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 19011

Title: 1H, 15N and 13C backbone chemical shift assignment of the titin A60 domain   PubMed: 24469996

Deposition date: 2013-02-06 Original release date: 2014-02-13

Authors: Czajlik, Andras; Thompson, Gary; Khan, Ghulam N; Kalverda, Arnout; Homans, Steve W; Trinick, John

Citation: Czajlik, Andras; Thompson, Gary; Khan, Ghulam; Kalverda, Arnout; Homans, Steve; Trinick, John. "(1)H, (15)N and (13)C backbone chemical shift assignment of titin domains A59-A60 and A60 alone."  Biomol. NMR Assignments ., .-. (2014).

Assembly members:
C1CT, polymer, 134 residues, 14951.7543 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
C1CT: MGHHHHHHSSGHENLYFQGT LDPIDIDPPGKPEVINITRN SVTLIWTEPKYDGGHKLTGY IVEKRDLPSKSWMKANHVNV PECAFTVTDLVEGGKYEFRI RAKNTAGAISAPSESTETII CKDEYEAPTIVLAE

Data sets:
Data typeCount
13C chemical shifts331
15N chemical shifts111
1H chemical shifts111

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1C1CT1

Entities:

Entity 1, C1CT 134 residues - 14951.7543 Da.

1   METGLYHISHISHISHISHISHISSERSER
2   GLYHISGLUASNLEUTYRPHEGLNGLYTHR
3   LEUASPPROILEASPILEASPPROPROGLY
4   LYSPROGLUVALILEASNILETHRARGASN
5   SERVALTHRLEUILETRPTHRGLUPROLYS
6   TYRASPGLYGLYHISLYSLEUTHRGLYTYR
7   ILEVALGLULYSARGASPLEUPROSERLYS
8   SERTRPMETLYSALAASNHISVALASNVAL
9   PROGLUCYSALAPHETHRVALTHRASPLEU
10   VALGLUGLYGLYLYSTYRGLUPHEARGILE
11   ARGALALYSASNTHRALAGLYALAILESER
12   ALAPROSERGLUSERTHRGLUTHRILEILE
13   CYSLYSASPGLUTYRGLUALAPROTHRILE
14   VALLEUALAGLU

Samples:

Titin_A60: C1CT, [U-100% 13C; U-100% 15N], 1.0 ± 0.0001 mM; NaCl 500.0 ± 0.005 mM; MES 50.0 ± 0.001 mM; DTT 10.0 ± 0.0001 mM; sodium azide 1.0 ± 0.0001 mM; complete protease inhibitor 1.0 ± 0.0001 mM; DSS 10.0 ± 1e-06 mM

sample_condition_1: pH: 6.500; pressure: 1.000 atm; temperature: 293.000 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC/HMQCTitin_A60isotropicsample_condition_1
3D HNCATitin_A60isotropicsample_condition_1
3D H[N[co[{CA|ca[C]}]]]Titin_A60isotropicsample_condition_1
3D H[N[ca[CO]]]Titin_A60isotropicsample_condition_1
3D HNCOTitin_A60isotropicsample_condition_1

Software:

ANALYSIS v1.0, CCPN - peak assignment

ANALYSIS v2.1, CCPN - peak assignment

CcpNmr_Entry_completion_Interface v2.1, PDBe & CCPN - data deposition

NMRPipe v5.5, NMRPipe - data processing

NMR spectrometers:

  • Varian UnityInova 750 MHz
  • Varian UnityInova 600 MHz

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