HEADER HYDROLASE/HYDROLASE INHIBITOR 11-OCT-13 4N6G
TITLE TAILORING SMALL MOLECULES FOR AN ALLOSTERIC SITE ON PROCASPASE-6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASPASE-6;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 24-293;
COMPND 5 SYNONYM: CASP-6, APOPTOTIC PROTEASE MCH-2, CASPASE-6 SUBUNIT P18,
COMPND 6 CASPASE-6 SUBUNIT P11;
COMPND 7 EC: 3.4.22.59;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CASP6, MCH2, PROCASPASE-6;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS PROCASPSE-6, CASPASE-6 ZYMOGEN, ALLOSTERIC, STRUCTURE BASED DRUG
KEYWDS 2 DESIGN, CYSTEINE PROTEASE, HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR
KEYWDS 3 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.MURRAY,M.STEFFEK
REVDAT 4 28-FEB-24 4N6G 1 REMARK SEQADV
REVDAT 3 24-JAN-18 4N6G 1 AUTHOR
REVDAT 2 22-JAN-14 4N6G 1 JRNL
REVDAT 1 01-JAN-14 4N6G 0
JRNL AUTH J.MURRAY,A.M.GIANNETTI,M.STEFFEK,P.GIBBONS,B.R.HEARN,
JRNL AUTH 2 F.COHEN,C.TAM,C.POZNIAK,B.BRAVO,J.LEWCOCK,P.JAISHANKAR,
JRNL AUTH 3 C.Q.LY,X.ZHAO,Y.TANG,P.CHUGHA,M.R.ARKIN,J.FLYGARE,A.R.RENSLO
JRNL TITL TAILORING SMALL MOLECULES FOR AN ALLOSTERIC SITE ON
JRNL TITL 2 PROCASPASE-6.
JRNL REF CHEMMEDCHEM V. 9 73 2014
JRNL REFN ISSN 1860-7179
JRNL PMID 24259468
JRNL DOI 10.1002/CMDC.201300424
REMARK 2
REMARK 2 RESOLUTION. 2.14 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1492
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) : 2.14
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 82.08
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.430
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 30564
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.140
REMARK 3 FREE R VALUE TEST SET COUNT : 1570
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 82.1436 - 4.7562 1.00 2854 131 0.1870 0.1980
REMARK 3 2 4.7562 - 3.7752 1.00 2700 137 0.1438 0.1581
REMARK 3 3 3.7752 - 3.2979 1.00 2654 145 0.1590 0.2152
REMARK 3 4 3.2979 - 2.9964 1.00 2631 153 0.1842 0.2467
REMARK 3 5 2.9964 - 2.7816 1.00 2615 151 0.1848 0.2315
REMARK 3 6 2.7816 - 2.6176 1.00 2607 142 0.2046 0.2578
REMARK 3 7 2.6176 - 2.4865 1.00 2594 135 0.1956 0.2261
REMARK 3 8 2.4865 - 2.3783 1.00 2582 156 0.1909 0.2334
REMARK 3 9 2.3783 - 2.2867 1.00 2606 134 0.2028 0.2388
REMARK 3 10 2.2867 - 2.2078 1.00 2590 141 0.2115 0.2621
REMARK 3 11 2.2078 - 2.1387 0.99 2561 145 0.2228 0.3034
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) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.380
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.01
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 : 0.013 4107
REMARK 3 ANGLE : 1.382 5540
REMARK 3 CHIRALITY : 0.064 593
REMARK 3 PLANARITY : 0.008 722
REMARK 3 DIHEDRAL : 13.473 1495
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): 17.4123 23.3701 -19.3325
REMARK 3 T TENSOR
REMARK 3 T11: 0.2028 T22: 0.1697
REMARK 3 T33: 0.1455 T12: 0.0133
REMARK 3 T13: -0.0472 T23: -0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 2.7412 L22: 3.6407
REMARK 3 L33: 2.4724 L12: -0.4036
REMARK 3 L13: -0.9550 L23: 0.4505
REMARK 3 S TENSOR
REMARK 3 S11: -0.0232 S12: -0.0010 S13: 0.0757
REMARK 3 S21: 0.1199 S22: -0.0207 S23: 0.2348
REMARK 3 S31: -0.1685 S32: -0.1558 S33: 0.0486
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): 44.4974 26.5204 -14.5834
REMARK 3 T TENSOR
REMARK 3 T11: 0.1038 T22: 0.2404
REMARK 3 T33: 0.2173 T12: -0.0048
REMARK 3 T13: 0.0260 T23: -0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 3.2106 L22: 3.3913
REMARK 3 L33: 3.0972 L12: 0.5040
REMARK 3 L13: 0.6921 L23: 0.2691
REMARK 3 S TENSOR
REMARK 3 S11: -0.0989 S12: 0.1238 S13: 0.0763
REMARK 3 S21: -0.1255 S22: 0.0983 S23: -0.2842
REMARK 3 S31: -0.0618 S32: 0.3001 S33: 0.0048
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 4N6G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-OCT-13.
REMARK 100 THE DEPOSITION ID IS D_1000082811.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-APR-10
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 : ALS
REMARK 200 BEAMLINE : 5.0.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97946
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.20, XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30628
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.142
REMARK 200 RESOLUTION RANGE LOW (A) : 116.215
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.14
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.70
REMARK 200 R MERGE FOR SHELL (I) : 0.55100
REMARK 200 R SYM FOR SHELL (I) : 0.55100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2-METHYL-2,4-PENTANEDIOL, 0.3 M
REMARK 280 AMMONIUM PHOSPHATE MONOBASIC, 0.1 M TRIS, PH 8.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 39.76300
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 58.04150
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 58.04150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 59.64450
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 58.04150
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 58.04150
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 19.88150
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 58.04150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 58.04150
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 59.64450
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 58.04150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 58.04150
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 19.88150
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 39.76300
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 B 534 LIES ON A SPECIAL POSITION.
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 21
REMARK 465 GLY A 22
REMARK 465 SER A 23
REMARK 465 ALA A 24
REMARK 465 LEU A 175
REMARK 465 ASP A 176
REMARK 465 VAL A 177
REMARK 465 VAL A 178
REMARK 465 ASP A 179
REMARK 465 ASN A 180
REMARK 465 GLN A 181
REMARK 465 THR A 182
REMARK 465 GLU A 183
REMARK 465 LYS A 184
REMARK 465 LEU A 185
REMARK 465 ASN A 293
REMARK 465 GLY A 294
REMARK 465 ASN A 295
REMARK 465 SER A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 465 HIS A 300
REMARK 465 HIS A 301
REMARK 465 HIS A 302
REMARK 465 MET B 21
REMARK 465 GLY B 22
REMARK 465 SER B 23
REMARK 465 ALA B 24
REMARK 465 PHE B 25
REMARK 465 TYR B 26
REMARK 465 LYS B 27
REMARK 465 ARG B 28
REMARK 465 GLU B 29
REMARK 465 HIS B 168
REMARK 465 ASP B 169
REMARK 465 VAL B 170
REMARK 465 PRO B 171
REMARK 465 VAL B 172
REMARK 465 ILE B 173
REMARK 465 PRO B 174
REMARK 465 LEU B 175
REMARK 465 ASP B 176
REMARK 465 VAL B 177
REMARK 465 VAL B 178
REMARK 465 ASP B 179
REMARK 465 ASN B 180
REMARK 465 GLN B 181
REMARK 465 THR B 182
REMARK 465 GLU B 183
REMARK 465 LYS B 184
REMARK 465 LEU B 185
REMARK 465 ASP B 186
REMARK 465 SER B 292
REMARK 465 ASN B 293
REMARK 465 GLY B 294
REMARK 465 ASN B 295
REMARK 465 SER B 296
REMARK 465 HIS B 297
REMARK 465 HIS B 298
REMARK 465 HIS B 299
REMARK 465 HIS B 300
REMARK 465 HIS B 301
REMARK 465 HIS B 302
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 PHE A 25 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE A 173 CG1 CG2 CD1
REMARK 470 ASP A 186 CG OD1 OD2
REMARK 470 THR A 187 OG1 CG2
REMARK 470 ARG A 260 CG CD NE CZ NH1 NH2
REMARK 470 CYS A 264 SG
REMARK 470 LYS A 265 CG CD CE NZ
REMARK 470 ASP A 266 CG OD1 OD2
REMARK 470 ILE A 270 CG1 CG2 CD1
REMARK 470 MET B 30 CG SD CE
REMARK 470 THR B 187 OG1 CG2
REMARK 470 ARG B 260 CG CD NE CZ NH1 NH2
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 PHE A 263 O LYS A 265 2.19
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 ARG A 44 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 44 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 CYS A 264 N - CA - C ANGL. DEV. = -16.8 DEGREES
REMARK 500 PRO A 267 CA - N - CD ANGL. DEV. = -9.4 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 GLU A 29 -69.45 -132.80
REMARK 500 SER A 120 -166.68 -165.62
REMARK 500 GLN A 167 52.01 -101.35
REMARK 500 HIS A 168 49.08 -96.30
REMARK 500 SER A 196 -22.67 -142.88
REMARK 500 SER A 242 -36.23 -132.76
REMARK 500 LYS A 265 -179.31 95.49
REMARK 500 MET B 39 43.48 -109.36
REMARK 500 ARG B 64 64.33 -119.87
REMARK 500 SER B 120 -166.71 -165.02
REMARK 500 SER B 196 -24.19 -144.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 CYS A 264 LYS A 265 -134.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 2GQ B 401
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2GQ B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4N5D RELATED DB: PDB
REMARK 900 RELATED ID: 4N7J RELATED DB: PDB
REMARK 900 RELATED ID: 4N7M RELATED DB: PDB
REMARK 900 RELATED ID: 4NBK RELATED DB: PDB
REMARK 900 RELATED ID: 4NBL RELATED DB: PDB
REMARK 900 RELATED ID: 4NBN RELATED DB: PDB
DBREF 4N6G A 24 293 UNP P55212 CASP6_HUMAN 24 293
DBREF 4N6G B 24 293 UNP P55212 CASP6_HUMAN 24 293
SEQADV 4N6G MET A 21 UNP P55212 INITIATING METHIONINE
SEQADV 4N6G GLY A 22 UNP P55212 EXPRESSION TAG
SEQADV 4N6G SER A 23 UNP P55212 EXPRESSION TAG
SEQADV 4N6G ALA A 163 UNP P55212 CYS 163 ENGINEERED MUTATION
SEQADV 4N6G GLY A 294 UNP P55212 EXPRESSION TAG
SEQADV 4N6G ASN A 295 UNP P55212 EXPRESSION TAG
SEQADV 4N6G SER A 296 UNP P55212 EXPRESSION TAG
SEQADV 4N6G HIS A 297 UNP P55212 EXPRESSION TAG
SEQADV 4N6G HIS A 298 UNP P55212 EXPRESSION TAG
SEQADV 4N6G HIS A 299 UNP P55212 EXPRESSION TAG
SEQADV 4N6G HIS A 300 UNP P55212 EXPRESSION TAG
SEQADV 4N6G HIS A 301 UNP P55212 EXPRESSION TAG
SEQADV 4N6G HIS A 302 UNP P55212 EXPRESSION TAG
SEQADV 4N6G MET B 21 UNP P55212 INITIATING METHIONINE
SEQADV 4N6G GLY B 22 UNP P55212 EXPRESSION TAG
SEQADV 4N6G SER B 23 UNP P55212 EXPRESSION TAG
SEQADV 4N6G ALA B 163 UNP P55212 CYS 163 ENGINEERED MUTATION
SEQADV 4N6G GLY B 294 UNP P55212 EXPRESSION TAG
SEQADV 4N6G ASN B 295 UNP P55212 EXPRESSION TAG
SEQADV 4N6G SER B 296 UNP P55212 EXPRESSION TAG
SEQADV 4N6G HIS B 297 UNP P55212 EXPRESSION TAG
SEQADV 4N6G HIS B 298 UNP P55212 EXPRESSION TAG
SEQADV 4N6G HIS B 299 UNP P55212 EXPRESSION TAG
SEQADV 4N6G HIS B 300 UNP P55212 EXPRESSION TAG
SEQADV 4N6G HIS B 301 UNP P55212 EXPRESSION TAG
SEQADV 4N6G HIS B 302 UNP P55212 EXPRESSION TAG
SEQRES 1 A 282 MET GLY SER ALA PHE TYR LYS ARG GLU MET PHE ASP PRO
SEQRES 2 A 282 ALA GLU LYS TYR LYS MET ASP HIS ARG ARG ARG GLY ILE
SEQRES 3 A 282 ALA LEU ILE PHE ASN HIS GLU ARG PHE PHE TRP HIS LEU
SEQRES 4 A 282 THR LEU PRO GLU ARG ARG GLY THR CYS ALA ASP ARG ASP
SEQRES 5 A 282 ASN LEU THR ARG ARG PHE SER ASP LEU GLY PHE GLU VAL
SEQRES 6 A 282 LYS CYS PHE ASN ASP LEU LYS ALA GLU GLU LEU LEU LEU
SEQRES 7 A 282 LYS ILE HIS GLU VAL SER THR VAL SER HIS ALA ASP ALA
SEQRES 8 A 282 ASP CYS PHE VAL CYS VAL PHE LEU SER HIS GLY GLU GLY
SEQRES 9 A 282 ASN HIS ILE TYR ALA TYR ASP ALA LYS ILE GLU ILE GLN
SEQRES 10 A 282 THR LEU THR GLY LEU PHE LYS GLY ASP LYS CYS HIS SER
SEQRES 11 A 282 LEU VAL GLY LYS PRO LYS ILE PHE ILE ILE GLN ALA ALA
SEQRES 12 A 282 ARG GLY ASN GLN HIS ASP VAL PRO VAL ILE PRO LEU ASP
SEQRES 13 A 282 VAL VAL ASP ASN GLN THR GLU LYS LEU ASP THR ASN ILE
SEQRES 14 A 282 THR GLU VAL ASP ALA ALA SER VAL TYR THR LEU PRO ALA
SEQRES 15 A 282 GLY ALA ASP PHE LEU MET CYS TYR SER VAL ALA GLU GLY
SEQRES 16 A 282 TYR TYR SER HIS ARG GLU THR VAL ASN GLY SER TRP TYR
SEQRES 17 A 282 ILE GLN ASP LEU CYS GLU MET LEU GLY LYS TYR GLY SER
SEQRES 18 A 282 SER LEU GLU PHE THR GLU LEU LEU THR LEU VAL ASN ARG
SEQRES 19 A 282 LYS VAL SER GLN ARG ARG VAL ASP PHE CYS LYS ASP PRO
SEQRES 20 A 282 SER ALA ILE GLY LYS LYS GLN VAL PRO CYS PHE ALA SER
SEQRES 21 A 282 MET LEU THR LYS LYS LEU HIS PHE PHE PRO LYS SER ASN
SEQRES 22 A 282 GLY ASN SER HIS HIS HIS HIS HIS HIS
SEQRES 1 B 282 MET GLY SER ALA PHE TYR LYS ARG GLU MET PHE ASP PRO
SEQRES 2 B 282 ALA GLU LYS TYR LYS MET ASP HIS ARG ARG ARG GLY ILE
SEQRES 3 B 282 ALA LEU ILE PHE ASN HIS GLU ARG PHE PHE TRP HIS LEU
SEQRES 4 B 282 THR LEU PRO GLU ARG ARG GLY THR CYS ALA ASP ARG ASP
SEQRES 5 B 282 ASN LEU THR ARG ARG PHE SER ASP LEU GLY PHE GLU VAL
SEQRES 6 B 282 LYS CYS PHE ASN ASP LEU LYS ALA GLU GLU LEU LEU LEU
SEQRES 7 B 282 LYS ILE HIS GLU VAL SER THR VAL SER HIS ALA ASP ALA
SEQRES 8 B 282 ASP CYS PHE VAL CYS VAL PHE LEU SER HIS GLY GLU GLY
SEQRES 9 B 282 ASN HIS ILE TYR ALA TYR ASP ALA LYS ILE GLU ILE GLN
SEQRES 10 B 282 THR LEU THR GLY LEU PHE LYS GLY ASP LYS CYS HIS SER
SEQRES 11 B 282 LEU VAL GLY LYS PRO LYS ILE PHE ILE ILE GLN ALA ALA
SEQRES 12 B 282 ARG GLY ASN GLN HIS ASP VAL PRO VAL ILE PRO LEU ASP
SEQRES 13 B 282 VAL VAL ASP ASN GLN THR GLU LYS LEU ASP THR ASN ILE
SEQRES 14 B 282 THR GLU VAL ASP ALA ALA SER VAL TYR THR LEU PRO ALA
SEQRES 15 B 282 GLY ALA ASP PHE LEU MET CYS TYR SER VAL ALA GLU GLY
SEQRES 16 B 282 TYR TYR SER HIS ARG GLU THR VAL ASN GLY SER TRP TYR
SEQRES 17 B 282 ILE GLN ASP LEU CYS GLU MET LEU GLY LYS TYR GLY SER
SEQRES 18 B 282 SER LEU GLU PHE THR GLU LEU LEU THR LEU VAL ASN ARG
SEQRES 19 B 282 LYS VAL SER GLN ARG ARG VAL ASP PHE CYS LYS ASP PRO
SEQRES 20 B 282 SER ALA ILE GLY LYS LYS GLN VAL PRO CYS PHE ALA SER
SEQRES 21 B 282 MET LEU THR LYS LYS LEU HIS PHE PHE PRO LYS SER ASN
SEQRES 22 B 282 GLY ASN SER HIS HIS HIS HIS HIS HIS
HET PO4 A 401 5
HET PO4 A 402 5
HET 2GQ B 401 12
HET PO4 B 402 5
HET PO4 B 403 5
HETNAM PO4 PHOSPHATE ION
HETNAM 2GQ 3-(PYRROLIDIN-1-YL)ISOQUINOLIN-1(2H)-ONE
FORMUL 3 PO4 4(O4 P 3-)
FORMUL 5 2GQ C13 H14 N2 O
FORMUL 8 HOH *208(H2 O)
HELIX 1 1 PHE A 56 THR A 60 5 5
HELIX 2 2 GLY A 66 LEU A 81 1 16
HELIX 3 3 LYS A 92 VAL A 106 1 15
HELIX 4 4 ILE A 136 GLY A 141 1 6
HELIX 5 5 LEU A 142 VAL A 152 5 11
HELIX 6 6 TRP A 227 GLY A 240 1 14
HELIX 7 7 GLU A 244 ARG A 259 1 16
HELIX 8 8 ASP A 266 ILE A 270 5 5
HELIX 9 9 PHE B 56 THR B 60 5 5
HELIX 10 10 GLY B 66 LEU B 81 1 16
HELIX 11 11 LYS B 92 VAL B 106 1 15
HELIX 12 12 ILE B 136 LEU B 142 1 7
HELIX 13 13 CYS B 148 VAL B 152 5 5
HELIX 14 14 TRP B 227 GLY B 240 1 14
HELIX 15 15 GLU B 244 GLN B 258 1 15
HELIX 16 16 ASP B 266 ILE B 270 5 5
SHEET 1 A12 GLU A 84 ASN A 89 0
SHEET 2 A12 ARG A 43 ASN A 51 1 N ALA A 47 O GLU A 84
SHEET 3 A12 ALA A 111 GLU A 123 1 O VAL A 117 N PHE A 50
SHEET 4 A12 LYS A 156 ALA A 163 1 O ILE A 157 N CYS A 116
SHEET 5 A12 PHE A 206 TYR A 210 1 O CYS A 209 N PHE A 158
SHEET 6 A12 CYS A 277 SER A 280 -1 O CYS A 277 N TYR A 210
SHEET 7 A12 CYS B 277 SER B 280 -1 O PHE B 278 N SER A 280
SHEET 8 A12 PHE B 206 TYR B 210 -1 N TYR B 210 O CYS B 277
SHEET 9 A12 LYS B 156 ALA B 163 1 N ILE B 160 O CYS B 209
SHEET 10 A12 ALA B 111 GLU B 123 1 N CYS B 116 O ILE B 157
SHEET 11 A12 ARG B 43 ASN B 51 1 N LEU B 48 O VAL B 117
SHEET 12 A12 GLU B 84 ASN B 89 1 O LYS B 86 N ALA B 47
SHEET 1 B12 LYS A 133 GLU A 135 0
SHEET 2 B12 HIS A 126 TYR A 128 -1 N ILE A 127 O ILE A 134
SHEET 3 B12 ALA A 111 GLU A 123 -1 N GLU A 123 O HIS A 126
SHEET 4 B12 LYS A 156 ALA A 163 1 O ILE A 157 N CYS A 116
SHEET 5 B12 PHE A 206 TYR A 210 1 O CYS A 209 N PHE A 158
SHEET 6 B12 CYS A 277 SER A 280 -1 O CYS A 277 N TYR A 210
SHEET 7 B12 CYS B 277 SER B 280 -1 O PHE B 278 N SER A 280
SHEET 8 B12 PHE B 206 TYR B 210 -1 N TYR B 210 O CYS B 277
SHEET 9 B12 LYS B 156 ALA B 163 1 N ILE B 160 O CYS B 209
SHEET 10 B12 ALA B 111 GLU B 123 1 N CYS B 116 O ILE B 157
SHEET 11 B12 HIS B 126 TYR B 128 -1 O HIS B 126 N GLU B 123
SHEET 12 B12 LYS B 133 GLU B 135 -1 O ILE B 134 N ILE B 127
SHEET 1 C 3 THR A 190 ALA A 194 0
SHEET 2 C 3 TYR A 217 GLU A 221 -1 O ARG A 220 N GLU A 191
SHEET 3 C 3 GLY A 225 SER A 226 -1 O GLY A 225 N GLU A 221
SHEET 1 D 3 THR B 190 ALA B 194 0
SHEET 2 D 3 TYR B 217 GLU B 221 -1 O ARG B 220 N GLU B 191
SHEET 3 D 3 GLY B 225 SER B 226 -1 O GLY B 225 N GLU B 221
SITE 1 AC1 9 ARG A 64 SER A 120 HIS A 121 GLN A 161
SITE 2 AC1 9 ALA A 162 ALA A 163 ASP A 193 ARG A 220
SITE 3 AC1 9 HOH A 566
SITE 1 AC2 9 LYS A 144 GLY A 145 VAL A 152 GLY A 153
SITE 2 AC2 9 LYS A 156 ALA A 204 ASP A 205 PHE A 206
SITE 3 AC2 9 HOH A 538
SITE 1 AC3 4 TYR A 198 LEU A 200 TYR B 198 LEU B 200
SITE 1 AC4 10 ARG B 64 SER B 120 HIS B 121 GLN B 161
SITE 2 AC4 10 ALA B 162 ALA B 163 ASP B 193 ARG B 220
SITE 3 AC4 10 HOH B 511 HOH B 553
SITE 1 AC5 9 PHE B 143 LYS B 144 GLY B 145 LYS B 156
SITE 2 AC5 9 ALA B 204 ASP B 205 PHE B 206 HOH B 504
SITE 3 AC5 9 HOH B 596
CRYST1 116.083 116.083 79.526 90.00 90.00 90.00 P 43 21 2 16
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 0.008615 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008615 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012575 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
