BMRB Entry 15841

Title:
Solution NMR Structure of Protein FeoA from Clostridium thermocellum, Northeast Structural Genomics Consortium Target CmR17
Deposition date:
2008-06-29
Original release date:
2008-08-19
Authors:
Zeri, Ana; Singarapu, Kiran; Mills, Jeffrey; Wu, Yibing; Garcia, Erwin; Wang, Huang; Jiang, Mei; Foote, Erica; Xiao, Rong; Nair, Rajesh; Everett, John; Swapna, G; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Szyperski, Thomas
Citation:

Citation: Zeri, Ana; Singarapu, Kiran; Mills, Jeffrey; Wu, Yibing; Garcia, Erwin; Wang, Huang; Jiang, Mei; Foote, Erica; Xiao, Rong; Nair, Rajesh; Everett, John; Swapna, G; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of Protein FeoA from Clostridium thermocellum, Northeast Structural Genomics Consortium Target CmR17"  .

Assembly members:

Assembly members:
CmR17, polymer, 81 residues, 9247.962 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts363
15N chemical shifts82
1H chemical shifts595

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CmR171

Entities:

Entity 1, CmR17 81 residues - 9247.962 Da.

1   METPHESERLEUARGASPALALYSCYSGLY
2   GLNTHRVALLYSVALVALLYSLEUHISGLY
3   THRGLYALALEULYSARGARGILEMETASP
4   METGLYILETHRARGGLYCYSGLUILETYR
5   ILEARGLYSVALALAPROLEUGLYASPPRO
6   ILEGLNILEASNVALARGGLYTYRGLULEU
7   SERLEUARGLYSSERALAALAGLUMETILE
8   GLUVALGLULEUGLUHISHISHISHISHIS
9   HIS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 1.1 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_2: entity, [U-10% 13C; U-100% 15N], 1.2 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 0.5 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
GFT (4,3)D HCCH COSYsample_1isotropicsample_conditions_1
GFT (4,3)D simNOESYsample_1isotropicsample_conditions_1
GFT (4,3)D HNCABCAsample_1isotropicsample_conditions_1
GFT (4,3)D CABCACONHsample_1isotropicsample_conditions_1
GFT (4,3)D HABCABCONHNsample_1isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

AutoStruct, Huang, Tejero, Powers and Montelione - structure solution

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

VNMRJ, Varian - collection

XEASY, Bartels et al. - data analysis, peak picking

Molmol, Koradi, Billeter and Wuthrich - data analysis, refinement

SPSCAN, Glaser - processing

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ GAE86915
EMBL CDG35310
GB ABN51854 ADU74670 EEU02157 EFB38990 EIC05553
REF WP_003516537 WP_003520966

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