HEADER HORMONE RECEPTOR/PEPTIDE 19-MAY-11 2YJA
TITLE STAPLED PEPTIDES BINDING TO ESTROGEN RECEPTOR ALPHA.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STAPLED PEPTIDE;
COMPND 3 CHAIN: A;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: ESTROGEN RECEPTOR;
COMPND 6 CHAIN: B;
COMPND 7 FRAGMENT: LIGAND-BINDING DOMAIN, RESIDUES 299-551;
COMPND 8 SYNONYM: ER, ER-ALPHA, ESTRADIOL RECEPTOR, NUCLEAR RECEPTOR
COMPND 9 SUBFAMILY 3 GROUP A MEMBER 1;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 9606;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 8 ORGANISM_COMMON: HUMAN;
SOURCE 9 ORGANISM_TAXID: 9606;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HORMONE RECEPTOR-PEPTIDE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.PHILLIPS,L.R.ROBERTS,M.SCHADE,R.BAZIN,A.BENT,N.L.DAVIES,S.L.IRVING,
AUTHOR 2 R.MOORE,A.D.PANNIFER,D.G.BROWN,A.R.PICKFORD,A.SCOTT,B.XU
REVDAT 1 03-AUG-11 2YJA 0
JRNL AUTH C.PHILLIPS,L.R.ROBERTS,M.SCHADE,R.BAZIN,A.BENT,N.L.DAVIES,
JRNL AUTH 2 R.MOORE,A.D.PANNIFER,A.R.PICKFORD,S.H.PRIOR,C.M.READ,
JRNL AUTH 3 A.SCOTT,D.G.BROWN,B.XU,S.L.IRVING
JRNL TITL DESIGN AND STRUCTURE OF STAPLED PEPTIDES BINDING TO
JRNL TITL 2 ESTROGEN RECEPTORS.
JRNL REF J.AM.CHEM.SOC. V. 133 9696 2011
JRNL REFN ISSN 0002-7863
JRNL PMID 21612236
JRNL DOI 10.1021/JA202946K
REMARK 2
REMARK 2 RESOLUTION. 1.82 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.9.3
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.82
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.71
REMARK 3 NUMBER OF REFLECTIONS : 23603
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) : 0.1994
REMARK 3 R VALUE (WORKING SET) : 0.1976
REMARK 3 FREE R VALUE : 0.2342
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.03
REMARK 3 FREE R VALUE TEST SET COUNT : 1188
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 : 12
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.82
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.90
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.71
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2294
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2104
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2181
REMARK 3 BIN R VALUE (WORKING SET) : 0.2077
REMARK 3 BIN FREE R VALUE : 0.2620
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.93
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 113
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 : 2028
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 124
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.84
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.42
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.8883
REMARK 3 B22 (A**2) : -2.1269
REMARK 3 B33 (A**2) : 0.2387
REMARK 3 B12 (A**2) : 0.0000
REMARK 3 B13 (A**2) : 0.0000
REMARK 3 B23 (A**2) : 0.0000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.200
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.144
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.133
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.140
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.132
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 : 0.9349
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.9107
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2116 ; 2.00 ; HARMONIC
REMARK 3 BOND ANGLES : 2866 ; 2.00 ; HARMONIC
REMARK 3 TORSION ANGLES : 721 ; 2.00 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 65 ; 2.00 ; HARMONIC
REMARK 3 GENERAL PLANES : 309 ; 5.00 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2116 ; 20.00 ; 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 : 273 ; 5.00 ; 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 : 2650 ; 4.00 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.02
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.72
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 22.33
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: IDEAL-DIST CONTACT TERM CONTACT
REMARK 3 SETUP. ALL ATOMS HAVE CCP4 ATOM TYPE FROM LIBRARY.
REMARK 4
REMARK 4 2YJA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-MAY-11.
REMARK 100 THE PDBE ID CODE IS EBI-48339.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23603
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.80
REMARK 200 RESOLUTION RANGE LOW (A) : 32.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : 6.2
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 32.59600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 32.59600
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 37.51600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 55.20350
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 37.51600
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 55.20350
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 32.59600
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 37.51600
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 55.20350
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 32.59600
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 37.51600
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 55.20350
REMARK 290 SMTRY3 8 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.5 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 75.03200
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 32.59600
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 B 297
REMARK 465 SER B 298
REMARK 465 LYS B 299
REMARK 465 ARG B 300
REMARK 465 SER B 301
REMARK 465 LYS B 302
REMARK 465 LYS B 303
REMARK 465 ASN B 304
REMARK 465 HIS B 550
REMARK 465 ALA B 551
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 B 549 O
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 ASP B 332 76.70 39.97
REMARK 500 LEU B 462 -146.10 -78.24
REMARK 500 SER B 464 65.62 -26.29
REMARK 500 THR B 465 -155.15 51.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 SER A 11 23.3 L L OUTSIDE RANGE
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 EST B1550
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2YAT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESTRADIOL DERIVED METAL CHELATE AND
REMARK 900 ESTROGEN RECEPTOR-LIGAND BINDING DOMAIN COMPLEX
REMARK 900 RELATED ID: 1XP1 RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN
REMARK 900 INCOMPLEX WITH COMPOUND 15
REMARK 900 RELATED ID: 1QKT RELATED DB: PDB
REMARK 900 RELATED ID: 1R5K RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN
REMARK 900 INCOMPLEX WITH GW5638
REMARK 900 RELATED ID: 1ZKY RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN
REMARK 900 INCOMPLEX WITH OBCP-3M AND A GLUCOCORTICOID
REMARK 900 RECEPTORINTERACTING PROTEIN 1 NR BOX II PEPTIDE
REMARK 900 RELATED ID: 2BJ4 RELATED DB: PDB
REMARK 900 ESTROGEN RECEPTOR ALPHA LBD IN COMPLEX WITH A PHAGE-
REMARK 900 DISPLAY DERIVED PEPTIDE ANTAGONIST
REMARK 900 RELATED ID: 1AKF RELATED DB: PDB
REMARK 900 HOMOLOGOUS-EXTENSION-BASED MODEL OF HUMAN ESTROGEN
REMARK 900 RECEPTOR WITH BOUND ESTRADIOL, THEORETICAL MODEL
REMARK 900 RELATED ID: 1HCP RELATED DB: PDB
REMARK 900 MOL_ID: 1; MOLECULE: HUMAN/CHICKEN ESTROGEN RECEPTOR;
REMARK 900 CHAIN: NULL; DOMAIN: DEOXYRIBONUCLEIC ACID-BINDING DOMAIN
REMARK 900 (ERDBD); ENGINEERED: YES
REMARK 900 RELATED ID: 1HCQ RELATED DB: PDB
REMARK 900 MOL_ID: 1; MOLECULE: HUMAN/CHICKEN ESTROGEN RECEPTOR;
REMARK 900 CHAIN: A, B, E, F; DOMAIN: DEOXYRIBONUCLEIC ACID-
REMARK 900 BINDING DOMAIN (ERDBD); ENGINEERED: YES; MOL_ID: 2;
REMARK 900 MOLECULE: DEOXYRIBONUCLEIC ACID (5'-D(
REMARK 900 CPCPAPGPGPTPCPAPCPAPGPTPGP APCPCPTPG)-3') (DOT)
REMARK 900 DEOXYRIBONUCLEIC ACID (5'-D(CPCPAPGPGPTPCPA
REMARK 900 PCPTPGPTPGPAPCPCPTPG)-3'); CHAIN: C, D, G, H
REMARK 900 RELATED ID: 1A52 RELATED DB: PDB
REMARK 900 ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN COMPLEXED
REMARK 900 TO ESTRADIOL
REMARK 900 RELATED ID: 1QKU RELATED DB: PDB
REMARK 900 RELATED ID: 1G50 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A WILD TYPE HER ALPHA LBD AT
REMARK 900 2.9ANGSTROM RESOLUTION
REMARK 900 RELATED ID: 1XP6 RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN
REMARK 900 INCOMPLEX WITH COMPOUND 16
REMARK 900 RELATED ID: 1PCG RELATED DB: PDB
REMARK 900 HELIX-STABILIZED CYCLIC PEPTIDES AS SELECTIVE INHIBITORS
REMARK 900 OFSTEROID RECEPTOR-COACTIVATOR INTERACTIONS
REMARK 900 RELATED ID: 2B1V RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN
REMARK 900 INCOMPLEX WITH OBCP-1M AND A GLUCOCORTICOID
REMARK 900 RECEPTORINTERACTING PROTEIN 1 NR BOX II PEPTIDE
REMARK 900 RELATED ID: 2JF9 RELATED DB: PDB
REMARK 900 ESTROGEN RECEPTOR ALPHA LBD IN COMPLEX WITH A
REMARK 900 TAMOXIFEN-SPECIFIC PEPTIDE ANTAGONIST
REMARK 900 RELATED ID: 1UOM RELATED DB: PDB
REMARK 900 THE STRUCTURE OF ESTROGEN RECEPTOR IN COMPLEX WITH A
REMARK 900 SELECTIVE AND POTENT TETRAHYDROISOCHIOLIN LIGAND.
REMARK 900 RELATED ID: 1YIM RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN
REMARK 900 INCOMPLEX WITH COMPOUND 4
REMARK 900 RELATED ID: 2AYR RELATED DB: PDB
REMARK 900 A SERM DESIGNED FOR THE TREATMENT OF UTERINE LEIOMYOMA
REMARK 900 WITHUNIQUE TISSUE SPECIFICITY FOR UTERUS AND OVARIES
REMARK 900 IN RATS
REMARK 900 RELATED ID: 3ERT RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN IN
REMARK 900 COMPLEX WITH 4-HYDROXYTAMOXIFEN
REMARK 900 RELATED ID: 1YIN RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN
REMARK 900 INCOMPLEX WITH COMPOUND 3F
REMARK 900 RELATED ID: 1ERR RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR LIGAND-BINDING DOMAIN IN COMPLEX
REMARK 900 WITH RALOXIFENE
REMARK 900 RELATED ID: 1X7R RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESTROGEN RECEPTOR ALPHA COMPLEXED
REMARK 900 WITHGENISTEIN
REMARK 900 RELATED ID: 3ERD RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN
REMARK 900 INCOMPLEX WITH DIETHYLSTILBESTROL AND A
REMARK 900 GLUCOCORTICOIDRECEPTOR INTERACTING PROTEIN 1 NR BOX II
REMARK 900 PEPTIDE
REMARK 900 RELATED ID: 1L2I RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN
REMARK 900 INCOMPLEX WITH (R,R)-5,11-CIS-DIETHYL-5,6,11,12
REMARK 900 -TETRAHYDROCHRYSENE-2,8-DIOL AND A GLUCOCORTICOID
REMARK 900 RECEPTORINTERACTING PROTEIN 1 NR BOX II PEPTIDE
REMARK 900 RELATED ID: 1XP9 RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN
REMARK 900 INCOMPLEX WITH COMPOUND 18
REMARK 900 RELATED ID: 2FAI RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN
REMARK 900 INCOMPLEX WITH OBCP-2M AND A GLUCOCORTICOID
REMARK 900 RECEPTORINTERACTING PROTEIN 1 NR BOX II PEPTIDE
REMARK 900 RELATED ID: 1GWR RELATED DB: PDB
REMARK 900 HUMAN OESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN IN
REMARK 900 COMPLEX WITH 17BETA-OESTRADIOL AND TIF2 NRBOX3 PEPTIDE
REMARK 900 RELATED ID: 1SJ0 RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN
REMARK 900 INCOMPLEX WITH THE ANTAGONIST LIGAND 4-D
REMARK 900 RELATED ID: 2JFA RELATED DB: PDB
REMARK 900 ESTROGEN RECEPTOR ALPHA LBD IN COMPLEX WITH AN
REMARK 900 AFFINITY-SELECTED COREPRESSOR PEPTIDE
REMARK 900 RELATED ID: 1GWQ RELATED DB: PDB
REMARK 900 HUMAN OESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN IN
REMARK 900 COMPLEX WITH RALOXIFENE CORE AND TIF2 NRBOX2 PEPTIDE
REMARK 900 RELATED ID: 1XPC RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN
REMARK 900 INCOMPLEX WITH COMPOUND 19
REMARK 900 RELATED ID: 1X7E RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESTROGEN RECEPTOR ALPHA COMPLEXED
REMARK 900 WITHWAY-244
REMARK 900 RELATED ID: 1XQC RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF ERALPHA LBD BOUND TO
REMARK 900 ATETRAHYDROISOQUINOLINE SERM LIGAND AT 2.05A RESOLUTION
REMARK 900 RELATED ID: 1ERE RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR LIGAND-BINDING DOMAIN IN COMPLEX
REMARK 900 WITH 17BETA-ESTRADIOL
REMARK 900 RELATED ID: 2YJD RELATED DB: PDB
REMARK 900 STAPLED PEPTIDE BOUND TO ESTROGEN RECEPTOR BETA
REMARK 900 RELATED ID: 2LDD RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE ESTROGEN RECEPTOR-BINDING
REMARK 900 STAPLED PEPTIDE SP6 (AC-EKHKILXRLLXDS-NH2)
REMARK 900 RELATED ID: 2LDA RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE ESTROGEN RECEPTOR-BINDING
REMARK 900 STAPLED PEPTIDE SP2 (AC-HKXLHQXLQDS-NH2)
REMARK 900 RELATED ID: 2LDC RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE ESTROGEN RECEPTOR-BINDING
REMARK 900 STAPLED PEPTIDE SP1 (AC-HXILHXLLQDS-NH2)
DBREF 2YJA A 0 12 PDB 2YJA 2YJA 0 12
DBREF 2YJA B 299 551 UNP P03372 ESR1_HUMAN 299 551
SEQADV 2YJA GLY B 297 UNP P03372 EXPRESSION TAG
SEQADV 2YJA SER B 298 UNP P03372 EXPRESSION TAG
SEQRES 1 A 13 ACE HIS LYS MK8 LEU HIS GLN MK8 LEU GLN ASP SER NH2
SEQRES 1 B 255 GLY SER LYS ARG SER LYS LYS ASN SER LEU ALA LEU SER
SEQRES 2 B 255 LEU THR ALA ASP GLN MET VAL SER ALA LEU LEU ASP ALA
SEQRES 3 B 255 GLU PRO PRO ILE LEU TYR SER GLU TYR ASP PRO THR ARG
SEQRES 4 B 255 PRO PHE SER GLU ALA SER MET MET GLY LEU LEU THR ASN
SEQRES 5 B 255 LEU ALA ASP ARG GLU LEU VAL HIS MET ILE ASN TRP ALA
SEQRES 6 B 255 LYS ARG VAL PRO GLY PHE VAL ASP LEU THR LEU HIS ASP
SEQRES 7 B 255 GLN VAL HIS LEU LEU GLU CYS ALA TRP LEU GLU ILE LEU
SEQRES 8 B 255 MET ILE GLY LEU VAL TRP ARG SER MET GLU HIS PRO GLY
SEQRES 9 B 255 LYS LEU LEU PHE ALA PRO ASN LEU LEU LEU ASP ARG ASN
SEQRES 10 B 255 GLN GLY LYS CYS VAL GLU GLY MET VAL GLU ILE PHE ASP
SEQRES 11 B 255 MET LEU LEU ALA THR SER SER ARG PHE ARG MET MET ASN
SEQRES 12 B 255 LEU GLN GLY GLU GLU PHE VAL CYS LEU LYS SER ILE ILE
SEQRES 13 B 255 LEU LEU ASN SER GLY VAL TYR THR PHE LEU SER SER THR
SEQRES 14 B 255 LEU LYS SER LEU GLU GLU LYS ASP HIS ILE HIS ARG VAL
SEQRES 15 B 255 LEU ASP LYS ILE THR ASP THR LEU ILE HIS LEU MET ALA
SEQRES 16 B 255 LYS ALA GLY LEU THR LEU GLN GLN GLN HIS GLN ARG LEU
SEQRES 17 B 255 ALA GLN LEU LEU LEU ILE LEU SER HIS ILE ARG HIS MET
SEQRES 18 B 255 SER ASN LYS GLY MET GLU HIS LEU TYR SER MET LYS CYS
SEQRES 19 B 255 LYS ASN VAL VAL PRO LEU TYR ASP LEU LEU LEU GLU MET
SEQRES 20 B 255 LEU ASP ALA HIS ARG LEU HIS ALA
MODRES 2YJA MK8 A 3 LEU 2-METHYL-L-NORLEUCINE
MODRES 2YJA MK8 A 7 LEU 2-METHYL-L-NORLEUCINE
HET ACE A 0 3
HET MK8 A 3 9
HET MK8 A 7 9
HET NH2 A 12 1
HET EST B1550 20
HETNAM ACE ACETYL GROUP
HETNAM MK8 2-METHYL-L-NORLEUCINE
HETNAM NH2 AMINO GROUP
HETNAM EST ESTRADIOL
FORMUL 3 ACE C2 H4 O
FORMUL 4 MK8 2(C7 H15 N O2)
FORMUL 5 NH2 H2 N
FORMUL 6 EST C18 H24 O2
FORMUL 7 HOH *124(H2 O)
HELIX 1 1 LYS A 2 ASP A 10 1 9
HELIX 2 2 LEU B 306 LEU B 310 5 5
HELIX 3 3 THR B 311 ALA B 322 1 12
HELIX 4 4 SER B 338 VAL B 364 1 27
HELIX 5 5 GLY B 366 LEU B 370 5 5
HELIX 6 6 THR B 371 SER B 395 1 25
HELIX 7 7 ARG B 412 LYS B 416 1 5
HELIX 8 8 GLY B 420 MET B 438 1 19
HELIX 9 9 GLN B 441 SER B 456 1 16
HELIX 10 10 SER B 464 ALA B 493 1 30
HELIX 11 11 THR B 496 LYS B 531 1 36
HELIX 12 12 TYR B 537 ALA B 546 1 10
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 PHE B 404
LINK C ACE A 0 N HIS A 1 1555 1555 1.38
LINK C LYS A 2 N MK8 A 3 1555 1555 1.38
LINK C MK8 A 3 N LEU A 4 1555 1555 1.39
LINK CE MK8 A 3 CE MK8 A 7 1555 1555 1.30
LINK C GLN A 6 N MK8 A 7 1555 1555 1.37
LINK C MK8 A 7 N LEU A 8 1555 1555 1.37
LINK C SER A 11 N NH2 A 12 1555 1555 1.36
CISPEP 1 ARG B 335 PRO B 336 0 1.00
SITE 1 AC1 10 MET B 343 LEU B 346 GLU B 353 LEU B 387
SITE 2 AC1 10 ARG B 394 PHE B 404 MET B 421 HIS B 524
SITE 3 AC1 10 LEU B 525 HOH B2025
CRYST1 75.032 110.407 65.192 90.00 90.00 90.00 C 2 2 21 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 0.013328 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009057 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015339 0.00000
HETATM 1 C ACE A 0 39.454 6.254 -6.975 1.00 81.67 C
HETATM 2 O ACE A 0 39.944 7.015 -7.795 1.00 82.21 O
HETATM 3 CH3 ACE A 0 39.794 4.787 -7.069 1.00 82.07 C
(ATOM LINES ARE NOT SHOWN.)
END
