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 15049

Title: Resonance assignment of the first and second KH (hnRNP-K homology) domains of human poly(C)-binding protein-2 (PCBP2)   PubMed: 17479348

Authors: Du, Zhihua; Fenn, Sebastian; James, Thomas

Citation: Du, Zhihua; Fenn, Sebastian; James, Thomas. "Resonance assignment of the first and second KH (hnRNP-K homology) domains of human poly(C)-binding protein-2 (PCBP2)"  J. Biomol. NMR 38, 197-197 (2007).

Assembly members:
PCBP2_KH1_and_KH2_domains, polymer, 168 residues, Formula weight is not available

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):
PCBP2_KH1_and_KH2_domains: MKHHHHHHKNVTLTIRLLMH GKEVGSIIGKKGESVKKMRE ESGARINISEGNCPERIITL AGPTNAIFKAFAMIIGKLEE DISSSMTNSTAASRPPVTLR LVVPASQCGSLIGKGGCKIK EIRESTGAQVQVAGDMLPNS TERAITIAGIPQSIIECVKQ ICVVMLET

Data sets:
  • assigned_chemical_shifts
Data typeCount
13C chemical shifts626
15N chemical shifts172
1H chemical shifts1126

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Kh1+Kh21

Entities:

Entity 1, Kh1+Kh2 168 residues - Formula weight is not available

residues M2-K10 is a non-native tag

1   METLYSHISHISHISHISHISHISLYSASN
2   VALTHRLEUTHRILEARGLEULEUMETHIS
3   GLYLYSGLUVALGLYSERILEILEGLYLYS
4   LYSGLYGLUSERVALLYSLYSMETARGGLU
5   GLUSERGLYALAARGILEASNILESERGLU
6   GLYASNCYSPROGLUARGILEILETHRLEU
7   ALAGLYPROTHRASNALAILEPHELYSALA
8   PHEALAMETILEILEGLYLYSLEUGLUGLU
9   ASPILESERSERSERMETTHRASNSERTHR
10   ALAALASERARGPROPROVALTHRLEUARG
11   LEUVALVALPROALASERGLNCYSGLYSER
12   LEUILEGLYLYSGLYGLYCYSLYSILELYS
13   GLUILEARGGLUSERTHRGLYALAGLNVAL
14   GLNVALALAGLYASPMETLEUPROASNSER
15   THRGLUARGALAILETHRILEALAGLYILE
16   PROGLNSERILEILEGLUCYSVALLYSGLN
17   ILECYSVALVALMETLEUGLUTHR

Samples:

sample_1: PCBP2 KH1 and KH2 domains, [U-100% 13C; U-100% 15N], 1 mM; H2O 10%; D2O 90%

sample_conditions_1: ionic strength: 50 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_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAE41029 BAG59482
GB KFP19120 KFQ73073
REF XP_002721142 XP_004951015 XP_004951016 XP_004951017 XP_004951018