BMRB Entry 16336
Click here to enlarge.
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/BMR16336
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solution Structure Of Protein NMB1076 From Neisseria meningitidis. Northeast Structural Genomics Consortium Target MR101B.
Deposition date: 2009-06-08 Original release date: 2009-07-07
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
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 406 |
| 15N chemical shifts | 129 |
| 1H chemical shifts | 873 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NMB1076 | 1 |
Entities:
Entity 1, NMB1076 149 residues - 17002.334 Da.
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | SER | HIS | ||||
| 2 | MET | ASP | TYR | PRO | SER | PHE | ASP | LYS | PHE | LEU | ||||
| 3 | GLY | THR | GLU | ASN | ALA | GLU | LEU | VAL | TYR | VAL | ||||
| 4 | LEU | ARG | HIS | LYS | HIS | GLY | GLN | PHE | ILE | TYR | ||||
| 5 | VAL | TRP | GLY | GLU | GLU | GLY | ALA | GLY | LYS | SER | ||||
| 6 | HIS | LEU | LEU | GLN | ALA | TRP | VAL | ALA | GLN | ALA | ||||
| 7 | LEU | GLU | ALA | GLY | LYS | ASN | ALA | ALA | TYR | ILE | ||||
| 8 | ASP | ALA | ALA | SER | MET | PRO | LEU | THR | ASP | ALA | ||||
| 9 | ALA | PHE | GLU | ALA | GLU | TYR | LEU | ALA | VAL | ASP | ||||
| 10 | GLN | VAL | GLU | LYS | LEU | GLY | ASN | GLU | GLU | GLN | ||||
| 11 | ALA | LEU | LEU | PHE | SER | ILE | PHE | ASN | ARG | PHE | ||||
| 12 | ARG | ASN | SER | GLY | LYS | GLY | PHE | LEU | LEU | LEU | ||||
| 13 | GLY | SER | GLU | TYR | THR | PRO | GLN | GLN | LEU | VAL | ||||
| 14 | ILE | ARG | GLU | ASP | LEU | ARG | THR | ARG | MET | ALA | ||||
| 15 | TYR | CYS | LEU | VAL | TYR | GLU | VAL | LYS | PRO |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 15N-13C RESOLVED SIMULTANIOUS NOESY | sample_2 | isotropic | sample_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 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts