BMRB Entry 18879
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18879
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Title: SP-B C-terminal (residues 59-80) peptide in DPC micelles
Deposition date: 2012-12-06 Original release date: 2013-12-16
Authors: Kuznetsova, Anna; Vanni, Julieann; Long, Joanna
Citation: Kuznetsova, Anna; Vanni, Julieann; Long, Joanna. "Solution NMR structures of the C-terminal segment of surfactant protein B (residues 59-80) in DPC detergent micelles and methanol." Biochemistry ., .-..
Assembly members:
entity, polymer, 22 residues, 2500.072 Da.
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):
entity: DTLLGRILPQLVCRLVLRCS
ID
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 24 |
| 1H chemical shifts | 173 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SP-B | 1 |
Entities:
Entity 1, SP-B 22 residues - 2500.072 Da.
there is homoserine lactone residue (HSL) at the end of the sequence after D80 that is left due to cyanogen bromide cleavage of the peptide from fusion construct at the methionines before D59 and after D80
| 1 | ASP | THR | LEU | LEU | GLY | ARG | ILE | LEU | PRO | GLN | ||||
| 2 | LEU | VAL | CYS | ARG | LEU | VAL | LEU | ARG | CYS | SER | ||||
| 3 | ILE | ASP |
Samples:
SP-B_residues_59-80_in_DPC_micelles: entity, [U-100% 15N], 1.2 mM; D2O, [U-100% 2H], 5%; DPC, [U-100% 2H], 80 mM; TSP 1 mM; sodium phosphate 50 mM; H2O 95%
315K: ionic strength: 130 mM; pH: 4.5; pressure: 1 atm; temperature: 315 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | SP-B_residues_59-80_in_DPC_micelles | isotropic | 315K |
| 2D 1H-1H TOCSY | SP-B_residues_59-80_in_DPC_micelles | isotropic | 315K |
| 2D 1H-1H NOESY | SP-B_residues_59-80_in_DPC_micelles | isotropic | 315K |
| 3D 1H-15N TOCSY | SP-B_residues_59-80_in_DPC_micelles | isotropic | 315K |
| 3D 1H-15N NOESY | SP-B_residues_59-80_in_DPC_micelles | isotropic | 315K |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis, processing
SPARKY, Goddard - chemical shift assignment, data analysis, peak picking
X-PLOR NIH v2.32, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution
TOPSPIN, Bruker Biospin - collection, data analysis
MolProbity, Ian W. Davis, Vincent B. Chen, Robert M. Immormino et. al - evaluation of structure refinement, structure evaluation
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
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SPARKY: Backbone
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