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 17668

Title: NMR solution structure of ZiaAN sub mutant   PubMed: 22198771

Deposition date: 2011-05-26 Original release date: 2011-11-22

Authors: Banci, Lucia; Bertini, Ivano; Felli, Isabella; Pavelkova, Anna

Citation: Tottey, Steve; Patterson, Carl; Banci, Lucia; Bertini, Ivano; Felli, Isabella; Pavelkova, Anna; Dainty, Samantha; Pernil, Rafael; Waldron, Kevin; Foster, Andrew; Robinson, Nigel. "Cyanobacterial metallochaperone inhibits deleterious side reactions of copper."  Proc. Natl. Acad. Sci. U.S.A. 109, 95-100 (2012).

Assembly members:
ZiaAn sub mutant, polymer, 106 residues, 7586.802 Da.

Natural source:   Common Name: Synechocystis sp. PCC 6803   Taxonomy ID: 1148   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Synechocystis sp.

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET29

Entity Sequences (FASTA):
ZiaAn sub mutant: PLKTQQMQVGGMRCAACASS IERALERLKGVAEASVTVAT GRLTVTYDPKQVSEITIQER IAALGYTLAEPKSSVTLNGH KHPHSHREEGHSHSHGAGEF NLKQEL

Data sets:
Data typeCount
13C chemical shifts403
15N chemical shifts99
1H chemical shifts512

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1ZiaAn sub mutant1

Entities:

Entity 1, ZiaAn sub mutant 106 residues - 7586.802 Da.

1   PROLEULYSTHRGLNGLNMETGLNVALGLY
2   GLYMETARGCYSALAALACYSALASERSER
3   ILEGLUARGALALEUGLUARGLEULYSGLY
4   VALALAGLUALASERVALTHRVALALATHR
5   GLYARGLEUTHRVALTHRTYRASPPROLYS
6   GLNVALSERGLUILETHRILEGLNGLUARG
7   ILEALAALALEUGLYTYRTHRLEUALAGLU
8   PROLYSSERSERVALTHRLEUASNGLYHIS
9   LYSHISPROHISSERHISARGGLUGLUGLY
10   HISSERHISSERHISGLYALAGLYGLUPHE
11   ASNLEULYSGLNGLULEU

Samples:

sample_1: ZiaAN sub, [U-99% 13C; U-99% 15N], 0.5 mM; sodium phosphate 50 mM; H20 90%; D20 10%

sample_conditions_1: ionic strength: 50 mM; pH: 7.00; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 800 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