HEADER TRANSFERASE 22-DEC-15 5FHI
TITLE CRYSTALLOGRAPHIC STRUCTURE OF PSOE WITHOUT CO
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONE S-TRANSFERASE, PUTATIVE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NEOSARTORYA FUMIGATA (STRAIN ATCC MYA-4609 /
SOURCE 3 AF293 / CBS 101355 / FGSC A1100);
SOURCE 4 ORGANISM_TAXID: 330879;
SOURCE 5 STRAIN: ATCC MYA-4609 / AF293 / CBS 101355 / FGSC A1100;
SOURCE 6 GENE: AFUA_8G00580;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GST, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.HARA,H.HASHIMOTO,T.YAMAMOTO,Y.TSUNEMATSU,K.WATANABE
REVDAT 3 20-MAR-24 5FHI 1 REMARK
REVDAT 2 05-JUL-17 5FHI 1 JRNL
REVDAT 1 20-APR-16 5FHI 0
JRNL AUTH T.YAMAMOTO,Y.TSUNEMATSU,K.HARA,T.SUZUKI,S.KISHIMOTO,
JRNL AUTH 2 H.KAWAGISHI,H.NOGUCHI,H.HASHIMOTO,Y.TANG,K.HOTTA,K.WATANABE
JRNL TITL OXIDATIVE TRANS TO CIS ISOMERIZATION OF OLEFINS IN
JRNL TITL 2 POLYKETIDE BIOSYNTHESIS.
JRNL REF ANGEW. CHEM. INT. ED. ENGL. V. 55 6207 2016
JRNL REFN ESSN 1521-3773
JRNL PMID 27072782
JRNL DOI 10.1002/ANIE.201600940
REMARK 2
REMARK 2 RESOLUTION. 2.41 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.41
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.60
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 12786
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.050
REMARK 3 FREE R VALUE TEST SET COUNT : 1279
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 47.6068 - 6.1934 1.00 1255 137 0.1542 0.1935
REMARK 3 2 6.1934 - 4.9175 1.00 1237 134 0.1587 0.1789
REMARK 3 3 4.9175 - 4.2964 1.00 1241 141 0.1364 0.1837
REMARK 3 4 4.2964 - 3.9038 1.00 1252 134 0.1535 0.2321
REMARK 3 5 3.9038 - 3.6241 1.00 1236 137 0.1759 0.2450
REMARK 3 6 3.6241 - 3.4105 1.00 1235 139 0.1926 0.2982
REMARK 3 7 3.4105 - 3.2397 1.00 1244 138 0.2134 0.2961
REMARK 3 8 3.2397 - 3.0987 1.00 1239 141 0.2115 0.2849
REMARK 3 9 3.0987 - 2.9794 1.00 1234 143 0.2201 0.2737
REMARK 3 10 2.9794 - 2.8766 1.00 1242 137 0.2138 0.3153
REMARK 3 11 2.8766 - 2.7867 1.00 1231 139 0.2327 0.3308
REMARK 3 12 2.7867 - 2.7071 1.00 1223 139 0.2305 0.2787
REMARK 3 13 2.7071 - 2.6358 1.00 1276 137 0.2284 0.2852
REMARK 3 14 2.6358 - 2.5715 1.00 1210 140 0.2460 0.2770
REMARK 3 15 2.5715 - 2.5130 1.00 1252 142 0.2277 0.2449
REMARK 3 16 2.5130 - 2.4596 1.00 1227 136 0.2733 0.3493
REMARK 3 17 2.4596 - 2.4104 0.96 1201 136 0.3113 0.3875
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.560
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 : 0.015 1789
REMARK 3 ANGLE : 1.448 2424
REMARK 3 CHIRALITY : 0.059 268
REMARK 3 PLANARITY : 0.010 314
REMARK 3 DIHEDRAL : 16.860 655
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: THE ENTRY CONTAINS FRIEDEL PAIRS IN
REMARK 3 F_PLUS/MINUS AND I_PLUS/MINUS COLUMNS
REMARK 4
REMARK 4 5FHI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000216595.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-MAY-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-1A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.10
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12786
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.410
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 19.45
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 30.5400
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: NULL
REMARK 200 SOFTWARE USED: AUTOSOL, PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: THE ENTRY CONTAINS FRIEDEL PAIRS IN F_PLUS/MINUS AND
REMARK 200 I_PLUS/MINUS COLUMNS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEGMME 5000, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 34.17733
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 17.08867
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 25.63300
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 8.54433
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 42.72167
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 34.17733
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 17.08867
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 8.54433
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 25.63300
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 42.72167
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: 4780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 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 0.00000
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 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 PRO A 216
REMARK 465 GLU A 217
REMARK 465 LYS A 218
REMARK 465 LYS A 219
REMARK 465 PRO A 220
REMARK 465 GLU A 221
REMARK 465 THR A 222
REMARK 465 VAL A 223
REMARK 465 PRO A 224
REMARK 465 LYS A 225
REMARK 465 ASN A 226
REMARK 465 GLY A 227
REMARK 465 ALA A 228
REMARK 465 ALA A 229
REMARK 465 VAL A 230
REMARK 465 ALA A 231
REMARK 465 ILE A 232
REMARK 465 GLU A 233
REMARK 465 ALA A 234
REMARK 465 THR A 235
REMARK 465 GLN A 236
REMARK 465 ALA A 237
REMARK 465 GLY A 238
REMARK 465 HIS A 239
REMARK 465 HIS A 240
REMARK 465 HIS A 241
REMARK 465 HIS A 242
REMARK 465 HIS A 243
REMARK 465 HIS A 244
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 HH22 ARG A 177 O LEU A 206 1.52
REMARK 500 NH2 ARG A 177 O LEU A 206 2.03
REMARK 500 OH TYR A 119 OD1 ASN A 214 2.10
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 HH TYR A 88 HH TYR A 88 8555 1.21
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 ASP A 57 -47.06 -29.76
REMARK 500 GLU A 63 115.35 78.68
REMARK 500 ILE A 102 -60.25 -121.54
REMARK 500 VAL A 116 -70.38 -54.14
REMARK 500 ASP A 120 116.47 -169.34
REMARK 500 ASP A 201 -179.33 -63.46
REMARK 500 ASP A 207 -67.36 -93.11
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 301
DBREF 5FHI A 1 237 UNP Q4WB03 Q4WB03_ASPFU 1 237
SEQADV 5FHI GLY A 238 UNP Q4WB03 EXPRESSION TAG
SEQADV 5FHI HIS A 239 UNP Q4WB03 EXPRESSION TAG
SEQADV 5FHI HIS A 240 UNP Q4WB03 EXPRESSION TAG
SEQADV 5FHI HIS A 241 UNP Q4WB03 EXPRESSION TAG
SEQADV 5FHI HIS A 242 UNP Q4WB03 EXPRESSION TAG
SEQADV 5FHI HIS A 243 UNP Q4WB03 EXPRESSION TAG
SEQADV 5FHI HIS A 244 UNP Q4WB03 EXPRESSION TAG
SEQRES 1 A 244 MET VAL PHE GLY THR LEU TYR THR PHE PRO GLY ASP GLN
SEQRES 2 A 244 CYS ARG THR ILE ALA ILE LYS ALA VAL ALA LYS ALA ASN
SEQRES 3 A 244 GLY LEU ASP LEU ASP ILE ARG GLU THR PRO ARG THR PRO
SEQRES 4 A 244 ASP HIS LEU SER ILE SER LYS LEU GLY LYS VAL PRO ALA
SEQRES 5 A 244 PHE GLN GLY ALA ASP SER PHE LYS LEU PHE GLU CYS MET
SEQRES 6 A 244 ALA ILE ALA LEU TYR ILE THR SER GLN ASN GLU GLN THR
SEQRES 7 A 244 THR LEU LEU GLY LYS ASP LYS LYS GLU TYR ALA GLU ILE
SEQRES 8 A 244 ILE LYS TRP MET SER PHE PHE ASN THR GLU ILE VAL ILE
SEQRES 9 A 244 LEU MET THR GLN GLN LEU LEU PRO GLN LEU GLY VAL ILE
SEQRES 10 A 244 PRO TYR ASP ARG ASP GLN VAL GLU PHE PHE ALA ASN MET
SEQRES 11 A 244 THR GLN ARG SER VAL ASP VAL VAL GLU GLU TYR LEU GLN
SEQRES 12 A 244 ASP ARG THR PHE LEU VAL GLY ASP GLN LEU SER LEU ALA
SEQRES 13 A 244 ASP LEU PHE CYS ALA GLY ASN ILE SER LEU GLY PHE GLN
SEQRES 14 A 244 PHE PHE TYR GLY LYS ALA TRP ARG GLN GLN ASN PRO ASN
SEQRES 15 A 244 VAL SER ARG TRP TYR GLU MET VAL CYS HIS GLN PRO ILE
SEQRES 16 A 244 TYR ALA ALA VAL THR ASP LYS PHE GLN LEU LEU ASP GLU
SEQRES 17 A 244 PRO LYS LEU THR ASN ASN PRO PRO GLU LYS LYS PRO GLU
SEQRES 18 A 244 THR VAL PRO LYS ASN GLY ALA ALA VAL ALA ILE GLU ALA
SEQRES 19 A 244 THR GLN ALA GLY HIS HIS HIS HIS HIS HIS
HET GSH A 301 35
HETNAM GSH GLUTATHIONE
FORMUL 2 GSH C10 H17 N3 O6 S
FORMUL 3 HOH *24(H2 O)
HELIX 1 AA1 THR A 16 ASN A 26 1 11
HELIX 2 AA2 THR A 38 SER A 45 1 8
HELIX 3 AA3 GLU A 63 GLN A 74 1 12
HELIX 4 AA4 ASP A 84 ILE A 102 1 19
HELIX 5 AA5 ILE A 102 LEU A 111 1 10
HELIX 6 AA6 PRO A 112 LEU A 114 5 3
HELIX 7 AA7 ASP A 120 LEU A 142 1 23
HELIX 8 AA8 SER A 154 PHE A 171 1 18
HELIX 9 AA9 GLY A 173 ASN A 180 1 8
HELIX 10 AB1 ASN A 180 CYS A 191 1 12
HELIX 11 AB2 GLN A 193 ALA A 198 1 6
SHEET 1 AA1 4 ASP A 29 ARG A 33 0
SHEET 2 AA1 4 VAL A 2 TYR A 7 1 N PHE A 3 O ASP A 29
SHEET 3 AA1 4 ALA A 52 GLY A 55 -1 O GLN A 54 N THR A 5
SHEET 4 AA1 4 LYS A 60 PHE A 62 -1 O LEU A 61 N PHE A 53
CISPEP 1 VAL A 50 PRO A 51 0 -3.20
CISPEP 2 ASN A 213 ASN A 214 0 10.57
SITE 1 AC1 11 GLN A 13 ARG A 15 ARG A 37 LYS A 49
SITE 2 AC1 11 VAL A 50 GLU A 63 CYS A 64 ASN A 99
SITE 3 AC1 11 THR A 100 GLU A 101 HOH A 420
CRYST1 145.413 145.413 51.266 90.00 90.00 120.00 P 65 2 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 0.006877 0.003970 0.000000 0.00000
SCALE2 0.000000 0.007941 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019506 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
