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 15837

Title: NMR CHEMICAL SHIFT ASSIGNMENTS OF IRON(II) TRANSPORT PROTEIN A FROM CLOSTRIDIUM THERMOCELLUM , NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET VR131

Deposition date: 2008-06-27 Original release date: 2008-08-22

Authors: LIU, GAOHUA; WANG, HUANG; FOOTE, ERICA; JIANG, MEI; XIAO, RONG; SWAPNA, G.V.T; NAIR, RAJESH; EVERETT, JOHN; ACTON, THOMAS; ROST, BURKHARD; Montelione, Gaetano

Citation: LIU, GAOHUA; XIAO, RONG; Montelione, Gaetano. "NMR CHEMICAL SHIFT ASSIGNMENTS OF IRON(II) TRANSPORT PROTEIN A FROM CLOSTRIDIUM THERMOCELLUM , NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET VR131"  .

Assembly members:
IRON(II) TRANSPORT PROTEIN A, polymer, 324 residues, 36536.531 Da.

Natural source:   Common Name: not available   Taxonomy ID: 1515   Superkingdom: not available   Kingdom: Clostridium   Genus/species: thermocellum not available

Experimental source:   Production method: recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . 'pET 21-23C

Entity Sequences (FASTA):
IRON(II) TRANSPORT PROTEIN A: MKLSRLVPGVPARIKRLEVS GELHEKLVGMGFVPGEEIEI VQVAPLGDPIVCKIGNRNIT LRKREADLIEVEVVGGELPL ILADDGTYEITKLNGGRRFL FRMKNLGIESGKKIQVSGRR YYIEGREIDLGYGEATKIWV RRVSDAGEESHPQKLEHHHH HHMKLSRLVPGVPARIKRLE VSGELHEKLVGMGFVPGEEI EIVQVAPLGDPIVCKIGNRN ITLRKREADLIEVEVVGGEL PLILADDGTYEITKLNGGRR FLFRMKNLGIESGKKIQVSG RRYYIEGREIDLGYGEATKI WVRRVSDAGEESHPQKLEHH HHHH

Data sets:
Data typeCount
13C chemical shifts547
15N chemical shifts164
1H chemical shifts1168

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1IRON(II) TRANSPORT PROTEIN A1

Entities:

Entity 1, IRON(II) TRANSPORT PROTEIN A 324 residues - 36536.531 Da.

1   METLYSLEUSERARGLEUVALPROGLYVAL
2   PROALAARGILELYSARGLEUGLUVALSER
3   GLYGLULEUHISGLULYSLEUVALGLYMET
4   GLYPHEVALPROGLYGLUGLUILEGLUILE
5   VALGLNVALALAPROLEUGLYASPPROILE
6   VALCYSLYSILEGLYASNARGASNILETHR
7   LEUARGLYSARGGLUALAASPLEUILEGLU
8   VALGLUVALVALGLYGLYGLULEUPROLEU
9   ILELEUALAASPASPGLYTHRTYRGLUILE
10   THRLYSLEUASNGLYGLYARGARGPHELEU
11   PHEARGMETLYSASNLEUGLYILEGLUSER
12   GLYLYSLYSILEGLNVALSERGLYARGARG
13   TYRTYRILEGLUGLYARGGLUILEASPLEU
14   GLYTYRGLYGLUALATHRLYSILETRPVAL
15   ARGARGVALSERASPALAGLYGLUGLUSER
16   HISPROGLNLYSLEUGLUHISHISHISHIS
17   HISHISMETLYSLEUSERARGLEUVALPRO
18   GLYVALPROALAARGILELYSARGLEUGLU
19   VALSERGLYGLULEUHISGLULYSLEUVAL
20   GLYMETGLYPHEVALPROGLYGLUGLUILE
21   GLUILEVALGLNVALALAPROLEUGLYASP
22   PROILEVALCYSLYSILEGLYASNARGASN
23   ILETHRLEUARGLYSARGGLUALAASPLEU
24   ILEGLUVALGLUVALVALGLYGLYGLULEU
25   PROLEUILELEUALAASPASPGLYTHRTYR
26   GLUILETHRLYSLEUASNGLYGLYARGARG
27   PHELEUPHEARGMETLYSASNLEUGLYILE
28   GLUSERGLYLYSLYSILEGLNVALSERGLY
29   ARGARGTYRTYRILEGLUGLYARGGLUILE
30   ASPLEUGLYTYRGLYGLUALATHRLYSILE
31   TRPVALARGARGVALSERASPALAGLYGLU
32   GLUSERHISPROGLNLYSLEUGLUHISHIS
33   HISHISHISHIS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 0.92 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_12: entity, [U-10% 13C; U-100% 15N], 0.65 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESY (aliph)sample_1isotropicsample_conditions_1
3D SIMULTANEOUS CN-NOESYsample_1isotropicsample_conditions_1
4,3D GFT CABCACONHNsample_1isotropicsample_conditions_1
4,3D GFT HNNCABCAsample_1isotropicsample_conditions_1
4,3D GFT HABCABCONHNsample_1isotropicsample_conditions_1
3D CCH-COSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_12isotropicsample_conditions_1
3D 1H-13C NOESY (arom)sample_1isotropicsample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

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

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

XEASY v1.3.1, Bartels et al. - data analysis

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB

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