HEADER HORMONE/GROWTH FACTOR RECEPTOR 02-MAR-04 1SJ0
TITLE HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN IN COMPLEX WITH
TITLE 2 THE ANTAGONIST LIGAND 4-D
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTROGEN RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN;
COMPND 5 SYNONYM: ER, ESTRADIOL RECEPTOR, ER-ALPHA;
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: ESR1, NR3A1, ESR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS NUCLEAR RECEPTOR, TRANSCRIPTION FACTOR, ER-ALPHA, ANTAGONIST,
KEYWDS 2 HORMONE-GROWTH FACTOR RECEPTOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.KIM,J.Y.WU,E.T.BIRZIN,W.CHAN,L.Y.PAI,Y.T.YANG,R.T.MOSLEY,
AUTHOR 2 P.M.FITZGERALD,N.SHARMA,F.DININNO,S.P.ROHRER,J.M.SCHAEFFER,
AUTHOR 3 M.L.HAMMOND
REVDAT 5 14-FEB-24 1SJ0 1 REMARK
REVDAT 4 11-OCT-17 1SJ0 1 REMARK
REVDAT 3 13-JUL-11 1SJ0 1 VERSN
REVDAT 2 24-FEB-09 1SJ0 1 VERSN
REVDAT 1 27-APR-04 1SJ0 0
JRNL AUTH S.KIM,J.Y.WU,E.T.BIRZIN,K.FRISCH,W.CHAN,L.Y.PAI,Y.T.YANG,
JRNL AUTH 2 R.T.MOSLEY,P.M.FITZGERALD,N.SHARMA,J.DAHLLUND,A.G.THORSELL,
JRNL AUTH 3 F.DININNO,S.P.ROHRER,J.M.SCHAEFFER,M.L.HAMMOND
JRNL TITL ESTROGEN RECEPTOR LIGANDS. II. DISCOVERY OF BENZOXATHIINS AS
JRNL TITL 2 POTENT, SELECTIVE ESTROGEN RECEPTOR ALPHA MODULATORS.
JRNL REF J.MED.CHEM. V. 47 2171 2004
JRNL REFN ISSN 0022-2623
JRNL PMID 15084115
JRNL DOI 10.1021/JM034243O
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL 97-1
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 82.8
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.218
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 950
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 18187
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.214
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 914
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 17369
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1934
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 152
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2217.0
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 0.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 0
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 8469
REMARK 3 NUMBER OF RESTRAINTS : 8090
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 ANGLE DISTANCES (A) : 0.020
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.246
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.023
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.029
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.007
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.092
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1SJ0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1000021745.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-MAY-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.1
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) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : X-GEN
REMARK 200 DATA SCALING SOFTWARE : X-GEN
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19370
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 99.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 82.8
REMARK 200 DATA REDUNDANCY : 6.228
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : 0.07000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 39.9830
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 54.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.32
REMARK 200 R MERGE FOR SHELL (I) : 0.35580
REMARK 200 R SYM FOR SHELL (I) : 0.35580
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.042
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: ISOMORPHOUS 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 (%): 49.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2-10% PEG 3350, 0.02-0.20 MMGCL2, PH
REMARK 280 7.1 IMIDAZOLE , VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 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+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 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-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 184.05333
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 92.02667
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 138.04000
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 46.01333
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 230.06667
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 184.05333
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 92.02667
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 46.01333
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 138.04000
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 230.06667
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 5050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 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 BIOMT1 2 0.500000 -0.866025 0.000000 29.24000
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 50.64517
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 46.01333
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1001 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1002 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1049 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1099 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1102 LIES ON A SPECIAL POSITION.
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 LYS A 531
REMARK 465 ASN A 532
REMARK 465 PRO A 552
REMARK 465 THR A 553
REMARK 465 SER A 554
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 ARG A 335 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 352 NE - CZ - NH1 ANGL. DEV. = -3.9 DEGREES
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 SER A 309 -10.67 -141.40
REMARK 500 LEU A 408 83.43 -153.71
REMARK 500 LEU A 462 -101.63 -29.60
REMARK 500 SER A 463 -136.53 -93.13
REMARK 500 SER A 464 86.78 -166.76
REMARK 500 SER A 527 41.21 150.49
REMARK 500 ASP A 545 69.41 -69.32
REMARK 500 HIS A 550 36.27 -82.07
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 E4D A 600
DBREF 1SJ0 A 307 554 UNP P03372 ESR1_HUMAN 307 554
SEQRES 1 A 248 ALA LEU SER LEU THR ALA ASP GLN MET VAL SER ALA LEU
SEQRES 2 A 248 LEU ASP ALA GLU PRO PRO ILE LEU TYR SER GLU TYR ASP
SEQRES 3 A 248 PRO THR ARG PRO PHE SER GLU ALA SER MET MET GLY LEU
SEQRES 4 A 248 LEU THR ASN LEU ALA ASP ARG GLU LEU VAL HIS MET ILE
SEQRES 5 A 248 ASN TRP ALA LYS ARG VAL PRO GLY PHE VAL ASP LEU THR
SEQRES 6 A 248 LEU HIS ASP GLN VAL HIS LEU LEU GLU CYS ALA TRP LEU
SEQRES 7 A 248 GLU ILE LEU MET ILE GLY LEU VAL TRP ARG SER MET GLU
SEQRES 8 A 248 HIS PRO GLY LYS LEU LEU PHE ALA PRO ASN LEU LEU LEU
SEQRES 9 A 248 ASP ARG ASN GLN GLY LYS CYS VAL GLU GLY MET VAL GLU
SEQRES 10 A 248 ILE PHE ASP MET LEU LEU ALA THR SER SER ARG PHE ARG
SEQRES 11 A 248 MET MET ASN LEU GLN GLY GLU GLU PHE VAL CYS LEU LYS
SEQRES 12 A 248 SER ILE ILE LEU LEU ASN SER GLY VAL TYR THR PHE LEU
SEQRES 13 A 248 SER SER THR LEU LYS SER LEU GLU GLU LYS ASP HIS ILE
SEQRES 14 A 248 HIS ARG VAL LEU ASP LYS ILE THR ASP THR LEU ILE HIS
SEQRES 15 A 248 LEU MET ALA LYS ALA GLY LEU THR LEU GLN GLN GLN HIS
SEQRES 16 A 248 GLN ARG LEU ALA GLN LEU LEU LEU ILE LEU SER HIS ILE
SEQRES 17 A 248 ARG HIS MET SER ASN LYS GLY MET GLU HIS LEU TYR SER
SEQRES 18 A 248 MET LYS CYS LYS ASN VAL VAL PRO LEU TYR ASP LEU LEU
SEQRES 19 A 248 LEU GLU MET LEU ASP ALA HIS ARG LEU HIS ALA PRO THR
SEQRES 20 A 248 SER
HET E4D A 600 33
HETNAM E4D (2S,3R)-2-(4-(2-(PIPERIDIN-1-YL)ETHOXY)PHENYL)-2,3-
HETNAM 2 E4D DIHYDRO-3-(4-HYDROXYPHENYL)BENZO[B][1,4]OXATHIIN-6-OL
HETSYN E4D COMPOUND 4-D
FORMUL 2 E4D C27 H29 N O4 S
FORMUL 3 HOH *152(H2 O)
HELIX 1 1 THR A 311 GLU A 323 1 13
HELIX 2 2 PRO A 336 ALA A 340 5 5
HELIX 3 3 SER A 341 ARG A 363 1 23
HELIX 4 4 THR A 371 MET A 396 1 26
HELIX 5 5 ARG A 412 CYS A 417 1 6
HELIX 6 6 MET A 421 ASN A 439 1 19
HELIX 7 7 GLN A 441 SER A 456 1 16
HELIX 8 8 GLY A 457 PHE A 461 5 5
HELIX 9 9 THR A 465 ALA A 493 1 29
HELIX 10 10 THR A 496 TYR A 526 1 31
HELIX 11 11 PRO A 535 ASP A 545 1 11
SHEET 1 A 2 LYS A 401 ALA A 405 0
SHEET 2 A 2 LEU A 408 ASP A 411 -1 O LEU A 410 N LEU A 402
SITE 1 AC1 14 MET A 343 LEU A 346 ALA A 350 ASP A 351
SITE 2 AC1 14 GLU A 353 LEU A 354 TRP A 383 LEU A 387
SITE 3 AC1 14 ARG A 394 GLY A 521 HIS A 524 LEU A 525
SITE 4 AC1 14 CYS A 530 HOH A1005
CRYST1 58.480 58.480 276.080 90.00 90.00 120.00 P 65 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 0.017100 0.009873 0.000000 0.00000
SCALE2 0.000000 0.019745 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003622 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
