BMRB Entry 15834

Title:
Solution NMR structure of FeoA protein from Chlorobium tepidum. Northeast Structural Genomics Consortium target CtR121
Deposition date:
2008-06-27
Original release date:
2008-07-24
Authors:
Eletsky, Alexander; Sathyamoorthy, Bharathwaj; Mills, Jeffrey; Zeri, Ana; Zhao, Li; Hamilton, Keith; Foote, Erica; Xiao, Rong; Nair, Rajesh; Baran, Michael; Swapna, G.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Szyperski, Thomas
Citation:

Citation: Eletsky, Alexander; Sathyamoorthy, Bharathwaj; Mills, Jeffrey; Zeri, Ana; Zhao, Li; Hamilton, Keith; Foote, Erica; Xiao, Rong; Nair, Rajesh; Baran, Michael; Swapna, G.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR structure of FeoA protein from Chlorobium tepidum. Northeast Structural Genomics Consortium target CtR121"  Proteins: Struct. Funct. Genet. ., .-..

Assembly members:

Assembly members:
FeoA_protein, polymer, 105 residues, 11872.900 Da.

Natural source:

Natural source:   Common Name: Chlorobium tepidum   Taxonomy ID: 1097   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Chlorobium tepidum

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET 21-23C

Data sets:
Data typeCount
13C chemical shifts416
15N chemical shifts104
1H chemical shifts682
coupling constants68

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FeoA_protein1

Entities:

Entity 1, FeoA_protein 105 residues - 11872.900 Da.

8-residue C-terminal tag LEHHHHHH

1   METLYSLEUSERGLULEULYSALAGLYASP
2   ARGALAGLUVALTHRSERVALALAALAGLU
3   PROALAVALARGARGARGLEUMETASPLEU
4   GLYLEUVALARGGLYALALYSLEULYSVAL
5   LEUARGPHEALAPROLEUGLYASPPROILE
6   GLUVALASNCYSASNGLYMETLEULEUTHR
7   METARGARGASNGLUALAGLUGLYILETHR
8   VALHISILELEUALAGLYASPGLUGLYHIS
9   PROHISGLYTRPPROGLYPHEARGARGARG
10   HISARGPHEGLYLYSARGALALEUGLUHIS
11   HISHISHISHISHIS

Samples:

NC: FeoA protein, [U-100% 13C; U-100% 15N], 1.26 mM; sodium azide 0.02%; DTT 100 mM; calcium chloride 5 mM; sodium chloride 100 mM; MES 20 mM; DSS 50 uM; H2O 90%; D2O, [U-100% 2H], 10%

NC5: FeoA protein, [U-5% 13C; U-100% 15N], 1.26 mM; sodium azide 0.02%; DTT 100 mM; calcium chloride 5 mM; sodium chloride 100 mM; MES 20 mM; DSS 50 uM; H2O 90%; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 115 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicsample_conditions_1
2D 1H-13C HSQCNCisotropicsample_conditions_1
3D HNCONCisotropicsample_conditions_1
3D CBCA(CO)NHNCisotropicsample_conditions_1
3D HNCACBNCisotropicsample_conditions_1
3D HBHA(CO)NHNCisotropicsample_conditions_1
3D HCCH-TOCSYNCisotropicsample_conditions_1
(4,3)D GFT HCCH-COSY aliNCisotropicsample_conditions_1
(4,3)D GFT L-HCCH-COSY aroNCisotropicsample_conditions_1
3D HNHANCisotropicsample_conditions_1
3D HNCO (hbond)NCisotropicsample_conditions_1
3D 1H-15N,13Cali,13Caro NOESYNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC 28msNC5isotropicsample_conditions_1

Software:

VNMRJ v2.1B, Varian - collection

PROSA v6.0.2, Guntert - processing

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

XEASY v1.3.13, Bartels et al. - data analysis

AutoAssign v1.15.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

CSI v2.0, Wishat and Sykes - data analysis

TALOS v2003.027.13.05, Cornilescu, Delaglio and Bax - data analysis

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

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - structure solution

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

PSVS v1.3, Bhattacharya and Montelione - validation

NMR spectrometers:

  • Varian INOVA 750 MHz

Related Database Links:

PDB
GB AAM71305
REF NP_660963 WP_010931751

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