BMRB Entry 25266
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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/BMR25266
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Title: Solution structure of decorin binding protein B from Borrelia burgdorferi
Deposition date: 2014-10-03 Original release date: 2015-08-17
Authors: Wang, Xu; Feng, Wei
Citation: Wang, Xu; Feng, Wei; Chao, Alex. "Structure of Decorin Binding Protein B from Borrelia Spirochetes" Not known ., .-..
Assembly members:
DBPB, polymer, 167 residues, 36406.660 Da.
Natural source: Common Name: Lyme disease spirochete Taxonomy ID: 139 Superkingdom: Bacteria Kingdom: not available Genus/species: Borrelia burgdorferi
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
DBPB: SSIGLVERTNAALESSSKDL
KNKILKIKKEATGKGVLFEA
FTGLKTGSKVTSGGLALREA
KVQAIVETGKFLKIIEEEAL
KLKETGNSGQFLAMFDLMLE
VVESLEDVGIIGLKARVLEE
SKNNPINTAERLLAAKAQIE
NQLKVVKEKQNIENGGEKKN
NKSKKKK
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 711 |
15N chemical shifts | 173 |
1H chemical shifts | 1004 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | entity | 1 |
Entities:
Entity 1, entity 167 residues - 36406.660 Da.
1 | SER | SER | ILE | GLY | LEU | VAL | GLU | ARG | THR | ASN | ||||
2 | ALA | ALA | LEU | GLU | SER | SER | SER | LYS | ASP | LEU | ||||
3 | LYS | ASN | LYS | ILE | LEU | LYS | ILE | LYS | LYS | GLU | ||||
4 | ALA | THR | GLY | LYS | GLY | VAL | LEU | PHE | GLU | ALA | ||||
5 | PHE | THR | GLY | LEU | LYS | THR | GLY | SER | LYS | VAL | ||||
6 | THR | SER | GLY | GLY | LEU | ALA | LEU | ARG | GLU | ALA | ||||
7 | LYS | VAL | GLN | ALA | ILE | VAL | GLU | THR | GLY | LYS | ||||
8 | PHE | LEU | LYS | ILE | ILE | GLU | GLU | GLU | ALA | LEU | ||||
9 | LYS | LEU | LYS | GLU | THR | GLY | ASN | SER | GLY | GLN | ||||
10 | PHE | LEU | ALA | MET | PHE | ASP | LEU | MET | LEU | GLU | ||||
11 | VAL | VAL | GLU | SER | LEU | GLU | ASP | VAL | GLY | ILE | ||||
12 | ILE | GLY | LEU | LYS | ALA | ARG | VAL | LEU | GLU | GLU | ||||
13 | SER | LYS | ASN | ASN | PRO | ILE | ASN | THR | ALA | GLU | ||||
14 | ARG | LEU | LEU | ALA | ALA | LYS | ALA | GLN | ILE | GLU | ||||
15 | ASN | GLN | LEU | LYS | VAL | VAL | LYS | GLU | LYS | GLN | ||||
16 | ASN | ILE | GLU | ASN | GLY | GLY | GLU | LYS | LYS | ASN | ||||
17 | ASN | LYS | SER | LYS | LYS | LYS | LYS |
Samples:
sample: DBPB, [U-100% 13C; U-100% 15N], 0.8 mM; sodium phosphate 50 mM; sodium chloride 150 mM; H2O 95%; D2O 5%
sample_conditions: ionic strength: 0.2 M; pH: 5.0; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample | isotropic | sample_conditions |
2D 1H-15N HSQC | sample | isotropic | sample_conditions |
3D 1H-13C NOESY aliphatic | sample | isotropic | sample_conditions |
3D HNCACB | sample | isotropic | sample_conditions |
3D CBCA(CO)NH | sample | isotropic | sample_conditions |
3D H(CCO)NH | sample | isotropic | sample_conditions |
3D C(CO)NH | sample | isotropic | sample_conditions |
3D 1H-13C NOESY | sample | isotropic | sample_conditions |
3D 1H-15N NOESY | sample | isotropic | sample_conditions |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - data analysis
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement
NMR spectrometers:
- Varian INOVA 800 MHz
- Bruker Avance 600 MHz
Related Database Links:
PDB | |
GB | AAC18819 AAC18824 AAC66244 AAC70021 AAC70023 |
REF | NP_045698 WP_010258353 WP_010890381 WP_012666179 WP_012672539 |
SP | C6C2E5 P0CL68 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts