HEADER HYDROLASE/HYDROLASE INHIBITOR 13-OCT-10 3P8F
TITLE CRYSTAL STRUCTURE OF MT-SP1 IN COMPLEX WITH SFTI-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ST14 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN (UNP RESIDUES 182-422);
COMPND 5 SYNONYM: MEMBRANE-TYPE SERINE PROTEASE 1;
COMPND 6 EC: 3.4.21.109;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: TRYPSIN INHIBITOR 1;
COMPND 11 CHAIN: I;
COMPND 12 FRAGMENT: UNP RESIDUES 40-53;
COMPND 13 SYNONYM: SFTI-1;
COMPND 14 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: ST14;
SOURCE 6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: YEAST;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: X33;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PPICZALPHA;
SOURCE 12 MOL_ID: 2;
SOURCE 13 SYNTHETIC: YES;
SOURCE 14 ORGANISM_SCIENTIFIC: HELIANTHUS ANNUUS;
SOURCE 15 ORGANISM_COMMON: COMMON SUNFLOWER;
SOURCE 16 ORGANISM_TAXID: 4232;
SOURCE 17 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED.
KEYWDS PROTEIN-INHIBITOR COMPLEX, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.YUAN,M.HUANG,L.CHEN
REVDAT 3 08-NOV-17 3P8F 1 REMARK
REVDAT 2 15-APR-15 3P8F 1 REMARK
REVDAT 1 10-AUG-11 3P8F 0
JRNL AUTH C.YUAN,L.CHEN,E.J.MEEHAN,N.DALY,D.J.CRAIK,M.HUANG,J.C.NGO
JRNL TITL STRUCTURE OF CATALYTIC DOMAIN OF MATRIPTASE IN COMPLEX WITH
JRNL TITL 2 SUNFLOWER TRYPSIN INHIBITOR-1.
JRNL REF BMC STRUCT.BIOL. V. 11 30 2011
JRNL REFN ESSN 1472-6807
JRNL PMID 21693064
JRNL DOI 10.1186/1472-6807-11-30
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.79
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 17987
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 964
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 25.7960 - 3.8222 0.95 2665 100 0.1637 0.1798
REMARK 3 2 3.8222 - 3.0353 0.99 2582 137 0.1841 0.2504
REMARK 3 3 3.0353 - 2.6521 1.00 2597 138 0.2082 0.2680
REMARK 3 4 2.6521 - 2.4098 1.00 2545 163 0.2229 0.2657
REMARK 3 5 2.4098 - 2.2372 1.00 2537 138 0.2285 0.3074
REMARK 3 6 2.2372 - 2.1053 1.00 2527 154 0.2446 0.3235
REMARK 3 7 2.1053 - 1.9999 0.99 2531 134 0.3027 0.3535
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.95
REMARK 3 K_SOL : 0.32
REMARK 3 B_SOL : 39.04
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.680
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.150
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) : -1.02540
REMARK 3 B22 (A**2) : -1.02540
REMARK 3 B33 (A**2) : 2.05080
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 : 0.003 2047
REMARK 3 ANGLE : 0.643 2777
REMARK 3 CHIRALITY : 0.045 292
REMARK 3 PLANARITY : 0.003 366
REMARK 3 DIHEDRAL : 14.188 733
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -9.6529 -20.4148 -21.1565
REMARK 3 T TENSOR
REMARK 3 T11: 0.2387 T22: 0.3681
REMARK 3 T33: 0.3292 T12: 0.0355
REMARK 3 T13: 0.0781 T23: 0.0911
REMARK 3 L TENSOR
REMARK 3 L11: 2.6626 L22: 3.9208
REMARK 3 L33: 4.5134 L12: 0.4130
REMARK 3 L13: 0.2045 L23: -1.2449
REMARK 3 S TENSOR
REMARK 3 S11: 0.2017 S12: 0.0022 S13: 0.1711
REMARK 3 S21: -0.2827 S22: 0.0408 S23: 0.1056
REMARK 3 S31: 0.0718 S32: -0.3080 S33: -0.1825
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES
REMARK 4
REMARK 4 3P8F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-OCT-10.
REMARK 100 THE DEPOSITION ID IS D_1000062086.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUL-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.04
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19001
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 59.030
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 12.10
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 11.10
REMARK 200 R MERGE FOR SHELL (I) : 0.52600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS.HCL PH 8.0, 22% PEG 8K, 20MM
REMARK 280 CACL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 297K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 47.04700
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 37.93100
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 37.93100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 23.52350
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 37.93100
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 37.93100
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 70.57050
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 37.93100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 37.93100
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 23.52350
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 37.93100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 37.93100
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 70.57050
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 47.04700
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: 1980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, I
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 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 THE TRYPSIN INHIBITOR 1 IS POLYPEPTIDE, A MEMBER OF TRYPSIN
REMARK 400 INHIBITOR CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: TRYPSIN INHIBITOR 1
REMARK 400 CHAIN: I
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: NULL
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 N GLY I 1 O ASP I 14 1.71
REMARK 500 O HOH A 1146 O HOH A 1169 1.91
REMARK 500 O THR A 150 O HOH A 1158 1.93
REMARK 500 CZ ARG A 119 OE1 GSH A 1001 1.97
REMARK 500 OH TYR A 114 O HOH A 1186 2.04
REMARK 500 OE2 GLU A 82 O HOH A 1178 2.11
REMARK 500 O ALA A 126 O HOH A 1190 2.12
REMARK 500 NH2 ARG A 119 OE1 GSH A 1001 2.12
REMARK 500 NH1 ARG A 119 OE1 GSH A 1001 2.12
REMARK 500 O HOH A 1159 O HOH I 106 2.12
REMARK 500 OD1 ASP A 125 O HOH A 1185 2.13
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 O HOH A 1183 O HOH A 1185 6544 1.83
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 ARG A 60C 5.53 -62.30
REMARK 500 SER A 214 -76.30 -122.75
REMARK 500 LYS I 5 35.06 -94.73
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 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN I OF TRYPSIN INHIBITOR 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3P8G RELATED DB: PDB
DBREF 3P8F A 16 244 UNP Q8WVC1 Q8WVC1_HUMAN 182 422
DBREF 3P8F I 1 14 UNP Q4GWU5 SFTI1_HELAN 40 53
SEQADV 3P8F GLN A 164 UNP Q8WVC1 ASN 339 ENGINEERED MUTATION
SEQRES 1 A 241 VAL VAL GLY GLY THR ASP ALA ASP GLU GLY GLU TRP PRO
SEQRES 2 A 241 TRP GLN VAL SER LEU HIS ALA LEU GLY GLN GLY HIS ILE
SEQRES 3 A 241 CYS GLY ALA SER LEU ILE SER PRO ASN TRP LEU VAL SER
SEQRES 4 A 241 ALA ALA HIS CYS TYR ILE ASP ASP ARG GLY PHE ARG TYR
SEQRES 5 A 241 SER ASP PRO THR GLN TRP THR ALA PHE LEU GLY LEU HIS
SEQRES 6 A 241 ASP GLN SER GLN ARG SER ALA PRO GLY VAL GLN GLU ARG
SEQRES 7 A 241 ARG LEU LYS ARG ILE ILE SER HIS PRO PHE PHE ASN ASP
SEQRES 8 A 241 PHE THR PHE ASP TYR ASP ILE ALA LEU LEU GLU LEU GLU
SEQRES 9 A 241 LYS PRO ALA GLU TYR SER SER MET VAL ARG PRO ILE CYS
SEQRES 10 A 241 LEU PRO ASP ALA SER HIS VAL PHE PRO ALA GLY LYS ALA
SEQRES 11 A 241 ILE TRP VAL THR GLY TRP GLY HIS THR GLN TYR GLY GLY
SEQRES 12 A 241 THR GLY ALA LEU ILE LEU GLN LYS GLY GLU ILE ARG VAL
SEQRES 13 A 241 ILE GLN GLN THR THR CYS GLU ASN LEU LEU PRO GLN GLN
SEQRES 14 A 241 ILE THR PRO ARG MET MET CYS VAL GLY PHE LEU SER GLY
SEQRES 15 A 241 GLY VAL ASP SER CYS GLN GLY ASP SER GLY GLY PRO LEU
SEQRES 16 A 241 SER SER VAL GLU ALA ASP GLY ARG ILE PHE GLN ALA GLY
SEQRES 17 A 241 VAL VAL SER TRP GLY ASP GLY CYS ALA GLN ARG ASN LYS
SEQRES 18 A 241 PRO GLY VAL TYR THR ARG LEU PRO LEU PHE ARG ASP TRP
SEQRES 19 A 241 ILE LYS GLU ASN THR GLY VAL
SEQRES 1 I 14 GLY ARG CYS THR LYS SER ILE PRO PRO ILE CYS PHE PRO
SEQRES 2 I 14 ASP
HET GSH A1001 20
HETNAM GSH GLUTATHIONE
FORMUL 3 GSH C10 H17 N3 O6 S
FORMUL 4 HOH *101(H2 O)
HELIX 1 1 ALA A 55 ILE A 60 5 6
HELIX 2 2 ASP A 60I THR A 62 5 3
HELIX 3 3 GLN A 164 LEU A 172 1 9
HELIX 4 4 PHE A 234 GLY A 243 1 10
SHEET 1 A 6 THR A 20 ASP A 21 0
SHEET 2 A 6 GLN A 156 VAL A 162 -1 O LYS A 157 N THR A 20
SHEET 3 A 6 ALA A 135 GLY A 140 -1 N ILE A 136 O ILE A 160
SHEET 4 A 6 PRO A 198 VAL A 202 -1 O SER A 200 N TRP A 137
SHEET 5 A 6 ILE A 207 ASP A 217 -1 O PHE A 208 N SER A 201
SHEET 6 A 6 ARG I 2 THR I 4 -1 O CYS I 3 N GLY A 216
SHEET 1 B 6 THR A 20 ASP A 21 0
SHEET 2 B 6 GLN A 156 VAL A 162 -1 O LYS A 157 N THR A 20
SHEET 3 B 6 MET A 180 GLY A 184 -1 O GLY A 184 N ARG A 161
SHEET 4 B 6 GLY A 226 ARG A 230 -1 O TYR A 228 N MET A 181
SHEET 5 B 6 ILE A 207 ASP A 217 -1 N TRP A 215 O VAL A 227
SHEET 6 B 6 ARG I 2 THR I 4 -1 O CYS I 3 N GLY A 216
SHEET 1 C 7 GLN A 30 ALA A 35 0
SHEET 2 C 7 GLY A 39 LEU A 46 -1 O ALA A 44 N VAL A 31
SHEET 3 C 7 TRP A 51 SER A 54 -1 O VAL A 53 N SER A 45
SHEET 4 C 7 ALA A 104 LEU A 108 -1 O LEU A 106 N LEU A 52
SHEET 5 C 7 GLN A 81 SER A 90 -1 N LYS A 86 O GLU A 107
SHEET 6 C 7 TRP A 64 LEU A 68 -1 N ALA A 66 O ARG A 83
SHEET 7 C 7 GLN A 30 ALA A 35 -1 N SER A 32 O PHE A 67
SSBOND 1 CYS A 42 CYS A 58 1555 1555 2.03
SSBOND 2 CYS A 168 CYS A 182 1555 1555 2.03
SSBOND 3 CYS A 191 CYS A 220 1555 1555 2.04
SSBOND 4 CYS I 3 CYS I 11 1555 1555 2.04
LINK SG CYS A 122 SG2 GSH A1001 1555 1555 2.20
LINK N GLY I 1 C ASP I 14 1555 1555 1.44
CISPEP 1 ILE I 7 PRO I 8 0 -2.87
SITE 1 AC1 4 ARG A 119 PRO A 120 CYS A 122 ILE A 207
SITE 1 AC2 20 ILE A 41 CYS A 42 HIS A 57 ARG A 60C
SITE 2 AC2 20 TYR A 60G PHE A 97 PHE A 99 ASP A 125
SITE 3 AC2 20 GLN A 175 SER A 190 CYS A 191 GLN A 192
SITE 4 AC2 20 GLY A 193 ASP A 194 SER A 195 PHE A 208
SITE 5 AC2 20 SER A 214 TRP A 215 GLY A 216 ASP A 217
CRYST1 75.862 75.862 94.094 90.00 90.00 90.00 P 41 21 2 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 0.013182 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013182 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010628 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
