HEADER TRANSCRIPTION 02-NOV-15 5EJV
TITLE RORY IN COMPLEX WITH T090131718 AND COACTIVATOR PEPTIDE EBI96
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUCLEAR RECEPTOR ROR-GAMMA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN (UNP RESIDUES 259-518);
COMPND 5 SYNONYM: NUCLEAR RECEPTOR RZR-GAMMA,NUCLEAR RECEPTOR SUBFAMILY 1
COMPND 6 GROUP F MEMBER 3,RAR-RELATED ORPHAN RECEPTOR C,RETINOID-RELATED
COMPND 7 ORPHAN RECEPTOR-GAMMA;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: EBI96 COACTIVATOR PEPTIDE;
COMPND 11 CHAIN: C, D;
COMPND 12 FRAGMENT: COACTIVATOR PEPTIDE;
COMPND 13 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: RORC, NR1F3, RORG, RZRG;
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: PGEX;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 14 ORGANISM_TAXID: 32630;
SOURCE 15 OTHER_DETAILS: PEPTIDE SYNTHESIS
KEYWDS RORGAMMA, T090131718, COACTIVATOR PEPTIDE, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR D.M.MARCOTTE
REVDAT 3 27-SEP-23 5EJV 1 JRNL REMARK
REVDAT 2 29-JUN-16 5EJV 1 JRNL
REVDAT 1 27-APR-16 5EJV 0
JRNL AUTH I.J.ENYEDY,N.A.POWELL,J.CARAVELLA,K.VAN VLOTEN,J.CHAO,
JRNL AUTH 2 D.BANERJEE,D.MARCOTTE,L.SILVIAN,A.MCKENZIE,V.S.HONG,
JRNL AUTH 3 J.D.FONTENOT
JRNL TITL DISCOVERY OF BIARYLS AS ROR GAMMA INVERSE AGONISTS BY USING
JRNL TITL 2 STRUCTURE-BASED DESIGN.
JRNL REF BIOORG.MED.CHEM.LETT. V. 26 2459 2016
JRNL REFN ESSN 1464-3405
JRNL PMID 27080181
JRNL DOI 10.1016/J.BMCL.2016.03.109
REMARK 2
REMARK 2 RESOLUTION. 2.58 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0131
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) : 2.58
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 63.14
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 18768
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) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 968
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) : 2.58
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.65
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1397
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.2230
REMARK 3 BIN FREE R VALUE SET COUNT : 62
REMARK 3 BIN FREE R VALUE : 0.2870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4163
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 62
REMARK 3 SOLVENT ATOMS : 32
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.39
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.11000
REMARK 3 B22 (A**2) : 0.11000
REMARK 3 B33 (A**2) : -0.23000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.739
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.289
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.209
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.848
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4322 ; 0.019 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4131 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5846 ; 2.074 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9457 ; 1.152 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 509 ; 5.346 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 207 ;32.671 ;22.995
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 765 ;18.181 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;21.843 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 645 ; 0.133 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4797 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1077 ; 0.002 ; 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): 2048 ; 2.713 ; 3.847
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2047 ; 2.709 ; 3.846
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2553 ; 4.133 ; 5.766
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 : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 263 A 507
REMARK 3 ORIGIN FOR THE GROUP (A): 10.5978 62.8275 -20.3193
REMARK 3 T TENSOR
REMARK 3 T11: 0.0086 T22: 0.0113
REMARK 3 T33: 0.0220 T12: -0.0008
REMARK 3 T13: 0.0034 T23: 0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 0.3802 L22: 0.4089
REMARK 3 L33: 0.5377 L12: -0.2439
REMARK 3 L13: 0.1416 L23: 0.1104
REMARK 3 S TENSOR
REMARK 3 S11: 0.0083 S12: 0.0185 S13: -0.0271
REMARK 3 S21: -0.0050 S22: 0.0391 S23: 0.0492
REMARK 3 S31: 0.0049 S32: 0.0466 S33: -0.0474
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 11
REMARK 3 ORIGIN FOR THE GROUP (A): 26.0182 59.5553 -10.1587
REMARK 3 T TENSOR
REMARK 3 T11: 0.0407 T22: 0.0993
REMARK 3 T33: 0.0376 T12: 0.0609
REMARK 3 T13: -0.0176 T23: -0.0163
REMARK 3 L TENSOR
REMARK 3 L11: 1.4183 L22: 3.5637
REMARK 3 L33: 6.5141 L12: -2.1252
REMARK 3 L13: 0.7745 L23: 0.3557
REMARK 3 S TENSOR
REMARK 3 S11: -0.0066 S12: -0.0155 S13: 0.0810
REMARK 3 S21: 0.0098 S22: 0.0494 S23: -0.1472
REMARK 3 S31: -0.0393 S32: 0.0439 S33: -0.0428
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 264 B 508
REMARK 3 ORIGIN FOR THE GROUP (A): 40.9907 91.6913 -27.2662
REMARK 3 T TENSOR
REMARK 3 T11: 0.0087 T22: 0.0177
REMARK 3 T33: 0.0250 T12: 0.0069
REMARK 3 T13: 0.0132 T23: 0.0143
REMARK 3 L TENSOR
REMARK 3 L11: 0.2267 L22: 1.1297
REMARK 3 L33: 0.8032 L12: -0.3055
REMARK 3 L13: 0.0443 L23: 0.6090
REMARK 3 S TENSOR
REMARK 3 S11: -0.0296 S12: 0.0104 S13: -0.0230
REMARK 3 S21: 0.0601 S22: 0.0048 S23: 0.0626
REMARK 3 S31: 0.0203 S32: 0.0540 S33: 0.0248
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 2 D 13
REMARK 3 ORIGIN FOR THE GROUP (A): 55.7884 85.2317 -18.2785
REMARK 3 T TENSOR
REMARK 3 T11: 0.1211 T22: 0.0698
REMARK 3 T33: 0.2345 T12: 0.0255
REMARK 3 T13: -0.0818 T23: -0.0562
REMARK 3 L TENSOR
REMARK 3 L11: 0.6554 L22: 10.3806
REMARK 3 L33: 0.1065 L12: -2.5820
REMARK 3 L13: 0.1935 L23: -0.7768
REMARK 3 S TENSOR
REMARK 3 S11: -0.1070 S12: -0.0678 S13: 0.0030
REMARK 3 S21: 0.1545 S22: 0.2461 S23: 0.0144
REMARK 3 S31: 0.0171 S32: 0.0061 S33: -0.1391
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 5EJV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1000215041.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-APR-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 31-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19787
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.580
REMARK 200 RESOLUTION RANGE LOW (A) : 63.140
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.13600
REMARK 200 R SYM (I) : 0.13600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.58
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.72
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.40
REMARK 200 R MERGE FOR SHELL (I) : 0.91200
REMARK 200 R SYM FOR SHELL (I) : 0.91200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.800
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: 3L0L
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M NA ACETATE/0.2M NASCN/0.1M TRIS
REMARK 280 PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41
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,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
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 80.22050
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 40.11025
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 120.33075
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 257
REMARK 465 PRO A 258
REMARK 465 THR A 259
REMARK 465 PRO A 260
REMARK 465 GLU A 261
REMARK 465 ALA A 262
REMARK 465 THR A 508
REMARK 465 GLU A 509
REMARK 465 THR A 510
REMARK 465 GLU A 511
REMARK 465 SER A 512
REMARK 465 PRO A 513
REMARK 465 VAL A 514
REMARK 465 GLY A 515
REMARK 465 LEU A 516
REMARK 465 SER A 517
REMARK 465 LYS A 518
REMARK 465 VAL C -2
REMARK 465 GLU C -1
REMARK 465 SER C 0
REMARK 465 VAL C 12
REMARK 465 SER C 13
REMARK 465 PRO C 14
REMARK 465 GLN C 15
REMARK 465 PRO C 16
REMARK 465 GLY B 257
REMARK 465 PRO B 258
REMARK 465 THR B 259
REMARK 465 PRO B 260
REMARK 465 GLU B 261
REMARK 465 ALA B 262
REMARK 465 PRO B 263
REMARK 465 GLU B 509
REMARK 465 THR B 510
REMARK 465 GLU B 511
REMARK 465 SER B 512
REMARK 465 PRO B 513
REMARK 465 VAL B 514
REMARK 465 GLY B 515
REMARK 465 LEU B 516
REMARK 465 SER B 517
REMARK 465 LYS B 518
REMARK 465 VAL D -2
REMARK 465 GLU D -1
REMARK 465 SER D 0
REMARK 465 GLU D 1
REMARK 465 PRO D 14
REMARK 465 GLN D 15
REMARK 465 PRO D 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 GLU A 290 CG CD OE1 OE2
REMARK 470 GLU A 303 CG CD OE1 OE2
REMARK 470 LYS A 469 CG CD CE NZ
REMARK 470 GLU C 11 CG CD OE1 OE2
REMARK 470 TYR B 264 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN B 346 CG CD OE1 NE2
REMARK 470 LYS B 469 CG CD CE NZ
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 A 333 CD GLU A 333 OE2 0.066
REMARK 500 GLN A 460 CG GLN A 460 CD 0.143
REMARK 500 SER B 398 CB SER B 398 OG -0.097
REMARK 500 ASP B 402 CB ASP B 402 CG 0.138
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 MET A 358 CG - SD - CE ANGL. DEV. = -9.7 DEGREES
REMARK 500 ARG A 367 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 HIS A 479 N - CA - CB ANGL. DEV. = 11.4 DEGREES
REMARK 500 TRP B 314 CB - CA - C ANGL. DEV. = 12.6 DEGREES
REMARK 500 ARG B 364 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG B 364 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG B 367 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG B 367 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 SER B 398 CB - CA - C ANGL. DEV. = -12.2 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 GLN A 286 -60.85 75.65
REMARK 500 PHE C 2 56.47 -146.18
REMARK 500 GLN B 286 -61.32 80.65
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 444 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 444 B 601
DBREF 5EJV A 259 518 UNP P51449 RORG_HUMAN 259 518
DBREF 5EJV C -2 16 PDB 5EJV 5EJV -2 16
DBREF 5EJV B 259 518 UNP P51449 RORG_HUMAN 259 518
DBREF 5EJV D -2 16 PDB 5EJV 5EJV -2 16
SEQADV 5EJV GLY A 257 UNP P51449 EXPRESSION TAG
SEQADV 5EJV PRO A 258 UNP P51449 EXPRESSION TAG
SEQADV 5EJV GLY B 257 UNP P51449 EXPRESSION TAG
SEQADV 5EJV PRO B 258 UNP P51449 EXPRESSION TAG
SEQRES 1 A 262 GLY PRO THR PRO GLU ALA PRO TYR ALA SER LEU THR GLU
SEQRES 2 A 262 ILE GLU HIS LEU VAL GLN SER VAL CYS LYS SER TYR ARG
SEQRES 3 A 262 GLU THR CYS GLN LEU ARG LEU GLU ASP LEU LEU ARG GLN
SEQRES 4 A 262 ARG SER ASN ILE PHE SER ARG GLU GLU VAL THR GLY TYR
SEQRES 5 A 262 GLN ARG LYS SER MET TRP GLU MET TRP GLU ARG CYS ALA
SEQRES 6 A 262 HIS HIS LEU THR GLU ALA ILE GLN TYR VAL VAL GLU PHE
SEQRES 7 A 262 ALA LYS ARG LEU SER GLY PHE MET GLU LEU CYS GLN ASN
SEQRES 8 A 262 ASP GLN ILE VAL LEU LEU LYS ALA GLY ALA MET GLU VAL
SEQRES 9 A 262 VAL LEU VAL ARG MET CYS ARG ALA TYR ASN ALA ASP ASN
SEQRES 10 A 262 ARG THR VAL PHE PHE GLU GLY LYS TYR GLY GLY MET GLU
SEQRES 11 A 262 LEU PHE ARG ALA LEU GLY CYS SER GLU LEU ILE SER SER
SEQRES 12 A 262 ILE PHE ASP PHE SER HIS SER LEU SER ALA LEU HIS PHE
SEQRES 13 A 262 SER GLU ASP GLU ILE ALA LEU TYR THR ALA LEU VAL LEU
SEQRES 14 A 262 ILE ASN ALA HIS ARG PRO GLY LEU GLN GLU LYS ARG LYS
SEQRES 15 A 262 VAL GLU GLN LEU GLN TYR ASN LEU GLU LEU ALA PHE HIS
SEQRES 16 A 262 HIS HIS LEU CYS LYS THR HIS ARG GLN SER ILE LEU ALA
SEQRES 17 A 262 LYS LEU PRO PRO LYS GLY LYS LEU ARG SER LEU CYS SER
SEQRES 18 A 262 GLN HIS VAL GLU ARG LEU GLN ILE PHE GLN HIS LEU HIS
SEQRES 19 A 262 PRO ILE VAL VAL GLN ALA ALA PHE PRO PRO LEU TYR LYS
SEQRES 20 A 262 GLU LEU PHE SER THR GLU THR GLU SER PRO VAL GLY LEU
SEQRES 21 A 262 SER LYS
SEQRES 1 C 19 VAL GLU SER GLU PHE PRO TYR LEU LEU SER LEU LEU GLY
SEQRES 2 C 19 GLU VAL SER PRO GLN PRO
SEQRES 1 B 262 GLY PRO THR PRO GLU ALA PRO TYR ALA SER LEU THR GLU
SEQRES 2 B 262 ILE GLU HIS LEU VAL GLN SER VAL CYS LYS SER TYR ARG
SEQRES 3 B 262 GLU THR CYS GLN LEU ARG LEU GLU ASP LEU LEU ARG GLN
SEQRES 4 B 262 ARG SER ASN ILE PHE SER ARG GLU GLU VAL THR GLY TYR
SEQRES 5 B 262 GLN ARG LYS SER MET TRP GLU MET TRP GLU ARG CYS ALA
SEQRES 6 B 262 HIS HIS LEU THR GLU ALA ILE GLN TYR VAL VAL GLU PHE
SEQRES 7 B 262 ALA LYS ARG LEU SER GLY PHE MET GLU LEU CYS GLN ASN
SEQRES 8 B 262 ASP GLN ILE VAL LEU LEU LYS ALA GLY ALA MET GLU VAL
SEQRES 9 B 262 VAL LEU VAL ARG MET CYS ARG ALA TYR ASN ALA ASP ASN
SEQRES 10 B 262 ARG THR VAL PHE PHE GLU GLY LYS TYR GLY GLY MET GLU
SEQRES 11 B 262 LEU PHE ARG ALA LEU GLY CYS SER GLU LEU ILE SER SER
SEQRES 12 B 262 ILE PHE ASP PHE SER HIS SER LEU SER ALA LEU HIS PHE
SEQRES 13 B 262 SER GLU ASP GLU ILE ALA LEU TYR THR ALA LEU VAL LEU
SEQRES 14 B 262 ILE ASN ALA HIS ARG PRO GLY LEU GLN GLU LYS ARG LYS
SEQRES 15 B 262 VAL GLU GLN LEU GLN TYR ASN LEU GLU LEU ALA PHE HIS
SEQRES 16 B 262 HIS HIS LEU CYS LYS THR HIS ARG GLN SER ILE LEU ALA
SEQRES 17 B 262 LYS LEU PRO PRO LYS GLY LYS LEU ARG SER LEU CYS SER
SEQRES 18 B 262 GLN HIS VAL GLU ARG LEU GLN ILE PHE GLN HIS LEU HIS
SEQRES 19 B 262 PRO ILE VAL VAL GLN ALA ALA PHE PRO PRO LEU TYR LYS
SEQRES 20 B 262 GLU LEU PHE SER THR GLU THR GLU SER PRO VAL GLY LEU
SEQRES 21 B 262 SER LYS
SEQRES 1 D 19 VAL GLU SER GLU PHE PRO TYR LEU LEU SER LEU LEU GLY
SEQRES 2 D 19 GLU VAL SER PRO GLN PRO
HET 444 A 601 31
HET 444 B 601 31
HETNAM 444 N-(2,2,2-TRIFLUOROETHYL)-N-{4-[2,2,2-TRIFLUORO-1-
HETNAM 2 444 HYDROXY-1-(TRIFLUOROMETHYL)
HETNAM 3 444 ETHYL]PHENYL}BENZENESULFONAMIDE
FORMUL 5 444 2(C17 H12 F9 N O3 S)
FORMUL 7 HOH *32(H2 O)
HELIX 1 AA1 SER A 266 GLU A 283 1 18
HELIX 2 AA2 ARG A 288 GLN A 295 1 8
HELIX 3 AA3 SER A 301 LYS A 311 1 11
HELIX 4 AA4 SER A 312 LEU A 338 1 27
HELIX 5 AA5 GLY A 340 LEU A 344 5 5
HELIX 6 AA6 CYS A 345 MET A 365 1 21
HELIX 7 AA7 GLY A 384 GLY A 392 5 9
HELIX 8 AA8 CYS A 393 ALA A 409 1 17
HELIX 9 AA9 SER A 413 ILE A 426 1 14
HELIX 10 AB1 GLU A 435 THR A 457 1 23
HELIX 11 AB2 ARG A 459 LEU A 466 5 8
HELIX 12 AB3 GLY A 470 HIS A 490 1 21
HELIX 13 AB4 HIS A 490 PHE A 498 1 9
HELIX 14 AB5 PRO A 499 SER A 507 1 9
HELIX 15 AB6 PHE C 2 GLU C 11 1 10
HELIX 16 AB7 SER B 266 GLU B 283 1 18
HELIX 17 AB8 ARG B 288 GLN B 295 1 8
HELIX 18 AB9 SER B 301 ARG B 310 1 10
HELIX 19 AC1 SER B 312 LEU B 338 1 27
HELIX 20 AC2 CYS B 345 MET B 365 1 21
HELIX 21 AC3 GLY B 384 GLY B 392 5 9
HELIX 22 AC4 CYS B 393 ALA B 409 1 17
HELIX 23 AC5 SER B 413 ILE B 426 1 14
HELIX 24 AC6 GLU B 435 THR B 457 1 23
HELIX 25 AC7 ARG B 459 LEU B 466 5 8
HELIX 26 AC8 PRO B 468 HIS B 490 1 23
HELIX 27 AC9 HIS B 490 PHE B 498 1 9
HELIX 28 AD1 PRO B 499 SER B 507 1 9
HELIX 29 AD2 PRO D 3 GLY D 10 1 8
SHEET 1 AA1 3 TYR A 369 ASN A 370 0
SHEET 2 AA1 3 THR A 375 PHE A 378 -1 O THR A 375 N ASN A 370
SHEET 3 AA1 3 LYS A 381 GLY A 383 -1 O LYS A 381 N PHE A 378
SHEET 1 AA2 3 TYR B 369 ASN B 370 0
SHEET 2 AA2 3 THR B 375 PHE B 378 -1 O THR B 375 N ASN B 370
SHEET 3 AA2 3 LYS B 381 GLY B 383 -1 O LYS B 381 N PHE B 378
SITE 1 AC1 11 TRP A 317 CYS A 320 ALA A 321 LEU A 324
SITE 2 AC1 11 MET A 365 PHE A 378 PHE A 388 LEU A 396
SITE 3 AC1 11 ILE A 397 ILE A 400 HIS A 479
SITE 1 AC2 8 TRP B 317 CYS B 320 MET B 358 MET B 365
SITE 2 AC2 8 LEU B 396 ILE B 397 ILE B 400 HIS B 479
CRYST1 63.139 63.139 160.441 90.00 90.00 90.00 P 41 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 0.015838 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015838 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006233 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
