BMRB Entry 25494

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25494

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Title:
First and second KH domains of hnRNP E1
Deposition date:
2015-02-19
Original release date:
2016-06-30
Authors:
Li, Yang; Hennig, Mirko
Citation:

Citation: Li, Yang; Mirko, Hennig. "(1)H, (15)N and (13)C backbone resonance assignments of the N-terminal, tandem KH domains of human hnRNP E1"  Biomol NMR Assign. 9, 431-434 (2015).
PubMed: 26143480

Assembly members:

Assembly members:
First_and_Second_KH_domains_of_hnRNP_E1, polymer, 167 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-23a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
First_and_Second_KH_domains_of_hnRNP_E1: MLTIRLLMHGKEVGSIIGKK GESVKRIREESGARINISEG NSPERIITLTGPTNAIFKAF AMIIDKLEEDINSSMTNSTA ASRPPVTLRLVVPATQAGSL IGKGGAKIKEIRESTGAQVQ VAGDMLPNSTERAITIAGVP QSVTEAVKQISLVMLETLWL EHHHHHH

Data sets:
Data typeCount
13C chemical shifts421
15N chemical shifts148
1H chemical shifts555

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 167 residues - Formula weight is not available

1   METLEUTHRILEARGLEULEUMETHISGLY
2   LYSGLUVALGLYSERILEILEGLYLYSLYS
3   GLYGLUSERVALLYSARGILEARGGLUGLU
4   SERGLYALAARGILEASNILESERGLUGLY
5   ASNSERPROGLUARGILEILETHRLEUTHR
6   GLYPROTHRASNALAILEPHELYSALAPHE
7   ALAMETILEILEASPLYSLEUGLUGLUASP
8   ILEASNSERSERMETTHRASNSERTHRALA
9   ALASERARGPROPROVALTHRLEUARGLEU
10   VALVALPROALATHRGLNALAGLYSERLEU
11   ILEGLYLYSGLYGLYALALYSILELYSGLU
12   ILEARGGLUSERTHRGLYALAGLNVALGLN
13   VALALAGLYASPMETLEUPROASNSERTHR
14   GLUARGALAILETHRILEALAGLYVALPRO
15   GLNSERVALTHRGLUALAVALLYSGLNILE
16   SERLEUVALMETLEUGLUTHRLEUTRPLEU
17   GLUHISHISHISHISHISHIS

Samples:

sample_1: entity, [U-13C; U-15N], 300 uM; H2O 90%; D2O 10%

sample_2: entity, [U-15N], 300 uM; H2O 90%; D2O 10%

sample_3: entity, [U-13C; U-15N], 300 uM; D2O 100%

sample_conditions_1: ionic strength: 800 mM; pH: 5.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1

Software:

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

CCPNMR, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

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