HEADER TRANSCRIPTION/TRANSCRIPTION INHIBITOR 18-FEB-15 4YAX
TITLE CRYSTAL STRUCTURE OF TRIM24 PHD-BROMODOMAIN COMPLEXED WITH N-[6-(4-
TITLE 2 METHOXYPHENOXY)-1,3-DIMETHYL-2-OXO-2,3-DIHYDRO-1H-1,3-BENZODIAZOL-5-
TITLE 3 YL]BENZENESULFONAMIDE (5G)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTION INTERMEDIARY FACTOR 1-ALPHA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: BROMODOMAIN (UNP RESIDUES 824-1006);
COMPND 5 SYNONYM: TIF1-ALPHA,E3 UBIQUITIN-PROTEIN LIGASE TRIM24,RING FINGER
COMPND 6 PROTEIN 82,TRIPARTITE MOTIF-CONTAINING PROTEIN 24;
COMPND 7 EC: 6.3.2.-;
COMPND 8 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: TRIM24, RNF82, TIF1, TIF1A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PRSFDUET-1
KEYWDS CENTER FOR BIOMOLECULAR STRUCTURE AND FUNCTION, BROMODOMAIN, TRIM24,
KEYWDS 2 INHIBITOR, TRANSCRIPTION-TRANSCRIPTION INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR G.PONCET-MONTANGE,W.PALMER,P.JONES
REVDAT 3 27-SEP-23 4YAX 1 JRNL REMARK
REVDAT 2 09-MAR-16 4YAX 1 JRNL
REVDAT 1 24-JUN-15 4YAX 0
JRNL AUTH W.S.PALMER,G.PONCET-MONTANGE,G.LIU,A.PETROCCHI,N.REYNA,
JRNL AUTH 2 G.SUBRAMANIAN,J.THEROFF,A.YAU,M.KOST-ALIMOVA,
JRNL AUTH 3 J.P.BARDENHAGEN,E.LEO,H.E.SHEPARD,T.N.TIEU,X.SHI,Y.ZHAN,
JRNL AUTH 4 S.ZHAO,M.C.BARTON,G.DRAETTA,C.TONIATTI,P.JONES,M.GECK DO,
JRNL AUTH 5 J.N.ANDERSEN
JRNL TITL STRUCTURE-GUIDED DESIGN OF IACS-9571, A SELECTIVE
JRNL TITL 2 HIGH-AFFINITY DUAL TRIM24-BRPF1 BROMODOMAIN INHIBITOR.
JRNL REF J.MED.CHEM. V. 59 1440 2016
JRNL REFN ISSN 0022-2623
JRNL PMID 26061247
JRNL DOI 10.1021/ACS.JMEDCHEM.5B00405
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 120.67
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 17581
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) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 969
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) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.31
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1236
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.32
REMARK 3 BIN R VALUE (WORKING SET) : 0.2480
REMARK 3 BIN FREE R VALUE SET COUNT : 69
REMARK 3 BIN FREE R VALUE : 0.2560
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2904
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 77
REMARK 3 SOLVENT ATOMS : 384
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : -0.02000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.02000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.364
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.240
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.184
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.591
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.904
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3093 ; 0.012 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 2865 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4204 ; 1.450 ; 2.019
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6670 ; 0.813 ; 3.004
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 366 ; 5.988 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 141 ;37.831 ;25.319
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 539 ;16.293 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;13.045 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 447 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3411 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 663 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1446 ; 2.116 ; 2.513
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1445 ; 2.116 ; 2.513
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1806 ; 3.699 ; 3.741
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.30
REMARK 3 ION PROBE RADIUS : 0.70
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 4
REMARK 4 4YAX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-FEB-15.
REMARK 100 THE DEPOSITION ID IS D_1000207141.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JUN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1159
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.3.11
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18553
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 120.670
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.11600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.0000
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) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.47700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 3O34
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.2-2.4M AMMONIUM SULFATE, 0.1M HEPES
REMARK 280 BUFFER PH 7.5, 2% PEG400 AND 8-9% GLYCEROL, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 45.02000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 18.55500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 45.02000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 18.55500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: MONOMERIC
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 HIS A 887
REMARK 465 ASN A 888
REMARK 465 SER A 889
REMARK 465 GLU A 890
REMARK 465 SER B 823
REMARK 465 SER B 886
REMARK 465 HIS B 887
REMARK 465 ASN B 888
REMARK 465 SER B 889
REMARK 465 GLU B 890
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 O HOH A 1246 O HOH A 1271 1.97
REMARK 500 O HOH B 1233 O HOH B 1248 2.03
REMARK 500 O HOH A 1272 O HOH A 1388 2.05
REMARK 500 O HOH A 1328 O HOH A 1347 2.07
REMARK 500 O HOH A 1249 O HOH A 1262 2.09
REMARK 500 O LEU A 930 O HOH A 1201 2.11
REMARK 500 O VAL A 928 OH TYR A 936 2.14
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 TYR A 956 57.76 -111.73
REMARK 500 ASN B 825 155.51 68.80
REMARK 500 VAL B 831 -60.38 -90.60
REMARK 500 ASP B 983 16.09 53.51
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 B1379 DISTANCE = 6.51 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1103 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 829 SG
REMARK 620 2 CYS A 832 SG 111.8
REMARK 620 3 HIS A 849 ND1 109.0 93.1
REMARK 620 4 CYS A 852 SG 112.1 119.2 109.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1102 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 841 SG
REMARK 620 2 CYS A 844 SG 110.1
REMARK 620 3 CYS A 867 SG 107.9 113.6
REMARK 620 4 CYS A 870 SG 114.1 100.1 111.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 829 SG
REMARK 620 2 CYS B 832 SG 111.6
REMARK 620 3 HIS B 849 ND1 100.2 98.9
REMARK 620 4 CYS B 852 SG 110.4 117.9 116.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1102 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 841 SG
REMARK 620 2 CYS B 844 SG 111.7
REMARK 620 3 CYS B 867 SG 110.7 109.5
REMARK 620 4 CYS B 870 SG 114.5 98.2 111.6
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 4AE A 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 1103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 4AE B 1104
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4YAB RELATED DB: PDB
REMARK 900 RELATED ID: 4YAD RELATED DB: PDB
REMARK 900 RELATED ID: 4YAT RELATED DB: PDB
REMARK 900 RELATED ID: 4YBM RELATED DB: PDB
REMARK 900 RELATED ID: 4YBS RELATED DB: PDB
REMARK 900 RELATED ID: 4YBT RELATED DB: PDB
DBREF 4YAX A 824 1006 UNP O15164 TIF1A_HUMAN 824 1006
DBREF 4YAX B 824 1006 UNP O15164 TIF1A_HUMAN 824 1006
SEQADV 4YAX SER A 823 UNP O15164 EXPRESSION TAG
SEQADV 4YAX SER B 823 UNP O15164 EXPRESSION TAG
SEQRES 1 A 184 SER PRO ASN GLU ASP TRP CYS ALA VAL CYS GLN ASN GLY
SEQRES 2 A 184 GLY GLU LEU LEU CYS CYS GLU LYS CYS PRO LYS VAL PHE
SEQRES 3 A 184 HIS LEU SER CYS HIS VAL PRO THR LEU THR ASN PHE PRO
SEQRES 4 A 184 SER GLY GLU TRP ILE CYS THR PHE CYS ARG ASP LEU SER
SEQRES 5 A 184 LYS PRO GLU VAL GLU TYR ASP CYS ASP ALA PRO SER HIS
SEQRES 6 A 184 ASN SER GLU LYS LYS LYS THR GLU GLY LEU VAL LYS LEU
SEQRES 7 A 184 THR PRO ILE ASP LYS ARG LYS CYS GLU ARG LEU LEU LEU
SEQRES 8 A 184 PHE LEU TYR CYS HIS GLU MET SER LEU ALA PHE GLN ASP
SEQRES 9 A 184 PRO VAL PRO LEU THR VAL PRO ASP TYR TYR LYS ILE ILE
SEQRES 10 A 184 LYS ASN PRO MET ASP LEU SER THR ILE LYS LYS ARG LEU
SEQRES 11 A 184 GLN GLU ASP TYR SER MET TYR SER LYS PRO GLU ASP PHE
SEQRES 12 A 184 VAL ALA ASP PHE ARG LEU ILE PHE GLN ASN CYS ALA GLU
SEQRES 13 A 184 PHE ASN GLU PRO ASP SER GLU VAL ALA ASN ALA GLY ILE
SEQRES 14 A 184 LYS LEU GLU ASN TYR PHE GLU GLU LEU LEU LYS ASN LEU
SEQRES 15 A 184 TYR PRO
SEQRES 1 B 184 SER PRO ASN GLU ASP TRP CYS ALA VAL CYS GLN ASN GLY
SEQRES 2 B 184 GLY GLU LEU LEU CYS CYS GLU LYS CYS PRO LYS VAL PHE
SEQRES 3 B 184 HIS LEU SER CYS HIS VAL PRO THR LEU THR ASN PHE PRO
SEQRES 4 B 184 SER GLY GLU TRP ILE CYS THR PHE CYS ARG ASP LEU SER
SEQRES 5 B 184 LYS PRO GLU VAL GLU TYR ASP CYS ASP ALA PRO SER HIS
SEQRES 6 B 184 ASN SER GLU LYS LYS LYS THR GLU GLY LEU VAL LYS LEU
SEQRES 7 B 184 THR PRO ILE ASP LYS ARG LYS CYS GLU ARG LEU LEU LEU
SEQRES 8 B 184 PHE LEU TYR CYS HIS GLU MET SER LEU ALA PHE GLN ASP
SEQRES 9 B 184 PRO VAL PRO LEU THR VAL PRO ASP TYR TYR LYS ILE ILE
SEQRES 10 B 184 LYS ASN PRO MET ASP LEU SER THR ILE LYS LYS ARG LEU
SEQRES 11 B 184 GLN GLU ASP TYR SER MET TYR SER LYS PRO GLU ASP PHE
SEQRES 12 B 184 VAL ALA ASP PHE ARG LEU ILE PHE GLN ASN CYS ALA GLU
SEQRES 13 B 184 PHE ASN GLU PRO ASP SER GLU VAL ALA ASN ALA GLY ILE
SEQRES 14 B 184 LYS LEU GLU ASN TYR PHE GLU GLU LEU LEU LYS ASN LEU
SEQRES 15 B 184 TYR PRO
HET 4AE A1101 31
HET ZN A1102 1
HET ZN A1103 1
HET GOL A1104 6
HET ZN B1101 1
HET ZN B1102 1
HET SO4 B1103 5
HET 4AE B1104 31
HETNAM 4AE N-[6-(4-METHOXYPHENOXY)-1,3-DIMETHYL-2-OXO-2,3-DIHYDRO-
HETNAM 2 4AE 1H-BENZIMIDAZOL-5-YL]BENZENESULFONAMIDE
HETNAM ZN ZINC ION
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 4AE 2(C22 H21 N3 O5 S)
FORMUL 4 ZN 4(ZN 2+)
FORMUL 6 GOL C3 H8 O3
FORMUL 9 SO4 O4 S 2-
FORMUL 11 HOH *384(H2 O)
HELIX 1 AA1 TYR A 880 ALA A 884 5 5
HELIX 2 AA2 THR A 901 HIS A 918 1 18
HELIX 3 AA3 SER A 921 ASP A 926 1 6
HELIX 4 AA4 ASP A 934 ILE A 939 1 6
HELIX 5 AA5 ASP A 944 GLU A 954 1 11
HELIX 6 AA6 LYS A 961 ASN A 980 1 20
HELIX 7 AA7 SER A 984 TYR A 1005 1 22
HELIX 8 AA8 TYR B 880 ALA B 884 5 5
HELIX 9 AA9 THR B 901 HIS B 918 1 18
HELIX 10 AB1 GLU B 919 GLN B 925 5 7
HELIX 11 AB2 ASP B 934 ILE B 939 1 6
HELIX 12 AB3 ASP B 944 GLU B 954 1 11
HELIX 13 AB4 LYS B 961 ASN B 980 1 20
HELIX 14 AB5 SER B 984 TYR B 1005 1 22
SHEET 1 AA1 2 LEU A 839 CYS A 840 0
SHEET 2 AA1 2 VAL A 847 PHE A 848 -1 O PHE A 848 N LEU A 839
SHEET 1 AA2 2 LEU B 839 CYS B 840 0
SHEET 2 AA2 2 VAL B 847 PHE B 848 -1 O PHE B 848 N LEU B 839
LINK SG CYS A 829 ZN ZN A1103 1555 1555 2.23
LINK SG CYS A 832 ZN ZN A1103 1555 1555 2.28
LINK SG CYS A 841 ZN ZN A1102 1555 1555 2.26
LINK SG CYS A 844 ZN ZN A1102 1555 1555 2.35
LINK ND1 HIS A 849 ZN ZN A1103 1555 1555 2.34
LINK SG CYS A 852 ZN ZN A1103 1555 1555 2.12
LINK SG CYS A 867 ZN ZN A1102 1555 1555 2.45
LINK SG CYS A 870 ZN ZN A1102 1555 1555 2.15
LINK SG CYS B 829 ZN ZN B1101 1555 1555 2.25
LINK SG CYS B 832 ZN ZN B1101 1555 1555 2.26
LINK SG CYS B 841 ZN ZN B1102 1555 1555 2.09
LINK SG CYS B 844 ZN ZN B1102 1555 1555 2.32
LINK ND1 HIS B 849 ZN ZN B1101 1555 1555 2.18
LINK SG CYS B 852 ZN ZN B1101 1555 1555 2.25
LINK SG CYS B 867 ZN ZN B1102 1555 1555 2.43
LINK SG CYS B 870 ZN ZN B1102 1555 1555 2.26
CISPEP 1 VAL A 854 PRO A 855 0 -6.40
CISPEP 2 VAL B 854 PRO B 855 0 -4.32
SITE 1 AC1 10 LEU A 922 ALA A 923 VAL A 928 PRO A 929
SITE 2 AC1 10 VAL A 932 PHE A 979 ASN A 980 VAL A 986
SITE 3 AC1 10 HOH A1304 LEU B 930
SITE 1 AC2 4 CYS A 841 CYS A 844 CYS A 867 CYS A 870
SITE 1 AC3 4 CYS A 829 CYS A 832 HIS A 849 CYS A 852
SITE 1 AC4 6 TRP A 828 ASN A 834 GLY A 835 ASP B 827
SITE 2 AC4 6 GLY B 835 GLY B 836
SITE 1 AC5 4 CYS B 829 CYS B 832 HIS B 849 CYS B 852
SITE 1 AC6 4 CYS B 841 CYS B 844 CYS B 867 CYS B 870
SITE 1 AC7 2 LYS B 950 ARG B 951
SITE 1 AC8 7 LEU A 930 ALA B 923 VAL B 928 PRO B 929
SITE 2 AC8 7 PHE B 979 ASN B 980 HOH B1265
CRYST1 90.040 37.110 128.750 90.00 110.41 90.00 C 1 2 1 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 0.011106 0.000000 0.004133 0.00000
SCALE2 0.000000 0.026947 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008287 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
