BMRB Entry 30469

Title:
NMR structure of the second qRRM2 domain of human hnRNP H   PubMed: 30122033
Deposition date:
2018-05-16
Original release date:
2018-08-31
Authors:
Srinivasa, R.
Citation:

Citation: Penumutchu, Srinivasa; Chiu, Liang-Yuan; Meagher, Jennifer; Hansen, Alexandar; Stuckey, Jeanne; Tolbert, Blanton. "Differential Conformational Dynamics Encoded by the Linker between Quasi RNA Recognition Motifs of Heterogeneous Nuclear Ribonucleoprotein H."  J. Am. Chem. Soc. 140, 11661-11673 (2018).

Assembly members:

Assembly members:
qRRM2 domain of Heterogeneous nuclear ribonucleoprotein H2, polymer, 105 residues, 11791.324 Da.

Natural source:

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

Experimental source:

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):

Entity Sequences (FASTA):
qRRM2 domain of Heterogeneous nuclear ribonucleoprotein H2: SNAMDWVLKHTGPNSPDTAN DGFVRLRGLPFGCSKEEIVQ FFSGLEIVPNGITLPVDFQG RSTGEAFVQFASQEIAEKAL KKHKERIGHRYIEIFKSSRA EVRTH

Data sets:
Data typeCount
13C chemical shifts380
15N chemical shifts97
1H chemical shifts617

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 105 residues - 11791.324 Da.

1   SERASNALAMETASPTRPVALLEULYSHIS
2   THRGLYPROASNSERPROASPTHRALAASN
3   ASPGLYPHEVALARGLEUARGGLYLEUPRO
4   PHEGLYCYSSERLYSGLUGLUILEVALGLN
5   PHEPHESERGLYLEUGLUILEVALPROASN
6   GLYILETHRLEUPROVALASPPHEGLNGLY
7   ARGSERTHRGLYGLUALAPHEVALGLNPHE
8   ALASERGLNGLUILEALAGLULYSALALEU
9   LYSLYSHISLYSGLUARGILEGLYHISARG
10   TYRILEGLUILEPHELYSSERSERARGALA
11   GLUVALARGTHRHIS

Samples:

sample_1: qRRM2 domain of hnRNP H, C13_N15, 1.5 ± 0.1 mM

sample_conditions_1: ionic strength: 40 mM; pH: 6.2; pressure: 760 mmHg; temperature: 305 K

Experiments:

NameSampleSample stateSample conditions
1H-15N HSQCsample_1isotropicsample_conditions_1
HNCAsample_1isotropicsample_conditions_1
HN(CO)CAsample_1isotropicsample_conditions_1
HNCACBsample_1isotropicsample_conditions_1
CBCA(CO)NHsample_1isotropicsample_conditions_1
HNCOsample_1isotropicsample_conditions_1
HN(CA)COsample_1isotropicsample_conditions_1
HBHA(CO)NHsample_1isotropicsample_conditions_1
(H)CCCH-TOCSYsample_1isotropicsample_conditions_1
H(C)CCH-TOCSYsample_1isotropicsample_conditions_1
3D NOESY-(13C-1H)-HSQCsample_1isotropicsample_conditions_1
3D NOESY-(15N-1H)-HSQCsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

SPARKY, Goddard - chemical shift assignment, peak picking

ARIA, Linge, O'Donoghue and Nilges - structure calculation

NMR spectrometers:

  • Bruker AvanceIII 900 MHz
  • Bruker AvanceIII 800 MHz

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