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 16929

Title: NMR structure and calcium-binding properties of the tellurite resistance protein TerD from Klebsiella pneumoniae   PubMed: 21112337

Deposition date: 2010-05-14 Original release date: 2010-12-02

Authors: Pan, Yun-Ru; Lou, Yuan-Chou; Rizo, Josep; Chen, Chinpan

Citation: Pan, Yun-Ru; Lou, Yuan-Chao; Seven, Alpay; Rizo, Josep; Chen, Chinpan. "NMR Structure and Calcium-Binding Properties of the Tellurite Resistance Protein TerD from Klebsiella pneumoniae."  J. Mol. Biol. 405, 1188-1201 (2011).

Assembly members:
TerD, polymer, 200 residues, 21558.7 Da.
CA, non-polymer, 40.078 Da.

Natural source:   Common Name: K. pneumoniae   Taxonomy ID: 573   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Klebsiella pneumoniae

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

Entity Sequences (FASTA):
TerD: MSVSLSKGGNVSLSKTAPSM KNVLVGLGWDARSTDGQDFD LDASAFLLAANGKVRGDADF IFYNNLKSADGSVTHTGDNR TGEGDGDDESLKIKLDAVPG DVDKIIFVVTIHDAQARRQS FGQVSGAFIRLVNDDNQTEV ARYDLTEDASTETAMLFGEL YRHNGEWKFRAVGQGYAGGL ASVCAQYGINASLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts806
15N chemical shifts203
1H chemical shifts1209

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TerD1
2CA2

Entities:

Entity 1, TerD 200 residues - 21558.7 Da.

1   METSERVALSERLEUSERLYSGLYGLYASN
2   VALSERLEUSERLYSTHRALAPROSERMET
3   LYSASNVALLEUVALGLYLEUGLYTRPASP
4   ALAARGSERTHRASPGLYGLNASPPHEASP
5   LEUASPALASERALAPHELEULEUALAALA
6   ASNGLYLYSVALARGGLYASPALAASPPHE
7   ILEPHETYRASNASNLEULYSSERALAASP
8   GLYSERVALTHRHISTHRGLYASPASNARG
9   THRGLYGLUGLYASPGLYASPASPGLUSER
10   LEULYSILELYSLEUASPALAVALPROGLY
11   ASPVALASPLYSILEILEPHEVALVALTHR
12   ILEHISASPALAGLNALAARGARGGLNSER
13   PHEGLYGLNVALSERGLYALAPHEILEARG
14   LEUVALASNASPASPASNGLNTHRGLUVAL
15   ALAARGTYRASPLEUTHRGLUASPALASER
16   THRGLUTHRALAMETLEUPHEGLYGLULEU
17   TYRARGHISASNGLYGLUTRPLYSPHEARG
18   ALAVALGLYGLNGLYTYRALAGLYGLYLEU
19   ALASERVALCYSALAGLNTYRGLYILEASN
20   ALASERLEUGLUHISHISHISHISHISHIS

Entity 2, CA - Ca - 40.078 Da.

1   CA

Samples:

KP-TerD: potassium phosphate 20 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.02 M; pH: 7; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCKP-TerDisotropicsample_conditions_1
2D 1H-13C HSQCKP-TerDisotropicsample_conditions_1
3D CBCA(CO)NHKP-TerDisotropicsample_conditions_1
3D HNCACBKP-TerDisotropicsample_conditions_1
3D HNCOKP-TerDisotropicsample_conditions_1
3D HN(CO)CAKP-TerDisotropicsample_conditions_1
3D C(CO)NHKP-TerDisotropicsample_conditions_1
3D 1H-15N NOESYKP-TerDisotropicsample_conditions_1
3D 1H-13C NOESYKP-TerDisotropicsample_conditions_1
3D HCCH-TOCSYKP-TerDisotropicsample_conditions_1
3D HBHA(CO)NHKP-TerDisotropicsample_conditions_1
3D HNHAKP-TerDisotropicsample_conditions_1
2D 1H-1H NOESYKP-TerDisotropicsample_conditions_1
2D CACO (ipap)KP-TerDisotropicsample_conditions_1

Software:

AURELIA v3.1.6, Linge, O, . - data analysis

xwinnmr v3.5, Bruker Biospin - processing

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

VNMR v5.0, Johnson, One Moon Scientific - chemical shift assignment

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

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAH66157
EMBL CAJ86458 CDI26595 CDM79667 CEO83282 CEP33510
GB AAA98292 AAR07677 ABF67755 ABU77054 ACI11978
PRF 2009362B
REF NP_943327 WP_000116676 WP_000116677 WP_004026609 WP_004181727
SP P18781

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