HEADER HYDROLASE/HYDROLASE INHIBITOR 17-AUG-06 2J30
TITLE THE ROLE OF LOOP BUNDLE HYDROGEN BONDS IN THE MATURATION AND ACTIVITY
TITLE 2 OF (PRO)CASPASE-3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASPASE-3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 29-277;
COMPND 5 SYNONYM: CASP-3, APOPAIN, CYSTEINE PROTEASE CPP32, CPP-32, PROTEIN
COMPND 6 YAMA, SREBP CLEAVAGE ACTIVITY 1, SCA-1, CASPASE-3 SUBUNIT P17,
COMPND 7 CASPASE-3 SUBUNIT P12;
COMPND 8 EC: 3.4.22.56;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: ACE-ASP-GLU-VAL-ASP-CHLOROMETHYLKETONE INHIBITOR;
COMPND 12 CHAIN: B;
COMPND 13 SYNONYM: AC-DEVD-CMK;
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: CASP3, CPP32;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 11 ORGANISM_TAXID: 32630
KEYWDS HYDROLASE, PRO-CASPASE3, THIOL PROTEASE, HYDROLASE-HYDROLASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.FEENEY,C.POP,P.SWARTZ,C.MATTOS,A.C.CLARK
REVDAT 5 08-MAY-19 2J30 1 REMARK LINK
REVDAT 4 21-DEC-16 2J30 1 SOURCE
REVDAT 3 13-JUL-11 2J30 1 VERSN
REVDAT 2 24-FEB-09 2J30 1 VERSN
REVDAT 1 08-NOV-06 2J30 0
JRNL AUTH B.FEENEY,C.POP,P.SWARTZ,C.MATTOS,A.C.CLARK
JRNL TITL ROLE OF LOOP BUNDLE HYDROGEN BONDS IN THE MATURATION AND
JRNL TITL 2 ACTIVITY OF (PRO)CASPASE-3.
JRNL REF BIOCHEMISTRY V. 45 13249 2006
JRNL REFN ISSN 0006-2960
JRNL PMID 17073446
JRNL DOI 10.1021/BI0611964
REMARK 2
REMARK 2 RESOLUTION. 1.40 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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1033475.180
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.1
REMARK 3 NUMBER OF REFLECTIONS : 49971
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) : 0.197
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.400
REMARK 3 FREE R VALUE TEST SET COUNT : 4709
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
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) : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.49
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 72.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6274
REMARK 3 BIN R VALUE (WORKING SET) : 0.3050
REMARK 3 BIN FREE R VALUE : 0.3090
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 303
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2010
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 287
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.60000
REMARK 3 B22 (A**2) : 2.44000
REMARK 3 B33 (A**2) : -4.05000
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) : 0.17
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) : 0.18
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.15
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.080
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) : 1.070 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.680 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.060 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.950 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 43.83
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.PARAM
REMARK 3 PARAMETER FILE 2 : WATER.PARAM
REMARK 3 PARAMETER FILE 3 : ACE.PARAM
REMARK 3 PARAMETER FILE 4 : ASK.PARAM
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 : ACE.TOP
REMARK 3 TOPOLOGY FILE 4 : ASK.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2J30 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-AUG-06.
REMARK 100 THE DEPOSITION ID IS D_1290029739.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.50
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) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54279
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 46.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.75000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.350
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
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 (%): 48.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEINS WERE DIALYZED IN A BUFFER OF
REMARK 280 10 MM TRIS-HCL, PH 8.5, 1 MM DTT. THE PROTEIN WAS CONCENTRATED
REMARK 280 TO 10 MG/ML USING AMICON ULTRAFREE CENTRIFUGAL FILTER DEVICES,
REMARK 280 AND INHIBITOR, AC-DEVD-CMK RECONSTITUTED IN DMSO, WAS THEN ADDED
REMARK 280 AT 5:1 WT:WT, INHIBITOR TO PEPTIDE. THE PROTEIN WAS DILUTED TO A
REMARK 280 CONCENTRATION OF 8 MG/ML BY ADDING 10 MM TRIS-HCL, PH 8.5,
REMARK 280 CONCENTRATED DTT AND CONCENTRATED NAN3 SO THAT THE FINAL BUFFER
REMARK 280 WAS 10 MM TRIS-HCL, PH 8.5, 10 MM DTT, 3 MM NAN3. 2 UL OF
REMARK 280 CONCENTRATED PROTEIN WAS MIXED 1:1 WITH WELL BUFFER THAT
REMARK 280 CONTAINED 100 MM SODIUM CITRATE, PH 5, 3 MM NAN3, 10 MM DTT AND
REMARK 280 17% PEG 6000 W/V. SOLUTIONS WERE INCUBATED AT 18 DEG C USING THE
REMARK 280 HANGING DROP METHOD. CRYSTALS GREW WITHIN THREE DAYS FOR WILD-
REMARK 280 TYPE CASPASE-3 AND WITHIN TWO WEEKS FOR THE MUTANTS. THE IDEAL
REMARK 280 FREEZING CONDITIONS WERE FOUND TO BE WITH 80% MOTHER LIQUOR AND
REMARK 280 20% PEG 400., PH 8.50, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
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 34.36600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.19750
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 48.17600
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 34.36600
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.19750
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 48.17600
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 34.36600
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 42.19750
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 48.17600
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 34.36600
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 42.19750
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 48.17600
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: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 17040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 68.73200
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 84.39500
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 68.73200
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 96.35200
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 84.39500
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 96.35200
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2047 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2134 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 THE AC-ASP-GLU-VAL-ASP-CMK IS PEPTIDE-LIKE, A MEMBER OF INHIBITOR
REMARK 400 CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: AC-ASP-GLU-VAL-ASP-CMK
REMARK 400 CHAIN: B
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 ASP A 175
REMARK 465 SER A 176
REMARK 465 GLY A 177
REMARK 465 VAL A 178
REMARK 465 ASP A 179
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 -174.47 -170.96
REMARK 500 MET A 182 -138.91 -164.14
REMARK 500 ALA A 183 169.34 81.31
REMARK 500 CYS A 184 78.59 26.53
REMARK 500 LYS A 229 -49.31 -131.90
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 A2023 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH A2033 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH A2037 DISTANCE = 7.24 ANGSTROMS
REMARK 525 HOH A2056 DISTANCE = 6.27 ANGSTROMS
REMARK 525 HOH A2059 DISTANCE = 6.42 ANGSTROMS
REMARK 525 HOH A2115 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH B2144 DISTANCE = 6.50 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF ACE-ASP-GLU-VAL-ASP
REMARK 800 -CHLOROMETHYLKETONE INHIBITOR
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.
REMARK 900 RELATED ID: 2CNO RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF CASPASE-3 IN COMPLEX WITH AZA-PEPTIDE EPOXIDE
REMARK 900 INHIBITORS.
REMARK 900 RELATED ID: 2J31 RELATED DB: PDB
REMARK 900 THE ROLE OF LOOP BUNDLE HYDROGEN BONDS IN THE MATURATION AND
REMARK 900 ACTIVITY OF(PRO)CASPASE -3
REMARK 900 RELATED ID: 2J32 RELATED DB: PDB
REMARK 900 THE ROLE OF LOOP BUNDLE HYDROGEN BONDS IN THE MATURATION AND
REMARK 900 ACTIVITY OF(PRO)CASPASE -3
REMARK 900 RELATED ID: 2J33 RELATED DB: PDB
REMARK 900 THE ROLE OF LOOP BUNDLE HYDROGEN BONDS IN THE MATURATION AND
REMARK 900 ACTIVITY OF (PRO) CASPASE-3
DBREF 2J30 A 29 277 UNP P42574 CASP3_HUMAN 29 277
DBREF 2J30 B 1 6 PDB 2J30 2J30 1 6
SEQADV 2J30 HIS A 278 UNP P42574 EXPRESSION TAG
SEQRES 1 A 250 SER GLY ILE SER LEU ASP ASN SER TYR LYS MET ASP TYR
SEQRES 2 A 250 PRO GLU MET GLY LEU CYS ILE ILE ILE ASN ASN LYS ASN
SEQRES 3 A 250 PHE HIS LYS SER THR GLY MET THR SER ARG SER GLY THR
SEQRES 4 A 250 ASP VAL ASP ALA ALA ASN LEU ARG GLU THR PHE ARG ASN
SEQRES 5 A 250 LEU LYS TYR GLU VAL ARG ASN LYS ASN ASP LEU THR ARG
SEQRES 6 A 250 GLU GLU ILE VAL GLU LEU MET ARG ASP VAL SER LYS GLU
SEQRES 7 A 250 ASP HIS SER LYS ARG SER SER PHE VAL CYS VAL LEU LEU
SEQRES 8 A 250 SER HIS GLY GLU GLU GLY ILE ILE PHE GLY THR ASN GLY
SEQRES 9 A 250 PRO VAL ASP LEU LYS LYS ILE THR ASN PHE PHE ARG GLY
SEQRES 10 A 250 ASP ARG CYS ARG SER LEU THR GLY LYS PRO LYS LEU PHE
SEQRES 11 A 250 ILE ILE GLN ALA CYS ARG GLY THR GLU LEU ASP CYS GLY
SEQRES 12 A 250 ILE GLU THR ASP SER GLY VAL ASP ASP ASP MET ALA CYS
SEQRES 13 A 250 HIS LYS ILE PRO VAL GLU ALA ASP PHE LEU TYR ALA TYR
SEQRES 14 A 250 SER THR ALA PRO GLY TYR TYR SER TRP ARG ASN SER LYS
SEQRES 15 A 250 ASP GLY SER TRP PHE ILE GLN SER LEU CYS ALA MET LEU
SEQRES 16 A 250 LYS GLN TYR ALA ASP LYS LEU GLU PHE MET HIS ILE LEU
SEQRES 17 A 250 THR ARG VAL ASN ARG LYS VAL ALA THR GLU PHE GLU SER
SEQRES 18 A 250 PHE SER PHE ASP ALA THR PHE HIS ALA LYS LYS GLN ILE
SEQRES 19 A 250 PRO CYS ILE VAL SER MET LEU THR LYS GLU LEU TYR PHE
SEQRES 20 A 250 TYR HIS HIS
SEQRES 1 B 6 ACE ASP GLU VAL ASP 0QE
HET ACE B 1 3
HET 0QE B 6 1
HETNAM ACE ACETYL GROUP
HETNAM 0QE CHLOROMETHANE
HETSYN 0QE CHLORO METHYL GROUP
FORMUL 2 ACE C2 H4 O
FORMUL 2 0QE C H3 CL
FORMUL 3 HOH *287(H2 O)
HELIX 1 1 HIS A 56 GLY A 60 5 5
HELIX 2 2 GLY A 66 LEU A 81 1 16
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 A 214 ALA A 227 1 14
HELIX 7 7 GLU A 231 PHE A 247 1 17
HELIX 8 8 ASP A 253 HIS A 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 A 193 TYR A 197 1 O LEU A 194 N PHE A 158
SHEET 6 AA 6 CYS A 264 SER A 267 -1 O CYS A 264 N TYR A 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 AC 3 GLY A 212 SER A 213 0
SHEET 2 AC 3 TRP A 206 ASN A 208 -1 O ASN A 208 N GLY A 212
SHEET 3 AC 3 GLU B 3 VAL B 4 -1 O GLU B 3 N ARG A 207
LINK C ACE B 1 N ASP B 2 1555 1555 1.33
LINK C ASP B 5 C1 0QE B 6 1555 1555 1.53
SITE 1 AC1 25 SER A 58 ARG A 64 SER A 65 HIS A 121
SITE 2 AC1 25 GLY A 122 GLN A 161 CYS A 163 SER A 205
SITE 3 AC1 25 TRP A 206 ARG A 207 ASN A 208 SER A 209
SITE 4 AC1 25 TRP A 214 SER A 249 PHE A 250 HOH A2042
SITE 5 AC1 25 HOH A2227 HOH A2261 HOH A2262 0QE B 6
SITE 6 AC1 25 HOH B2001 HOH B2002 HOH B2003 HOH B2004
SITE 7 AC1 25 HOH B2005
CRYST1 68.732 84.395 96.352 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 0.014549 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011849 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010379 0.00000
(ATOM LINES ARE NOT SHOWN.)
END