HEADER TRANSCRIPTION/TRANSCRIPTION REGULATOR 24-SEP-10 3OZ0
TITLE PPAR DELTA IN COMPLEX WITH AZPPARD02
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR DELTA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: NUCLEAR RECEPTOR PROTEIN, UNP RESIDUES 165-441;
COMPND 5 SYNONYM: PPAR-DELTA, NUCI, NUCLEAR HORMONE RECEPTOR 1, NUC1, NUCLEAR
COMPND 6 RECEPTOR SUBFAMILY 1 GROUP C MEMBER 2, PEROXISOME PROLIFERATOR-
COMPND 7 ACTIVATED RECEPTOR BETA, PPAR-BETA;
COMPND 8 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: PPARD, NR1C2, PPARB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSCRIPTION FACTOR, TRANSCRIPTION, NUCLEAR RECEPTOR FOLD,
KEYWDS 2 TRANSCRIPTION REGULATION, TRANSCRIPTION-TRANSCRIPTION REGULATOR
KEYWDS 3 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.OGG
REVDAT 4 06-SEP-23 3OZ0 1 REMARK SEQADV
REVDAT 3 08-NOV-17 3OZ0 1 REMARK
REVDAT 2 29-FEB-12 3OZ0 1 AUTHOR VERSN
REVDAT 1 19-JAN-11 3OZ0 0
JRNL AUTH C.A.LUCKHURST,L.A.STEIN,M.FURBER,N.WEBB,M.J.RATCLIFFE,
JRNL AUTH 2 G.ALLENBY,S.BOTTERELL,W.TOMLINSON,B.MARTIN,A.WALDING
JRNL TITL DISCOVERY OF ISOINDOLINE AND TETRAHYDROISOQUINOLINE
JRNL TITL 2 DERIVATIVES AS POTENT, SELECTIVE PPARδ AGONISTS
JRNL REF BIOORG.MED.CHEM.LETT. V. 21 492 2011
JRNL REFN ISSN 0960-894X
JRNL PMID 21094606
JRNL DOI 10.1016/J.BMCL.2010.10.117
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.49
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 5457
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 + TEST SET) : 0.220
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.900
REMARK 3 FREE R VALUE TEST SET COUNT : 536
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 404
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.59
REMARK 3 BIN R VALUE (WORKING SET) : 0.3110
REMARK 3 BIN FREE R VALUE SET COUNT : 46
REMARK 3 BIN FREE R VALUE : 0.3450
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2101
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.73000
REMARK 3 B22 (A**2) : -2.05000
REMARK 3 B33 (A**2) : 0.48000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 4.08000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.529
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.391
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.567
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.919
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.861
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2137 ; 0.005 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1976 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2902 ; 0.825 ; 1.980
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4568 ; 0.693 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 258 ; 4.271 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 92 ;30.219 ;24.130
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 360 ;14.575 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;17.174 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 335 ; 0.044 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2337 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 438 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 516 ; 0.177 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1964 ; 0.150 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1079 ; 0.172 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1107 ; 0.082 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 42 ; 0.115 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 6 ; 0.091 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 47 ; 0.146 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.125 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1705 ; 0.780 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 519 ; 0.094 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2103 ; 0.933 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 988 ; 1.276 ; 4.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 799 ; 1.929 ; 6.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3OZ0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-SEP-10.
REMARK 100 THE DEPOSITION ID IS D_1000061749.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-SEP-09
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 : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9134
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6381
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 56.490
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.6
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.45000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 2GWX
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG, PH 8.5, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
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 56.62900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.56700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 56.62900
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 24.56700
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 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 193
REMARK 465 GLY A 194
REMARK 465 HIS A 195
REMARK 465 HIS A 196
REMARK 465 HIS A 197
REMARK 465 HIS A 198
REMARK 465 HIS A 199
REMARK 465 HIS A 200
REMARK 465 GLY A 201
REMARK 465 SER A 202
REMARK 465 GLN A 203
REMARK 465 TYR A 204
REMARK 465 ASN A 205
REMARK 465 PRO A 206
REMARK 465 GLN A 207
REMARK 465 VAL A 208
REMARK 465 ALA A 209
REMARK 465 ASP A 210
REMARK 465 GLY A 239
REMARK 465 LYS A 240
REMARK 465 ALA A 241
REMARK 465 SER A 242
REMARK 465 HIS A 243
REMARK 465 THR A 244
REMARK 465 TYR A 477
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 224 CD CE NZ
REMARK 480 LYS A 232 CG CD CE NZ
REMARK 480 GLU A 253 CG CD OE1 OE2
REMARK 480 LYS A 260 CG CD CE NZ
REMARK 480 LYS A 265 CD CE NZ
REMARK 480 GLU A 291 CG CD OE1 OE2
REMARK 480 LYS A 336 CD CE NZ
REMARK 480 LYS A 373 NZ
REMARK 480 GLN A 429 CG CD OE1 NE2
REMARK 480 ARG A 455 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 457 CD CE NZ
REMARK 480 LYS A 458 CD CE NZ
REMARK 480 LYS A 474 CD CE NZ
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 ALA A 258 93.94 -67.02
REMARK 500 GLU A 259 -77.71 -137.46
REMARK 500 LYS A 260 -15.05 58.21
REMARK 500 ASN A 269 -75.75 -119.24
REMARK 500 TYR A 274 -59.99 175.97
REMARK 500 SER A 305 -11.35 78.42
REMARK 500 ASP A 396 56.94 -93.31
REMARK 500 MET A 401 -72.53 -75.49
REMARK 500 ASP A 427 50.85 -95.39
REMARK 500 ALA A 428 77.79 -152.27
REMARK 500 ASP A 475 73.51 67.28
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 3OZ A 1
DBREF 3OZ0 A 201 477 UNP Q03181 PPARD_HUMAN 165 441
SEQADV 3OZ0 MET A 193 UNP Q03181 EXPRESSION TAG
SEQADV 3OZ0 GLY A 194 UNP Q03181 EXPRESSION TAG
SEQADV 3OZ0 HIS A 195 UNP Q03181 EXPRESSION TAG
SEQADV 3OZ0 HIS A 196 UNP Q03181 EXPRESSION TAG
SEQADV 3OZ0 HIS A 197 UNP Q03181 EXPRESSION TAG
SEQADV 3OZ0 HIS A 198 UNP Q03181 EXPRESSION TAG
SEQADV 3OZ0 HIS A 199 UNP Q03181 EXPRESSION TAG
SEQADV 3OZ0 HIS A 200 UNP Q03181 EXPRESSION TAG
SEQRES 1 A 285 MET GLY HIS HIS HIS HIS HIS HIS GLY SER GLN TYR ASN
SEQRES 2 A 285 PRO GLN VAL ALA ASP LEU LYS ALA PHE SER LYS HIS ILE
SEQRES 3 A 285 TYR ASN ALA TYR LEU LYS ASN PHE ASN MET THR LYS LYS
SEQRES 4 A 285 LYS ALA ARG SER ILE LEU THR GLY LYS ALA SER HIS THR
SEQRES 5 A 285 ALA PRO PHE VAL ILE HIS ASP ILE GLU THR LEU TRP GLN
SEQRES 6 A 285 ALA GLU LYS GLY LEU VAL TRP LYS GLN LEU VAL ASN GLY
SEQRES 7 A 285 LEU PRO PRO TYR LYS GLU ILE SER VAL HIS VAL PHE TYR
SEQRES 8 A 285 ARG CYS GLN CYS THR THR VAL GLU THR VAL ARG GLU LEU
SEQRES 9 A 285 THR GLU PHE ALA LYS SER ILE PRO SER PHE SER SER LEU
SEQRES 10 A 285 PHE LEU ASN ASP GLN VAL THR LEU LEU LYS TYR GLY VAL
SEQRES 11 A 285 HIS GLU ALA ILE PHE ALA MET LEU ALA SER ILE VAL ASN
SEQRES 12 A 285 LYS ASP GLY LEU LEU VAL ALA ASN GLY SER GLY PHE VAL
SEQRES 13 A 285 THR ARG GLU PHE LEU ARG SER LEU ARG LYS PRO PHE SER
SEQRES 14 A 285 ASP ILE ILE GLU PRO LYS PHE GLU PHE ALA VAL LYS PHE
SEQRES 15 A 285 ASN ALA LEU GLU LEU ASP ASP SER ASP LEU ALA LEU PHE
SEQRES 16 A 285 ILE ALA ALA ILE ILE LEU CYS GLY ASP ARG PRO GLY LEU
SEQRES 17 A 285 MET ASN VAL PRO ARG VAL GLU ALA ILE GLN ASP THR ILE
SEQRES 18 A 285 LEU ARG ALA LEU GLU PHE HIS LEU GLN ALA ASN HIS PRO
SEQRES 19 A 285 ASP ALA GLN TYR LEU PHE PRO LYS LEU LEU GLN LYS MET
SEQRES 20 A 285 ALA ASP LEU ARG GLN LEU VAL THR GLU HIS ALA GLN MET
SEQRES 21 A 285 MET GLN ARG ILE LYS LYS THR GLU THR GLU THR SER LEU
SEQRES 22 A 285 HIS PRO LEU LEU GLN GLU ILE TYR LYS ASP MET TYR
HET 3OZ A 1 33
HETNAM 3OZ [4-({(1S)-1-[(2,4-DICHLOROPHENYL)CARBAMOYL]-1,3-
HETNAM 2 3OZ DIHYDRO-2H-ISOINDOL-2-YL}METHYL)-2-
HETNAM 3 3OZ METHYLPHENOXY]ACETIC ACID
FORMUL 2 3OZ C25 H22 CL2 N2 O4
HELIX 1 1 LEU A 211 PHE A 226 1 16
HELIX 2 2 THR A 229 THR A 238 1 10
HELIX 3 3 ASP A 251 ALA A 258 1 8
HELIX 4 4 GLY A 261 VAL A 268 1 8
HELIX 5 5 TYR A 274 ILE A 303 1 30
HELIX 6 6 PHE A 310 ALA A 331 1 22
HELIX 7 7 ARG A 350 SER A 355 1 6
HELIX 8 8 ARG A 357 ALA A 376 1 20
HELIX 9 9 ASP A 380 LEU A 393 1 14
HELIX 10 10 ASN A 402 HIS A 425 1 24
HELIX 11 11 TYR A 430 GLU A 460 1 31
HELIX 12 12 HIS A 466 LYS A 474 1 9
SHEET 1 A 4 PHE A 247 ILE A 249 0
SHEET 2 A 4 GLY A 346 THR A 349 1 O PHE A 347 N ILE A 249
SHEET 3 A 4 GLY A 338 VAL A 341 -1 N VAL A 341 O GLY A 346
SHEET 4 A 4 VAL A 334 ASN A 335 -1 N ASN A 335 O GLY A 338
SITE 1 AC1 19 VAL A 281 PHE A 282 ARG A 284 CYS A 285
SITE 2 AC1 19 THR A 288 THR A 289 HIS A 323 PHE A 327
SITE 3 AC1 19 LEU A 330 VAL A 334 LEU A 339 VAL A 341
SITE 4 AC1 19 LEU A 353 ILE A 363 LYS A 367 HIS A 449
SITE 5 AC1 19 MET A 453 LEU A 469 TYR A 473
CRYST1 113.258 49.134 58.574 90.00 105.34 90.00 C 1 2 1 4
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 0.008829 0.000000 0.002421 0.00000
SCALE2 0.000000 0.020353 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017703 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
