HEADER HYDROLASE/HYDROLASE INHIBITOR 22-MAY-06 2CNO
TITLE CRYSTAL STRUCTURES OF CASPASE-3 IN COMPLEX WITH AZA-PEPTIDE EPOXIDE
TITLE 2 INHIBITORS.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASPASE-3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ALPHA SUBUNIT, RESIDUES 29-175;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: CASPASE-3;
COMPND 8 CHAIN: B;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: AZA-PEPTIDE EPOXIDE;
COMPND 12 CHAIN: C;
COMPND 13 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;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
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: PET11D;
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;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET11D;
SOURCE 21 MOL_ID: 3;
SOURCE 22 SYNTHETIC: YES;
SOURCE 23 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 24 ORGANISM_TAXID: 32630
KEYWDS THIOL PROTEASE, PHOSPHORYLATION, CYSTEINE-PROTEASE, PROTEASE-
KEYWDS 2 INHIBITOR COMPLEX, EPOXIDES, APOPTOSIS, HYDROLASE, AZA-PEPTIDE,
KEYWDS 3 EPOXYSUCCINYL, ICE, YAMA, CPP32, CLAN CD, AZA-ASP, ZYMOGEN,
KEYWDS 4 HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.GANESAN,S.JELAKOVIC,A.J.CAMPBELL,Z.Z.LI,J.L.ASGIAN,J.C.POWERS,
AUTHOR 2 M.G.GRUTTER
REVDAT 4 23-AUG-23 2CNO 1 COMPND SOURCE REMARK DBREF
REVDAT 4 2 1 SEQADV SEQRES HET HETNAM
REVDAT 4 3 1 HETSYN FORMUL LINK SITE
REVDAT 4 4 1 ATOM
REVDAT 3 13-JUL-11 2CNO 1 VERSN
REVDAT 2 24-FEB-09 2CNO 1 VERSN
REVDAT 1 22-MAY-07 2CNO 0
JRNL AUTH R.GANESAN,S.JELAKOVIC,A.J.CAMPBELL,Z.Z.LI,J.L.ASGIAN,
JRNL AUTH 2 J.C.POWERS,M.G.GRUTTER
JRNL TITL EXPLORING THE S4 AND S1 PRIME SUBSITE SPECIFICITIES IN
JRNL TITL 2 CASPASE-3 WITH AZA-PEPTIDE EPOXIDE INHIBITORS
JRNL REF BIOCHEMISTRY V. 45 9059 2006
JRNL REFN ISSN 0006-2960
JRNL PMID 16866351
JRNL DOI 10.1021/BI060364P
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.69
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 3559522.010
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 85.8
REMARK 3 NUMBER OF REFLECTIONS : 17682
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) : 0.168
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 522
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.009
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.07
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 36.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1210
REMARK 3 BIN R VALUE (WORKING SET) : 0.1750
REMARK 3 BIN FREE R VALUE : 0.2410
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 34
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.041
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1979
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 299
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 9.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.93000
REMARK 3 B22 (A**2) : 0.39100
REMARK 3 B33 (A**2) : 1.54700
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) : 0.17
REMARK 3 ESD FROM SIGMAA (A) : 0.06
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) : 0.23
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.08
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) : 23.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.650
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) : 1.190 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.750 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.060 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.000 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 63.10
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.PARAM
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: CHAIN A ASP175 CHAIN B SER176-CYS184
REMARK 4
REMARK 4 2CNO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-MAY-06.
REMARK 100 THE DEPOSITION ID IS D_1290028848.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-OCT-04
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.75
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.90001
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17682
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.02000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 31.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 0.04000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 25.30
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
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 (%): 45.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG6000, 100 MM SODIUM CITRATE PH 4.75
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 34.58500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.76500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 47.88000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 34.58500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.76500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 47.88000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 34.58500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 41.76500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 47.88000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 34.58500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 41.76500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 47.88000
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: HEXAMERIC
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 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 69.17000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 95.76000
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 ALA B 175
REMARK 465 SER B 176
REMARK 465 GLY B 177
REMARK 465 VAL B 178
REMARK 465 ASP B 179
REMARK 465 ASP B 180
REMARK 465 ASP B 181
REMARK 465 MET B 182
REMARK 465 ALA B 183
REMARK 465 CYS B 184
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASP A 175 CA C O CB CG OD1 OD2
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 SG CYS A 163 C4 MY0 C 4 2.15
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 OE2 GLU A 123 OE2 GLU A 123 2665 1.82
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 SER A 120 -176.31 -173.15
REMARK 500 ASP B 192 31.55 70.94
REMARK 500 LYS B 229 -36.63 -132.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B2001 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH B2003 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH B2004 DISTANCE = 6.83 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 THE STARTING INHIBITOR COMPOUND IS AZA-PEPTIDE EPOXIDE CBZ-GLU-VAL-
REMARK 600 AZAASP-EPCO-NH(CH2)2PH. NUCLEOPHILIC ATTACK OF ACTIVE SITE CYSTEINE
REMARK 600 CYS 163 ON C3 CARBON OF OXIRANE RING RESULTS IN FORMATION OF A
REMARK 600 COVALENT THIOETHER BOND AND RING OPENING (INHIBITOR COMPOUND M60)
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CP3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX OF APOPAIN WITH THE TETRAPEPTIDE
REMARK 900 INHIBITOR ACE-DVAD- FMC
REMARK 900 RELATED ID: 1GFW RELATED DB: PDB
REMARK 900 THE 2.8 ANGSTROM CRYSTAL STRUCTURE OF CASPASE-3 (APOPAIN ORCPP32)IN
REMARK 900 COMPLEX WITH AN ISATIN SULFONAMIDE INHIBITOR.
REMARK 900 RELATED ID: 1I3O RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX OF XIAP- BIR2 AND CASPASE 3
REMARK 900 RELATED ID: 1NME RELATED DB: PDB
REMARK 900 STRUCTURE OF CASP-3 WITH TETHERED SALICYLATE
REMARK 900 RELATED ID: 1NMQ RELATED DB: PDB
REMARK 900 EXTENDEND TETHERING: IN SITU ASSEMBLY OF INHIBITORS
REMARK 900 RELATED ID: 1NMS RELATED DB: PDB
REMARK 900 CASPASE-3 TETHERED TO IRREVERSIBLE INHIBITOR
REMARK 900 RELATED ID: 1PAU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX OF APOPAIN WITH THE TETRAPEPTIDE
REMARK 900 ALDEHYDE INHIBITOR AC -DEVD-CHO
REMARK 900 RELATED ID: 1QX3 RELATED DB: PDB
REMARK 900 CONFORMATIONAL RESTRICTIONS IN THE ACTIVE SITE OFUNLIGANDED HUMAN
REMARK 900 CASPASE-3
REMARK 900 RELATED ID: 1RE1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CASPASE-3 WITH A NICOTINIC ACIDALDEHYDE
REMARK 900 INHIBITOR
REMARK 900 RELATED ID: 1RHJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE -3 WITH APRYAZINONE
REMARK 900 INHIBITOR
REMARK 900 RELATED ID: 1RHK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE -3 WITH A PHENYL-PROPYL-
REMARK 900 KETONE INHIBITOR
REMARK 900 RELATED ID: 1RHM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE -3 WITH ANICOTINIC ACID
REMARK 900 ALDEHYDE INHIBITOR
REMARK 900 RELATED ID: 1RHQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE -3 WITH
REMARK 900 ABROMOMETHOXYPHENYL INHIBITOR
REMARK 900 RELATED ID: 1RHR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE -3 WITH ACINNAMIC ACID
REMARK 900 METHYL ESTER INHIBITOR
REMARK 900 RELATED ID: 1RHU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE -3 WITH A 5,6,
REMARK 900 7TRICYCLIC PEPTIDOMIMETIC INHIBITOR
REMARK 900 RELATED ID: 2C1E RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF CASPASE-3 IN COMPLEX WITH AZA-PEPTIDE MICHAEL
REMARK 900 ACCEPTOR INHIBITORS.
REMARK 900 RELATED ID: 2C2K RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF CASPASE-3 IN COMPLEX WITH AZA-PEPTIDE MICHAEL
REMARK 900 ACCEPTOR INHIBITORS.
REMARK 900 RELATED ID: 2C2M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF CASPASE-3 IN COMPLEX WITH AZA-PEPTIDE MICHAEL
REMARK 900 ACCEPTOR INHIBITORS.
REMARK 900 RELATED ID: 2C2O RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF CASPASE-3 IN COMPLEX WITH AZA-PEPTIDE MICHAEL
REMARK 900 ACCEPTOR INHIBITORS.
REMARK 900 RELATED ID: 2CDR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF CASPASE-3 IN COMPLEX WITH AZA-PEPTIDE EPOXIDE
REMARK 900 INHIBITORS.
REMARK 900 RELATED ID: 2CJX RELATED DB: PDB
REMARK 900 EXTENDED SUBSTRATE RECOGNITION IN CASPASE-3 REVEALED BY HIGH
REMARK 900 RESOLUTION X-RAY STRUCTURE ANALYSIS
REMARK 900 RELATED ID: 2CJY RELATED DB: PDB
REMARK 900 EXTENDED SUBSTRATE RECOGNITION IN CASPASE-3 REVEALED BY HIGH
REMARK 900 RESOLUTION X-RAY STRUCTURE ANALYSIS
REMARK 900 RELATED ID: 2CNK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF CASPASE-3 IN COMPLEX WITH AZA-PEPTIDE EPOXIDE
REMARK 900 INHIBITORS.
REMARK 900 RELATED ID: 2CNL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF CASPASE-3 IN COMPLEX WITH AZA-PEPTIDE EPOXIDE
REMARK 900 INHIBITORS.
REMARK 900 RELATED ID: 2CNN RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF CASPASE-3 IN COMPLEX WITH AZA-PEPTIDE EPOXIDE
REMARK 900 INHIBITORS.
DBREF 2CNO A 29 175 UNP P42574 CASP3_HUMAN 29 175
DBREF 2CNO B 176 277 UNP P42574 CASP3_HUMAN 176 277
DBREF 2CNO C 1 5 PDB 2CNO 2CNO 1 5
SEQADV 2CNO ALA B 175 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 103 ALA SER GLY VAL ASP ASP ASP MET ALA CYS HIS LYS ILE
SEQRES 2 B 103 PRO VAL GLU ALA ASP PHE LEU TYR ALA TYR SER THR ALA
SEQRES 3 B 103 PRO GLY TYR TYR SER TRP ARG ASN SER LYS ASP GLY SER
SEQRES 4 B 103 TRP PHE ILE GLN SER LEU CYS ALA MET LEU LYS GLN TYR
SEQRES 5 B 103 ALA ASP LYS LEU GLU PHE MET HIS ILE LEU THR ARG VAL
SEQRES 6 B 103 ASN ARG LYS VAL ALA THR GLU PHE GLU SER PHE SER PHE
SEQRES 7 B 103 ASP ALA THR PHE HIS ALA LYS LYS GLN ILE PRO CYS ILE
SEQRES 8 B 103 VAL SER MET LEU THR LYS GLU LEU TYR PHE TYR HIS
SEQRES 1 C 5 PHQ GLU VAL MY0 PEA
HET PHQ C 1 10
HET MY0 C 4 13
HET PEA C 5 9
HETNAM PHQ BENZYL CHLOROCARBONATE
HETNAM MY0 (2S)-4-[1-(CARBOXYMETHYL)HYDRAZINYL]-2-HYDROXY-4-
HETNAM 2 MY0 OXOBUTANOIC ACID
HETNAM PEA 2-PHENYLETHYLAMINE
FORMUL 3 PHQ C8 H7 CL O2
FORMUL 3 MY0 C6 H10 N2 O6
FORMUL 3 PEA C8 H12 N 1+
FORMUL 4 HOH *299(H2 O)
HELIX 1 1 HIS A 56 GLY A 60 5 5
HELIX 2 2 GLY A 66 ASN A 80 1 15
HELIX 3 3 THR A 92 LYS A 105 1 14
HELIX 4 4 LEU A 136 PHE A 142 1 7
HELIX 5 5 CYS A 148 THR A 152 5 5
HELIX 6 6 TRP B 214 ALA B 227 1 14
HELIX 7 7 GLU B 231 PHE B 247 1 17
HELIX 8 8 ASP B 253 HIS B 257 5 5
SHEET 1 AA 6 GLU A 84 ASN A 89 0
SHEET 2 AA 6 GLU A 43 ASN A 51 1 O GLY A 45 N GLU A 84
SHEET 3 AA 6 ARG A 111 LEU A 119 1 N SER A 112 O GLU A 43
SHEET 4 AA 6 LYS A 156 GLN A 161 1 O LEU A 157 N CYS A 116
SHEET 5 AA 6 PHE B 193 TYR B 197 1 O LEU B 194 N PHE A 158
SHEET 6 AA 6 CYS B 264 SER B 267 -1 O CYS B 264 N TYR B 197
SHEET 1 AB 3 GLY A 122 GLU A 123 0
SHEET 2 AB 3 ILE A 126 GLY A 129 -1 O ILE A 126 N GLU A 123
SHEET 3 AB 3 GLY A 132 ASP A 135 -1 O GLY A 132 N GLY A 129
SHEET 1 BA 2 ARG B 207 ASN B 208 0
SHEET 2 BA 2 GLY B 212 SER B 213 -1 O GLY B 212 N ASN B 208
LINK SG CYS A 163 C3 MY0 C 4 1555 1555 1.88
LINK C1 PHQ C 1 N GLU C 2 1555 1555 1.32
LINK C GLU C 2 N VAL C 3 1555 1555 1.33
LINK C VAL C 3 N MY0 C 4 1555 1555 1.30
LINK C MY0 C 4 N PEA C 5 1555 1555 1.40
CRYST1 69.170 83.530 95.760 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 0.014457 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011972 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010443 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
