HEADER TRANSCRIPTION 31-MAY-17 5Q0T
TITLE LIGAND BINDING TO FARNESOID-X-RECEPTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BILE ACID RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FARNESOID X-ACTIVATED RECEPTOR,FARNESOL RECEPTOR HRR-1,
COMPND 5 NUCLEAR RECEPTOR SUBFAMILY 1 GROUP H MEMBER 4,RETINOID X RECEPTOR-
COMPND 6 INTERACTING PROTEIN 14,RXR-INTERACTING PROTEIN 14;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: COACTIVATOR PEPTIDE SRC-1 HD3;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: UNP RESIDUES 744-757;
COMPND 12 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: NR1H4, BAR, FXR, HRR1, RIP14;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606
KEYWDS D3R, FXR, DOCKING, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.G.RUDOLPH,J.BENZ,D.BURGER,R.THOMA,A.RUF,C.JOSEPH,B.KUHN,C.SHAO,
AUTHOR 2 H.YANG,S.K.BURLEY
REVDAT 7 17-NOV-21 5Q0T 1 REMARK
REVDAT 6 10-FEB-21 5Q0T 1 AUTHOR JRNL
REVDAT 5 21-FEB-18 5Q0T 1 REMARK
REVDAT 4 31-JAN-18 5Q0T 1 JRNL
REVDAT 3 20-DEC-17 5Q0T 1 JRNL
REVDAT 2 19-JUL-17 5Q0T 1 AUTHOR JRNL
REVDAT 1 05-JUL-17 5Q0T 0
JRNL AUTH Z.GAIEB,S.LIU,S.GATHIAKA,M.CHIU,H.YANG,C.SHAO,V.A.FEHER,
JRNL AUTH 2 W.P.WALTERS,B.KUHN,M.G.RUDOLPH,S.K.BURLEY,M.K.GILSON,
JRNL AUTH 3 R.E.AMARO
JRNL TITL D3R GRAND CHALLENGE 2: BLIND PREDICTION OF PROTEIN-LIGAND
JRNL TITL 2 POSES, AFFINITY RANKINGS, AND RELATIVE BINDING FREE
JRNL TITL 3 ENERGIES.
JRNL REF J. COMPUT. AIDED MOL. DES. V. 32 1 2018
JRNL REFN ESSN 1573-4951
JRNL PMID 29204945
JRNL DOI 10.1007/S10822-017-0088-4
REMARK 2
REMARK 2 RESOLUTION. 2.14 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.3
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) : 2.14
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 11.21
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 81.2
REMARK 3 NUMBER OF REFLECTIONS : 10809
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.780
REMARK 3 FREE R VALUE TEST SET COUNT : 517
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 : 5
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.14
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.39
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 60.12
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2280
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2133
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2171
REMARK 3 BIN R VALUE (WORKING SET) : 0.2109
REMARK 3 BIN FREE R VALUE : 0.2581
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.78
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 109
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1904
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 40
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 70.96
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.19310
REMARK 3 B22 (A**2) : 2.19310
REMARK 3 B33 (A**2) : -4.38620
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) : 0.300
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.341
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.246
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.359
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.253
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 : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.919
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 1974 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 2667 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 712 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 55 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 273 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 1974 ; 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 : 255 ; 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 : 2296 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.03
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.39
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 20.31
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 32.2229 10.4251 -1.3189
REMARK 3 T TENSOR
REMARK 3 T11: -0.0647 T22: -0.1856
REMARK 3 T33: -0.1068 T12: 0.0555
REMARK 3 T13: 0.0604 T23: 0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 3.9886 L22: 2.0069
REMARK 3 L33: 2.3868 L12: 0.7843
REMARK 3 L13: 1.2320 L23: 0.6241
REMARK 3 S TENSOR
REMARK 3 S11: 0.2547 S12: 0.0009 S13: -0.1659
REMARK 3 S21: 0.1815 S22: -0.2588 S23: -0.1720
REMARK 3 S31: 0.3810 S32: 0.0714 S33: 0.0041
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5Q0T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUN-17.
REMARK 100 THE DEPOSITION ID IS D_1001401355.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-FEB-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10861
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.140
REMARK 200 RESOLUTION RANGE LOW (A) : 30.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 80.5
REMARK 200 DATA REDUNDANCY : 3.970
REMARK 200 R MERGE (I) : 0.05130
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.0400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.14
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 48.2
REMARK 200 DATA REDUNDANCY IN SHELL : 0.68
REMARK 200 R MERGE FOR SHELL (I) : 0.47850
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.5 M SODIUM FORMATE PH 7.0,
REMARK 280 EVAPORATION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 31.78000
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 15.89000
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 23.83500
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 7.94500
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 39.72500
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: 1090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 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 GLY A 244
REMARK 465 SER A 245
REMARK 465 HIS A 246
REMARK 465 MET A 456
REMARK 465 SER A 457
REMARK 465 TRP A 458
REMARK 465 ARG A 459
REMARK 465 VAL A 460
REMARK 465 ASN A 461
REMARK 465 ASP A 462
REMARK 465 GLN A 476
REMARK 465 LYS B 744
REMARK 465 ASP B 756
REMARK 465 GLU B 757
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 SER A 346 OG
REMARK 470 GLU A 471 CG CD OE1 OE2
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 LYS A 342 -98.85 -127.68
REMARK 500 LYS A 343 -27.89 -26.58
REMARK 500 LEU A 395 46.24 -86.14
REMARK 500 PRO A 431 5.62 -68.90
REMARK 500 HIS B 746 55.93 37.51
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 9LM A 501
DBREF 5Q0T A 248 476 UNP Q96RI1 NR1H4_HUMAN 258 486
DBREF 5Q0T B 744 757 UNP A8K1V4 A8K1V4_HUMAN 744 757
SEQADV 5Q0T GLY A 244 UNP Q96RI1 EXPRESSION TAG
SEQADV 5Q0T SER A 245 UNP Q96RI1 EXPRESSION TAG
SEQADV 5Q0T HIS A 246 UNP Q96RI1 EXPRESSION TAG
SEQADV 5Q0T MET A 247 UNP Q96RI1 EXPRESSION TAG
SEQADV 5Q0T ALA A 281 UNP Q96RI1 GLU 291 CONFLICT
SEQADV 5Q0T ALA A 354 UNP Q96RI1 GLU 364 CONFLICT
SEQRES 1 A 233 GLY SER HIS MET GLU LEU THR PRO ASP GLN GLN THR LEU
SEQRES 2 A 233 LEU HIS PHE ILE MET ASP SER TYR ASN LYS GLN ARG MET
SEQRES 3 A 233 PRO GLN GLU ILE THR ASN LYS ILE LEU LYS GLU ALA PHE
SEQRES 4 A 233 SER ALA GLU GLU ASN PHE LEU ILE LEU THR GLU MET ALA
SEQRES 5 A 233 THR ASN HIS VAL GLN VAL LEU VAL GLU PHE THR LYS LYS
SEQRES 6 A 233 LEU PRO GLY PHE GLN THR LEU ASP HIS GLU ASP GLN ILE
SEQRES 7 A 233 ALA LEU LEU LYS GLY SER ALA VAL GLU ALA MET PHE LEU
SEQRES 8 A 233 ARG SER ALA GLU ILE PHE ASN LYS LYS LEU PRO SER GLY
SEQRES 9 A 233 HIS SER ASP LEU LEU GLU ALA ARG ILE ARG ASN SER GLY
SEQRES 10 A 233 ILE SER ASP GLU TYR ILE THR PRO MET PHE SER PHE TYR
SEQRES 11 A 233 LYS SER ILE GLY GLU LEU LYS MET THR GLN GLU GLU TYR
SEQRES 12 A 233 ALA LEU LEU THR ALA ILE VAL ILE LEU SER PRO ASP ARG
SEQRES 13 A 233 GLN TYR ILE LYS ASP ARG GLU ALA VAL GLU LYS LEU GLN
SEQRES 14 A 233 GLU PRO LEU LEU ASP VAL LEU GLN LYS LEU CYS LYS ILE
SEQRES 15 A 233 HIS GLN PRO GLU ASN PRO GLN HIS PHE ALA CYS LEU LEU
SEQRES 16 A 233 GLY ARG LEU THR GLU LEU ARG THR PHE ASN HIS HIS HIS
SEQRES 17 A 233 ALA GLU MET LEU MET SER TRP ARG VAL ASN ASP HIS LYS
SEQRES 18 A 233 PHE THR PRO LEU LEU CYS GLU ILE TRP ASP VAL GLN
SEQRES 1 B 14 LYS ASP HIS GLN LEU LEU ARG TYR LEU LEU ASP LYS ASP
SEQRES 2 B 14 GLU
HET 9LM A 501 29
HETNAM 9LM 2-PHENYL-N-(PROPAN-2-YL)-6-[(THIOPHEN-2-YL)SULFONYL]-4,
HETNAM 2 9LM 5,6,7-TETRAHYDRO-1H-PYRROLO[2,3-C]PYRIDINE-1-
HETNAM 3 9LM CARBOXAMIDE
FORMUL 3 9LM C21 H23 N3 O3 S2
FORMUL 4 HOH *40(H2 O)
HELIX 1 AA1 THR A 250 GLN A 267 1 18
HELIX 2 AA2 PRO A 270 GLU A 280 1 11
HELIX 3 AA3 SER A 283 LYS A 308 1 26
HELIX 4 AA4 GLY A 311 LEU A 315 5 5
HELIX 5 AA5 ASP A 316 LYS A 342 1 27
HELIX 6 AA6 PRO A 345 ARG A 357 1 13
HELIX 7 AA7 SER A 362 LEU A 379 1 18
HELIX 8 AA8 THR A 382 LEU A 395 1 14
HELIX 9 AA9 ASP A 404 GLN A 427 1 24
HELIX 10 AB1 GLN A 432 LEU A 455 1 24
HELIX 11 AB2 THR A 466 ASP A 474 1 9
HELIX 12 AB3 HIS B 746 LYS B 755 1 10
SITE 1 AC1 15 PHE A 288 LEU A 291 THR A 292 MET A 294
SITE 2 AC1 15 ALA A 295 MET A 332 ARG A 335 SER A 336
SITE 3 AC1 15 ILE A 339 LEU A 352 ILE A 356 TYR A 373
SITE 4 AC1 15 HIS A 451 PHE A 465 TRP A 473
CRYST1 93.940 93.940 47.670 90.00 90.00 120.00 P 65 6
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 0.010645 0.006146 0.000000 0.00000
SCALE2 0.000000 0.012292 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020978 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
