HEADER HYDROLASE/HYDROLASE INHIBITOR 03-SEP-08 3EDR
TITLE THE CRYSTAL STRUCTURE OF CASPASE-7 IN COMPLEX WITH ACETYL-LDESD-CHO
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASPASE-7;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: P20 SUBUNIT (UNP RESIDUES 24 TO 196);
COMPND 5 SYNONYM: CASP-7, ICE-LIKE APOPTOTIC PROTEASE 3, ICE-LAP3, APOPTOTIC
COMPND 6 PROTEASE MCH-3, CMH-1, CASPASE-7 SUBUNIT P20, CASPASE-7 SUBUNIT P11;
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 (UNP RESIDUES 207 TO 303);
COMPND 13 SYNONYM: CASP-7, ICE-LIKE APOPTOTIC PROTEASE 3, ICE-LAP3, APOPTOTIC
COMPND 14 PROTEASE MCH-3, CMH-1, CASPASE-7 SUBUNIT P20, CASPASE-7 SUBUNIT P11;
COMPND 15 EC: 3.4.22.60;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 3;
COMPND 18 MOLECULE: INHIBITOR AC-LDESD-CHO PEPTIDE;
COMPND 19 CHAIN: E, F;
COMPND 20 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;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
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;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
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 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST);
SOURCE 24 ORGANISM_TAXID: 559292;
SOURCE 25 OTHER_DETAILS: THE PEPTIDE WAS OBTAINED FROM EMD CHEMICALS, INC.,
SOURCE 26 NJ.
KEYWDS CASPASE, PEPTIDE INHIBITOR, APOPTOSIS, THIOL PROTEASE, HYDROLASE-
KEYWDS 2 HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.AGNISWAMY
REVDAT 5 15-NOV-23 3EDR 1 REMARK
REVDAT 4 30-AUG-23 3EDR 1 LINK
REVDAT 3 13-JUL-11 3EDR 1 VERSN
REVDAT 2 24-FEB-09 3EDR 1 VERSN
REVDAT 1 28-OCT-08 3EDR 0
JRNL AUTH G.FU,A.A.CHUMANEVICH,J.AGNISWAMY,B.FANG,R.W.HARRISON,
JRNL AUTH 2 I.T.WEBER
JRNL TITL STRUCTURAL BASIS FOR EXECUTIONER CASPASE RECOGNITION OF P5
JRNL TITL 2 POSITION IN SUBSTRATES.
JRNL REF APOPTOSIS V. 13 1291 2008
JRNL REFN ISSN 1360-8185
JRNL PMID 18780184
JRNL DOI 10.1007/S10495-008-0259-9
REMARK 2
REMARK 2 RESOLUTION. 2.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 2.45
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) (%) : 89.3
REMARK 3 NUMBER OF REFLECTIONS : 25635
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 SET) : 0.201
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1273
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 : 3861
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 82
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) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.400
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 3EDR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-SEP-08.
REMARK 100 THE DEPOSITION ID IS D_1000049195.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUN-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
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 : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28712
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.450
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 (%) : 90.3
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : 0.09500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.5200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 57.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.38900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.890
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 (%): 63.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.1M SODIUM FORMATE,0.1M SODIUM
REMARK 280 CITRATE, PH 5.5, VAPOR DIFFUSION, HANGING DROP, 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 125.13867
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 62.56933
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 62.56933
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 125.13867
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: 16850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.0 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 THE INHIBITOR IS COVALENTLY CONNECTED TO CYS OF THE ENZYME TO FORM
REMARK 400 A HEMITHIOKETAL
REMARK 400
REMARK 400 THE N-ACETYL-L-LEUCYL-L-ALPHA-ASPARTYL-L-ALPHA-GLUTAMYL-L-SERYL-L-
REMARK 400 ASPARTIC ALDEHYDE IS PEPTIDE-LIKE, A MEMBER OF INHIBITOR CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: N-ACETYL-L-LEUCYL-L-ALPHA-ASPARTYL-L-ALPHA-GLUTAMYL-L-SERYL-
REMARK 400 L-ASPARTIC 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 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 B 207
REMARK 465 ASN B 208
REMARK 465 PRO B 209
REMARK 465 ARG B 210
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 ALA D 507
REMARK 465 ASN D 508
REMARK 465 PRO D 509
REMARK 465 ARG D 510
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 LYS B 212 N - CA - C ANGL. DEV. = 16.9 DEGREES
REMARK 500 PRO C 356 N - CA - C ANGL. DEV. = 16.5 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 ASP A 113 72.31 30.07
REMARK 500 SER A 143 -171.25 179.33
REMARK 500 ASN A 148 -5.87 73.58
REMARK 500 CYS A 171 79.43 -164.79
REMARK 500 GLU B 274 108.63 -165.79
REMARK 500 PHE B 301 38.90 -91.64
REMARK 500 PRO C 356 -81.84 -38.05
REMARK 500 SER C 443 -166.89 -168.90
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 CHAIN E OF INHIBITOR AC-LDESD
REMARK 800 -CHO PEPTIDE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN F OF INHIBITOR AC-LDESD
REMARK 800 -CHO PEPTIDE
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3EDQ RELATED DB: PDB
DBREF 3EDR A 24 196 UNP P55210 CASP7_HUMAN 24 196
DBREF 3EDR B 207 303 UNP P55210 CASP7_HUMAN 207 303
DBREF 3EDR C 324 496 UNP P55210 CASP7_HUMAN 24 196
DBREF 3EDR D 507 603 UNP P55210 CASP7_HUMAN 207 303
DBREF 3EDR E 701 706 PDB 3EDR 3EDR 701 706
DBREF 3EDR F 801 806 PDB 3EDR 3EDR 801 806
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 6 ACE LEU ASP GLU SER ASJ
SEQRES 1 F 6 ACE LEU ASP GLU SER ASJ
HET ACE E 701 3
HET ASJ E 706 8
HET ACE F 801 3
HET ASJ F 806 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 *82(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 HIS A 165 1 7
HELIX 5 5 PHE A 166 LEU A 175 5 10
HELIX 6 6 TRP B 240 GLY B 253 1 14
HELIX 7 7 GLU B 257 PHE B 273 1 17
HELIX 8 8 VAL C 355 GLN C 359 5 5
HELIX 9 9 ASP C 379 GLY C 383 5 5
HELIX 10 10 GLY C 389 GLY C 405 1 17
HELIX 11 11 SER C 415 SER C 427 1 13
HELIX 12 12 ILE C 459 ALA C 464 1 6
HELIX 13 13 HIS C 465 ARG C 467 5 3
HELIX 14 14 CYS C 471 LEU C 475 5 5
HELIX 15 15 TRP D 540 GLY D 553 1 14
HELIX 16 16 GLU D 557 PHE D 573 1 17
SHEET 1 A12 PHE A 106 ASN A 112 0
SHEET 2 A12 GLY A 68 ASN A 74 1 N GLY A 68 O ASP A 107
SHEET 3 A12 PHE A 137 LEU A 142 1 O ILE A 140 N ILE A 71
SHEET 4 A12 LYS A 179 GLN A 184 1 O GLN A 184 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 VAL D 591 N SER B 293
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 PHE C 481 O ALA D 522
SHEET 10 A12 PHE C 437 LEU C 442 1 N LEU C 441 O GLN C 484
SHEET 11 A12 LYS C 369 ASN C 374 1 N ILE C 371 O ILE C 440
SHEET 12 A12 ASP C 407 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 GLY A 152 -1 O VAL A 149 N GLU A 146
SHEET 3 B 3 GLY A 155 PRO A 158 -1 O GLY A 155 N GLY A 152
SHEET 1 C 2 GLY A 188 GLU A 190 0
SHEET 2 C 2 GLY B 228 TYR B 229 1 O GLY B 228 N GLU A 190
SHEET 1 D 3 GLY B 238 SER B 239 0
SHEET 2 D 3 TRP B 232 SER B 234 -1 N SER B 234 O GLY B 238
SHEET 3 D 3 GLU E 704 SER E 705 -1 O GLU E 704 N ARG B 233
SHEET 1 E 3 GLY C 445 GLU C 446 0
SHEET 2 E 3 VAL C 449 TYR C 451 -1 O VAL C 449 N GLU C 446
SHEET 3 E 3 VAL C 456 PRO C 458 -1 O THR C 457 N ILE C 450
SHEET 1 F 3 GLY D 538 SER D 539 0
SHEET 2 F 3 TRP D 532 SER D 534 -1 N SER D 534 O GLY D 538
SHEET 3 F 3 GLU F 804 SER F 805 -1 O GLU F 804 N ARG D 533
LINK SG CYS A 186 C ASJ E 706 1555 1555 1.78
LINK SG CYS C 486 C ASJ F 806 1555 1555 1.78
LINK C ACE E 701 N LEU E 702 1555 1555 1.39
LINK C SER E 705 N ASJ E 706 1555 1555 1.34
LINK C ACE F 801 N LEU F 802 1555 1555 1.39
LINK C SER F 805 N ASJ F 806 1555 1555 1.33
SITE 1 AC1 14 ARG A 87 HIS A 144 GLY A 145 GLN A 184
SITE 2 AC1 14 CYS A 186 TYR B 230 SER B 231 TRP B 232
SITE 3 AC1 14 ARG B 233 SER B 234 PRO B 235 SER B 275
SITE 4 AC1 14 GLN B 276 ASP B 278
SITE 1 AC2 18 ARG C 387 HIS C 444 GLY C 445 GLN C 484
SITE 2 AC2 18 CYS C 486 TYR D 530 SER D 531 TRP D 532
SITE 3 AC2 18 ARG D 533 SER D 534 PRO D 535 TRP D 540
SITE 4 AC2 18 SER D 575 GLN D 576 SER D 577 ASP D 578
SITE 5 AC2 18 HOH F 16 HOH F 81
CRYST1 88.637 88.637 187.708 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 0.011282 0.006514 0.000000 0.00000
SCALE2 0.000000 0.013027 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005327 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
