HEADER TRANSFERASE 04-FEB-15 5AGY
TITLE CRYSTAL STRUCTURE OF A TAU CLASS GST MUTANT FROM GLYCINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONE S-TRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: GMGSTU4-MUTANT;
COMPND 5 EC: 2.5.1.18;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GLYCINE MAX;
SOURCE 3 ORGANISM_COMMON: SOYBEAN;
SOURCE 4 ORGANISM_TAXID: 3847;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSFERASE, BINDING SITE, CATALYTIC DOMAIN, ENZYME, INDUCTION,
KEYWDS 2 DETOXIFICATION, HERBICIDES, KINETICS, SITE-DIRECTED MUTAGENESIS, SOY
KEYWDS 3 BEANS, GLUTATHIONE TRANSFERASE, PROTEIN STABILITY, CATALYTIC
KEYWDS 4 MECHANISM, XENOBIOTIC BINDING, ALLOSTERISM
EXPDTA X-RAY DIFFRACTION
AUTHOR I.AXARLI,A.W.MULETA,D.VLACHAKIS,S.KOSSIDA,G.KOTZIA,P.DHAVALA,
AUTHOR 2 A.C.PAPAGEORGIOU,N.E.LABROU
REVDAT 4 10-JAN-24 5AGY 1 REMARK
REVDAT 3 17-JUL-19 5AGY 1 REMARK
REVDAT 2 09-MAR-16 5AGY 1 JRNL
REVDAT 1 16-DEC-15 5AGY 0
JRNL AUTH I.AXARLI,A.W.MULETA,D.VLACHAKIS,S.KOSSIDA,G.KOTZIA,
JRNL AUTH 2 A.MALTEZOS,P.DHAVALA,A.C.PAPAGEORGIOU,N.E.LABROU
JRNL TITL DIRECTED EVOLUTION OF TAU CLASS GLUTATHIONE TRANSFERASES
JRNL TITL 2 REVEALS A SITE THAT REGULATES CATALYTIC EFFICIENCY AND MASKS
JRNL TITL 3 COOPERATIVITY.
JRNL REF BIOCHEM.J. V. 473 559 2016
JRNL REFN ISSN 0264-6021
JRNL PMID 26637269
JRNL DOI 10.1042/BJ20150930
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.79
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 48816
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.187
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1999
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 19.7954 - 4.2052 1.00 3565 153 0.1621 0.1545
REMARK 3 2 4.2052 - 3.3430 1.00 3406 145 0.1435 0.1723
REMARK 3 3 3.3430 - 2.9220 1.00 3391 145 0.1720 0.1860
REMARK 3 4 2.9220 - 2.6555 1.00 3370 144 0.1693 0.1983
REMARK 3 5 2.6555 - 2.4655 1.00 3356 143 0.1634 0.1664
REMARK 3 6 2.4655 - 2.3204 1.00 3335 142 0.1581 0.1723
REMARK 3 7 2.3204 - 2.2044 1.00 3336 143 0.1609 0.2181
REMARK 3 8 2.2044 - 2.1085 1.00 3315 141 0.1681 0.1973
REMARK 3 9 2.1085 - 2.0274 0.99 3309 142 0.1678 0.2058
REMARK 3 10 2.0274 - 1.9575 1.00 3310 142 0.1725 0.2047
REMARK 3 11 1.9575 - 1.8964 1.00 3299 140 0.1837 0.2448
REMARK 3 12 1.8964 - 1.8422 0.99 3308 140 0.2034 0.2363
REMARK 3 13 1.8422 - 1.7937 0.99 3287 141 0.2227 0.2510
REMARK 3 14 1.7937 - 1.7500 0.98 3230 138 0.2491 0.3057
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.39
REMARK 3 B_SOL : 47.86
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.630
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.014 4062
REMARK 3 ANGLE : 1.002 5262
REMARK 3 CHIRALITY : 0.068 557
REMARK 3 PLANARITY : 0.004 671
REMARK 3 DIHEDRAL : 12.909 1525
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5AGY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-FEB-15.
REMARK 100 THE DEPOSITION ID IS D_1290062925.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-MAY-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW7A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48837
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 19.790
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 6.950
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : 0.45000
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: PDB ENTRY 1OYJ
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4K 27.5%, NH4OAC 0.2 M, NAOAC 0.1
REMARK 280 M, PH 5.0, 10 MM GTB
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 31.12050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.53900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.80100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.53900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.12050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.80100
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 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 MET B 1
REMARK 465 GLN B 2
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 GLU A 66 110.78 80.52
REMARK 500 ASN A 82 75.42 23.53
REMARK 500 GLU B 66 108.70 79.54
REMARK 500 ILE B 218 -78.51 -85.47
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 A2023 DISTANCE = 6.50 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4NM A 1220
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4NM A 1221
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTB A 1222
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTB B 1220
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4NM B 1221
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1223
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 1222
DBREF 5AGY A 3 219 UNP O49235 O49235_SOYBN 3 219
DBREF 5AGY B 3 219 UNP O49235 O49235_SOYBN 3 219
SEQADV 5AGY MET A 1 UNP O49235 EXPRESSION TAG
SEQADV 5AGY GLN A 2 UNP O49235 EXPRESSION TAG
SEQADV 5AGY GLN A 38 UNP O49235 ARG 38 ENGINEERED MUTATION
SEQADV 5AGY LYS A 46 UNP O49235 GLN 46 ENGINEERED MUTATION
SEQADV 5AGY CYS A 114 UNP O49235 TRP 114 ENGINEERED MUTATION
SEQADV 5AGY VAL A 183 UNP O49235 ILE 183 ENGINEERED MUTATION
SEQADV 5AGY MET B 1 UNP O49235 EXPRESSION TAG
SEQADV 5AGY GLN B 2 UNP O49235 EXPRESSION TAG
SEQADV 5AGY GLN B 38 UNP O49235 ARG 38 ENGINEERED MUTATION
SEQADV 5AGY LYS B 46 UNP O49235 GLN 46 ENGINEERED MUTATION
SEQADV 5AGY CYS B 114 UNP O49235 TRP 114 ENGINEERED MUTATION
SEQADV 5AGY VAL B 183 UNP O49235 ILE 183 ENGINEERED MUTATION
SEQRES 1 A 219 MET GLN ASP GLU VAL VAL LEU LEU ASP PHE TRP PRO SER
SEQRES 2 A 219 PRO PHE GLY MET ARG VAL ARG ILE ALA LEU ALA GLU LYS
SEQRES 3 A 219 GLY ILE LYS TYR GLU TYR LYS GLU GLU ASP LEU GLN ASN
SEQRES 4 A 219 LYS SER PRO LEU LEU LEU LYS MET ASN PRO VAL HIS LYS
SEQRES 5 A 219 LYS ILE PRO VAL LEU ILE HIS ASN GLY LYS PRO ILE CYS
SEQRES 6 A 219 GLU SER LEU ILE ALA VAL GLN TYR ILE GLU GLU VAL TRP
SEQRES 7 A 219 ASN ASP ARG ASN PRO LEU LEU PRO SER ASP PRO TYR GLN
SEQRES 8 A 219 ARG ALA GLN THR ARG PHE TRP ALA ASP TYR VAL ASP LYS
SEQRES 9 A 219 LYS ILE TYR ASP LEU GLY ARG LYS ILE CYS THR SER LYS
SEQRES 10 A 219 GLY GLU GLU LYS GLU ALA ALA LYS LYS GLU PHE ILE GLU
SEQRES 11 A 219 ALA LEU LYS LEU LEU GLU GLU GLN LEU GLY ASP LYS THR
SEQRES 12 A 219 TYR PHE GLY GLY ASP ASN LEU GLY PHE VAL ASP ILE ALA
SEQRES 13 A 219 LEU VAL PRO PHE TYR THR TRP PHE LYS ALA TYR GLU THR
SEQRES 14 A 219 PHE GLY THR LEU ASN ILE GLU SER GLU CYS PRO LYS PHE
SEQRES 15 A 219 VAL ALA TRP ALA LYS ARG CYS LEU GLN LYS GLU SER VAL
SEQRES 16 A 219 ALA LYS SER LEU PRO ASP GLN GLN LYS VAL TYR GLU PHE
SEQRES 17 A 219 ILE MET ASP LEU ARG LYS LYS LEU GLY ILE GLU
SEQRES 1 B 219 MET GLN ASP GLU VAL VAL LEU LEU ASP PHE TRP PRO SER
SEQRES 2 B 219 PRO PHE GLY MET ARG VAL ARG ILE ALA LEU ALA GLU LYS
SEQRES 3 B 219 GLY ILE LYS TYR GLU TYR LYS GLU GLU ASP LEU GLN ASN
SEQRES 4 B 219 LYS SER PRO LEU LEU LEU LYS MET ASN PRO VAL HIS LYS
SEQRES 5 B 219 LYS ILE PRO VAL LEU ILE HIS ASN GLY LYS PRO ILE CYS
SEQRES 6 B 219 GLU SER LEU ILE ALA VAL GLN TYR ILE GLU GLU VAL TRP
SEQRES 7 B 219 ASN ASP ARG ASN PRO LEU LEU PRO SER ASP PRO TYR GLN
SEQRES 8 B 219 ARG ALA GLN THR ARG PHE TRP ALA ASP TYR VAL ASP LYS
SEQRES 9 B 219 LYS ILE TYR ASP LEU GLY ARG LYS ILE CYS THR SER LYS
SEQRES 10 B 219 GLY GLU GLU LYS GLU ALA ALA LYS LYS GLU PHE ILE GLU
SEQRES 11 B 219 ALA LEU LYS LEU LEU GLU GLU GLN LEU GLY ASP LYS THR
SEQRES 12 B 219 TYR PHE GLY GLY ASP ASN LEU GLY PHE VAL ASP ILE ALA
SEQRES 13 B 219 LEU VAL PRO PHE TYR THR TRP PHE LYS ALA TYR GLU THR
SEQRES 14 B 219 PHE GLY THR LEU ASN ILE GLU SER GLU CYS PRO LYS PHE
SEQRES 15 B 219 VAL ALA TRP ALA LYS ARG CYS LEU GLN LYS GLU SER VAL
SEQRES 16 B 219 ALA LYS SER LEU PRO ASP GLN GLN LYS VAL TYR GLU PHE
SEQRES 17 B 219 ILE MET ASP LEU ARG LYS LYS LEU GLY ILE GLU
HET 4NM A1220 11
HET 4NM A1221 11
HET GTB A1222 30
HET PO4 A1223 5
HET GTB B1220 30
HET 4NM B1221 11
HET PO4 B1222 5
HETNAM 4NM 4-NITROPHENYL METHANETHIOL
HETNAM GTB S-(P-NITROBENZYL)GLUTATHIONE
HETNAM PO4 PHOSPHATE ION
FORMUL 3 4NM 3(C7 H8 N O2 S 1+)
FORMUL 5 GTB 2(C17 H22 N4 O8 S)
FORMUL 6 PO4 2(O4 P 3-)
FORMUL 10 HOH *410(H2 O)
HELIX 1 1 SER A 13 LYS A 26 1 14
HELIX 2 2 SER A 41 ASN A 48 1 8
HELIX 3 3 GLU A 66 TRP A 78 1 13
HELIX 4 4 ASP A 88 SER A 116 1 29
HELIX 5 5 LYS A 117 GLY A 140 1 24
HELIX 6 6 GLY A 151 VAL A 158 1 8
HELIX 7 7 PRO A 159 THR A 162 5 4
HELIX 8 8 TRP A 163 THR A 172 1 10
HELIX 9 9 ASN A 174 CYS A 179 1 6
HELIX 10 10 CYS A 179 GLN A 191 1 13
HELIX 11 11 LYS A 192 LYS A 197 1 6
HELIX 12 12 ASP A 201 LEU A 216 1 16
HELIX 13 13 SER B 13 GLY B 27 1 15
HELIX 14 14 SER B 41 ASN B 48 1 8
HELIX 15 15 GLU B 66 TRP B 78 1 13
HELIX 16 16 ASP B 88 SER B 116 1 29
HELIX 17 17 LYS B 117 GLY B 140 1 24
HELIX 18 18 GLY B 151 VAL B 158 1 8
HELIX 19 19 PRO B 159 THR B 162 5 4
HELIX 20 20 TRP B 163 THR B 172 1 10
HELIX 21 21 ASN B 174 CYS B 179 1 6
HELIX 22 22 CYS B 179 GLN B 191 1 13
HELIX 23 23 LYS B 192 LYS B 197 1 6
HELIX 24 24 ASP B 201 LEU B 216 1 16
SHEET 1 AA 4 GLU A 31 GLU A 34 0
SHEET 2 AA 4 VAL A 5 ASP A 9 1 O VAL A 5 N GLU A 31
SHEET 3 AA 4 VAL A 56 HIS A 59 -1 O VAL A 56 N LEU A 8
SHEET 4 AA 4 LYS A 62 CYS A 65 -1 O LYS A 62 N HIS A 59
SHEET 1 BA 4 GLU B 31 GLU B 34 0
SHEET 2 BA 4 VAL B 5 ASP B 9 1 O VAL B 5 N GLU B 31
SHEET 3 BA 4 VAL B 56 HIS B 59 -1 O VAL B 56 N LEU B 8
SHEET 4 BA 4 LYS B 62 CYS B 65 -1 O LYS B 62 N HIS B 59
CISPEP 1 ILE A 54 PRO A 55 0 1.03
CISPEP 2 ILE B 54 PRO B 55 0 0.82
SITE 1 AC1 8 TRP A 11 ARG A 20 TYR A 32 LYS A 197
SITE 2 AC1 8 SER A 198 LEU A 199 PRO A 200 SER B 177
SITE 1 AC2 8 TYR A 107 ARG A 111 CYS A 114 THR A 115
SITE 2 AC2 8 TRP A 163 ILE A 209 LEU A 212 GTB A1222
SITE 1 AC3 21 SER A 13 PHE A 15 LYS A 40 LYS A 53
SITE 2 AC3 21 ILE A 54 PRO A 55 GLU A 66 SER A 67
SITE 3 AC3 21 TYR A 107 PHE A 208 LEU A 212 4NM A1221
SITE 4 AC3 21 PO4 A1223 HOH A2018 HOH A2056 HOH A2081
SITE 5 AC3 21 HOH A2143 HOH A2237 HOH A2238 HOH A2239
SITE 6 AC3 21 LYS B 104
SITE 1 AC4 18 SER B 13 PHE B 15 LEU B 37 LYS B 40
SITE 2 AC4 18 LYS B 53 ILE B 54 PRO B 55 GLU B 66
SITE 3 AC4 18 SER B 67 TYR B 107 PHE B 208 LEU B 212
SITE 4 AC4 18 PO4 B1222 HOH B2017 HOH B2066 HOH B2105
SITE 5 AC4 18 HOH B2169 HOH B2170
SITE 1 AC5 7 TYR B 107 ARG B 111 CYS B 114 THR B 115
SITE 2 AC5 7 TRP B 163 ILE B 209 LEU B 212
SITE 1 AC6 5 HIS A 51 LYS A 53 GLU A 66 GTB A1222
SITE 2 AC6 5 LYS B 104
SITE 1 AC7 4 LYS A 104 LYS B 53 GLU B 66 GTB B1220
CRYST1 62.241 77.602 99.078 90.00 90.00 90.00 P 21 21 21 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 0.016067 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012886 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010093 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
