BMRB Entry 18563

Title:
Solution NMR Structure of Ig like domain (805-892) of Obscurin-like protein 1 from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR8578K
Deposition date:
2012-06-30
Original release date:
2013-01-03
Authors:
Pulavarti, Surya VSRK; Eletsky, Alex; Sukumaran, Dinesh; Lee, Dan; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Pederson, Kari; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas
Citation:

Citation: Pulavarti, Surya VSRK; Eletsky, Alex; Sukumaran, Dinesh; Lee, Dan; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Pederson, Kari; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of Ig like domain (805-892) of Obscurin-like protein 1 from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR8578K"  To be published ., .-..

Assembly members:

Assembly members:
HR8578K, polymer, 91 residues, 10165.419 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15Avi6HT_NESG

Data sets:
Data typeCount
1H chemical shifts612
13C chemical shifts393
15N chemical shifts92

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HR8578K1

Entities:

Entity 1, HR8578K 91 residues - 10165.419 Da.

1   SERHISMETPROVALHISILEVALASPPRO
2   ARGGLUHISVALPHEVALHISALAILETHR
3   SERGLUCYSVALMETLEUALACYSGLUVAL
4   ASPARGGLUASPALAPROVALARGTRPTYR
5   LYSASPGLYGLNGLUVALGLUGLUSERASP
6   PHEVALVALLEUGLUASNGLUGLYPROHIS
7   ARGARGLEUVALLEUPROALATHRGLNPRO
8   SERASPGLYGLYGLUPHEGLNCYSVALALA
9   GLYASPGLUCYSALATYRPHETHRVALTHR
10   ILE

Samples:

sample_1: HR8578K.009, [U-100% 13C; U-100% 15N], 1.0 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM; H2O 90%

sample_2: HR8578K.010, [U-5% 13C; U-100% 15N], 1.0 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM; H2O 90%

sample_3: HR8578K.010, [U-5% 13C; U-100% 15N], 0.6 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM; PF1 Phage 12.5 mg/mL; H2O 80%

sample_4: HR8578K.010, [U-5% 13C; U-100% 15N], 0.6 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM; PEG 4%; H2O 80%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C (CT-27 ms) HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-13C (CT-28 ms) HSQCsample_2isotropicsample_conditions_1
2D 1H-13C (CT-56 ms) HSQCsample_1isotropicsample_conditions_1
2D 1H-13C (CT-42 ms) HSQCsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-COSY (Aliphatic)sample_1isotropicsample_conditions_1
3D HCCH-COSY (Aromatic)sample_1isotropicsample_conditions_1
2D 1H-15N HSQC J-modsample_3anisotropicsample_conditions_1
2D 1H-15N HSQC J-modsample_4anisotropicsample_conditions_1
2D 1H-15N HSQC J-modsample_2isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization

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

AutoStructure v2.1, Huang, Tejero, Powers and Montelione - data analysis,refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

CARA v1.8.4, Keller and Wuthrich - peak picking, data analysis

XEASY, Bartels et al. - data analysis,peak picking,chemical shift assignment

CSI, Wishart, D.S. and B.D. Sykes. - data analysis

VNMRJ, Varian - collection

PROSA, Guntert - processing

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PALES, PALES (Zweckstetter, Bax) - geometry optimization

PSVS, Bhattacharya, Montelione - structure validation

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz

Related Database Links:

UNP O75147
NCBI 23363
PDB
AlphaFold S4R3M6

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