BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 16567

Title: 1H, 13C, and 15N chemical shift assignments for the RNA recognition motif of Nab3   PubMed: 20309651

Deposition date: 2009-10-19 Original release date: 2010-05-04

Authors: Stefl, Richard; Kubicek, Karel; Pergoli, Roberto; Hobor, Fruzsina; Pasulka, Josef

Citation: Pergoli, Roberto; Kubicek, Karel; Hobor, Fruzsina; Pasulka, Josef; Stefl, Richard. "1H, 13C, and 15N chemical shift assignments for the RNA recognition motif of Nab3."  Biomol. NMR Assignments 4, 119-121 (2010).

Assembly members:
RNA_binding_polypeptide, polymer, 104 residues, Formula weight is not available

Natural source:   Common Name: baker   Taxonomy ID: 4932   Superkingdom: not available   Kingdom: not available   Genus/species: Eukaryota Fungi

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

Entity Sequences (FASTA):
RNA_binding_polypeptide: MTEMHNIPPKSRLFIGNLPL KNVSKEDLFRIFSPYGHIMQ INIKNAFGFIQFDNPQSVRD AIECESQEMNFGKKLILEVS SSNARPQFDHGDHGTNLEHH HHHH

Data sets:
Data typeCount
13C chemical shifts201
15N chemical shifts60
1H chemical shifts376

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1subunit 11

Entities:

Entity 1, subunit 1 104 residues - Formula weight is not available

1   METTHRGLUMETHISASNILEPROPROLYS
2   SERARGLEUPHEILEGLYASNLEUPROLEU
3   LYSASNVALSERLYSGLUASPLEUPHEARG
4   ILEPHESERPROTYRGLYHISILEMETGLN
5   ILEASNILELYSASNALAPHEGLYPHEILE
6   GLNPHEASPASNPROGLNSERVALARGASP
7   ALAILEGLUCYSGLUSERGLNGLUMETASN
8   PHEGLYLYSLYSLEUILELEUGLUVALSER
9   SERSERASNALAARGPROGLNPHEASPHIS
10   GLYASPHISGLYTHRASNLEUGLUHISHIS
11   HISHISHISHIS

Samples:

sample_1: RNA binding polypeptide, [U-99% 13C; U-99% 15N], 3 mM

sample_conditions_1: ionic strength: 0.3 M; pH: 8; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin, Goddard - chemical shift assignment, collection

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker Avance 900 MHz

Related Database Links:

PDB
DBJ BAA07154 GAA26786
EMBL CAA97903 CAY86769
GB AAA81910 AHY77991 AJP41959 AJU23403 AJU24091
PRF 2201484A
REF NP_015134
SP P38996
TPG DAA11244

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