HEADER TRANSCRIPTION/TRANSCRIPTION ACTIVATOR 21-JUL-10 3O1D
TITLE STRUCTURE-FUNCTION STUDY OF GEMINI DERIVATIVES WITH TWO DIFFERENT SIDE
TITLE 2 CHAINS AT C-20, GEMINI-0072 AND GEMINI-0097.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VITAMIN D3 RECEPTOR A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN (UNP RESIDUES 156-453);
COMPND 5 SYNONYM: VDR-A, 1,25-DIHYDROXYVITAMIN D3 RECEPTOR A, NUCLEAR RECEPTOR
COMPND 6 SUBFAMILY 1 GROUP I MEMBER 1-A;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: NUCLEAR RECEPTOR COACTIVATOR 2;
COMPND 10 CHAIN: B;
COMPND 11 SYNONYM: NCOA-2, TRANSCRIPTIONAL INTERMEDIARY FACTOR 2, HTIF2, CLASS
COMPND 12 E BASIC HELIX-LOOP-HELIX PROTEIN 75, BHLHE75;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DANIO RERIO;
SOURCE 3 ORGANISM_COMMON: LEOPARD DANIO,ZEBRA DANIO,ZEBRA FISH;
SOURCE 4 ORGANISM_TAXID: 7955;
SOURCE 5 GENE: VDRA, NR1I1A, VDR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 OTHER_DETAILS: 13-MER PEPTIDE
KEYWDS TRANSCRIPTION FACTOR, VITAMIN D, NUCLEUS, TRANSCRIPTION-TRANSCRIPTION
KEYWDS 2 ACTIVATOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR T.HUET,D.MORAS,N.ROCHEL
REVDAT 4 21-FEB-24 3O1D 1 REMARK HETSYN
REVDAT 3 10-MAR-21 3O1D 1 REMARK SEQADV
REVDAT 2 21-MAR-12 3O1D 1 JRNL VERSN
REVDAT 1 06-JUL-11 3O1D 0
JRNL AUTH T.HUET,H.MAEHR,H.J.LEE,M.R.USKOKOVIC,N.SUH,D.MORAS,N.ROCHEL
JRNL TITL STRUCTURE-FUNCTION STUDY OF GEMINI DERIVATIVES WITH TWO
JRNL TITL 2 DIFFERENT SIDE CHAINS AT C-20, GEMINI-0072 AND GEMINI-0097.
JRNL REF MEDCHEMCOMM V. 2 424 2011
JRNL REFN ISSN 2040-2503
JRNL PMID 22180837
JRNL DOI 10.1039/C1MD00059D
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.1_357)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.88
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 3 NUMBER OF REFLECTIONS : 13747
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 699
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 24.8855 - 4.1003 0.92 2691 141 0.1781 0.2205
REMARK 3 2 4.1003 - 3.2568 0.91 2497 119 0.1993 0.2859
REMARK 3 3 3.2568 - 2.8458 1.00 2680 119 0.2270 0.2819
REMARK 3 4 2.8458 - 2.5859 0.99 2611 162 0.2616 0.3106
REMARK 3 5 2.5859 - 2.4007 0.99 2569 158 0.2885 0.3436
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.37
REMARK 3 B_SOL : 73.38
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.330
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 9.18300
REMARK 3 B22 (A**2) : 9.18300
REMARK 3 B33 (A**2) : -18.36610
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 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 : 0.003 2099
REMARK 3 ANGLE : 0.861 2840
REMARK 3 CHIRALITY : 0.050 324
REMARK 3 PLANARITY : 0.002 356
REMARK 3 DIHEDRAL : 18.254 815
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 8.8392 36.7782 42.1761
REMARK 3 T TENSOR
REMARK 3 T11: 0.3494 T22: 0.4349
REMARK 3 T33: 0.3239 T12: 0.1158
REMARK 3 T13: -0.0604 T23: -0.0483
REMARK 3 L TENSOR
REMARK 3 L11: 0.8624 L22: 2.0688
REMARK 3 L33: 2.8290 L12: -0.0416
REMARK 3 L13: 0.3517 L23: 1.6098
REMARK 3 S TENSOR
REMARK 3 S11: -0.1703 S12: -0.3865 S13: -0.0078
REMARK 3 S21: 0.3948 S22: 0.0823 S23: -0.0116
REMARK 3 S31: 0.2387 S32: -0.1112 S33: 0.0547
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 3O1D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-AUG-10.
REMARK 100 THE DEPOSITION ID IS D_1000060541.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-DEC-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93340
REMARK 200 MONOCHROMATOR : DIAMOND
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13853
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 14.800
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM BIS-TRIS PH6.5, 1.6 M LITHIUM
REMARK 280 SULFATE, 50 MM MAGNESIUM SULFATE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 297K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
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 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 176.42667
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 88.21333
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 132.32000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 44.10667
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 220.53333
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 176.42667
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 88.21333
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 44.10667
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 132.32000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 220.53333
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 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 350 BIOMT1 2 0.500000 -0.866025 0.000000 33.05400
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 57.25121
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 44.10667
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 152
REMARK 465 SER A 153
REMARK 465 GLU A 191
REMARK 465 GLY A 192
REMARK 465 PRO A 193
REMARK 465 VAL A 194
REMARK 465 THR A 195
REMARK 465 ARG A 196
REMARK 465 SER A 197
REMARK 465 ALA A 198
REMARK 465 SER A 199
REMARK 465 ARG A 200
REMARK 465 ALA A 201
REMARK 465 ALA A 202
REMARK 465 SER A 203
REMARK 465 LEU A 204
REMARK 465 HIS A 205
REMARK 465 SER A 206
REMARK 465 LEU A 207
REMARK 465 SER A 208
REMARK 465 ASP A 209
REMARK 465 ALA A 210
REMARK 465 SER A 211
REMARK 465 SER A 212
REMARK 465 ASP A 213
REMARK 465 SER A 214
REMARK 465 PHE A 215
REMARK 465 ASN A 216
REMARK 465 HIS A 217
REMARK 465 SER A 218
REMARK 465 PRO A 219
REMARK 465 GLU A 220
REMARK 465 SER A 221
REMARK 465 VAL A 222
REMARK 465 ASP A 223
REMARK 465 THR A 224
REMARK 465 LYS A 225
REMARK 465 LEU A 226
REMARK 465 ASN A 227
REMARK 465 PHE A 228
REMARK 465 SER A 229
REMARK 465 ASN A 230
REMARK 465 LEU A 231
REMARK 465 LEU A 232
REMARK 465 MET A 233
REMARK 465 MET A 234
REMARK 465 TYR A 235
REMARK 465 GLN A 236
REMARK 465 ASP A 237
REMARK 465 SER A 238
REMARK 465 GLY A 239
REMARK 465 SER A 240
REMARK 465 PRO A 241
REMARK 465 ASP A 242
REMARK 465 SER A 243
REMARK 465 SER A 244
REMARK 465 GLU A 245
REMARK 465 GLU A 246
REMARK 465 ASP A 247
REMARK 465 GLN A 248
REMARK 465 GLN A 249
REMARK 465 SER A 250
REMARK 465 ASP B 696
REMARK 465 SER B 697
REMARK 465 SER B 698
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 LYS B 686 CG CD CE NZ
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ASP A 158 OD1 OD2
REMARK 480 GLU A 159 CG CD OE1 OE2
REMARK 480 LYS A 173 CE NZ
REMARK 480 ARG A 280 NE CZ NH1 NH2
REMARK 480 GLU A 310 CG CD OE1 OE2
REMARK 480 LYS A 322 CD CE NZ
REMARK 480 ILE A 325 CG1 CG2 CD1
REMARK 480 LYS A 330 CE NZ
REMARK 480 LEU A 337 CG CD1 CD2
REMARK 480 GLU A 339 CG CD OE1 OE2
REMARK 480 LYS A 343 CG CD CE NZ
REMARK 480 LYS A 352 CE NZ
REMARK 480 GLN A 375 CG CD OE1 NE2
REMARK 480 VAL A 378 CG1 CG2
REMARK 480 ILE A 380 CG2
REMARK 480 LEU A 404 CG CD1 CD2
REMARK 480 GLU A 451 CG CD OE1 OE2
REMARK 480 SER A 453 OG
REMARK 480 LYS B 688 CD CE NZ
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 ASP A 158 1.85 -64.65
REMARK 500 GLN A 375 -66.11 -98.53
REMARK 500 HIS B 687 65.31 -119.91
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 G72 A 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2HC4 RELATED DB: PDB
REMARK 900 RELATED ID: 2HCD RELATED DB: PDB
REMARK 900 RELATED ID: 3O1E RELATED DB: PDB
DBREF 3O1D A 156 453 UNP Q9PTN2 VDRA_DANRE 156 453
DBREF 3O1D B 686 698 UNP Q15596 NCOA2_HUMAN 686 698
SEQADV 3O1D GLY A 152 UNP Q9PTN2 EXPRESSION TAG
SEQADV 3O1D SER A 153 UNP Q9PTN2 EXPRESSION TAG
SEQADV 3O1D HIS A 154 UNP Q9PTN2 EXPRESSION TAG
SEQADV 3O1D MET A 155 UNP Q9PTN2 EXPRESSION TAG
SEQRES 1 A 302 GLY SER HIS MET LEU SER ASP GLU GLN MET GLN ILE ILE
SEQRES 2 A 302 ASN SER LEU VAL GLU ALA HIS HIS LYS THR TYR ASP ASP
SEQRES 3 A 302 SER TYR SER ASP PHE VAL ARG PHE ARG PRO PRO VAL ARG
SEQRES 4 A 302 GLU GLY PRO VAL THR ARG SER ALA SER ARG ALA ALA SER
SEQRES 5 A 302 LEU HIS SER LEU SER ASP ALA SER SER ASP SER PHE ASN
SEQRES 6 A 302 HIS SER PRO GLU SER VAL ASP THR LYS LEU ASN PHE SER
SEQRES 7 A 302 ASN LEU LEU MET MET TYR GLN ASP SER GLY SER PRO ASP
SEQRES 8 A 302 SER SER GLU GLU ASP GLN GLN SER ARG LEU SER MET LEU
SEQRES 9 A 302 PRO HIS LEU ALA ASP LEU VAL SER TYR SER ILE GLN LYS
SEQRES 10 A 302 VAL ILE GLY PHE ALA LYS MET ILE PRO GLY PHE ARG ASP
SEQRES 11 A 302 LEU THR ALA GLU ASP GLN ILE ALA LEU LEU LYS SER SER
SEQRES 12 A 302 ALA ILE GLU ILE ILE MET LEU ARG SER ASN GLN SER PHE
SEQRES 13 A 302 SER LEU GLU ASP MET SER TRP SER CYS GLY GLY PRO ASP
SEQRES 14 A 302 PHE LYS TYR CYS ILE ASN ASP VAL THR LYS ALA GLY HIS
SEQRES 15 A 302 THR LEU GLU LEU LEU GLU PRO LEU VAL LYS PHE GLN VAL
SEQRES 16 A 302 GLY LEU LYS LYS LEU LYS LEU HIS GLU GLU GLU HIS VAL
SEQRES 17 A 302 LEU LEU MET ALA ILE CYS LEU LEU SER PRO ASP ARG PRO
SEQRES 18 A 302 GLY VAL GLN ASP HIS VAL ARG ILE GLU ALA LEU GLN ASP
SEQRES 19 A 302 ARG LEU CYS ASP VAL LEU GLN ALA TYR ILE ARG ILE GLN
SEQRES 20 A 302 HIS PRO GLY GLY ARG LEU LEU TYR ALA LYS MET ILE GLN
SEQRES 21 A 302 LYS LEU ALA ASP LEU ARG SER LEU ASN GLU GLU HIS SER
SEQRES 22 A 302 LYS GLN TYR ARG SER LEU SER PHE GLN PRO GLU HIS SER
SEQRES 23 A 302 MET GLN LEU THR PRO LEU VAL LEU GLU VAL PHE GLY SER
SEQRES 24 A 302 GLU VAL SER
SEQRES 1 B 13 LYS HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP SER SER
HET G72 A 1 41
HETNAM G72 (1R,3R,7E,17BETA)-17-[(1S)-6,6,6-TRIFLUORO-5-HYDROXY-1-
HETNAM 2 G72 (4-HYDROXY-4-METHYLPENTYL)-5-(TRIFLUOROMETHYL)HEX-3-
HETNAM 3 G72 YN-1-YL]-9,10-SECOESTRA-5,7-DIENE-1,3-DIOL
HETSYN G72 1,25-DIHYDROXY-20S-21(3-TRIDEUTEROMETHYL-3-HYDROXY-4,4,
HETSYN 2 G72 4-TRIDEUTEROBUTYL)-23-YNE-26,27-HEXAFLUORO-19-NOR-
HETSYN 3 G72 CHOLECALCIFEROL; GEMINI-0072
FORMUL 3 G72 C31 H44 F6 O4
FORMUL 4 HOH *63(H2 O)
HELIX 1 1 GLU A 159 TYR A 175 1 17
HELIX 2 2 TYR A 179 PHE A 185 5 7
HELIX 3 3 MET A 254 LYS A 274 1 21
HELIX 4 4 GLY A 278 LEU A 282 5 5
HELIX 5 5 THR A 283 SER A 303 1 21
HELIX 6 6 CYS A 324 LYS A 330 1 7
HELIX 7 7 THR A 334 LEU A 351 1 18
HELIX 8 8 HIS A 354 LEU A 367 1 14
HELIX 9 9 ASP A 376 HIS A 399 1 24
HELIX 10 10 LEU A 404 PHE A 432 1 29
HELIX 11 11 GLN A 433 MET A 438 1 6
HELIX 12 12 THR A 441 PHE A 448 1 8
HELIX 13 13 HIS B 687 LEU B 694 1 8
SHEET 1 A 3 PHE A 307 SER A 308 0
SHEET 2 A 3 SER A 313 SER A 315 -1 O SER A 313 N SER A 308
SHEET 3 A 3 LYS A 322 TYR A 323 -1 O TYR A 323 N TRP A 314
SITE 1 AC1 19 TYR A 175 LEU A 255 VAL A 262 SER A 265
SITE 2 AC1 19 MET A 300 ARG A 302 SER A 303 SER A 306
SITE 3 AC1 19 TRP A 314 CYS A 316 ALA A 331 HIS A 333
SITE 4 AC1 19 LEU A 341 LEU A 419 HIS A 423 TYR A 427
SITE 5 AC1 19 LEU A 430 LEU A 440 PHE A 448
CRYST1 66.108 66.108 264.640 90.00 90.00 120.00 P 65 2 2 12
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 0.015127 0.008733 0.000000 0.00000
SCALE2 0.000000 0.017467 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003779 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
