HEADER TRANSFERASE 18-JAN-10 3LFL
TITLE CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE TRANSFERASE OMEGA 1, DELTA 155
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONE S-TRANSFERASE OMEGA-1;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: GSTO 1-1;
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: GSTO1, GSTTLP28;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GLUTATHIONE S-TRANSFERASE OMEGA 1 DEL155, PROTEIN-GLUTATHIONE
KEYWDS 2 COMPLEX, N-TERMINAL THIOREDOXIN-LIKE DOMAIN, C-TERMINAL ALPHA-
KEYWDS 3 HELICAL DOMAIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR BROCK J.
REVDAT 5 09-MAY-12 3LFL 1 REMARK
REVDAT 4 14-DEC-11 3LFL 1 HETATM HETNAM VERSN
REVDAT 3 23-FEB-11 3LFL 1 JRNL
REVDAT 2 01-DEC-10 3LFL 1 JRNL
REVDAT 1 24-NOV-10 3LFL 0
JRNL AUTH H.ZHOU,J.BROCK,M.G.CASAROTTO,A.J.OAKLEY,P.G.BOARD
JRNL TITL NOVEL FOLDING AND STABILITY DEFECTS CAUSE A DEFICIENCY OF
JRNL TITL 2 HUMAN GLUTATHIONE TRANSFERASE OMEGA 1.
JRNL REF J.BIOL.CHEM. V. 286 4271 2011
JRNL REFN ISSN 0021-9258
JRNL PMID 21106529
JRNL DOI 10.1074/JBC.M110.197822
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.51
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 72.1
REMARK 3 NUMBER OF REFLECTIONS : 33943
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1731
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 36.5100 - 4.8050 0.83 3289 182 0.1650 0.1940
REMARK 3 2 4.8050 - 3.8150 0.55 2054 135 0.1540 0.1960
REMARK 3 3 3.8150 - 3.3330 0.50 1875 106 0.1820 0.2240
REMARK 3 4 3.3330 - 3.0280 0.54 2052 92 0.2010 0.2510
REMARK 3 5 3.0280 - 2.8110 0.59 2198 111 0.2090 0.2870
REMARK 3 6 2.8110 - 2.6460 0.66 2435 141 0.2160 0.2880
REMARK 3 7 2.6460 - 2.5130 0.74 2719 145 0.2150 0.2900
REMARK 3 8 2.5130 - 2.4040 0.78 2861 167 0.2250 0.3290
REMARK 3 9 2.4040 - 2.3110 0.82 3014 155 0.2200 0.2770
REMARK 3 10 2.3110 - 2.2320 0.86 3150 157 0.2220 0.2920
REMARK 3 11 2.2320 - 2.1620 0.88 3228 175 0.2280 0.3150
REMARK 3 12 2.1620 - 2.1000 0.90 3337 165 0.2360 0.2980
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.34
REMARK 3 B_SOL : 37.94
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.820
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.08800
REMARK 3 B22 (A**2) : 0.00700
REMARK 3 B33 (A**2) : -2.09500
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 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 : 0.007 5768
REMARK 3 ANGLE : 1.026 7777
REMARK 3 CHIRALITY : 0.070 823
REMARK 3 PLANARITY : 0.011 982
REMARK 3 DIHEDRAL : 17.617 2213
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 3LFL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JAN-10.
REMARK 100 THE RCSB ID CODE IS RCSB057216.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54060
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44498
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 200 DATA REDUNDANCY : 8.800
REMARK 200 R MERGE (I) : 0.12800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.37000
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS PH 8.5, 0.2M TRIMETHYL AMINE
REMARK 280 N-OXIDE DIHYDRATE, 20% (W/V) POLYETHYLENE GLYCOL MONOMETHYL ETHER
REMARK 280 2000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
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 36.50450
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 100.97100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.50450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 100.97100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 3800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 73.00900
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 3890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 1
REMARK 465 SER A 2
REMARK 465 GLY A 3
REMARK 465 GLU A 4
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLY B 3
REMARK 465 GLU B 4
REMARK 465 ASN B 231
REMARK 465 SER B 232
REMARK 465 PRO B 233
REMARK 465 GLU B 234
REMARK 465 ALA B 235
REMARK 465 CYS B 236
REMARK 465 ASP B 237
REMARK 465 TYR B 238
REMARK 465 GLY B 239
REMARK 465 LEU B 240
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 GLY C 3
REMARK 465 GLU C 4
REMARK 465 LEU C 229
REMARK 465 GLN C 230
REMARK 465 ASN C 231
REMARK 465 SER C 232
REMARK 465 PRO C 233
REMARK 465 GLU C 234
REMARK 465 ALA C 235
REMARK 465 CYS C 236
REMARK 465 ASP C 237
REMARK 465 TYR C 238
REMARK 465 GLY C 239
REMARK 465 LEU C 240
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 SER A 5 N CB OG
REMARK 480 LYS A 136 CB CG CD CE NZ
REMARK 480 ASP A 138 N
REMARK 480 SER B 5 N CA CB OG
REMARK 480 GLN B 134 CG CD OE1 NE2
REMARK 480 LYS B 136 CG CD CE NZ
REMARK 480 GLU B 137 CB CG CD OE1 OE2
REMARK 480 LYS C 136 CD CE NZ
REMARK 480 TYR C 139 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 480 LYS C 143 CD CE NZ
REMARK 480 SER C 217 CB OG
REMARK 480 LYS C 219 CG CD CE NZ
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 ASN A 58 66.04 -116.46
REMARK 500 GLU A 85 112.16 73.51
REMARK 500 ASN A 158 60.15 39.02
REMARK 500 ALA B 6 17.02 176.12
REMARK 500 GLU B 85 111.89 73.97
REMARK 500 ASP B 138 -70.26 -60.25
REMARK 500 ASN B 158 -75.23 -24.42
REMARK 500 LYS B 187 35.21 71.30
REMARK 500 ALA C 6 114.94 169.77
REMARK 500 ARG C 7 149.09 108.01
REMARK 500 ASN C 58 74.17 -163.12
REMARK 500 GLU C 85 115.12 74.18
REMARK 500 SER C 133 102.89 -5.26
REMARK 500 GLU C 226 -66.56 64.40
REMARK 500 LEU C 227 47.36 -76.89
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 GSH A 241
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTT A 242
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH B 241
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTT B 242
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTT C 241
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH C 242
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EEM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE TRANSFERASE OMEGA 1
REMARK 900 NATIVE
DBREF 3LFL A 1 240 UNP P78417 GSTO1_HUMAN 1 241
DBREF 3LFL B 1 240 UNP P78417 GSTO1_HUMAN 1 241
DBREF 3LFL C 1 240 UNP P78417 GSTO1_HUMAN 1 241
SEQADV 3LFL A UNP P78417 GLU 154 DELETION
SEQADV 3LFL B UNP P78417 GLU 154 DELETION
SEQADV 3LFL C UNP P78417 GLU 154 DELETION
SEQRES 1 A 240 MET SER GLY GLU SER ALA ARG SER LEU GLY LYS GLY SER
SEQRES 2 A 240 ALA PRO PRO GLY PRO VAL PRO GLU GLY SER ILE ARG ILE
SEQRES 3 A 240 TYR SER MET ARG PHE CYS PRO PHE ALA GLU ARG THR ARG
SEQRES 4 A 240 LEU VAL LEU LYS ALA LYS GLY ILE ARG HIS GLU VAL ILE
SEQRES 5 A 240 ASN ILE ASN LEU LYS ASN LYS PRO GLU TRP PHE PHE LYS
SEQRES 6 A 240 LYS ASN PRO PHE GLY LEU VAL PRO VAL LEU GLU ASN SER
SEQRES 7 A 240 GLN GLY GLN LEU ILE TYR GLU SER ALA ILE THR CYS GLU
SEQRES 8 A 240 TYR LEU ASP GLU ALA TYR PRO GLY LYS LYS LEU LEU PRO
SEQRES 9 A 240 ASP ASP PRO TYR GLU LYS ALA CYS GLN LYS MET ILE LEU
SEQRES 10 A 240 GLU LEU PHE SER LYS VAL PRO SER LEU VAL GLY SER PHE
SEQRES 11 A 240 ILE ARG SER GLN ASN LYS GLU ASP TYR ALA GLY LEU LYS
SEQRES 12 A 240 GLU GLU PHE ARG LYS GLU PHE THR LYS LEU GLU VAL LEU
SEQRES 13 A 240 THR ASN LYS LYS THR THR PHE PHE GLY GLY ASN SER ILE
SEQRES 14 A 240 SER MET ILE ASP TYR LEU ILE TRP PRO TRP PHE GLU ARG
SEQRES 15 A 240 LEU GLU ALA MET LYS LEU ASN GLU CYS VAL ASP HIS THR
SEQRES 16 A 240 PRO LYS LEU LYS LEU TRP MET ALA ALA MET LYS GLU ASP
SEQRES 17 A 240 PRO THR VAL SER ALA LEU LEU THR SER GLU LYS ASP TRP
SEQRES 18 A 240 GLN GLY PHE LEU GLU LEU TYR LEU GLN ASN SER PRO GLU
SEQRES 19 A 240 ALA CYS ASP TYR GLY LEU
SEQRES 1 B 240 MET SER GLY GLU SER ALA ARG SER LEU GLY LYS GLY SER
SEQRES 2 B 240 ALA PRO PRO GLY PRO VAL PRO GLU GLY SER ILE ARG ILE
SEQRES 3 B 240 TYR SER MET ARG PHE CYS PRO PHE ALA GLU ARG THR ARG
SEQRES 4 B 240 LEU VAL LEU LYS ALA LYS GLY ILE ARG HIS GLU VAL ILE
SEQRES 5 B 240 ASN ILE ASN LEU LYS ASN LYS PRO GLU TRP PHE PHE LYS
SEQRES 6 B 240 LYS ASN PRO PHE GLY LEU VAL PRO VAL LEU GLU ASN SER
SEQRES 7 B 240 GLN GLY GLN LEU ILE TYR GLU SER ALA ILE THR CYS GLU
SEQRES 8 B 240 TYR LEU ASP GLU ALA TYR PRO GLY LYS LYS LEU LEU PRO
SEQRES 9 B 240 ASP ASP PRO TYR GLU LYS ALA CYS GLN LYS MET ILE LEU
SEQRES 10 B 240 GLU LEU PHE SER LYS VAL PRO SER LEU VAL GLY SER PHE
SEQRES 11 B 240 ILE ARG SER GLN ASN LYS GLU ASP TYR ALA GLY LEU LYS
SEQRES 12 B 240 GLU GLU PHE ARG LYS GLU PHE THR LYS LEU GLU VAL LEU
SEQRES 13 B 240 THR ASN LYS LYS THR THR PHE PHE GLY GLY ASN SER ILE
SEQRES 14 B 240 SER MET ILE ASP TYR LEU ILE TRP PRO TRP PHE GLU ARG
SEQRES 15 B 240 LEU GLU ALA MET LYS LEU ASN GLU CYS VAL ASP HIS THR
SEQRES 16 B 240 PRO LYS LEU LYS LEU TRP MET ALA ALA MET LYS GLU ASP
SEQRES 17 B 240 PRO THR VAL SER ALA LEU LEU THR SER GLU LYS ASP TRP
SEQRES 18 B 240 GLN GLY PHE LEU GLU LEU TYR LEU GLN ASN SER PRO GLU
SEQRES 19 B 240 ALA CYS ASP TYR GLY LEU
SEQRES 1 C 240 MET SER GLY GLU SER ALA ARG SER LEU GLY LYS GLY SER
SEQRES 2 C 240 ALA PRO PRO GLY PRO VAL PRO GLU GLY SER ILE ARG ILE
SEQRES 3 C 240 TYR SER MET ARG PHE CYS PRO PHE ALA GLU ARG THR ARG
SEQRES 4 C 240 LEU VAL LEU LYS ALA LYS GLY ILE ARG HIS GLU VAL ILE
SEQRES 5 C 240 ASN ILE ASN LEU LYS ASN LYS PRO GLU TRP PHE PHE LYS
SEQRES 6 C 240 LYS ASN PRO PHE GLY LEU VAL PRO VAL LEU GLU ASN SER
SEQRES 7 C 240 GLN GLY GLN LEU ILE TYR GLU SER ALA ILE THR CYS GLU
SEQRES 8 C 240 TYR LEU ASP GLU ALA TYR PRO GLY LYS LYS LEU LEU PRO
SEQRES 9 C 240 ASP ASP PRO TYR GLU LYS ALA CYS GLN LYS MET ILE LEU
SEQRES 10 C 240 GLU LEU PHE SER LYS VAL PRO SER LEU VAL GLY SER PHE
SEQRES 11 C 240 ILE ARG SER GLN ASN LYS GLU ASP TYR ALA GLY LEU LYS
SEQRES 12 C 240 GLU GLU PHE ARG LYS GLU PHE THR LYS LEU GLU VAL LEU
SEQRES 13 C 240 THR ASN LYS LYS THR THR PHE PHE GLY GLY ASN SER ILE
SEQRES 14 C 240 SER MET ILE ASP TYR LEU ILE TRP PRO TRP PHE GLU ARG
SEQRES 15 C 240 LEU GLU ALA MET LYS LEU ASN GLU CYS VAL ASP HIS THR
SEQRES 16 C 240 PRO LYS LEU LYS LEU TRP MET ALA ALA MET LYS GLU ASP
SEQRES 17 C 240 PRO THR VAL SER ALA LEU LEU THR SER GLU LYS ASP TRP
SEQRES 18 C 240 GLN GLY PHE LEU GLU LEU TYR LEU GLN ASN SER PRO GLU
SEQRES 19 C 240 ALA CYS ASP TYR GLY LEU
HET GSH A 241 20
HET DTT A 242 8
HET GSH B 241 20
HET DTT B 242 8
HET DTT C 241 8
HET GSH C 242 20
HETNAM GSH GLUTATHIONE
HETNAM DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE
HETSYN DTT 1,4-DITHIOTHREITOL
FORMUL 4 GSH 3(C10 H17 N3 O6 S)
FORMUL 5 DTT 3(C4 H10 O2 S2)
FORMUL 10 HOH *328(H2 O)
HELIX 1 1 CYS A 32 LYS A 45 1 14
HELIX 2 2 PRO A 60 LYS A 66 5 7
HELIX 3 3 GLU A 85 TYR A 97 1 13
HELIX 4 4 ASP A 106 PHE A 120 1 15
HELIX 5 5 LYS A 122 ARG A 132 1 11
HELIX 6 6 ASN A 135 THR A 157 1 23
HELIX 7 7 SER A 170 MET A 186 1 17
HELIX 8 8 LEU A 188 ASP A 193 5 6
HELIX 9 9 THR A 195 ASP A 208 1 14
HELIX 10 10 ASP A 208 LEU A 215 1 8
HELIX 11 11 SER A 217 GLN A 230 1 14
HELIX 12 12 SER A 232 TYR A 238 5 7
HELIX 13 13 CYS B 32 LYS B 45 1 14
HELIX 14 14 TRP B 62 ASN B 67 1 6
HELIX 15 15 GLU B 85 TYR B 97 1 13
HELIX 16 16 ASP B 106 PHE B 120 1 15
HELIX 17 17 LYS B 122 ARG B 132 1 11
HELIX 18 18 ASN B 135 LEU B 156 1 22
HELIX 19 19 SER B 170 ARG B 182 1 13
HELIX 20 20 ARG B 182 LYS B 187 1 6
HELIX 21 21 LEU B 188 ASP B 193 5 6
HELIX 22 22 THR B 195 ASP B 208 1 14
HELIX 23 23 ASP B 208 LEU B 214 1 7
HELIX 24 24 SER B 217 ASP B 220 5 4
HELIX 25 25 TRP B 221 GLN B 230 1 10
HELIX 26 26 CYS C 32 LYS C 45 1 14
HELIX 27 27 TRP C 62 ASN C 67 1 6
HELIX 28 28 GLU C 85 TYR C 97 1 13
HELIX 29 29 ASP C 106 SER C 121 1 16
HELIX 30 30 LYS C 122 SER C 133 1 12
HELIX 31 31 GLU C 137 ASN C 158 1 22
HELIX 32 32 SER C 170 ARG C 182 1 13
HELIX 33 33 LEU C 188 ASP C 193 5 6
HELIX 34 34 THR C 195 ASP C 208 1 14
HELIX 35 35 ASP C 208 LEU C 215 1 8
HELIX 36 36 SER C 217 PHE C 224 5 8
SHEET 1 A 4 HIS A 49 ASN A 53 0
SHEET 2 A 4 ILE A 24 SER A 28 1 N ILE A 26 O GLU A 50
SHEET 3 A 4 VAL A 74 ASN A 77 -1 O VAL A 74 N TYR A 27
SHEET 4 A 4 LEU A 82 TYR A 84 -1 O ILE A 83 N LEU A 75
SHEET 1 B 4 HIS B 49 ASN B 53 0
SHEET 2 B 4 ILE B 24 SER B 28 1 N ILE B 26 O GLU B 50
SHEET 3 B 4 VAL B 74 ASN B 77 -1 O VAL B 74 N TYR B 27
SHEET 4 B 4 LEU B 82 TYR B 84 -1 O ILE B 83 N LEU B 75
SHEET 1 C 4 HIS C 49 ASN C 53 0
SHEET 2 C 4 ILE C 24 SER C 28 1 N ILE C 26 O ILE C 52
SHEET 3 C 4 VAL C 74 ASN C 77 -1 O GLU C 76 N ARG C 25
SHEET 4 C 4 LEU C 82 TYR C 84 -1 O ILE C 83 N LEU C 75
CISPEP 1 VAL A 72 PRO A 73 0 1.56
CISPEP 2 VAL B 72 PRO B 73 0 -0.70
CISPEP 3 ASN B 158 LYS B 159 0 -9.05
CISPEP 4 VAL C 72 PRO C 73 0 8.38
SITE 1 AC1 13 CYS A 32 PHE A 34 LEU A 56 LYS A 59
SITE 2 AC1 13 LEU A 71 VAL A 72 PRO A 73 GLU A 85
SITE 3 AC1 13 SER A 86 HOH A 248 HOH A 275 HOH A 304
SITE 4 AC1 13 HOH A 362
SITE 1 AC2 3 LYS A 143 ARG A 147 CYS A 191
SITE 1 AC3 10 CYS B 32 PHE B 34 LYS B 59 LEU B 71
SITE 2 AC3 10 VAL B 72 PRO B 73 GLU B 85 SER B 86
SITE 3 AC3 10 HOH B 271 HOH B 294
SITE 1 AC4 5 LYS B 143 ARG B 147 GLU B 190 CYS B 191
SITE 2 AC4 5 HOH B 283
SITE 1 AC5 2 ARG C 147 CYS C 191
SITE 1 AC6 12 CYS C 32 PHE C 34 LEU C 56 LYS C 59
SITE 2 AC6 12 LEU C 71 VAL C 72 PRO C 73 GLU C 85
SITE 3 AC6 12 SER C 86 HOH C 244 HOH C 289 HOH C 298
CRYST1 73.009 201.942 53.387 90.00 90.00 90.00 P 21 21 2 12
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 0.013697 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004952 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018731 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
