BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17508

Title: Solution NMR Structure of RRM domain of RNA-binding protein FUS from homo sapiens, Northeast Structural Genomics onsortium Target HR6430A

Authors: Liu, Gaohua; Xiao, Rong; Janjua, Haleema; Ciccosanti, Colleen; Wang, Huang; Lee, Hsiau-Wei; Acton, Thomas; Everett, John; Huang, Yuanpeng; Montelione, Gaetano

Citation: Liu, Gaohua; Xiao, Rong; Janjua, Haleema; Lee, Hsiau-Wei; Ciccosanti, Colleen; Acton, Thomas; Everett, John; Huang, Yuanpeng; Montelione, Gaetano. "Northeast Structural Genomics Consortium Target HR6430A"  To be published ., .-..

Assembly members:
HR6430A, polymer, 99 residues, 10970.295 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):
HR6430A: MGHHHHHHSHSDNNTIFVQG LGENVTIESVADYFKQIGII KTNKKTGQPMINLYTDRETG KLKGEATVSFDDPPSAKAAI DWFDGKEFSGNPIKVSFAT

Data sets:
Data typeCount
13C chemical shifts391
15N chemical shifts90
1H chemical shifts620
residual dipolar couplings69

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HR6430A1

Entities:

Entity 1, HR6430A 99 residues - 10970.295 Da.

1   METGLYHISHISHISHISHISHISSERHIS
2   SERASPASNASNTHRILEPHEVALGLNGLY
3   LEUGLYGLUASNVALTHRILEGLUSERVAL
4   ALAASPTYRPHELYSGLNILEGLYILEILE
5   LYSTHRASNLYSLYSTHRGLYGLNPROMET
6   ILEASNLEUTYRTHRASPARGGLUTHRGLY
7   LYSLEULYSGLYGLUALATHRVALSERPHE
8   ASPASPPROPROSERALALYSALAALAILE
9   ASPTRPPHEASPGLYLYSGLUPHESERGLY
10   ASNPROILELYSVALSERPHEALATHR

Samples:

sample_NC: HR6430A, [U-100% 13C; U-100% 15N], 0.83 mM; NaN3 0.02%; DTT 10 mM; CaCl2 5 mM; NaCl 100 mM; Proteinase Inhibitor 1; MES 20 mM; DSS 50 uM; H2O 95%; D2O 5%

sample_NC5: HR6430A, [U-5% 13C; U-100% 15N], 0.794 mM; NaN3 0.02%; DTT 10 mM; CaCl2 5 mM; NaCl 100 mM; Proteinase Inhibitor 1; MES 20 mM; DSS 50 uM; H2O 95%; D2O 5%

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_NCisotropicsample_conditions_1
2D 1H-13C HSQCsample_NC5isotropicsample_conditions_1
3D HNCOsample_NCisotropicsample_conditions_1
3D CBCA(CO)NHsample_NCisotropicsample_conditions_1
3D HNCACBsample_NCisotropicsample_conditions_1
3D 1H-13C arom NOESYsample_NCisotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYsample_NCisotropicsample_conditions_1
3D HCCH-TOCSYsample_NCisotropicsample_conditions_1
3D C(CO)NHsample_NCisotropicsample_conditions_1
3D HBHA(CO)NHsample_NCisotropicsample_conditions_1
2D 1H-15N HSQCsample_NC5isotropicsample_conditions_1

Software:

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

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

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

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

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

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

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

SPARKY, Goddard - data analysis

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

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
GB EDL17618 EDM17203 EGW03250 ELK10995
REF XP_004323165