BMRB Entry 16679

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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/BMR16679
MolProbity Validation Chart

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Title:
1H, 13C and 15N assignment of the C terminal domain of GNA2132 from Neisseria meningitidis
Deposition date:
2010-01-14
Original release date:
2010-04-08
Authors:
Esposito, Veronica; Veggi, Daniele; Musi, Valeria; Pizza, Mariagrazia; Pastore, Annalisa
Citation:

Citation: Esposito, Veronica; Musi, Valeria; Veggi, Daniele; Pastore, Annalisa; Pizza, Mariagrazia. "1H, 13C and 15N assignment of the C-terminal domain of GNA2132 from Neisseria meningitidis."  Biomol. NMR Assignments 4, 107-109 (2010).
PubMed: 20300890

Assembly members:

Assembly members:
GNA_2132, polymer, 193 residues, 20609.7 Da.

Natural source:

Natural source:   Common Name: Neisseria meningitidis   Taxonomy ID: 487   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Neisseria meningitidis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21b+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
GNA_2132: MASLPAEMPLIPVNQADTLI VDGEAVSLTGHSGNIFAPEG NYRYLTYGAEKLPGGSYALR VQGEPAKGEMLAGTAVYNGE VLHFHTENGRPYPTRGRFAA KVDFGSKSVDGIIDSGDDLH MGTQKFKAAIDGNGFKGTWT ENGGGDVSGRFYGPAGEEVA GKYSYRPTDAEKGGFGVFAG KKEQDLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts524
15N chemical shifts133
1H chemical shifts820

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1GNA 21321

Entities:

Entity 1, GNA 2132 193 residues - 20609.7 Da.

1   METALASERLEUPROALAGLUMETPROLEU
2   ILEPROVALASNGLNALAASPTHRLEUILE
3   VALASPGLYGLUALAVALSERLEUTHRGLY
4   HISSERGLYASNILEPHEALAPROGLUGLY
5   ASNTYRARGTYRLEUTHRTYRGLYALAGLU
6   LYSLEUPROGLYGLYSERTYRALALEUARG
7   VALGLNGLYGLUPROALALYSGLYGLUMET
8   LEUALAGLYTHRALAVALTYRASNGLYGLU
9   VALLEUHISPHEHISTHRGLUASNGLYARG
10   PROTYRPROTHRARGGLYARGPHEALAALA
11   LYSVALASPPHEGLYSERLYSSERVALASP
12   GLYILEILEASPSERGLYASPASPLEUHIS
13   METGLYTHRGLNLYSPHELYSALAALAILE
14   ASPGLYASNGLYPHELYSGLYTHRTRPTHR
15   GLUASNGLYGLYGLYASPVALSERGLYARG
16   PHETYRGLYPROALAGLYGLUGLUVALALA
17   GLYLYSTYRSERTYRARGPROTHRASPALA
18   GLULYSGLYGLYPHEGLYVALPHEALAGLY
19   LYSLYSGLUGLNASPLEUGLUHISHISHIS
20   HISHISHIS

Samples:

sample: GNA 2132, [U-100% 13C; U-100% 15N], 0.5 mM; TRIS 20 mM; sodium chloride 50 mM; DPC 30 mM

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsampleisotropicsample_conditions_1
3D HNCAsampleisotropicsample_conditions_1
3D HN(CO)CAsampleisotropicsample_conditions_1
3D HNCOsampleisotropicsample_conditions_1
3D HNCACBsampleisotropicsample_conditions_1
3D CBCA(CO)NHsampleisotropicsample_conditions_1
3D HCCH-TOCSYsampleisotropicsample_conditions_1
3D 1H-15N NOESYsampleisotropicsample_conditions_1
3D 1H-15N TOCSYsampleisotropicsample_conditions_1
3D 1H-13C NOESYsampleisotropicsample_conditions_1

Software:

SPARKY v3.114, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

PDB
EMBL CAX51093 CBA09711 CBN88224 CBX21586 CCA45797
GB AAF42440 AAF42567 AAF42570 AAF42571 AAF42572
REF NP_275117 WP_002218235 WP_002223217 WP_002224198 WP_002224716

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