HEADER TRANSCRIPTION 29-APR-15 4ZJW
TITLE RORGAMMA IN COMPLEX WITH INVERSE AGONIST 16
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUCLEAR RECEPTOR ROR-GAMMA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN (UNP RESIDUES 265-487);
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
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
KEYWDS RORGAMMA LIGAND BINDING DOMAIN, INVERSE AGONIST 16, BIOGEN,
KEYWDS 2 TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR D.J.MARCOTTE
REVDAT 4 27-SEP-23 4ZJW 1 REMARK
REVDAT 3 01-NOV-17 4ZJW 1 SOURCE JRNL REMARK
REVDAT 2 24-JUN-15 4ZJW 1 REMARK
REVDAT 1 17-JUN-15 4ZJW 0
JRNL AUTH J.CHAO,I.ENYEDY,K.VAN VLOTEN,D.MARCOTTE,K.GUERTIN,
JRNL AUTH 2 R.HUTCHINGS,N.POWELL,H.JONES,T.BOHNERT,C.C.PENG,L.SILVIAN,
JRNL AUTH 3 V.S.HONG,K.LITTLE,D.BANERJEE,L.PENG,A.TAVERAS,J.L.VINEY,
JRNL AUTH 4 J.FONTENOT
JRNL TITL DISCOVERY OF BIARYL CARBOXYLAMIDES AS POTENT ROR GAMMA
JRNL TITL 2 INVERSE AGONISTS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 25 2991 2015
JRNL REFN ESSN 1464-3405
JRNL PMID 26048806
JRNL DOI 10.1016/J.BMCL.2015.05.026
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0107
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 60.64
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 15138
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) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 821
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1140
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2280
REMARK 3 BIN FREE R VALUE SET COUNT : 57
REMARK 3 BIN FREE R VALUE : 0.3180
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3555
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 31
REMARK 3 SOLVENT ATOMS : 70
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.19
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.03000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : 0.02000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.01000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 1.288
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.314
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.240
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.885
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.906
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3659 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3504 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4929 ; 1.655 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8017 ; 1.025 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 439 ; 5.781 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 177 ;31.673 ;23.220
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 665 ;16.494 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 29 ;21.272 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 543 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4115 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 910 ; 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): 1761 ; 2.564 ; 3.632
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1760 ; 2.557 ; 3.631
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2197 ; 3.965 ; 5.441
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 : 1.20
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 : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4ZJW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-APR-15.
REMARK 100 THE DEPOSITION ID IS D_1000209431.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-OCT-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
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) : 0.9793
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 3.2.5
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39149
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.351
REMARK 200 RESOLUTION RANGE LOW (A) : 33.577
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.17900
REMARK 200 R SYM (I) : 0.17900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.56
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.16400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 3BOW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM ACETATE. 15% PEG3350,
REMARK 280 0.1M BISTRIS PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 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 62.79300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.15650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 62.79300
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 28.15650
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 300 REMARK: SEC CONFIRMS MONOMERIC STATE
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 GLY A 263
REMARK 465 SER A 264
REMARK 465 ALA A 265
REMARK 465 SER A 266
REMARK 465 LEU A 267
REMARK 465 GLN A 487
REMARK 465 GLY B 263
REMARK 465 SER B 264
REMARK 465 ALA B 265
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 269 CG CD OE1 OE2
REMARK 470 ARG A 302 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 469 CG CD CE NZ
REMARK 470 ARG A 473 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 478 CG CD OE1 NE2
REMARK 470 ARG B 288 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 437 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 440 CG CD OE1 OE2
REMARK 470 ARG B 473 CG CD NE CZ NH1 NH2
REMARK 470 CYS B 476 O
REMARK 470 SER B 477 OG
REMARK 470 GLU B 481 CG CD OE1 OE2
REMARK 470 GLN B 484 CG CD OE1 NE2
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 ARG B 430 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG B 430 NE - CZ - NH2 ANGL. DEV. = -4.0 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 SER A 339 125.80 -30.26
REMARK 500 CYS A 393 74.37 -152.23
REMARK 500 SER A 477 -62.19 -120.50
REMARK 500 GLN A 478 115.18 -38.74
REMARK 500 HIS A 479 -9.57 72.55
REMARK 500 GLU A 481 154.06 148.16
REMARK 500 PHE B 378 115.19 -160.04
REMARK 500 CYS B 393 72.12 -151.59
REMARK 500 SER B 477 -36.44 -169.41
REMARK 500 HIS B 479 -5.01 83.45
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 4P1 A 501
DBREF 4ZJW A 265 487 UNP P51449 RORG_HUMAN 265 487
DBREF 4ZJW B 265 487 UNP P51449 RORG_HUMAN 265 487
SEQADV 4ZJW GLY A 263 UNP P51449 EXPRESSION TAG
SEQADV 4ZJW SER A 264 UNP P51449 EXPRESSION TAG
SEQADV 4ZJW GLY B 263 UNP P51449 EXPRESSION TAG
SEQADV 4ZJW SER B 264 UNP P51449 EXPRESSION TAG
SEQRES 1 A 225 GLY SER ALA SER LEU THR GLU ILE GLU HIS LEU VAL GLN
SEQRES 2 A 225 SER VAL CYS LYS SER TYR ARG GLU THR CYS GLN LEU ARG
SEQRES 3 A 225 LEU GLU ASP LEU LEU ARG GLN ARG SER ASN ILE PHE SER
SEQRES 4 A 225 ARG GLU GLU VAL THR GLY TYR GLN ARG LYS SER MET TRP
SEQRES 5 A 225 GLU MET TRP GLU ARG CYS ALA HIS HIS LEU THR GLU ALA
SEQRES 6 A 225 ILE GLN TYR VAL VAL GLU PHE ALA LYS ARG LEU SER GLY
SEQRES 7 A 225 PHE MET GLU LEU CYS GLN ASN ASP GLN ILE VAL LEU LEU
SEQRES 8 A 225 LYS ALA GLY ALA MET GLU VAL VAL LEU VAL ARG MET CYS
SEQRES 9 A 225 ARG ALA TYR ASN ALA ASP ASN ARG THR VAL PHE PHE GLU
SEQRES 10 A 225 GLY LYS TYR GLY GLY MET GLU LEU PHE ARG ALA LEU GLY
SEQRES 11 A 225 CYS SER GLU LEU ILE SER SER ILE PHE ASP PHE SER HIS
SEQRES 12 A 225 SER LEU SER ALA LEU HIS PHE SER GLU ASP GLU ILE ALA
SEQRES 13 A 225 LEU TYR THR ALA LEU VAL LEU ILE ASN ALA HIS ARG PRO
SEQRES 14 A 225 GLY LEU GLN GLU LYS ARG LYS VAL GLU GLN LEU GLN TYR
SEQRES 15 A 225 ASN LEU GLU LEU ALA PHE HIS HIS HIS LEU CYS LYS THR
SEQRES 16 A 225 HIS ARG GLN SER ILE LEU ALA LYS LEU PRO PRO LYS GLY
SEQRES 17 A 225 LYS LEU ARG SER LEU CYS SER GLN HIS VAL GLU ARG LEU
SEQRES 18 A 225 GLN ILE PHE GLN
SEQRES 1 B 225 GLY SER ALA SER LEU THR GLU ILE GLU HIS LEU VAL GLN
SEQRES 2 B 225 SER VAL CYS LYS SER TYR ARG GLU THR CYS GLN LEU ARG
SEQRES 3 B 225 LEU GLU ASP LEU LEU ARG GLN ARG SER ASN ILE PHE SER
SEQRES 4 B 225 ARG GLU GLU VAL THR GLY TYR GLN ARG LYS SER MET TRP
SEQRES 5 B 225 GLU MET TRP GLU ARG CYS ALA HIS HIS LEU THR GLU ALA
SEQRES 6 B 225 ILE GLN TYR VAL VAL GLU PHE ALA LYS ARG LEU SER GLY
SEQRES 7 B 225 PHE MET GLU LEU CYS GLN ASN ASP GLN ILE VAL LEU LEU
SEQRES 8 B 225 LYS ALA GLY ALA MET GLU VAL VAL LEU VAL ARG MET CYS
SEQRES 9 B 225 ARG ALA TYR ASN ALA ASP ASN ARG THR VAL PHE PHE GLU
SEQRES 10 B 225 GLY LYS TYR GLY GLY MET GLU LEU PHE ARG ALA LEU GLY
SEQRES 11 B 225 CYS SER GLU LEU ILE SER SER ILE PHE ASP PHE SER HIS
SEQRES 12 B 225 SER LEU SER ALA LEU HIS PHE SER GLU ASP GLU ILE ALA
SEQRES 13 B 225 LEU TYR THR ALA LEU VAL LEU ILE ASN ALA HIS ARG PRO
SEQRES 14 B 225 GLY LEU GLN GLU LYS ARG LYS VAL GLU GLN LEU GLN TYR
SEQRES 15 B 225 ASN LEU GLU LEU ALA PHE HIS HIS HIS LEU CYS LYS THR
SEQRES 16 B 225 HIS ARG GLN SER ILE LEU ALA LYS LEU PRO PRO LYS GLY
SEQRES 17 B 225 LYS LEU ARG SER LEU CYS SER GLN HIS VAL GLU ARG LEU
SEQRES 18 B 225 GLN ILE PHE GLN
HET 4P1 A 501 31
HETNAM 4P1 4-CHLORO-3-[1-(2-CHLORO-6-FLUOROBENZOYL)-1,2,3,4-
HETNAM 2 4P1 TETRAHYDROQUINOLIN-6-YL]-N-METHYLBENZAMIDE
FORMUL 3 4P1 C24 H19 CL2 F N2 O2
FORMUL 4 HOH *70(H2 O)
HELIX 1 AA1 THR A 268 THR A 284 1 17
HELIX 2 AA2 ARG A 288 GLN A 295 1 8
HELIX 3 AA3 ARG A 296 ASN A 298 5 3
HELIX 4 AA4 SER A 301 ARG A 310 1 10
HELIX 5 AA5 SER A 312 LEU A 338 1 27
HELIX 6 AA6 GLY A 340 LEU A 344 5 5
HELIX 7 AA7 CYS A 345 CYS A 366 1 22
HELIX 8 AA8 GLY A 384 ARG A 389 5 6
HELIX 9 AA9 CYS A 393 ALA A 409 1 17
HELIX 10 AB1 SER A 413 ILE A 426 1 14
HELIX 11 AB2 GLU A 435 THR A 457 1 23
HELIX 12 AB3 ARG A 459 LEU A 466 5 8
HELIX 13 AB4 GLY A 470 CYS A 476 1 7
HELIX 14 AB5 ARG A 482 PHE A 486 5 5
HELIX 15 AB6 LEU B 267 CYS B 285 1 19
HELIX 16 AB7 ARG B 288 GLN B 295 1 8
HELIX 17 AB8 ARG B 296 ASN B 298 5 3
HELIX 18 AB9 SER B 301 ARG B 310 1 10
HELIX 19 AC1 SER B 312 ARG B 337 1 26
HELIX 20 AC2 CYS B 345 CYS B 366 1 22
HELIX 21 AC3 GLY B 384 ARG B 389 5 6
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 GLY B 470 CYS B 476 1 7
HELIX 27 AC9 ARG B 482 GLN B 487 5 6
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 GLY A 383 N VAL A 376
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 GLY B 383 N VAL B 376
SITE 1 AC1 6 GLN A 286 PHE A 378 GLU A 379 LEU A 391
SITE 2 AC1 6 ILE A 400 VAL A 480
CRYST1 125.586 56.313 79.517 90.00 124.66 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 0.007963 0.000000 0.005506 0.00000
SCALE2 0.000000 0.017758 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015289 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
