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

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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
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:

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).
PubMed: 12534273

Assembly members:

Assembly members:
residues 251-284 of rat striated muscle tropomyosin, polymer, 37 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pSBET-HTb

Entity Sequences (FASTA):

Entity Sequences (FASTA):
residues 251-284 of rat striated muscle tropomyosin: GCGKSIDDLEDELYAQKLKY KAISEELDHALKDMTSI

Data sets:
Data typeCount
13C chemical shifts162
15N chemical shifts37
1H chemical shifts263
coupling constants26

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1tropomyosin peptide fragment, chain 11
2tropomyosin peptide fragment, chain 21

Entities:

Entity 1, tropomyosin peptide fragment, chain 1 37 residues - Formula weight is not available

1   GLYCYSGLYLYSSERILEASPASPLEUGLU
2   ASPGLULEUTYRALAGLNLYSLEULYSTYR
3   LYSALAILESERGLUGLULEUASPHISALA
4   LEULYSASPMETTHRSERILE

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:

NameSampleSample stateSample conditions
15N-1H HSQCnot availablenot availableCondition_1
(HA)(CA)CO(CA)NHnot availablenot availableCondition_1
HNC0not availablenot availableCondition_1
HN(CO)CAnot availablenot availableCondition_1
HNCAnot availablenot availableCondition_1
CBCANHnot availablenot availableCondition_1
CBCA(CO)NHnot availablenot availableCondition_1
HA(CA)NHnot availablenot availableCondition_1
HA(CA)(CO)CANHnot availablenot availableCondition_1
CCH-COSYnot availablenot availableCondition_1
HCCH-COSYnot availablenot availableCondition_1
2QF-COSYnot availablenot availableCondition_1
15N Edited NOESYnot availablenot availableCondition_1
13C Edited NOESYnot availablenot availableCondition_1
13C X-Filtered NOESYnot availablenot availableCondition_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 peaks
SPARKY: Backbone or all simulated peaks