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 16126

Title: Solution structure of HypA protein   PubMed: 19621959

Deposition date: 2009-01-20 Original release date: 2009-07-08

Authors: Xia, Wei; Li, Hongyan; Sze, Kong-hung

Citation: Xia, Wei; Li, Hongyan; Sze, Kong-hung; Sun, Hongzhe. "Structure of a nickel chaperone, HypA, from Helicobacter pylori reveals two distinct metal binding sites"  J. Am. Chem. Soc. 131, 10031-10040 (2009).

Assembly members:
HypA, polymer, 119 residues, 13365.460 Da.
ZN, non-polymer, 65.409 Da.

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

Entity Sequences (FASTA):
HypA: GSMHEYSVVSSLIALCEEHA KKNQAHKIERVVVGIGERSA MDKSLFVSAFETFREESLVC KDAILDIVDEKVELECKDCS HVFKPNALDYGVCEKCHSKN VIITQGNEMRLLSLEMLAE

Data sets:
Data typeCount
13C chemical shifts498
15N chemical shifts126
1H chemical shifts813

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HypA1
2Zn2

Entities:

Entity 1, HypA 119 residues - 13365.460 Da.

1   GLYSERMETHISGLUTYRSERVALVALSER
2   SERLEUILEALALEUCYSGLUGLUHISALA
3   LYSLYSASNGLNALAHISLYSILEGLUARG
4   VALVALVALGLYILEGLYGLUARGSERALA
5   METASPLYSSERLEUPHEVALSERALAPHE
6   GLUTHRPHEARGGLUGLUSERLEUVALCYS
7   LYSASPALAILELEUASPILEVALASPGLU
8   LYSVALGLULEUGLUCYSLYSASPCYSSER
9   HISVALPHELYSPROASNALALEUASPTYR
10   GLYVALCYSGLULYSCYSHISSERLYSASN
11   VALILEILETHRGLNGLYASNGLUMETARG
12   LEULEUSERLEUGLUMETLEUALAGLU

Entity 2, Zn - Zn - 65.409 Da.

1   ZN

Samples:

13C-15N_HypA: HypA, [U-99% 13C; U-99% 15N], 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC13C-15N_HypAisotropicsample_conditions_1
2D 1H-13C HSQC13C-15N_HypAisotropicsample_conditions_1
3D HNCO13C-15N_HypAisotropicsample_conditions_1
3D HN(CA)CO13C-15N_HypAisotropicsample_conditions_1
3D CBCA(CO)NH13C-15N_HypAisotropicsample_conditions_1
3D HNCACB13C-15N_HypAisotropicsample_conditions_1
3D HCCH-COSY13C-15N_HypAisotropicsample_conditions_1
3D HCCH-TOCSY13C-15N_HypAisotropicsample_conditions_1
3D 1H-15N NOESY13C-15N_HypAisotropicsample_conditions_1
3D 1H-13C NOESY13C-15N_HypAisotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER v7.0, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAJ55092 BAJ56561 BAJ58417 BAJ59961 BAM96786
EMBL CAJ99986 CAX29022 CBI66635
GB AAD06365 AAD07910 ABF84919 ACD47943 ACI27578
REF NP_207663 WP_000545266 WP_000545267 WP_000545269 WP_000545270
SP P0A0U4 P0A0U5

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