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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/BMR15965
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
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Citation: Greenfield, Norma; Kotlyanskaya, Lucy; Hitchcock-DeGregori, Sarah. "Structure of the N Terminus of a Nonmuscle alpha-Tropomyosin in Complex with the C Terminus: Implications for Actin Binding" Biochemistry 48, 1272-1283 (2009).
PubMed: 19170537
Assembly members:
TM1b(1-19)Zip, polymer, 38 residues, 4331.956 Da.
TM9d(252-284), polymer, 37 residues, 4115.06 Da.
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: pPROEX HTa
Entity Sequences (FASTA):
TM1b(1-19)Zip: GAGSSSLEAVRRKIRSLQEQ
NYHLENEVARLKKLVGER
TM9d(252-284): GCGGSIDDLEEKVAHAKEEN
LSMHQMLDQTLLELNNM
Data type | Count |
13C chemical shifts | 123 |
15N chemical shifts | 41 |
1H chemical shifts | 273 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | entity_2 | 2 |
2 | entity_1 | 1 |
Entity 2, entity_2 37 residues - 4115.06 Da.
Residues 252-284 are encoded by exon 8 and 9d or rat alpha tropomyosin (TPM1 gene). Residues 248-251, GCGG were added to allow disulfide cross linking.
1 | GLY | CYS | GLY | GLY | SER | ILE | ASP | ASP | LEU | GLU | ||||
2 | GLU | LYS | VAL | ALA | HIS | ALA | LYS | GLU | GLU | ASN | ||||
3 | LEU | SER | MET | HIS | GLN | MET | LEU | ASP | GLN | THR | ||||
4 | LEU | LEU | GLU | LEU | ASN | ASN | MET |
Entity 1, entity_1 38 residues - 4331.956 Da.
Residue 0 is a glycine group replacing a native acetyl group residue 1-19 are the first 19 residues of a rat non-muscle low molecular weight tropomyosin encoded by exon 1b (TPM1 gene). 0 is a glycine residue that substitutes for the native acetyl group. Residues 20-37 are the last 18 residues of the yeast transcription factor GCN4.
1 | GLY | ALA | GLY | SER | SER | SER | LEU | GLU | ALA | VAL | ||||
2 | ARG | ARG | LYS | ILE | ARG | SER | LEU | GLN | GLU | GLN | ||||
3 | ASN | TYR | HIS | LEU | GLU | ASN | GLU | VAL | ALA | ARG | ||||
4 | LEU | LYS | LYS | LEU | VAL | GLY | GLU | ARG |
sample_1: TM1b(1-14)Zip, [U-99% 13C; U-99% 15N], 1 ± 0.1 mM; TM9d(252-284) 1 ± 0.1 mM; NaCl 100 mM; sodium phosphate 10 mM
sample_2: TM1b(1-19)Zip, [U-15N], 1 ± 0.1 mM; TM9d(252-284) 1 ± 0.1 mM; NaCl 100 mM; sodium phosphate 10 mM
sample_3: TM1b(1-19)Zip, [U-99% 13C; U-99% 15N], 0.5 ± 0.05 mM; TM1b(1-19)Zip 0.5 ± 0.05 mM; TM9d(252-284) 1 ± 0.1 mM; NaCl 100 mM; sodium phosphate 10 mM
sample_conditions_1: ionic strength: 0.14 M; pH: 6.4; pressure: 1 atm; temperature: 293 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
13C 15N X-filtered NOESY | sample_1 | isotropic | sample_conditions_1 |
13C 15N X-filtered NOESY | sample_3 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
AutoStruct v1.12, Huang, Tejero, Powers and Montelione - structure solution
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization
SPARKY v3.111, Goddard - peak picking
NMRPipe v1.1, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
PDB | |
DBJ | BAD92278 BAG11063 BAH12832 BAH13458 BAB22620 BAD18535 BAE88136 BAH13458 |
GB | AAA18098 AAA18099 AAA42253 AAH50473 AAH53545 AAA18097 AAA18098 AAA18099 AAA36771 AAA40483 |
REF | NP_001018008 NP_001029245 NP_001029246 NP_001029247 NP_001157724 NP_001018004 NP_001018006 NP_001018007 NP_001018020 NP_001029241 |
EMBL | CAA03930 CAA04505 CAA26258 CAA30930 CAB43309 |
PIR | A22165 |
PRF | 1105305A |
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