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 15738

Title: Carbon storage regulator from Helicobacter pylori

Deposition date: 2008-04-21 Original release date: 2014-03-05

Authors: Yang, Chun-Jun; Chen, Heng-Li; Cheng, Hsi-Tsung; Chiu, Chui-Lin; Cheng, Jya-Wei

Citation: Yang, Chun-Jun; Chen, Heng-Li; Cheng, Hsi-Tsung; Chiu, Chui-Lin; Cheng, Jya-Wei. "Structural Characterization and DNA Binding Sequence Selection of the CsrA Protein from Helicobacter pylori"  .

Assembly members:
HP1442, polymer, 85 residues, Formula weight is not available

Natural source:   Common Name: Helicobacter pylori   Taxonomy ID: 210   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Helicobacter pylori

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETBlue-2

Entity Sequences (FASTA):
HP1442: MALILSRKVNEGIVIDDNIH IKVISIDRGSVRLGFEAPES TLILRAELKEAIVSENQKAS VCVDESLLENIKKVIKPLEH HHHHH

Data sets:
Data typeCount
13C chemical shifts227
15N chemical shifts75
1H chemical shifts147

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HP1442, chain A1
2HP1442, chain B1

Entities:

Entity 1, HP1442, chain A 85 residues - Formula weight is not available

Residues 78-85 represent a non-native affinity tag and residue 2 is an artefact from cloning.

1   METALALEUILELEUSERARGLYSVALASN
2   GLUGLYILEVALILEASPASPASNILEHIS
3   ILELYSVALILESERILEASPARGGLYSER
4   VALARGLEUGLYPHEGLUALAPROGLUSER
5   THRLEUILELEUARGALAGLULEULYSGLU
6   ALAILEVALSERGLUASNGLNLYSALASER
7   VALCYSVALASPGLUSERLEULEUGLUASN
8   ILELYSLYSVALILELYSPROLEUGLUHIS
9   HISHISHISHISHIS

Samples:

sample_1: HP1442, [U-13C; U-15N], 1 mM; potassium phosphate 30 mM; sodium chloride 50 mM; EDTA 0.1 mM; DTT 5 mM; sodium azide 10 mM

sample_conditions_1: 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 CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, data analysis

xwinnmr, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

GB NP_208233 AAD08480 ABF85435 ACD48869 ACJ08568 ACX98483
UNP O25983
DBJ BAJ57406 BAJ58911 BAJ60431 BAM97263 BAM98719
EMBL CAX30116 CBI65651
REF NP_208233 WP_000906438 WP_000906439 WP_000906441 WP_000906442
SP B2UVI7 B6JNU0 O25983
AlphaFold O25983 O25983 B2UVI7 B6JNU0

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