HEADER HYDROLASE 14-NOV-03 1RHJ
TITLE CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE-3 WITH A PRYAZINONE
TITLE 2 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASPASE-3;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: P17 SUBUNIT;
COMPND 5 SYNONYM: CYSTEINE PROTEASE CPP32, YAMA PROTEIN, CPP-32, APOPAIN,
COMPND 6 CASP-3, SREBP CLEAVAGE ACTIVITY 1, SCA-1;
COMPND 7 EC: 3.4.22.-;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: CASPASE-3;
COMPND 11 CHAIN: B, D;
COMPND 12 FRAGMENT: P12 SUBUNIT;
COMPND 13 SYNONYM: CYSTEINE PROTEASE CPP32, YAMA PROTEIN, CPP-32, APOPAIN,
COMPND 14 CASP-3, SREBP CLEAVAGE ACTIVITY 1, SCA-1;
COMPND 15 EC: 3.4.22.-;
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 GENE: CASP3, CPP32;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET20B+;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: CASP3, CPP32;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS CYSTEINE PROTEASE, CASPASE-3, APOPAIN, CPP32, YAMA, COMPLEX
KEYWDS 2 (PROTEASE-INHIBITOR), HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.W.BECKER,J.ROTONDA,S.M.SOISSON
REVDAT 5 20-SEP-23 1RHJ 1 REMARK
REVDAT 4 21-DEC-22 1RHJ 1 REMARK SEQADV LINK
REVDAT 3 11-OCT-17 1RHJ 1 REMARK
REVDAT 2 24-FEB-09 1RHJ 1 VERSN
REVDAT 1 11-MAY-04 1RHJ 0
JRNL AUTH J.W.BECKER,J.ROTONDA,S.M.SOISSON,R.ASPIOTIS,C.BAYLY,
JRNL AUTH 2 S.FRANCOEUR,M.GALLANT,M.GARCIA-CALVO,A.GIROUX,E.GRIMM,Y.HAN,
JRNL AUTH 3 D.MCKAY,D.W.NICHOLSON,E.PETERSON,J.RENAUD,S.ROY,
JRNL AUTH 4 N.THORNBERRY,R.ZAMBONI
JRNL TITL REDUCING THE PEPTIDYL FEATURES OF CASPASE-3 INHIBITORS: A
JRNL TITL 2 STRUCTURAL ANALYSIS.
JRNL REF J.MED.CHEM. V. 47 2466 2004
JRNL REFN ISSN 0022-2623
JRNL PMID 15115390
JRNL DOI 10.1021/JM0305523
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX 2002
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN,ACCELRYS
REMARK 3 : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,
REMARK 3 : YIP,DZAKULA)
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 175071.300
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.1
REMARK 3 NUMBER OF REFLECTIONS : 29784
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 + TEST SET) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2987
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 29784
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4086
REMARK 3 BIN R VALUE (WORKING SET) : 0.2250
REMARK 3 BIN FREE R VALUE : 0.2850
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 469
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.013
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3740
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 82
REMARK 3 SOLVENT ATOMS : 233
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.58000
REMARK 3 B22 (A**2) : 3.84000
REMARK 3 B33 (A**2) : -4.42000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -3.76000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.18
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.27
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.000
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) : 1.320 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.070 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.220 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.200 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 40.66
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 : PROTEIN_REP.P
REMARK 3 PARAMETER FILE 2 : WATER_REP.PAR
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : PYR.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : PYR.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 1RHJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000020749.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-SEP-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30288
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 19.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 200 DATA REDUNDANCY : 3.360
REMARK 200 R MERGE (I) : 0.05600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.41
REMARK 200 R MERGE FOR SHELL (I) : 0.16400
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: CNX
REMARK 200 STARTING MODEL: PROTEIN PART OF 1PAU.PDB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG-6000, 100 MM CITRATE, 20 MM L
REMARK 280 -CYSTEINE, 5 MM GLYCEROL, 3 MM NAN(3), PH 4.8, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 34.38200
REMARK 290 SMTRY3 2 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 300 REMARK: THE ASYMMETRIC UNIT CONTAINS ONE BIOLOGICAL ASSEMBLY.
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 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 465 LEU B 403
REMARK 465 GLU B 404
REMARK 465 HIS B 405
REMARK 465 HIS B 406
REMARK 465 HIS B 407
REMARK 465 HIS B 408
REMARK 465 HIS B 409
REMARK 465 HIS B 410
REMARK 465 SER C 645
REMARK 465 GLY C 646
REMARK 465 ILE C 647
REMARK 465 SER C 648
REMARK 465 LEU C 649
REMARK 465 THR C 796
REMARK 465 ASP C 797
REMARK 465 SER D 810
REMARK 465 GLY D 811
REMARK 465 VAL D 812
REMARK 465 ASP D 813
REMARK 465 ASP D 814
REMARK 465 ASP D 815
REMARK 465 MET D 816
REMARK 465 ALA D 817
REMARK 465 CYS D 818
REMARK 465 HIS D 819
REMARK 465 HIS D 902
REMARK 465 LEU D 903
REMARK 465 GLU D 904
REMARK 465 HIS D 905
REMARK 465 HIS D 906
REMARK 465 HIS D 907
REMARK 465 HIS D 908
REMARK 465 HIS D 909
REMARK 465 HIS D 910
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 175A -1.66 -58.09
REMARK 500 LYS A 197 30.85 78.59
REMARK 500 ASP A 205 73.49 35.98
REMARK 500 SER A 236 -170.27 -175.07
REMARK 500 CYS A 270 79.46 -119.97
REMARK 500 LYS B 363 -58.21 -130.85
REMARK 500 PHE B 400 30.87 -84.23
REMARK 500 LYS C 697 32.34 72.22
REMARK 500 ASP C 705 75.67 42.63
REMARK 500 SER C 736 -170.78 -178.38
REMARK 500 ASP D 826 32.98 74.27
REMARK 500 LYS D 863 -46.64 -145.08
REMARK 500 PHE D 900 30.07 -84.79
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 PZN C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PZN A 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PAU RELATED DB: PDB
REMARK 900 CASPASE-3 COMPLEX WITH ACETYL-ASP-GLU-VAL-ASP-ALDEHYDE
REMARK 900 RELATED ID: 1RHK RELATED DB: PDB
REMARK 900 RELATED ID: 1RHM RELATED DB: PDB
REMARK 900 RELATED ID: 1RHQ RELATED DB: PDB
REMARK 900 RELATED ID: 1RHR RELATED DB: PDB
REMARK 900 RELATED ID: 1RHU RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE HIS TAGS ON CHAINS B AND D WERE NOT
REMARK 999 CLEAVED FOR THIS ENTRY.
DBREF 1RHJ A 145 297 UNP P42574 CASP3_HUMAN 29 175
DBREF 1RHJ B 310 402 UNP P42574 CASP3_HUMAN 176 277
DBREF 1RHJ C 645 797 UNP P42574 CASP3_HUMAN 29 175
DBREF 1RHJ D 810 902 UNP P42574 CASP3_HUMAN 176 277
SEQADV 1RHJ GLU B 324 UNP P42574 ASP 190 VARIANT
SEQADV 1RHJ LEU B 403 UNP P42574 EXPRESSION TAG
SEQADV 1RHJ GLU B 404 UNP P42574 EXPRESSION TAG
SEQADV 1RHJ HIS B 405 UNP P42574 EXPRESSION TAG
SEQADV 1RHJ HIS B 406 UNP P42574 EXPRESSION TAG
SEQADV 1RHJ HIS B 407 UNP P42574 EXPRESSION TAG
SEQADV 1RHJ HIS B 408 UNP P42574 EXPRESSION TAG
SEQADV 1RHJ HIS B 409 UNP P42574 EXPRESSION TAG
SEQADV 1RHJ HIS B 410 UNP P42574 EXPRESSION TAG
SEQADV 1RHJ GLU D 824 UNP P42574 ASP 190 VARIANT
SEQADV 1RHJ LEU D 903 UNP P42574 EXPRESSION TAG
SEQADV 1RHJ GLU D 904 UNP P42574 EXPRESSION TAG
SEQADV 1RHJ HIS D 905 UNP P42574 EXPRESSION TAG
SEQADV 1RHJ HIS D 906 UNP P42574 EXPRESSION TAG
SEQADV 1RHJ HIS D 907 UNP P42574 EXPRESSION TAG
SEQADV 1RHJ HIS D 908 UNP P42574 EXPRESSION TAG
SEQADV 1RHJ HIS D 909 UNP P42574 EXPRESSION TAG
SEQADV 1RHJ HIS D 910 UNP P42574 EXPRESSION TAG
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 110 SER GLY VAL ASP ASP ASP MET ALA CYS HIS LYS ILE PRO
SEQRES 2 B 110 VAL GLU ALA ASP PHE LEU TYR ALA TYR SER THR ALA PRO
SEQRES 3 B 110 GLY TYR TYR SER TRP ARG ASN SER LYS ASP GLY SER TRP
SEQRES 4 B 110 PHE ILE GLN SER LEU CYS ALA MET LEU LYS GLN TYR ALA
SEQRES 5 B 110 ASP LYS LEU GLU PHE MET HIS ILE LEU THR ARG VAL ASN
SEQRES 6 B 110 ARG LYS VAL ALA THR GLU PHE GLU SER PHE SER PHE ASP
SEQRES 7 B 110 ALA THR PHE HIS ALA LYS LYS GLN ILE PRO CYS ILE VAL
SEQRES 8 B 110 SER MET LEU THR LYS GLU LEU TYR PHE TYR HIS LEU GLU
SEQRES 9 B 110 HIS HIS HIS HIS HIS HIS
SEQRES 1 C 147 SER GLY ILE SER LEU ASP ASN SER TYR LYS MET ASP TYR
SEQRES 2 C 147 PRO GLU MET GLY LEU CYS ILE ILE ILE ASN ASN LYS ASN
SEQRES 3 C 147 PHE HIS LYS SER THR GLY MET THR SER ARG SER GLY THR
SEQRES 4 C 147 ASP VAL ASP ALA ALA ASN LEU ARG GLU THR PHE ARG ASN
SEQRES 5 C 147 LEU LYS TYR GLU VAL ARG ASN LYS ASN ASP LEU THR ARG
SEQRES 6 C 147 GLU GLU ILE VAL GLU LEU MET ARG ASP VAL SER LYS GLU
SEQRES 7 C 147 ASP HIS SER LYS ARG SER SER PHE VAL CYS VAL LEU LEU
SEQRES 8 C 147 SER HIS GLY GLU GLU GLY ILE ILE PHE GLY THR ASN GLY
SEQRES 9 C 147 PRO VAL ASP LEU LYS LYS ILE THR ASN PHE PHE ARG GLY
SEQRES 10 C 147 ASP ARG CYS ARG SER LEU THR GLY LYS PRO LYS LEU PHE
SEQRES 11 C 147 ILE ILE GLN ALA CYS ARG GLY THR GLU LEU ASP CYS GLY
SEQRES 12 C 147 ILE GLU THR ASP
SEQRES 1 D 110 SER GLY VAL ASP ASP ASP MET ALA CYS HIS LYS ILE PRO
SEQRES 2 D 110 VAL GLU ALA ASP PHE LEU TYR ALA TYR SER THR ALA PRO
SEQRES 3 D 110 GLY TYR TYR SER TRP ARG ASN SER LYS ASP GLY SER TRP
SEQRES 4 D 110 PHE ILE GLN SER LEU CYS ALA MET LEU LYS GLN TYR ALA
SEQRES 5 D 110 ASP LYS LEU GLU PHE MET HIS ILE LEU THR ARG VAL ASN
SEQRES 6 D 110 ARG LYS VAL ALA THR GLU PHE GLU SER PHE SER PHE ASP
SEQRES 7 D 110 ALA THR PHE HIS ALA LYS LYS GLN ILE PRO CYS ILE VAL
SEQRES 8 D 110 SER MET LEU THR LYS GLU LEU TYR PHE TYR HIS LEU GLU
SEQRES 9 D 110 HIS HIS HIS HIS HIS HIS
HET PZN A 501 41
HET PZN C 502 41
HETNAM PZN 3-(2-{5-TERT-BUTYL-3-[(4-METHYL-FURAZAN-3-YLMETHYL)-
HETNAM 2 PZN AMINO]-2-OXO-2H-PYRAZIN-1-YL}-BUTYRYLAMINO)-5-(HEXYL-
HETNAM 3 PZN METHYL-AMINO)-4-OXO-PENTANOIC ACID ANION
FORMUL 5 PZN 2(C28 H44 N7 O6 1-)
FORMUL 7 HOH *233(H2 O)
HELIX 1 1 HIS A 174 GLY A 175C 5 5
HELIX 2 2 GLY A 181 LEU A 196 1 16
HELIX 3 3 THR A 207 LYS A 220 1 14
HELIX 4 4 LEU A 258 PHE A 264 1 7
HELIX 5 5 CYS A 270 THR A 274 5 5
HELIX 6 6 TRP B 348 ALA B 361 1 14
HELIX 7 7 GLU B 365 PHE B 380 1 17
HELIX 8 8 ASP B 381E HIS B 381I 5 5
HELIX 9 9 HIS C 674 GLY C 675C 5 5
HELIX 10 10 GLY C 681 LEU C 696 1 16
HELIX 11 11 THR C 707 GLU C 721 1 15
HELIX 12 12 LEU C 758 PHE C 764 1 7
HELIX 13 13 CYS C 770 THR C 774 5 5
HELIX 14 14 TRP D 848 ALA D 861 1 14
HELIX 15 15 GLU D 865 PHE D 880 1 17
HELIX 16 16 ASP D 881E HIS D 881I 5 5
SHEET 1 A12 GLU A 199 ASN A 204 0
SHEET 2 A12 GLU A 162 ASN A 169 1 N ILE A 167 O ARG A 201
SHEET 3 A12 ARG A 227 LEU A 235 1 O VAL A 233 N ILE A 166
SHEET 4 A12 LYS A 278 GLN A 283 1 O LEU A 279 N PHE A 230
SHEET 5 A12 PHE B 327 TYR B 331 1 O LEU B 328 N PHE A 280
SHEET 6 A12 CYS B 388 SER B 392 -1 O VAL B 390 N TYR B 329
SHEET 7 A12 CYS D 888 MET D 893 -1 O SER D 892 N ILE B 389
SHEET 8 A12 PHE D 827 TYR D 831 -1 N TYR D 829 O VAL D 890
SHEET 9 A12 LYS C 778 GLN C 783 1 N PHE C 780 O LEU D 828
SHEET 10 A12 ARG C 727 LEU C 735 1 N PHE C 730 O LEU C 779
SHEET 11 A12 GLU C 662 ASN C 669 1 N ILE C 666 O VAL C 733
SHEET 12 A12 GLU C 699 ASN C 704 1 O LYS C 703 N ASN C 669
SHEET 1 B 3 GLY A 238 GLU A 239 0
SHEET 2 B 3 ILE A 242 GLY A 245 -1 O ILE A 242 N GLU A 239
SHEET 3 B 3 GLY A 254 ASP A 257 -1 O GLY A 254 N GLY A 245
SHEET 1 C 2 ARG B 341 ASN B 342 0
SHEET 2 C 2 GLY B 346 SER B 347 -1 O GLY B 346 N ASN B 342
SHEET 1 D 3 GLY C 738 GLU C 739 0
SHEET 2 D 3 ILE C 742 GLY C 745 -1 O ILE C 742 N GLU C 739
SHEET 3 D 3 GLY C 754 ASP C 757 -1 O GLY C 754 N GLY C 745
SHEET 1 E 2 ARG D 841 ASN D 842 0
SHEET 2 E 2 GLY D 846 SER D 847 -1 O GLY D 846 N ASN D 842
LINK SG CYS A 285 C9 PZN A 501 1555 1555 1.85
LINK C9 PZN C 502 SG CYS C 785 1555 1555 1.85
SITE 1 AC1 13 HOH C 190 ARG C 679 SER C 736 HIS C 737
SITE 2 AC1 13 GLY C 738 GLN C 783 CYS C 785 TYR D 838
SITE 3 AC1 13 SER D 839 TRP D 840 ARG D 841 SER D 881A
SITE 4 AC1 13 PHE D 881B
SITE 1 AC2 15 ARG A 179 HIS A 237 GLY A 238 GLN A 283
SITE 2 AC2 15 ALA A 284 CYS A 285 HOH A 519 HOH A 524
SITE 3 AC2 15 TYR B 338 SER B 339 TRP B 340 ARG B 341
SITE 4 AC2 15 SER B 381A PHE B 381B PHE B 381H
CRYST1 50.187 68.764 93.008 90.00 101.46 90.00 P 1 21 1 4
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 0.019925 0.000000 0.004039 0.00000
SCALE2 0.000000 0.014542 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010970 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
