BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15965

Title: Structural Transitions of the N Terminus of a Short Non-Muscle Tropomyosin upon Binding to the C Terminus in Solution   PubMed: 19170537

Deposition date: 2008-09-25 Original release date: 2009-04-02

Authors: Greenfield, Norma; Kotylanskaya, Lucy; Hitchcock-DeGregori, Sarah

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).

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 sets:
Data typeCount
13C chemical shifts123
15N chemical shifts41
1H chemical shifts273

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_22
2entity_11

Entities:

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   GLYCYSGLYGLYSERILEASPASPLEUGLU
2   GLULYSVALALAHISALALYSGLUGLUASN
3   LEUSERMETHISGLNMETLEUASPGLNTHR
4   LEULEUGLULEUASNASNMET

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   GLYALAGLYSERSERSERLEUGLUALAVAL
2   ARGARGLYSILEARGSERLEUGLNGLUGLN
3   ASNTYRHISLEUGLUASNGLUVALALAARG
4   LEULYSLYSLEUVALGLYGLUARG

Samples:

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
13C 15N X-filtered NOESYsample_1isotropicsample_conditions_1
13C 15N X-filtered NOESYsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Biospin 800 MHz

Related Database Links:

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

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts