECTIONS : 148953
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) : 0.238
REMARK 3 R VALUE (WORKING SET) : 0.237
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7460
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8972
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.72
REMARK 3 BIN R VALUE (WORKING SET) : 0.4290
REMARK 3 BIN FREE R VALUE SET COUNT : 474
REMARK 3 BIN FREE R VALUE : 0.4250
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7298
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 138
REMARK 3 SOLVENT ATOMS : 712
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.76000
REMARK 3 B22 (A**2) : 0.03000
REMARK 3 B33 (A**2) : 1.02000
REMARK 3 B12 (A**2) : -0.12000
REMARK 3 B13 (A**2) : 0.21000
REMARK 3 B23 (A**2) : 0.53000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.102
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.100
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.070
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.939
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7747 ; 0.027 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 5279 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10554 ; 2.114 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12812 ; 1.099 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 944 ; 6.571 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 358 ;36.284 ;23.184
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1246 ;14.056 ;15.048
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 68 ;16.972 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1146 ; 0.139 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8590 ; 0.013 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1574 ; 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): 4692 ; 1.401 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1870 ; 0.468 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7576 ; 2.266 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3055 ; 3.465 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2978 ; 5.334 ; 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 3GP3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAR-09.
REMARK 100 THE RCSB ID CODE IS RCSB052138.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-DEC-08
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL2000
REMARK 200 DATA SCALING SOFTWARE : HKL2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 149575
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
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 (%) : 95.3
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.0620
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.59800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
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 (%): 43.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: EMERALD CRYO B-4: 100MM MES PH 7.5, 5%
REMARK 280 PEG 1000, 10% GLYCEROL, 30% PEG 600, 11.7 MG/ML PROTEIN, VAPOR
REMARK 280 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, 3, 4
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: MONOMERIC
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 ASP A 230
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 465 MET C -7
REMARK 465 ALA C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 HIS C -3
REMARK 465 HIS C -2
REMARK 465 HIS C -1
REMARK 465 HIS C 0
REMARK 465 GLN C 231
REMARK 465 GLU C 232
REMARK 465 ALA C 233
REMARK 465 ILE C 234
REMARK 465 ALA C 235
REMARK 465 LYS C 236
REMARK 465 ALA C 237
REMARK 465 GLN C 238
REMARK 465 ALA C 239
REMARK 465 ALA C 240
REMARK 465 VAL C 241
REMARK 465 ALA C 242
REMARK 465 GLN C 243
REMARK 465 GLN C 244
REMARK 465 GLY C 245
REMARK 465 LYS C 246
REMARK 465 SER C 247
REMARK 465 ALA C 248
REMARK 465 ALA C 249
REMARK 465 MET D -7
REMARK 465 ALA D -6
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 HIS D -3
REMARK 465 HIS D -2
REMARK 465 HIS D -1
REMARK 465 HIS D 0
REMARK 465 GLN D 231
REMARK 465 GLU D 232
REMARK 465 ALA D 233
REMARK 465 ILE D 234
REMARK 465 ALA D 235
REMARK 465 LYS D 236
REMARK 465 ALA D 237
REMARK 465 GLN D 238
REMARK 465 ALA D 239
REMARK 465 ALA D 240
REMARK 465 VAL D 241
REMARK 465 ALA D 242
REMARK 465 GLN D 243
REMARK 465 GLN D 244
REMARK 465 GLY D 245
REMARK 465 LYS D 246
REMARK 465 SER D 247
REMARK 465 ALA D 248
REMARK 465 ALA D 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 ASP A 118 CG OD1 OD2
REMARK 470 GLU A 129 CG CD OE1 OE2
REMARK 470 LYS A 140 CG CD CE NZ
REMARK 470 GLU A 218 CG CD OE1 OE2
REMARK 470 ASP B 118 CG OD1 OD2
REMARK 470 GLU B 129 CG CD OE1 OE2
REMARK 470 LYS B 140 CG CD CE NZ
REMARK 470 GLU B 218 CG CD OE1 OE2
REMARK 470 GLN C 38 CG CD OE1 NE2
REMARK 470 GLU C 129 CG CD OE1 OE2
REMARK 470 LYS C 140 CG CD CE NZ
REMARK 470 GLN D 38 CG CD OE1 NE2
REMARK 470 GLU D 129 CG CD OE1 OE2
REMARK 470 LYS D 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 31 O HOH A 602 1.78
REMARK 500 O HOH B 541 O HOH C 501 1.95
REMARK 500 NE2 HIS D 9 P PO3 D 252 2.00
REMARK 500 NE2 HIS C 9 P PO3 C 252 2.00
REMARK 500 NE2 HIS B 9 P PO3 B 251 2.00
REMARK 500 NE2 HIS A 9 P PO3 A 251 2.01
REMARK 500 OH TYR B 117 O HOH B 650 2.03
REMARK 500 OH TYR B 192 O HOH B 421 2.09
REMARK 500 OE1 GLU C 30 O HOH C 534 2.10
REMARK 500 O HOH D 321 O HOH D 400 2.11
REMARK 500 O THR D 149 O HOH D 691 2.16
REMARK 500 OE1 GLN A 31 NH1 ARG A 34 2.18
REMARK 500 O HOH B 281 O HOH B 434 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP A 66 CZ3 TRP A 66 CH2 -0.098
REMARK 500 GLU A 87 CD GLU A 87 OE2 -0.070
REMARK 500 GLU B 30 CD GLU B 30 OE2 0.069
REMARK 500 PRO C 78 CG PRO C 78 CD -0.216
REMARK 500 CYS C 151 CB CYS C 151 SG -0.215
REMARK 500 VAL D 77 CB VAL D 77 CG1 0.178
REMARK 500 GLU D 150 CA GLU D 150 CB 0.180
REMARK 500 CYS D 151 CB CYS D 151 SG -0.107
REMARK 500 ASP D 194 CB ASP D 194 CG 0.127
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 84 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ASP A 198 CB - CG - OD1 ANGL. DEV. = 7.6 DEGREES
REMARK 500 ASP B 128 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG B 143 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG B 187 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ASP B 217 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 LEU C 42 CA - CB - CG ANGL. DEV. = 16.3 DEGREES
REMARK 500 TYR C 138 CD1 - CE1 - CZ ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG C 158 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG C 158 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG C 187 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG D 60 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 GLU D 150 N - CA - CB ANGL. DEV. = 14.7 DEGREES
REMARK 500 ARG D 187 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ASP D 194 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
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 SER A 166 -51.45 -138.71
REMARK 500 ALA A 181 -140.57 -147.01
REMARK 500 ALA B 181 -139.29 -148.11
REMARK 500 SER C 166 -53.08 -132.11
REMARK 500 ALA C 181 -141.34 -145.32
REMARK 500 ASN D 86 151.83 -47.48
REMARK 500 SER D 166 -53.58 -133.34
REMARK 500 ALA D 181 -143.23 -151.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO3 A 251
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SEP A 252
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO3 B 251
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SEP B 252
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 C 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 C 251
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO3 C 252
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SEP C 253
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 D 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 D 251
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO3 D 252
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SEP D 253
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3EZN RELATED DB: PDB
REMARK 900 APO STRUCTURE
REMARK 900 RELATED ID: 3FDZ RELATED DB: PDB
REMARK 900 STRUCTURE WITH 2,3-DIPHOSPHOGLYCERIC ACID IN ONE MOLECULE
REMARK 900 AND 3-PHOSPHOGLYCERIC ACID IN THE OTHER
REMARK 900 RELATED ID: BUPSA.00114.A RELATED DB: TARGETDB
REMARK 900 RELATED ID: 3GP5 RELATED DB: PDB
REMARK 900 RELATED ID: 3GW8 RELATED DB: PDB
DBREF 3GP3 A 1 249 UNP Q63XU7 GPMA_BURPS 1 249
DBREF 3GP3 B 1 249 UNP Q63XU7 GPMA_BURPS 1 249
DBREF 3GP3 C 1 249 UNP Q63XU7 GPMA_BURPS 1 249
DBREF 3GP3 D 1 249 UNP Q63XU7 GPMA_BURPS 1 249
SEQADV 3GP3 MET A -7 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 ALA A -6 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 HIS A -5 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 HIS A -4 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 HIS A -3 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 HIS A -2 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 HIS A -1 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 HIS A 0 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 MET B -7 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 ALA B -6 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 HIS B -5 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 HIS B -4 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 HIS B -3 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 HIS B -2 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 HIS B -1 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 HIS B 0 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 MET C -7 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 ALA C -6 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 HIS C -5 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 HIS C -4 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 HIS C -3 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 HIS C -2 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 HIS C -1 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 HIS C 0 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 MET D -7 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 ALA D -6 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 HIS D -5 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 HIS D -4 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 HIS D -3 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 HIS D -2 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 HIS D -1 UNP Q63XU7 EXPRESSION TAG
SEQADV 3GP3 HIS D 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
SEQRES 1 C 257 MET ALA HIS HIS HIS HIS HIS HIS MET TYR LYS LEU VAL
SEQRES 2 C 257 LEU ILE ARG HIS GLY GLU SER THR TRP ASN LYS GLU ASN
SEQRES 3 C 257 ARG PHE THR GLY TRP VAL ASP VAL ASP LEU THR GLU GLN
SEQRES 4 C 257 GLY ASN ARG GLU ALA ARG GLN ALA GLY GLN LEU LEU LYS
SEQRES 5 C 257 GLU ALA GLY TYR THR PHE ASP ILE ALA TYR THR SER VAL
SEQRES 6 C 257 LEU LYS ARG ALA ILE ARG THR LEU TRP HIS VAL GLN ASP
SEQRES 7 C 257 GLN MET ASP LEU MET TYR VAL PRO VAL VAL HIS SER TRP
SEQRES 8 C 257 ARG LEU ASN GLU ARG HIS TYR GLY ALA LEU SER GLY LEU
SEQRES 9 C 257 ASN LYS ALA GLU THR ALA ALA LYS TYR GLY ASP GLU GLN
SEQRES 10 C 257 VAL LEU VAL TRP ARG ARG SER TYR ASP THR PRO PRO PRO
SEQRES 11 C 257 ALA LEU GLU PRO GLY ASP GLU ARG ALA PRO TYR ALA ASP
SEQRES 12 C 257 PRO ARG TYR ALA LYS VAL PRO ARG GLU GLN LEU PRO LEU
SEQRES 13 C 257 THR GLU CYS LEU LYS ASP THR VAL ALA ARG VAL LEU PRO
SEQRES 14 C 257 LEU TRP ASN GLU SER ILE ALA PRO ALA VAL LYS ALA GLY
SEQRES 15 C 257 LYS GLN VAL LEU ILE ALA ALA HIS GLY ASN SER LEU ARG
SEQRES 16 C 257 ALA LEU ILE LYS TYR LEU ASP GLY ILE SER ASP ALA ASP
SEQRES 17 C 257 ILE VAL GLY LEU ASN ILE PRO ASN GLY VAL PRO LEU VAL
SEQRES 18 C 257 TYR GLU LEU ASP GLU SER LEU THR PRO ILE ARG HIS TYR
SEQRES 19 C 257 TYR LEU GLY ASP GLN GLU ALA ILE ALA LYS ALA GLN ALA
SEQRES 20 C 257 ALA VAL ALA GLN GLN GLY LYS SER ALA ALA
SEQRES 1 D 257 MET ALA HIS HIS HIS HIS HIS HIS MET TYR LYS LEU VAL
SEQRES 2 D 257 LEU ILE ARG HIS GLY GLU SER THR TRP ASN LYS GLU ASN
SEQRES 3 D 257 ARG PHE THR GLY TRP VAL ASP VAL ASP LEU THR GLU GLN
SEQRES 4 D 257 GLY ASN ARG GLU ALA ARG GLN ALA GLY GLN LEU LEU LYS
SEQRES 5 D 257 GLU ALA GLY TYR THR PHE ASP ILE ALA TYR THR SER VAL
SEQRES 6 D 257 LEU LYS ARG ALA ILE ARG THR LEU TRP HIS VAL GLN ASP
SEQRES 7 D 257 GLN MET ASP LEU MET TYR VAL PRO VAL VAL HIS SER TRP
SEQRES 8 D 257 ARG LEU ASN GLU ARG HIS TYR GLY ALA LEU SER GLY LEU
SEQRES 9 D 257 ASN LYS ALA GLU THR ALA ALA LYS TYR GLY ASP GLU GLN
SEQRES 10 D 257 VAL LEU VAL TRP ARG ARG SER TYR ASP THR PRO PRO PRO
SEQRES 11 D 257 ALA LEU GLU PRO GLY ASP GLU ARG ALA PRO TYR ALA ASP
SEQRES 12 D 257 PRO ARG TYR ALA LYS VAL PRO ARG GLU GLN LEU PRO LEU
SEQRES 13 D 257 THR GLU CYS LEU LYS ASP THR VAL ALA ARG VAL LEU PRO
SEQRES 14 D 257 LEU TRP ASN GLU SER ILE ALA PRO ALA VAL LYS ALA GLY
SEQRES 15 D 257 LYS GLN VAL LEU ILE ALA ALA HIS GLY ASN SER LEU ARG
SEQRES 16 D 257 ALA LEU ILE LYS TYR LEU ASP GLY ILE SER ASP ALA ASP
SEQRES 17 D 257 ILE VAL GLY LEU ASN ILE PRO ASN GLY VAL PRO LEU VAL
SEQRES 18 D 257 TYR GLU LEU ASP GLU SER LEU THR PRO ILE ARG HIS TYR
SEQRES 19 D 257 TYR LEU GLY ASP GLN GLU ALA ILE ALA LYS ALA GLN ALA
SEQRES 20 D 257 ALA VAL ALA GLN GLN GLY LYS SER ALA ALA
HET PG4 A 250 13
HET PO3 A 251 4
HET SEP A 252 11
HET PG4 B 250 13
HET PO3 B 251 4
HET SEP B 252 11
HET PG4 C 250 13
HET PG4 C 251 13
HET PO3 C 252 4
HET SEP C 253 11
HET PG4 D 250 13
HET PG4 D 251 13
HET PO3 D 252 4
HET SEP D 253 11
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM PO3 PHOSPHITE ION
HETNAM SEP PHOSPHOSERINE
HETSYN SEP PHOSPHONOSERINE
FORMUL 5 PG4 6(C8 H18 O5)
FORMUL 6 PO3 4(O3 P 3-)
FORMUL 7 SEP 4(C3 H8 N O6 P)
FORMUL 19 HOH *712(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 ASP A 194 1 13
HELIX 13 13 ALA A 199 LEU A 204 5 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 ALA B 199 LEU B 204 5 6
HELIX 27 27 SER C 12 GLU C 17 1 6
HELIX 28 28 THR C 29 ALA C 46 1 18
HELIX 29 29 LEU C 58 ASP C 73 1 16
HELIX 30 30 TRP C 83 ASN C 86 5 4
HELIX 31 31 TYR C 90 SER C 94 5 5
HELIX 32 32 ASN C 97 GLY C 106 1 10
HELIX 33 33 GLY C 106 SER C 116 1 11
HELIX 34 34 ASP C 135 ALA C 139 5 5
HELIX 35 35 PRO C 142 LEU C 146 5 5
HELIX 36 36 CYS C 151 SER C 166 1 16
HELIX 37 37 SER C 166 ALA C 173 1 8
HELIX 38 38 HIS C 182 GLY C 195 1 14
HELIX 39 39 SER C 197 VAL C 202 1 6
HELIX 40 40 SER D 12 GLU D 17 1 6
HELIX 41 41 THR D 29 ALA D 46 1 18
HELIX 42 42 LEU D 58 ASP D 73 1 16
HELIX 43 43 TRP D 83 ASN D 86 5 4
HELIX 44 44 TYR D 90 SER D 94 5 5
HELIX 45 45 ASN D 97 GLY D 106 1 10
HELIX 46 46 GLY D 106 SER D 116 1 11
HELIX 47 47 ASP D 135 ALA D 139 5 5
HELIX 48 48 PRO D 142 LEU D 146 5 5
HELIX 49 49 CYS D 151 SER D 166 1 16
HELIX 50 50 SER D 166 ALA D 173 1 8
HELIX 51 51 HIS D 182 GLY D 195 1 14
HELIX 52 52 ASP D 200 LEU D 204 5 5
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 216 N TYR A 2
SHEET 6 A 6 PRO A 222 TYR A 227 -1 O TYR A 226 N VAL A 213
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
SHEET 1 C 6 VAL C 79 HIS C 81 0
SHEET 2 C 6 ILE C 52 THR C 55 1 N THR C 55 O VAL C 80
SHEET 3 C 6 VAL C 177 ALA C 181 1 O ALA C 180 N TYR C 54
SHEET 4 C 6 TYR C 2 ARG C 8 1 N ILE C 7 O ALA C 181
SHEET 5 C 6 LEU C 212 LEU C 216 -1 O LEU C 212 N LEU C 6
SHEET 6 C 6 PRO C 222 TYR C 227 -1 O TYR C 226 N VAL C 213
SHEET 1 D 6 VAL D 79 HIS D 81 0
SHEET 2 D 6 ILE D 52 THR D 55 1 N THR D 55 O VAL D 80
SHEET 3 D 6 VAL D 177 ALA D 181 1 O ALA D 180 N TYR D 54
SHEET 4 D 6 TYR D 2 ARG D 8 1 N ILE D 7 O ALA D 181
SHEET 5 D 6 LEU D 212 LEU D 216 -1 O LEU D 216 N TYR D 2
SHEET 6 D 6 PRO D 222 TYR D 227 -1 O TYR D 226 N VAL D 213
SITE 1 AC1 3 ASP A 51 ALA A 173 LYS A 175
SITE 1 AC2 9 ARG A 8 HIS A 9 ASN A 15 ARG A 60
SITE 2 AC2 9 GLU A 87 HIS A 182 GLY A 183 SEP A 252
SITE 3 AC2 9 HOH A 274
SITE 1 AC3 14 ARG A 8 ASN A 15 ARG A 19 THR A 21
SITE 2 AC3 14 GLY A 22 GLU A 87 ARG A 88 TYR A 90
SITE 3 AC3 14 LYS A 98 ARG A 114 ARG A 115 ASN A 184
SITE 4 AC3 14 PO3 A 251 HOH A 278
SITE 1 AC4 3 ASP B 51 ALA B 173 LYS B 175
SITE 1 AC5 9 ARG B 8 HIS B 9 ASN B 15 ARG B 60
SITE 2 AC5 9 GLU B 87 HIS B 182 GLY B 183 SEP B 252
SITE 3 AC5 9 HOH B 279
SITE 1 AC6 13 ARG B 8 ASN B 15 ARG B 19 THR B 21
SITE 2 AC6 13 GLY B 22 GLU B 87 TYR B 90 LYS B 98
SITE 3 AC6 13 ARG B 114 ARG B 115 ASN B 184 PO3 B 251
SITE 4 AC6 13 HOH B 299
SITE 1 AC7 4 ASP C 51 ALA C 173 LYS C 175 HOH C 552
SITE 1 AC8 5 ILE C 196 LEU C 204 HIS C 225 HOH C 332
SITE 2 AC8 5 HOH C 556
SITE 1 AC9 8 ARG C 8 HIS C 9 ASN C 15 ARG C 60
SITE 2 AC9 8 GLU C 87 HIS C 182 GLY C 183 SEP C 253
SITE 1 BC1 14 ARG C 8 ASN C 15 ARG C 19 PHE C 20
SITE 2 BC1 14 THR C 21 GLY C 22 GLU C 87 TYR C 90
SITE 3 BC1 14 LYS C 98 ARG C 114 ARG C 115 ASN C 184
SITE 4 BC1 14 PO3 C 252 HOH C 305
SITE 1 BC2 4 ASP D 51 ALA D 173 LYS D 175 HOH D 601
SITE 1 BC3 8 ILE D 190 ILE D 196 TYR D 214 HIS D 225
SITE 2 BC3 8 TYR D 227 HOH D 282 HOH D 374 HOH D 706
SITE 1 BC4 9 ARG D 8 HIS D 9 ASN D 15 ARG D 60
SITE 2 BC4 9 GLU D 87 HIS D 182 GLY D 183 SEP D 253
SITE 3 BC4 9 HOH D 290
SITE 1 BC5 14 ARG D 8 ASN D 15 ARG D 19 PHE D 20
SITE 2 BC5 14 THR D 21 GLY D 22 GLU D 87 TYR D 90
SITE 3 BC5 14 LYS D 98 ARG D 114 ARG D 115 ASN D 184
SITE 4 BC5 14 PO3 D 252 HOH D 295
CRYST1 49.263 72.045 78.036 107.96 93.00 104.20 P 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 0.020299 0.005137 0.002935 0.00000
SCALE2 0.000000 0.014318 0.005035 0.00000
SCALE3 0.000000 0.000000 0.013603 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
