BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 19010

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19010

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Title: 1H, 15N and 13C backbone chemical shift assignment of the titin A59-A60 domain tandem   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 N; Kalverda, Arnout; Homans, Steve W; 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:
Titin_C1, polymer, 218 residues, 24209.5448 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):
Titin_C1: MGSSHHHHHHSSGLVPRGSH MPPPPNIVDVRHDSVSLTWT DPKKTGGSPITGYHLEFKER NSLLWKRANKTPIRMRDFKV TGLTEGLEYEFRVMAINLAG VGKPSLPSEPVVALDPIDPP GKPEVINITRNSVTLIWTEP KYDGGHKLTGYIVEKRDLPS KSWMKANHVNVPECAFTVTD LVEGGKYEFRIRAKNTAGAI SAPSESTETIICKDEYEA

Data sets:
Data typeCount
13C chemical shifts475
15N chemical shifts154
1H chemical shifts154

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Titin C11

Entities:

Entity 1, Titin C1 218 residues - 24209.5448 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METPROPROPROPROASNILEVALASPVAL
4   ARGHISASPSERVALSERLEUTHRTRPTHR
5   ASPPROLYSLYSTHRGLYGLYSERPROILE
6   THRGLYTYRHISLEUGLUPHELYSGLUARG
7   ASNSERLEULEUTRPLYSARGALAASNLYS
8   THRPROILEARGMETARGASPPHELYSVAL
9   THRGLYLEUTHRGLUGLYLEUGLUTYRGLU
10   PHEARGVALMETALAILEASNLEUALAGLY
11   VALGLYLYSPROSERLEUPROSERGLUPRO
12   VALVALALALEUASPPROILEASPPROPRO
13   GLYLYSPROGLUVALILEASNILETHRARG
14   ASNSERVALTHRLEUILETRPTHRGLUPRO
15   LYSTYRASPGLYGLYHISLYSLEUTHRGLY
16   TYRILEVALGLULYSARGASPLEUPROSER
17   LYSSERTRPMETLYSALAASNHISVALASN
18   VALPROGLUCYSALAPHETHRVALTHRASP
19   LEUVALGLUGLYGLYLYSTYRGLUPHEARG
20   ILEARGALALYSASNTHRALAGLYALAILE
21   SERALAPROSERGLUSERTHRGLUTHRILE
22   ILECYSLYSASPGLUTYRGLUALA

Samples:

TitinA59-A60: Titin_C1, [U-13C; U-15N; U-2H], 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/HMQCTitinA59-A60isotropicsample_condition_1
2D 1H-15N HSQC/HMQCTitinA59-A60isotropicsample_condition_1
3D HNCATitinA59-A60isotropicsample_condition_1
3D HNCACBTitinA59-A60isotropicsample_condition_1
(H[N[co[{CA|ca[C]}]]])TitinA59-A60isotropicsample_condition_1
(H[N[ca[CO]]])TitinA59-A60isotropicsample_condition_1
3D HNCATitinA59-A60isotropicsample_condition_1
3D HN(CO)CATitinA59-A60isotropicsample_condition_1
3D HNCACBTitinA59-A60isotropicsample_condition_1
(H[N[co[{CA|ca[C]}]]])TitinA59-A60isotropicsample_condition_1
3D HNCOTitinA59-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