HEADER GENE REGULATION 24-NOV-14 4X1G
TITLE CRYSTAL STRUCTURE OF THE HPXR-LBD IN COMPLEX WITH THE SYNTHETIC
TITLE 2 ESTROGEN 17ALPHA-ETHINYLESTRADIOL AND THE PESTICIDE TRANS-NONACHLOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUCLEAR RECEPTOR SUBFAMILY 1 GROUP I MEMBER 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 130-434;
COMPND 5 SYNONYM: ORPHAN NUCLEAR RECEPTOR PAR1,ORPHAN NUCLEAR RECEPTOR PXR,
COMPND 6 PREGNANE X RECEPTOR,STEROID AND XENOBIOTIC RECEPTOR,SXR;
COMPND 7 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: NR1I2, PXR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PRSETA
KEYWDS HORMONE RECEPTOR, ESTROGEN, PESTICIDE, GENE REGULATION
EXPDTA X-RAY DIFFRACTION
AUTHOR V.DELFOSSE,T.HUET,W.BOURGUET
REVDAT 4 10-JAN-24 4X1G 1 REMARK
REVDAT 3 04-JUL-18 4X1G 1 AUTHOR
REVDAT 2 16-SEP-15 4X1G 1 JRNL
REVDAT 1 09-SEP-15 4X1G 0
JRNL AUTH V.DELFOSSE,B.DENDELE,T.HUET,M.GRIMALDI,A.BOULAHTOUF,
JRNL AUTH 2 S.GERBAL-CHALOIN,B.BEUCHER,D.ROECKLIN,C.MULLER,R.RAHMANI,
JRNL AUTH 3 V.CAVAILLES,M.DAUJAT-CHAVANIEU,V.VIVAT,J.M.PASCUSSI,
JRNL AUTH 4 P.BALAGUER,W.BOURGUET
JRNL TITL SYNERGISTIC ACTIVATION OF HUMAN PREGNANE X RECEPTOR BY
JRNL TITL 2 BINARY COCKTAILS OF PHARMACEUTICAL AND ENVIRONMENTAL
JRNL TITL 3 COMPOUNDS.
JRNL REF NAT COMMUN V. 6 8089 2015
JRNL REFN ESSN 2041-1723
JRNL PMID 26333997
JRNL DOI 10.1038/NCOMMS9089
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 17316
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 866
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 38.7211 - 4.0873 0.95 2818 149 0.1581 0.1758
REMARK 3 2 4.0873 - 3.2448 0.97 2733 144 0.1525 0.1947
REMARK 3 3 3.2448 - 2.8347 0.98 2736 144 0.1914 0.2603
REMARK 3 4 2.8347 - 2.5756 0.99 2740 144 0.1960 0.2470
REMARK 3 5 2.5756 - 2.3910 0.99 2708 142 0.2110 0.2849
REMARK 3 6 2.3910 - 2.2501 0.99 2715 143 0.2065 0.2887
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.410
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 2318
REMARK 3 ANGLE : 1.067 3160
REMARK 3 CHIRALITY : 0.039 357
REMARK 3 PLANARITY : 0.005 397
REMARK 3 DIHEDRAL : 13.682 878
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4X1G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-NOV-14.
REMARK 100 THE DEPOSITION ID IS D_1000204889.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-MAY-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.1
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8726
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17316
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 40.850
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.20
REMARK 200 R MERGE FOR SHELL (I) : 0.45000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX (PHENIX.REFINE: 1.8.4_1496)
REMARK 200 STARTING MODEL: 1ILG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM NACL, 50 MM LICL, 100 MM
REMARK 280 IMIDAZOLE, 10% ISOPROPANOL, PH 7.1, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 42.74500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 45.67000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 45.67000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 64.11750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 45.67000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 45.67000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 21.37250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 45.67000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 45.67000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 64.11750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 45.67000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 45.67000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 21.37250
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 42.74500
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: 2020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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 0.000000 -1.000000 0.000000 91.34000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 91.34000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -42.74500
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 119
REMARK 465 LYS A 120
REMARK 465 LYS A 121
REMARK 465 GLY A 122
REMARK 465 HIS A 123
REMARK 465 HIS A 124
REMARK 465 HIS A 125
REMARK 465 HIS A 126
REMARK 465 HIS A 127
REMARK 465 HIS A 128
REMARK 465 GLY A 129
REMARK 465 SER A 130
REMARK 465 GLU A 131
REMARK 465 ARG A 132
REMARK 465 THR A 133
REMARK 465 GLY A 134
REMARK 465 THR A 135
REMARK 465 GLN A 136
REMARK 465 PRO A 137
REMARK 465 LEU A 138
REMARK 465 GLY A 139
REMARK 465 VAL A 140
REMARK 465 GLN A 141
REMARK 465 LEU A 178
REMARK 465 SER A 179
REMARK 465 SER A 180
REMARK 465 GLY A 181
REMARK 465 CYS A 182
REMARK 465 GLU A 183
REMARK 465 LEU A 184
REMARK 465 PRO A 185
REMARK 465 GLU A 186
REMARK 465 SER A 187
REMARK 465 LEU A 188
REMARK 465 GLN A 189
REMARK 465 ALA A 190
REMARK 465 PRO A 191
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 GLU A 146 CD OE1 OE2
REMARK 470 ARG A 152 CD NE CZ NH1 NH2
REMARK 470 LYS A 170 CD CE NZ
REMARK 470 VAL A 177 CG1 CG2
REMARK 470 SER A 192 OG
REMARK 470 ARG A 193 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 194 CG CD OE1 OE2
REMARK 470 LYS A 204 CG CD CE NZ
REMARK 470 LEU A 209 CG CD1 CD2
REMARK 470 LYS A 210 CD CE NZ
REMARK 470 GLU A 218 CG CD OE1 OE2
REMARK 470 LYS A 226 CE NZ
REMARK 470 SER A 231 OG
REMARK 470 LYS A 234 CG CD CE NZ
REMARK 470 LYS A 259 CE NZ
REMARK 470 ASP A 310 CG OD1 OD2
REMARK 470 PHE A 315 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN A 316 CG CD OE1 NE2
REMARK 470 LEU A 318 CG CD1 CD2
REMARK 470 LYS A 325 CE NZ
REMARK 470 LYS A 332 CD CE NZ
REMARK 470 ARG A 360 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE1 GLN A 406 O HOH A 698 2.09
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 CYS A 301 67.96 -102.36
REMARK 500 HIS A 418 86.68 -152.32
REMARK 500 PHE A 420 -13.17 -157.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 696 DISTANCE = 6.41 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 3WF A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 3WG A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPA A 504
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4X1F RELATED DB: PDB
DBREF 4X1G A 130 434 UNP O75469 NR1I2_HUMAN 130 434
SEQADV 4X1G MET A 119 UNP O75469 INITIATING METHIONINE
SEQADV 4X1G LYS A 120 UNP O75469 EXPRESSION TAG
SEQADV 4X1G LYS A 121 UNP O75469 EXPRESSION TAG
SEQADV 4X1G GLY A 122 UNP O75469 EXPRESSION TAG
SEQADV 4X1G HIS A 123 UNP O75469 EXPRESSION TAG
SEQADV 4X1G HIS A 124 UNP O75469 EXPRESSION TAG
SEQADV 4X1G HIS A 125 UNP O75469 EXPRESSION TAG
SEQADV 4X1G HIS A 126 UNP O75469 EXPRESSION TAG
SEQADV 4X1G HIS A 127 UNP O75469 EXPRESSION TAG
SEQADV 4X1G HIS A 128 UNP O75469 EXPRESSION TAG
SEQADV 4X1G GLY A 129 UNP O75469 EXPRESSION TAG
SEQRES 1 A 316 MET LYS LYS GLY HIS HIS HIS HIS HIS HIS GLY SER GLU
SEQRES 2 A 316 ARG THR GLY THR GLN PRO LEU GLY VAL GLN GLY LEU THR
SEQRES 3 A 316 GLU GLU GLN ARG MET MET ILE ARG GLU LEU MET ASP ALA
SEQRES 4 A 316 GLN MET LYS THR PHE ASP THR THR PHE SER HIS PHE LYS
SEQRES 5 A 316 ASN PHE ARG LEU PRO GLY VAL LEU SER SER GLY CYS GLU
SEQRES 6 A 316 LEU PRO GLU SER LEU GLN ALA PRO SER ARG GLU GLU ALA
SEQRES 7 A 316 ALA LYS TRP SER GLN VAL ARG LYS ASP LEU CYS SER LEU
SEQRES 8 A 316 LYS VAL SER LEU GLN LEU ARG GLY GLU ASP GLY SER VAL
SEQRES 9 A 316 TRP ASN TYR LYS PRO PRO ALA ASP SER GLY GLY LYS GLU
SEQRES 10 A 316 ILE PHE SER LEU LEU PRO HIS MET ALA ASP MET SER THR
SEQRES 11 A 316 TYR MET PHE LYS GLY ILE ILE SER PHE ALA LYS VAL ILE
SEQRES 12 A 316 SER TYR PHE ARG ASP LEU PRO ILE GLU ASP GLN ILE SER
SEQRES 13 A 316 LEU LEU LYS GLY ALA ALA PHE GLU LEU CYS GLN LEU ARG
SEQRES 14 A 316 PHE ASN THR VAL PHE ASN ALA GLU THR GLY THR TRP GLU
SEQRES 15 A 316 CYS GLY ARG LEU SER TYR CYS LEU GLU ASP THR ALA GLY
SEQRES 16 A 316 GLY PHE GLN GLN LEU LEU LEU GLU PRO MET LEU LYS PHE
SEQRES 17 A 316 HIS TYR MET LEU LYS LYS LEU GLN LEU HIS GLU GLU GLU
SEQRES 18 A 316 TYR VAL LEU MET GLN ALA ILE SER LEU PHE SER PRO ASP
SEQRES 19 A 316 ARG PRO GLY VAL LEU GLN HIS ARG VAL VAL ASP GLN LEU
SEQRES 20 A 316 GLN GLU GLN PHE ALA ILE THR LEU LYS SER TYR ILE GLU
SEQRES 21 A 316 CYS ASN ARG PRO GLN PRO ALA HIS ARG PHE LEU PHE LEU
SEQRES 22 A 316 LYS ILE MET ALA MET LEU THR GLU LEU ARG SER ILE ASN
SEQRES 23 A 316 ALA GLN HIS THR GLN ARG LEU LEU ARG ILE GLN ASP ILE
SEQRES 24 A 316 HIS PRO PHE ALA THR PRO LEU MET GLN GLU LEU PHE GLY
SEQRES 25 A 316 ILE THR GLY SER
HET 3WF A 501 22
HET 3WG A 502 19
HET MPD A 503 8
HET IPA A 504 4
HETNAM 3WF ETHINYL ESTRADIOL
HETNAM 3WG TRANS-NONACHLOR
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM IPA ISOPROPYL ALCOHOL
HETSYN IPA 2-PROPANOL
FORMUL 2 3WF C20 H24 O2
FORMUL 3 3WG C10 H5 CL9
FORMUL 4 MPD C6 H14 O2
FORMUL 5 IPA C3 H8 O
FORMUL 6 HOH *122(H2 O)
HELIX 1 AA1 THR A 144 PHE A 162 1 19
HELIX 2 AA2 ARG A 193 CYS A 207 1 15
HELIX 3 AA3 GLY A 233 SER A 238 5 6
HELIX 4 AA4 LEU A 239 ILE A 261 1 23
HELIX 5 AA5 ILE A 261 ASP A 266 1 6
HELIX 6 AA6 PRO A 268 THR A 290 1 23
HELIX 7 AA7 GLY A 313 LEU A 319 1 7
HELIX 8 AA8 GLU A 321 LEU A 333 1 13
HELIX 9 AA9 HIS A 336 PHE A 349 1 14
HELIX 10 AB1 GLN A 358 ARG A 381 1 24
HELIX 11 AB2 GLN A 383 ARG A 387 5 5
HELIX 12 AB3 PHE A 388 HIS A 418 1 31
HELIX 13 AB4 THR A 422 GLY A 430 1 9
SHEET 1 AA1 5 VAL A 222 TYR A 225 0
SHEET 2 AA1 5 VAL A 211 ARG A 216 -1 N LEU A 213 O TYR A 225
SHEET 3 AA1 5 LEU A 304 LEU A 308 -1 O CYS A 307 N SER A 212
SHEET 4 AA1 5 THR A 298 CYS A 301 -1 N TRP A 299 O TYR A 306
SHEET 5 AA1 5 PHE A 292 ASN A 293 -1 N ASN A 293 O THR A 298
SITE 1 AC1 10 ASP A 205 LEU A 206 LEU A 240 SER A 247
SITE 2 AC1 10 PHE A 251 HIS A 407 ARG A 410 ILE A 414
SITE 3 AC1 10 MET A 425 3WG A 502
SITE 1 AC2 9 MET A 243 PHE A 281 GLN A 285 PHE A 288
SITE 2 AC2 9 TRP A 299 TYR A 306 MET A 323 HIS A 407
SITE 3 AC2 9 3WF A 501
SITE 1 AC3 4 GLU A 337 TYR A 340 ARG A 387 HOH A 670
SITE 1 AC4 3 LYS A 160 ASP A 163 HOH A 695
CRYST1 91.340 91.340 85.490 90.00 90.00 90.00 P 43 21 2 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 0.010948 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010948 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011697 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
