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 17169

Title: Solution NMR Structure of DRBM 2 domain of Interleukin enhancer-binding factor 3 from homo sapiens, Northeast Structural Genomics Consortium Target HR4527E

Deposition date: 2010-09-03 Original release date: 2010-10-01

Authors: Liu, Gaohua; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Ciccosanti, COLLEEN; Shastry, Ritu; Everett, John; Montelione, Gaetano

Citation: Liu, Gaohua; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano. "Northeast Structural Genomics Consortium Target HR4527E"  To be published ., .-..

Assembly members:
HR4527E, polymer, 91 residues, 10189.764 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
HR4527E: MGHHHHHHSHMLTKHGKNPV MELNEKRRGLKYELISETGG SHDKRFVMEVEVDGQKFQGA GSNKKVAKAYAALAALEKLF PDTPLALDANK

Data sets:
Data typeCount
13C chemical shifts283
15N chemical shifts82
1H chemical shifts583

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HR4527E1

Entities:

Entity 1, HR4527E 91 residues - 10189.764 Da.

1   METGLYHISHISHISHISHISHISSERHIS
2   METLEUTHRLYSHISGLYLYSASNPROVAL
3   METGLULEUASNGLULYSARGARGGLYLEU
4   LYSTYRGLULEUILESERGLUTHRGLYGLY
5   SERHISASPLYSARGPHEVALMETGLUVAL
6   GLUVALASPGLYGLNLYSPHEGLNGLYALA
7   GLYSERASNLYSLYSVALALALYSALATYR
8   ALAALALEUALAALALEUGLULYSLEUPHE
9   PROASPTHRPROLEUALALEUASPALAASN
10   LYS

Samples:

sample_NC5: HR4527E, [U-5% 13C; U-100% 15N], 0.7 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_NC5isotropicsample_conditions_1
2D 1H-13C HSQCsample_NC5isotropicsample_conditions_1
3D HNCOsample_NC5isotropicsample_conditions_1
3D CBCA(CO)NHsample_NC5isotropicsample_conditions_1
3D HNCACBsample_NC5isotropicsample_conditions_1
3D 1H-13C arom NOESYsample_NC5isotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYsample_NC5isotropicsample_conditions_1

Software:

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinemen, structure solution

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis, refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, data analysis

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

XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

SPARKY, Goddard - data analysis

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PALES, PALES (Zweckstetter, Bax) - geometry optimization

REDCAT, Valafar, Prestegard - geometry optimization

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinemen, structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAC40448
EMBL CAC01122 CAC01123 CAC01124

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