BMRB Entry 5610
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR5610
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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Title: The Structure of the Carboxyl Terminus of Striated alpha-Tropomyosin in Solution Reveals an Unusual Parallel Arrangement of Interacting alpha-Helices PubMed: 12534273
Deposition date: 2002-12-06 Original release date: 2006-04-28
Authors: Greenfield, Norma; Swapna, G.V.T.; Huang, Yuanpeng; Palm, Thomas; Graboski, Janet; Montelione, Gaetano; Hitchcock-DeGregori, Sarah
Citation: Greenfield, Norma; Swapna, G.V.T.; Huang, Yuanpeng; Palm, Thomas; Graboski, S.; Montelione, Gaetano; Hitchcock-DeGregori, Sarah. "The Structure of the Carboxyl Terminus of Striated alpha-Tropomyosin in Solution Reveals an Unusual Parallel Arrangement of Interacting alpha-Helices" Biochemistry 42, 614-619 (2003).
Assembly members:
residues 251-284 of rat striated muscle tropomyosin, polymer, 37 residues, Formula weight is not available
Natural source: Common Name: Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pSBET-HTb
Entity Sequences (FASTA):
residues 251-284 of rat striated muscle tropomyosin: GCGKSIDDLEDELYAQKLKY
KAISEELDHALKDMTSI
- assigned_chemical_shifts
- coupling_constants
| Data type | Count |
| 13C chemical shifts | 162 |
| 15N chemical shifts | 37 |
| 1H chemical shifts | 263 |
| coupling constants | 26 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | tropomyosin peptide fragment, chain 1 | 1 |
| 2 | tropomyosin peptide fragment, chain 2 | 1 |
Entities:
Entity 1, tropomyosin peptide fragment, chain 1 37 residues - Formula weight is not available
| 1 | GLY | CYS | GLY | LYS | SER | ILE | ASP | ASP | LEU | GLU | ||||
| 2 | ASP | GLU | LEU | TYR | ALA | GLN | LYS | LEU | LYS | TYR | ||||
| 3 | LYS | ALA | ILE | SER | GLU | GLU | LEU | ASP | HIS | ALA | ||||
| 4 | LEU | LYS | ASP | MET | THR | SER | ILE |
Samples:
Sample_1: residues 251-284 of rat striated muscle tropomyosin, [U-98% 15N], 0.4 – 1.2 mM; NaCl 100 mM; Na phosphate 10 mM
Sample_2: residues 251-284 of rat striated muscle tropomyosin, [U-99% 13C; U-98% 15N], 0.4 – 1.2 mM
Sample_3: residues 251-284 of rat striated muscle tropomyosin, [U-98% 15N; U-99% 13C], 0.4 mM; residues 251-284 of rat striated muscle tropomyosin 0.4 mM
Sample_4: residues 251-284 of rat striated muscle tropomyosin 0.8 mM
Condition_1: ionic strength: 0.12 M; pH: 6.5; temperature: 183 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 15N-1H HSQC | not available | not available | Condition_1 |
| (HA)(CA)CO(CA)NH | not available | not available | Condition_1 |
| HNC0 | not available | not available | Condition_1 |
| HN(CO)CA | not available | not available | Condition_1 |
| HNCA | not available | not available | Condition_1 |
| CBCANH | not available | not available | Condition_1 |
| CBCA(CO)NH | not available | not available | Condition_1 |
| HA(CA)NH | not available | not available | Condition_1 |
| HA(CA)(CO)CANH | not available | not available | Condition_1 |
| CCH-COSY | not available | not available | Condition_1 |
| HCCH-COSY | not available | not available | Condition_1 |
| 2QF-COSY | not available | not available | Condition_1 |
| 15N Edited NOESY | not available | not available | Condition_1 |
| 13C Edited NOESY | not available | not available | Condition_1 |
| 13C X-Filtered NOESY | not available | not available | Condition_1 |
Software:
VNMR - data collection, processing
AutoStruct - NOE assignments, structural calculations
DYANA - structural calculations
SPARKY - peak selection, spectra alignments
NMR spectrometers:
- Varian INOVA 500 MHz
- Varian INOVA 600 MHz
Related Database Links:
| BMRB | 7080 |
| PDB | |
| DBJ | BAB21978 BAC36973 BAC85248 BAD86590 BAE40499 |
| EMBL | CAA26259 CAA28393 CAA34344 CAA41056 CAA43577 |
| GB | AAA18096 AAA21801 AAA21803 AAA48577 AAA48610 |
| PRF | 1105305B |
| REF | NP_001013608 NP_001018005 NP_001029247 NP_001090952 NP_001099158 |
| SP | P04268 P04692 P09493 P13105 P42639 |
| AlphaFold | P04268 P04692 P09493 P13105 P42639 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts