BMRB Entry 16370

Title:
Solution NMR Structure of the Ig-like C2-type 2 Domain of Human Myotilin. Northeast Structural Genomics Target HR3158.
Deposition date:
2009-06-29
Original release date:
2009-06-29
Authors:
Rossi, Paolo; Shastry, Ritu; Ciccosanti, Colleen; Hamilton, Keith; Xiao, Rong; Acton, Thomas; G.V.T., Swapna; Nair, Rajeesh; Everett, John; Rost, Burkhard; Montelione, Gaetano
Citation:

Citation: Rossi, Paolo; Montelione, Gaetano. "Solution NMR Structure of the Ig-like C2-type 2 Domain of Human Myotilin. Northeast Structural Genomics Target HR3158."  .

Assembly members:

Assembly members:
Ig-like C2-type 2 Domain, polymer, 116 residues, 13338.323 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 14-15C

Data sets:
Data typeCount
13C chemical shifts458
15N chemical shifts113
1H chemical shifts726

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Ig-like C2-type 2 Domain1

Entities:

Entity 1, Ig-like C2-type 2 Domain 116 residues - 13338.323 Da.

1   METGLYHISHISHISHISHISHISSERHIS
2   GLUHISLYSARGALAPROMETPHEILETYR
3   LYSPROGLNSERLYSLYSVALLEUGLUGLY
4   ASPSERVALLYSLEUGLUCYSGLNILESER
5   ALAILEPROPROPROLYSLEUPHETRPLYS
6   ARGASNASNGLUMETVALGLNPHEASNTHR
7   ASPARGILESERLEUTYRGLNASPASNTHR
8   GLYARGVALTHRLEULEUILELYSASPVAL
9   ASNLYSLYSASPALAGLYTRPTYRTHRVAL
10   SERALAVALASNGLUALAGLYVALTHRTHR
11   CYSASNTHRARGLEUASPVALTHRALAARG
12   PROASNGLNTHRLEUPRO

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 0.87 mM; sodium chloride 200 mM; MES 20 mM; DSS 50 uM; DTT 10 mM; sodium azide 0.02%; Calcium Chloride 5 mM; H2O 90%; D2O 10%

sample_2: entity, [U-5% 13C], 0.68 mM; sodium chloride 200 mM; MES 20 mM; DSS 50 uM; DTT 10 mM; sodium azide 0.02%; Calcium Chloride 5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC hiressample_2isotropicsample_conditions_1
2D 1H-15N het_NOEsample_2isotropicsample_conditions_1
1D 15N_T1 seriessample_2isotropicsample_conditions_1
1D 15N_T2 seriessample_2isotropicsample_conditions_1

Software:

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

TOPSPIN v2.1, Bruker Biospin - collection

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

SPARKY v2.113, Goddard - data analysis

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

PINE, Bahrami, Markley, Assadi, and Eghbalnia - data analysis

Molmol, Koradi, Billeter and Wuthrich - structure visualization

PSVS v1.3, Bhattacharya and Montelione - structure validation

PyMol, DeLano Scientific - structure visualization

PDBStat v5.1, Tejero, Montelione - PDB processing

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB

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