BMRB Entry 17025

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17025
MolProbity Validation Chart

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Title:
Solution NMR Structure of protein BVU3908 from Bacteroides vulgatus, Northeast Structural Genomics Consortium Target BvR153
Deposition date:
2010-06-29
Original release date:
2010-08-23
Authors:
Eletsky, Alexander; Lee, Hsiau-Wei; Wang, Dongyan; Ciccosanti, Colleen; Hamilton, Keith; Acton, Thomas; Xiao, Rong; Everett, John; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas
Citation:

Citation: Eletsky, Alexander; Lee, Hsiau-Wei; Wang, Dongyan; Ciccosanti, Colleen; Hamilton, Keith; Acton, Thomas; Xiao, Rong; Everett, John; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of protein BVU3908 from Bacteroides vulgatus"  To be published ., .-..

Assembly members:

Assembly members:
BvR153, polymer, 77 residues, 8775.338 Da.

Natural source:

Natural source:   Common Name: B. vulgatus   Taxonomy ID: 821   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacteroides vulgatus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BvR153: MKMLKEKAGALAGQIWEALN GTEGLTQKQIKKATKLKADK DFFLGLGWLLREDKVVTSEV EGEIFVKLVLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts337
15N chemical shifts76
1H chemical shifts552
residual dipolar couplings108

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BvR153_11
2BvR153_21

Entities:

Entity 1, BvR153_1 77 residues - 8775.338 Da.

Residues 70-77 represent a non-native affinity tag

1   METLYSMETLEULYSGLULYSALAGLYALA
2   LEUALAGLYGLNILETRPGLUALALEUASN
3   GLYTHRGLUGLYLEUTHRGLNLYSGLNILE
4   LYSLYSALATHRLYSLEULYSALAASPLYS
5   ASPPHEPHELEUGLYLEUGLYTRPLEULEU
6   ARGGLUASPLYSVALVALTHRSERGLUVAL
7   GLUGLYGLUILEPHEVALLYSLEUVALLEU
8   GLUHISHISHISHISHISHIS

Samples:

NC5_PAAG: BvR153, [U-5% 13C; U-100% 15N], 1.0 mM; MES 18 mM; sodium chloride 92 mM; calcium chloride 34.6 mM; sodium azide 0.018%; H2O 80%; D2O 20%

NC: BvR153, [U-100% 13C; U-100% 15N], 1.2 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; sodium azide 0.02%; H2O 90%; D2O 10%

NC5: BvR153, [U-5% 13C; U-100% 15N], 1.1 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; sodium azide 0.02%; H2O 90%; D2O 10%

NC5_PEG: BvR153, [U-5% 13C; U-100% 15N], 0.7 mM; MES 13 mM; sodium chloride 67 mM; calcium chloride 3.4 mM; sodium azide 0.013%; C12E5 polyethylene glycol 4%; hexanol 4%; H2O 80%; D2O 20%

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC aliphaticNCisotropicsample_conditions_1
3D HNCONCisotropicsample_conditions_1
3D CBCA(CO)NHNCisotropicsample_conditions_1
3D HNCACBNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC aromaticNCisotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYNCisotropicsample_conditions_1
3D HN(CA)CONCisotropicsample_conditions_1
3D HBHA(CO)NHNCisotropicsample_conditions_1
3D HCCH-COSY aliphaticNCisotropicsample_conditions_1
3D HCCH-COSY aromaticNCisotropicsample_conditions_1
3D HCCH-TOCSY aliphaticNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC methylNC5isotropicsample_conditions_1
2D J-modulation 1H-15N HSQCNC5isotropicsample_conditions_1
2D J-modulation 1H-15N HSQCNC5_PEGanisotropicsample_conditions_1
2D J-modulation 1H-15N HSQCNC5_PAAGanisotropicsample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinement, structure solution

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinement, 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, data analysis

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

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

VNMRJ v2.1B, Varian - collection

TALOS+ v1.2009.0721.18, Shen, Cornilescu, Delaglio and Bax - geometry optimization

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

PROSA v6.4, Guntert - processing

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 500 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
EMBL CDF18736 CUO49642 CUP55985 CUQ36368
GB ABR41511 AII64041 AII69947 ALA75681 ALK85985
REF WP_005841464 WP_007832517 WP_038607296

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