HEADER HYDROLASE 16-DEC-03 1RWM
TITLE CRYSTAL STRUCTURE OF HUMAN CASPASE-1 IN COMPLEX WITH 4-OXO-3-[2-(5-
TITLE 2 {[4-(QUINOXALIN-2-YLAMINO)-BENZOYLAMINO]-METHYL}-THIOPHEN-2-YL)-
TITLE 3 ACETYLAMINO]-PENTANOIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERLEUKIN-1 BETA CONVERTASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: INTERLEUKIN-1 BETA CONVERTASE P20;
COMPND 5 SYNONYM: IL-1BC, IL-1 BETA CONVERTING ENZYME, ICE, INTERLEUKIN-1 BETA
COMPND 6 CONVERTING ENZYME, P45, CASPASE-1, CASP-1;
COMPND 7 EC: 3.4.22.36;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: INTERLEUKIN-1 BETA CONVERTASE;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: INTERLEUKIN-1 BETA CONVERTASE P10;
COMPND 13 SYNONYM: IL-1BC, IL-1 BETA CONVERTING ENZYME, ICE, INTERLEUKIN-1 BETA
COMPND 14 CONVERTING ENZYME, P45, CASPASE-1, CASP-1;
COMPND 15 EC: 3.4.22.36;
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: CASP1, IL1BC, IL1BCE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 CODON+;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PRSET;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: CASP1, IL1BC, IL1BCE;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21 CODON+;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PRSET
KEYWDS PROTEIN-SMALL MOLECULE INHIBITOR COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.J.ROMANOWSKI,N.D.WAAL,B.T.FAHR,T.O'BRIEN
REVDAT 5 23-AUG-23 1RWM 1 REMARK LINK
REVDAT 4 13-JUL-11 1RWM 1 VERSN
REVDAT 3 24-FEB-09 1RWM 1 VERSN
REVDAT 2 03-MAY-05 1RWM 1 JRNL
REVDAT 1 28-DEC-04 1RWM 0
JRNL AUTH T.O'BRIEN,B.T.FAHR,M.M.SOPKO,J.W.LAM,N.D.WAAL,B.C.RAIMUNDO,
JRNL AUTH 2 H.E.PURKEY,P.PHAM,M.J.ROMANOWSKI
JRNL TITL STRUCTURAL ANALYSIS OF CASPASE-1 INHIBITORS DERIVED FROM
JRNL TITL 2 TETHERING.
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 61 451 2005
JRNL REFN ESSN 1744-3091
JRNL PMID 16511067
JRNL DOI 10.1107/S1744309105010109
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.19
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 3 NUMBER OF REFLECTIONS : 8766
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 437
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 15
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.79
REMARK 3 REFLECTION IN BIN (WORKING SET) : 830
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2200
REMARK 3 BIN FREE R VALUE SET COUNT : 50
REMARK 3 BIN FREE R VALUE : 0.2880
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2069
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 37
REMARK 3 SOLVENT ATOMS : 69
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.99
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.49000
REMARK 3 B22 (A**2) : 1.49000
REMARK 3 B33 (A**2) : -2.99000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 3.180
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.352
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.268
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.025
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.924
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.877
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2152 ; 0.006 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2898 ; 1.111 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 259 ; 5.038 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 316 ; 0.060 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1623 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 976 ; 0.174 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 80 ; 0.122 ; 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): 59 ; 0.133 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.132 ; 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): 1302 ; 1.890 ; 2.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2114 ; 3.284 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 850 ; 1.781 ; 2.500
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 784 ; 3.024 ; 5.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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: NULL
REMARK 4
REMARK 4 1RWM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-04.
REMARK 100 THE DEPOSITION ID IS D_1000021099.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JAN-03
REMARK 200 TEMPERATURE (KELVIN) : 180
REMARK 200 PH : 6.0
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 RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : YALE MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR (MSC/RIGAKU)
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9552
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.12800
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) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.38200
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: PDB ID 1ICE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M PIPES, 200MM LI2SO4, 25% PEG2K
REMARK 280 MME, 10MM DTT, 3MM NAN3, 2MM MGCL2, PH 6.0, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 278K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 80.58200
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 31.61050
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 31.61050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 120.87300
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 31.61050
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 31.61050
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 40.29100
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 31.61050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 31.61050
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 120.87300
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 31.61050
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 31.61050
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 40.29100
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 80.58200
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: HETEROTETRAMER (DIMER OF TWO HETERODIMERS). EACH
REMARK 300 HETERODIMER IS REPRESENTED BY CHAINS A (THE P20 SUBUNIT) AND B (THE
REMARK 300 P10 SUBUNIT) OF HUMAN CASPASE-1.
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 18460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -102.0 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 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 ASN A 120
REMARK 465 PRO A 121
REMARK 465 ALA A 122
REMARK 465 MET A 123
REMARK 465 PRO A 124
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 254 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
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 149 -113.75 -74.54
REMARK 500 ASN A 266 -168.95 -71.36
REMARK 500 ASP B 336 -12.85 83.57
REMARK 500 ASP B 381 -141.27 -149.41
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 Q2Y A 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ICE RELATED DB: PDB
REMARK 900 RELATED ID: 1BMQ RELATED DB: PDB
REMARK 900 RELATED ID: 1IBC RELATED DB: PDB
REMARK 900 RELATED ID: 1RWK RELATED DB: PDB
REMARK 900 RELATED ID: 1RWN RELATED DB: PDB
REMARK 900 RELATED ID: 1RWO RELATED DB: PDB
REMARK 900 RELATED ID: 1RWP RELATED DB: PDB
REMARK 900 RELATED ID: 1RWV RELATED DB: PDB
REMARK 900 RELATED ID: 1RWW RELATED DB: PDB
REMARK 900 RELATED ID: 1RWX RELATED DB: PDB
DBREF 1RWM A 120 297 UNP P29466 CASP1_HUMAN 120 297
DBREF 1RWM B 317 404 UNP P29466 CASP1_HUMAN 317 404
SEQRES 1 A 178 ASN PRO ALA MET PRO THR SER SER GLY SER GLU GLY ASN
SEQRES 2 A 178 VAL LYS LEU CYS SER LEU GLU GLU ALA GLN ARG ILE TRP
SEQRES 3 A 178 LYS GLN LYS SER ALA GLU ILE TYR PRO ILE MET ASP LYS
SEQRES 4 A 178 SER SER ARG THR ARG LEU ALA LEU ILE ILE CYS ASN GLU
SEQRES 5 A 178 GLU PHE ASP SER ILE PRO ARG ARG THR GLY ALA GLU VAL
SEQRES 6 A 178 ASP ILE THR GLY MET THR MET LEU LEU GLN ASN LEU GLY
SEQRES 7 A 178 TYR SER VAL ASP VAL LYS LYS ASN LEU THR ALA SER ASP
SEQRES 8 A 178 MET THR THR GLU LEU GLU ALA PHE ALA HIS ARG PRO GLU
SEQRES 9 A 178 HIS LYS THR SER ASP SER THR PHE LEU VAL PHE MET SER
SEQRES 10 A 178 HIS GLY ILE ARG GLU GLY ILE CYS GLY LYS LYS HIS SER
SEQRES 11 A 178 GLU GLN VAL PRO ASP ILE LEU GLN LEU ASN ALA ILE PHE
SEQRES 12 A 178 ASN MET LEU ASN THR LYS ASN CYS PRO SER LEU LYS ASP
SEQRES 13 A 178 LYS PRO LYS VAL ILE ILE ILE GLN ALA CYS ARG GLY ASP
SEQRES 14 A 178 SER PRO GLY VAL VAL TRP PHE LYS ASP
SEQRES 1 B 88 ALA ILE LYS LYS ALA HIS ILE GLU LYS ASP PHE ILE ALA
SEQRES 2 B 88 PHE CYS SER SER THR PRO ASP ASN VAL SER TRP ARG HIS
SEQRES 3 B 88 PRO THR MET GLY SER VAL PHE ILE GLY ARG LEU ILE GLU
SEQRES 4 B 88 HIS MET GLN GLU TYR ALA CYS SER CYS ASP VAL GLU GLU
SEQRES 5 B 88 ILE PHE ARG LYS VAL ARG PHE SER PHE GLU GLN PRO ASP
SEQRES 6 B 88 GLY ARG ALA GLN MET PRO THR THR GLU ARG VAL THR LEU
SEQRES 7 B 88 THR ARG CYS PHE TYR LEU PHE PRO GLY HIS
HET Q2Y A 501 37
HETNAM Q2Y 4-OXO-3-[2-(5-{[4-(QUINOXALIN-2-YLAMINO)-BENZOYLAMINO]-
HETNAM 2 Q2Y METHYL}-THIOPHEN-2-YL)-ACETYLAMINO]-PENTANOIC ACID
FORMUL 3 Q2Y C27 H25 N5 O5 S
FORMUL 4 HOH *69(H2 O)
HELIX 1 1 SER A 137 LYS A 148 1 12
HELIX 2 2 GLY A 181 LEU A 196 1 16
HELIX 3 3 THR A 207 ALA A 219 1 13
HELIX 4 4 HIS A 220 SER A 227 5 8
HELIX 5 5 GLN A 257 ASN A 266 1 10
HELIX 6 6 CYS A 270 LYS A 274 5 5
HELIX 7 7 VAL B 348 ALA B 361 1 14
HELIX 8 8 ASP B 365 SER B 376 1 12
SHEET 1 A 6 SER A 199 LYS A 204 0
SHEET 2 A 6 LEU A 164 CYS A 169 1 N ILE A 167 O ASP A 201
SHEET 3 A 6 THR A 230 MET A 235 1 O VAL A 233 N ILE A 168
SHEET 4 A 6 LYS A 278 GLN A 283 1 O VAL A 279 N LEU A 232
SHEET 5 A 6 PHE B 327 CYS B 331 1 O ILE B 328 N ILE A 280
SHEET 6 A 6 THR B 388 GLU B 390 -1 O THR B 388 N CYS B 331
SHEET 1 B 2 ILE A 243 CYS A 244 0
SHEET 2 B 2 ILE A 255 LEU A 256 -1 O LEU A 256 N ILE A 243
SHEET 1 C 2 ARG B 341 HIS B 342 0
SHEET 2 C 2 GLY B 346 SER B 347 -1 O GLY B 346 N HIS B 342
LINK SG CYS A 285 C18 Q2Y A 501 1555 1555 1.62
SITE 1 AC1 10 ARG A 179 HIS A 237 GLY A 238 GLN A 283
SITE 2 AC1 10 CYS A 285 SER B 339 ARG B 341 HIS B 342
SITE 3 AC1 10 ARG B 352 ARG B 383
CRYST1 63.221 63.221 161.164 90.00 90.00 90.00 P 43 21 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 0.015818 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015818 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006205 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
