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 11527

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for PriB   PubMed: 24200676

Deposition date: 2013-06-08 Original release date: 2017-03-13

Authors: Abe, Yoshito; Takenawa, Taichi; Shioi, Seijiro; Fujiyama, Saki; Aramaki, Takahiko; Katayama, Tsutomu; Ueda, Tadashi

Citation: Fujiyama, Saki; Abe, Yoshito; Takenawa, Taichi; Aramaki, Takahiko; Shioi, Seijiro; Katayama, Tsutomu; Ueda, Tadashi. "Involvement of histidine in complex formation of PriB and single-stranded DNA"  Biochim. Biophys. Acta 1844, 299-307 (2014).

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

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET22b

Entity Sequences (FASTA):
PriB: MTNRLVLSGTVCRAPLRKVS PSGIPHCQFVLEHRSVQEEA GFHRQAWCQMPVIVSGHENQ AITHSITVGSRITVQGFISC HKAKNGLSKMVLHAEQIELI DSGD

Data sets:
Data typeCount
13C chemical shifts282
15N chemical shifts93
1H chemical shifts93

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PriB homodimer, subunit 11
2PriB homodimer, subunit 21

Entities:

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

1   METTHRASNARGLEUVALLEUSERGLYTHR
2   VALCYSARGALAPROLEUARGLYSVALSER
3   PROSERGLYILEPROHISCYSGLNPHEVAL
4   LEUGLUHISARGSERVALGLNGLUGLUALA
5   GLYPHEHISARGGLNALATRPCYSGLNMET
6   PROVALILEVALSERGLYHISGLUASNGLN
7   ALAILETHRHISSERILETHRVALGLYSER
8   ARGILETHRVALGLNGLYPHEILESERCYS
9   HISLYSALALYSASNGLYLEUSERLYSMET
10   VALLEUHISALAGLUGLNILEGLULEUILE
11   ASPSERGLYASP

Samples:

sample_1: PriB, [U-98% 13C; U-98% 15N], 0.5 – 0.8 mM; HEPES 20 mM; ammonium sulfate 200 mM; D2O 10%; H2O 90%; DTT 5 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

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

Olivia, hokkaido university - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB

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