HEADER TRANSCRIPTION 29-JAN-10 3ADS
TITLE HUMAN PPARGAMMA LIGAND-BINDING DOMAIN IN COMPLEX WITH INDOMETHACIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: LIGAND-BINDING DOMAIN, RESIDUES IN UNP 223-505;
COMPND 5 SYNONYM: PPAR-GAMMA, NUCLEAR RECEPTOR SUBFAMILY 1 GROUP C MEMBER 3;
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 GENE: PPARGAMMA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS NUCLEAR RECEPTOR, LIGAND-DEPENDENT TRANSCRIPTION FACTOR, LIGAND-
KEYWDS 2 BINDING DOMAIN, ACTIVATOR, DIABETES MELLITUS, DISEASE MUTATION, DNA-
KEYWDS 3 BINDING, METAL-BINDING, NUCLEUS, OBESITY, PHOSPHOPROTEIN, RECEPTOR,
KEYWDS 4 TRANSCRIPTION, TRANSCRIPTION REGULATION, ZINC-FINGER
EXPDTA X-RAY DIFFRACTION
AUTHOR T.WAKU,T.SHIRAKI,T.OYAMA,K.MORIKAWA
REVDAT 2 01-NOV-23 3ADS 1 REMARK SEQADV
REVDAT 1 22-DEC-10 3ADS 0
JRNL AUTH T.WAKU,T.SHIRAKI,T.OYAMA,K.MAEBARA,R.NAKAMORI,K.MORIKAWA
JRNL TITL THE NUCLEAR RECEPTOR PPARGAMMA INDIVIDUALLY RESPONDS TO
JRNL TITL 2 SEROTONIN- AND FATTY ACID-METABOLITES
JRNL REF EMBO J. V. 29 3395 2010
JRNL REFN ISSN 0261-4189
JRNL PMID 20717101
JRNL DOI 10.1038/EMBOJ.2010.197
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.4
REMARK 3 NUMBER OF REFLECTIONS : 28608
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) : 0.228
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1407
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) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.39
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2740
REMARK 3 BIN FREE R VALUE : 0.3240
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 214
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.022
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4098
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 75
REMARK 3 SOLVENT ATOMS : 97
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) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.26
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) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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) : 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 3ADS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-FEB-10.
REMARK 100 THE DEPOSITION ID IS D_1000029126.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-NOV-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL38B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
REMARK 200 MONOCHROMATOR : FIXED EXIT SI 111 DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU JUPITER 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29605
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
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 (%) : 95.6
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.27500
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 1PRG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 0.8M SODIUM CITRATE, PH
REMARK 280 7.5, VAPOR 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 46.52250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.51550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 46.52250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.51550
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: DIMERIC
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -46.52250
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 30.51550
REMARK 350 BIOMT3 2 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 191
REMARK 465 SER A 192
REMARK 465 HIS A 193
REMARK 465 MET A 194
REMARK 465 ALA A 195
REMARK 465 GLU 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 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 191
REMARK 465 SER B 192
REMARK 465 HIS B 193
REMARK 465 MET B 194
REMARK 465 ALA B 195
REMARK 465 GLU 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 241
REMARK 465 THR B 242
REMARK 465 ASP B 243
REMARK 465 HIS B 266
REMARK 465 ILE B 267
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 SER B 464
REMARK 465 LEU B 465
REMARK 465 LYS B 474
REMARK 465 ASP B 475
REMARK 465 LEU B 476
REMARK 465 TYR B 477
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 GLN A 203 CG CD OE1 NE2
REMARK 470 LEU A 204 CG CD1 CD2
REMARK 470 ASN A 205 CG OD1 ND2
REMARK 470 PRO A 206 CG CD
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 THR A 242 N LYS A 244 2.13
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 THR A 242 167.28 -44.07
REMARK 500 ASP A 243 26.72 -55.06
REMARK 500 LYS A 358 -62.89 -14.30
REMARK 500 SER A 394 -76.87 -70.34
REMARK 500 SER A 464 -151.00 -80.61
REMARK 500 LEU A 465 114.17 167.50
REMARK 500 ASP A 475 18.32 57.24
REMARK 500 LYS B 263 100.35 60.59
REMARK 500 PHE B 264 -141.86 -91.88
REMARK 500 GLU B 276 104.94 78.80
REMARK 500 SER B 342 64.89 39.58
REMARK 500 ARG B 357 -160.74 -72.54
REMARK 500 LYS B 358 -137.54 30.28
REMARK 500 LYS B 457 26.36 -64.99
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 IMN A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMN A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMN B 3
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3ADT RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEX WITH 5-HYDROXY-INDOLE ACETATE
REMARK 900 RELATED ID: 3ADU RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEX WITH 5-METHOXY-INDOLE ACETATE
REMARK 900 RELATED ID: 3ADV RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEX WITH SEROTONIN
REMARK 900 RELATED ID: 3ADW RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEX WITH 5-METHOXY-INDOLE ACETATE AND 15-OXO-
REMARK 900 EICOSATETRAENOIC ACID
REMARK 900 RELATED ID: 3ADX RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEX WITH INDOMETHACIN AND NITRO-233
DBREF 3ADS A 195 477 UNP P37231 PPARG_HUMAN 223 505
DBREF 3ADS B 195 477 UNP P37231 PPARG_HUMAN 223 505
SEQADV 3ADS GLY A 191 UNP P37231 EXPRESSION TAG
SEQADV 3ADS SER A 192 UNP P37231 EXPRESSION TAG
SEQADV 3ADS HIS A 193 UNP P37231 EXPRESSION TAG
SEQADV 3ADS MET A 194 UNP P37231 EXPRESSION TAG
SEQADV 3ADS GLY B 191 UNP P37231 EXPRESSION TAG
SEQADV 3ADS SER B 192 UNP P37231 EXPRESSION TAG
SEQADV 3ADS HIS B 193 UNP P37231 EXPRESSION TAG
SEQADV 3ADS MET B 194 UNP P37231 EXPRESSION TAG
SEQRES 1 A 287 GLY SER HIS MET ALA GLU ILE SER SER ASP ILE ASP GLN
SEQRES 2 A 287 LEU ASN PRO GLU SER ALA ASP LEU ARG ALA LEU ALA LYS
SEQRES 3 A 287 HIS LEU TYR ASP SER TYR ILE LYS SER PHE PRO LEU THR
SEQRES 4 A 287 LYS ALA LYS ALA ARG ALA ILE LEU THR GLY LYS THR THR
SEQRES 5 A 287 ASP LYS SER PRO PHE VAL ILE TYR ASP MET ASN SER LEU
SEQRES 6 A 287 MET MET GLY GLU ASP LYS ILE LYS PHE LYS HIS ILE THR
SEQRES 7 A 287 PRO LEU GLN GLU GLN SER LYS GLU VAL ALA ILE ARG ILE
SEQRES 8 A 287 PHE GLN GLY CYS GLN PHE ARG SER VAL GLU ALA VAL GLN
SEQRES 9 A 287 GLU ILE THR GLU TYR ALA LYS SER ILE PRO GLY PHE VAL
SEQRES 10 A 287 ASN LEU ASP LEU ASN ASP GLN VAL THR LEU LEU LYS TYR
SEQRES 11 A 287 GLY VAL HIS GLU ILE ILE TYR THR MET LEU ALA SER LEU
SEQRES 12 A 287 MET ASN LYS ASP GLY VAL LEU ILE SER GLU GLY GLN GLY
SEQRES 13 A 287 PHE MET THR ARG GLU PHE LEU LYS SER LEU ARG LYS PRO
SEQRES 14 A 287 PHE GLY ASP PHE MET GLU PRO LYS PHE GLU PHE ALA VAL
SEQRES 15 A 287 LYS PHE ASN ALA LEU GLU LEU ASP ASP SER ASP LEU ALA
SEQRES 16 A 287 ILE PHE ILE ALA VAL ILE ILE LEU SER GLY ASP ARG PRO
SEQRES 17 A 287 GLY LEU LEU ASN VAL LYS PRO ILE GLU ASP ILE GLN ASP
SEQRES 18 A 287 ASN LEU LEU GLN ALA LEU GLU LEU GLN LEU LYS LEU ASN
SEQRES 19 A 287 HIS PRO GLU SER SER GLN LEU PHE ALA LYS LEU LEU GLN
SEQRES 20 A 287 LYS MET THR ASP LEU ARG GLN ILE VAL THR GLU HIS VAL
SEQRES 21 A 287 GLN LEU LEU GLN VAL ILE LYS LYS THR GLU THR ASP MET
SEQRES 22 A 287 SER LEU HIS PRO LEU LEU GLN GLU ILE TYR LYS ASP LEU
SEQRES 23 A 287 TYR
SEQRES 1 B 287 GLY SER HIS MET ALA GLU ILE SER SER ASP ILE ASP GLN
SEQRES 2 B 287 LEU ASN PRO GLU SER ALA ASP LEU ARG ALA LEU ALA LYS
SEQRES 3 B 287 HIS LEU TYR ASP SER TYR ILE LYS SER PHE PRO LEU THR
SEQRES 4 B 287 LYS ALA LYS ALA ARG ALA ILE LEU THR GLY LYS THR THR
SEQRES 5 B 287 ASP LYS SER PRO PHE VAL ILE TYR ASP MET ASN SER LEU
SEQRES 6 B 287 MET MET GLY GLU ASP LYS ILE LYS PHE LYS HIS ILE THR
SEQRES 7 B 287 PRO LEU GLN GLU GLN SER LYS GLU VAL ALA ILE ARG ILE
SEQRES 8 B 287 PHE GLN GLY CYS GLN PHE ARG SER VAL GLU ALA VAL GLN
SEQRES 9 B 287 GLU ILE THR GLU TYR ALA LYS SER ILE PRO GLY PHE VAL
SEQRES 10 B 287 ASN LEU ASP LEU ASN ASP GLN VAL THR LEU LEU LYS TYR
SEQRES 11 B 287 GLY VAL HIS GLU ILE ILE TYR THR MET LEU ALA SER LEU
SEQRES 12 B 287 MET ASN LYS ASP GLY VAL LEU ILE SER GLU GLY GLN GLY
SEQRES 13 B 287 PHE MET THR ARG GLU PHE LEU LYS SER LEU ARG LYS PRO
SEQRES 14 B 287 PHE GLY ASP PHE MET GLU PRO LYS PHE GLU PHE ALA VAL
SEQRES 15 B 287 LYS PHE ASN ALA LEU GLU LEU ASP ASP SER ASP LEU ALA
SEQRES 16 B 287 ILE PHE ILE ALA VAL ILE ILE LEU SER GLY ASP ARG PRO
SEQRES 17 B 287 GLY LEU LEU ASN VAL LYS PRO ILE GLU ASP ILE GLN ASP
SEQRES 18 B 287 ASN LEU LEU GLN ALA LEU GLU LEU GLN LEU LYS LEU ASN
SEQRES 19 B 287 HIS PRO GLU SER SER GLN LEU PHE ALA LYS LEU LEU GLN
SEQRES 20 B 287 LYS MET THR ASP LEU ARG GLN ILE VAL THR GLU HIS VAL
SEQRES 21 B 287 GLN LEU LEU GLN VAL ILE LYS LYS THR GLU THR ASP MET
SEQRES 22 B 287 SER LEU HIS PRO LEU LEU GLN GLU ILE TYR LYS ASP LEU
SEQRES 23 B 287 TYR
HET IMN A 1 25
HET IMN A 2 25
HET IMN B 3 25
HETNAM IMN INDOMETHACIN
FORMUL 3 IMN 3(C19 H16 CL N O4)
FORMUL 6 HOH *97(H2 O)
HELIX 1 1 ASN A 205 PHE A 226 1 22
HELIX 2 2 THR A 229 GLY A 239 1 11
HELIX 3 3 ASP A 251 ILE A 262 1 12
HELIX 4 4 GLU A 276 ILE A 303 1 28
HELIX 5 5 ASP A 310 ALA A 331 1 22
HELIX 6 6 ARG A 350 SER A 355 1 6
HELIX 7 7 PRO A 359 PHE A 363 5 5
HELIX 8 8 MET A 364 ASN A 375 1 12
HELIX 9 9 ALA A 376 GLU A 378 5 3
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 GLY B 239 1 11
HELIX 16 16 ASP B 251 ILE B 262 1 12
HELIX 17 17 GLU B 276 LYS B 301 1 26
HELIX 18 18 GLY B 305 LEU B 309 5 5
HELIX 19 19 ASP B 310 LEU B 333 1 24
HELIX 20 20 ARG B 350 SER B 355 1 6
HELIX 21 21 PRO B 359 PHE B 363 5 5
HELIX 22 22 MET B 364 ALA B 376 1 13
HELIX 23 23 ASP B 380 LEU B 393 1 14
HELIX 24 24 ASN B 402 HIS B 425 1 24
HELIX 25 25 GLN B 430 LYS B 457 1 28
HELIX 26 26 HIS B 466 TYR B 473 1 8
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 THR B 349 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
SITE 1 AC1 10 ARG A 280 GLY A 284 CYS A 285 ARG A 288
SITE 2 AC1 10 LEU A 330 LEU A 340 ILE A 341 SER A 342
SITE 3 AC1 10 MET A 348 MET A 364
SITE 1 AC2 15 ILE A 281 PHE A 282 CYS A 285 SER A 289
SITE 2 AC2 15 HIS A 323 TYR A 327 LEU A 330 LEU A 356
SITE 3 AC2 15 PHE A 360 PHE A 363 MET A 364 HIS A 449
SITE 4 AC2 15 LEU A 453 LEU A 469 TYR A 473
SITE 1 AC3 11 ILE B 281 ARG B 288 SER B 289 ALA B 292
SITE 2 AC3 11 ILE B 326 LEU B 330 LEU B 333 LEU B 340
SITE 3 AC3 11 ILE B 341 GLU B 343 MET B 364
CRYST1 93.045 61.031 118.403 90.00 102.99 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 0.010747 0.000000 0.002479 0.00000
SCALE2 0.000000 0.016385 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008668 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
