HEADER HYDROLASE/HYDROLASE INHIBITOR 06-JUN-96 1PAU
TITLE CRYSTAL STRUCTURE OF THE COMPLEX OF APOPAIN WITH THE TETRAPEPTIDE
TITLE 2 ALDEHYDE INHIBITOR AC-DEVD-CHO
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APOPAIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CASPASE-3, CPP32, YAMA;
COMPND 5 EC: 3.4.22.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: APOPAIN;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: CASPASE-3, CPP32, YAMA;
COMPND 11 EC: 3.4.22.-;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: ACE-ASP-GLU-VAL-ASJ;
COMPND 15 CHAIN: C;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 13 MOL_ID: 3;
SOURCE 14 SYNTHETIC: YES
KEYWDS CYSTEINE PROTEASE, CASPASE-3, APOPAIN, CPP32, YAMA, PROTEASE-
KEYWDS 2 INHIBITOR COMPLEX, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.ROTONDA,J.W.BECKER
REVDAT 5 09-AUG-23 1PAU 1 LINK
REVDAT 4 29-NOV-17 1PAU 1 HELIX
REVDAT 3 13-JUL-11 1PAU 1 VERSN
REVDAT 2 24-FEB-09 1PAU 1 VERSN
REVDAT 1 07-JUL-97 1PAU 0
JRNL AUTH J.ROTONDA,D.W.NICHOLSON,K.M.FAZIL,M.GALLANT,Y.GAREAU,
JRNL AUTH 2 M.LABELLE,E.P.PETERSON,D.M.RASPER,R.RUEL,J.P.VAILLANCOURT,
JRNL AUTH 3 N.A.THORNBERRY,J.W.BECKER
JRNL TITL THE THREE-DIMENSIONAL STRUCTURE OF APOPAIN/CPP32, A KEY
JRNL TITL 2 MEDIATOR OF APOPTOSIS.
JRNL REF NAT.STRUCT.BIOL. V. 3 619 1996
JRNL REFN ISSN 1072-8368
JRNL PMID 8673606
JRNL DOI 10.1038/NSB0796-619
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.W.NICHOLSON,A.ALI,N.A.THORNBERRY,J.P.VAILLANCOURT,
REMARK 1 AUTH 2 C.K.DING,M.GALLANT,Y.GAREAU,P.R.GRIFFIN,M.LABELLE,
REMARK 1 AUTH 3 Y.A.LAZEBNIK,N.A.MUNDAY,S.M.RAJU,M.E.SMULSON,T.T.YAMIN,
REMARK 1 AUTH 4 V.L.YU,D.K.MILLER
REMARK 1 TITL IDENTIFICATION AND INHIBITION OF THE ICE/CED-3 PROTEASE
REMARK 1 TITL 2 NECESSARY FOR MAMMALIAN APOPTOSIS
REMARK 1 REF NATURE V. 376 37 1995
REMARK 1 REFN ISSN 0028-0836
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 78.0
REMARK 3 NUMBER OF REFLECTIONS : 7987
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE-R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.600
REMARK 3 FREE R VALUE TEST SET COUNT : 845
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.59
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 35.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 321
REMARK 3 BIN R VALUE (WORKING SET) : 0.2570
REMARK 3 BIN FREE R VALUE : 0.3300
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 38
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 : 1905
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 34
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.34
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.56
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) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.308
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.14
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.091
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 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 : APOPAIN.PAR
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : APOPAIN.PRO
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THERE IS NO ELECTRON DENSITY FOR RESIDUES A 145 - A 149,
REMARK 3 A 296 - A 297, B 310 - B 319, AND B 402, PRESUMABLY DUE TO
REMARK 3 DISORDER. MASS SPECTROMETRY INDICATES THAT THESE RESIDUES
REMARK 3 ARE PRESENT IN THE SPECIES CRYSTALLIZED.
REMARK 4
REMARK 4 1PAU 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_1000175574.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-NOV-95
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 5.0-8.0
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 : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SAINT
REMARK 200 DATA SCALING SOFTWARE : SAINT
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8929
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 36.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.1
REMARK 200 DATA REDUNDANCY : 2.330
REMARK 200 R MERGE (I) : 0.06340
REMARK 200 R SYM (I) : 0.05550
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.27
REMARK 200 R MERGE FOR SHELL (I) : 0.25700
REMARK 200 R SYM FOR SHELL (I) : 0.26200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.590
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: PROTEIN COMPONENT OF INTERLEUKIN-1BETA CONVERTING
REMARK 200 ENZYME (PDB ENTRY 1ICE)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROP VAPOR DIFFUSION. 1.5
REMARK 280 MICROLITER DROPS OF PROTEIN:INHIBITOR SOLUTION (8.7 MG/ML IN 10
REMARK 280 MILLIMOLAR TRIS-HCL PH 8.5, 10 MILLIMOLAR DTT, 3 MILLIMOLAR
REMARK 280 SODIUM AZIDE) WERE MIXED WITH AN EQUAL VOLUME OF RESERVOIR
REMARK 280 BUFFER (7% PEG-6000 (W/W), 0.10 MOLAR SODIUM CITRATE PH 5.0, 10
REMARK 280 MILLIMOLAR DTT, 3 MILLIMOLAR SODIUM AZIDE) AND INCUBATED AT ROOM
REMARK 280 TEMPERATURE, VAPOR DIFFUSION - HANGING DROP, VAPOR DIFFUSION,
REMARK 280 HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 34.90500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.31000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 48.39500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 34.90500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.31000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 48.39500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 34.90500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 42.31000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 48.39500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 34.90500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 42.31000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 48.39500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 33490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -177.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 69.81000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 169.24000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 69.81000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 169.24000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 69.81000
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 400
REMARK 400 COMPOUND
REMARK 400 THE INHIBITOR IS COVALENTLY CONNECTED TO CYS OF THE ENZYME TO FORM
REMARK 400 A HEMITHIOKETAL.
REMARK 400
REMARK 400 THE AC-ASP-GLU-VAL-ASP-ALDEHYDE IS PEPTIDE-LIKE, A MEMBER OF
REMARK 400 INHIBITOR CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: AC-ASP-GLU-VAL-ASP-ALDEHYDE
REMARK 400 CHAIN: C
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: NULL
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 SER A 145
REMARK 465 GLY A 146
REMARK 465 ILE A 147
REMARK 465 SER A 148
REMARK 465 LEU A 149
REMARK 465 THR A 296
REMARK 465 ASP A 297
REMARK 465 SER B 310
REMARK 465 GLY B 311
REMARK 465 VAL B 312
REMARK 465 ASP B 313
REMARK 465 ASP B 314
REMARK 465 ASP B 315
REMARK 465 MET B 316
REMARK 465 ALA B 317
REMARK 465 CYS B 318
REMARK 465 HIS B 319
REMARK 465 HIS B 402
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 SER A 236 -176.93 -177.47
REMARK 500 LYS B 363 -38.30 -143.41
REMARK 500 PHE B 400 42.08 -102.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: S1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: INHIBITOR BINDING SUB-SITE S1.
REMARK 800
REMARK 800 SITE_IDENTIFIER: S2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: INHIBITOR BINDING SUB-SITE S2.
REMARK 800
REMARK 800 SITE_IDENTIFIER: S3
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: INHIBITOR BINDING SUB-SITE S3.
REMARK 800
REMARK 800 SITE_IDENTIFIER: S4
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: INHIBITOR BINDING SUB-SITE S4.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN C OF ACE-ASP-GLU-VAL-ASA
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AMINO ACID RESIDUES ARE NUMBERED TO FACILITATE COMPARISON
REMARK 999 WITH THE INTERLEUKIN 1-BETA CONVERTING ENZYME (ICE, PDB
REMARK 999 ENTRY 1ICE). RESIDUES IN APOPAIN ARE ASSIGNED THE NUMBERS
REMARK 999 OF THE HOMOLOGOUS RESIDUES IN THE ALIGNED THREE-DIMENSIONAL
REMARK 999 STRUCTURE OF ICE. APOPAIN SEQUENCE NUMBERS ARE OMITTED
REMARK 999 WHEN NO ICE-RELATED RESIDUE IS PRESENT IN APOPAIN, AND
REMARK 999 APOPAIN-SPECIFIC INSERTIONS ARE INDICATED BY THE ADDITION
REMARK 999 OF LETTERS TO THE ICE SEQUENCE NUMBERS.
DBREF 1PAU A 145 297 UNP P42574 ICE3_HUMAN 29 175
DBREF 1PAU B 310 402 UNP P42574 ICE3_HUMAN 176 277
DBREF 1PAU C 501 505 PDB 1PAU 1PAU 501 505
SEQRES 1 A 147 SER GLY ILE SER LEU ASP ASN SER TYR LYS MET ASP TYR
SEQRES 2 A 147 PRO GLU MET GLY LEU CYS ILE ILE ILE ASN ASN LYS ASN
SEQRES 3 A 147 PHE HIS LYS SER THR GLY MET THR SER ARG SER GLY THR
SEQRES 4 A 147 ASP VAL ASP ALA ALA ASN LEU ARG GLU THR PHE ARG ASN
SEQRES 5 A 147 LEU LYS TYR GLU VAL ARG ASN LYS ASN ASP LEU THR ARG
SEQRES 6 A 147 GLU GLU ILE VAL GLU LEU MET ARG ASP VAL SER LYS GLU
SEQRES 7 A 147 ASP HIS SER LYS ARG SER SER PHE VAL CYS VAL LEU LEU
SEQRES 8 A 147 SER HIS GLY GLU GLU GLY ILE ILE PHE GLY THR ASN GLY
SEQRES 9 A 147 PRO VAL ASP LEU LYS LYS ILE THR ASN PHE PHE ARG GLY
SEQRES 10 A 147 ASP ARG CYS ARG SER LEU THR GLY LYS PRO LYS LEU PHE
SEQRES 11 A 147 ILE ILE GLN ALA CYS ARG GLY THR GLU LEU ASP CYS GLY
SEQRES 12 A 147 ILE GLU THR ASP
SEQRES 1 B 102 SER GLY VAL ASP ASP ASP MET ALA CYS HIS LYS ILE PRO
SEQRES 2 B 102 VAL GLU ALA ASP PHE LEU TYR ALA TYR SER THR ALA PRO
SEQRES 3 B 102 GLY TYR TYR SER TRP ARG ASN SER LYS ASP GLY SER TRP
SEQRES 4 B 102 PHE ILE GLN SER LEU CYS ALA MET LEU LYS GLN TYR ALA
SEQRES 5 B 102 ASP LYS LEU GLU PHE MET HIS ILE LEU THR ARG VAL ASN
SEQRES 6 B 102 ARG LYS VAL ALA THR GLU PHE GLU SER PHE SER PHE ASP
SEQRES 7 B 102 ALA THR PHE HIS ALA LYS LYS GLN ILE PRO CYS ILE VAL
SEQRES 8 B 102 SER MET LEU THR LYS GLU LEU TYR PHE TYR HIS
SEQRES 1 C 5 ACE ASP GLU VAL ASJ
HET ACE C 501 3
HET ASJ C 505 8
HETNAM ACE ACETYL GROUP
HETNAM ASJ (3S)-3-AMINO-4-HYDROXYBUTANOIC ACID
FORMUL 3 ACE C2 H4 O
FORMUL 3 ASJ C4 H9 N O3
FORMUL 4 HOH *34(H2 O)
HELIX 1 A THR A 182 ASN A 195 1 14
HELIX 2 B ARG A 208 LYS A 220 1 13
HELIX 3 C LEU A 258 PHE A 264 1 7
HELIX 4 D TRP B 348 ALA B 361 1 14
HELIX 5 E PHE B 366 GLU B 379A 1 15
SHEET 1 1 6 GLU A 199 ASN A 204 0
SHEET 2 1 6 GLU A 162 ASN A 169 1 O CYS A 165 N ARG A 201
SHEET 3 1 6 ARG A 227 LEU A 235 1 O VAL A 231 N ILE A 166
SHEET 4 1 6 LYS A 278 GLN A 283 1 O LEU A 279 N CYS A 232
SHEET 5 1 6 PHE B 327 TYR B 331 1 O LEU B 328 N PHE A 280
SHEET 6 1 6 CYS B 388 MET B 393 -1 O VAL B 390 N TYR B 329
SHEET 1 2 3 GLY B 346 SER B 347 0
SHEET 2 2 3 TRP B 340 ASN B 342 -1 O ASN B 342 N GLY B 346
SHEET 3 2 3 ASP C 502 VAL C 504 -1 O GLU C 503 N ARG B 341
SHEET 1 3 3 GLY A 238 GLU A 239 0
SHEET 2 3 3 ILE A 242 GLY A 245 -1 O ILE A 242 N GLU A 239
SHEET 3 3 3 GLY A 254 ASP A 257 -1 O VAL A 256 N ILE A 243
LINK SG CYS A 285 C ASJ C 505 1555 1555 1.77
LINK C ACE C 501 N ASP C 502 1555 1555 1.33
LINK C VAL C 504 N ASJ C 505 1555 1555 1.33
SITE 1 S1 10 ARG A 179 SER A 236 HIS A 237 GLY A 238
SITE 2 S1 10 GLN A 283 ALA A 284 CYS A 285 SER B 339
SITE 3 S1 10 TRP B 340 ARG B 341
SITE 1 S2 6 CYS A 285 TYR B 338 SER B 339 TRP B 340
SITE 2 S2 6 ARG B 341 PHE B 381H
SITE 1 S3 6 SER A 178 ARG A 179 SER A 180 TRP B 340
SITE 2 S3 6 ARG B 341 SER B 343
SITE 1 S4 8 TRP B 340 ARG B 341 ASN B 342 GLY B 346
SITE 2 S4 8 SER B 347 TRP B 348 SER B 381A PHE B 381B
SITE 1 AC1 15 SER A 175A ARG A 179 HIS A 237 GLN A 283
SITE 2 AC1 15 CYS A 285 TYR B 338 SER B 339 TRP B 340
SITE 3 AC1 15 ARG B 341 ASN B 342 SER B 343 SER B 381A
SITE 4 AC1 15 PHE B 381B HOH B 626 HOH C 619
CRYST1 69.810 84.620 96.790 90.00 90.00 90.00 I 2 2 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 0.014325 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011818 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010332 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
