BMRB Entry 16240
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16240
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Title: Solution structure of full-length SlyD from E.coli PubMed: 19760519
Deposition date: 2009-04-03 Original release date: 2009-09-24
Authors: Martino, Luigi; Kelly, Geoff; Conte, Maria
Citation: Martino, Luigi; Kelly, Geoff; Conte, Maria. "Resonance assignment of SlyD from E. coli" Biomol. NMR Assignments 3, 235-237 (2009).
Assembly members:
SlyD, polymer, 196 residues, 20883.012 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
SlyD: MKVAKDLVVSLAYQVRTEDG
VLVDESPVSAPLDYLHGHGS
LISGLETALEGHEVGDKFDV
AVGANDAYGQYDENLVQRVP
KDVFMGVDELQVGMRFLAET
DQGPVPVEITAVEDDHVVVD
GNHMLAGQNLKFNVEVVAIR
EATEEELAHGHVHGAHDHHH
DHDHDGCCGGHGHDHGHEHG
GEGCCGGKGNGGCGCH
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 609 |
15N chemical shifts | 148 |
1H chemical shifts | 920 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | SlyD | 1 |
Entities:
Entity 1, SlyD 196 residues - 20883.012 Da.
Full length native protein
1 | MET | LYS | VAL | ALA | LYS | ASP | LEU | VAL | VAL | SER | ||||
2 | LEU | ALA | TYR | GLN | VAL | ARG | THR | GLU | ASP | GLY | ||||
3 | VAL | LEU | VAL | ASP | GLU | SER | PRO | VAL | SER | ALA | ||||
4 | PRO | LEU | ASP | TYR | LEU | HIS | GLY | HIS | GLY | SER | ||||
5 | LEU | ILE | SER | GLY | LEU | GLU | THR | ALA | LEU | GLU | ||||
6 | GLY | HIS | GLU | VAL | GLY | ASP | LYS | PHE | ASP | VAL | ||||
7 | ALA | VAL | GLY | ALA | ASN | ASP | ALA | TYR | GLY | GLN | ||||
8 | TYR | ASP | GLU | ASN | LEU | VAL | GLN | ARG | VAL | PRO | ||||
9 | LYS | ASP | VAL | PHE | MET | GLY | VAL | ASP | GLU | LEU | ||||
10 | GLN | VAL | GLY | MET | ARG | PHE | LEU | ALA | GLU | THR | ||||
11 | ASP | GLN | GLY | PRO | VAL | PRO | VAL | GLU | ILE | THR | ||||
12 | ALA | VAL | GLU | ASP | ASP | HIS | VAL | VAL | VAL | ASP | ||||
13 | GLY | ASN | HIS | MET | LEU | ALA | GLY | GLN | ASN | LEU | ||||
14 | LYS | PHE | ASN | VAL | GLU | VAL | VAL | ALA | ILE | ARG | ||||
15 | GLU | ALA | THR | GLU | GLU | GLU | LEU | ALA | HIS | GLY | ||||
16 | HIS | VAL | HIS | GLY | ALA | HIS | ASP | HIS | HIS | HIS | ||||
17 | ASP | HIS | ASP | HIS | ASP | GLY | CYS | CYS | GLY | GLY | ||||
18 | HIS | GLY | HIS | ASP | HIS | GLY | HIS | GLU | HIS | GLY | ||||
19 | GLY | GLU | GLY | CYS | CYS | GLY | GLY | LYS | GLY | ASN | ||||
20 | GLY | GLY | CYS | GLY | CYS | HIS |
Samples:
sample_1: entity, [U-100% 13C; U-100% 15N], 0.5 0.9 mM; TRIS 20 mM; potassium chloride 100 mM; DTT 1 mM
sample_conditions_1: ionic strength: 100 mM; pH: 7.25; pressure: 1.0 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
3D HNHA | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TALOS, Cornilescu, Delaglio and Bax - data analysis
VNMR, Varian - collection
TOPSPIN, Bruker Biospin - collection
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker Avance 700 MHz
- Bruker Avance 600 MHz
- Varian INOVA 800 MHz
- Varian INOVA 600 MHz
Related Database Links:
BMRB | 15950 |
PDB | |
DBJ | BAB37623 BAE77942 BAG79134 BAH65509 BAI27607 |
EMBL | CAA79705 CAD08158 CAP77801 CAQ33668 CAQ90798 |
GB | AAA18574 AAA58146 AAC41458 AAC76374 AAG58456 |
PIR | AB1004 |
REF | NP_312227 NP_417808 NP_458445 NP_462359 NP_709123 |
SP | P0A9K9 P0A9L0 P0A9L1 P0A9L2 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts