HEADER TRANSCRIPTION 09-MAR-01 1I7I
TITLE CRYSTAL STRUCTURE OF THE LIGAND BINDING DOMAIN OF HUMAN PPAR-GAMMA IN
TITLE 2 COMPLEX WITH THE AGONIST AZ 242
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN;
COMPND 5 SYNONYM: PPAR-GAMMA;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ANTI PARALLEL HELIX SANDWICH, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.F.W.PETERSEN,P.CRONET,R.FOLMER,N.BLOMBERG,K.SJOBLOM,U.KARLSSON,E.-
AUTHOR 2 L.LINDSTEDT,K.BAMBERG
REVDAT 4 09-AUG-23 1I7I 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1I7I 1 VERSN
REVDAT 2 01-APR-03 1I7I 1 JRNL
REVDAT 1 09-MAR-02 1I7I 0
JRNL AUTH P.CRONET,J.F.PETERSEN,R.FOLMER,N.BLOMBERG,K.SJOBLOM,
JRNL AUTH 2 U.KARLSSON,E.L.LINDSTEDT,K.BAMBERG
JRNL TITL STRUCTURE OF THE PPARALPHA AND -GAMMA LIGAND BINDING DOMAIN
JRNL TITL 2 IN COMPLEX WITH AZ 242; LIGAND SELECTIVITY AND AGONIST
JRNL TITL 3 ACTIVATION IN THE PPAR FAMILY.
JRNL REF STRUCTURE V. 9 699 2001
JRNL REFN ISSN 0969-2126
JRNL PMID 11587644
JRNL DOI 10.1016/S0969-2126(01)00634-7
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX 2000
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN,ACCELRYS
REMARK 3 : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,
REMARK 3 : YIP,DZAKULA)
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1562646.620
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.3
REMARK 3 NUMBER OF REFLECTIONS : 25313
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) : 0.238
REMARK 3 R VALUE (WORKING SET) : 0.238
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1224
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.50
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4076
REMARK 3 BIN R VALUE (WORKING SET) : 0.3240
REMARK 3 BIN FREE R VALUE : 0.3440
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 205
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.024
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4132
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 56
REMARK 3 SOLVENT ATOMS : 62
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.67000
REMARK 3 B22 (A**2) : 7.31000
REMARK 3 B33 (A**2) : -4.64000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 9.36000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.34
REMARK 3 ESD FROM SIGMAA (A) : 0.32
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.43
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.33
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 18.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.770
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.500 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.470 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.770 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.840 ; 2.500
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : C1.PAR
REMARK 3 PARAMETER FILE 3 : WATER.PARAM
REMARK 3 PARAMETER FILE 4 : CIS_PEPTIDE.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : C1.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1I7I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013001.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25345
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.3
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.43
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.41900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY: 2PRG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, HEPES, PH 7.5, VAPOR
REMARK 280 DIFFUSION, HANGING 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 46.46400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.89050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 46.46400
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.89050
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 GLY A 186
REMARK 465 SER A 187
REMARK 465 HIS A 188
REMARK 465 MET A 189
REMARK 465 ALA A 190
REMARK 465 GLU A 191
REMARK 465 ILE A 192
REMARK 465 SER A 193
REMARK 465 SER A 194
REMARK 465 ASP A 195
REMARK 465 ILE A 196
REMARK 465 ILE A 197
REMARK 465 SER A 198
REMARK 465 SER A 199
REMARK 465 ASP A 200
REMARK 465 ILE A 201
REMARK 465 ASP A 202
REMARK 465 GLN A 203
REMARK 465 LEU A 204
REMARK 465 ASN A 205
REMARK 465 PRO A 206
REMARK 465 PHE A 264
REMARK 465 LYS A 265
REMARK 465 HIS A 266
REMARK 465 ILE A 267
REMARK 465 THR A 268
REMARK 465 PRO A 269
REMARK 465 LEU A 270
REMARK 465 GLN A 271
REMARK 465 GLU A 272
REMARK 465 GLN A 273
REMARK 465 SER A 274
REMARK 465 LYS A 275
REMARK 465 TYR A 477
REMARK 465 GLY B 186
REMARK 465 SER B 187
REMARK 465 HIS B 188
REMARK 465 MET B 189
REMARK 465 ALA B 190
REMARK 465 GLU B 191
REMARK 465 ILE B 192
REMARK 465 SER B 193
REMARK 465 SER B 194
REMARK 465 ASP B 195
REMARK 465 ILE B 196
REMARK 465 ILE B 197
REMARK 465 SER B 198
REMARK 465 SER B 199
REMARK 465 ASP B 200
REMARK 465 ILE B 201
REMARK 465 ASP B 202
REMARK 465 GLN B 203
REMARK 465 LEU B 204
REMARK 465 ASN B 205
REMARK 465 PRO B 206
REMARK 465 THR B 268
REMARK 465 PRO B 269
REMARK 465 LEU B 270
REMARK 465 GLN B 271
REMARK 465 GLU B 272
REMARK 465 GLN B 273
REMARK 465 SER B 274
REMARK 465 ASP B 462
REMARK 465 MET B 463
REMARK 465 LYS B 474
REMARK 465 ASP B 475
REMARK 465 LEU B 476
REMARK 465 TYR B 477
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 THR A 242 24.75 -71.75
REMARK 500 LYS A 244 107.08 -166.51
REMARK 500 LYS A 358 -80.35 12.99
REMARK 500 ASP A 362 5.60 -152.17
REMARK 500 LEU A 393 59.04 -93.51
REMARK 500 SER A 394 -73.18 -73.07
REMARK 500 LYS A 474 108.23 -56.49
REMARK 500 ASP A 475 112.66 61.29
REMARK 500 LEU B 237 -147.93 -62.62
REMARK 500 THR B 238 -44.96 -25.53
REMARK 500 LYS B 240 -82.87 -49.21
REMARK 500 THR B 242 64.11 -62.48
REMARK 500 LYS B 244 83.91 161.50
REMARK 500 GLU B 276 150.52 -37.62
REMARK 500 SER B 355 54.87 -109.42
REMARK 500 PRO B 359 34.78 -92.54
REMARK 500 SER B 394 -74.25 -67.88
REMARK 500 LYS B 457 38.79 -67.15
REMARK 500 LYS B 458 40.93 -148.23
REMARK 500 THR B 459 -52.49 -159.75
REMARK 500 HIS B 466 -30.04 164.77
REMARK 500 PRO B 467 -84.75 -33.53
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 AZ2 A 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZ2 B 478
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1I7G RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE LIGAND BINDING DOMAIN FROM HUMAN PPAR-
REMARK 900 ALPHA IN COMPLEX WITH THE AGONIST AZ 242
DBREF 1I7I A 197 477 UNP P37231 PPAT_HUMAN 225 505
DBREF 1I7I B 197 477 UNP P37231 PPAT_HUMAN 225 505
SEQADV 1I7I GLY A 186 UNP P37231 CLONING ARTIFACT
SEQADV 1I7I SER A 187 UNP P37231 CLONING ARTIFACT
SEQADV 1I7I HIS A 188 UNP P37231 CLONING ARTIFACT
SEQADV 1I7I MET A 189 UNP P37231 CLONING ARTIFACT
SEQADV 1I7I ALA A 190 UNP P37231 CLONING ARTIFACT
SEQADV 1I7I GLU A 191 UNP P37231 CLONING ARTIFACT
SEQADV 1I7I ILE A 192 UNP P37231 CLONING ARTIFACT
SEQADV 1I7I SER A 193 UNP P37231 CLONING ARTIFACT
SEQADV 1I7I SER A 194 UNP P37231 CLONING ARTIFACT
SEQADV 1I7I ASP A 195 UNP P37231 CLONING ARTIFACT
SEQADV 1I7I ILE A 196 UNP P37231 CLONING ARTIFACT
SEQADV 1I7I GLY B 186 UNP P37231 CLONING ARTIFACT
SEQADV 1I7I SER B 187 UNP P37231 CLONING ARTIFACT
SEQADV 1I7I HIS B 188 UNP P37231 CLONING ARTIFACT
SEQADV 1I7I MET B 189 UNP P37231 CLONING ARTIFACT
SEQADV 1I7I ALA B 190 UNP P37231 CLONING ARTIFACT
SEQADV 1I7I GLU B 191 UNP P37231 CLONING ARTIFACT
SEQADV 1I7I ILE B 192 UNP P37231 CLONING ARTIFACT
SEQADV 1I7I SER B 193 UNP P37231 CLONING ARTIFACT
SEQADV 1I7I SER B 194 UNP P37231 CLONING ARTIFACT
SEQADV 1I7I ASP B 195 UNP P37231 CLONING ARTIFACT
SEQADV 1I7I ILE B 196 UNP P37231 CLONING ARTIFACT
SEQRES 1 A 292 GLY SER HIS MET ALA GLU ILE SER SER ASP ILE ILE SER
SEQRES 2 A 292 SER ASP ILE ASP GLN LEU ASN PRO GLU SER ALA ASP LEU
SEQRES 3 A 292 ARG ALA LEU ALA LYS HIS LEU TYR ASP SER TYR ILE LYS
SEQRES 4 A 292 SER PHE PRO LEU THR LYS ALA LYS ALA ARG ALA ILE LEU
SEQRES 5 A 292 THR GLY LYS THR THR ASP LYS SER PRO PHE VAL ILE TYR
SEQRES 6 A 292 ASP MET ASN SER LEU MET MET GLY GLU ASP LYS ILE LYS
SEQRES 7 A 292 PHE LYS HIS ILE THR PRO LEU GLN GLU GLN SER LYS GLU
SEQRES 8 A 292 VAL ALA ILE ARG ILE PHE GLN GLY CYS GLN PHE ARG SER
SEQRES 9 A 292 VAL GLU ALA VAL GLN GLU ILE THR GLU TYR ALA LYS SER
SEQRES 10 A 292 ILE PRO GLY PHE VAL ASN LEU ASP LEU ASN ASP GLN VAL
SEQRES 11 A 292 THR LEU LEU LYS TYR GLY VAL HIS GLU ILE ILE TYR THR
SEQRES 12 A 292 MET LEU ALA SER LEU MET ASN LYS ASP GLY VAL LEU ILE
SEQRES 13 A 292 SER GLU GLY GLN GLY PHE MET THR ARG GLU PHE LEU LYS
SEQRES 14 A 292 SER LEU ARG LYS PRO PHE GLY ASP PHE MET GLU PRO LYS
SEQRES 15 A 292 PHE GLU PHE ALA VAL LYS PHE ASN ALA LEU GLU LEU ASP
SEQRES 16 A 292 ASP SER ASP LEU ALA ILE PHE ILE ALA VAL ILE ILE LEU
SEQRES 17 A 292 SER GLY ASP ARG PRO GLY LEU LEU ASN VAL LYS PRO ILE
SEQRES 18 A 292 GLU ASP ILE GLN ASP ASN LEU LEU GLN ALA LEU GLU LEU
SEQRES 19 A 292 GLN LEU LYS LEU ASN HIS PRO GLU SER SER GLN LEU PHE
SEQRES 20 A 292 ALA LYS LEU LEU GLN LYS MET THR ASP LEU ARG GLN ILE
SEQRES 21 A 292 VAL THR GLU HIS VAL GLN LEU LEU GLN VAL ILE LYS LYS
SEQRES 22 A 292 THR GLU THR ASP MET SER LEU HIS PRO LEU LEU GLN GLU
SEQRES 23 A 292 ILE TYR LYS ASP LEU TYR
SEQRES 1 B 292 GLY SER HIS MET ALA GLU ILE SER SER ASP ILE ILE SER
SEQRES 2 B 292 SER ASP ILE ASP GLN LEU ASN PRO GLU SER ALA ASP LEU
SEQRES 3 B 292 ARG ALA LEU ALA LYS HIS LEU TYR ASP SER TYR ILE LYS
SEQRES 4 B 292 SER PHE PRO LEU THR LYS ALA LYS ALA ARG ALA ILE LEU
SEQRES 5 B 292 THR GLY LYS THR THR ASP LYS SER PRO PHE VAL ILE TYR
SEQRES 6 B 292 ASP MET ASN SER LEU MET MET GLY GLU ASP LYS ILE LYS
SEQRES 7 B 292 PHE LYS HIS ILE THR PRO LEU GLN GLU GLN SER LYS GLU
SEQRES 8 B 292 VAL ALA ILE ARG ILE PHE GLN GLY CYS GLN PHE ARG SER
SEQRES 9 B 292 VAL GLU ALA VAL GLN GLU ILE THR GLU TYR ALA LYS SER
SEQRES 10 B 292 ILE PRO GLY PHE VAL ASN LEU ASP LEU ASN ASP GLN VAL
SEQRES 11 B 292 THR LEU LEU LYS TYR GLY VAL HIS GLU ILE ILE TYR THR
SEQRES 12 B 292 MET LEU ALA SER LEU MET ASN LYS ASP GLY VAL LEU ILE
SEQRES 13 B 292 SER GLU GLY GLN GLY PHE MET THR ARG GLU PHE LEU LYS
SEQRES 14 B 292 SER LEU ARG LYS PRO PHE GLY ASP PHE MET GLU PRO LYS
SEQRES 15 B 292 PHE GLU PHE ALA VAL LYS PHE ASN ALA LEU GLU LEU ASP
SEQRES 16 B 292 ASP SER ASP LEU ALA ILE PHE ILE ALA VAL ILE ILE LEU
SEQRES 17 B 292 SER GLY ASP ARG PRO GLY LEU LEU ASN VAL LYS PRO ILE
SEQRES 18 B 292 GLU ASP ILE GLN ASP ASN LEU LEU GLN ALA LEU GLU LEU
SEQRES 19 B 292 GLN LEU LYS LEU ASN HIS PRO GLU SER SER GLN LEU PHE
SEQRES 20 B 292 ALA LYS LEU LEU GLN LYS MET THR ASP LEU ARG GLN ILE
SEQRES 21 B 292 VAL THR GLU HIS VAL GLN LEU LEU GLN VAL ILE LYS LYS
SEQRES 22 B 292 THR GLU THR ASP MET SER LEU HIS PRO LEU LEU GLN GLU
SEQRES 23 B 292 ILE TYR LYS ASP LEU TYR
HET AZ2 A 101 28
HET AZ2 B 478 28
HETNAM AZ2 (2S)-2-ETHOXY-3-[4-(2-{4-[(METHYLSULFONYL)
HETNAM 2 AZ2 OXY]PHENYL}ETHOXY)PHENYL]PROPANOIC ACID
HETSYN AZ2 AZ 242
FORMUL 3 AZ2 2(C20 H24 O7 S)
FORMUL 5 HOH *62(H2 O)
HELIX 1 1 GLU A 207 PHE A 226 1 20
HELIX 2 2 THR A 229 THR A 238 1 10
HELIX 3 3 ASP A 251 ILE A 262 1 12
HELIX 4 4 GLU A 276 SER A 302 1 27
HELIX 5 5 GLY A 305 LEU A 309 5 5
HELIX 6 6 ASP A 310 SER A 332 1 23
HELIX 7 7 SER A 342 GLY A 344 5 3
HELIX 8 8 ARG A 350 SER A 355 1 6
HELIX 9 9 MET A 364 ALA A 376 1 13
HELIX 10 10 ASP A 380 LEU A 393 1 14
HELIX 11 11 ASN A 402 HIS A 425 1 24
HELIX 12 12 GLN A 430 GLU A 460 1 31
HELIX 13 13 HIS A 466 LYS A 474 1 9
HELIX 14 14 GLU B 207 PHE B 226 1 20
HELIX 15 15 THR B 229 LEU B 237 1 9
HELIX 16 16 ASP B 251 ILE B 262 1 12
HELIX 17 17 GLU B 276 ILE B 303 1 28
HELIX 18 18 GLY B 305 LEU B 309 5 5
HELIX 19 19 ASP B 310 ALA B 331 1 22
HELIX 20 20 ARG B 350 SER B 355 1 6
HELIX 21 21 MET B 364 ALA B 376 1 13
HELIX 22 22 ASP B 380 LEU B 393 1 14
HELIX 23 23 ASN B 402 HIS B 425 1 24
HELIX 24 24 GLN B 430 LYS B 457 1 28
HELIX 25 25 HIS B 466 GLU B 471 1 6
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 ILE A 341 -1 N VAL A 339 O MET A 348
SHEET 4 A 4 MET A 334 ASN A 335 -1 N ASN A 335 O GLY A 338
SHEET 1 B 4 PHE B 247 ILE B 249 0
SHEET 2 B 4 GLY B 346 THR B 349 1 O PHE B 347 N ILE B 249
SHEET 3 B 4 GLY B 338 ILE B 341 -1 N VAL B 339 O MET B 348
SHEET 4 B 4 MET B 334 ASN B 335 -1 N ASN B 335 O GLY B 338
CISPEP 1 LYS B 358 PRO B 359 0 0.67
SITE 1 AC1 10 PHE A 282 GLY A 284 CYS A 285 SER A 289
SITE 2 AC1 10 HIS A 323 MET A 348 MET A 364 HIS A 449
SITE 3 AC1 10 LEU A 469 TYR A 473
SITE 1 AC2 12 PHE B 264 HIS B 266 ILE B 281 PHE B 282
SITE 2 AC2 12 GLY B 284 CYS B 285 SER B 289 HIS B 323
SITE 3 AC2 12 ILE B 341 MET B 348 MET B 364 HIS B 449
CRYST1 92.928 61.781 118.981 90.00 101.52 90.00 C 1 2 1 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 0.010761 0.000000 0.002193 0.00000
SCALE2 0.000000 0.016186 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008577 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
