BMRB Entry 19851
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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/BMR19851
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Title: NMR structure of the protein YP_001712342.1 from Acinetobacter baumannii
Deposition date: 2014-03-14 Original release date: 2014-04-22
Authors: Proudfoot, Andrew; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt
Citation: Proudfoot, Andrew; Wuthrich, Kurt; Serrano, Pedro; Geralt, Michael; Dutta, Samit. "NMR structure of the protein YP_002937094.1 from Eubacterium rectale" Not known ., .-..
Assembly members:
entity, polymer, 107 residues, 12156.859 Da.
Natural source: Common Name: Acinetobacter baumannii Taxonomy ID: 470 Superkingdom: Bacteria Kingdom: not available Genus/species: Acinetobacter baumannii
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: GTDFGTTNNFVSPNLQLKQN
VLPPTPKNIPLPAFGQRIIG
WGTGAEGARQRLENIQPADV
SMIKKQGTTLEMITAWQDFY
EQEQQRNENNPTAKYRARLM
KKIADLW
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 362 |
| 15N chemical shifts | 115 |
| 1H chemical shifts | 750 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 107 residues - 12156.859 Da.
| 1 | GLY | THR | ASP | PHE | GLY | THR | THR | ASN | ASN | PHE | ||||
| 2 | VAL | SER | PRO | ASN | LEU | GLN | LEU | LYS | GLN | ASN | ||||
| 3 | VAL | LEU | PRO | PRO | THR | PRO | LYS | ASN | ILE | PRO | ||||
| 4 | LEU | PRO | ALA | PHE | GLY | GLN | ARG | ILE | ILE | GLY | ||||
| 5 | TRP | GLY | THR | GLY | ALA | GLU | GLY | ALA | ARG | GLN | ||||
| 6 | ARG | LEU | GLU | ASN | ILE | GLN | PRO | ALA | ASP | VAL | ||||
| 7 | SER | MET | ILE | LYS | LYS | GLN | GLY | THR | THR | LEU | ||||
| 8 | GLU | MET | ILE | THR | ALA | TRP | GLN | ASP | PHE | TYR | ||||
| 9 | GLU | GLN | GLU | GLN | GLN | ARG | ASN | GLU | ASN | ASN | ||||
| 10 | PRO | THR | ALA | LYS | TYR | ARG | ALA | ARG | LEU | MET | ||||
| 11 | LYS | LYS | ILE | ALA | ASP | LEU | TRP |
Samples:
sample_1: entity, [U-98% 13C; U-98% 15N], 1.2 mM; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 5 mM
sample_conditions_1: ionic strength: 0.220 M; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| APSY 4D-HACANH | sample_1 | isotropic | sample_conditions_1 |
| APSY 5D-CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| APSY 5D-HACACONH | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Bruker Biospin, Guntert P. - chemical shift assignment, collection, processing, refinement
UNIO, Herrmann and Wuthrich - chemical shift assignment, structure solution
Opalp, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
CARA, Keller and Wuthrich - chemical shift assignment, refinement
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
MDDNMR, Maxim Mayzel, Vladislav Orekhov - processing
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAN88776 BAP67935 |
| EMBL | CAM87951 CAP02179 CDG77613 CQR69588 CQR89098 |
| GB | ABS89932 ACJ40142 ACJ58428 ADX02293 ADX91089 |
| REF | WP_000266118 WP_000266120 WP_000266121 WP_000266122 WP_000266123 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts