BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17770

Title: Sequence specific backbone resonance assignment of Vitamin D receptor ligand binding domain (VDRLBD) complexed with 1,25(OH)2 D3 and LXXLL motif (DRIP205)   PubMed: 22112050

Deposition date: 2011-07-07 Original release date: 2012-01-05

Authors: Singarapu, Kiran; Zhu, Jinge; Westler, William; Deluca, Hector; Markley, John

Citation: Singarapu, Kiran; Zhu, Jinge; Tonelli, Marco; Rao, Hongyu; Assadi-Porter, Fariba; Westler, William; DeLuca, Hector; Markley, John. "Ligand-specific structural changes in the vitamin d receptor in solution"  Biochemistry 50, 11025-11033 (2011).

Assembly members:
VDRLBD, polymer, 262 residues, Formula weight is not available
3EV, non-polymer, 416.636 Da.

Natural source:   Common Name: Rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET29b

Entity Sequences (FASTA):
VDRLBD: MLKDSLRPKLSEEQQHIIAI LLDAHHKTYDPTYADFRDFR PPVRVDGSTGSVTLDLSPLS MLPHLADLVSYSIQKVIGFA KMIPGFRDLTSDDQIVLLKS SAIEVIMLRSNQSFTMDDMS WDCGSQDYKYDVTDVSKAGH TLELIEPLIKFQVGLKKLNL HEEEHVLLMAICIVSPDRPG VQDAKLVEAIQDRLSNTLQT YIRCRHPPPGSHQLYAKMIQ KLADLRSLNEEHSKQYRSLS FQPENSMKLTPLVLEVFGNE IS

Data sets:
Data typeCount
13C chemical shifts717
15N chemical shifts235
1H chemical shifts235

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1VDRLBD1
23EV2

Entities:

Entity 1, VDRLBD 262 residues - Formula weight is not available

1   METLEULYSASPSERLEUARGPROLYSLEU
2   SERGLUGLUGLNGLNHISILEILEALAILE
3   LEULEUASPALAHISHISLYSTHRTYRASP
4   PROTHRTYRALAASPPHEARGASPPHEARG
5   PROPROVALARGVALASPGLYSERTHRGLY
6   SERVALTHRLEUASPLEUSERPROLEUSER
7   METLEUPROHISLEUALAASPLEUVALSER
8   TYRSERILEGLNLYSVALILEGLYPHEALA
9   LYSMETILEPROGLYPHEARGASPLEUTHR
10   SERASPASPGLNILEVALLEULEULYSSER
11   SERALAILEGLUVALILEMETLEUARGSER
12   ASNGLNSERPHETHRMETASPASPMETSER
13   TRPASPCYSGLYSERGLNASPTYRLYSTYR
14   ASPVALTHRASPVALSERLYSALAGLYHIS
15   THRLEUGLULEUILEGLUPROLEUILELYS
16   PHEGLNVALGLYLEULYSLYSLEUASNLEU
17   HISGLUGLUGLUHISVALLEULEUMETALA
18   ILECYSILEVALSERPROASPARGPROGLY
19   VALGLNASPALALYSLEUVALGLUALAILE
20   GLNASPARGLEUSERASNTHRLEUGLNTHR
21   TYRILEARGCYSARGHISPROPROPROGLY
22   SERHISGLNLEUTYRALALYSMETILEGLN
23   LYSLEUALAASPLEUARGSERLEUASNGLU
24   GLUHISSERLYSGLNTYRARGSERLEUSER
25   PHEGLNPROGLUASNSERMETLYSLEUTHR
26   PROLEUVALLEUGLUVALPHEGLYASNGLU
27   ILESER

Entity 2, 3EV - C27 H44 O3 - 416.636 Da.

1   3EV

Samples:

sample_1: VDRLBD, [U-100% 13C; U-100% 15N; U-100% 2H], 0.5 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 50 mM; pH: 7.4; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC-TROSYsample_1isotropicsample_conditions_1
3D HNCA-TROSYsample_1isotropicsample_conditions_1
3D HN(CO)CA-TROSYsample_1isotropicsample_conditions_1
3D HN(CA)CB-TROSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESY-TROSYsample_1isotropicsample_conditions_1
3D HNCO-TROSYsample_1isotropicsample_conditions_1

Software:

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TALOS, Cornilescu, Delaglio and Bax - data analysis

VNMRJ, Varian - collection

XEASY, Bartels et al. - data analysis

NMR spectrometers:

  • Varian INOVA 900 MHz

Related Database Links:

PDB

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts