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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18459
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Berry, Jamie-Lee; Phelan, Marie; Collins, Richard; Adomavicius, Tomas; Tnjum, Tone; Frye, Stefan; Bird, Louise; Owens, Ray; Ford, Robert; Lian, Lu-Yun; Derrick, Jeremy. "Structure and assembly of a trans-periplasmic channel for type IV pili in Neisseria meningitidis." PLoS Pathog. 8, .-. (2012).
PubMed: 23028322
Assembly members:
TYPE_IV_PILUS_BIOGENESIS_AND_COMPETENCE_PROTEIN_P, polymer, 128 residues, 14465.3886 Da.
Natural source: Common Name: b-proteobacteria Taxonomy ID: 487 Superkingdom: Bacteria Kingdom: Neisseria Genus/species: Neisseria meningitidis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pETM11
Entity Sequences (FASTA):
TYPE_IV_PILUS_BIOGENESIS_AND_COMPETENCE_PROTEIN_P: MKHHHHHHPMSDYDIPTTEN
LYFEGAMGFTGRKISLDFQD
VEIRTILQILAKESGMNIVA
SDSVNGKMTLSLKDVPWDQA
LDLVMQARNLDMRQQGNIVN
IAPRDELLAKDKAFLQAEKD
IADLGALY
Data type | Count |
13C chemical shifts | 518 |
15N chemical shifts | 133 |
1H chemical shifts | 869 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | TYPE IV PILUS BIOGENESIS AND COMPETENCE PROTEIN P | 1 |
Entity 1, TYPE IV PILUS BIOGENESIS AND COMPETENCE PROTEIN P 128 residues - 14465.3886 Da.
1 | MET | LYS | HIS | HIS | HIS | HIS | HIS | HIS | PRO | MET | ||||
2 | SER | ASP | TYR | ASP | ILE | PRO | THR | THR | GLU | ASN | ||||
3 | LEU | TYR | PHE | GLU | GLY | ALA | MET | GLY | PHE | THR | ||||
4 | GLY | ARG | LYS | ILE | SER | LEU | ASP | PHE | GLN | ASP | ||||
5 | VAL | GLU | ILE | ARG | THR | ILE | LEU | GLN | ILE | LEU | ||||
6 | ALA | LYS | GLU | SER | GLY | MET | ASN | ILE | VAL | ALA | ||||
7 | SER | ASP | SER | VAL | ASN | GLY | LYS | MET | THR | LEU | ||||
8 | SER | LEU | LYS | ASP | VAL | PRO | TRP | ASP | GLN | ALA | ||||
9 | LEU | ASP | LEU | VAL | MET | GLN | ALA | ARG | ASN | LEU | ||||
10 | ASP | MET | ARG | GLN | GLN | GLY | ASN | ILE | VAL | ASN | ||||
11 | ILE | ALA | PRO | ARG | ASP | GLU | LEU | LEU | ALA | LYS | ||||
12 | ASP | LYS | ALA | PHE | LEU | GLN | ALA | GLU | LYS | ASP | ||||
13 | ILE | ALA | ASP | LEU | GLY | ALA | LEU | TYR |
sample_1: TYPE IV PILUS BIOGENESIS AND COMPETENCE PROTEIN P, [U-13C; U-15N], 0.5 mM; H2O 10%; D2O 90%
sample_conditions_1: ionic strength: 100.000 mM; pH: 6.800; pressure: 1.000 atm; temperature: 298.000 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D CBCA(CO)NH | sample_1 | solution | sample_conditions_1 |
3D HNCACB | sample_1 | solution | sample_conditions_1 |
3D HN(CA)CO 3D HNCO | sample_1 | solution | sample_conditions_1 |
2D 1H-15N HSQC | sample_1 | solution | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | solution | sample_conditions_1 |
3D HBHANH | sample_1 | solution | sample_conditions_1 |
2D hbCBcgcdHD | sample_1 | solution | sample_conditions_1 |
2D ali 1H-13C HSQC | sample_1 | solution | sample_conditions_1 |
2D aro 1H-13C HSQC | sample_1 | solution | sample_conditions_1 |
3D ali HC-NOESY | sample_1 | solution | sample_conditions_1 |
3D aro HC-NOESY | sample_1 | solution | sample_conditions_1 |
3D HN-NOESY | sample_1 | solution | sample_conditions_1 |
3D ali HCcH-TOCSY | sample_1 | solution | sample_conditions_1 |
3D aro HCcH-TOCSY | sample_1 | solution | sample_conditions_1 |
3D HNCACB | sample_1 | solution | sample_conditions_1 |
AutoDep v4.3, PDBe - collection
CCPN_analysis vany, CCPN - chemical shift assignment
CNS1.2 vany, Brunger, Adams, Clore, Gros, Nilges and Read - chemical shift assignment
CYANA2.1 vany, Guntert, Mumenthaler and Wuthrich - chemical shift assignment
TALOSPLUS vany, Cornilescu, Delaglio and Bax - chemical shift assignment
Topspin2.1 vany, Bruker Biospin - chemical shift assignment
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks