HEADER TRANSCRIPTION/INHIBITOR 28-JUL-16 5L11
TITLE HUMAN LIVER RECEPTOR HOMOLOGUE-1 (LRH-1) BOUND TO RJW100 AND A
TITLE 2 FRAGMENT OF TIF-2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUCLEAR RECEPTOR SUBFAMILY 5 GROUP A MEMBER 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 299-541;
COMPND 5 SYNONYM: ALPHA-1-FETOPROTEIN TRANSCRIPTION FACTOR,B1-BINDING FACTOR,
COMPND 6 HB1F,CYP7A PROMOTER-BINDING FACTOR,HEPATOCYTIC TRANSCRIPTION FACTOR,
COMPND 7 LIVER RECEPTOR HOMOLOG 1,LRH-1;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: TIF2;
COMPND 11 CHAIN: C;
COMPND 12 FRAGMENT: UNP RESIDUES 740-753;
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: NR5A2, B1F, CPF, FTF;
SOURCE 6 EXPRESSION_SYSTEM: ENTEROBACTERIA PHAGE L1;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 268588;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_TAXID: 9606
KEYWDS NUCLEAR RECEPTOR, AGONIST, TRANSCRIPTION-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.G.MAYS,E.A.ORTLUND
REVDAT 6 04-OCT-23 5L11 1 REMARK
REVDAT 5 25-DEC-19 5L11 1 REMARK
REVDAT 4 20-SEP-17 5L11 1 REMARK
REVDAT 3 14-DEC-16 5L11 1 JRNL
REVDAT 2 19-OCT-16 5L11 1 JRNL
REVDAT 1 12-OCT-16 5L11 0
JRNL AUTH S.G.MAYS,C.D.OKAFOR,R.J.WHITBY,D.GOSWAMI,J.STEC,A.R.FLYNN,
JRNL AUTH 2 M.C.DUGAN,N.T.JUI,P.R.GRIFFIN,E.A.ORTLUND
JRNL TITL CRYSTAL STRUCTURES OF THE NUCLEAR RECEPTOR, LIVER RECEPTOR
JRNL TITL 2 HOMOLOG 1, BOUND TO SYNTHETIC AGONISTS.
JRNL REF J. BIOL. CHEM. V. 291 25281 2016
JRNL REFN ESSN 1083-351X
JRNL PMID 27694446
JRNL DOI 10.1074/JBC.M116.753541
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10.1_2155
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.49
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 21026
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.990
REMARK 3 FREE R VALUE TEST SET COUNT : 1470
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 35.4970 - 4.1098 0.99 2032 152 0.1843 0.2449
REMARK 3 2 4.1098 - 3.2628 1.00 1888 141 0.1681 0.2027
REMARK 3 3 3.2628 - 2.8506 1.00 1858 139 0.2011 0.2282
REMARK 3 4 2.8506 - 2.5900 1.00 1824 137 0.2120 0.2524
REMARK 3 5 2.5900 - 2.4044 0.99 1827 139 0.2109 0.2723
REMARK 3 6 2.4044 - 2.2627 0.98 1769 132 0.2109 0.2455
REMARK 3 7 2.2627 - 2.1494 0.97 1748 132 0.2131 0.2505
REMARK 3 8 2.1494 - 2.0558 0.97 1743 131 0.2292 0.2548
REMARK 3 9 2.0558 - 1.9767 0.96 1714 129 0.2367 0.3054
REMARK 3 10 1.9767 - 1.9085 0.92 1649 124 0.2569 0.2529
REMARK 3 11 1.9085 - 1.8488 0.85 1504 114 0.2892 0.3291
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.190
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.49
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.15
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 : 0.004 2075
REMARK 3 ANGLE : 0.578 2803
REMARK 3 CHIRALITY : 0.035 318
REMARK 3 PLANARITY : 0.002 355
REMARK 3 DIHEDRAL : 11.782 1261
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND RESID 300:340 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.626 32.812 23.979
REMARK 3 T TENSOR
REMARK 3 T11: 0.3331 T22: 0.2872
REMARK 3 T33: 0.2598 T12: 0.0399
REMARK 3 T13: -0.0227 T23: -0.0038
REMARK 3 L TENSOR
REMARK 3 L11: 2.7334 L22: 8.1549
REMARK 3 L33: 2.7449 L12: 2.7390
REMARK 3 L13: -1.1465 L23: -2.3103
REMARK 3 S TENSOR
REMARK 3 S11: 0.1890 S12: -0.0744 S13: -0.3450
REMARK 3 S21: 0.7044 S22: -0.1776 S23: -0.1959
REMARK 3 S31: 0.1113 S32: -0.1499 S33: -0.0079
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN A AND RESID 341:397 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.812 38.168 16.026
REMARK 3 T TENSOR
REMARK 3 T11: 0.1872 T22: 0.2021
REMARK 3 T33: 0.1385 T12: 0.0612
REMARK 3 T13: -0.0046 T23: -0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 2.6311 L22: 3.4250
REMARK 3 L33: 2.2312 L12: -0.0559
REMARK 3 L13: -0.8679 L23: 0.0383
REMARK 3 S TENSOR
REMARK 3 S11: 0.1753 S12: 0.2040 S13: 0.1315
REMARK 3 S21: 0.1443 S22: -0.1886 S23: 0.0108
REMARK 3 S31: -0.0749 S32: -0.2090 S33: 0.0315
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN A AND RESID 398:421 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.902 19.645 14.435
REMARK 3 T TENSOR
REMARK 3 T11: 0.4331 T22: 0.2637
REMARK 3 T33: 0.3782 T12: 0.0934
REMARK 3 T13: 0.0761 T23: 0.0310
REMARK 3 L TENSOR
REMARK 3 L11: 1.6382 L22: 5.5280
REMARK 3 L33: 3.5200 L12: 0.8673
REMARK 3 L13: 1.8133 L23: 3.3962
REMARK 3 S TENSOR
REMARK 3 S11: -0.0289 S12: -0.0190 S13: -0.1849
REMARK 3 S21: -0.2105 S22: 0.1203 S23: -0.4611
REMARK 3 S31: 0.4344 S32: 0.2561 S33: -0.0170
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN A AND RESID 422:440 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.199 26.281 3.831
REMARK 3 T TENSOR
REMARK 3 T11: 0.3480 T22: 0.3134
REMARK 3 T33: 0.3541 T12: 0.1079
REMARK 3 T13: 0.0615 T23: -0.0616
REMARK 3 L TENSOR
REMARK 3 L11: 2.5720 L22: 2.1916
REMARK 3 L33: 1.3961 L12: 2.1405
REMARK 3 L13: -1.8784 L23: -1.6436
REMARK 3 S TENSOR
REMARK 3 S11: -0.2962 S12: 0.3475 S13: -0.5849
REMARK 3 S21: -0.3655 S22: 0.2651 S23: -0.4245
REMARK 3 S31: 0.2753 S32: 0.0981 S33: -0.0830
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: ( CHAIN A AND RESID 441:494 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.255 47.801 6.535
REMARK 3 T TENSOR
REMARK 3 T11: 0.3349 T22: 0.2846
REMARK 3 T33: 0.2340 T12: 0.1455
REMARK 3 T13: 0.0619 T23: 0.0551
REMARK 3 L TENSOR
REMARK 3 L11: 3.4544 L22: 3.3425
REMARK 3 L33: 3.0135 L12: -0.0124
REMARK 3 L13: -0.2946 L23: -0.4526
REMARK 3 S TENSOR
REMARK 3 S11: 0.0651 S12: 0.6312 S13: 0.1735
REMARK 3 S21: -0.0886 S22: -0.1166 S23: -0.3111
REMARK 3 S31: -0.0685 S32: 0.0042 S33: 0.0523
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: ( CHAIN A AND RESID 495:522 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.284 32.649 3.561
REMARK 3 T TENSOR
REMARK 3 T11: 0.4153 T22: 0.4708
REMARK 3 T33: 0.2522 T12: 0.1495
REMARK 3 T13: -0.0112 T23: -0.0967
REMARK 3 L TENSOR
REMARK 3 L11: 4.9135 L22: 3.7336
REMARK 3 L33: 0.6890 L12: 3.6382
REMARK 3 L13: -1.3097 L23: -0.9575
REMARK 3 S TENSOR
REMARK 3 S11: 0.0687 S12: 0.4271 S13: -0.2046
REMARK 3 S21: -0.2499 S22: -0.1522 S23: 0.0465
REMARK 3 S31: -0.0806 S32: -0.3040 S33: 0.0533
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: ( CHAIN A AND RESID 523:536 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.126 28.093 14.937
REMARK 3 T TENSOR
REMARK 3 T11: 0.2896 T22: 0.3937
REMARK 3 T33: 0.2894 T12: -0.0104
REMARK 3 T13: -0.0218 T23: -0.0999
REMARK 3 L TENSOR
REMARK 3 L11: 5.5773 L22: 3.2425
REMARK 3 L33: 7.0022 L12: 4.1377
REMARK 3 L13: 2.4968 L23: 2.8441
REMARK 3 S TENSOR
REMARK 3 S11: 0.3113 S12: 0.0952 S13: -0.2541
REMARK 3 S21: 0.3432 S22: -0.3832 S23: 0.5301
REMARK 3 S31: 0.1273 S32: -0.7430 S33: 0.2589
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: ( CHAIN C AND RESID 742:752 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.989 42.871 23.486
REMARK 3 T TENSOR
REMARK 3 T11: 0.2993 T22: 0.2777
REMARK 3 T33: 0.2642 T12: 0.0031
REMARK 3 T13: 0.1031 T23: 0.0169
REMARK 3 L TENSOR
REMARK 3 L11: 5.0645 L22: 7.3104
REMARK 3 L33: 3.6374 L12: -0.6103
REMARK 3 L13: -1.8435 L23: 1.4582
REMARK 3 S TENSOR
REMARK 3 S11: 0.6922 S12: 0.0560 S13: 0.3340
REMARK 3 S21: 0.0080 S22: -0.4378 S23: -0.0009
REMARK 3 S31: -0.4543 S32: -0.3758 S33: -0.1858
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 5L11 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUL-16.
REMARK 100 THE DEPOSITION ID IS D_1000222705.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-OCT-14
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 130 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21130
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.849
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 8.900
REMARK 200 R MERGE (I) : 0.09400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.1
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 0.58200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: 3PLZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05 M SODIUM ACETATE, PH 4.6, PEG
REMARK 280 4000 5-11%, GLYCEROL 5-10%, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 110.12950
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 23.20900
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 23.20900
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 165.19425
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 23.20900
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 23.20900
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 55.06475
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 23.20900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 23.20900
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 165.19425
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 23.20900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 23.20900
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 55.06475
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 110.12950
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: 1140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 789 LIES ON A SPECIAL POSITION.
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 SER A 297
REMARK 465 ASN A 298
REMARK 465 ALA A 299
REMARK 465 PRO A 527
REMARK 465 TYR A 528
REMARK 465 ASN A 529
REMARK 465 HIS A 537
REMARK 465 ALA A 538
REMARK 465 LYS A 539
REMARK 465 ARG A 540
REMARK 465 ALA A 541
REMARK 465 LYS C 740
REMARK 465 GLU C 741
REMARK 465 ASP C 753
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 767 O HOH A 769 2.02
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 GLU A 337 34.39 -140.21
REMARK 500 PHE A 365 -55.38 73.34
REMARK 500 ASN A 466 59.57 -115.40
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 RJW A 601
DBREF 5L11 A 299 541 UNP O00482 NR5A2_HUMAN 299 541
DBREF 5L11 C 740 753 PDB 5L11 5L11 740 753
SEQADV 5L11 SER A 297 UNP O00482 EXPRESSION TAG
SEQADV 5L11 ASN A 298 UNP O00482 EXPRESSION TAG
SEQRES 1 A 245 SER ASN ALA SER ILE PRO HIS LEU ILE LEU GLU LEU LEU
SEQRES 2 A 245 LYS CYS GLU PRO ASP GLU PRO GLN VAL GLN ALA LYS ILE
SEQRES 3 A 245 MET ALA TYR LEU GLN GLN GLU GLN ALA ASN ARG SER LYS
SEQRES 4 A 245 HIS GLU LYS LEU SER THR PHE GLY LEU MET CYS LYS MET
SEQRES 5 A 245 ALA ASP GLN THR LEU PHE SER ILE VAL GLU TRP ALA ARG
SEQRES 6 A 245 SER SER ILE PHE PHE ARG GLU LEU LYS VAL ASP ASP GLN
SEQRES 7 A 245 MET LYS LEU LEU GLN ASN CYS TRP SER GLU LEU LEU ILE
SEQRES 8 A 245 LEU ASP HIS ILE TYR ARG GLN VAL VAL HIS GLY LYS GLU
SEQRES 9 A 245 GLY SER ILE PHE LEU VAL THR GLY GLN GLN VAL ASP TYR
SEQRES 10 A 245 SER ILE ILE ALA SER GLN ALA GLY ALA THR LEU ASN ASN
SEQRES 11 A 245 LEU MET SER HIS ALA GLN GLU LEU VAL ALA LYS LEU ARG
SEQRES 12 A 245 SER LEU GLN PHE ASP GLN ARG GLU PHE VAL CYS LEU LYS
SEQRES 13 A 245 PHE LEU VAL LEU PHE SER LEU ASP VAL LYS ASN LEU GLU
SEQRES 14 A 245 ASN PHE GLN LEU VAL GLU GLY VAL GLN GLU GLN VAL ASN
SEQRES 15 A 245 ALA ALA LEU LEU ASP TYR THR MET CYS ASN TYR PRO GLN
SEQRES 16 A 245 GLN THR GLU LYS PHE GLY GLN LEU LEU LEU ARG LEU PRO
SEQRES 17 A 245 GLU ILE ARG ALA ILE SER MET GLN ALA GLU GLU TYR LEU
SEQRES 18 A 245 TYR TYR LYS HIS LEU ASN GLY ASP VAL PRO TYR ASN ASN
SEQRES 19 A 245 LEU LEU ILE GLU MET LEU HIS ALA LYS ARG ALA
SEQRES 1 C 14 LYS GLU ASN ALA LEU LEU ARG TYR LEU LEU ASP LYS ASP
SEQRES 2 C 14 ASP
HET RJW A 601 63
HETNAM RJW (1R,3AR,6AR)-5-HEXYL-4-PHENYL-3A-(1-PHENYLETHENYL)-1,2,
HETNAM 2 RJW 3,3A,6,6A-HEXAHYDROPENTALEN-1-OL
FORMUL 3 RJW C28 H34 O
FORMUL 4 HOH *92(H2 O)
HELIX 1 AA1 PRO A 302 CYS A 311 1 10
HELIX 2 AA2 ASP A 314 ARG A 333 1 20
HELIX 3 AA3 SER A 334 LYS A 338 5 5
HELIX 4 AA4 SER A 340 SER A 363 1 24
HELIX 5 AA5 PHE A 365 LEU A 369 5 5
HELIX 6 AA6 LYS A 370 GLY A 398 1 29
HELIX 7 AA7 TYR A 413 LEU A 441 1 29
HELIX 8 AA8 ASP A 444 PHE A 457 1 14
HELIX 9 AA9 ASN A 466 TYR A 489 1 24
HELIX 10 AB1 GLU A 494 ASN A 523 1 30
HELIX 11 AB2 LEU A 531 LEU A 536 1 6
HELIX 12 AB3 ALA C 743 LYS C 751 1 9
SHEET 1 AA1 2 SER A 402 PHE A 404 0
SHEET 2 AA1 2 GLN A 410 ASP A 412 -1 O VAL A 411 N ILE A 403
SITE 1 AC1 7 PHE A 342 MET A 345 MET A 348 ALA A 349
SITE 2 AC1 7 HIS A 390 LEU A 517 HOH A 720
CRYST1 46.418 46.418 220.259 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 0.021543 0.000000 0.000000 0.00000
SCALE2 0.000000 0.021543 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004540 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
