BMRB Entry 17521

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17521
MolProbity Validation Chart

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Title:
Solution structure of an E. coli lipoprotein
Deposition date:
2011-03-11
Original release date:
2011-06-01
Authors:
Pardi, Arthur; Warner, Lisa
Citation:

Citation: Warner, Lisa; Varga, Krisztina; Lange, Oliver; Baker, Susan; Baker, David; Sousa, Marcelo; Pardi, Arthur. "Structure of the BamC two-domain protein obtained by Rosetta with a limited NMR data set."  J. Mol. Biol. 411, 83-95 (2011).
PubMed: 21624375

Assembly members:

Assembly members:
BamC, polymer, 249 residues, 12648.172 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET41b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BamC: GAMGDTASLLVENGRGNTLW PQVVSVLQAKNYTITQRDDA GQTLTTDWVQWNRLDEDEQY RGRYQISVKPQGYQQAVTVK LLNLEQAGKPVADAASMQRY STEMMNVISAGLDKSATDAA NAAQNRASTTMDVQSAADDT GLPMLVVRGPFNVVWQRLPA ALEKVGMKVTDSTRSQGNMA VTYKPLSDSDWQELGASDPG LASGDYKLQVGDLDNRSSLQ FIDPKGHTLTQSQNDALVAV FQAAFSKPG

Data sets:
Data typeCount
13C chemical shifts941
15N chemical shifts243
1H chemical shifts1352
residual dipolar couplings156

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1BamC1

Entities:

Entity 1, BamC 249 residues - 12648.172 Da.

1   GLYALAMETGLYASPTHRALASERLEULEU
2   VALGLUASNGLYARGGLYASNTHRLEUTRP
3   PROGLNVALVALSERVALLEUGLNALALYS
4   ASNTYRTHRILETHRGLNARGASPASPALA
5   GLYGLNTHRLEUTHRTHRASPTRPVALGLN
6   TRPASNARGLEUASPGLUASPGLUGLNTYR
7   ARGGLYARGTYRGLNILESERVALLYSPRO
8   GLNGLYTYRGLNGLNALAVALTHRVALLYS
9   LEULEUASNLEUGLUGLNALAGLYLYSPRO
10   VALALAASPALAALASERMETGLNARGTYR
11   SERTHRGLUMETMETASNVALILESERALA
12   GLYLEUASPLYSSERALATHRASPALAALA
13   ASNALAALAGLNASNARGALASERTHRTHR
14   METASPVALGLNSERALAALAASPASPTHR
15   GLYLEUPROMETLEUVALVALARGGLYPRO
16   PHEASNVALVALTRPGLNARGLEUPROALA
17   ALALEUGLULYSVALGLYMETLYSVALTHR
18   ASPSERTHRARGSERGLNGLYASNMETALA
19   VALTHRTYRLYSPROLEUSERASPSERASP
20   TRPGLNGLULEUGLYALASERASPPROGLY
21   LEUALASERGLYASPTYRLYSLEUGLNVAL
22   GLYASPLEUASPASNARGSERSERLEUGLN
23   PHEILEASPPROLYSGLYHISTHRLEUTHR
24   GLNSERGLNASNASPALALEUVALALAVAL
25   PHEGLNALAALAPHESERLYSPROGLY

Samples:

sample_1: BamC 1.1 mM; sodium phosphate 50 mM; sodium chloride 50 mM; EDTA 0.1 mM; sodium azide 0.02%; HALT 1 X; H2O 90%; D2O 10%

sample_2: BamC 1.1 mM; sodium phosphate 50 mM; sodium chloride 50 mM; EDTA 0.1 mM; sodium azide 0.02%; HALT 1 X; D2O 100%

sample_3: BamC 1.1 mM; sodium phosphate 50 mM; sodium chloride 50 mM; EDTA 0.1 mM; sodium azide 0.02%; HALT 1 X; Pf1 phage 21 mg/ml; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.2 M; pH: 6.6; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNHAHBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D (H)C(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
2D 1H-15N HSQC IPAPsample_3anisotropicsample_conditions_1
2D 1H-15N HSQC IPAPsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

CS-NOE-RDC_Rosetta, David Baker - structure solution

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

NMR spectrometers:

  • Varian VNMRS 900 MHz
  • Varian VNMRS 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

BMRB 16035
PDB
DBJ BAA16354 BAB36762 BAG78285 BAI26723 BAI31755
EMBL CAA40661 CAP76938 CAQ32848 CAQ99368 CAR03928
GB AAA24447 AAC75530 AAG57587 AAN44023 AAN81455
REF NP_311366 NP_416972 NP_708316 WP_000968412 WP_001295468
SP P0A903 P0A904
AlphaFold P0A903 P0A904

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