HEADER HYDROLASE/HYDROLASE INHIBITOR 21-FEB-16 5IAB
TITLE CASPASE 3 V266D
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASPASE-3;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: CASP-3,APOPAIN,CYSTEINE PROTEASE CPP32,CPP-32,PROTEIN YAMA,
COMPND 5 SREBP CLEAVAGE ACTIVITY 1,SCA-1;
COMPND 6 EC: 3.4.22.56;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: ACE-ASP-GLU-VAL-ASK;
COMPND 11 CHAIN: D, E;
COMPND 12 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: UNIDENTIFIED;
SOURCE 11 ORGANISM_TAXID: 32644
KEYWDS ALLOSTERY, SATURATION MUTAGENESIS, CONFORMATIONAL SELECTION, NATIVE
KEYWDS 2 ENSEMBLE, PROTEIN SOLVATION, PROTEIN STRUCTURE, PROTEIN DYNAMICS,
KEYWDS 3 HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.J.MACIAG,S.H.MACKENZIE,M.B.TUCKER,J.L.SCHIPPER,P.D.SWARTZ,A.C.CLARK
REVDAT 1 26-OCT-16 5IAB 0
JRNL AUTH J.J.MACIAG,S.H.MACKENZIE,M.B.TUCKER,J.L.SCHIPPER,P.SWARTZ,
JRNL AUTH 2 A.C.CLARK
JRNL TITL TUNABLE ALLOSTERIC LIBRARY OF CASPASE-3 IDENTIFIES COUPLING
JRNL TITL 2 BETWEEN CONSERVED WATER MOLECULES AND CONFORMATIONAL
JRNL TITL 3 SELECTION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 113 E6080 2016
JRNL REFN ESSN 1091-6490
JRNL PMID 27681633
JRNL DOI 10.1073/PNAS.1603549113
REMARK 2
REMARK 2 RESOLUTION. 1.79 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.79
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.80
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 54012
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.740
REMARK 3 FREE R VALUE TEST SET COUNT : 2018
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 33.8042 - 4.3040 1.00 3798 150 0.1544 0.1651
REMARK 3 2 4.3040 - 3.4173 1.00 3753 145 0.1412 0.1798
REMARK 3 3 3.4173 - 2.9856 1.00 3733 144 0.1758 0.2295
REMARK 3 4 2.9856 - 2.7128 1.00 3751 143 0.1853 0.2311
REMARK 3 5 2.7128 - 2.5184 1.00 3724 150 0.1870 0.2110
REMARK 3 6 2.5184 - 2.3699 1.00 3723 141 0.1684 0.2247
REMARK 3 7 2.3699 - 2.2513 1.00 3731 149 0.1667 0.2175
REMARK 3 8 2.2513 - 2.1533 1.00 3713 142 0.1689 0.1988
REMARK 3 9 2.1533 - 2.0704 1.00 3719 140 0.1840 0.2412
REMARK 3 10 2.0704 - 1.9990 1.00 3739 151 0.1876 0.2402
REMARK 3 11 1.9990 - 1.9365 1.00 3697 136 0.1887 0.2420
REMARK 3 12 1.9365 - 1.8811 1.00 3728 148 0.2035 0.2785
REMARK 3 13 1.8811 - 1.8316 1.00 3704 130 0.2395 0.2726
REMARK 3 14 1.8316 - 1.7869 0.94 3481 149 0.2625 0.3076
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.470
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 4089
REMARK 3 ANGLE : 0.996 5522
REMARK 3 CHIRALITY : 0.062 598
REMARK 3 PLANARITY : 0.005 709
REMARK 3 DIHEDRAL : 15.915 2517
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5IAB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1000218529.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-BM
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 : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54012
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.787
REMARK 200 RESOLUTION RANGE LOW (A) : 33.798
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 1.3400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CASPASE-3 VARIANTS WERE CRYSTALLIZED
REMARK 280 IN THE PRESENCE OF AC-DEVD-CMK. PROTEINS WERE DIALYZED IN A
REMARK 280 BUFFER OF 10 MM TRIS-HCL, PH 8.5, 1 MM DTT. THE PROTEIN WAS
REMARK 280 CONCENTRATED TO 10 MG/ML USING AMICON ULTRAFREE CENTRIFUGAL
REMARK 280 FILTER DEVICES, AND INHIBITOR, AC-DEVD-CMK RECONSTITUTED IN DMSO,
REMARK 280 WAS THEN ADDED AT 5:1 WT:WT, INHIBITOR TO PEPTIDE. THE PROTEIN
REMARK 280 WAS DILUTED TO A CONCENTRATION OF 8 MG/ML BY ADDING 10 MM TRIS-
REMARK 280 HCL, PH 8.5, CONCENTRATED DTT AND CONCENTRATED NAN3 SO THAT THE
REMARK 280 FINAL BUFFER WAS 10 MM TRIS-HCL, PH 8.5, 10 MM DTT, 3 MM NAN3. 2
REMARK 280 UL OF 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., VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
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 54.29500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.35450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 54.29500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 48.35450
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: 6780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D, E
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 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: D, E
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 MET A 1
REMARK 465 GLU A 2
REMARK 465 ASN A 3
REMARK 465 THR A 4
REMARK 465 GLU A 5
REMARK 465 ASN A 6
REMARK 465 SER A 7
REMARK 465 VAL A 8
REMARK 465 ASP A 9
REMARK 465 SER A 10
REMARK 465 LYS A 11
REMARK 465 SER A 12
REMARK 465 ILE A 13
REMARK 465 LYS A 14
REMARK 465 ASN A 15
REMARK 465 LEU A 16
REMARK 465 GLU A 17
REMARK 465 PRO A 18
REMARK 465 LYS A 19
REMARK 465 ILE A 20
REMARK 465 ILE A 21
REMARK 465 HIS A 22
REMARK 465 GLY A 23
REMARK 465 SER A 24
REMARK 465 GLU A 25
REMARK 465 SER A 26
REMARK 465 MET A 27
REMARK 465 ASP A 28
REMARK 465 SER A 29
REMARK 465 GLY A 30
REMARK 465 ILE A 31
REMARK 465 SER A 32
REMARK 465 LEU A 33
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 465 ASP A 180
REMARK 465 ASP A 181
REMARK 465 MET A 182
REMARK 465 ALA A 183
REMARK 465 CYS A 184
REMARK 465 MET C 1
REMARK 465 GLU C 2
REMARK 465 ASN C 3
REMARK 465 THR C 4
REMARK 465 GLU C 5
REMARK 465 ASN C 6
REMARK 465 SER C 7
REMARK 465 VAL C 8
REMARK 465 ASP C 9
REMARK 465 SER C 10
REMARK 465 LYS C 11
REMARK 465 SER C 12
REMARK 465 ILE C 13
REMARK 465 LYS C 14
REMARK 465 ASN C 15
REMARK 465 LEU C 16
REMARK 465 GLU C 17
REMARK 465 PRO C 18
REMARK 465 LYS C 19
REMARK 465 ILE C 20
REMARK 465 ILE C 21
REMARK 465 HIS C 22
REMARK 465 GLY C 23
REMARK 465 SER C 24
REMARK 465 GLU C 25
REMARK 465 SER C 26
REMARK 465 MET C 27
REMARK 465 ASP C 28
REMARK 465 SER C 29
REMARK 465 GLY C 30
REMARK 465 ILE C 31
REMARK 465 SER C 32
REMARK 465 LEU C 33
REMARK 465 ASP C 34
REMARK 465 ASP C 175
REMARK 465 SER C 176
REMARK 465 GLY C 177
REMARK 465 VAL C 178
REMARK 465 ASP C 179
REMARK 465 ASP C 180
REMARK 465 ASP C 181
REMARK 465 MET C 182
REMARK 465 ALA C 183
REMARK 465 CYS C 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 THR A 174 OG1 CG2
REMARK 470 THR C 174 OG1 CG2
REMARK 470 HIS C 185 CG ND1 CD2 CE1 NE2
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 O HOH C 306 O HOH C 324 2.14
REMARK 500
REMARK 500 REMARK: NULL
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 CYS A 163 CA - CB - SG ANGL. DEV. = 16.9 DEGREES
REMARK 500 CYS C 163 CA - CB - SG ANGL. DEV. = 14.3 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 ARG C 144 150.86 -49.91
REMARK 500 LYS C 229 -33.35 -134.63
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 C 468 DISTANCE = 6.03 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DTT A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ACE D 1 and ASP D 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ASP D 5 and 0QE D 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ACE E 1 and ASP E 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ASP E 5 and 0QE E 6
DBREF 5IAB A 1 277 UNP P42574 CASP3_HUMAN 1 277
DBREF 5IAB C 1 277 UNP P42574 CASP3_HUMAN 1 277
DBREF 5IAB D 1 6 PDB 5IAB 5IAB 1 6
DBREF 5IAB E 1 6 PDB 5IAB 5IAB 1 6
SEQADV 5IAB ASP A 266 UNP P42574 VAL 266 ENGINEERED MUTATION
SEQADV 5IAB LEU A 278 UNP P42574 EXPRESSION TAG
SEQADV 5IAB ASP C 266 UNP P42574 VAL 266 ENGINEERED MUTATION
SEQADV 5IAB LEU C 278 UNP P42574 EXPRESSION TAG
SEQRES 1 A 278 MET GLU ASN THR GLU ASN SER VAL ASP SER LYS SER ILE
SEQRES 2 A 278 LYS ASN LEU GLU PRO LYS ILE ILE HIS GLY SER GLU SER
SEQRES 3 A 278 MET ASP SER GLY ILE SER LEU ASP ASN SER TYR LYS MET
SEQRES 4 A 278 ASP TYR PRO GLU MET GLY LEU CYS ILE ILE ILE ASN ASN
SEQRES 5 A 278 LYS ASN PHE HIS LYS SER THR GLY MET THR SER ARG SER
SEQRES 6 A 278 GLY THR ASP VAL ASP ALA ALA ASN LEU ARG GLU THR PHE
SEQRES 7 A 278 ARG ASN LEU LYS TYR GLU VAL ARG ASN LYS ASN ASP LEU
SEQRES 8 A 278 THR ARG GLU GLU ILE VAL GLU LEU MET ARG ASP VAL SER
SEQRES 9 A 278 LYS GLU ASP HIS SER LYS ARG SER SER PHE VAL CYS VAL
SEQRES 10 A 278 LEU LEU SER HIS GLY GLU GLU GLY ILE ILE PHE GLY THR
SEQRES 11 A 278 ASN GLY PRO VAL ASP LEU LYS LYS ILE THR ASN PHE PHE
SEQRES 12 A 278 ARG GLY ASP ARG CYS ARG SER LEU THR GLY LYS PRO LYS
SEQRES 13 A 278 LEU PHE ILE ILE GLN ALA CYS ARG GLY THR GLU LEU ASP
SEQRES 14 A 278 CYS GLY ILE GLU THR ASP SER GLY VAL ASP ASP ASP MET
SEQRES 15 A 278 ALA CYS HIS LYS ILE PRO VAL GLU ALA ASP PHE LEU TYR
SEQRES 16 A 278 ALA TYR SER THR ALA PRO GLY TYR TYR SER TRP ARG ASN
SEQRES 17 A 278 SER LYS ASP GLY SER TRP PHE ILE GLN SER LEU CYS ALA
SEQRES 18 A 278 MET LEU LYS GLN TYR ALA ASP LYS LEU GLU PHE MET HIS
SEQRES 19 A 278 ILE LEU THR ARG VAL ASN ARG LYS VAL ALA THR GLU PHE
SEQRES 20 A 278 GLU SER PHE SER PHE ASP ALA THR PHE HIS ALA LYS LYS
SEQRES 21 A 278 GLN ILE PRO CYS ILE ASP SER MET LEU THR LYS GLU LEU
SEQRES 22 A 278 TYR PHE TYR HIS LEU
SEQRES 1 C 278 MET GLU ASN THR GLU ASN SER VAL ASP SER LYS SER ILE
SEQRES 2 C 278 LYS ASN LEU GLU PRO LYS ILE ILE HIS GLY SER GLU SER
SEQRES 3 C 278 MET ASP SER GLY ILE SER LEU ASP ASN SER TYR LYS MET
SEQRES 4 C 278 ASP TYR PRO GLU MET GLY LEU CYS ILE ILE ILE ASN ASN
SEQRES 5 C 278 LYS ASN PHE HIS LYS SER THR GLY MET THR SER ARG SER
SEQRES 6 C 278 GLY THR ASP VAL ASP ALA ALA ASN LEU ARG GLU THR PHE
SEQRES 7 C 278 ARG ASN LEU LYS TYR GLU VAL ARG ASN LYS ASN ASP LEU
SEQRES 8 C 278 THR ARG GLU GLU ILE VAL GLU LEU MET ARG ASP VAL SER
SEQRES 9 C 278 LYS GLU ASP HIS SER LYS ARG SER SER PHE VAL CYS VAL
SEQRES 10 C 278 LEU LEU SER HIS GLY GLU GLU GLY ILE ILE PHE GLY THR
SEQRES 11 C 278 ASN GLY PRO VAL ASP LEU LYS LYS ILE THR ASN PHE PHE
SEQRES 12 C 278 ARG GLY ASP ARG CYS ARG SER LEU THR GLY LYS PRO LYS
SEQRES 13 C 278 LEU PHE ILE ILE GLN ALA CYS ARG GLY THR GLU LEU ASP
SEQRES 14 C 278 CYS GLY ILE GLU THR ASP SER GLY VAL ASP ASP ASP MET
SEQRES 15 C 278 ALA CYS HIS LYS ILE PRO VAL GLU ALA ASP PHE LEU TYR
SEQRES 16 C 278 ALA TYR SER THR ALA PRO GLY TYR TYR SER TRP ARG ASN
SEQRES 17 C 278 SER LYS ASP GLY SER TRP PHE ILE GLN SER LEU CYS ALA
SEQRES 18 C 278 MET LEU LYS GLN TYR ALA ASP LYS LEU GLU PHE MET HIS
SEQRES 19 C 278 ILE LEU THR ARG VAL ASN ARG LYS VAL ALA THR GLU PHE
SEQRES 20 C 278 GLU SER PHE SER PHE ASP ALA THR PHE HIS ALA LYS LYS
SEQRES 21 C 278 GLN ILE PRO CYS ILE ASP SER MET LEU THR LYS GLU LEU
SEQRES 22 C 278 TYR PHE TYR HIS LEU
SEQRES 1 D 6 ACE ASP GLU VAL ASP 0QE
SEQRES 1 E 6 ACE ASP GLU VAL ASP 0QE
HET ACE D 1 3
HET 0QE D 6 2
HET ACE E 1 3
HET 0QE E 6 2
HET DTT A 301 8
HETNAM ACE ACETYL GROUP
HETNAM 0QE CHLOROMETHANE
HETNAM DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE
HETSYN 0QE CHLORO METHYL GROUP
HETSYN DTT 1,4-DITHIOTHREITOL
FORMUL 3 ACE 2(C2 H4 O)
FORMUL 3 0QE 2(C H3 CL)
FORMUL 5 DTT C4 H10 O2 S2
FORMUL 6 HOH *353(H2 O)
HELIX 1 AA1 GLY A 66 LEU A 81 1 16
HELIX 2 AA2 THR A 92 LYS A 105 1 14
HELIX 3 AA3 LEU A 136 ASN A 141 1 6
HELIX 4 AA4 PHE A 142 ARG A 144 5 3
HELIX 5 AA5 CYS A 148 THR A 152 5 5
HELIX 6 AA6 TRP A 214 ALA A 227 1 14
HELIX 7 AA7 GLU A 231 PHE A 247 1 17
HELIX 8 AA8 ASP A 253 HIS A 257 5 5
HELIX 9 AA9 HIS C 56 GLY C 60 5 5
HELIX 10 AB1 GLY C 66 LEU C 81 1 16
HELIX 11 AB2 THR C 92 LYS C 105 1 14
HELIX 12 AB3 LEU C 136 PHE C 142 1 7
HELIX 13 AB4 CYS C 148 THR C 152 5 5
HELIX 14 AB5 TRP C 214 ALA C 227 1 14
HELIX 15 AB6 GLU C 231 PHE C 247 1 17
HELIX 16 AB7 ASP C 253 HIS C 257 5 5
SHEET 1 AA112 GLU A 84 ASN A 89 0
SHEET 2 AA112 GLU A 43 ASN A 51 1 N ASN A 51 O LYS A 88
SHEET 3 AA112 ARG A 111 LEU A 119 1 O VAL A 117 N ILE A 48
SHEET 4 AA112 LYS A 156 GLN A 161 1 O LEU A 157 N PHE A 114
SHEET 5 AA112 PHE A 193 TYR A 197 1 O LEU A 194 N PHE A 158
SHEET 6 AA112 CYS A 264 SER A 267 -1 O ASP A 266 N TYR A 195
SHEET 7 AA112 CYS C 264 SER C 267 -1 O SER C 267 N ILE A 265
SHEET 8 AA112 PHE C 193 TYR C 197 -1 N TYR C 195 O ASP C 266
SHEET 9 AA112 LYS C 156 GLN C 161 1 N PHE C 158 O LEU C 194
SHEET 10 AA112 ARG C 111 LEU C 119 1 N PHE C 114 O LEU C 157
SHEET 11 AA112 GLU C 43 ASN C 51 1 N ILE C 48 O VAL C 117
SHEET 12 AA112 GLU C 84 ASN C 89 1 O LYS C 88 N ASN C 51
SHEET 1 AA2 3 GLY A 122 GLU A 123 0
SHEET 2 AA2 3 ILE A 126 GLY A 129 -1 O ILE A 126 N GLU A 123
SHEET 3 AA2 3 GLY A 132 ASP A 135 -1 O GLY A 132 N GLY A 129
SHEET 1 AA3 2 LYS A 186 ILE A 187 0
SHEET 2 AA3 2 ILE C 172 GLU C 173 -1 O ILE C 172 N ILE A 187
SHEET 1 AA4 3 GLY A 212 SER A 213 0
SHEET 2 AA4 3 TRP A 206 ASN A 208 -1 N ASN A 208 O GLY A 212
SHEET 3 AA4 3 GLU E 3 VAL E 4 -1 O GLU E 3 N ARG A 207
SHEET 1 AA5 3 GLY C 122 GLU C 123 0
SHEET 2 AA5 3 ILE C 126 GLY C 129 -1 O ILE C 126 N GLU C 123
SHEET 3 AA5 3 GLY C 132 ASP C 135 -1 O VAL C 134 N ILE C 127
SHEET 1 AA6 3 GLY C 212 SER C 213 0
SHEET 2 AA6 3 TRP C 206 ASN C 208 -1 N ASN C 208 O GLY C 212
SHEET 3 AA6 3 GLU D 3 VAL D 4 -1 O GLU D 3 N ARG C 207
LINK C ACE D 1 N ASP D 2 1555 1555 1.33
LINK C ASP D 5 C1 0QE D 6 1555 1555 1.52
LINK C ACE E 1 N ASP E 2 1555 1555 1.33
LINK C ASP E 5 C1 0QE E 6 1555 1555 1.52
SITE 1 AC1 5 ARG A 75 ARG A 86 ASN A 87 LYS A 88
SITE 2 AC1 5 HOH A 458
SITE 1 AC2 11 ARG C 207 ASN C 208 SER C 209 TRP C 214
SITE 2 AC2 11 SER C 249 PHE C 250 HOH C 365 GLU D 3
SITE 3 AC2 11 HOH D 203 HOH D 204 HOH D 205
SITE 1 AC3 9 ARG C 64 SER C 120 HIS C 121 GLN C 161
SITE 2 AC3 9 CYS C 163 SER C 205 ARG C 207 VAL D 4
SITE 3 AC3 9 HOH D 201
SITE 1 AC4 12 TRP A 206 ARG A 207 ASN A 208 SER A 209
SITE 2 AC4 12 TRP A 214 SER A 249 PHE A 250 HOH A 465
SITE 3 AC4 12 GLU E 3 HOH E 203 HOH E 204 HOH E 206
SITE 1 AC5 9 ARG A 64 SER A 120 HIS A 121 GLN A 161
SITE 2 AC5 9 CYS A 163 TYR A 204 SER A 205 ARG A 207
SITE 3 AC5 9 VAL E 4
CRYST1 108.590 96.709 68.929 90.00 126.30 90.00 C 1 2 1 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 0.009209 0.000000 0.006764 0.00000
SCALE2 0.000000 0.010340 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
