HEADER HYDROLASE/HYDROLASE INHIBITOR 12-JUL-07 2QL5
TITLE CRYSTAL STRUCTURE OF CASPASE-7 WITH INHIBITOR AC-DMQD-CHO
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASPASE-7;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: P20 SUBUNIT;
COMPND 5 SYNONYM: CASP-7, ICE-LIKE APOPTOTIC PROTEASE 3, ICE-LAP3, APOPTOTIC
COMPND 6 PROTEASE MCH-3, CMH-1;
COMPND 7 EC: 3.4.22.60;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: CASPASE-7;
COMPND 11 CHAIN: B, D;
COMPND 12 FRAGMENT: P10 SUBUNIT;
COMPND 13 SYNONYM: CASP-7, ICE-LIKE APOPTOTIC PROTEASE 3, ICE-LAP3, APOPTOTIC
COMPND 14 PROTEASE MCH-3, CMH-1;
COMPND 15 EC: 3.4.22.60;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 3;
COMPND 18 MOLECULE: INHIBITOR;
COMPND 19 CHAIN: E, F;
COMPND 20 ENGINEERED: YES;
COMPND 21 MOL_ID: 4;
COMPND 22 MOLECULE: PEPTIDE;
COMPND 23 CHAIN: G;
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: CASP7, MCH3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET23B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: CASP7, MCH3;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET23B;
SOURCE 21 MOL_ID: 3;
SOURCE 22 SYNTHETIC: YES;
SOURCE 23 MOL_ID: 4;
SOURCE 24 SYNTHETIC: YES
KEYWDS CYSTEINE PROTEASE, APOPTOSIS, THIOL PROTEASE, ZYMOGEN, HYDROLASE-
KEYWDS 2 HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.AGNISWAMY,B.FANG,I.WEBER
REVDAT 9 15-NOV-23 2QL5 1 REMARK
REVDAT 8 30-AUG-23 2QL5 1 REMARK LINK
REVDAT 7 26-JUN-13 2QL5 1 HET HETATM HETNAM LINK
REVDAT 7 2 1 FORMUL SEQRES REMARK
REVDAT 6 19-JUN-13 2QL5 1 REMARK
REVDAT 5 13-JUL-11 2QL5 1 VERSN
REVDAT 4 24-FEB-09 2QL5 1 VERSN
REVDAT 3 29-APR-08 2QL5 1 REMARK
REVDAT 2 09-OCT-07 2QL5 1 JRNL
REVDAT 1 28-AUG-07 2QL5 0
JRNL AUTH J.AGNISWAMY,B.FANG,I.T.WEBER
JRNL TITL PLASTICITY OF S2-S4 SPECIFICITY POCKETS OF EXECUTIONER
JRNL TITL 2 CASPASE-7 REVEALED BY STRUCTURAL AND KINETIC ANALYSIS.
JRNL REF FEBS J. V. 274 4752 2007
JRNL REFN ISSN 1742-464X
JRNL PMID 17697120
JRNL DOI 10.1111/J.1742-4658.2007.05994.X
REMARK 2
REMARK 2 RESOLUTION. 2.34 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.34
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 27256
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1497
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3825
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 13
REMARK 3 SOLVENT ATOMS : 125
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2QL5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-07.
REMARK 100 THE DEPOSITION ID IS D_1000043735.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUN-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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) : 1.000
REMARK 200 MONOCHROMATOR : SI 220
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27256
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.340
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 (%) : 85.0
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.4600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.34
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.34200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.960
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1F1J
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14.5% PEG 3350, 0.3M DIAMMONIUM
REMARK 280 HYDROGEN CITRATE, PH 7.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 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+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 125.13800
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 62.56900
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 62.56900
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 125.13800
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: HEPTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEPTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G
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 CASPASE-7 INHIBITOR AC-DMQD-CHO IS PEPTIDE-LIKE, A MEMBER OF
REMARK 400 INHIBITOR CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: CASPASE-7 INHIBITOR AC-DMQD-CHO
REMARK 400 CHAIN: E, F
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 ALA A 24
REMARK 465 LYS A 25
REMARK 465 PRO A 26
REMARK 465 ASP A 27
REMARK 465 ARG A 28
REMARK 465 SER A 29
REMARK 465 SER A 30
REMARK 465 PHE A 31
REMARK 465 VAL A 32
REMARK 465 PRO A 33
REMARK 465 SER A 34
REMARK 465 LEU A 35
REMARK 465 PHE A 36
REMARK 465 SER A 37
REMARK 465 LYS A 38
REMARK 465 LYS A 39
REMARK 465 LYS A 40
REMARK 465 LYS A 41
REMARK 465 ASN A 42
REMARK 465 VAL A 43
REMARK 465 THR A 44
REMARK 465 MET A 45
REMARK 465 ARG A 46
REMARK 465 SER A 47
REMARK 465 ILE A 48
REMARK 465 LYS A 49
REMARK 465 THR A 50
REMARK 465 THR A 51
REMARK 465 ARG A 52
REMARK 465 ASP A 53
REMARK 465 ARG A 54
REMARK 465 VAL A 55
REMARK 465 PRO A 56
REMARK 465 ALA B 207
REMARK 465 ASN B 208
REMARK 465 PRO B 209
REMARK 465 ARG B 210
REMARK 465 TYR B 211
REMARK 465 ALA C 324
REMARK 465 LYS C 325
REMARK 465 PRO C 326
REMARK 465 ASP C 327
REMARK 465 ARG C 328
REMARK 465 SER C 329
REMARK 465 SER C 330
REMARK 465 PHE C 331
REMARK 465 VAL C 332
REMARK 465 PRO C 333
REMARK 465 SER C 334
REMARK 465 LEU C 335
REMARK 465 PHE C 336
REMARK 465 SER C 337
REMARK 465 LYS C 338
REMARK 465 LYS C 339
REMARK 465 LYS C 340
REMARK 465 LYS C 341
REMARK 465 ASN C 342
REMARK 465 VAL C 343
REMARK 465 THR C 344
REMARK 465 MET C 345
REMARK 465 ARG C 346
REMARK 465 SER C 347
REMARK 465 ILE C 348
REMARK 465 LYS C 349
REMARK 465 THR C 350
REMARK 465 THR C 351
REMARK 465 ARG C 352
REMARK 465 ASP C 353
REMARK 465 ARG C 354
REMARK 465 VAL C 355
REMARK 465 PRO C 356
REMARK 465 ALA D 507
REMARK 465 ASN D 508
REMARK 465 PRO D 509
REMARK 465 ARG D 510
REMARK 465 TYR D 511
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 LEU C 422 CA - CB - CG ANGL. DEV. = 14.2 DEGREES
REMARK 500 ASP F 802 N - CA - CB ANGL. DEV. = -12.2 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 ASP A 113 60.43 35.77
REMARK 500 CYS A 136 -165.22 -164.46
REMARK 500 SER A 143 -171.52 -173.25
REMARK 500 ASN A 148 -3.85 68.34
REMARK 500 CYS A 171 76.86 -158.28
REMARK 500 SER C 443 -171.53 -170.02
REMARK 500 CYS C 471 66.51 -161.41
REMARK 500 SER D 602 -156.06 -98.72
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 CIT D 850
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN E OF INHIBITOR
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN F OF INHIBITOR
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN G OF PEPTIDE
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2QL7 RELATED DB: PDB
REMARK 900 RELATED ID: 2QL9 RELATED DB: PDB
REMARK 900 RELATED ID: 2QLB RELATED DB: PDB
REMARK 900 RELATED ID: 2QLF RELATED DB: PDB
REMARK 900 RELATED ID: 2QLJ RELATED DB: PDB
DBREF 2QL5 A 24 196 UNP P55210 CASP7_HUMAN 24 196
DBREF 2QL5 B 207 303 UNP P55210 CASP7_HUMAN 207 303
DBREF 2QL5 C 324 496 UNP P55210 CASP7_HUMAN 24 196
DBREF 2QL5 D 507 603 UNP P55210 CASP7_HUMAN 207 303
DBREF 2QL5 E 701 705 PDB 2QL5 2QL5 701 705
DBREF 2QL5 F 801 805 PDB 2QL5 2QL5 801 805
DBREF 2QL5 G 810 814 PDB 2QL5 2QL5 810 814
SEQRES 1 A 173 ALA LYS PRO ASP ARG SER SER PHE VAL PRO SER LEU PHE
SEQRES 2 A 173 SER LYS LYS LYS LYS ASN VAL THR MET ARG SER ILE LYS
SEQRES 3 A 173 THR THR ARG ASP ARG VAL PRO THR TYR GLN TYR ASN MET
SEQRES 4 A 173 ASN PHE GLU LYS LEU GLY LYS CYS ILE ILE ILE ASN ASN
SEQRES 5 A 173 LYS ASN PHE ASP LYS VAL THR GLY MET GLY VAL ARG ASN
SEQRES 6 A 173 GLY THR ASP LYS ASP ALA GLU ALA LEU PHE LYS CYS PHE
SEQRES 7 A 173 ARG SER LEU GLY PHE ASP VAL ILE VAL TYR ASN ASP CYS
SEQRES 8 A 173 SER CYS ALA LYS MET GLN ASP LEU LEU LYS LYS ALA SER
SEQRES 9 A 173 GLU GLU ASP HIS THR ASN ALA ALA CYS PHE ALA CYS ILE
SEQRES 10 A 173 LEU LEU SER HIS GLY GLU GLU ASN VAL ILE TYR GLY LYS
SEQRES 11 A 173 ASP GLY VAL THR PRO ILE LYS ASP LEU THR ALA HIS PHE
SEQRES 12 A 173 ARG GLY ASP ARG CYS LYS THR LEU LEU GLU LYS PRO LYS
SEQRES 13 A 173 LEU PHE PHE ILE GLN ALA CYS ARG GLY THR GLU LEU ASP
SEQRES 14 A 173 ASP GLY ILE GLN
SEQRES 1 B 97 ALA ASN PRO ARG TYR LYS ILE PRO VAL GLU ALA ASP PHE
SEQRES 2 B 97 LEU PHE ALA TYR SER THR VAL PRO GLY TYR TYR SER TRP
SEQRES 3 B 97 ARG SER PRO GLY ARG GLY SER TRP PHE VAL GLN ALA LEU
SEQRES 4 B 97 CYS SER ILE LEU GLU GLU HIS GLY LYS ASP LEU GLU ILE
SEQRES 5 B 97 MET GLN ILE LEU THR ARG VAL ASN ASP ARG VAL ALA ARG
SEQRES 6 B 97 HIS PHE GLU SER GLN SER ASP ASP PRO HIS PHE HIS GLU
SEQRES 7 B 97 LYS LYS GLN ILE PRO CYS VAL VAL SER MET LEU THR LYS
SEQRES 8 B 97 GLU LEU TYR PHE SER GLN
SEQRES 1 C 173 ALA LYS PRO ASP ARG SER SER PHE VAL PRO SER LEU PHE
SEQRES 2 C 173 SER LYS LYS LYS LYS ASN VAL THR MET ARG SER ILE LYS
SEQRES 3 C 173 THR THR ARG ASP ARG VAL PRO THR TYR GLN TYR ASN MET
SEQRES 4 C 173 ASN PHE GLU LYS LEU GLY LYS CYS ILE ILE ILE ASN ASN
SEQRES 5 C 173 LYS ASN PHE ASP LYS VAL THR GLY MET GLY VAL ARG ASN
SEQRES 6 C 173 GLY THR ASP LYS ASP ALA GLU ALA LEU PHE LYS CYS PHE
SEQRES 7 C 173 ARG SER LEU GLY PHE ASP VAL ILE VAL TYR ASN ASP CYS
SEQRES 8 C 173 SER CYS ALA LYS MET GLN ASP LEU LEU LYS LYS ALA SER
SEQRES 9 C 173 GLU GLU ASP HIS THR ASN ALA ALA CYS PHE ALA CYS ILE
SEQRES 10 C 173 LEU LEU SER HIS GLY GLU GLU ASN VAL ILE TYR GLY LYS
SEQRES 11 C 173 ASP GLY VAL THR PRO ILE LYS ASP LEU THR ALA HIS PHE
SEQRES 12 C 173 ARG GLY ASP ARG CYS LYS THR LEU LEU GLU LYS PRO LYS
SEQRES 13 C 173 LEU PHE PHE ILE GLN ALA CYS ARG GLY THR GLU LEU ASP
SEQRES 14 C 173 ASP GLY ILE GLN
SEQRES 1 D 97 ALA ASN PRO ARG TYR LYS ILE PRO VAL GLU ALA ASP PHE
SEQRES 2 D 97 LEU PHE ALA TYR SER THR VAL PRO GLY TYR TYR SER TRP
SEQRES 3 D 97 ARG SER PRO GLY ARG GLY SER TRP PHE VAL GLN ALA LEU
SEQRES 4 D 97 CYS SER ILE LEU GLU GLU HIS GLY LYS ASP LEU GLU ILE
SEQRES 5 D 97 MET GLN ILE LEU THR ARG VAL ASN ASP ARG VAL ALA ARG
SEQRES 6 D 97 HIS PHE GLU SER GLN SER ASP ASP PRO HIS PHE HIS GLU
SEQRES 7 D 97 LYS LYS GLN ILE PRO CYS VAL VAL SER MET LEU THR LYS
SEQRES 8 D 97 GLU LEU TYR PHE SER GLN
SEQRES 1 E 5 ACE ASP MET GLN ASJ
SEQRES 1 F 5 ACE ASP MET GLN ASJ
SEQRES 1 G 5 GLN GLY HIS GLY GLU
HET ACE E 701 3
HET ASJ E 705 8
HET ACE F 801 3
HET ASJ F 805 8
HET CIT D 850 13
HETNAM ACE ACETYL GROUP
HETNAM ASJ (3S)-3-AMINO-4-HYDROXYBUTANOIC ACID
HETNAM CIT CITRIC ACID
FORMUL 5 ACE 2(C2 H4 O)
FORMUL 5 ASJ 2(C4 H9 N O3)
FORMUL 8 CIT C6 H8 O7
FORMUL 9 HOH *125(H2 O)
HELIX 1 1 ASP A 79 GLY A 83 5 5
HELIX 2 2 GLY A 89 GLY A 105 1 17
HELIX 3 3 SER A 115 GLU A 129 1 15
HELIX 4 4 ILE A 159 ALA A 164 1 6
HELIX 5 5 HIS A 165 ARG A 167 5 3
HELIX 6 6 CYS A 171 LEU A 175 5 5
HELIX 7 7 TRP B 240 GLY B 253 1 14
HELIX 8 8 GLU B 257 PHE B 273 1 17
HELIX 9 9 ASP B 279 HIS B 283 5 5
HELIX 10 10 ASP C 379 GLY C 383 5 5
HELIX 11 11 GLY C 389 GLY C 405 1 17
HELIX 12 12 SER C 415 GLU C 429 1 15
HELIX 13 13 ILE C 459 ALA C 464 1 6
HELIX 14 14 HIS C 465 ARG C 467 5 3
HELIX 15 15 CYS C 471 LEU C 475 5 5
HELIX 16 16 TRP D 540 GLY D 553 1 14
HELIX 17 17 GLU D 557 PHE D 573 1 17
HELIX 18 18 ASP D 579 HIS D 583 5 5
SHEET 1 A12 PHE A 106 ASN A 112 0
SHEET 2 A12 LYS A 66 ASN A 74 1 N ASN A 74 O TYR A 111
SHEET 3 A12 ALA A 134 LEU A 142 1 O ILE A 140 N ILE A 71
SHEET 4 A12 LYS A 179 GLN A 184 1 O PHE A 182 N LEU A 141
SHEET 5 A12 PHE B 219 TYR B 223 1 O ALA B 222 N PHE A 181
SHEET 6 A12 CYS B 290 SER B 293 -1 O VAL B 292 N PHE B 221
SHEET 7 A12 CYS D 590 SER D 593 -1 O SER D 593 N VAL B 291
SHEET 8 A12 PHE D 519 TYR D 523 -1 N PHE D 521 O VAL D 592
SHEET 9 A12 LYS C 479 GLN C 484 1 N ILE C 483 O ALA D 522
SHEET 10 A12 ALA C 434 LEU C 442 1 N LEU C 441 O GLN C 484
SHEET 11 A12 LYS C 366 ASN C 374 1 N ILE C 371 O ILE C 440
SHEET 12 A12 PHE C 406 ASN C 412 1 O TYR C 411 N ASN C 374
SHEET 1 B 3 GLY A 145 GLU A 146 0
SHEET 2 B 3 VAL A 149 TYR A 151 -1 O VAL A 149 N GLU A 146
SHEET 3 B 3 VAL A 156 PRO A 158 -1 O THR A 157 N ILE A 150
SHEET 1 C 3 GLY B 238 SER B 239 0
SHEET 2 C 3 TRP B 232 SER B 234 -1 N SER B 234 O GLY B 238
SHEET 3 C 3 MET E 703 GLN E 704 -1 O MET E 703 N ARG B 233
SHEET 1 D 3 GLY C 445 GLU C 446 0
SHEET 2 D 3 VAL C 449 TYR C 451 -1 O VAL C 449 N GLU C 446
SHEET 3 D 3 VAL C 456 PRO C 458 -1 O THR C 457 N ILE C 450
SHEET 1 E 3 GLY D 538 SER D 539 0
SHEET 2 E 3 TRP D 532 SER D 534 -1 N SER D 534 O GLY D 538
SHEET 3 E 3 MET F 803 GLN F 804 -1 O MET F 803 N ARG D 533
LINK SG CYS A 186 C ASJ E 705 1555 1555 1.76
LINK SG CYS C 486 C ASJ F 805 1555 1555 1.82
LINK C ACE E 701 N ASP E 702 1555 1555 1.39
LINK C GLN E 704 N ASJ E 705 1555 1555 1.33
LINK C ACE F 801 N ASP F 802 1555 1555 1.31
LINK C GLN F 804 N ASJ F 805 1555 1555 1.33
SITE 1 AC1 8 ARG A 187 PRO B 227 CYS B 290 VAL B 292
SITE 2 AC1 8 ARG C 487 TYR D 523 PRO D 527 VAL D 592
SITE 1 AC2 16 ARG A 87 SER A 143 HIS A 144 GLY A 145
SITE 2 AC2 16 GLN A 184 CYS A 186 TYR B 230 SER B 231
SITE 3 AC2 16 TRP B 232 ARG B 233 SER B 234 PRO B 235
SITE 4 AC2 16 SER B 275 GLN B 276 PHE B 282 HOH E 51
SITE 1 AC3 16 ARG C 387 HIS C 444 GLY C 445 GLN C 484
SITE 2 AC3 16 CYS C 486 TYR D 530 SER D 531 TRP D 532
SITE 3 AC3 16 ARG D 533 SER D 534 PRO D 535 SER D 575
SITE 4 AC3 16 GLN D 576 PHE D 582 HOH F 4 HOH F 36
SITE 1 AC4 8 GLN A 59 GLN B 260 GLU B 298 TYR B 300
SITE 2 AC4 8 SER B 302 GLN C 359 GLN D 560 TYR D 600
CRYST1 87.255 87.255 187.707 90.00 90.00 120.00 P 32 2 1 12
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 0.011461 0.006617 0.000000 0.00000
SCALE2 0.000000 0.013234 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005327 0.00000
(ATOM LINES ARE NOT SHOWN.)
END