HEADER ISOMERASE 20-APR-19 6JWK
TITLE CRYSTAL STRUCTURE OF MALEYLPYRUVATE ISOMERASE FROM PSEUDOMONAS
TITLE 2 AERUGINOSA PAO1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE GLUTATHIONE S-TRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: MALEYLPYRUVATE ISOMERASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA (STRAIN ATCC 15692 / DSM
SOURCE 3 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1);
SOURCE 4 ORGANISM_TAXID: 208964;
SOURCE 5 STRAIN: ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228
SOURCE 6 / 1C / PRS 101 / PAO1;
SOURCE 7 GENE: PA2473;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.HONG,H.SEO,K.-J.KIM
REVDAT 3 22-NOV-23 6JWK 1 REMARK
REVDAT 2 12-JUN-19 6JWK 1 JRNL
REVDAT 1 29-MAY-19 6JWK 0
JRNL AUTH H.HONG,H.SEO,K.J.KIM
JRNL TITL STRUCTURE AND BIOCHEMICAL STUDIES OF A PSEUDOMONAD
JRNL TITL 2 MALEYLPYRUVATE ISOMERASE FROM PSEUDOMONAS AERUGINOSA PAO1.
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 514 991 2019
JRNL REFN ESSN 1090-2104
JRNL PMID 31092332
JRNL DOI 10.1016/J.BBRC.2019.05.048
REMARK 2
REMARK 2 RESOLUTION. 1.86 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0238
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) : 1.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.78
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 50772
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) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2633
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) : 1.86
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3462
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.28
REMARK 3 BIN R VALUE (WORKING SET) : 0.3350
REMARK 3 BIN FREE R VALUE SET COUNT : 172
REMARK 3 BIN FREE R VALUE : 0.3690
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3016
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 39
REMARK 3 SOLVENT ATOMS : 149
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.91
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.46000
REMARK 3 B22 (A**2) : 0.46000
REMARK 3 B33 (A**2) : -0.92000
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): 0.107
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.108
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.078
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.745
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3112 ; 0.012 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 2956 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4231 ; 1.785 ; 1.637
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6795 ; 1.454 ; 1.568
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 380 ; 6.300 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 180 ;33.040 ;20.222
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 491 ;14.073 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;20.359 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 388 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3476 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 690 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 U VALUES: REFINED INDIVIDUALLY
REMARK 4
REMARK 4 6JWK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-MAY-19.
REMARK 100 THE DEPOSITION ID IS D_1300011921.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-MAY-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
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 : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53417
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.860
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 (%) : 96.9
REMARK 200 DATA REDUNDANCY : 15.40
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.89
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.1
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.30500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 1FW1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, LITHIUM SULFATE, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 92.36250
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 41.51100
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 41.51100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 138.54375
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 41.51100
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 41.51100
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 46.18125
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 41.51100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.51100
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 138.54375
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 41.51100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.51100
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 46.18125
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 92.36250
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: 5160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 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 VAL A 31
REMARK 465 ASN A 32
REMARK 465 LEU A 33
REMARK 465 ARG A 34
REMARK 465 GLN A 35
REMARK 465 GLY A 36
REMARK 465 GLU A 37
REMARK 465 GLN A 38
REMARK 465 LEU A 39
REMARK 465 ARG A 40
REMARK 465 PRO A 41
REMARK 465 ALA A 42
REMARK 465 ASP A 43
REMARK 465 ARG A 44
REMARK 465 GLN A 45
REMARK 465 ARG A 46
REMARK 465 ASN A 47
REMARK 465 PRO A 48
REMARK 465 MET A 49
REMARK 465 GLY A 50
REMARK 465 ALA A 51
REMARK 465 PRO A 213
REMARK 465 ASP A 214
REMARK 465 LEU A 215
REMARK 465 GLU A 216
REMARK 465 HIS A 217
REMARK 465 HIS A 218
REMARK 465 HIS A 219
REMARK 465 HIS A 220
REMARK 465 HIS A 221
REMARK 465 HIS A 222
REMARK 465 ASN B 32
REMARK 465 LEU B 33
REMARK 465 ARG B 34
REMARK 465 GLN B 35
REMARK 465 GLY B 36
REMARK 465 GLU B 37
REMARK 465 GLN B 38
REMARK 465 LEU B 39
REMARK 465 ARG B 40
REMARK 465 PRO B 41
REMARK 465 ALA B 42
REMARK 465 ASP B 43
REMARK 465 ARG B 44
REMARK 465 GLN B 45
REMARK 465 ARG B 46
REMARK 465 ASN B 47
REMARK 465 PRO B 48
REMARK 465 MET B 49
REMARK 465 GLY B 50
REMARK 465 PRO B 213
REMARK 465 ASP B 214
REMARK 465 LEU B 215
REMARK 465 GLU B 216
REMARK 465 HIS B 217
REMARK 465 HIS B 218
REMARK 465 HIS B 219
REMARK 465 HIS B 220
REMARK 465 HIS B 221
REMARK 465 HIS B 222
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 GLU B 95 CD GLU B 95 OE2 0.068
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 GLN A 77 87.80 -150.81
REMARK 500 GLN B 65 103.93 78.81
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 GOL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 303
DBREF 6JWK A 1 214 UNP Q9I109 Q9I109_PSEAE 1 214
DBREF 6JWK B 1 214 UNP Q9I109 Q9I109_PSEAE 1 214
SEQADV 6JWK LEU A 215 UNP Q9I109 EXPRESSION TAG
SEQADV 6JWK GLU A 216 UNP Q9I109 EXPRESSION TAG
SEQADV 6JWK HIS A 217 UNP Q9I109 EXPRESSION TAG
SEQADV 6JWK HIS A 218 UNP Q9I109 EXPRESSION TAG
SEQADV 6JWK HIS A 219 UNP Q9I109 EXPRESSION TAG
SEQADV 6JWK HIS A 220 UNP Q9I109 EXPRESSION TAG
SEQADV 6JWK HIS A 221 UNP Q9I109 EXPRESSION TAG
SEQADV 6JWK HIS A 222 UNP Q9I109 EXPRESSION TAG
SEQADV 6JWK LEU B 215 UNP Q9I109 EXPRESSION TAG
SEQADV 6JWK GLU B 216 UNP Q9I109 EXPRESSION TAG
SEQADV 6JWK HIS B 217 UNP Q9I109 EXPRESSION TAG
SEQADV 6JWK HIS B 218 UNP Q9I109 EXPRESSION TAG
SEQADV 6JWK HIS B 219 UNP Q9I109 EXPRESSION TAG
SEQADV 6JWK HIS B 220 UNP Q9I109 EXPRESSION TAG
SEQADV 6JWK HIS B 221 UNP Q9I109 EXPRESSION TAG
SEQADV 6JWK HIS B 222 UNP Q9I109 EXPRESSION TAG
SEQRES 1 A 222 MET GLN LEU TYR SER PHE PHE ASN SER SER THR SER TYR
SEQRES 2 A 222 ARG VAL ARG ILE ALA LEU ALA LEU LYS GLY LEU ASP TYR
SEQRES 3 A 222 GLN VAL VAL PRO VAL ASN LEU ARG GLN GLY GLU GLN LEU
SEQRES 4 A 222 ARG PRO ALA ASP ARG GLN ARG ASN PRO MET GLY ALA LEU
SEQRES 5 A 222 PRO THR LEU VAL ASP ALA ASP GLY ARG ARG PHE SER GLN
SEQRES 6 A 222 SER LEU ALA ILE ILE ASP TYR LEU ASP ALA VAL GLN PRO
SEQRES 7 A 222 GLU PRO ARG LEU ILE PRO LEU ASP PRO LEU HIS ARG ALA
SEQRES 8 A 222 GLN ALA LEU GLU LEU ALA LEU LEU VAL ALA CYS ASP ILE
SEQRES 9 A 222 HIS PRO LEU ASN ASN VAL ARG VAL LEU LYS TYR LEU THR
SEQRES 10 A 222 GLN VAL LEU GLY ILE ASP ALA GLU ASP ARG GLN ARG TRP
SEQRES 11 A 222 TYR ALA HIS TRP VAL ALA GLU GLY LEU ALA ALA ALA GLU
SEQRES 12 A 222 THR LEU LEU ASN ARG HIS ARG ARG GLY ALA PHE PHE ALA
SEQRES 13 A 222 GLY ALA ALA ALA GLY ILE VAL GLU CYS CYS LEU VAL PRO
SEQRES 14 A 222 GLN LEU ALA ASN ALA ARG ARG MET GLY CYS ASP LEU ALA
SEQRES 15 A 222 PRO TYR PRO ALA LEU LEU GLU LEU GLU GLY ARG CYS LEU
SEQRES 16 A 222 ALA LEU GLU ALA PHE GLN ARG ALA SER PRO GLU ARG GLN
SEQRES 17 A 222 PRO ASP TYR LEU PRO ASP LEU GLU HIS HIS HIS HIS HIS
SEQRES 18 A 222 HIS
SEQRES 1 B 222 MET GLN LEU TYR SER PHE PHE ASN SER SER THR SER TYR
SEQRES 2 B 222 ARG VAL ARG ILE ALA LEU ALA LEU LYS GLY LEU ASP TYR
SEQRES 3 B 222 GLN VAL VAL PRO VAL ASN LEU ARG GLN GLY GLU GLN LEU
SEQRES 4 B 222 ARG PRO ALA ASP ARG GLN ARG ASN PRO MET GLY ALA LEU
SEQRES 5 B 222 PRO THR LEU VAL ASP ALA ASP GLY ARG ARG PHE SER GLN
SEQRES 6 B 222 SER LEU ALA ILE ILE ASP TYR LEU ASP ALA VAL GLN PRO
SEQRES 7 B 222 GLU PRO ARG LEU ILE PRO LEU ASP PRO LEU HIS ARG ALA
SEQRES 8 B 222 GLN ALA LEU GLU LEU ALA LEU LEU VAL ALA CYS ASP ILE
SEQRES 9 B 222 HIS PRO LEU ASN ASN VAL ARG VAL LEU LYS TYR LEU THR
SEQRES 10 B 222 GLN VAL LEU GLY ILE ASP ALA GLU ASP ARG GLN ARG TRP
SEQRES 11 B 222 TYR ALA HIS TRP VAL ALA GLU GLY LEU ALA ALA ALA GLU
SEQRES 12 B 222 THR LEU LEU ASN ARG HIS ARG ARG GLY ALA PHE PHE ALA
SEQRES 13 B 222 GLY ALA ALA ALA GLY ILE VAL GLU CYS CYS LEU VAL PRO
SEQRES 14 B 222 GLN LEU ALA ASN ALA ARG ARG MET GLY CYS ASP LEU ALA
SEQRES 15 B 222 PRO TYR PRO ALA LEU LEU GLU LEU GLU GLY ARG CYS LEU
SEQRES 16 B 222 ALA LEU GLU ALA PHE GLN ARG ALA SER PRO GLU ARG GLN
SEQRES 17 B 222 PRO ASP TYR LEU PRO ASP LEU GLU HIS HIS HIS HIS HIS
SEQRES 18 B 222 HIS
HET GOL A 301 6
HET GOL A 302 6
HET SO4 A 303 5
HET SO4 A 304 5
HET GOL B 301 6
HET GOL B 302 6
HET SO4 B 303 5
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 4(C3 H8 O3)
FORMUL 5 SO4 3(O4 S 2-)
FORMUL 10 HOH *149(H2 O)
HELIX 1 AA1 SER A 9 GLY A 23 1 15
HELIX 2 AA2 GLN A 65 GLN A 77 1 13
HELIX 3 AA3 ASP A 86 ILE A 104 1 19
HELIX 4 AA4 ILE A 104 ASN A 109 1 6
HELIX 5 AA5 ASN A 109 VAL A 119 1 11
HELIX 6 AA6 ASP A 123 ARG A 150 1 28
HELIX 7 AA7 GLY A 161 MET A 177 1 17
HELIX 8 AA8 TYR A 184 ALA A 196 1 13
HELIX 9 AA9 LEU A 197 SER A 204 1 8
HELIX 10 AB1 PRO A 205 GLN A 208 5 4
HELIX 11 AB2 SER B 9 GLY B 23 1 15
HELIX 12 AB3 LEU B 24 TYR B 26 5 3
HELIX 13 AB4 GLN B 65 GLN B 77 1 13
HELIX 14 AB5 ASP B 86 ILE B 104 1 19
HELIX 15 AB6 ILE B 104 ASN B 109 1 6
HELIX 16 AB7 ASN B 109 GLY B 121 1 13
HELIX 17 AB8 ASP B 123 ARG B 150 1 28
HELIX 18 AB9 GLY B 161 MET B 177 1 17
HELIX 19 AC1 TYR B 184 ALA B 196 1 13
HELIX 20 AC2 LEU B 197 SER B 204 1 8
HELIX 21 AC3 PRO B 205 GLN B 208 5 4
SHEET 1 AA1 4 GLN A 27 VAL A 29 0
SHEET 2 AA1 4 GLN A 2 TYR A 4 1 N LEU A 3 O VAL A 29
SHEET 3 AA1 4 THR A 54 VAL A 56 -1 O THR A 54 N TYR A 4
SHEET 4 AA1 4 ARG A 62 PHE A 63 -1 O PHE A 63 N LEU A 55
SHEET 1 AA2 4 VAL B 28 PRO B 30 0
SHEET 2 AA2 4 GLN B 2 SER B 5 1 N LEU B 3 O VAL B 29
SHEET 3 AA2 4 THR B 54 VAL B 56 -1 O VAL B 56 N GLN B 2
SHEET 4 AA2 4 ARG B 62 PHE B 63 -1 O PHE B 63 N LEU B 55
CISPEP 1 LEU A 52 PRO A 53 0 -9.49
CISPEP 2 GLU A 79 PRO A 80 0 -11.63
CISPEP 3 LEU B 52 PRO B 53 0 -6.70
CISPEP 4 GLU B 79 PRO B 80 0 -11.93
SITE 1 AC1 8 TYR A 13 VAL A 168 LEU A 195 PRO A 205
SITE 2 AC1 8 GLU A 206 HOH A 406 ARG B 175 GOL B 302
SITE 1 AC2 3 LEU A 67 ARG A 90 ASP B 71
SITE 1 AC3 5 SER A 9 SER A 10 THR A 11 HIS A 105
SITE 2 AC3 5 ASN A 109
SITE 1 AC4 7 ARG A 61 ARG A 148 ARG B 62 GLN B 92
SITE 2 AC4 7 ARG B 148 HIS B 149 ARG B 151
SITE 1 AC5 4 LEU A 99 ASP A 103 HOH A 414 ARG B 111
SITE 1 AC6 5 LEU A 195 SER A 204 GOL A 301 ARG B 175
SITE 2 AC6 5 HOH B 410
SITE 1 AC7 6 SER B 9 SER B 10 THR B 11 HIS B 105
SITE 2 AC7 6 ASN B 109 VAL B 110
CRYST1 83.022 83.022 184.725 90.00 90.00 90.00 P 43 21 2 16
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 0.012045 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012045 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005413 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
