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
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Title: SOLUTION STRUCTURE OF THE FACTOR H BINDING PROTEIN PubMed: 19196709
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: 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).
Assembly members:
Factor H-binding Protein, polymer, 255 residues, 25971.215 Da.
Natural source: Common Name: Neisseria meningitidis 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):
Factor H-binding Protein: MVAADIGAGLADALTAPLDH
KDKGLQSLTLDQSVRKNEKL
KLAAQGAEKTYGNGDSLNTG
KLKNDKVSRFDFIRQIEVDG
QLITLESGEFQVYKQSHSAL
TAFQTEQIQDSEHSGKMVAK
RQFRIGDIAGEHTSFDKLPE
GGRATYRGTAFGSDDAGGKL
TYTIDFAAKQGNGKIEHLKS
PELNVDLAAADIKPDGKRHA
VISGSVLYNQAEKGSYSLGI
FGGKAQEVAGSAEVKTVNGI
RHIGLAAKQHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 932 |
| 15N chemical shifts | 257 |
| 1H chemical shifts | 1629 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Factor H-binding Protein | 1 |
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 | MET | VAL | ALA | ALA | ASP | ILE | GLY | ALA | GLY | LEU | ||||
| 2 | ALA | ASP | ALA | LEU | THR | ALA | PRO | LEU | ASP | HIS | ||||
| 3 | LYS | ASP | LYS | GLY | LEU | GLN | SER | LEU | THR | LEU | ||||
| 4 | ASP | GLN | SER | VAL | ARG | LYS | ASN | GLU | LYS | LEU | ||||
| 5 | LYS | LEU | ALA | ALA | GLN | GLY | ALA | GLU | LYS | THR | ||||
| 6 | TYR | GLY | ASN | GLY | ASP | SER | LEU | ASN | THR | GLY | ||||
| 7 | LYS | LEU | LYS | ASN | ASP | LYS | VAL | SER | ARG | PHE | ||||
| 8 | ASP | PHE | ILE | ARG | GLN | ILE | GLU | VAL | ASP | GLY | ||||
| 9 | GLN | LEU | ILE | THR | LEU | GLU | SER | GLY | GLU | PHE | ||||
| 10 | GLN | VAL | TYR | LYS | GLN | SER | HIS | SER | ALA | LEU | ||||
| 11 | THR | ALA | PHE | GLN | THR | GLU | GLN | ILE | GLN | ASP | ||||
| 12 | SER | GLU | HIS | SER | GLY | LYS | MET | VAL | ALA | LYS | ||||
| 13 | ARG | GLN | PHE | ARG | ILE | GLY | ASP | ILE | ALA | GLY | ||||
| 14 | GLU | HIS | THR | SER | PHE | ASP | LYS | LEU | PRO | GLU | ||||
| 15 | GLY | GLY | ARG | ALA | THR | TYR | ARG | GLY | THR | ALA | ||||
| 16 | PHE | GLY | SER | ASP | ASP | ALA | GLY | GLY | LYS | LEU | ||||
| 17 | THR | TYR | THR | ILE | ASP | PHE | ALA | ALA | LYS | GLN | ||||
| 18 | GLY | ASN | GLY | LYS | ILE | GLU | HIS | LEU | LYS | SER | ||||
| 19 | PRO | GLU | LEU | ASN | VAL | ASP | LEU | ALA | ALA | ALA | ||||
| 20 | ASP | ILE | LYS | PRO | ASP | GLY | LYS | ARG | HIS | ALA | ||||
| 21 | VAL | ILE | SER | GLY | SER | VAL | LEU | TYR | ASN | GLN | ||||
| 22 | ALA | GLU | LYS | GLY | SER | TYR | SER | LEU | GLY | ILE | ||||
| 23 | PHE | GLY | GLY | LYS | ALA | GLN | GLU | VAL | ALA | GLY | ||||
| 24 | SER | ALA | GLU | VAL | LYS | THR | VAL | ASN | GLY | ILE | ||||
| 25 | ARG | HIS | ILE | GLY | LEU | ALA | ALA | LYS | GLN | HIS | ||||
| 26 | HIS | HIS | HIS | HIS | HIS |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_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 simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts