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 16098

Title: Solution structure of Apo-form YjaB from Escherichia coli   PubMed: 19343803

Deposition date: 2008-12-30 Original release date: 2009-04-17

Authors: Lu, Jie; Wang, Xu; Jin, Changwen

Citation: Lu, Jie; Wang, Xu; Xia, Bin; Jin, Changwen. "Solution structure of Apo-YjaB form Escherichia coli"  Proteins 76, 261-265 (2009).

Assembly members:
Apo-form YjaB, polymer, 147 residues, 16464.789 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Entity Sequences (FASTA):
Apo-form YjaB: MVISIRRSRHEEGEELVAIW CRSVDATHDFLSAEYRTELE DLVRSFLPEAPLWVAVNERD QPVGFMLLSGQHMDALFIDP DVRGCGVGRVLVEHALSMAP ELTTNVNEQNEQAVGFYKKV GFKVTGRSEVDDLGKPYPLL NLAYVGA

Data sets:
Data typeCount
13C chemical shifts622
15N chemical shifts146
1H chemical shifts1013

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Apo-form YjaB1

Entities:

Entity 1, Apo-form YjaB 147 residues - 16464.789 Da.

1   METVALILESERILEARGARGSERARGHIS
2   GLUGLUGLYGLUGLULEUVALALAILETRP
3   CYSARGSERVALASPALATHRHISASPPHE
4   LEUSERALAGLUTYRARGTHRGLULEUGLU
5   ASPLEUVALARGSERPHELEUPROGLUALA
6   PROLEUTRPVALALAVALASNGLUARGASP
7   GLNPROVALGLYPHEMETLEULEUSERGLY
8   GLNHISMETASPALALEUPHEILEASPPRO
9   ASPVALARGGLYCYSGLYVALGLYARGVAL
10   LEUVALGLUHISALALEUSERMETALAPRO
11   GLULEUTHRTHRASNVALASNGLUGLNASN
12   GLUGLNALAVALGLYPHETYRLYSLYSVAL
13   GLYPHELYSVALTHRGLYARGSERGLUVAL
14   ASPASPLEUGLYLYSPROTYRPROLEULEU
15   ASNLEUALATYRVALGLYALA

Samples:

sample_1: TRIS 30 mM; sodium chloride 100 mM; DTT 10 mM; YjaB protein, [U-13C; U-15N], 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 130 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

NMRPipe v2.1, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView v5, Johnson, One Moon Scientific - data analysis

xwinnmr v3.5, Bruker Biospin - collection

CYANA v2.0, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER v7, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - structure refinement

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAE78014 BAI28268 BAI33451 BAI38569 BAJ45724
EMBL CAA26570 CAQ34361 CAR00982 CAV01265 CBJ03773
GB AAC43106 AAC76982 AAZ90685 ABB64225 ABV08412
REF NP_418436 WP_000236960 WP_000236962 WP_000236972 WP_000236973
SP P09163
AlphaFold P09163

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