HEADER HYDROLASE/HYDROLASE INHIBITOR 19-MAY-08 3D6M
TITLE CRYSTAL STRUCTURE OF HUMAN CASPASE-1 WITH A NATURALLY-OCCURRING
TITLE 2 LYS319->ARG SUBSTITUTION IN COMPLEX WITH 3-[2-(2-
TITLE 3 BENZYLOXYCARBONYLAMINO-3-METHYL-BUTYRYLAMINO)-PROPIONYLAMINO]-4-OXO-
TITLE 4 PENTANOIC ACID (Z-VAD-FMK)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASPASE-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CASP1 P20;
COMPND 5 SYNONYM: CASP-1, INTERLEUKIN-1 BETA CONVERTASE, IL-1BC, IL-1 BETA-
COMPND 6 CONVERTING ENZYME, ICE, INTERLEUKIN-1 BETA-CONVERTING ENZYME, P45,
COMPND 7 CASPASE-1 SUBUNIT P20, CASPASE-1 SUBUNIT P10;
COMPND 8 EC: 3.4.22.36;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: CASPASE-1;
COMPND 12 CHAIN: B;
COMPND 13 FRAGMENT: CASP1 P10;
COMPND 14 SYNONYM: CASP-1, INTERLEUKIN-1 BETA CONVERTASE, IL-1BC, IL-1 BETA-
COMPND 15 CONVERTING ENZYME, ICE, INTERLEUKIN-1 BETA-CONVERTING ENZYME, P45,
COMPND 16 CASPASE-1 SUBUNIT P20, CASPASE-1 SUBUNIT P10;
COMPND 17 EC: 3.4.22.36;
COMPND 18 ENGINEERED: YES;
COMPND 19 MUTATION: YES;
COMPND 20 MOL_ID: 3;
COMPND 21 MOLECULE: N-[(BENZYLOXY)CARBONYL]-L-VALYL-N-[(2S)-1-CARBOXY-4-FLUORO-
COMPND 22 3-OXOBUTAN-2-YL]-L-ALANINAMIDE;
COMPND 23 CHAIN: C;
COMPND 24 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(DE3) CODON+;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PRSET B;
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(DE3) CODON+;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PRSET B;
SOURCE 21 MOL_ID: 3;
SOURCE 22 SYNTHETIC: YES
KEYWDS CATALYTIC DOMAIN, NATURALLY-OCCURRING MUTATION, APOPTOSIS, HYDROLASE,
KEYWDS 2 PROTEASE, THIOL PROTEASE, ZYMOGEN, HYDROLASE-HYDROLASE INHIBITOR
KEYWDS 3 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.ROSEN-WOLFF,J.ROESLER,M.J.ROMANOWSKI
REVDAT 3 23-MAY-12 3D6M 1 DBREF
REVDAT 2 13-JUL-11 3D6M 1 VERSN
REVDAT 1 02-MAR-10 3D6M 0
JRNL AUTH A.ROSEN-WOLFF,M.J.ROMANOWSKI,L.RITTER,S.FLECKS,N.QUOOS,
JRNL AUTH 2 J.GRAMATT,C.PETZOLD,H.D.NGUYEN,M.GAHR,J.ROESLER
JRNL TITL MUTATED, STRUCTURALLY ALTERED CASPASE-1 WITH DECREASED
JRNL TITL 2 ENZYMATIC AND INCREASED RIP2-MEDITATED INFLAMMATORY ACTIVITY
JRNL TITL 3 LEADS TO A NEW TYPE OF PERIODIC FEVER (ICE FEVER).
JRNL REF TO BE PUBLISHED 2008
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 29468
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1567
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.86
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2786
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2620
REMARK 3 BIN FREE R VALUE SET COUNT : 170
REMARK 3 BIN FREE R VALUE : 0.3110
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2099
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 238
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.16
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.08000
REMARK 3 B22 (A**2) : 1.08000
REMARK 3 B33 (A**2) : -2.16000
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): 0.122
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.128
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.083
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.612
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2160 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2913 ; 1.056 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 259 ; 5.620 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 97 ;34.581 ;23.608
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 390 ;13.146 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;17.082 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 328 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1602 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1019 ; 0.179 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1488 ; 0.297 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 190 ; 0.110 ; 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): 81 ; 0.149 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 37 ; 0.137 ; 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): 1352 ; 2.339 ; 2.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2133 ; 3.485 ; 5.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 903 ; 2.771 ; 2.500
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 780 ; 4.317 ; 5.000
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 125 A 125
REMARK 3 RESIDUE RANGE : B 317 B 317
REMARK 3 RESIDUE RANGE : A 1 A 1
REMARK 3 ORIGIN FOR THE GROUP (A): 65.6028 23.9630 40.7380
REMARK 3 T TENSOR
REMARK 3 T11: 0.1062 T22: -0.0850
REMARK 3 T33: -0.1367 T12: -0.1082
REMARK 3 T13: 0.0905 T23: 0.0327
REMARK 3 L TENSOR
REMARK 3 L11: 2.8996 L22: 2.0258
REMARK 3 L33: 0.3639 L12: 0.5471
REMARK 3 L13: 0.5224 L23: 0.8188
REMARK 3 S TENSOR
REMARK 3 S11: 0.0724 S12: -0.0621 S13: 0.4225
REMARK 3 S21: -0.2431 S22: -0.1406 S23: -0.2096
REMARK 3 S31: -0.3074 S32: 0.0115 S33: 0.0682
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 3D6M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAY-08.
REMARK 100 THE RCSB ID CODE IS RCSB047657.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-SEP-06
REMARK 200 TEMPERATURE (KELVIN) : 160
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : ASYMMETRIC CURVED CRYSTAL;
REMARK 200 CRYSTAL TYPE S(220)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31131
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.0000
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) : 1.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.32300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1SC3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS OBTAINED BY HANGING-DROP
REMARK 280 VAPOR DIFFUSION AT 4 C (277K) AGAINST A RESERVOIR OF 0.1 M PIPES
REMARK 280 PH 6.0, 75-175 MM (NH4)2SO4, 25% PEG 2000 MME, 10 MM DTT, 3 MM
REMARK 280 NAN3, AND 2 MM MGCL2. ALL CRYSTALS CRYOPROTECTED IN MOTHER
REMARK 280 LIQUORS SUPPLEMENTED WITH 20% (V/V) GLYCEROL FOR 30-90 SEC AND
REMARK 280 IMMERSION IN LIQUID NITROGEN., VAPOR DIFFUSION, HANGING DROP
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 80.89150
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 31.48400
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 31.48400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 121.33725
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 31.48400
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 31.48400
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 40.44575
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 31.48400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 31.48400
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 121.33725
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 31.48400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 31.48400
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 40.44575
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 80.89150
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: DIMER OF THE P20/P10 DIMER
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 18470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, 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 62.96800
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 62.96800
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 80.89150
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 B 212 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 177 LIES ON A SPECIAL POSITION.
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 MET A 119
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 465 MET B 316
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 225 CD CE NZ
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 172 CD OE1 OE2
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 OE2 GLU A 172 O HOH A 452 1.96
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 172 CG GLU A 172 CD -0.440
REMARK 500 ASP C 4 C ASP C 4 O 0.190
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 -92.00 -73.97
REMARK 500 ALA A 284 149.36 -171.77
REMARK 500 ASP B 336 -11.57 86.17
REMARK 500 ASP B 381 -154.46 -105.87
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 B 120 DISTANCE = 5.22 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN C OF N-[(BENZYLOXY)
REMARK 800 CARBONYL]-L-VALYL-N-[(2S)-1-CARBOXY-4-FLUORO- 3-OXOBUTAN-2-YL]-L-
REMARK 800 ALANINAMIDE
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3D6F RELATED DB: PDB
REMARK 900 RELATED ID: 3D6H RELATED DB: PDB
REMARK 900 RELATED ID: 1SC3 RELATED DB: PDB
DBREF 3D6M A 120 297 UNP P29466 CASP1_HUMAN 120 297
DBREF 3D6M B 317 404 UNP P29466 CASP1_HUMAN 317 404
DBREF 3D6M C 1 5 PDB 3D6M 3D6M 1 5
SEQADV 3D6M MET A 119 UNP P29466 EXPRESSION TAG
SEQADV 3D6M MET B 316 UNP P29466 EXPRESSION TAG
SEQADV 3D6M ARG B 319 UNP P29466 LYS 319 ENGINEERED
SEQRES 1 A 179 MET ASN PRO ALA MET PRO THR SER SER GLY SER GLU GLY
SEQRES 2 A 179 ASN VAL LYS LEU CYS SER LEU GLU GLU ALA GLN ARG ILE
SEQRES 3 A 179 TRP LYS GLN LYS SER ALA GLU ILE TYR PRO ILE MET ASP
SEQRES 4 A 179 LYS SER SER ARG THR ARG LEU ALA LEU ILE ILE CYS ASN
SEQRES 5 A 179 GLU GLU PHE ASP SER ILE PRO ARG ARG THR GLY ALA GLU
SEQRES 6 A 179 VAL ASP ILE THR GLY MET THR MET LEU LEU GLN ASN LEU
SEQRES 7 A 179 GLY TYR SER VAL ASP VAL LYS LYS ASN LEU THR ALA SER
SEQRES 8 A 179 ASP MET THR THR GLU LEU GLU ALA PHE ALA HIS ARG PRO
SEQRES 9 A 179 GLU HIS LYS THR SER ASP SER THR PHE LEU VAL PHE MET
SEQRES 10 A 179 SER HIS GLY ILE ARG GLU GLY ILE CYS GLY LYS LYS HIS
SEQRES 11 A 179 SER GLU GLN VAL PRO ASP ILE LEU GLN LEU ASN ALA ILE
SEQRES 12 A 179 PHE ASN MET LEU ASN THR LYS ASN CYS PRO SER LEU LYS
SEQRES 13 A 179 ASP LYS PRO LYS VAL ILE ILE ILE GLN ALA CYS ARG GLY
SEQRES 14 A 179 ASP SER PRO GLY VAL VAL TRP PHE LYS ASP
SEQRES 1 B 89 MET ALA ILE ARG LYS ALA HIS ILE GLU LYS ASP PHE ILE
SEQRES 2 B 89 ALA PHE CYS SER SER THR PRO ASP ASN VAL SER TRP ARG
SEQRES 3 B 89 HIS PRO THR MET GLY SER VAL PHE ILE GLY ARG LEU ILE
SEQRES 4 B 89 GLU HIS MET GLN GLU TYR ALA CYS SER CYS ASP VAL GLU
SEQRES 5 B 89 GLU ILE PHE ARG LYS VAL ARG PHE SER PHE GLU GLN PRO
SEQRES 6 B 89 ASP GLY ARG ALA GLN MET PRO THR THR GLU ARG VAL THR
SEQRES 7 B 89 LEU THR ARG CYS PHE TYR LEU PHE PRO GLY HIS
SEQRES 1 C 5 PHQ VAL ALA ASP CF0
HET PHQ C 1 10
HET CF0 C 5 1
HETNAM PHQ BENZYL CHLOROCARBONATE
HETNAM CF0 FLUOROMETHANE
HETSYN CF0 FLUORO METHYL GROUP
FORMUL 3 PHQ C8 H7 CL O2
FORMUL 3 CF0 C H3 F
FORMUL 4 HOH *238(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 HIS A 220 1 14
HELIX 4 4 ARG A 221 SER A 227 5 7
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 PHE B 377 1 13
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 LYS A 203
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 ILE A 281 N PHE A 234
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 3 GLY A 238 ILE A 239 0
SHEET 2 B 3 GLY A 242 CYS A 244 -1 O GLY A 242 N ILE A 239
SHEET 3 B 3 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 C1 PHQ C 1 N VAL C 2 1555 1555 1.33
LINK C ASP C 4 C1 CF0 C 5 1555 1555 1.53
LINK SG CYS A 285 C1 CF0 C 5 1555 1555 1.81
SITE 1 AC1 13 ARG A 179 HIS A 237 GLY A 238 GLN A 283
SITE 2 AC1 13 CYS A 285 SER B 339 TRP B 340 ARG B 341
SITE 3 AC1 13 HIS B 342 PRO B 343 ARG B 383 HOH C 367
SITE 4 AC1 13 HOH C 429
CRYST1 62.968 62.968 161.783 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 0.015881 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015881 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006181 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
