HEADER HYDROLASE 03-NOV-09 3KJQ
TITLE CASPASE 8 WITH COVALENT INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASPASE-8;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CASP-8, ICE-LIKE APOPTOTIC PROTEASE 5, MORT1-ASSOCIATED CED-
COMPND 5 3 HOMOLOG, MACH, FADD-HOMOLOGOUS ICE/CED-3-LIKE PROTEASE, FADD-LIKE
COMPND 6 ICE, FLICE, APOPTOTIC CYSTEINE PROTEASE, APOPTOTIC PROTEASE MCH-5,
COMPND 7 CAP4, CASPASE-8 SUBUNIT P18, CASPASE-8 SUBUNIT P10;
COMPND 8 EC: 3.4.22.61;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: CASPASE-8;
COMPND 12 CHAIN: B;
COMPND 13 SYNONYM: CASP-8, ICE-LIKE APOPTOTIC PROTEASE 5, MORT1-ASSOCIATED CED-
COMPND 14 3 HOMOLOG, MACH, FADD-HOMOLOGOUS ICE/CED-3-LIKE PROTEASE, FADD-LIKE
COMPND 15 ICE, FLICE, APOPTOTIC CYSTEINE PROTEASE, APOPTOTIC PROTEASE MCH-5,
COMPND 16 CAP4, CASPASE-8 SUBUNIT P18, CASPASE-8 SUBUNIT P10;
COMPND 17 EC: 3.4.22.61;
COMPND 18 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: CASP8, MCH5;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: CASP8, MCH5;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CASPASE 8, APOPTOSIS, KINETICS, PEPTIDOMIMETIC INHIBITOR, URAZOLE,
KEYWDS 2 DISEASE MUTATION, PHOSPHOPROTEIN, PROTEASE, THIOL PROTEASE, ZYMOGEN,
KEYWDS 3 ALLOSTERIC, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.KAMTEKAR,W.WATT,B.C.FINZEL,M.S.HARRIS,J.BLINN,Z.WANG,A.G.TOMASSELLI
REVDAT 1 11-AUG-10 3KJQ 0
JRNL AUTH Z.WANG,W.WATT,N.A.BROOKS,M.S.HARRIS,J.URBAN,D.BOATMAN,
JRNL AUTH 2 M.MCMILLAN,M.KAHN,R.L.HEINRIKSON,B.C.FINZEL,A.J.WITTWER,
JRNL AUTH 3 J.BLINN,S.KAMTEKAR,A.G.TOMASSELLI
JRNL TITL KINETIC AND STRUCTURAL CHARACTERIZATION OF CASPASE-3 AND
JRNL TITL 2 CASPASE-8 INHIBITION BY A NOVEL CLASS OF IRREVERSIBLE
JRNL TITL 3 INHIBITORS.
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1804 1817 2010
JRNL REFN ISSN 0006-3002
JRNL PMID 20580860
JRNL DOI 10.1016/J.BBAPAP.2010.05.007
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 26415
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) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2933
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1880
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.92
REMARK 3 BIN R VALUE (WORKING SET) : 0.2410
REMARK 3 BIN FREE R VALUE SET COUNT : 198
REMARK 3 BIN FREE R VALUE : 0.2930
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1924
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 146
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.64000
REMARK 3 B22 (A**2) : 0.64000
REMARK 3 B33 (A**2) : -0.96000
REMARK 3 B12 (A**2) : 0.32000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.117
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.110
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.063
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.957
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2036 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1366 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2757 ; 1.242 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3348 ; 0.877 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 248 ; 5.966 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 94 ;35.464 ;24.787
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 355 ;12.755 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;15.512 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 299 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2269 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 384 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 376 ; 0.190 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1411 ; 0.181 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 981 ; 0.180 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 989 ; 0.082 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 124 ; 0.116 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 15 ; 0.162 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 52 ; 0.224 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 10 ; 0.126 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1250 ; 0.751 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 489 ; 0.137 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1981 ; 1.205 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 876 ; 1.924 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 772 ; 2.968 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3KJQ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-NOV-09.
REMARK 100 THE RCSB ID CODE IS RCSB056077.
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
REMARK 200 PH : 7.8
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 : SI(111) DOUBLE-CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29346
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 MICROLITERS OF 100 MM INHIBITOR
REMARK 280 STOCK IN DMSO WAS ADDED TO 100 MICROLITERS OF 8.4 MG/ML PROTEIN
REMARK 280 IN 20 MM TRIS, 100 MM DTT, PH 8.0. PROTEIN SOLUTION WAS MIXED
REMARK 280 WITH AN EQUAL VOLUME OF WELL SOLUTION (1.0-1.1 M CITRATE, 50 MM
REMARK 280 HEPES OR PIPES PH 6.5, 25 MM DTT), VAPOR DIFFUSION, TEMPERATURE
REMARK 280 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.61567
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 87.23133
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 87.23133
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 43.61567
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -90.0 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 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 43.61567
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 211
REMARK 465 PRO A 212
REMARK 465 ARG A 213
REMARK 465 GLU A 214
REMARK 465 GLN A 215
REMARK 465 ASP A 216
REMARK 465 SER A 217
REMARK 465 GLU A 218
REMARK 465 SER A 219
REMARK 465 GLN A 220
REMARK 465 THR A 221
REMARK 465 LEU A 222
REMARK 465 LEU B 385
REMARK 465 SER B 386
REMARK 465 SER B 387
REMARK 465 PRO B 388
REMARK 465 GLN B 389
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 LYS A 246 CD CE NZ
REMARK 470 GLU A 372 CG CD OE1 OE2
REMARK 470 ASP B 479 CG OD1 OD2
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 MET A 228 70.80 -151.26
REMARK 500 ASN B 408 -4.38 79.35
REMARK 500 GLU B 417 -30.21 -139.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 B94 A 480
REMARK 610 B94 A 481
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B94 A 480
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B94 A 481
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KJF RELATED DB: PDB
REMARK 900 CASPASE 3 BOUND TO A COVALENT INHIBITOR
REMARK 900 RELATED ID: 3KJN RELATED DB: PDB
REMARK 900 CASPASE 8 BOUND TO A COVALENT INHIBITOR
DBREF 3KJQ A 211 374 UNP Q14790 CASP8_HUMAN 211 374
DBREF 3KJQ B 385 479 UNP Q14790 CASP8_HUMAN 385 479
SEQRES 1 A 164 SER PRO ARG GLU GLN ASP SER GLU SER GLN THR LEU ASP
SEQRES 2 A 164 LYS VAL TYR GLN MET LYS SER LYS PRO ARG GLY TYR CYS
SEQRES 3 A 164 LEU ILE ILE ASN ASN HIS ASN PHE ALA LYS ALA ARG GLU
SEQRES 4 A 164 LYS VAL PRO LYS LEU HIS SER ILE ARG ASP ARG ASN GLY
SEQRES 5 A 164 THR HIS LEU ASP ALA GLY ALA LEU THR THR THR PHE GLU
SEQRES 6 A 164 GLU LEU HIS PHE GLU ILE LYS PRO HIS ASP ASP CYS THR
SEQRES 7 A 164 VAL GLU GLN ILE TYR GLU ILE LEU LYS ILE TYR GLN LEU
SEQRES 8 A 164 MET ASP HIS SER ASN MET ASP CYS PHE ILE CYS CYS ILE
SEQRES 9 A 164 LEU SER HIS GLY ASP LYS GLY ILE ILE TYR GLY THR ASP
SEQRES 10 A 164 GLY GLN GLU ALA PRO ILE TYR GLU LEU THR SER GLN PHE
SEQRES 11 A 164 THR GLY LEU LYS CYS PRO SER LEU ALA GLY LYS PRO LYS
SEQRES 12 A 164 VAL PHE PHE ILE GLN ALA CYS GLN GLY ASP ASN TYR GLN
SEQRES 13 A 164 LYS GLY ILE PRO VAL GLU THR ASP
SEQRES 1 B 95 LEU SER SER PRO GLN THR ARG TYR ILE PRO ASP GLU ALA
SEQRES 2 B 95 ASP PHE LEU LEU GLY MET ALA THR VAL ASN ASN CYS VAL
SEQRES 3 B 95 SER TYR ARG ASN PRO ALA GLU GLY THR TRP TYR ILE GLN
SEQRES 4 B 95 SER LEU CYS GLN SER LEU ARG GLU ARG CYS PRO ARG GLY
SEQRES 5 B 95 ASP ASP ILE LEU THR ILE LEU THR GLU VAL ASN TYR GLU
SEQRES 6 B 95 VAL SER ASN LYS ASP ASP LYS LYS ASN MET GLY LYS GLN
SEQRES 7 B 95 MET PRO GLN PRO THR PHE THR LEU ARG LYS LYS LEU VAL
SEQRES 8 B 95 PHE PRO SER ASP
HET B94 A 480 29
HET B94 A 481 19
HETNAM B94 (3S)-3-({[(5S,8R)-2-(3-CARBOXYPROPYL)-8-(2-{[(4-
HETNAM 2 B94 CHLOROPHENYL)ACETYL]AMINO}ETHYL)-1,3-DIOXO-2,3,5,8-
HETNAM 3 B94 TETRAHYDRO-1H-[1,2,4]TRIAZOLO[1,2-A]PYRIDAZIN-5-
HETNAM 4 B94 YL]CARBONYL}AMINO)-4-OXOPENTANOIC ACID
FORMUL 3 B94 2(C26 H30 CL N5 O9)
FORMUL 5 HOH *146(H2 O)
HELIX 1 1 PHE A 244 VAL A 251 1 8
HELIX 2 2 PRO A 252 HIS A 255 5 4
HELIX 3 3 GLY A 262 LEU A 277 1 16
HELIX 4 4 THR A 288 MET A 302 1 15
HELIX 5 5 ILE A 333 SER A 338 1 6
HELIX 6 6 GLN A 339 THR A 341 5 3
HELIX 7 7 CYS A 345 ALA A 349 5 5
HELIX 8 8 TRP B 420 CYS B 433 1 14
HELIX 9 9 PRO B 434 GLY B 436 5 3
HELIX 10 10 ASP B 438 ASN B 452 1 15
SHEET 1 A 6 GLU A 280 ASP A 285 0
SHEET 2 A 6 TYR A 235 ASN A 240 1 N ASN A 240 O HIS A 284
SHEET 3 A 6 PHE A 310 LEU A 315 1 O CYS A 313 N ILE A 239
SHEET 4 A 6 LYS A 353 GLN A 358 1 O GLN A 358 N ILE A 314
SHEET 5 A 6 PHE B 399 MET B 403 1 O GLY B 402 N PHE A 355
SHEET 6 A 6 GLN B 465 PHE B 468 -1 O THR B 467 N LEU B 401
SHEET 1 B 3 GLY A 318 ASP A 319 0
SHEET 2 B 3 ILE A 322 TYR A 324 -1 O ILE A 322 N ASP A 319
SHEET 3 B 3 GLU A 330 PRO A 332 -1 O ALA A 331 N ILE A 323
SHEET 1 C 2 ARG B 413 ASN B 414 0
SHEET 2 C 2 GLY B 418 THR B 419 -1 O GLY B 418 N ASN B 414
LINK SG CYS A 360 C1 B94 A 480 1555 1555 1.81
CISPEP 1 LYS A 231 PRO A 232 0 -0.13
SITE 1 AC1 12 ARG A 258 ARG A 260 HIS A 317 GLY A 318
SITE 2 AC1 12 GLN A 358 CYS A 360 HOH A 519 HOH A 542
SITE 3 AC1 12 HOH A 545 SER B 411 TYR B 412 ARG B 413
SITE 1 AC2 8 TYR A 334 THR A 337 SER A 338 GLU B 396
SITE 2 AC2 8 PHE B 399 GLN B 465 THR B 467 THR B 469
CRYST1 63.974 63.974 130.847 90.00 90.00 120.00 P 31 2 1 6
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 0.015631 0.009025 0.000000 0.00000
SCALE2 0.000000 0.018050 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007643 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
