HEADER TRANSCRIPTION 29-JAN-07 2JFA
TITLE ESTROGEN RECEPTOR ALPHA LBD IN COMPLEX WITH AN AFFINITY-SELECTED
TITLE 2 COREPRESSOR PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTROGEN RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LIGAND-BINDING DOMAIN, RESIDUES 304-533;
COMPND 5 SYNONYM: ER, ESTRADIOL RECEPTOR, ER-ALPHA, ESTROGEN RECEPTOR ALPHA;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: ESTROGEN RECEPTOR;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: LIGAND-BINDING DOMAIN, RESIDUES 304-533;
COMPND 11 SYNONYM: ER, ESTRADIOL RECEPTOR, ER-ALPHA, ESTROGEN RECEPTOR ALPHA;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: COREPRESSOR PEPTIDE;
COMPND 15 CHAIN: P, Q;
COMPND 16 ENGINEERED: YES;
COMPND 17 OTHER_DETAILS: BT1 PEPTIDE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: C41;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET15B;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 15 EXPRESSION_SYSTEM_VARIANT: C41;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PET15B;
SOURCE 17 MOL_ID: 3;
SOURCE 18 SYNTHETIC: YES;
SOURCE 19 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 20 ORGANISM_TAXID: 32630
KEYWDS TRANSCRIPTION, TRANSCRIPTION FACTOR, PHAGE DISPLAY, METAL-BINDING,
KEYWDS 2 COREPRESSOR, LIPID-BINDING, TRANSCRIPTION REGULATION, LIGAND-BINDING
KEYWDS 3 DOMAIN (LBD), NUCLEAR PROTEIN, PHOSPHORYLATION, STEROID- BINDING,
KEYWDS 4 RECEPTOR, ZINC-FINGER, DNA-BINDING, NUCLEAR RECEPTOR, PEPTIDE
KEYWDS 5 ANTAGONIST
EXPDTA X-RAY DIFFRACTION
AUTHOR N.HELDRING,T.PAWSON,D.MCDONNELL,E.TREUTER,J.A.GUSTAFSSON,A.C.W.PIKE
REVDAT 7 13-DEC-23 2JFA 1 REMARK LINK
REVDAT 6 24-JAN-18 2JFA 1 SOURCE
REVDAT 5 21-DEC-16 2JFA 1 SOURCE AUTHOR
REVDAT 4 13-JUL-11 2JFA 1 VERSN
REVDAT 3 24-FEB-09 2JFA 1 VERSN
REVDAT 2 10-APR-07 2JFA 1 JRNL
REVDAT 1 20-FEB-07 2JFA 0
JRNL AUTH N.HELDRING,T.PAWSON,D.MCDONNELL,E.TREUTER,J.A.GUSTAFSSON,
JRNL AUTH 2 A.C.W.PIKE
JRNL TITL STRUCTURAL INSIGHTS INTO COREPRESSOR RECOGNITION BY
JRNL TITL 2 ANTAGONIST-BOUND ESTROGEN RECEPTORS.
JRNL REF J.BIOL.CHEM. V. 282 10449 2007
JRNL REFN ISSN 0021-9258
JRNL PMID 17283072
JRNL DOI 10.1074/JBC.M611424200
REMARK 2
REMARK 2 RESOLUTION. 2.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 32733
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) : 0.193
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1735
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.62
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2409
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2760
REMARK 3 BIN FREE R VALUE SET COUNT : 115
REMARK 3 BIN FREE R VALUE : 0.3170
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3695
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 88
REMARK 3 SOLVENT ATOMS : 86
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 59.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.46
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.73000
REMARK 3 B22 (A**2) : 2.73000
REMARK 3 B33 (A**2) : -4.09000
REMARK 3 B12 (A**2) : 1.36000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.239
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.191
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.131
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.100
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3880 ; 0.015 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2553 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5245 ; 1.561 ; 1.996
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6270 ; 1.867 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 469 ; 5.214 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 156 ;39.706 ;23.974
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 702 ;15.092 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;20.921 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 610 ; 0.082 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4161 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 740 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 860 ; 0.240 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2504 ; 0.186 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1837 ; 0.191 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1935 ; 0.090 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 93 ; 0.130 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 12 ; 0.173 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 37 ; 0.223 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 2 ; 0.337 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2431 ; 0.714 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3772 ; 1.222 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1661 ; 2.094 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1473 ; 3.264 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 306 A 329 1
REMARK 3 1 B 306 B 329 1
REMARK 3 2 A 343 A 407 1
REMARK 3 2 B 343 B 407 1
REMARK 3 3 A 408 A 416 4
REMARK 3 3 B 408 B 416 4
REMARK 3 4 A 417 A 529 1
REMARK 3 4 B 417 B 529 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 2612 ; 0.06 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 2612 ; 0.06 ; 0.05
REMARK 3 MEDIUM POSITIONAL 1 A (A): 128 ; 0.65 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 128 ; 0.65 ; 0.50
REMARK 3 TIGHT THERMAL 1 A (A**2): 2612 ; 0.21 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 2612 ; 0.21 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 128 ; 0.62 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 128 ; 0.62 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : P Q
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 P 1 P 15 5
REMARK 3 1 Q 1 Q 15 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 P (A): 76 ; 0.20 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 Q (A): 76 ; 0.20 ; 0.50
REMARK 3 LOOSE POSITIONAL 2 P (A): 69 ; 0.51 ; 5.00
REMARK 3 LOOSE POSITIONAL 2 Q (A): 69 ; 0.51 ; 5.00
REMARK 3 MEDIUM THERMAL 2 P (A**2): 76 ; 0.36 ; 2.00
REMARK 3 MEDIUM THERMAL 2 Q (A**2): 76 ; 0.36 ; 2.00
REMARK 3 LOOSE THERMAL 2 P (A**2): 69 ; 0.71 ; 10.00
REMARK 3 LOOSE THERMAL 2 Q (A**2): 69 ; 0.71 ; 10.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 305 A 529
REMARK 3 RESIDUE RANGE : P 1 P 15
REMARK 3 ORIGIN FOR THE GROUP (A): -45.5705 43.1328 3.3047
REMARK 3 T TENSOR
REMARK 3 T11: -0.1812 T22: -0.1974
REMARK 3 T33: -0.1663 T12: -0.0989
REMARK 3 T13: -0.0227 T23: 0.0664
REMARK 3 L TENSOR
REMARK 3 L11: 3.7031 L22: 2.6532
REMARK 3 L33: 4.1096 L12: 0.9712
REMARK 3 L13: -0.8511 L23: -0.6257
REMARK 3 S TENSOR
REMARK 3 S11: 0.0646 S12: -0.2096 S13: -0.0502
REMARK 3 S21: 0.1631 S22: -0.2071 S23: -0.4369
REMARK 3 S31: -0.2556 S32: 0.5885 S33: 0.1425
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 306 B 528
REMARK 3 RESIDUE RANGE : Q 1 Q 15
REMARK 3 ORIGIN FOR THE GROUP (A): -54.2592 19.1866 1.1008
REMARK 3 T TENSOR
REMARK 3 T11: -0.1033 T22: -0.2606
REMARK 3 T33: -0.2165 T12: -0.0813
REMARK 3 T13: 0.0559 T23: 0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 1.3728 L22: 4.4881
REMARK 3 L33: 3.1255 L12: -1.1708
REMARK 3 L13: 0.7789 L23: -1.7628
REMARK 3 S TENSOR
REMARK 3 S11: 0.0695 S12: 0.1559 S13: -0.0392
REMARK 3 S21: -0.3318 S22: -0.2276 S23: -0.2875
REMARK 3 S31: 0.4430 S32: 0.1298 S33: 0.1581
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2JFA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-JAN-07.
REMARK 100 THE DEPOSITION ID IS D_1290029163.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-SEP-05
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.60
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34500
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.40
REMARK 200 R MERGE FOR SHELL (I) : 0.46000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 2BJ4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 73.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.35M AMMONIUM SULPHATE, 0.7M LITHIUM
REMARK 280 SULPHATE, 0.07M TRI-SODIUM CITRATE PH5.6, PH 5.60
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
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 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 75.61933
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 37.80967
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 37.80967
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 75.61933
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, P, Q
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 MET A 282
REMARK 465 GLY A 283
REMARK 465 SER A 284
REMARK 465 SER A 285
REMARK 465 HIS A 286
REMARK 465 HIS A 287
REMARK 465 HIS A 288
REMARK 465 HIS A 289
REMARK 465 HIS A 290
REMARK 465 HIS A 291
REMARK 465 SER A 292
REMARK 465 SER A 293
REMARK 465 GLY A 294
REMARK 465 LEU A 295
REMARK 465 VAL A 296
REMARK 465 PRO A 297
REMARK 465 ARG A 298
REMARK 465 GLY A 299
REMARK 465 SER A 300
REMARK 465 HIS A 301
REMARK 465 MET A 302
REMARK 465 GLU A 303
REMARK 465 ASN A 304
REMARK 465 ASP A 332
REMARK 465 PRO A 333
REMARK 465 THR A 334
REMARK 465 ARG A 335
REMARK 465 CYS A 530
REMARK 465 LYS A 531
REMARK 465 ASN A 532
REMARK 465 VAL A 533
REMARK 465 MET B 282
REMARK 465 GLY B 283
REMARK 465 SER B 284
REMARK 465 SER B 285
REMARK 465 HIS B 286
REMARK 465 HIS B 287
REMARK 465 HIS B 288
REMARK 465 HIS B 289
REMARK 465 HIS B 290
REMARK 465 HIS B 291
REMARK 465 SER B 292
REMARK 465 SER B 293
REMARK 465 GLY B 294
REMARK 465 LEU B 295
REMARK 465 VAL B 296
REMARK 465 PRO B 297
REMARK 465 ARG B 298
REMARK 465 GLY B 299
REMARK 465 SER B 300
REMARK 465 HIS B 301
REMARK 465 MET B 302
REMARK 465 GLU B 303
REMARK 465 ASN B 304
REMARK 465 SER B 305
REMARK 465 LYS B 529
REMARK 465 CYS B 530
REMARK 465 LYS B 531
REMARK 465 ASN B 532
REMARK 465 VAL B 533
REMARK 465 ASP P 16
REMARK 465 ASP Q 16
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 LEU A 306 CG CD1 CD2
REMARK 470 TYR A 331 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 419 CG CD OE1 OE2
REMARK 470 TYR A 459 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A 462 CG CD1 CD2
REMARK 470 SER A 464 OG
REMARK 470 LYS A 481 CE NZ
REMARK 470 LYS A 492 NZ
REMARK 470 LYS A 529 CG CD CE NZ
REMARK 470 GLU B 339 CG CD OE1 OE2
REMARK 470 GLU B 419 CD OE1 OE2
REMARK 470 GLU B 423 CG CD OE1 OE2
REMARK 470 TYR B 459 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU B 462 CG CD1 CD2
REMARK 470 SER B 463 OG
REMARK 470 SER B 464 OG
REMARK 470 LYS B 492 CD CE NZ
REMARK 470 ASP P 1 CG OD1 OD2
REMARK 470 GLN P 4 CG CD OE1 NE2
REMARK 470 ARG P 11 CG CD NE CZ NH1 NH2
REMARK 470 ASP Q 1 CG OD1 OD2
REMARK 470 PHE Q 3 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN Q 4 CG CD OE1 NE2
REMARK 470 GLN Q 7 CG CD OE1 NE2
REMARK 470 ARG Q 11 CG CD NE CZ NH1 NH2
REMARK 470 ASP Q 15 CG OD1 OD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU B 397 CG GLU B 397 CD 0.093
REMARK 500
REMARK 500 REMARK: NULL
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 GLU A 385 OE1 - CD - OE2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 GLU A 471 OE1 - CD - OE2 ANGL. DEV. = -7.8 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 THR B 460 33.62 -97.98
REMARK 500 LEU B 462 171.37 -59.84
REMARK 500 SER B 464 -1.87 74.85
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 SO4 A 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RAL A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RAL B 600
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A52 RELATED DB: PDB
REMARK 900 ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN COMPLEXED TO ESTRADIOL
REMARK 900 RELATED ID: 1AKF RELATED DB: PDB
REMARK 900 HOMOLOGOUS-EXTENSION-BASED MODEL OF HUMAN ESTROGEN RECEPTOR WITH
REMARK 900 BOUND ESTRADIOL, THEORETICAL MODEL
REMARK 900 RELATED ID: 1ERE RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR LIGAND-BINDING DOMAIN IN COMPLEX WITH
REMARK 900 17BETA-ESTRADIOL
REMARK 900 RELATED ID: 1ERR RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR LIGAND-BINDING DOMAIN IN COMPLEX WITH
REMARK 900 RALOXIFENE
REMARK 900 RELATED ID: 1G50 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A WILD TYPE HER ALPHA LBD AT 2.9ANGSTROM
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1GWQ RELATED DB: PDB
REMARK 900 HUMAN OESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN IN COMPLEX
REMARK 900 WITH RALOXIFENE CORE AND TIF2 NRBOX2 PEPTIDE
REMARK 900 RELATED ID: 1GWR RELATED DB: PDB
REMARK 900 HUMAN OESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN IN COMPLEX
REMARK 900 WITH 17BETA-OESTRADIOL AND TIF2 NRBOX3 PEPTIDE
REMARK 900 RELATED ID: 1HCP RELATED DB: PDB
REMARK 900 RELATED ID: 1HCQ RELATED DB: PDB
REMARK 900 RELATED ID: 1L2I RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN INCOMPLEX WITH
REMARK 900 (R,R)-5,11-CIS- DIETHYL-5,6,11,12-TETRAHYDROCHRYSENE-2,8- DIOL AND
REMARK 900 A GLUCOCORTICOID RECEPTORINTERACTING PROTEIN 1 NR BOX II PEPTIDE
REMARK 900 RELATED ID: 1PCG RELATED DB: PDB
REMARK 900 HELIX-STABILIZED CYCLIC PEPTIDES AS SELECTIVE INHIBITORS OFSTEROID
REMARK 900 RECEPTOR-COACTIVATOR INTERACTIONS
REMARK 900 RELATED ID: 1QKT RELATED DB: PDB
REMARK 900 RELATED ID: 1QKU RELATED DB: PDB
REMARK 900 RELATED ID: 1R5K RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN INCOMPLEX WITH
REMARK 900 GW5638
REMARK 900 RELATED ID: 1SJ0 RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN INCOMPLEX WITH
REMARK 900 THE ANTAGONIST LIGAND 4-D
REMARK 900 RELATED ID: 1UOM RELATED DB: PDB
REMARK 900 THE STRUCTURE OF ESTROGEN RECEPTOR IN COMPLEX WITH A SELECTIVE AND
REMARK 900 POTENT TETRAHYDROISOCHIOLIN LIGAND.
REMARK 900 RELATED ID: 1X7E RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESTROGEN RECEPTOR ALPHA COMPLEXED WITHWAY-244
REMARK 900 RELATED ID: 1X7R RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESTROGEN RECEPTOR ALPHA COMPLEXED WITHGENISTEIN
REMARK 900 RELATED ID: 1XP1 RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN INCOMPLEX WITH
REMARK 900 COMPOUND 15
REMARK 900 RELATED ID: 1XP6 RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN INCOMPLEX WITH
REMARK 900 COMPOUND 16
REMARK 900 RELATED ID: 1XP9 RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN INCOMPLEX WITH
REMARK 900 COMPOUND 18
REMARK 900 RELATED ID: 1XPC RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN INCOMPLEX WITH
REMARK 900 COMPOUND 19
REMARK 900 RELATED ID: 1XQC RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF ERALPHA LBD BOUND TO ATETRAHYDROISOQUINOLINE
REMARK 900 SERM LIGAND AT 2.05A RESOLUTION
REMARK 900 RELATED ID: 1YIM RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN INCOMPLEX WITH
REMARK 900 COMPOUND 4
REMARK 900 RELATED ID: 1YIN RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN INCOMPLEX WITH
REMARK 900 COMPOUND 3F
REMARK 900 RELATED ID: 1ZKY RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN INCOMPLEX WITH
REMARK 900 OBCP-3M AND A GLUCOCORTICOID RECEPTORINTERACTING PROTEIN 1 NR BOX
REMARK 900 II PEPTIDE
REMARK 900 RELATED ID: 2AYR RELATED DB: PDB
REMARK 900 A SERM DESIGNED FOR THE TREATMENT OF UTERINE LEIOMYOMA WITHUNIQUE
REMARK 900 TISSUE SPECIFICITY FOR UTERUS AND OVARIES IN RATS
REMARK 900 RELATED ID: 2B1V RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN INCOMPLEX WITH
REMARK 900 OBCP-1M AND A GLUCOCORTICOID RECEPTORINTERACTING PROTEIN 1 NR BOX
REMARK 900 II PEPTIDE
REMARK 900 RELATED ID: 2BJ4 RELATED DB: PDB
REMARK 900 ESTROGEN RECEPTOR ALPHA LBD IN COMPLEX WITH A PHAGE-DISPLAY DERIVED
REMARK 900 PEPTIDE ANTAGONIST
REMARK 900 RELATED ID: 2FAI RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN INCOMPLEX WITH
REMARK 900 OBCP-2M AND A GLUCOCORTICOID RECEPTORINTERACTING PROTEIN 1 NR BOX
REMARK 900 II PEPTIDE
REMARK 900 RELATED ID: 3ERD RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN INCOMPLEX WITH
REMARK 900 DIETHYLSTILBESTROL AND A GLUCOCORTICOIDRECEPTOR INTERACTING PROTEIN
REMARK 900 1 NR BOX II PEPTIDE
REMARK 900 RELATED ID: 3ERT RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN IN COMPLEX WITH
REMARK 900 4-HYDROXYTAMOXIFEN
REMARK 900 RELATED ID: 2JF9 RELATED DB: PDB
REMARK 900 ESTROGEN RECEPTOR ALPHA LBD IN COMPLEX WITH A TAMOXIFEN-SPECIFIC
REMARK 900 PEPTIDE ANTAGONIST
DBREF 2JFA A 282 303 PDB 2JFA 2JFA 282 303
DBREF 2JFA A 304 533 UNP P03372 ESR1_HUMAN 304 533
DBREF 2JFA B 282 303 PDB 2JFA 2JFA 282 303
DBREF 2JFA B 304 533 UNP P03372 ESR1_HUMAN 304 533
DBREF 2JFA P 1 16 PDB 2JFA 2JFA 1 16
DBREF 2JFA Q 1 16 PDB 2JFA 2JFA 1 16
SEQRES 1 A 252 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 252 LEU VAL PRO ARG GLY SER HIS MET GLU ASN SER LEU ALA
SEQRES 3 A 252 LEU SER LEU THR ALA ASP GLN MET VAL SER ALA LEU LEU
SEQRES 4 A 252 ASP ALA GLU PRO PRO ILE LEU TYR SER GLU TYR ASP PRO
SEQRES 5 A 252 THR ARG PRO PHE SER GLU ALA SER MET MET GLY LEU LEU
SEQRES 6 A 252 THR ASN LEU ALA ASP ARG GLU LEU VAL HIS MET ILE ASN
SEQRES 7 A 252 TRP ALA LYS ARG VAL PRO GLY PHE VAL ASP LEU THR LEU
SEQRES 8 A 252 HIS ASP GLN VAL HIS LEU LEU GLU CYS ALA TRP LEU GLU
SEQRES 9 A 252 ILE LEU MET ILE GLY LEU VAL TRP ARG SER MET GLU HIS
SEQRES 10 A 252 PRO GLY LYS LEU LEU PHE ALA PRO ASN LEU LEU LEU ASP
SEQRES 11 A 252 ARG ASN GLN GLY LYS CYS VAL GLU GLY MET VAL GLU ILE
SEQRES 12 A 252 PHE ASP MET LEU LEU ALA THR SER SER ARG PHE ARG MET
SEQRES 13 A 252 MET ASN LEU GLN GLY GLU GLU PHE VAL CYS LEU LYS SER
SEQRES 14 A 252 ILE ILE LEU LEU ASN SER GLY VAL TYR THR PHE LEU SER
SEQRES 15 A 252 SER THR LEU LYS SER LEU GLU GLU LYS ASP HIS ILE HIS
SEQRES 16 A 252 ARG VAL LEU ASP LYS ILE THR ASP THR LEU ILE HIS LEU
SEQRES 17 A 252 MET ALA LYS ALA GLY LEU THR LEU GLN GLN GLN HIS GLN
SEQRES 18 A 252 ARG LEU ALA GLN LEU LEU LEU ILE LEU SER HIS ILE ARG
SEQRES 19 A 252 HIS MET SER ASN LYS GLY MET GLU HIS LEU TYR SER MET
SEQRES 20 A 252 LYS CYS LYS ASN VAL
SEQRES 1 B 252 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 252 LEU VAL PRO ARG GLY SER HIS MET GLU ASN SER LEU ALA
SEQRES 3 B 252 LEU SER LEU THR ALA ASP GLN MET VAL SER ALA LEU LEU
SEQRES 4 B 252 ASP ALA GLU PRO PRO ILE LEU TYR SER GLU TYR ASP PRO
SEQRES 5 B 252 THR ARG PRO PHE SER GLU ALA SER MET MET GLY LEU LEU
SEQRES 6 B 252 THR ASN LEU ALA ASP ARG GLU LEU VAL HIS MET ILE ASN
SEQRES 7 B 252 TRP ALA LYS ARG VAL PRO GLY PHE VAL ASP LEU THR LEU
SEQRES 8 B 252 HIS ASP GLN VAL HIS LEU LEU GLU CYS ALA TRP LEU GLU
SEQRES 9 B 252 ILE LEU MET ILE GLY LEU VAL TRP ARG SER MET GLU HIS
SEQRES 10 B 252 PRO GLY LYS LEU LEU PHE ALA PRO ASN LEU LEU LEU ASP
SEQRES 11 B 252 ARG ASN GLN GLY LYS CCS VAL GLU GLY MET VAL GLU ILE
SEQRES 12 B 252 PHE ASP MET LEU LEU ALA THR SER SER ARG PHE ARG MET
SEQRES 13 B 252 MET ASN LEU GLN GLY GLU GLU PHE VAL CYS LEU LYS SER
SEQRES 14 B 252 ILE ILE LEU LEU ASN SER GLY VAL TYR THR PHE LEU SER
SEQRES 15 B 252 SER THR LEU LYS SER LEU GLU GLU LYS ASP HIS ILE HIS
SEQRES 16 B 252 ARG VAL LEU ASP LYS ILE THR ASP THR LEU ILE HIS LEU
SEQRES 17 B 252 MET ALA LYS ALA GLY LEU THR LEU GLN GLN GLN HIS GLN
SEQRES 18 B 252 ARG LEU ALA GLN LEU LEU LEU ILE LEU SER HIS ILE ARG
SEQRES 19 B 252 HIS MET SER ASN LYS GLY MET GLU HIS LEU TYR SER MET
SEQRES 20 B 252 LYS CYS LYS ASN VAL
SEQRES 1 P 16 ASP ALA PHE GLN LEU ARG GLN LEU ILE LEU ARG GLY LEU
SEQRES 2 P 16 GLN ASP ASP
SEQRES 1 Q 16 ASP ALA PHE GLN LEU ARG GLN LEU ILE LEU ARG GLY LEU
SEQRES 2 Q 16 GLN ASP ASP
MODRES 2JFA CCS B 417 CYS CARBOXYMETHYLATED CYSTEINE
HET CCS B 417 10
HET RAL A 600 34
HET SO4 A 610 5
HET SO4 A 620 5
HET RAL B 600 34
HET SO4 B 610 5
HET SO4 B 620 5
HETNAM CCS CARBOXYMETHYLATED CYSTEINE
HETNAM RAL RALOXIFENE
HETNAM SO4 SULFATE ION
FORMUL 2 CCS C5 H9 N O4 S
FORMUL 5 RAL 2(C28 H27 N O4 S)
FORMUL 6 SO4 4(O4 S 2-)
FORMUL 11 HOH *86(H2 O)
HELIX 1 1 LEU A 306 LEU A 310 5 5
HELIX 2 2 THR A 311 ALA A 322 1 12
HELIX 3 3 SER A 338 VAL A 364 1 27
HELIX 4 4 GLY A 366 LEU A 370 5 5
HELIX 5 5 THR A 371 SER A 395 1 25
HELIX 6 6 ARG A 412 LYS A 416 1 5
HELIX 7 7 MET A 421 MET A 438 1 18
HELIX 8 8 GLN A 441 GLY A 457 1 17
HELIX 9 9 VAL A 458 PHE A 461 5 4
HELIX 10 10 THR A 465 ALA A 493 1 29
HELIX 11 11 THR A 496 SER A 527 1 32
HELIX 12 12 LEU B 306 LEU B 310 5 5
HELIX 13 13 THR B 311 GLU B 323 1 13
HELIX 14 14 SER B 341 VAL B 364 1 24
HELIX 15 15 GLY B 366 LEU B 370 5 5
HELIX 16 16 THR B 371 SER B 395 1 25
HELIX 17 17 ASN B 413 VAL B 418 5 6
HELIX 18 18 MET B 421 ASN B 439 1 19
HELIX 19 19 GLN B 441 GLY B 457 1 17
HELIX 20 20 THR B 465 ALA B 493 1 29
HELIX 21 21 THR B 496 SER B 527 1 32
HELIX 22 22 ALA P 2 ASP P 15 1 14
HELIX 23 23 ALA Q 2 ASP Q 15 1 14
SHEET 1 AA 2 LYS A 401 ALA A 405 0
SHEET 2 AA 2 LEU A 408 ASP A 411 -1 O LEU A 408 N PHE A 404
SHEET 1 BA 2 LYS B 401 ALA B 405 0
SHEET 2 BA 2 LEU B 408 ASP B 411 -1 O LEU B 408 N ALA B 405
LINK C LYS B 416 N CCS B 417 1555 1555 1.33
LINK C CCS B 417 N VAL B 418 1555 1555 1.33
SITE 1 AC1 3 ARG A 352 HIS A 356 HOH A2046
SITE 1 AC2 5 PRO A 325 HIS A 356 ASN A 359 ARG A 363
SITE 2 AC2 5 HOH A2012
SITE 1 AC3 3 ARG B 352 HIS B 356 HOH B2040
SITE 1 AC4 4 HIS B 356 ASN B 359 ARG B 363 HOH B2013
SITE 1 AC5 14 LEU A 346 THR A 347 ALA A 350 ASP A 351
SITE 2 AC5 14 GLU A 353 LEU A 354 TRP A 383 LEU A 387
SITE 3 AC5 14 ARG A 394 MET A 421 ILE A 424 HIS A 524
SITE 4 AC5 14 HOH A2011 ASP P 1
SITE 1 AC6 13 MET B 343 LEU B 346 THR B 347 ALA B 350
SITE 2 AC6 13 ASP B 351 GLU B 353 LEU B 354 TRP B 383
SITE 3 AC6 13 ARG B 394 MET B 421 ILE B 424 HIS B 524
SITE 4 AC6 13 HOH B2012
CRYST1 126.573 126.573 113.429 90.00 90.00 120.00 P 32 2 1 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 0.007901 0.004561 0.000000 0.00000
SCALE2 0.000000 0.009123 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008816 0.00000
MTRIX1 1 0.741000 -0.671000 0.005000 8.46374 1
MTRIX2 1 -0.671000 -0.741000 0.019000 20.93542 1
MTRIX3 1 -0.009000 -0.018000 -1.000000 4.34764 1
MTRIX1 2 0.767000 -0.642000 -0.009000 8.53135 1
MTRIX2 2 -0.642000 -0.767000 -0.021000 24.03974 1
MTRIX3 2 0.007000 0.022000 -1.000000 2.94325 1
(ATOM LINES ARE NOT SHOWN.)
END
