HEADER APOPTOSIS/INHIBITOR 29-OCT-17 6BGR
TITLE CASPASE-3 MUTANT - S150E
CAVEAT 6BGR THE DISTANCE BETWEEN THE S OF CYS 163 AND THE C-TERMINUS OF
CAVEAT 2 6BGR THE INHIBITOR IS TOO LONG FOR COVALENT BOND.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASPASE-3;
COMPND 3 CHAIN: A;
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: CASPASE-3;
COMPND 11 CHAIN: B;
COMPND 12 SYNONYM: CASP-3,APOPAIN,CYSTEINE PROTEASE CPP32,CPP-32,PROTEIN YAMA,
COMPND 13 SREBP CLEAVAGE ACTIVITY 1,SCA-1;
COMPND 14 EC: 3.4.22.56;
COMPND 15 ENGINEERED: YES;
COMPND 16 MOL_ID: 3;
COMPND 17 MOLECULE: AC-ASP-GLU-VAL-ASP-CMK;
COMPND 18 CHAIN: C;
COMPND 19 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 K-12;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: CASP3, CPP32;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 15 MOL_ID: 3;
SOURCE 16 SYNTHETIC: YES;
SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 18 ORGANISM_TAXID: 9606
KEYWDS ALLOSTERIC REGULATION; APOPTOSIS; BIOPHYSICS; CASPASE; COMPUTATIONAL
KEYWDS 2 BIOLOGY; X-RAY CRYSTALLOGRAPHY; FLUORESCENCE; MOLECULAR DYNAMICS;
KEYWDS 3 PROTEIN EVOLUTION, APOPTOSIS, APOPTOSIS-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.E.THOMAS,R.GRINSHPON,P.D.SWARTZ,A.C.CLARK
REVDAT 2 25-APR-18 6BGR 1 JRNL
REVDAT 1 21-FEB-18 6BGR 0
JRNL AUTH M.E.THOMAS,R.GRINSHPON,P.SWARTZ,A.C.CLARK
JRNL TITL MODIFICATIONS TO A COMMON PHOSPHORYLATION NETWORK PROVIDE
JRNL TITL 2 INDIVIDUALIZED CONTROL IN CASPASES.
JRNL REF J. BIOL. CHEM. V. 293 5447 2018
JRNL REFN ESSN 1083-351X
JRNL PMID 29414778
JRNL DOI 10.1074/JBC.RA117.000728
REMARK 2
REMARK 2 RESOLUTION. 2.16 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.12_2829: ???)
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) : 2.16
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.10
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 15158
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1516
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 34.1072 - 4.7989 1.00 1339 149 0.1696 0.2058
REMARK 3 2 4.7989 - 3.8107 1.00 1268 141 0.1314 0.1782
REMARK 3 3 3.8107 - 3.3294 1.00 1269 141 0.1547 0.2254
REMARK 3 4 3.3294 - 3.0252 1.00 1230 137 0.1930 0.2363
REMARK 3 5 3.0252 - 2.8085 1.00 1260 140 0.1923 0.2647
REMARK 3 6 2.8085 - 2.6430 1.00 1244 137 0.2097 0.2988
REMARK 3 7 2.6430 - 2.5107 1.00 1237 138 0.1993 0.2743
REMARK 3 8 2.5107 - 2.4014 1.00 1236 138 0.1951 0.2687
REMARK 3 9 2.4014 - 2.3090 1.00 1228 136 0.1951 0.3001
REMARK 3 10 2.3090 - 2.2293 0.99 1241 138 0.2034 0.2523
REMARK 3 11 2.2293 - 2.1596 0.88 1090 121 0.2076 0.2847
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) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.840
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 : 0.008 2014
REMARK 3 ANGLE : 1.185 2709
REMARK 3 CHIRALITY : 0.113 293
REMARK 3 PLANARITY : 0.005 349
REMARK 3 DIHEDRAL : 4.410 2530
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: AUTHORS INDICATE THAT IS NOT POSSIBLE
REMARK 3 TO DEFINE THE COVALENT BOND BETWEEN THE CYSTEINE SULFUR ATOM AND
REMARK 3 THE CARBON ATOM OF THE INHIBITOR IN PHENIX.
REMARK 4
REMARK 4 6BGR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-OCT-17.
REMARK 100 THE DEPOSITION ID IS D_1000230862.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15158
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.160
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 (%) : 98.8
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.4000
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: NULL
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 (%): 42.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE OBTAINED AT 18 C BY THE
REMARK 280 HANGING DROP VAPOR DIFFUSION METHOD USING 4 ML DROPS THAT
REMARK 280 CONTAINED EQUAL VOLUMES OF PROTEIN AND RESERVOIR SOLUTIONS OVER
REMARK 280 A 0.5 ML SOLUTION OF 100 MM SODIUM CITRATE, PH 4.9-5.2, 8-18 %
REMARK 280 PEG 6000 (W/V), 10 MM DTT, AND 3 MM NAN3. CRYSTALS APPEARED
REMARK 280 WITHIN 3-5 DAYS AND WERE BRIEFLY IMMERSED IN A CRYOGENIC
REMARK 280 SOLUTION CONTAINING 10% MPD (2-METHYLPENTANE-2,4-DIOL) AND 90%
REMARK 280 RESERVOIR SOLUTION., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 34.10300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.22600
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 48.26600
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 34.10300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.22600
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 48.26600
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 34.10300
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 42.22600
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 48.26600
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 34.10300
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 42.22600
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 48.26600
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 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 A 469 LIES ON A SPECIAL POSITION.
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: C
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 ASP A 175
REMARK 465 SER B 176
REMARK 465 GLY B 177
REMARK 465 VAL B 178
REMARK 465 ASP B 179
REMARK 465 ASP B 180
REMARK 465 ASP B 181
REMARK 465 MET B 182
REMARK 465 ALA B 183
REMARK 465 CYS B 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 ILE A 31 CG1 CG2 CD1
REMARK 470 ASP A 34 CG OD1 OD2
REMARK 470 LYS A 57 CG CD CE NZ
REMARK 470 LYS A 88 CE NZ
REMARK 470 LYS A 105 CE NZ
REMARK 470 GLU A 173 CG CD OE1 OE2
REMARK 470 LYS B 224 CD CE NZ
REMARK 470 LYS B 229 CG CD CE NZ
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 SG CYS A 163 C ASP C 5 1.46
REMARK 500 N CYS A 163 C1 0QE C 6 1.95
REMARK 500 NH1 ARG A 75 O HOH A 401 1.99
REMARK 500 CB CYS A 163 O ASP C 5 2.07
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 ASP C 5 CB - CG - OD2 ANGL. DEV. = 9.6 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 34 50.88 -109.18
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 AZI A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AZI A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AZI A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AZI B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ac-Asp-Glu-Val-Asp-CMK chain C
DBREF 6BGR A 1 175 UNP P42574 CASP3_HUMAN 1 175
DBREF 6BGR B 176 277 UNP P42574 CASP3_HUMAN 176 277
DBREF 6BGR C 1 6 PDB 6BGR 6BGR 1 6
SEQADV 6BGR GLU A 150 UNP P42574 SER 150 ENGINEERED MUTATION
SEQRES 1 A 175 MET GLU ASN THR GLU ASN SER VAL ASP SER LYS SER ILE
SEQRES 2 A 175 LYS ASN LEU GLU PRO LYS ILE ILE HIS GLY SER GLU SER
SEQRES 3 A 175 MET ASP SER GLY ILE SER LEU ASP ASN SER TYR LYS MET
SEQRES 4 A 175 ASP TYR PRO GLU MET GLY LEU CYS ILE ILE ILE ASN ASN
SEQRES 5 A 175 LYS ASN PHE HIS LYS SER THR GLY MET THR SER ARG SER
SEQRES 6 A 175 GLY THR ASP VAL ASP ALA ALA ASN LEU ARG GLU THR PHE
SEQRES 7 A 175 ARG ASN LEU LYS TYR GLU VAL ARG ASN LYS ASN ASP LEU
SEQRES 8 A 175 THR ARG GLU GLU ILE VAL GLU LEU MET ARG ASP VAL SER
SEQRES 9 A 175 LYS GLU ASP HIS SER LYS ARG SER SER PHE VAL CYS VAL
SEQRES 10 A 175 LEU LEU SER HIS GLY GLU GLU GLY ILE ILE PHE GLY THR
SEQRES 11 A 175 ASN GLY PRO VAL ASP LEU LYS LYS ILE THR ASN PHE PHE
SEQRES 12 A 175 ARG GLY ASP ARG CYS ARG GLU LEU THR GLY LYS PRO LYS
SEQRES 13 A 175 LEU PHE ILE ILE GLN ALA CYS ARG GLY THR GLU LEU ASP
SEQRES 14 A 175 CYS GLY ILE GLU THR ASP
SEQRES 1 B 102 SER GLY VAL ASP ASP ASP MET ALA CYS HIS LYS ILE PRO
SEQRES 2 B 102 VAL GLU ALA ASP PHE LEU TYR ALA TYR SER THR ALA PRO
SEQRES 3 B 102 GLY TYR TYR SER TRP ARG ASN SER LYS ASP GLY SER TRP
SEQRES 4 B 102 PHE ILE GLN SER LEU CYS ALA MET LEU LYS GLN TYR ALA
SEQRES 5 B 102 ASP LYS LEU GLU PHE MET HIS ILE LEU THR ARG VAL ASN
SEQRES 6 B 102 ARG LYS VAL ALA THR GLU PHE GLU SER PHE SER PHE ASP
SEQRES 7 B 102 ALA THR PHE HIS ALA LYS LYS GLN ILE PRO CYS ILE VAL
SEQRES 8 B 102 SER MET LEU THR LYS GLU LEU TYR PHE TYR HIS
SEQRES 1 C 6 ACE ASP GLU VAL ASP 0QE
HET ACE C 1 3
HET 0QE C 6 1
HET AZI A 301 3
HET AZI A 302 3
HET AZI A 303 3
HET AZI B 301 3
HETNAM ACE ACETYL GROUP
HETNAM 0QE CHLOROMETHANE
HETNAM AZI AZIDE ION
HETSYN 0QE CHLORO METHYL GROUP
FORMUL 3 ACE C2 H4 O
FORMUL 3 0QE C H3 CL
FORMUL 4 AZI 4(N3 1-)
FORMUL 8 HOH *132(H2 O)
HELIX 1 AA1 HIS A 56 GLY A 60 5 5
HELIX 2 AA2 GLY A 66 LEU A 81 1 16
HELIX 3 AA3 THR A 92 GLU A 106 1 15
HELIX 4 AA4 LEU A 136 PHE A 142 1 7
HELIX 5 AA5 CYS A 148 THR A 152 5 5
HELIX 6 AA6 TRP B 214 ALA B 227 1 14
HELIX 7 AA7 GLU B 231 PHE B 247 1 17
HELIX 8 AA8 ASP B 253 HIS B 257 5 5
SHEET 1 AA1 6 GLU A 84 ASN A 89 0
SHEET 2 AA1 6 LEU A 46 ASN A 51 1 N ASN A 51 O LYS A 88
SHEET 3 AA1 6 PHE A 114 LEU A 119 1 O VAL A 117 N ILE A 48
SHEET 4 AA1 6 LYS A 156 GLN A 161 1 O LEU A 157 N PHE A 114
SHEET 5 AA1 6 PHE B 193 TYR B 197 1 O LEU B 194 N PHE A 158
SHEET 6 AA1 6 CYS B 264 SER B 267 -1 O VAL B 266 N TYR B 195
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 GLY A 165 GLU A 167 0
SHEET 2 AA3 2 GLY B 202 TYR B 203 1 O GLY B 202 N GLU A 167
SHEET 1 AA4 3 GLY B 212 SER B 213 0
SHEET 2 AA4 3 TRP B 206 ASN B 208 -1 N ASN B 208 O GLY B 212
SHEET 3 AA4 3 GLU C 3 VAL C 4 -1 O GLU C 3 N ARG B 207
LINK SG CYS A 163 O ASP C 5 1555 1555 1.57
LINK C ACE C 1 N ASP C 2 1555 1555 1.32
LINK C ASP C 5 C1 0QE C 6 1555 1555 1.60
SITE 1 AC1 6 LYS A 38 SER A 112 GLY A 153 LYS A 154
SITE 2 AC1 6 PRO A 155 HOH A 418
SITE 1 AC2 4 GLU A 123 GLU A 124 ARG A 164 GLY A 165
SITE 1 AC3 2 THR A 92 GLU A 94
SITE 1 AC4 3 ALA B 221 GLN B 225 HOH B 431
SITE 1 AC5 16 SER A 58 ARG A 64 HIS A 121 GLN A 161
SITE 2 AC5 16 ALA A 162 CYS A 163 SER B 205 TRP B 206
SITE 3 AC5 16 ARG B 207 ASN B 208 SER B 209 TRP B 214
SITE 4 AC5 16 SER B 249 PHE B 250 HOH C 101 HOH C 102
CRYST1 68.206 84.452 96.532 90.00 90.00 90.00 I 2 2 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 0.014661 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011841 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010359 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
