BMRB Entry 25645
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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/BMR25645
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Title: Chemical Shift Assignments and Structure of HSPB1_ACD PubMed: 26243512
Deposition date: 2015-06-03 Original release date: 2015-08-17
Authors: Rajagopal, Ponni; Shi, Lei; Klevit, Rachel
Citation: Rajagopal, Ponni; Liu, Ying; Shi, Lei; Clouser, Amanda; Klevit, Rachel. "Structure of the alpha-crystallin domain from the redox-sensitive chaperone, HSPB1" J. Biomol. NMR 63, 223-228 (2015).
Assembly members:
entity, polymer, 98 residues, 10894.250 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: MQLSSGVSEIRHTADRWRVS
LDVNHFAPDELTVKTKDGVV
EITGKHEERQDEHGYISRCF
TRKYTLPPGVDPTQVSSSLS
PEGTLTVEAPMPKLATQS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 176 |
| 15N chemical shifts | 81 |
| 1H chemical shifts | 233 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 1 |
Entities:
Entity 1, entity_1 98 residues - 10894.250 Da.
| 1 | MET | GLN | LEU | SER | SER | GLY | VAL | SER | GLU | ILE | ||||
| 2 | ARG | HIS | THR | ALA | ASP | ARG | TRP | ARG | VAL | SER | ||||
| 3 | LEU | ASP | VAL | ASN | HIS | PHE | ALA | PRO | ASP | GLU | ||||
| 4 | LEU | THR | VAL | LYS | THR | LYS | ASP | GLY | VAL | VAL | ||||
| 5 | GLU | ILE | THR | GLY | LYS | HIS | GLU | GLU | ARG | GLN | ||||
| 6 | ASP | GLU | HIS | GLY | TYR | ILE | SER | ARG | CYS | PHE | ||||
| 7 | THR | ARG | LYS | TYR | THR | LEU | PRO | PRO | GLY | VAL | ||||
| 8 | ASP | PRO | THR | GLN | VAL | SER | SER | SER | LEU | SER | ||||
| 9 | PRO | GLU | GLY | THR | LEU | THR | VAL | GLU | ALA | PRO | ||||
| 10 | MET | PRO | LYS | LEU | ALA | THR | GLN | SER |
Samples:
sample_1: entity, [U-100% 13C; U-100% 15N], 1.0 mM; sodium phosphate 50 mM; sodium chloride 100 mM; PMSF 1 mM; EDTA 0.1 mM; D2O 10%; H2O 90%
sample_2: entity, [U-100% 13C; U-100% 15N; U-80% 2H], 1.0 mM; sodium phosphate 50 mM; sodium chloride 100 mM; PMSF 1 mM; EDTA 0.1 mM; D2O 10%; H2O 90%
sample_3: entity, [U-100% 13C; U-100% 15N; U-50% 2H], 1.0 mM; sodium phosphate 50 mM; sodium chloride 100 mM; PMSF 1 mM; EDTA 0.1 mM; D2O 10%; H2O 90%
sample_conditions_1: ionic strength: 100 mM; pH: 7.5; pressure: 1 atm; temperature: 295 K
sample_conditions_2: ionic strength: 100 mM; pH: 7.5; pressure: 1 atm; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | 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_2 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(COCA)CB | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_3 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_2 |
| 2D 1H-15N HSQC | sample_1 | anisotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking
CS-Rosetta, Shen, Vernon, Baker and Bax - structure solution
CcpNMr, CCPN - data analysis
X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution
PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift calculation
NMR spectrometers:
- Varian INOVA 900 MHz
- Bruker Avance 600 MHz
- Bruker Avance 500 MHz
- Varian INOVA 600 MHz
- Varian INOVA 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts