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Biological Magnetic Resonance Data Bank


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BMRB Entry 16064

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16064
MolProbity Validation Chart

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Title: Solution NMR structure of Bacteroides fragilis protein BF1650. Northeast Structural Genomics Consortium target BfR218

Deposition date: 2008-12-17 Original release date: 2009-05-07

Authors: Eletsky, Alexander; Wu, Yibing; Sukumaran, Dinesh; Lee, Hsiau-Wei; Lee, Dong; Jiang, Mei; Foote, Erica; Xiao, Rong; Nair, Rajesh; Everett, John; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Prestegard, James; Szyperski, Thomas

Citation: Eletsky, Alexander; Wu, Yibing; Sukumaran, Dinesh; Lee, Hsiau-Wei; Lee, Dong; Jiang, Mei; Foote, Erica; Xiao, Rong; Nair, Rajesh; Everett, John; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Prestegard, James; Szyperski, Thomas. "Solution NMR structure of Bacteroides fragilis protein BF1650. Northeast Structural Genomics Consortium target BfR218"  Proteins: Struct. Funct. Genet. ., .-..

Assembly members:
bfr218_protein, polymer, 99 residues, 11658.180 Da.

Natural source:   Common Name: Bacteroides fragilis   Taxonomy ID: 817   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacteroides fragilis

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

Entity Sequences (FASTA):
bfr218_protein: MDQLKTIKELINQGDIENAL QALEEFLQTEPVGKDEAYYL MGNAYRKLGDWQKALNNYQS AIELNPDSPALQARKMVMDI LNFYNKDMYNQLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts408
15N chemical shifts108
1H chemical shifts692

Time Domain Data

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1bfr218_protein1

Entities:

Entity 1, bfr218_protein 99 residues - 11658.180 Da.

The last 8 residues represent a non-native affinity tag

1   METASPGLNLEULYSTHRILELYSGLULEU
2   ILEASNGLNGLYASPILEGLUASNALALEU
3   GLNALALEUGLUGLUPHELEUGLNTHRGLU
4   PROVALGLYLYSASPGLUALATYRTYRLEU
5   METGLYASNALATYRARGLYSLEUGLYASP
6   TRPGLNLYSALALEUASNASNTYRGLNSER
7   ALAILEGLULEUASNPROASPSERPROALA
8   LEUGLNALAARGLYSMETVALMETASPILE
9   LEUASNPHETYRASNLYSASPMETTYRASN
10   GLNLEUGLUHISHISHISHISHISHIS

Samples:

NC: MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; sodium azide 0.02%; bfr218 protein, [U-100% 13C; U-100% 15N], 0.89 mM; H2O 90%; D2O 10%

NC5: MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; sodium azide 0.02%; bfr218 protein, [U-5% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%

NC5_phage: MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; sodium azide 0.02%; bfr218 protein, [U-5% 13C; U-100% 15N], 1 mM; Pf1 phage 2.65 g/l; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 215 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicsample_conditions_1
2D 1H-13C HSQC aliNCisotropicsample_conditions_1
2D 1H-13C HSQC aroNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC aliNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC aroNCisotropicsample_conditions_1
3D HNNCONCisotropicsample_conditions_1
(4,3)D GFT CABCA(CO)NHNNCisotropicsample_conditions_1
(4,3)D GFT HNNCABCANCisotropicsample_conditions_1
(4,3)D HABCAB(CO)NHNNCisotropicsample_conditions_1
(4,3)D GFT HCCH-COSY aliNCisotropicsample_conditions_1
(4,3)D GFT HCCH-COSY aroNCisotropicsample_conditions_1
3D (H)CCH-TOCSY aliNCisotropicsample_conditions_1
3D HN(CA)CONCisotropicsample_conditions_1
3D 1H-15N,13C NOESYNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC ali 28msNC5isotropicsample_conditions_1
2D MEXICONCisotropicsample_conditions_1
2D 1H-15N HSQCNC5_phageanisotropicsample_conditions_1
2D 1H-15N TROSYNC5_phageanisotropicsample_conditions_1
2D 1H-15N HSQCNC5isotropicsample_conditions_1
2D 1H-15N TROSYNC5isotropicsample_conditions_1

Software:

VNMRJ v2.1B, Varian - collection

PROSA v6.0.2, Guntert - processing

CARA v1.8.4.2, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

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

TALOS v2007.068.09.07, Cornilescu, Delaglio and Bax - data analysis

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

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

CNS v1.2.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

PSVS v1.3, Bhattacharya and Montelione - structure validation

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 500 MHz

Related Database Links:

PDB
DBJ BAD48398
EMBL CAH07358 CBW22188 CDD38126 CUA18170
GB AKA51470 EES87140 EEZ26991 EGN08814 EIK39617
REF WP_005786499 WP_005800636 WP_032574002 WP_032576056 WP_042986797

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