HEADER TRANSFERASE 20-MAY-15 4ZXG
TITLE LIGANDIN BINDING SITE OF PFGST
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONE S-TRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 3-207;
COMPND 5 SYNONYM: PFGST;
COMPND 6 EC: 2.5.1.18;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM;
SOURCE 3 ORGANISM_TAXID: 5833;
SOURCE 4 GENE: GST;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GST, PLASMODIUM FALCIPARUM, HEMIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.PERBANDT,R.EBERLE,C.BETZEL
REVDAT 4 10-JAN-24 4ZXG 1 REMARK
REVDAT 3 07-MAR-18 4ZXG 1 REMARK
REVDAT 2 09-SEP-15 4ZXG 1 JRNL
REVDAT 1 24-JUN-15 4ZXG 0
JRNL AUTH M.PERBANDT,R.EBERLE,L.FISCHER-RIEPE,H.CANG,E.LIEBAU,C.BETZEL
JRNL TITL HIGH RESOLUTION STRUCTURES OF PLASMODIUM FALCIPARUM GST
JRNL TITL 2 COMPLEXES PROVIDE NOVEL INSIGHTS INTO THE DIMER-TETRAMER
JRNL TITL 3 TRANSITION AND A NOVEL LIGAND-BINDING SITE.
JRNL REF J.STRUCT.BIOL. V. 191 365 2015
JRNL REFN ESSN 1095-8657
JRNL PMID 26072058
JRNL DOI 10.1016/J.JSB.2015.06.008
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 273546
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3161
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 56
REMARK 3 SOLVENT ATOMS : 273
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.46
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4ZXG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-MAY-15.
REMARK 100 THE DEPOSITION ID IS D_1000210043.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-OCT-12
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 : PETRA III, EMBL C/O DESY
REMARK 200 BEAMLINE : P14 (MX2)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.24
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 273546
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.02600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 30.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PHASER
REMARK 200 STARTING MODEL: 1PA3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, MES, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-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 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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 43.20000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.45000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 43.20000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.45000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -134.0 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 BIOMT1 2 -1.000000 0.000000 0.000000 172.80000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 60.90000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 432 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 449 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 443 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 448 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 510 LIES ON A SPECIAL POSITION.
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 ASN A 148
REMARK 465 ASP A 149
REMARK 465 SER A 178
REMARK 465 ASN B 38
REMARK 465 GLY B 39
REMARK 465 HIS B 143
REMARK 465 THR B 144
REMARK 465 ASN B 145
REMARK 465 ASN B 146
REMARK 465 ASN B 147
REMARK 465 ASN B 148
REMARK 465 PRO B 177
REMARK 465 SER B 178
REMARK 465 SER B 179
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 3 OD1
REMARK 470 ILE A 5 CD1
REMARK 470 VAL A 37 CG1
REMARK 470 LYS A 46 CD CE NZ
REMARK 470 LYS A 50 CG CD CE NZ
REMARK 470 GLU A 51 CG CD OE2
REMARK 470 LEU A 67 CD1
REMARK 470 LYS A 81 CD CE NZ
REMARK 470 LYS A 82 CE NZ
REMARK 470 GLU A 126 CD OE1 OE2
REMARK 470 LYS A 130 CE NZ
REMARK 470 LYS A 137 CD
REMARK 470 LYS A 140 CD CE NZ
REMARK 470 LYS A 141 NZ
REMARK 470 ASN A 142 CB
REMARK 470 THR A 144 C CB OG1 CG2
REMARK 470 ASN A 147 CB
REMARK 470 ASN A 156 OD1 ND2
REMARK 470 PRO A 177 CB CG CD
REMARK 470 SER A 179 CB OG
REMARK 470 LYS A 181 CB CG CD CE NZ
REMARK 470 LYS A 200 CD CE NZ
REMARK 470 ASN A 201 OD1
REMARK 470 ILE A 203 CD1
REMARK 470 ASN A 205 CG OD1 ND2
REMARK 470 LYS A 207 CA CB CG CD CE NZ
REMARK 470 ASP B 3 CB CG OD1
REMARK 470 ASN B 4 CA CB CG OD1 ND2
REMARK 470 ARG B 13 NH1 NH2
REMARK 470 ILE B 28 CD1
REMARK 470 GLU B 29 CD OE1 OE2
REMARK 470 LYS B 33 CD CE NZ
REMARK 470 VAL B 37 CG1 CG2
REMARK 470 ASP B 40 CG OD2
REMARK 470 VAL B 43 CG1 CG2
REMARK 470 LYS B 46 CD CE NZ
REMARK 470 LYS B 50 CE NZ
REMARK 470 GLU B 51 CG CD OE1 OE2
REMARK 470 LYS B 52 NZ
REMARK 470 ASP B 66 OD2
REMARK 470 LYS B 81 CD CE NZ
REMARK 470 LEU B 91 CG CD1 CD2
REMARK 470 GLU B 126 CG
REMARK 470 LYS B 137 CD CE NZ
REMARK 470 LYS B 140 CE NZ
REMARK 470 LYS B 141 CD CE NZ
REMARK 470 ASP B 149 C O CB CG OD1 OD2
REMARK 470 LYS B 150 N CA CB CG CD CE NZ
REMARK 470 TYR B 151 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR B 151 OH
REMARK 470 ASN B 156 OD1 ND2
REMARK 470 GLU B 173 OE2
REMARK 470 LYS B 181 CA CB CG CD CE NZ
REMARK 470 ASN B 182 CG OD1 ND2
REMARK 470 ASN B 190 CB CG OD1 ND2
REMARK 470 LYS B 200 CG CD CE NZ
REMARK 470 ASN B 205 OD1
REMARK 470 LYS B 207 CB 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 O HOH A 490 O HOH A 528 1.42
REMARK 500 O HOH A 504 O HOH A 528 1.69
REMARK 500 O HOH A 428 O HOH A 441 1.73
REMARK 500 O HOH A 466 O HOH A 531 2.05
REMARK 500 O HOH A 488 O HOH A 511 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O1 GOL B 302 O3 GOL B 302 2765 1.77
REMARK 500 O1 GOL B 302 O2 GOL B 302 2765 1.93
REMARK 500 O1 GOL B 302 C3 GOL B 302 2765 2.16
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 LEU A 124 N LEU A 124 CA 0.157
REMARK 500 LEU A 124 N LEU A 124 CA 0.159
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 LEU A 124 CA - C - N ANGL. DEV. = -13.6 DEGREES
REMARK 500 LEU A 124 CA - C - N ANGL. DEV. = -14.4 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 GLN A 71 104.23 83.62
REMARK 500 GLN A 71 106.66 83.62
REMARK 500 GLN B 71 110.20 82.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 LEU A 124 14.27
REMARK 500 LEU A 124 14.57
REMARK 500 THR B 113 12.88
REMARK 500 THR B 113 12.34
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 B 510 DISTANCE = 6.37 ANGSTROMS
REMARK 525 HOH B 516 DISTANCE = 6.51 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 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 GOL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand LYS B 181 bound to ASN A
REMARK 800 148
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand LYS B 181 bound to ASN A
REMARK 800 148
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand LYS B 181 bound to ASN A
REMARK 800 148
DBREF 4ZXG A 3 207 UNP Q8MU52 GST_PLAFA 3 207
DBREF 4ZXG B 3 207 UNP Q8MU52 GST_PLAFA 3 207
SEQRES 1 A 205 ASP ASN ILE VAL LEU TYR TYR PHE ASP ALA ARG GLY LYS
SEQRES 2 A 205 ALA GLU LEU ILE ARG LEU ILE PHE ALA TYR LEU GLY ILE
SEQRES 3 A 205 GLU TYR THR ASP LYS ARG PHE GLY VAL ASN GLY ASP ALA
SEQRES 4 A 205 PHE VAL GLU PHE LYS ASN PHE LYS LYS GLU LYS ASP THR
SEQRES 5 A 205 PRO PHE GLU GLN VAL PRO ILE LEU GLN ILE GLY ASP LEU
SEQRES 6 A 205 ILE LEU ALA GLN SER GLN ALA ILE VAL ARG TYR LEU SER
SEQRES 7 A 205 LYS LYS TYR ASN ILE CYS GLY GLU SER GLU LEU ASN GLU
SEQRES 8 A 205 PHE TYR ALA ASP MET ILE PHE CYS GLY VAL GLN ASP ILE
SEQRES 9 A 205 HIS TYR LYS PHE ASN ASN THR ASN LEU PHE LYS GLN ASN
SEQRES 10 A 205 GLU THR THR PHE LEU ASN GLU ASP LEU PRO LYS TRP SER
SEQRES 11 A 205 GLY TYR PHE GLU LYS LEU LEU LYS LYS ASN HIS THR ASN
SEQRES 12 A 205 ASN ASN ASN ASP LYS TYR TYR PHE VAL GLY ASN ASN LEU
SEQRES 13 A 205 THR TYR ALA ASP LEU ALA VAL PHE ASN LEU TYR ASP ASP
SEQRES 14 A 205 ILE GLU THR LYS TYR PRO SER SER LEU LYS ASN PHE PRO
SEQRES 15 A 205 LEU LEU LYS ALA HIS ASN GLU PHE ILE SER ASN LEU PRO
SEQRES 16 A 205 ASN ILE LYS ASN TYR ILE THR ASN ARG LYS
SEQRES 1 B 205 ASP ASN ILE VAL LEU TYR TYR PHE ASP ALA ARG GLY LYS
SEQRES 2 B 205 ALA GLU LEU ILE ARG LEU ILE PHE ALA TYR LEU GLY ILE
SEQRES 3 B 205 GLU TYR THR ASP LYS ARG PHE GLY VAL ASN GLY ASP ALA
SEQRES 4 B 205 PHE VAL GLU PHE LYS ASN PHE LYS LYS GLU LYS ASP THR
SEQRES 5 B 205 PRO PHE GLU GLN VAL PRO ILE LEU GLN ILE GLY ASP LEU
SEQRES 6 B 205 ILE LEU ALA GLN SER GLN ALA ILE VAL ARG TYR LEU SER
SEQRES 7 B 205 LYS LYS TYR ASN ILE CYS GLY GLU SER GLU LEU ASN GLU
SEQRES 8 B 205 PHE TYR ALA ASP MET ILE PHE CYS GLY VAL GLN ASP ILE
SEQRES 9 B 205 HIS TYR LYS PHE ASN ASN THR ASN LEU PHE LYS GLN ASN
SEQRES 10 B 205 GLU THR THR PHE LEU ASN GLU ASP LEU PRO LYS TRP SER
SEQRES 11 B 205 GLY TYR PHE GLU LYS LEU LEU LYS LYS ASN HIS THR ASN
SEQRES 12 B 205 ASN ASN ASN ASP LYS TYR TYR PHE VAL GLY ASN ASN LEU
SEQRES 13 B 205 THR TYR ALA ASP LEU ALA VAL PHE ASN LEU TYR ASP ASP
SEQRES 14 B 205 ILE GLU THR LYS TYR PRO SER SER LEU LYS ASN PHE PRO
SEQRES 15 B 205 LEU LEU LYS ALA HIS ASN GLU PHE ILE SER ASN LEU PRO
SEQRES 16 B 205 ASN ILE LYS ASN TYR ILE THR ASN ARG LYS
HET SO4 A 301 5
HET SO4 A 302 5
HET SO4 A 303 5
HET GOL A 304 6
HET MES A 305 12
HET SO4 B 301 5
HET GOL B 302 6
HET MES B 303 12
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 SO4 4(O4 S 2-)
FORMUL 6 GOL 2(C3 H8 O3)
FORMUL 7 MES 2(C6 H13 N O4 S)
FORMUL 11 HOH *273(H2 O)
HELIX 1 AA1 ALA A 16 GLY A 27 1 12
HELIX 2 AA2 ASP A 40 LYS A 52 1 13
HELIX 3 AA3 GLN A 71 TYR A 83 1 13
HELIX 4 AA4 SER A 89 ASN A 112 1 24
HELIX 5 AA5 ASN A 119 ASP A 127 1 9
HELIX 6 AA6 ASP A 127 ASN A 142 1 16
HELIX 7 AA7 THR A 159 TYR A 176 1 18
HELIX 8 AA8 PHE A 183 ASN A 195 1 13
HELIX 9 AA9 LEU A 196 ARG A 206 1 11
HELIX 10 AB1 ALA B 16 GLY B 27 1 12
HELIX 11 AB2 ALA B 41 LYS B 52 1 12
HELIX 12 AB3 GLN B 71 TYR B 83 1 13
HELIX 13 AB4 SER B 89 ASN B 112 1 24
HELIX 14 AB5 ASN B 119 GLU B 126 1 8
HELIX 15 AB6 GLU B 126 ASN B 142 1 17
HELIX 16 AB7 THR B 159 TYR B 176 1 18
HELIX 17 AB8 PHE B 183 LEU B 196 1 14
HELIX 18 AB9 LEU B 196 ARG B 206 1 11
SHEET 1 AA1 4 THR A 31 PHE A 35 0
SHEET 2 AA1 4 ILE A 5 PHE A 10 1 N LEU A 7 O THR A 31
SHEET 3 AA1 4 ILE A 61 ILE A 64 -1 O GLN A 63 N VAL A 6
SHEET 4 AA1 4 LEU A 67 ALA A 70 -1 O LEU A 69 N LEU A 62
SHEET 1 AA2 4 THR B 31 PHE B 35 0
SHEET 2 AA2 4 VAL B 6 PHE B 10 1 N TYR B 9 O PHE B 35
SHEET 3 AA2 4 ILE B 61 ILE B 64 -1 O GLN B 63 N VAL B 6
SHEET 4 AA2 4 LEU B 67 ALA B 70 -1 O LEU B 67 N ILE B 64
CISPEP 1 VAL A 59 PRO A 60 0 9.28
CISPEP 2 VAL B 59 PRO B 60 0 7.93
SITE 1 AC1 2 TYR A 8 LYS A 52
SITE 1 AC2 1 MES A 305
SITE 1 AC3 3 TYR A 83 HOH A 406 ASN B 84
SITE 1 AC4 4 ASN A 84 GLU A 88 LYS B 82 TYR B 83
SITE 1 AC5 6 TYR A 25 LEU A 26 LEU A 196 PRO A 197
SITE 2 AC5 6 ASN A 198 SO4 A 302
SITE 1 AC6 7 LYS B 15 GLN B 71 SER B 72 GLN B 73
SITE 2 AC6 7 HOH B 405 HOH B 415 HOH B 432
SITE 1 AC7 3 TYR B 108 HOH B 408 HOH B 434
SITE 1 AC8 5 TYR B 25 LEU B 26 LEU B 196 PRO B 197
SITE 2 AC8 5 ASN B 198
SITE 1 AC9 4 ASN A 201 LEU B 180 ASN B 182 PHE B 183
SITE 1 AD1 4 ASN A 201 LEU B 180 ASN B 182 PHE B 183
SITE 1 AD2 4 ASN A 201 LEU B 180 ASN B 182 PHE B 183
CRYST1 86.400 60.900 74.800 90.00 90.00 90.00 P 21 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.011574 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016420 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013369 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
