BMRB Entry 27777

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27777

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Title:
1H-15N HSQC assignment for Insulin-like growth factor 2 mRNA-binding protein 1 domain KH1-2
Deposition date:
2019-02-07
Original release date:
2019-03-06
Authors:
Kelly, Geoff
Citation:

Citation: Dagil, Robert; Ball, Neil; Ogrodowicz, Roksana; Hobor, Fruzsina; Purkiss, Andrew; Kelly, Geoff; Martin, Stephen; Taylor, Ian; Ramos, Andres. "IMP1 KH1 and KH2 domains create a structural platform with unique RNA recognition and re-modelling properties."  Nucleic Acids Res. 47, 4334-4348 (2019).
PubMed: 30864660

Assembly members:

Assembly members:
IMP1_KH1-2, polymer, 179 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETM-30

Entity Sequences (FASTA):

Entity Sequences (FASTA):
IMP1_KH1-2: GAMVDIPLRLLVPTQYVGAI IGKEGATIRNITKQTQSKID VHRKENAGAAEKAISVHSTP EGCSSACKMILEIMHKEAKD TKTADEVPLKILAHNNFVGR LIGKEGRNLKKVEQDTETKI TISSLQDLTLYNPERTITVK GAIENCCRAEQEIMKKVREA YENDVAAMSLQSHLIPGLN

Data sets:
Data typeCount
15N chemical shifts142
1H chemical shifts142

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1domain KH1-21

Entities:

Entity 1, domain KH1-2 179 residues - Formula weight is not available

The deposited aa sequence for IMP1 KH1-2 contains the residues 194-369 from the full length construct (Uniprot Q9NZI8). The three first residues (191-193, residues GAM) are cloning artifacts from a TEV cleavage site.

1   GLYALAMETVALASPILEPROLEUARGLEU
2   LEUVALPROTHRGLNTYRVALGLYALAILE
3   ILEGLYLYSGLUGLYALATHRILEARGASN
4   ILETHRLYSGLNTHRGLNSERLYSILEASP
5   VALHISARGLYSGLUASNALAGLYALAALA
6   GLULYSALAILESERVALHISSERTHRPRO
7   GLUGLYCYSSERSERALACYSLYSMETILE
8   LEUGLUILEMETHISLYSGLUALALYSASP
9   THRLYSTHRALAASPGLUVALPROLEULYS
10   ILELEUALAHISASNASNPHEVALGLYARG
11   LEUILEGLYLYSGLUGLYARGASNLEULYS
12   LYSVALGLUGLNASPTHRGLUTHRLYSILE
13   THRILESERSERLEUGLNASPLEUTHRLEU
14   TYRASNPROGLUARGTHRILETHRVALLYS
15   GLYALAILEGLUASNCYSCYSARGALAGLU
16   GLNGLUILEMETLYSLYSVALARGGLUALA
17   TYRGLUASNASPVALALAALAMETSERLEU
18   GLNSERHISLEUILEPROGLYLEUASN

Samples:

sample_1: IMP1 KH1-2, [U-100% 13C; U-100% 15N], 560 uM; sodium phosphate 10 mM; sodium chloride 50 mM; TCEP 10 mM

sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

CCPN_Analysis v2, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 950 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz

Related Database Links:

UNP Q9NZI8
AlphaFold C9JT33

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