HEADER TRANSCRIPTION 06-OCT-17 6ENQ
TITLE STRUCTURE OF HUMAN PPAR GAMMA LBD IN COMPLEX WITH LANIFIBRANOR
TITLE 2 (IVA337)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PPAR-GAMMA,NUCLEAR RECEPTOR SUBFAMILY 1 GROUP C MEMBER 3;
COMPND 5 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: PPARG, NR1C3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS NUCLEAR HORMONE RECEPTOR, PPARGAMMA MODULATOR, LANIFIBRANOR,
KEYWDS 2 TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR B.BOUBIA,O.POUPARDIN,M.BARTH,J.AMAUDRUT,P.BROQUA,M.TALLANDIER,D.ZEYER
REVDAT 3 17-JAN-24 6ENQ 1 REMARK
REVDAT 2 04-APR-18 6ENQ 1 SOURCE JRNL REMARK
REVDAT 1 14-MAR-18 6ENQ 0
JRNL AUTH B.BOUBIA,O.POUPARDIN,M.BARTH,J.BINET,P.PERALBA,L.MOUNIER,
JRNL AUTH 2 E.JACQUIER,E.GAUTHIER,V.LEPAIS,M.CHATAR,S.FERRY,A.THOURIGNY,
JRNL AUTH 3 F.GUILLIER,J.LLACER,J.AMAUDRUT,P.DODEY,O.LACOMBE,P.MASSON,
JRNL AUTH 4 C.MONTALBETTI,G.WETTSTEIN,J.M.LUCCARINI,C.LEGENDRE,
JRNL AUTH 5 J.L.JUNIEN,P.BROQUA
JRNL TITL DESIGN, SYNTHESIS, AND EVALUATION OF A NOVEL SERIES OF
JRNL TITL 2 INDOLE SULFONAMIDE PEROXISOME PROLIFERATOR ACTIVATED
JRNL TITL 3 RECEPTOR (PPAR) ALPHA / GAMMA / DELTA TRIPLE ACTIVATORS:
JRNL TITL 4 DISCOVERY OF LANIFIBRANOR, A NEW ANTIFIBROTIC CLINICAL
JRNL TITL 5 CANDIDATE.
JRNL REF J. MED. CHEM. V. 61 2246 2018
JRNL REFN ISSN 1520-4804
JRNL PMID 29446942
JRNL DOI 10.1021/ACS.JMEDCHEM.7B01285
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX 2005
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
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) (%) : 92.8
REMARK 3 NUMBER OF REFLECTIONS : 29908
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.227
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.271
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4021
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 172
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.00
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
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 : NULL
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 6ENQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-OCT-17.
REMARK 100 THE DEPOSITION ID IS D_1200006863.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-NOV-05
REMARK 200 TEMPERATURE (KELVIN) : 123
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
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 : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32992
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
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 (%) : 97.6
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.34900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1PRG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NA CITRATE 0,9 M 1,2 - PROPANEDIOL 3,5
REMARK 280 % HEPES 0,1 M, 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 46.44000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 46.44000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 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 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 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 GLN A 203
REMARK 465 GLU A 259
REMARK 465 ASP A 260
REMARK 465 LYS A 261
REMARK 465 ILE A 262
REMARK 465 LYS A 263
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 LEU A 476
REMARK 465 TYR A 477
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 GLY B 239
REMARK 465 LYS B 240
REMARK 465 THR B 241
REMARK 465 THR B 242
REMARK 465 ASP B 243
REMARK 465 LYS B 244
REMARK 465 ASP B 260
REMARK 465 LYS B 261
REMARK 465 ILE B 262
REMARK 465 LYS B 263
REMARK 465 PHE B 264
REMARK 465 LYS B 265
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 LYS B 275
REMARK 465 LEU B 476
REMARK 465 TYR B 477
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 HOH A 649 O HOH A 689 2.09
REMARK 500 O HOH A 618 O HOH A 692 2.10
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 207 -43.12 -179.36
REMARK 500 ASP A 243 177.88 49.74
REMARK 500 ASP A 251 -178.75 -172.82
REMARK 500 SER A 394 -70.81 -74.30
REMARK 500 GLU A 460 76.87 -112.49
REMARK 500 LYS A 474 79.08 -66.33
REMARK 500 MET B 257 23.73 -79.21
REMARK 500 ARG B 357 -175.45 -47.54
REMARK 500 LYS B 458 37.03 -94.91
REMARK 500 THR B 459 -61.04 -131.89
REMARK 500 THR B 461 -113.07 -147.71
REMARK 500 SER B 464 0.89 -64.84
REMARK 500 PRO B 467 -56.92 -29.29
REMARK 500 LYS B 474 -113.16 -79.82
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 GLY A 239 LYS A 240 -63.68
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 BJB A 501
DBREF 6ENQ A 196 477 UNP P37231 PPARG_HUMAN 224 505
DBREF 6ENQ B 196 477 UNP P37231 PPARG_HUMAN 224 505
SEQRES 1 A 282 GLU ILE SER SER ASP ILE ASP GLN LEU ASN PRO GLU SER
SEQRES 2 A 282 ALA ASP LEU ARG ALA LEU ALA LYS HIS LEU TYR ASP SER
SEQRES 3 A 282 TYR ILE LYS SER PHE PRO LEU THR LYS ALA LYS ALA ARG
SEQRES 4 A 282 ALA ILE LEU THR GLY LYS THR THR ASP LYS SER PRO PHE
SEQRES 5 A 282 VAL ILE TYR ASP MET ASN SER LEU MET MET GLY GLU ASP
SEQRES 6 A 282 LYS ILE LYS PHE LYS HIS ILE THR PRO LEU GLN GLU GLN
SEQRES 7 A 282 SER LYS GLU VAL ALA ILE ARG ILE PHE GLN GLY CYS GLN
SEQRES 8 A 282 PHE ARG SER VAL GLU ALA VAL GLN GLU ILE THR GLU TYR
SEQRES 9 A 282 ALA LYS SER ILE PRO GLY PHE VAL ASN LEU ASP LEU ASN
SEQRES 10 A 282 ASP GLN VAL THR LEU LEU LYS TYR GLY VAL HIS GLU ILE
SEQRES 11 A 282 ILE TYR THR MET LEU ALA SER LEU MET ASN LYS ASP GLY
SEQRES 12 A 282 VAL LEU ILE SER GLU GLY GLN GLY PHE MET THR ARG GLU
SEQRES 13 A 282 PHE LEU LYS SER LEU ARG LYS PRO PHE GLY ASP PHE MET
SEQRES 14 A 282 GLU PRO LYS PHE GLU PHE ALA VAL LYS PHE ASN ALA LEU
SEQRES 15 A 282 GLU LEU ASP ASP SER ASP LEU ALA ILE PHE ILE ALA VAL
SEQRES 16 A 282 ILE ILE LEU SER GLY ASP ARG PRO GLY LEU LEU ASN VAL
SEQRES 17 A 282 LYS PRO ILE GLU ASP ILE GLN ASP ASN LEU LEU GLN ALA
SEQRES 18 A 282 LEU GLU LEU GLN LEU LYS LEU ASN HIS PRO GLU SER SER
SEQRES 19 A 282 GLN LEU PHE ALA LYS LEU LEU GLN LYS MET THR ASP LEU
SEQRES 20 A 282 ARG GLN ILE VAL THR GLU HIS VAL GLN LEU LEU GLN VAL
SEQRES 21 A 282 ILE LYS LYS THR GLU THR ASP MET SER LEU HIS PRO LEU
SEQRES 22 A 282 LEU GLN GLU ILE TYR LYS ASP LEU TYR
SEQRES 1 B 282 GLU ILE SER SER ASP ILE ASP GLN LEU ASN PRO GLU SER
SEQRES 2 B 282 ALA ASP LEU ARG ALA LEU ALA LYS HIS LEU TYR ASP SER
SEQRES 3 B 282 TYR ILE LYS SER PHE PRO LEU THR LYS ALA LYS ALA ARG
SEQRES 4 B 282 ALA ILE LEU THR GLY LYS THR THR ASP LYS SER PRO PHE
SEQRES 5 B 282 VAL ILE TYR ASP MET ASN SER LEU MET MET GLY GLU ASP
SEQRES 6 B 282 LYS ILE LYS PHE LYS HIS ILE THR PRO LEU GLN GLU GLN
SEQRES 7 B 282 SER LYS GLU VAL ALA ILE ARG ILE PHE GLN GLY CYS GLN
SEQRES 8 B 282 PHE ARG SER VAL GLU ALA VAL GLN GLU ILE THR GLU TYR
SEQRES 9 B 282 ALA LYS SER ILE PRO GLY PHE VAL ASN LEU ASP LEU ASN
SEQRES 10 B 282 ASP GLN VAL THR LEU LEU LYS TYR GLY VAL HIS GLU ILE
SEQRES 11 B 282 ILE TYR THR MET LEU ALA SER LEU MET ASN LYS ASP GLY
SEQRES 12 B 282 VAL LEU ILE SER GLU GLY GLN GLY PHE MET THR ARG GLU
SEQRES 13 B 282 PHE LEU LYS SER LEU ARG LYS PRO PHE GLY ASP PHE MET
SEQRES 14 B 282 GLU PRO LYS PHE GLU PHE ALA VAL LYS PHE ASN ALA LEU
SEQRES 15 B 282 GLU LEU ASP ASP SER ASP LEU ALA ILE PHE ILE ALA VAL
SEQRES 16 B 282 ILE ILE LEU SER GLY ASP ARG PRO GLY LEU LEU ASN VAL
SEQRES 17 B 282 LYS PRO ILE GLU ASP ILE GLN ASP ASN LEU LEU GLN ALA
SEQRES 18 B 282 LEU GLU LEU GLN LEU LYS LEU ASN HIS PRO GLU SER SER
SEQRES 19 B 282 GLN LEU PHE ALA LYS LEU LEU GLN LYS MET THR ASP LEU
SEQRES 20 B 282 ARG GLN ILE VAL THR GLU HIS VAL GLN LEU LEU GLN VAL
SEQRES 21 B 282 ILE LYS LYS THR GLU THR ASP MET SER LEU HIS PRO LEU
SEQRES 22 B 282 LEU GLN GLU ILE TYR LYS ASP LEU TYR
HET BJB A 501 28
HETNAM BJB 4-[1-(1,3-BENZOTHIAZOL-6-YLSULFONYL)-5-CHLORO-INDOL-2-
HETNAM 2 BJB YL]BUTANOIC ACID
FORMUL 3 BJB C19 H15 CL N2 O4 S2
FORMUL 4 HOH *172(H2 O)
HELIX 1 AA1 GLU A 207 PHE A 226 1 20
HELIX 2 AA2 THR A 229 GLY A 239 1 11
HELIX 3 AA3 ASP A 251 GLY A 258 1 8
HELIX 4 AA4 GLU A 276 ILE A 303 1 28
HELIX 5 AA5 GLY A 305 LEU A 309 5 5
HELIX 6 AA6 ASP A 310 LEU A 333 1 24
HELIX 7 AA7 SER A 342 GLY A 344 5 3
HELIX 8 AA8 ARG A 350 SER A 355 1 6
HELIX 9 AA9 PRO A 359 PHE A 363 5 5
HELIX 10 AB1 MET A 364 ASN A 375 1 12
HELIX 11 AB2 ALA A 376 GLU A 378 5 3
HELIX 12 AB3 ASP A 380 LEU A 393 1 14
HELIX 13 AB4 ASN A 402 HIS A 425 1 24
HELIX 14 AB5 GLN A 430 GLU A 460 1 31
HELIX 15 AB6 HIS A 466 LYS A 474 1 9
HELIX 16 AB7 SER B 208 PHE B 226 1 19
HELIX 17 AB8 THR B 229 LEU B 237 1 9
HELIX 18 AB9 ASP B 251 MET B 257 1 7
HELIX 19 AC1 VAL B 277 SER B 302 1 26
HELIX 20 AC2 GLY B 305 LEU B 309 5 5
HELIX 21 AC3 ASP B 310 ALA B 331 1 22
HELIX 22 AC4 SER B 342 GLY B 344 5 3
HELIX 23 AC5 ARG B 350 SER B 355 1 6
HELIX 24 AC6 MET B 364 ASN B 375 1 12
HELIX 25 AC7 ALA B 376 GLU B 378 5 3
HELIX 26 AC8 ASP B 380 LEU B 393 1 14
HELIX 27 AC9 ASN B 402 HIS B 425 1 24
HELIX 28 AD1 GLN B 430 LYS B 458 1 29
HELIX 29 AD2 HIS B 466 TYR B 473 1 8
SHEET 1 AA1 4 PHE A 247 ILE A 249 0
SHEET 2 AA1 4 GLY A 346 THR A 349 1 O PHE A 347 N ILE A 249
SHEET 3 AA1 4 GLY A 338 ILE A 341 -1 N VAL A 339 O MET A 348
SHEET 4 AA1 4 MET A 334 ASN A 335 -1 N ASN A 335 O GLY A 338
SHEET 1 AA2 4 PHE B 247 ILE B 249 0
SHEET 2 AA2 4 GLY B 346 THR B 349 1 O PHE B 347 N ILE B 249
SHEET 3 AA2 4 GLY B 338 ILE B 341 -1 N VAL B 339 O MET B 348
SHEET 4 AA2 4 MET B 334 ASN B 335 -1 N ASN B 335 O GLY B 338
CISPEP 1 LYS A 358 PRO A 359 0 -4.50
CISPEP 2 LYS B 358 PRO B 359 0 -3.83
SITE 1 AC1 12 LEU A 228 CYS A 285 ARG A 288 SER A 289
SITE 2 AC1 12 TYR A 327 LEU A 330 LEU A 333 VAL A 339
SITE 3 AC1 12 LEU A 340 GLU A 343 GLY A 344 HOH A 649
CRYST1 92.880 60.000 117.490 90.00 102.93 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 0.010767 0.000000 0.002472 0.00000
SCALE2 0.000000 0.016667 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008733 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
