HEADER TRANSFERASE/TRANSFERASE INHIBITOR 19-NOV-97 12GS
TITLE GLUTATHIONE S-TRANSFERASE COMPLEXED WITH S-NONYL-GLUTATHIONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONE S-TRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: GST;
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
KEYWDS COMPLEX (TRANSFERASE-NONYL-GLUTATHIONE), TRANSFERASE-TRANSFERASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.J.OAKLEY,M.LO BELLO,M.W.PARKER
REVDAT 6 02-AUG-23 12GS 1 REMARK
REVDAT 5 13-JUL-11 12GS 1 VERSN
REVDAT 4 24-FEB-09 12GS 1 VERSN
REVDAT 3 25-JAN-05 12GS 1 AUTHOR JRNL
REVDAT 2 02-FEB-99 12GS 1 AUTHOR
REVDAT 1 13-JAN-99 12GS 0
JRNL AUTH A.J.OAKLEY,M.LO BELLO,M.NUCCETELLI,A.P.MAZZETTI,M.W.PARKER
JRNL TITL THE LIGANDIN (NON-SUBSTRATE) BINDING SITE OF HUMAN PI CLASS
JRNL TITL 2 GLUTATHIONE TRANSFERASE IS LOCATED IN THE ELECTROPHILE
JRNL TITL 3 BINDING SITE (H-SITE).
JRNL REF J.MOL.BIOL. V. 291 913 1999
JRNL REFN ISSN 0022-2836
JRNL PMID 10452896
JRNL DOI 10.1006/JMBI.1999.3029
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.2
REMARK 3 NUMBER OF REFLECTIONS : 25488
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1228
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.17
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2274
REMARK 3 BIN R VALUE (WORKING SET) : 0.2400
REMARK 3 BIN FREE R VALUE : 0.3240
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 131
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.028
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3262
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 82
REMARK 3 SOLVENT ATOMS : 181
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.17
REMARK 3 LOW RESOLUTION CUTOFF (A) : 15.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.23
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.680
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.120 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.800 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.630 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.890 ; 2.500
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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : WATER.PRO
REMARK 3 PARAMETER FILE 3 : PARCYSH.PRO
REMARK 3 PARAMETER FILE 4 : MES.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : GGLU.PRO
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : CYN.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 12GS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170072.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JUL-96
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.4
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 RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE(002)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25403
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.6
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.4000
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) : 2.17
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.16800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.851
REMARK 200 STARTING MODEL: PDB ENTRY 1GSS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.4
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 38.95600
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.71350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 38.95600
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 44.71350
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 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 A 0
REMARK 465 PRO A 1
REMARK 465 MET B 0
REMARK 465 PRO B 1
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 B 303 O HOH B 306 0.09
REMARK 500 O HOH A 243 O HOH A 269 1.38
REMARK 500 O HOH B 220 O HOH B 310 1.53
REMARK 500 O HOH B 213 O HOH B 221 2.11
REMARK 500 O HOH A 269 O HOH A 289 2.19
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 64 109.20 81.90
REMARK 500 LEU A 78 50.59 -118.42
REMARK 500 ASN A 110 62.93 -169.41
REMARK 500 THR A 141 -104.27 -118.34
REMARK 500 GLN B 64 110.89 77.89
REMARK 500 ASN B 110 62.32 -169.06
REMARK 500 THR B 141 -103.77 -118.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 630
REMARK 630 MOLECULE TYPE: NULL
REMARK 630 MOLECULE NAME: L-GAMMA-GLUTAMYL-S-NONYL-L-CYSTEINYLGLYCINE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 0HH A 210
REMARK 630 0HH B 210
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: GGL GT9 GLY
REMARK 630 DETAILS: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0HH A 210
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0HH B 210
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A 211
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 211
DBREF 12GS A 1 209 UNP P09211 GTP_HUMAN 1 209
DBREF 12GS B 1 209 UNP P09211 GTP_HUMAN 1 209
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 0HH A 210 29
HET MES A 211 12
HET 0HH B 210 29
HET MES B 211 12
HETNAM 0HH L-GAMMA-GLUTAMYL-S-NONYL-L-CYSTEINYLGLYCINE
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
FORMUL 3 0HH 2(C19 H35 N3 O6 S)
FORMUL 4 MES 2(C6 H13 N O4 S)
FORMUL 7 HOH *181(H2 O)
HELIX 1 1 GLY A 12 ASP A 23 5 12
HELIX 2 2 VAL A 35 GLU A 40 1 6
HELIX 3 3 SER A 42 SER A 46 1 5
HELIX 4 4 SER A 65 LEU A 76 1 12
HELIX 5 5 GLN A 83 THR A 109 1 27
HELIX 6 6 TYR A 111 GLN A 135 1 25
HELIX 7 7 GLN A 137 GLY A 139 5 3
HELIX 8 8 PHE A 150 LEU A 165 1 16
HELIX 9 9 CYS A 169 ALA A 172 5 4
HELIX 10 10 PRO A 174 SER A 184 1 11
HELIX 11 11 PRO A 187 ALA A 194 1 8
HELIX 12 12 PRO A 196 VAL A 199 1 4
HELIX 13 13 GLY B 12 ASP B 23 5 12
HELIX 14 14 VAL B 35 GLU B 40 1 6
HELIX 15 15 SER B 42 SER B 46 1 5
HELIX 16 16 SER B 65 LEU B 76 1 12
HELIX 17 17 GLN B 83 THR B 109 1 27
HELIX 18 18 TYR B 111 GLN B 135 1 25
HELIX 19 19 GLN B 137 GLY B 139 5 3
HELIX 20 20 PHE B 150 LEU B 165 1 16
HELIX 21 21 PRO B 174 SER B 184 1 11
HELIX 22 22 PRO B 187 ALA B 194 1 8
HELIX 23 23 PRO B 196 VAL B 199 1 4
SHEET 1 A 4 TRP A 28 VAL A 33 0
SHEET 2 A 4 TYR A 3 PHE A 8 1 N TYR A 3 O LYS A 29
SHEET 3 A 4 LYS A 54 ASP A 57 -1 N GLN A 56 O THR A 4
SHEET 4 A 4 LEU A 60 TYR A 63 -1 N LEU A 62 O PHE A 55
SHEET 1 B 4 TRP B 28 VAL B 33 0
SHEET 2 B 4 TYR B 3 PHE B 8 1 N TYR B 3 O LYS B 29
SHEET 3 B 4 LYS B 54 ASP B 57 -1 N GLN B 56 O THR B 4
SHEET 4 B 4 LEU B 60 TYR B 63 -1 N LEU B 62 O PHE B 55
CISPEP 1 LEU A 52 PRO A 53 0 0.61
CISPEP 2 LEU B 52 PRO B 53 0 0.74
SITE 1 AC1 15 TYR A 7 PHE A 8 VAL A 10 ARG A 13
SITE 2 AC1 15 TRP A 38 LYS A 44 GLN A 51 LEU A 52
SITE 3 AC1 15 PRO A 53 GLN A 64 SER A 65 TYR A 108
SITE 4 AC1 15 HOH A 240 HOH A 291 ASP B 98
SITE 1 AC2 19 ASP A 98 TYR B 7 PHE B 8 VAL B 10
SITE 2 AC2 19 ARG B 13 TRP B 38 LYS B 44 GLY B 50
SITE 3 AC2 19 GLN B 51 LEU B 52 PRO B 53 GLN B 64
SITE 4 AC2 19 SER B 65 TYR B 108 GLY B 205 HOH B 214
SITE 5 AC2 19 HOH B 220 HOH B 310 HOH B 311
SITE 1 AC3 5 ALA A 22 TRP A 28 GLU A 30 GLU A 197
SITE 2 AC3 5 ASP B 171
SITE 1 AC4 5 ASP A 171 ALA B 22 TRP B 28 GLU B 30
SITE 2 AC4 5 GLU B 197
CRYST1 77.912 89.427 68.945 90.00 97.47 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 0.012835 0.000000 0.001683 0.00000
SCALE2 0.000000 0.011182 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014628 0.00000
MTRIX1 1 0.935996 0.142200 0.322010 -6.09111 1
MTRIX2 1 0.143708 -0.989434 0.019214 21.05086 1
MTRIX3 1 0.321339 0.028291 -0.946541 27.09144 1
(ATOM LINES ARE NOT SHOWN.)
END