BMRB Entry 18361
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18361
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Title: The chemical shifts and T1, T2, and 1H-15N NOE data for apo-IscU(N90A) PubMed: 22734684
Deposition date: 2012-03-28 Original release date: 2012-09-14
Authors: Kim, Jin Hae; Tonelli, Marco; Markley, John
Citation: Kim, Jin Hae; Tonelli, Marco; Kim, Taewook; Markley, John. "Three-Dimensional Structure and Determinants of Stability of the Iron-Sulfur Cluster Scaffold Protein IscU from Escherichia coli." Biochemistry 51, 5557-5563 (2012).
Assembly members:
IscU(N90A), polymer, 128 residues, Formula weight is not available
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
IscU(N90A): MAYSEKVIDHYENPRNVGSF
DNNDENVGSGMVGAPACGDV
MKLQIKVNDEGIIEDARFKT
YGCGSAIASSSLVTEWVKGK
SLDEAQAIKATDIAEELELP
PVKIHCSILAEDAIKAAIAD
YKSKREAK
- assigned_chemical_shifts
- heteronucl_NOEs
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
| Data type | Count |
| 13C chemical shifts | 258 |
| 15N chemical shifts | 87 |
| 1H chemical shifts | 87 |
| heteronuclear NOE values | 82 |
| T1 relaxation values | 82 |
| T2 relaxation values | 82 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | IscU(N90A) | 1 |
Entities:
Entity 1, IscU(N90A) 128 residues - Formula weight is not available
| 1 | MET | ALA | TYR | SER | GLU | LYS | VAL | ILE | ASP | HIS | ||||
| 2 | TYR | GLU | ASN | PRO | ARG | ASN | VAL | GLY | SER | PHE | ||||
| 3 | ASP | ASN | ASN | ASP | GLU | ASN | VAL | GLY | SER | GLY | ||||
| 4 | MET | VAL | GLY | ALA | PRO | ALA | CYS | GLY | ASP | VAL | ||||
| 5 | MET | LYS | LEU | GLN | ILE | LYS | VAL | ASN | ASP | GLU | ||||
| 6 | GLY | ILE | ILE | GLU | ASP | ALA | ARG | PHE | LYS | THR | ||||
| 7 | TYR | GLY | CYS | GLY | SER | ALA | ILE | ALA | SER | SER | ||||
| 8 | SER | LEU | VAL | THR | GLU | TRP | VAL | LYS | GLY | LYS | ||||
| 9 | SER | LEU | ASP | GLU | ALA | GLN | ALA | ILE | LYS | ALA | ||||
| 10 | THR | ASP | ILE | ALA | GLU | GLU | LEU | GLU | LEU | PRO | ||||
| 11 | PRO | VAL | LYS | ILE | HIS | CYS | SER | ILE | LEU | ALA | ||||
| 12 | GLU | ASP | ALA | ILE | LYS | ALA | ALA | ILE | ALA | ASP | ||||
| 13 | TYR | LYS | SER | LYS | ARG | GLU | ALA | LYS |
Samples:
sample_1: IscU(N90A), [U-13C; U-15N], 1.5 – 2 mM; TRIS 20 mM; DTT 5 mM; EDTA 0.5 mM; sodium chloride 150 mM; DSS 0.7 mM; D2O, [U-99% 2H], 7%; sodium azide 0.02%; H2O, [U-99% 2H], 93%
sample_conditions_1: ionic strength: 0.15 M; pH: 8; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
VNMRJ, Varian - collection
SPARKY, Goddard - chemical shift assignment, data analysis, peak picking
NMR spectrometers:
- Varian VNMRS 600 MHz
Related Database Links:
| BMRB | 15967 16245 16603 17282 17836 17837 17844 18359 18360 18362 18381 18750 18754 |
| PDB | |
| DBJ | BAA16423 BAB36818 BAG78339 BAI26774 BAI31803 |
| EMBL | CAD02745 CAP76981 CAQ32902 CAQ88187 CAQ99420 |
| GB | AAC75582 AAG57643 AAL21436 AAN44075 AAN81505 |
| PIR | AE0824 |
| REF | NP_311422 NP_417024 NP_457073 NP_461477 NP_708368 |
| SP | P0ACD4 P0ACD5 P0ACD6 P0ACD7 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts