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 15211

Title: Solution NMR structure of protein , Northeastprotein yxeF Structural Genomics Consortium target Sr500a

Authors: Wu, Yibing; Liu, Gaohua; Zhang, Qi; Bhatnagar, Sagar; Chen, Chen X.; Nwosu, Chioma; Xiao, Rong; Cunningham, Kellie; Locke, Jessica; Ma, Li-Chung; Swapna, G.V.T; Baran, Michael C.; Acton, Thomas; Montelione, Gaetano; Szyperski, Thomas

Citation: Wu, Yibing; Liu, Gaohua; Zhang, Qi; Bhatnagar, Sagar; Chen, Chen X.; Nwosu, Chioma; Xiao, Rong; Cunningham, Kellie; Locke, Jessica; Ma, Li-Chung; Swapna, G.V.T; Baran, Michael C.; Acton, Thomas; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR structure of protein, Northeastprotein yxeF Structural Genomics Consortium target Sr500a"  Protein Sci. ., .-..

Assembly members:
protein yxeF, polymer, 135 residues, 15450.332 Da.

Natural source:   Common Name: not available   Taxonomy ID: 1423   Superkingdom: Bacteria   Kingdom: Bacillus   Genus/species: subtilis subtilis

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

Entity Sequences (FASTA):
protein yxeF: MIMVSGCQQQKEETPFYYGT WDEGRAPGPTDGVKSATVTF TEDEVVETEVMEGRGEVQLP FMAYKVISQSTDGSIEIQYL GPYYPLKSTLKRGENGTLIW EQNGQRKTMTRIESKTGREE KDEKSKSLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts542
15N chemical shifts131
1H chemical shifts886

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1protein yxeF1

Entities:

Entity 1, protein yxeF 135 residues - 15450.332 Da.

1   METILEMETVALSERGLYCYSGLNGLNGLN
2   LYSGLUGLUTHRPROPHETYRTYRGLYTHR
3   TRPASPGLUGLYARGALAPROGLYPROTHR
4   ASPGLYVALLYSSERALATHRVALTHRPHE
5   THRGLUASPGLUVALVALGLUTHRGLUVAL
6   METGLUGLYARGGLYGLUVALGLNLEUPRO
7   PHEMETALATYRLYSVALILESERGLNSER
8   THRASPGLYSERILEGLUILEGLNTYRLEU
9   GLYPROTYRTYRPROLEULYSSERTHRLEU
10   LYSARGGLYGLUASNGLYTHRLEUILETRP
11   GLUGLNASNGLYGLNARGLYSTHRMETTHR
12   ARGILEGLUSERLYSTHRGLYARGGLUGLU
13   LYSASPGLULYSSERLYSSERLEUGLUHIS
14   HISHISHISHISHIS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 1 mM; Tris 10 mM; NaCl 100%; NaN3 0.02%

sample_2: entity, [U-10% 13C; U-100% 15N], 1 mM; Tris 10 mM; NaCl 100%; NaN3 0.02%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
4,3D, GFT HNNCABCAsample_1isotropicsample_conditions_1
4,3D, GFT CABCACONNHsample_1isotropicsample_conditions_1
4,3D, GFT HCCH COSYsample_1isotropicsample_conditions_1
3D, 15N-13C RESOLVED SIMULTANIOUS NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
1H-13C HSQCsample_2isotropicsample_conditions_1

Software:

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

NMRPipe v9.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

AutoStruct v1.0, Huang, Swapana, Rajan, Ke, Xia, Shukla, Inouye and Montelione - structure solution

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

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

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian Avance 600 MHz

Related Database Links:

PDB
DBJ BAA08322 BAI87653 BAM56043 BAM60055 GAK81370
EMBL CAB15993 CEI59768 CEJ79625 CJR72173 CON90429
GB ADV94782 AEP93027 AFQ59810 AGA22603 AGG63371
REF NP_391836 WP_003227095 WP_003244165 WP_014478470 WP_014481402
SP P54945