HEADER TRANSFERASE 23-JUN-05 2A2R
TITLE CRYSTAL STRUCTURE OF GLUTATHIONE TRANSFERASE PI IN COMPLEX WITH S-
TITLE 2 NITROSOGLUTATHIONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONE S-TRANSFERASE P;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: GLUTATHIONE TRANSFERASE PI, GST CLASS-PI, GSTP1-1;
COMPND 5 EC: 2.5.1.18;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: GSTP1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: XL-1 BLUE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PKHP1
KEYWDS TRANSFERASE, DETOXIFICATION, NITRIC OXIDE CARRIER, S-
KEYWDS 2 NITROSOGLUTATHIONE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.J.PARKER,C.J.MORTON,J.J.ADAMS,M.W.PARKER
REVDAT 3 25-OCT-23 2A2R 1 REMARK SEQADV HETSYN LINK
REVDAT 2 24-FEB-09 2A2R 1 VERSN
REVDAT 1 06-JUN-06 2A2R 0
JRNL AUTH R.TELLEZ-SANZ,E.CESAREO,M.NUCCETELLI,A.M.AGUILERA,C.BARON,
JRNL AUTH 2 L.J.PARKER,J.J.ADAMS,C.J.MORTON,M.LO BELLO,M.W.PARKER,
JRNL AUTH 3 L.GARCIA-FUENTES
JRNL TITL CALORIMETRIC AND STRUCTURAL STUDIES OF THE NITRIC OXIDE
JRNL TITL 2 CARRIER S-NITROSOGLUTATHIONE BOUND TO HUMAN GLUTATHIONE
JRNL TITL 3 TRANSFERASE P1-1
JRNL REF PROTEIN SCI. V. 15 1093 2006
JRNL REFN ISSN 0961-8368
JRNL PMID 16597834
JRNL DOI 10.1110/PS.052055206
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 87.2
REMARK 3 NUMBER OF REFLECTIONS : 77668
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 3922
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.42
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2100
REMARK 3 BIN FREE R VALUE : 0.2300
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 137
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3284
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 73
REMARK 3 SOLVENT ATOMS : 541
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.60
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.004
REMARK 3 BOND ANGLES (DEGREES) : 1.090
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : 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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2A2R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000033418.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-MAR-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-BM-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : GE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 86132
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 99.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.6800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.1
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.17800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.750
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 5GSS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MES, PEG 8000, CALCIUM CHLORIDE, DTT,
REMARK 280 GSH, PH 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 37.84550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.78600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 37.84550
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 44.78600
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER
REMARK 300 IN THE ASYMMETRIC UNIT
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: 2850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 0
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 64 110.43 84.50
REMARK 500 ASN A 110 56.37 -169.10
REMARK 500 THR A 141 -100.18 -118.65
REMARK 500 GLN B 64 109.20 85.97
REMARK 500 TYR B 79 35.91 -141.17
REMARK 500 ASN B 110 37.18 -156.29
REMARK 500 THR B 141 -102.64 -114.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 210 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 77 O
REMARK 620 2 GLN B 147 OE1 145.3
REMARK 620 3 HOH B2276 O 88.8 92.6
REMARK 620 4 HOH B2293 O 68.4 77.0 93.5
REMARK 620 5 HOH B2318 O 73.1 141.1 94.1 140.5
REMARK 620 6 HOH B2370 O 145.6 68.9 93.9 145.3 72.5
REMARK 620 7 HOH B2394 O 87.7 92.7 174.5 89.3 80.7 86.4
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 210
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A 1220
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSN A 1221
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 2220
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSN B 2221
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5GSS RELATED DB: PDB
REMARK 900 HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH GLUTATHIONE
REMARK 900 RELATED ID: 1ZGN RELATED DB: PDB
REMARK 900 HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH DINITROSYL-
REMARK 900 GLUTATHIONYL IRON COMPLEX
REMARK 900 RELATED ID: 2A2S RELATED DB: PDB
REMARK 900 GLUTATHIONE TRANSFERASE PI IN COMPLEX WITH S-NITROSOGLUTATHIONE
DBREF 2A2R A 1 209 UNP P09211 GSTP1_HUMAN 1 209
DBREF 2A2R B 1 209 UNP P09211 GSTP1_HUMAN 1 209
SEQADV 2A2R MET A 0 UNP P09211 INITIATING METHIONINE
SEQADV 2A2R MET B 0 UNP P09211 INITIATING METHIONINE
SEQRES 1 A 210 MET PRO PRO TYR THR VAL VAL TYR PHE PRO VAL ARG GLY
SEQRES 2 A 210 ARG CYS ALA ALA LEU ARG MET LEU LEU ALA ASP GLN GLY
SEQRES 3 A 210 GLN SER TRP LYS GLU GLU VAL VAL THR VAL GLU THR TRP
SEQRES 4 A 210 GLN GLU GLY SER LEU LYS ALA SER CYS LEU TYR GLY GLN
SEQRES 5 A 210 LEU PRO LYS PHE GLN ASP GLY ASP LEU THR LEU TYR GLN
SEQRES 6 A 210 SER ASN THR ILE LEU ARG HIS LEU GLY ARG THR LEU GLY
SEQRES 7 A 210 LEU TYR GLY LYS ASP GLN GLN GLU ALA ALA LEU VAL ASP
SEQRES 8 A 210 MET VAL ASN ASP GLY VAL GLU ASP LEU ARG CYS LYS TYR
SEQRES 9 A 210 ILE SER LEU ILE TYR THR ASN TYR GLU ALA GLY LYS ASP
SEQRES 10 A 210 ASP TYR VAL LYS ALA LEU PRO GLY GLN LEU LYS PRO PHE
SEQRES 11 A 210 GLU THR LEU LEU SER GLN ASN GLN GLY GLY LYS THR PHE
SEQRES 12 A 210 ILE VAL GLY ASP GLN ILE SER PHE ALA ASP TYR ASN LEU
SEQRES 13 A 210 LEU ASP LEU LEU LEU ILE HIS GLU VAL LEU ALA PRO GLY
SEQRES 14 A 210 CYS LEU ASP ALA PHE PRO LEU LEU SER ALA TYR VAL GLY
SEQRES 15 A 210 ARG LEU SER ALA ARG PRO LYS LEU LYS ALA PHE LEU ALA
SEQRES 16 A 210 SER PRO GLU TYR VAL ASN LEU PRO ILE ASN GLY ASN GLY
SEQRES 17 A 210 LYS GLN
SEQRES 1 B 210 MET PRO PRO TYR THR VAL VAL TYR PHE PRO VAL ARG GLY
SEQRES 2 B 210 ARG CYS ALA ALA LEU ARG MET LEU LEU ALA ASP GLN GLY
SEQRES 3 B 210 GLN SER TRP LYS GLU GLU VAL VAL THR VAL GLU THR TRP
SEQRES 4 B 210 GLN GLU GLY SER LEU LYS ALA SER CYS LEU TYR GLY GLN
SEQRES 5 B 210 LEU PRO LYS PHE GLN ASP GLY ASP LEU THR LEU TYR GLN
SEQRES 6 B 210 SER ASN THR ILE LEU ARG HIS LEU GLY ARG THR LEU GLY
SEQRES 7 B 210 LEU TYR GLY LYS ASP GLN GLN GLU ALA ALA LEU VAL ASP
SEQRES 8 B 210 MET VAL ASN ASP GLY VAL GLU ASP LEU ARG CYS LYS TYR
SEQRES 9 B 210 ILE SER LEU ILE TYR THR ASN TYR GLU ALA GLY LYS ASP
SEQRES 10 B 210 ASP TYR VAL LYS ALA LEU PRO GLY GLN LEU LYS PRO PHE
SEQRES 11 B 210 GLU THR LEU LEU SER GLN ASN GLN GLY GLY LYS THR PHE
SEQRES 12 B 210 ILE VAL GLY ASP GLN ILE SER PHE ALA ASP TYR ASN LEU
SEQRES 13 B 210 LEU ASP LEU LEU LEU ILE HIS GLU VAL LEU ALA PRO GLY
SEQRES 14 B 210 CYS LEU ASP ALA PHE PRO LEU LEU SER ALA TYR VAL GLY
SEQRES 15 B 210 ARG LEU SER ALA ARG PRO LYS LEU LYS ALA PHE LEU ALA
SEQRES 16 B 210 SER PRO GLU TYR VAL ASN LEU PRO ILE ASN GLY ASN GLY
SEQRES 17 B 210 LYS GLN
HET MES A1220 12
HET GSN A1221 66
HET CA B 210 1
HET CO3 B1001 4
HET MES B2220 12
HET GSN B2221 66
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM GSN 2-AMINO-5-[1-(CARBOXYLATOMETHYLCARBAMOYL)-2-
HETNAM 2 GSN NITROSOSULFANYL-ETHYL]AMINO-5-OXO-PENTANOATE
HETNAM CA CALCIUM ION
HETNAM CO3 CARBONATE ION
HETSYN GSN S-NITROSOGLUTATHIONE; S-NITROSO GAMMA-
HETSYN 2 GSN GLUTAMYLCYSTEINYLGLYCINE
FORMUL 3 MES 2(C6 H13 N O4 S)
FORMUL 4 GSN 2(C10 H14 N4 O7 S 2-)
FORMUL 5 CA CA 2+
FORMUL 6 CO3 C O3 2-
FORMUL 9 HOH *541(H2 O)
HELIX 1 1 ARG A 11 ARG A 13 5 3
HELIX 2 2 CYS A 14 GLN A 24 1 11
HELIX 3 3 THR A 34 GLY A 41 1 8
HELIX 4 4 GLY A 41 CYS A 47 1 7
HELIX 5 5 GLN A 64 LEU A 76 1 13
HELIX 6 6 ASP A 82 ASN A 110 1 29
HELIX 7 7 ASN A 110 GLN A 135 1 26
HELIX 8 8 ASN A 136 LYS A 140 5 5
HELIX 9 9 SER A 149 ALA A 166 1 18
HELIX 10 10 GLY A 168 ALA A 172 5 5
HELIX 11 11 PHE A 173 ALA A 185 1 13
HELIX 12 12 ARG A 186 SER A 195 1 10
HELIX 13 13 SER A 195 ASN A 200 1 6
HELIX 14 14 ARG B 11 ARG B 13 5 3
HELIX 15 15 CYS B 14 GLN B 24 1 11
HELIX 16 16 THR B 34 GLY B 41 1 8
HELIX 17 17 GLY B 41 CYS B 47 1 7
HELIX 18 18 GLN B 64 GLY B 77 1 14
HELIX 19 19 ASP B 82 ASN B 110 1 29
HELIX 20 20 ASN B 110 GLN B 135 1 26
HELIX 21 21 ASN B 136 LYS B 140 5 5
HELIX 22 22 SER B 149 ALA B 166 1 18
HELIX 23 23 PHE B 173 ALA B 185 1 13
HELIX 24 24 ARG B 186 SER B 195 1 10
HELIX 25 25 SER B 195 ASN B 200 1 6
SHEET 1 A 4 TRP A 28 VAL A 32 0
SHEET 2 A 4 TYR A 3 TYR A 7 1 N VAL A 5 O GLU A 31
SHEET 3 A 4 LYS A 54 ASP A 57 -1 O LYS A 54 N VAL A 6
SHEET 4 A 4 LEU A 60 TYR A 63 -1 O LEU A 62 N PHE A 55
SHEET 1 B 4 TRP B 28 VAL B 32 0
SHEET 2 B 4 TYR B 3 TYR B 7 1 N VAL B 5 O GLU B 31
SHEET 3 B 4 LYS B 54 ASP B 57 -1 O LYS B 54 N VAL B 6
SHEET 4 B 4 LEU B 60 TYR B 63 -1 O LEU B 62 N PHE B 55
LINK O GLY B 77 CA CA B 210 1555 1555 2.35
LINK OE1 GLN B 147 CA CA B 210 1555 1555 2.33
LINK CA CA B 210 O HOH B2276 1555 1555 2.38
LINK CA CA B 210 O HOH B2293 1555 1555 2.50
LINK CA CA B 210 O HOH B2318 1555 1555 2.44
LINK CA CA B 210 O HOH B2370 1555 1555 2.49
LINK CA CA B 210 O HOH B2394 1555 1555 2.38
CISPEP 1 LEU A 52 PRO A 53 0 0.68
CISPEP 2 PRO B 1 PRO B 2 0 0.03
CISPEP 3 LEU B 52 PRO B 53 0 0.66
SITE 1 AC1 7 GLY B 77 GLN B 147 HOH B2276 HOH B2293
SITE 2 AC1 7 HOH B2318 HOH B2370 HOH B2394
SITE 1 AC2 4 PHE B 142 ILE B 148 ARG B 186 HOH B2498
SITE 1 AC3 6 TRP A 28 GLU A 197 HOH A1284 HOH A1472
SITE 2 AC3 6 ASP B 171 HOH B2357
SITE 1 AC4 18 TYR A 7 PHE A 8 ARG A 13 TRP A 38
SITE 2 AC4 18 LYS A 44 GLN A 51 LEU A 52 PRO A 53
SITE 3 AC4 18 GLN A 64 SER A 65 ILE A 104 HOH A1227
SITE 4 AC4 18 HOH A1266 HOH A1267 HOH A1268 HOH A1319
SITE 5 AC4 18 HOH A1485 ASP B 98
SITE 1 AC5 10 ASP A 171 ALA A 172 ALA B 22 TRP B 28
SITE 2 AC5 10 PHE B 192 GLU B 197 HOH B2278 HOH B2345
SITE 3 AC5 10 HOH B2387 HOH B2461
SITE 1 AC6 20 ASP A 98 TYR B 7 PHE B 8 ARG B 13
SITE 2 AC6 20 TRP B 38 LYS B 44 GLN B 51 LEU B 52
SITE 3 AC6 20 PRO B 53 GLN B 64 SER B 65 ILE B 104
SITE 4 AC6 20 HOH B2237 HOH B2243 HOH B2256 HOH B2272
SITE 5 AC6 20 HOH B2308 HOH B2393 HOH B2434 HOH B2457
CRYST1 75.691 89.572 68.690 90.00 97.61 90.00 C 1 2 1 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 0.013212 0.000000 0.001765 0.00000
SCALE2 0.000000 0.011164 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014688 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
