BMRB Entry 27934

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27934

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Title:
Backbone 1H, 13C and 15N resonance assignments for IMP2 KH34
Deposition date:
2019-06-02
Original release date:
2019-11-08
Authors:
Biswas, Jeetayu; Patel, Vivek; Bhaskar, Varun; Chao, Jeffrey; Eliscovich, Carolina; Singer, Robert
Citation:

Citation: Biswas, Jeetayu; Patel, Vivek; Bhaskar, Varun; Chao, Jeffrey; Singer, Robert; Eliscovich, Carolina. "The structural basis for RNA selectivity by the IMP family of RNA binding proteins"  Nat. Comm. 10, 4440-4440 (2019).
PubMed: 31570709

Assembly members:

Assembly members:
IMP2_KH34, 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: pET22-HT

Entity Sequences (FASTA):

Entity Sequences (FASTA):
IMP2_KH34: HHHHHHGENLYFQGGSEQEI VNLFIPTQAVGAIIGKKGAH IKQLARFAGASIKIAPAEGP DVSERMVIITGPPEAQFKAQ GRIFGKLKEENFFNPKEEVK LEAHIRVPSSTAGRVIGKGG KTVNELQNLTSAEVIVPRDQ TPDENEEVIVRIIGHFFASQ TAQRKIREIVQQVKQQEQK

Data sets:
Data typeCount
13C chemical shifts334
15N chemical shifts153
1H chemical shifts153

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1KH Domains 3 and 41

Entities:

Entity 1, KH Domains 3 and 4 179 residues - Formula weight is not available

Residues 1-15 represent a protein purification tag (6X HIS) and TEV cleavage sequence.

1   HISHISHISHISHISHISGLYGLUASNLEU
2   TYRPHEGLNGLYGLYSERGLUGLNGLUILE
3   VALASNLEUPHEILEPROTHRGLNALAVAL
4   GLYALAILEILEGLYLYSLYSGLYALAHIS
5   ILELYSGLNLEUALAARGPHEALAGLYALA
6   SERILELYSILEALAPROALAGLUGLYPRO
7   ASPVALSERGLUARGMETVALILEILETHR
8   GLYPROPROGLUALAGLNPHELYSALAGLN
9   GLYARGILEPHEGLYLYSLEULYSGLUGLU
10   ASNPHEPHEASNPROLYSGLUGLUVALLYS
11   LEUGLUALAHISILEARGVALPROSERSER
12   THRALAGLYARGVALILEGLYLYSGLYGLY
13   LYSTHRVALASNGLULEUGLNASNLEUTHR
14   SERALAGLUVALILEVALPROARGASPGLN
15   THRPROASPGLUASNGLUGLUVALILEVAL
16   ARGILEILEGLYHISPHEPHEALASERGLN
17   THRALAGLNARGLYSILEARGGLUILEVAL
18   GLNGLNVALLYSGLNGLNGLUGLNLYS

Samples:

sample_1: IMP2 KH34, [U-13C; U-15N; U-2H], 200 uM

sample_conditions_1: ionic strength: 150 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1

Software:

VNMRJ, Varian - collection

TOPSPIN, Bruker Biospin - collection

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

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

CcpNMR, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker DRX 600 MHz
  • 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