HEADER HORMONE 15-MAR-17 5NFT
TITLE GLUCOCORTICOID RECEPTOR IN COMPLEX WITH AZD5423
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCOCORTICOID RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GR,NUCLEAR RECEPTOR SUBFAMILY 3 GROUP C MEMBER 1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: NUCLEAR RECEPTOR COACTIVATOR 2;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: NCOA-2,CLASS E BASIC HELIX-LOOP-HELIX PROTEIN 75,BHLHE75,
COMPND 10 TRANSCRIPTIONAL INTERMEDIARY FACTOR 2,HTIF2;
COMPND 11 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: NR3C1, GRL;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606
KEYWDS GLUCOCORTICOID RECEPTOR, NUCLEAR HORMONE RECEPTOR, STEROID RECEPTOR,
KEYWDS 2 LIGAND COMPLEX, PEPTIDE COMPLEX, HORMONE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.EDMAN,L.WISSLER
REVDAT 3 17-JAN-24 5NFT 1 REMARK
REVDAT 2 08-NOV-17 5NFT 1 JRNL
REVDAT 1 04-OCT-17 5NFT 0
JRNL AUTH M.HEMMERLING,S.NILSSON,K.EDMAN,S.EIREFELT,W.RUSSELL,
JRNL AUTH 2 R.HENDRICKX,E.JOHNSSON,C.KARRMAN MARDH,M.BERGER,H.REHWINKEL,
JRNL AUTH 3 A.ABRAHAMSSON,J.DAHMEN,A.R.ERIKSSON,B.GABOS,K.HENRIKSSON,
JRNL AUTH 4 N.HOSSAIN,S.IVANOVA,A.H.JANSSON,T.J.JENSEN,A.JERRE,
JRNL AUTH 5 H.JOHANSSON,T.KLINGSTEDT,M.LEPISTO,M.LINDSJO,I.MILE,
JRNL AUTH 6 G.NIKITIDIS,J.STEELE,U.TEHLER,L.WISSLER,T.HANSSON
JRNL TITL SELECTIVE NONSTEROIDAL GLUCOCORTICOID RECEPTOR MODULATORS
JRNL TITL 2 FOR THE INHALED TREATMENT OF PULMONARY DISEASES.
JRNL REF J. MED. CHEM. V. 60 8591 2017
JRNL REFN ISSN 1520-4804
JRNL PMID 28937774
JRNL DOI 10.1021/ACS.JMEDCHEM.7B01215
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.6
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.93
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 19795
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 1004
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.000
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.42
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.99
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2844
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1990
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2705
REMARK 3 BIN R VALUE (WORKING SET) : 0.1970
REMARK 3 BIN FREE R VALUE : 0.2350
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.89
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 139
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 : 2122
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 47
REMARK 3 SOLVENT ATOMS : 119
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 47.53
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.89660
REMARK 3 B22 (A**2) : -4.89660
REMARK 3 B33 (A**2) : 9.79330
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) : 0.260
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.206
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.170
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.199
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.168
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 : 0.938
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2223 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3002 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 796 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 57 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 318 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2223 ; 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 : 282 ; 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 : 2638 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 0.96
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.53
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.27
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 6.8163 -35.5630 -3.0379
REMARK 3 T TENSOR
REMARK 3 T11: -0.2201 T22: -0.0619
REMARK 3 T33: -0.1369 T12: 0.0347
REMARK 3 T13: 0.0324 T23: 0.0438
REMARK 3 L TENSOR
REMARK 3 L11: 1.6725 L22: 2.0183
REMARK 3 L33: 2.9792 L12: -0.1798
REMARK 3 L13: 0.9169 L23: -0.5630
REMARK 3 S TENSOR
REMARK 3 S11: 0.0121 S12: 0.0647 S13: -0.0079
REMARK 3 S21: -0.0159 S22: -0.1594 S23: -0.2742
REMARK 3 S31: 0.1805 S32: 0.5083 S33: 0.1474
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -8.4721 -22.7857 1.6059
REMARK 3 T TENSOR
REMARK 3 T11: -0.0935 T22: 0.0064
REMARK 3 T33: 0.0347 T12: 0.0354
REMARK 3 T13: 0.0273 T23: -0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 3.8621 L22: 1.6745
REMARK 3 L33: 0.5552 L12: -1.4079
REMARK 3 L13: 0.1164 L23: 2.7916
REMARK 3 S TENSOR
REMARK 3 S11: -0.0347 S12: -0.0147 S13: 0.1072
REMARK 3 S21: 0.0525 S22: 0.0298 S23: 0.0169
REMARK 3 S31: -0.0858 S32: -0.0792 S33: 0.0049
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5NFT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1200004043.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-APR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
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 : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19805
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 42.930
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 8.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.36
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 9.40
REMARK 200 R MERGE FOR SHELL (I) : 0.21200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 9.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4CSJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 UL OF PROTEIN AND 1UL OF WELL
REMARK 280 SOLUTION (8-12% PEG8000, 10-20% ETHYLENE GLYCOL AND 0.1 M HEPES
REMARK 280 PH 7.5), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 70.74600
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 35.37300
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 35.37300
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 70.74600
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: 1840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 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 498
REMARK 465 SER A 499
REMARK 465 ILE A 500
REMARK 465 GLN A 501
REMARK 465 GLN A 502
REMARK 465 ALA A 503
REMARK 465 THR A 504
REMARK 465 THR A 505
REMARK 465 GLY A 506
REMARK 465 VAL A 507
REMARK 465 SER A 508
REMARK 465 GLN A 509
REMARK 465 GLU A 510
REMARK 465 THR A 511
REMARK 465 SER A 512
REMARK 465 GLU A 513
REMARK 465 ASN A 514
REMARK 465 PRO A 515
REMARK 465 GLY A 516
REMARK 465 ASP A 517
REMARK 465 LYS A 518
REMARK 465 THR A 519
REMARK 465 ILE A 520
REMARK 465 VAL A 521
REMARK 465 PRO A 522
REMARK 465 ALA A 523
REMARK 465 THR A 524
REMARK 465 LEU A 525
REMARK 465 PRO A 526
REMARK 465 GLN A 527
REMARK 465 LEU A 528
REMARK 465 LYS A 777
REMARK 465 LYS B 740
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 LEU A 627 84.83 -156.72
REMARK 500 SER A 682 54.01 -105.65
REMARK 500 GLU A 705 105.63 -50.87
REMARK 500 ASN B 742 59.11 -113.88
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 A1014 DISTANCE = 5.95 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8W8 A 804
DBREF 5NFT A 500 777 UNP P04150 GCR_HUMAN 500 777
DBREF 5NFT B 740 753 UNP Q15596 NCOA2_HUMAN 740 753
SEQADV 5NFT GLY A 498 UNP P04150 EXPRESSION TAG
SEQADV 5NFT SER A 499 UNP P04150 EXPRESSION TAG
SEQADV 5NFT ASP A 517 UNP P04150 ASN 517 ENGINEERED MUTATION
SEQADV 5NFT MET A 571 UNP P04150 VAL 571 ENGINEERED MUTATION
SEQADV 5NFT SER A 602 UNP P04150 PHE 602 ENGINEERED MUTATION
SEQADV 5NFT ASP A 638 UNP P04150 CYS 638 ENGINEERED MUTATION
SEQADV 5NFT ALA A 684 UNP P04150 GLU 684 ENGINEERED MUTATION
SEQADV 5NFT SER A 712 UNP P04150 TRP 712 ENGINEERED MUTATION
SEQRES 1 A 280 GLY SER ILE GLN GLN ALA THR THR GLY VAL SER GLN GLU
SEQRES 2 A 280 THR SER GLU ASN PRO GLY ASP LYS THR ILE VAL PRO ALA
SEQRES 3 A 280 THR LEU PRO GLN LEU THR PRO THR LEU VAL SER LEU LEU
SEQRES 4 A 280 GLU VAL ILE GLU PRO GLU VAL LEU TYR ALA GLY TYR ASP
SEQRES 5 A 280 SER SER VAL PRO ASP SER THR TRP ARG ILE MET THR THR
SEQRES 6 A 280 LEU ASN MET LEU GLY GLY ARG GLN MET ILE ALA ALA VAL
SEQRES 7 A 280 LYS TRP ALA LYS ALA ILE PRO GLY PHE ARG ASN LEU HIS
SEQRES 8 A 280 LEU ASP ASP GLN MET THR LEU LEU GLN TYR SER TRP MET
SEQRES 9 A 280 SER LEU MET ALA PHE ALA LEU GLY TRP ARG SER TYR ARG
SEQRES 10 A 280 GLN SER SER ALA ASN LEU LEU CYS PHE ALA PRO ASP LEU
SEQRES 11 A 280 ILE ILE ASN GLU GLN ARG MET THR LEU PRO ASP MET TYR
SEQRES 12 A 280 ASP GLN CYS LYS HIS MET LEU TYR VAL SER SER GLU LEU
SEQRES 13 A 280 HIS ARG LEU GLN VAL SER TYR GLU GLU TYR LEU CYS MET
SEQRES 14 A 280 LYS THR LEU LEU LEU LEU SER SER VAL PRO LYS ASP GLY
SEQRES 15 A 280 LEU LYS SER GLN ALA LEU PHE ASP GLU ILE ARG MET THR
SEQRES 16 A 280 TYR ILE LYS GLU LEU GLY LYS ALA ILE VAL LYS ARG GLU
SEQRES 17 A 280 GLY ASN SER SER GLN ASN SER GLN ARG PHE TYR GLN LEU
SEQRES 18 A 280 THR LYS LEU LEU ASP SER MET HIS GLU VAL VAL GLU ASN
SEQRES 19 A 280 LEU LEU ASN TYR CYS PHE GLN THR PHE LEU ASP LYS THR
SEQRES 20 A 280 MET SER ILE GLU PHE PRO GLU MET LEU ALA GLU ILE ILE
SEQRES 21 A 280 THR ASN GLN ILE PRO LYS TYR SER ASN GLY ASN ILE LYS
SEQRES 22 A 280 LYS LEU LEU PHE HIS GLN LYS
SEQRES 1 B 14 LYS GLU ASN ALA LEU LEU ARG TYR LEU LEU ASP LYS ASP
SEQRES 2 B 14 ASP
HET EDO A 801 4
HET EDO A 802 4
HET EDO A 803 4
HET 8W8 A 804 35
HETNAM EDO 1,2-ETHANEDIOL
HETNAM 8W8 2,2,2-TRIS(FLUORANYL)-~{N}-[(1~{R},2~{S})-1-[1-(4-
HETNAM 2 8W8 FLUOROPHENYL)INDAZOL-5-YL]OXY-1-(3-METHOXYPHENYL)
HETNAM 3 8W8 PROPAN-2-YL]ETHANAMIDE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 3(C2 H6 O2)
FORMUL 6 8W8 C25 H21 F4 N3 O3
FORMUL 7 HOH *119(H2 O)
HELIX 1 AA1 THR A 531 ILE A 539 1 9
HELIX 2 AA2 SER A 555 ALA A 580 1 26
HELIX 3 AA3 GLY A 583 LEU A 587 5 5
HELIX 4 AA4 HIS A 588 SER A 616 1 29
HELIX 5 AA5 ASN A 630 THR A 635 1 6
HELIX 6 AA6 ASP A 638 LEU A 656 1 19
HELIX 7 AA7 SER A 659 LEU A 672 1 14
HELIX 8 AA8 SER A 682 ARG A 704 1 23
HELIX 9 AA9 ASN A 707 ASP A 742 1 36
HELIX 10 AB1 LYS A 743 SER A 746 5 4
HELIX 11 AB2 PRO A 750 ASN A 766 1 17
HELIX 12 AB3 ASN B 742 LYS B 751 1 10
SHEET 1 AA1 2 LEU A 621 ALA A 624 0
SHEET 2 AA1 2 LEU A 627 ILE A 629 -1 O ILE A 629 N LEU A 621
SHEET 1 AA2 2 SER A 674 VAL A 675 0
SHEET 2 AA2 2 LYS A 770 LYS A 771 -1 O LYS A 770 N VAL A 675
SITE 1 AC1 6 PRO A 541 ALA A 574 TRP A 577 LYS A 667
SITE 2 AC1 6 HOH A 925 HOH A 959
SITE 1 AC2 1 HIS A 645
SITE 1 AC3 2 PRO A 750 GLU A 751
SITE 1 AC4 16 MET A 560 LEU A 563 ASN A 564 LEU A 566
SITE 2 AC4 16 GLY A 567 GLN A 570 MET A 604 ALA A 607
SITE 3 AC4 16 LEU A 608 ARG A 611 PHE A 623 GLN A 642
SITE 4 AC4 16 TYR A 735 CYS A 736 THR A 739 PHE A 749
CRYST1 84.371 84.371 106.119 90.00 90.00 120.00 P 32 2 1 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 0.011852 0.006843 0.000000 0.00000
SCALE2 0.000000 0.013686 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009423 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
