HEADER HYDROLASE/HYDROLASE INHIBITOR 18-MAY-15 4ZVS
TITLE CASPASE-7 VARIANT 1 (V1) WITH REPROGRAMMED SUBSTRATE SPECIFICITY DUE
TITLE 2 TO Y230A/W232M/S234N SUBSTITUTIONS, BOUND TO DEVD INHIBITOR.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASPASE-7;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: UNP RESIDUES 34-231;
COMPND 5 SYNONYM: CASP-7,APOPTOTIC PROTEASE MCH-3,CMH-1,ICE-LIKE APOPTOTIC
COMPND 6 PROTEASE 3,ICE-LAP3;
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: UNP RESIDUES 232-336;
COMPND 13 SYNONYM: CASP-7,APOPTOTIC PROTEASE MCH-3,CMH-1,ICE-LIKE APOPTOTIC
COMPND 14 PROTEASE 3,ICE-LAP3;
COMPND 15 EC: 3.4.22.60;
COMPND 16 ENGINEERED: YES;
COMPND 17 MUTATION: YES;
COMPND 18 MOL_ID: 3;
COMPND 19 MOLECULE: DEVD INHIBITOR;
COMPND 20 CHAIN: E, F;
COMPND 21 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(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: CASP7, MCH3;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 15 MOL_ID: 3;
SOURCE 16 SYNTHETIC: YES;
SOURCE 17 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 18 ORGANISM_TAXID: 32630
KEYWDS DIRECTED EVOLUTION, PROTEASE, PEPTIDE INHIBITOR, DESIGNED ACTIVE SITE
KEYWDS 2 SPECIFICITY, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.J.MACPHERSON,M.E.HILL,J.A.HARDY
REVDAT 6 15-NOV-23 4ZVS 1 REMARK
REVDAT 5 27-SEP-23 4ZVS 1 REMARK
REVDAT 4 25-DEC-19 4ZVS 1 REMARK
REVDAT 3 20-SEP-17 4ZVS 1 REMARK
REVDAT 2 06-JUL-16 4ZVS 1 JRNL
REVDAT 1 20-APR-16 4ZVS 0
JRNL AUTH M.E.HILL,D.J.MACPHERSON,P.WU,O.JULIEN,J.A.WELLS,J.A.HARDY
JRNL TITL REPROGRAMMING CASPASE-7 SPECIFICITY BY REGIO-SPECIFIC
JRNL TITL 2 MUTATIONS AND SELECTION PROVIDES ALTERNATE SOLUTIONS FOR
JRNL TITL 3 SUBSTRATE RECOGNITION.
JRNL REF ACS CHEM.BIOL. V. 11 1603 2016
JRNL REFN ESSN 1554-8937
JRNL PMID 27032039
JRNL DOI 10.1021/ACSCHEMBIO.5B00971
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9-1692
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 29842
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.860
REMARK 3 FREE R VALUE TEST SET COUNT : 1450
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.390
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.870
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.78
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 : 2
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN C
REMARK 3 ATOM PAIRS NUMBER : 1262
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN B
REMARK 3 SELECTION : CHAIN D
REMARK 3 ATOM PAIRS NUMBER : 890
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4ZVS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAY-15.
REMARK 100 THE DEPOSITION ID IS D_1000209173.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JUL-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.078
REMARK 200 MONOCHROMATOR : SI (111) CHANNEL-CUT
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29874
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.11300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.84700
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: PHASER 2.5.1
REMARK 200 STARTING MODEL: 3EDR
REMARK 200
REMARK 200 REMARK: RHOMBUS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 300 MM DIAMMONIUM HYDROGREN CITRATE,
REMARK 280 14% PEG 3350, 10 MM GUANIDINIUM CHLORIDE, 10 MM DITHIOTHERITOL,
REMARK 280 PH 5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277.15K
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 124.79333
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 62.39667
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 62.39667
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 124.79333
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -84.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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-ALDEHYDE IS PEPTIDE-LIKE, A MEMBER OF
REMARK 400 INHIBITOR CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: AC-ASP-GLU-VAL-ASP-ALDEHYDE
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 MET A 1
REMARK 465 ALA A 2
REMARK 465 ASP A 3
REMARK 465 ASP A 4
REMARK 465 GLN A 5
REMARK 465 GLY A 6
REMARK 465 CYS A 7
REMARK 465 ILE A 8
REMARK 465 GLU A 9
REMARK 465 GLU A 10
REMARK 465 GLN A 11
REMARK 465 GLY A 12
REMARK 465 VAL A 13
REMARK 465 GLU A 14
REMARK 465 ASP A 15
REMARK 465 SER A 16
REMARK 465 ALA A 17
REMARK 465 ASN A 18
REMARK 465 GLU A 19
REMARK 465 ASP A 20
REMARK 465 SER A 21
REMARK 465 VAL A 22
REMARK 465 ASP A 23
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 THR A 57
REMARK 465 ALA A 197
REMARK 465 ASP A 198
REMARK 465 SER B 199
REMARK 465 GLY B 200
REMARK 465 PRO B 201
REMARK 465 ILE B 202
REMARK 465 ASN B 203
REMARK 465 ASP B 204
REMARK 465 THR B 205
REMARK 465 ASP B 206
REMARK 465 ALA B 207
REMARK 465 ASN B 208
REMARK 465 PRO B 209
REMARK 465 ARG B 210
REMARK 465 LEU B 304
REMARK 465 GLU B 305
REMARK 465 HIS B 306
REMARK 465 HIS B 307
REMARK 465 HIS B 308
REMARK 465 HIS B 309
REMARK 465 HIS B 310
REMARK 465 HIS B 311
REMARK 465 MET C 301
REMARK 465 ALA C 302
REMARK 465 ASP C 303
REMARK 465 ASP C 304
REMARK 465 GLN C 305
REMARK 465 GLY C 306
REMARK 465 CYS C 307
REMARK 465 ILE C 308
REMARK 465 GLU C 309
REMARK 465 GLU C 310
REMARK 465 GLN C 311
REMARK 465 GLY C 312
REMARK 465 VAL C 313
REMARK 465 GLU C 314
REMARK 465 ASP C 315
REMARK 465 SER C 316
REMARK 465 ALA C 317
REMARK 465 ASN C 318
REMARK 465 GLU C 319
REMARK 465 ASP C 320
REMARK 465 SER C 321
REMARK 465 VAL C 322
REMARK 465 ASP C 323
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 C 497
REMARK 465 ASP C 498
REMARK 465 SER D 499
REMARK 465 GLY D 500
REMARK 465 PRO D 501
REMARK 465 ILE D 502
REMARK 465 ASN D 503
REMARK 465 ASP D 504
REMARK 465 THR D 505
REMARK 465 ASP D 506
REMARK 465 ALA D 507
REMARK 465 ASN D 508
REMARK 465 PRO D 509
REMARK 465 ARG D 510
REMARK 465 LEU D 604
REMARK 465 GLU D 605
REMARK 465 HIS D 606
REMARK 465 HIS D 607
REMARK 465 HIS D 608
REMARK 465 HIS D 609
REMARK 465 HIS D 610
REMARK 465 HIS D 611
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 A 87 68.51 -102.27
REMARK 500 CYS A 171 79.44 -153.06
REMARK 500 ARG C 387 68.74 -101.63
REMARK 500 CYS C 471 76.91 -152.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ZVT RELATED DB: PDB
REMARK 900 CASPASE-7 Y230A/W232M/S234N BOUND TO VEID INHIBITOR
REMARK 900 RELATED ID: 4ZVU RELATED DB: PDB
REMARK 900 CASPASE-7 WILD-TYPE BOUND TO TETRAPEPTIDE INHIBITOR AC-VEID-CHO
REMARK 900 RELATED ID: 4ZVQ RELATED DB: PDB
REMARK 900 CASPASE-7 Y230V/W232M/Q276C BOUND TO VEID INHIBITOR
REMARK 900 RELATED ID: 4ZVP RELATED DB: PDB
REMARK 900 CASPASE-7 Y230V/W232M/Q276C BOUND TO DEVD INHIBITOR
REMARK 900 RELATED ID: 4ZVO RELATED DB: PDB
REMARK 900 CASPASE-7 Y230V/W232Y/S234V/Q276D BOUND TO VEID INHIBITOR
REMARK 900 RELATED ID: 4ZVR RELATED DB: PDB
REMARK 900 CASPASE-7 Y230V/W232Y/S234V/Q276D BOUND TO DEVD INHIBITOR
REMARK 900 RELATED ID: 1F1J RELATED DB: PDB
REMARK 900 WILD-TYPE CASPASE-7 BOUND TO DEVD INHIBITOR
REMARK 900 RELATED ID: 3EDR RELATED DB: PDB
REMARK 900 WILD-TYPE CASPASE-7 BOUND TO LDESD INBIBITOR
DBREF 4ZVS A 1 198 UNP P55210 CASP7_HUMAN 1 198
DBREF 4ZVS B 199 303 UNP P55210 CASP7_HUMAN 199 303
DBREF 4ZVS C 301 498 UNP P55210 CASP7_HUMAN 1 198
DBREF 4ZVS D 499 603 UNP P55210 CASP7_HUMAN 199 303
DBREF 4ZVS E 0 4 PDB 4ZVS 4ZVS 0 4
DBREF 4ZVS F 0 4 PDB 4ZVS 4ZVS 0 4
SEQADV 4ZVS ALA B 230 UNP P55210 TYR 230 ENGINEERED MUTATION
SEQADV 4ZVS MET B 232 UNP P55210 TRP 232 ENGINEERED MUTATION
SEQADV 4ZVS ASN B 234 UNP P55210 SER 234 ENGINEERED MUTATION
SEQADV 4ZVS LEU B 304 UNP P55210 EXPRESSION TAG
SEQADV 4ZVS GLU B 305 UNP P55210 EXPRESSION TAG
SEQADV 4ZVS HIS B 306 UNP P55210 EXPRESSION TAG
SEQADV 4ZVS HIS B 307 UNP P55210 EXPRESSION TAG
SEQADV 4ZVS HIS B 308 UNP P55210 EXPRESSION TAG
SEQADV 4ZVS HIS B 309 UNP P55210 EXPRESSION TAG
SEQADV 4ZVS HIS B 310 UNP P55210 EXPRESSION TAG
SEQADV 4ZVS HIS B 311 UNP P55210 EXPRESSION TAG
SEQADV 4ZVS ALA D 530 UNP P55210 TYR 230 ENGINEERED MUTATION
SEQADV 4ZVS MET D 532 UNP P55210 TRP 232 ENGINEERED MUTATION
SEQADV 4ZVS ASN D 534 UNP P55210 SER 234 ENGINEERED MUTATION
SEQADV 4ZVS LEU D 604 UNP P55210 EXPRESSION TAG
SEQADV 4ZVS GLU D 605 UNP P55210 EXPRESSION TAG
SEQADV 4ZVS HIS D 606 UNP P55210 EXPRESSION TAG
SEQADV 4ZVS HIS D 607 UNP P55210 EXPRESSION TAG
SEQADV 4ZVS HIS D 608 UNP P55210 EXPRESSION TAG
SEQADV 4ZVS HIS D 609 UNP P55210 EXPRESSION TAG
SEQADV 4ZVS HIS D 610 UNP P55210 EXPRESSION TAG
SEQADV 4ZVS HIS D 611 UNP P55210 EXPRESSION TAG
SEQRES 1 A 198 MET ALA ASP ASP GLN GLY CYS ILE GLU GLU GLN GLY VAL
SEQRES 2 A 198 GLU ASP SER ALA ASN GLU ASP SER VAL ASP ALA LYS PRO
SEQRES 3 A 198 ASP ARG SER SER PHE VAL PRO SER LEU PHE SER LYS LYS
SEQRES 4 A 198 LYS LYS ASN VAL THR MET ARG SER ILE LYS THR THR ARG
SEQRES 5 A 198 ASP ARG VAL PRO THR TYR GLN TYR ASN MET ASN PHE GLU
SEQRES 6 A 198 LYS LEU GLY LYS CYS ILE ILE ILE ASN ASN LYS ASN PHE
SEQRES 7 A 198 ASP LYS VAL THR GLY MET GLY VAL ARG ASN GLY THR ASP
SEQRES 8 A 198 LYS ASP ALA GLU ALA LEU PHE LYS CYS PHE ARG SER LEU
SEQRES 9 A 198 GLY PHE ASP VAL ILE VAL TYR ASN ASP CYS SER CYS ALA
SEQRES 10 A 198 LYS MET GLN ASP LEU LEU LYS LYS ALA SER GLU GLU ASP
SEQRES 11 A 198 HIS THR ASN ALA ALA CYS PHE ALA CYS ILE LEU LEU SER
SEQRES 12 A 198 HIS GLY GLU GLU ASN VAL ILE TYR GLY LYS ASP GLY VAL
SEQRES 13 A 198 THR PRO ILE LYS ASP LEU THR ALA HIS PHE ARG GLY ASP
SEQRES 14 A 198 ARG CYS LYS THR LEU LEU GLU LYS PRO LYS LEU PHE PHE
SEQRES 15 A 198 ILE GLN ALA CYS ARG GLY THR GLU LEU ASP ASP GLY ILE
SEQRES 16 A 198 GLN ALA ASP
SEQRES 1 B 113 SER GLY PRO ILE ASN ASP THR ASP ALA ASN PRO ARG TYR
SEQRES 2 B 113 LYS ILE PRO VAL GLU ALA ASP PHE LEU PHE ALA TYR SER
SEQRES 3 B 113 THR VAL PRO GLY TYR ALA SER MET ARG ASN PRO GLY ARG
SEQRES 4 B 113 GLY SER TRP PHE VAL GLN ALA LEU CYS SER ILE LEU GLU
SEQRES 5 B 113 GLU HIS GLY LYS ASP LEU GLU ILE MET GLN ILE LEU THR
SEQRES 6 B 113 ARG VAL ASN ASP ARG VAL ALA ARG HIS PHE GLU SER GLN
SEQRES 7 B 113 SER ASP ASP PRO HIS PHE HIS GLU LYS LYS GLN ILE PRO
SEQRES 8 B 113 CYS VAL VAL SER MET LEU THR LYS GLU LEU TYR PHE SER
SEQRES 9 B 113 GLN LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 198 MET ALA ASP ASP GLN GLY CYS ILE GLU GLU GLN GLY VAL
SEQRES 2 C 198 GLU ASP SER ALA ASN GLU ASP SER VAL ASP ALA LYS PRO
SEQRES 3 C 198 ASP ARG SER SER PHE VAL PRO SER LEU PHE SER LYS LYS
SEQRES 4 C 198 LYS LYS ASN VAL THR MET ARG SER ILE LYS THR THR ARG
SEQRES 5 C 198 ASP ARG VAL PRO THR TYR GLN TYR ASN MET ASN PHE GLU
SEQRES 6 C 198 LYS LEU GLY LYS CYS ILE ILE ILE ASN ASN LYS ASN PHE
SEQRES 7 C 198 ASP LYS VAL THR GLY MET GLY VAL ARG ASN GLY THR ASP
SEQRES 8 C 198 LYS ASP ALA GLU ALA LEU PHE LYS CYS PHE ARG SER LEU
SEQRES 9 C 198 GLY PHE ASP VAL ILE VAL TYR ASN ASP CYS SER CYS ALA
SEQRES 10 C 198 LYS MET GLN ASP LEU LEU LYS LYS ALA SER GLU GLU ASP
SEQRES 11 C 198 HIS THR ASN ALA ALA CYS PHE ALA CYS ILE LEU LEU SER
SEQRES 12 C 198 HIS GLY GLU GLU ASN VAL ILE TYR GLY LYS ASP GLY VAL
SEQRES 13 C 198 THR PRO ILE LYS ASP LEU THR ALA HIS PHE ARG GLY ASP
SEQRES 14 C 198 ARG CYS LYS THR LEU LEU GLU LYS PRO LYS LEU PHE PHE
SEQRES 15 C 198 ILE GLN ALA CYS ARG GLY THR GLU LEU ASP ASP GLY ILE
SEQRES 16 C 198 GLN ALA ASP
SEQRES 1 D 113 SER GLY PRO ILE ASN ASP THR ASP ALA ASN PRO ARG TYR
SEQRES 2 D 113 LYS ILE PRO VAL GLU ALA ASP PHE LEU PHE ALA TYR SER
SEQRES 3 D 113 THR VAL PRO GLY TYR ALA SER MET ARG ASN PRO GLY ARG
SEQRES 4 D 113 GLY SER TRP PHE VAL GLN ALA LEU CYS SER ILE LEU GLU
SEQRES 5 D 113 GLU HIS GLY LYS ASP LEU GLU ILE MET GLN ILE LEU THR
SEQRES 6 D 113 ARG VAL ASN ASP ARG VAL ALA ARG HIS PHE GLU SER GLN
SEQRES 7 D 113 SER ASP ASP PRO HIS PHE HIS GLU LYS LYS GLN ILE PRO
SEQRES 8 D 113 CYS VAL VAL SER MET LEU THR LYS GLU LEU TYR PHE SER
SEQRES 9 D 113 GLN LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 E 5 ACE ASP GLU VAL ASJ
SEQRES 1 F 5 ACE ASP GLU VAL ASJ
HET ACE E 0 3
HET ASJ E 4 8
HET ACE F 0 3
HET ASJ F 4 8
HETNAM ACE ACETYL GROUP
HETNAM ASJ (3S)-3-AMINO-4-HYDROXYBUTANOIC ACID
FORMUL 5 ACE 2(C2 H4 O)
FORMUL 5 ASJ 2(C4 H9 N O3)
FORMUL 7 HOH *111(H2 O)
HELIX 1 AA1 ASP A 79 GLY A 83 5 5
HELIX 2 AA2 GLY A 89 GLY A 105 1 17
HELIX 3 AA3 SER A 115 GLU A 129 1 15
HELIX 4 AA4 ILE A 159 ALA A 164 1 6
HELIX 5 AA5 HIS A 165 ARG A 167 5 3
HELIX 6 AA6 CYS A 171 LEU A 175 5 5
HELIX 7 AA7 TRP B 240 GLY B 253 1 14
HELIX 8 AA8 GLU B 257 PHE B 273 1 17
HELIX 9 AA9 ASP B 279 HIS B 283 5 5
HELIX 10 AB1 ASP C 379 GLY C 383 5 5
HELIX 11 AB2 GLY C 389 GLY C 405 1 17
HELIX 12 AB3 SER C 415 GLU C 429 1 15
HELIX 13 AB4 ILE C 459 HIS C 465 1 7
HELIX 14 AB5 CYS C 471 LEU C 475 5 5
HELIX 15 AB6 TRP D 540 GLY D 553 1 14
HELIX 16 AB7 GLU D 557 PHE D 573 1 17
HELIX 17 AB8 ASP D 579 HIS D 583 5 5
SHEET 1 AA112 PHE A 106 ASN A 112 0
SHEET 2 AA112 LYS A 66 ASN A 74 1 N ILE A 72 O TYR A 111
SHEET 3 AA112 ALA A 134 LEU A 142 1 O ILE A 140 N ILE A 71
SHEET 4 AA112 LYS A 179 GLN A 184 1 O PHE A 182 N LEU A 141
SHEET 5 AA112 PHE B 219 TYR B 223 1 O ALA B 222 N PHE A 181
SHEET 6 AA112 CYS B 290 SER B 293 -1 O VAL B 292 N PHE B 221
SHEET 7 AA112 CYS D 590 SER D 593 -1 O VAL D 591 N SER B 293
SHEET 8 AA112 PHE D 519 TYR D 523 -1 N PHE D 521 O VAL D 592
SHEET 9 AA112 LYS C 479 GLN C 484 1 N PHE C 481 O ALA D 522
SHEET 10 AA112 ALA C 434 LEU C 442 1 N LEU C 441 O PHE C 482
SHEET 11 AA112 LYS C 366 ASN C 374 1 N ILE C 371 O ILE C 440
SHEET 12 AA112 PHE C 406 ASN C 412 1 O TYR C 411 N ASN C 374
SHEET 1 AA2 3 GLY A 145 GLU A 146 0
SHEET 2 AA2 3 VAL A 149 TYR A 151 -1 O VAL A 149 N GLU A 146
SHEET 3 AA2 3 VAL A 156 PRO A 158 -1 O THR A 157 N ILE A 150
SHEET 1 AA3 3 GLY B 238 SER B 239 0
SHEET 2 AA3 3 MET B 232 ASN B 234 -1 N ASN B 234 O GLY B 238
SHEET 3 AA3 3 GLU E 2 VAL E 3 -1 O GLU E 2 N ARG B 233
SHEET 1 AA4 3 GLY C 445 GLU C 446 0
SHEET 2 AA4 3 VAL C 449 GLY C 452 -1 O VAL C 449 N GLU C 446
SHEET 3 AA4 3 GLY C 455 PRO C 458 -1 O GLY C 455 N GLY C 452
SHEET 1 AA5 3 GLY D 538 SER D 539 0
SHEET 2 AA5 3 MET D 532 ASN D 534 -1 N ASN D 534 O GLY D 538
SHEET 3 AA5 3 GLU F 2 VAL F 3 -1 O GLU F 2 N ARG D 533
LINK SG CYS A 186 C ASJ E 4 1555 1555 1.80
LINK SG CYS C 486 C ASJ F 4 1555 1555 1.80
LINK C ACE E 0 N ASP E 1 1555 1555 1.33
LINK C VAL E 3 N ASJ E 4 1555 1555 1.33
LINK C ACE F 0 N ASP F 1 1555 1555 1.34
LINK C VAL F 3 N ASJ F 4 1555 1555 1.33
CRYST1 88.105 88.105 187.190 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 0.011350 0.006553 0.000000 0.00000
SCALE2 0.000000 0.013106 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005342 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
