HEADER TRANSCRIPTION/TRANSCRIPTION INHIBITOR 18-JUN-15 5C4T
TITLE IDENTIFICATION OF A NOVEL ALLOSTERIC BINDING SITE FOR RORGT INHIBITORS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUCLEAR RECEPTOR ROR-GAMMA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LIGAND-BINDING RESIDUES 267-507;
COMPND 5 SYNONYM: NUCLEAR RECEPTOR RZR-GAMMA,NUCLEAR RECEPTOR SUBFAMILY 1
COMPND 6 GROUP F MEMBER 3,RAR-RELATED ORPHAN RECEPTOR C,RETINOID-RELATED
COMPND 7 ORPHAN RECEPTOR-GAMMA;
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: RORC, NR1F3, RORG, RZRG;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALLOSTERIC, INHIBITOR, TRANSCRIPTION-TRANSCRIPTION INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR G.PARTHASARATHY,S.SOISSON
REVDAT 2 06-MAR-24 5C4T 1 REMARK
REVDAT 1 16-DEC-15 5C4T 0
JRNL AUTH M.SCHEEPSTRA,S.LEYSEN,G.C.VAN ALMEN,J.R.MILLER,J.PIESVAUX,
JRNL AUTH 2 V.KUTILEK,H.VAN EENENNAAM,H.ZHANG,K.BARR,S.NAGPAL,
JRNL AUTH 3 S.M.SOISSON,M.KORNIENKO,K.WILEY,N.ELSEN,S.SHARMA,
JRNL AUTH 4 C.C.CORRELL,B.W.TROTTER,M.VAN DER STELT,A.OUBRIE,C.OTTMANN,
JRNL AUTH 5 G.PARTHASARATHY,L.BRUNSVELD
JRNL TITL IDENTIFICATION OF AN ALLOSTERIC BINDING SITE FOR ROR GAMMA T
JRNL TITL 2 INHIBITION.
JRNL REF NAT COMMUN V. 6 8833 2015
JRNL REFN ESSN 2041-1723
JRNL PMID 26640126
JRNL DOI 10.1038/NCOMMS9833
REMARK 2
REMARK 2 RESOLUTION. 1.77 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.5
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.77
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.45
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 33582
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 1715
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 : 17
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.77
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.82
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.55
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2724
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2314
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2596
REMARK 3 BIN R VALUE (WORKING SET) : 0.2294
REMARK 3 BIN FREE R VALUE : 0.2732
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 128
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 : 1979
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 85
REMARK 3 SOLVENT ATOMS : 101
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.48
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.43990
REMARK 3 B22 (A**2) : 1.43990
REMARK 3 B33 (A**2) : -2.87980
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.242
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.105
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.102
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.103
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.101
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2145 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 2895 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 771 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 48 ; 8.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 352 ; 8.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2145 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 250 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 2568 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.99
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.16
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.38
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5C4T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUN-15.
REMARK 100 THE DEPOSITION ID IS D_1000211029.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAR-12
REMARK 200 TEMPERATURE (KELVIN) : 273
REMARK 200 PH : 8 - 9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
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 : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33582
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.770
REMARK 200 RESOLUTION RANGE LOW (A) : 46.450
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 19.00
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.8300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: NULL
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 (%): 58.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2 TO 1.8M AMMONIUM SULFATE, 0.1 M
REMARK 280 TRIS HCL, PH 8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 33.46333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 66.92667
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 50.19500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 83.65833
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 16.73167
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 33.46333
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 66.92667
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 83.65833
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 50.19500
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 16.73167
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 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 4Y6 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 610
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5C4O RELATED DB: PDB
REMARK 900 RELATED ID: 5C4S RELATED DB: PDB
REMARK 900 RELATED ID: 5C4U RELATED DB: PDB
DBREF 5C4T A 267 507 UNP P51449 RORG_HUMAN 267 507
SEQADV 5C4T HIS A 455 UNP P51449 CYS 455 VARIANT
SEQRES 1 A 241 LEU THR GLU ILE GLU HIS LEU VAL GLN SER VAL CYS LYS
SEQRES 2 A 241 SER TYR ARG GLU THR CYS GLN LEU ARG LEU GLU ASP LEU
SEQRES 3 A 241 LEU ARG GLN ARG SER ASN ILE PHE SER ARG GLU GLU VAL
SEQRES 4 A 241 THR GLY TYR GLN ARG LYS SER MET TRP GLU MET TRP GLU
SEQRES 5 A 241 ARG CYS ALA HIS HIS LEU THR GLU ALA ILE GLN TYR VAL
SEQRES 6 A 241 VAL GLU PHE ALA LYS ARG LEU SER GLY PHE MET GLU LEU
SEQRES 7 A 241 CYS GLN ASN ASP GLN ILE VAL LEU LEU LYS ALA GLY ALA
SEQRES 8 A 241 MET GLU VAL VAL LEU VAL ARG MET CYS ARG ALA TYR ASN
SEQRES 9 A 241 ALA ASP ASN ARG THR VAL PHE PHE GLU GLY LYS TYR GLY
SEQRES 10 A 241 GLY MET GLU LEU PHE ARG ALA LEU GLY CYS SER GLU LEU
SEQRES 11 A 241 ILE SER SER ILE PHE ASP PHE SER HIS SER LEU SER ALA
SEQRES 12 A 241 LEU HIS PHE SER GLU ASP GLU ILE ALA LEU TYR THR ALA
SEQRES 13 A 241 LEU VAL LEU ILE ASN ALA HIS ARG PRO GLY LEU GLN GLU
SEQRES 14 A 241 LYS ARG LYS VAL GLU GLN LEU GLN TYR ASN LEU GLU LEU
SEQRES 15 A 241 ALA PHE HIS HIS HIS LEU HIS LYS THR HIS ARG GLN SER
SEQRES 16 A 241 ILE LEU ALA LYS LEU PRO PRO LYS GLY LYS LEU ARG SER
SEQRES 17 A 241 LEU CYS SER GLN HIS VAL GLU ARG LEU GLN ILE PHE GLN
SEQRES 18 A 241 HIS LEU HIS PRO ILE VAL VAL GLN ALA ALA PHE PRO PRO
SEQRES 19 A 241 LEU TYR LYS GLU LEU PHE SER
HET 4Y6 A 601 66
HET SO4 A 602 5
HET SO4 A 603 5
HET GOL A 604 6
HET GOL A 605 6
HET GOL A 606 6
HET GOL A 607 6
HET GOL A 608 6
HET GOL A 609 6
HET GOL A 610 6
HETNAM 4Y6 (1S)-4-{1-[2-CHLORO-6-(TRIFLUOROMETHYL)BENZOYL]-4-
HETNAM 2 4Y6 FLUORO-1H-INDAZOL-3-YL}-1-METHYLCYCLOHEX-3-ENE-1-
HETNAM 3 4Y6 CARBOXYLIC ACID
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 4Y6 C23 H17 CL F4 N2 O3
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 GOL 7(C3 H8 O3)
FORMUL 12 HOH *101(H2 O)
HELIX 1 AA1 THR A 268 THR A 284 1 17
HELIX 2 AA2 ARG A 288 GLN A 295 1 8
HELIX 3 AA3 ARG A 296 ASN A 298 5 3
HELIX 4 AA4 SER A 301 LYS A 311 1 11
HELIX 5 AA5 SER A 312 LEU A 338 1 27
HELIX 6 AA6 CYS A 345 MET A 365 1 21
HELIX 7 AA7 GLY A 384 GLY A 392 5 9
HELIX 8 AA8 CYS A 393 ALA A 409 1 17
HELIX 9 AA9 SER A 413 ILE A 426 1 14
HELIX 10 AB1 GLU A 435 THR A 457 1 23
HELIX 11 AB2 ARG A 459 LEU A 466 5 8
HELIX 12 AB3 PRO A 468 HIS A 490 1 23
HELIX 13 AB4 PHE A 498 SER A 507 1 10
SHEET 1 AA1 3 TYR A 369 ASN A 370 0
SHEET 2 AA1 3 THR A 375 PHE A 378 -1 O THR A 375 N ASN A 370
SHEET 3 AA1 3 LYS A 381 GLY A 383 -1 O LYS A 381 N PHE A 378
SITE 1 AC1 20 TRP A 317 LEU A 324 THR A 325 ILE A 328
SITE 2 AC1 20 GLN A 329 LEU A 353 LYS A 354 MET A 358
SITE 3 AC1 20 LEU A 483 GLN A 484 GLN A 487 VAL A 494
SITE 4 AC1 20 GLN A 495 ALA A 496 ALA A 497 PHE A 498
SITE 5 AC1 20 LEU A 501 TYR A 502 LEU A 505 PHE A 506
SITE 1 AC2 3 GLN A 349 ILE A 350 LEU A 353
SITE 1 AC3 4 GLN A 434 GLU A 435 LYS A 436 ARG A 437
SITE 1 AC4 6 GLU A 271 VAL A 274 TRP A 314 HIS A 453
SITE 2 AC4 6 LYS A 456 LEU A 489
SITE 1 AC5 4 GLU A 304 GLY A 307 TYR A 308 LYS A 311
SITE 1 AC6 2 LYS A 354 CYS A 476
SITE 1 AC7 2 ILE A 397 ILE A 400
SITE 1 AC8 3 GLN A 441 TYR A 444 GLN A 460
SITE 1 AC9 5 HIS A 323 PHE A 377 PHE A 378 GLU A 379
SITE 2 AC9 5 GLY A 380
SITE 1 AD1 5 GLU A 318 HIS A 322 ILE A 492 VAL A 493
SITE 2 AD1 5 HOH A 758
CRYST1 107.270 107.270 100.390 90.00 90.00 120.00 P 61 2 2 12
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 0.009322 0.005382 0.000000 0.00000
SCALE2 0.000000 0.010764 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009961 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
