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 16155

Title: Solution NMR structure of protein HS00059 from Homo Sapiens. Northeast Structural Genomics Consortium (NESG) target HT98A.

Deposition date: 2009-01-30 Original release date: 2009-03-12

Authors: Lemak, Alexander; Gutmanas, Aleksandras; Fares, Christophe; Quyang, Hui; Dhe-Paganon, Sirano; Montelione, Gaetano; Arrowsmith, Cheryl

Citation: Lemak, Alexander; Gutmanas, Aleksandras; Fares, Christophe; Quyang, Hui; Dhe-Paganon, Sirano; Montelione, Gaetano; Arrowsmith, Cheryl. "Solution NMR Structure of human protein HS00059"  Not known ., .-..

Assembly members:
hs00059, polymer, 112 residues, 14686.104 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):
hs00059: MHHHHHHSSGRENLYFQGNN EKVTLVRIADLENHNNDGGF WTVIDGKVYDIKDFQTQSLT ENSILAQFAGEDPVVALEAA LQFEDTRESMHAFCVGQYLE PDQEGVTIPDLG

Data typeCount
13C chemical shifts374
15N chemical shifts97
1H chemical shifts620

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hs000591

Entities:

Entity 1, hs00059 112 residues - 14686.104 Da.

1   METHISHISHISHISHISHISSERSERGLY
2   ARGGLUASNLEUTYRPHEGLNGLYASNASN
3   GLULYSVALTHRLEUVALARGILEALAASP
4   LEUGLUASNHISASNASNASPGLYGLYPHE
5   TRPTHRVALILEASPGLYLYSVALTYRASP
6   ILELYSASPPHEGLNTHRGLNSERLEUTHR
7   GLUASNSERILELEUALAGLNPHEALAGLY
8   GLUASPPROVALVALALALEUGLUALAALA
9   LEUGLNPHEGLUASPTHRARGGLUSERMET
10   HISALAPHECYSVALGLYGLNTYRLEUGLU
11   PROASPGLNGLUGLYVALTHRILEPROASP
12   LEUGLY

Samples:

sample_1: hs00059, [U-13C; U-15N], 0.5 mM; TRIS 10 mM; sodium chloride 300 mM; ZnSO4 10 uM; DTT 10 mM; NaN3 0.01%; benzamidine 10 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 300 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C_arom NOESYsample_1isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - peak picking

FMC, Lemak, Steren, Llinas, Arrowsmith - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - data analysis

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB

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