BMRB Entry 16058

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16058
MolProbity Validation Chart

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Title:
SOLUTION STRUCTURE OF THE FACTOR H BINDING PROTEIN
Deposition date:
2008-12-13
Original release date:
2009-02-09
Authors:
Cantini, Francesca; Veggi, Daniele; Dragonetti, Sara; Savino, Silvana; Scarselli, Maria; Romagnoli, Giacomo; Pizza, Mariagrazia; Banci, Lucia; Rappuoli, Rino
Citation:

Citation: Cantini, Francesca; Veggi, Daniele; Dragonetti, Sara; Savino, Silvana; Scarselli, Maria; Romagnoli, Giacomo; Pizza, Mariagrazia; Banci, Lucia; Rappuoli, Rino. "Solution Structure of the Factor H-binding Protein, a Survival Factor and Protective Antigen of Neisseria meningitidis"  J. Biol. Chem. 284, 9022-9026 (2009).
PubMed: 19196709

Assembly members:

Assembly members:
Factor H-binding Protein, polymer, 255 residues, 25971.215 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET20b+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Factor H-binding Protein: MVAADIGAGLADALTAPLDH KDKGLQSLTLDQSVRKNEKL KLAAQGAEKTYGNGDSLNTG KLKNDKVSRFDFIRQIEVDG QLITLESGEFQVYKQSHSAL TAFQTEQIQDSEHSGKMVAK RQFRIGDIAGEHTSFDKLPE GGRATYRGTAFGSDDAGGKL TYTIDFAAKQGNGKIEHLKS PELNVDLAAADIKPDGKRHA VISGSVLYNQAEKGSYSLGI FGGKAQEVAGSAEVKTVNGI RHIGLAAKQHHHHHH

Data sets:
Data typeCount
13C chemical shifts932
15N chemical shifts257
1H chemical shifts1629

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Factor H-binding Protein1

Entities:

Entity 1, Factor H-binding Protein 255 residues - 25971.215 Da.

Residues 1-7 represent a non-structured region and it has not been submitted to PDB. Residues 255-261 represent a non-native affinity tag

1   METVALALAALAASPILEGLYALAGLYLEU
2   ALAASPALALEUTHRALAPROLEUASPHIS
3   LYSASPLYSGLYLEUGLNSERLEUTHRLEU
4   ASPGLNSERVALARGLYSASNGLULYSLEU
5   LYSLEUALAALAGLNGLYALAGLULYSTHR
6   TYRGLYASNGLYASPSERLEUASNTHRGLY
7   LYSLEULYSASNASPLYSVALSERARGPHE
8   ASPPHEILEARGGLNILEGLUVALASPGLY
9   GLNLEUILETHRLEUGLUSERGLYGLUPHE
10   GLNVALTYRLYSGLNSERHISSERALALEU
11   THRALAPHEGLNTHRGLUGLNILEGLNASP
12   SERGLUHISSERGLYLYSMETVALALALYS
13   ARGGLNPHEARGILEGLYASPILEALAGLY
14   GLUHISTHRSERPHEASPLYSLEUPROGLU
15   GLYGLYARGALATHRTYRARGGLYTHRALA
16   PHEGLYSERASPASPALAGLYGLYLYSLEU
17   THRTYRTHRILEASPPHEALAALALYSGLN
18   GLYASNGLYLYSILEGLUHISLEULYSSER
19   PROGLULEUASNVALASPLEUALAALAALA
20   ASPILELYSPROASPGLYLYSARGHISALA
21   VALILESERGLYSERVALLEUTYRASNGLN
22   ALAGLULYSGLYSERTYRSERLEUGLYILE
23   PHEGLYGLYLYSALAGLNGLUVALALAGLY
24   SERALAGLUVALLYSTHRVALASNGLYILE
25   ARGHISILEGLYLEUALAALALYSGLNHIS
26   HISHISHISHISHIS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N; U-80% 2H], 0.4 ± 0.1 mM; potassium phosphate 50 mM; H2O 90%; D2O 10%

sample_2: entity, [U-98% 13C; U-98% 15N], 0.5 ± 0.1 mM; potassium phosphate 50 mM; H2O 90%; D2O 10%

sample_3: entity 0.8 ± 0.1 mM; potassium phosphate 50 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - collection

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CARA, Keller and Wuthrich - chemical shift assignment

XEASY, Bartels et al. - data analysis

ProcheckNMR v10, Laskowski and MacArthur - validation

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 900 MHz

Related Database Links:

PDB
EMBL CCA43599
GB AAF42204 AAR84468 AAR84469 AAR84470 AAR84471
REF NP_274866 WP_002225785 WP_002255070 WP_010981001 WP_039854169

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