BMRB Entry 17410

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17410

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Title:
1H, 15N and 13C backbone chemical shift assignment of the titin A67-A68 domain tandem
Deposition date:
2011-01-14
Original release date:
2011-08-17
Authors:
Czajlik, Andras; Thompson, Gary; Khan, Ghulam N; Kalverda, Arnout; Homans, Steve W; Trinick, John
Citation:

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 the titin A67-A68 domain tandem."  Biomol. NMR Assignments 6, 39-41 (2012).
PubMed: 21779926

Assembly members:

Assembly members:
Construct6, polymer, 215 residues, 23696.0575 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET 15b_A170

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Construct6: MGSSHHHHHHSSGLVPRGSH MPSPPDSLNIMDITKSTVSL AWPKPKHDGGSKITGYVIEA QRKGSDQWTHITTVKGLECV VRNLTEGEEYTFQVMAVNSA GRSAPRESRPVIVKEQTMLP ELDLRGIYQKLVIAKAGDNI KVEIPVLGRPKPTVTWKKGD QILKQTQRVNFETTATSTIL NINECVRSDSGPYPLTARNI VGEVGDVITIQVHDI

Data sets:
Data typeCount
13C chemical shifts550
15N chemical shifts180
1H chemical shifts180

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Construct61

Entities:

Entity 1, Construct6 215 residues - 23696.0575 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METPROSERPROPROASPSERLEUASNILE
4   METASPILETHRLYSSERTHRVALSERLEU
5   ALATRPPROLYSPROLYSHISASPGLYGLY
6   SERLYSILETHRGLYTYRVALILEGLUALA
7   GLNARGLYSGLYSERASPGLNTRPTHRHIS
8   ILETHRTHRVALLYSGLYLEUGLUCYSVAL
9   VALARGASNLEUTHRGLUGLYGLUGLUTYR
10   THRPHEGLNVALMETALAVALASNSERALA
11   GLYARGSERALAPROARGGLUSERARGPRO
12   VALILEVALLYSGLUGLNTHRMETLEUPRO
13   GLULEUASPLEUARGGLYILETYRGLNLYS
14   LEUVALILEALALYSALAGLYASPASNILE
15   LYSVALGLUILEPROVALLEUGLYARGPRO
16   LYSPROTHRVALTHRTRPLYSLYSGLYASP
17   GLNILELEULYSGLNTHRGLNARGVALASN
18   PHEGLUTHRTHRALATHRSERTHRILELEU
19   ASNILEASNGLUCYSVALARGSERASPSER
20   GLYPROTYRPROLEUTHRALAARGASNILE
21   VALGLYGLUVALGLYASPVALILETHRILE
22   GLNVALHISASPILE

Samples:

TitinA67-A68: Construct6, [U-13C; U-15N; U-2H], 1.00 ± 0.0002 mM; bis-tris 200.00 ± 0.001 mM; MES 200.00 ± 0.001 mM; sodium azide 1.00 ± 0.0001 mM; complete protease inhibitor 1.00 ± 0.0001 mM; dss, [U-100% 2H], 0.01 ± 1e-06 mM

MES-Bis-Tris: pH: 6.500; pressure: 1.000 atm; temperature: 293.000 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC/HMQCTitinA67-A68isotropicMES-Bis-Tris
3D HNCATitinA67-A68isotropicMES-Bis-Tris
3D HNCACBTitinA67-A68isotropicMES-Bis-Tris
3D HN(CO)CATitinA67-A68isotropicMES-Bis-Tris
3D HNCOTitinA67-A68isotropicMES-Bis-Tris
Expt_10 (H[N[ca[CO]]])TitinA67-A68isotropicMES-Bis-Tris
Expt_11 (H[N[co[{CA|ca[C]}]]])TitinA67-A68isotropicMES-Bis-Tris
3D HNCACBTitinA67-A68isotropicMES-Bis-Tris
2D 1H-15N HSQC/HMQCTitinA67-A68isotropicMES-Bis-Tris

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

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