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 16336

Title: Solution Structure Of Protein NMB1076 From Neisseria meningitidis. Northeast Structural Genomics Consortium Target MR101B.

Authors: Wu, Yibing; Maglaqui, Melissa; Eletsky, Alexander; Ciccosanti, Colleen; Sathyamoorthy, Bharathwaj; Jiang, Mei; Garcia, Erwin; Nair, R.; Rost, B.; Swapna, G.V.T; Acton, T.B.; Xiao, R.; Everett, J.K.; Montelione, G.T.; Szyperski, Thomas

Citation: Wu, Yibing; Maglaqui, Melissa; Eletsky, Alexander; Ciccosanti, Colleen; Sathyamoorthy, Bharathwaj; Jiang, Mei; Garcia, Erwin; Nair, R.; Rost, B.; Swapna, G.V.T; Acton, T.B.; Xiao, R.; Everett, J.K.; Montelione, G.T.; Szyperski, Thomas. "Solution Structure Of Protein NMB1076 From Neisseria meningitidis. Northeast Structural Genomics Consortium Target MR101B."  Not known ., .-..

Assembly members:
NMB1076, polymer, 149 residues, 17002.334 Da.

Natural source:   Common Name: b-proteobacteria   Taxonomy ID: 487   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Neisseria meningitidis

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

Entity Sequences (FASTA):
NMB1076: MGHHHHHHSHMDYPSFDKFL GTENAELVYVLRHKHGQFIY VWGEEGAGKSHLLQAWVAQA LEAGKNAAYIDAASMPLTDA AFEAEYLAVDQVEKLGNEEQ ALLFSIFNRFRNSGKGFLLL GSEYTPQQLVIREDLRTRMA YCLVYEVKP

Data sets:
Data typeCount
13C chemical shifts406
15N chemical shifts129
1H chemical shifts873

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NMB10761

Entities:

Entity 1, NMB1076 149 residues - 17002.334 Da.

1   METGLYHISHISHISHISHISHISSERHIS
2   METASPTYRPROSERPHEASPLYSPHELEU
3   GLYTHRGLUASNALAGLULEUVALTYRVAL
4   LEUARGHISLYSHISGLYGLNPHEILETYR
5   VALTRPGLYGLUGLUGLYALAGLYLYSSER
6   HISLEULEUGLNALATRPVALALAGLNALA
7   LEUGLUALAGLYLYSASNALAALATYRILE
8   ASPALAALASERMETPROLEUTHRASPALA
9   ALAPHEGLUALAGLUTYRLEUALAVALASP
10   GLNVALGLULYSLEUGLYASNGLUGLUGLN
11   ALALEULEUPHESERILEPHEASNARGPHE
12   ARGASNSERGLYLYSGLYPHELEULEULEU
13   GLYSERGLUTYRTHRPROGLNGLNLEUVAL
14   ILEARGGLUASPLEUARGTHRARGMETALA
15   TYRCYSLEUVALTYRGLUVALLYSPRO

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 1.0 mM; H2O 90%; D2O 10%

sample_2: entity, [U-5% 13C; U-100% 15N], 1.0 mM; H2O 90%; D2O 10%

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D CCH-TOCSYsample_2isotropicsample_conditions_1
3D 15N-13C RESOLVED SIMULTANIOUS NOESYsample_2isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

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

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

XEASY, Bartels et al. - peak picking

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

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
EMBL CAM08463 CAM10302 CAX50162 CBA05833 CBA08030
GB AAF41471 AAW89546 ABX73175 ACF29645 ADO31553
REF NP_274109 WP_002213636 WP_002259910 WP_003688563 WP_003693249