BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 25855

Title: Zipcode-binding-protein-1 KH3(DD)KH4 domains in complex with the RNA target UCGGACU   PubMed: 22547390

Deposition date: 2015-10-21 Original release date: 2017-01-19

Authors: Nicastro, Giuseppe; Ramos, Andres; Candel, Adela; Hollingworth, David

Citation: Hollingworth, David; Candel, Adela; Nicastro, Giuseppe; Martin, Stephen; Briata, Paola; Gherzi, Roberto; Ramos, Andres. "KH domains with impaired nucleic acid binding as a tool for functional analysis."  Nucleic Acids Res. 40, 6873-6886 (2012).

Assembly members:
entity_1, polymer, 191 residues, 20613.682 Da.
entity_2, polymer, 8 residues, Formula weight is not available

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
entity_1: GAMGPSSVSGAAPFSSFMPP EQETVHVFIPAQAVGAIIGK KGQHIKQLSRFASASIKIAP PETPDSKVRMVVITGPPEAQ FKAQGRIYGKLKEENFFGPK EEVKLETHIRVPASAAGRVI GKGGKTVNELQNLTAAEVVV PRDQTPDENEQVIVKIIGHF YASQMAQRKIRDILAQVKQQ HQKGQSGQLQA
entity_2: UCGGACU

Data sets:
Data typeCount

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 191 residues - 20613.682 Da.

1   GLYALAMETGLYPROSERSERVALSERGLY
2   ALAALAPROPHESERSERPHEMETPROPRO
3   GLUGLNGLUTHRVALHISVALPHEILEPRO
4   ALAGLNALAVALGLYALAILEILEGLYLYS
5   LYSGLYGLNHISILELYSGLNLEUSERARG
6   PHEALASERALASERILELYSILEALAPRO
7   PROGLUTHRPROASPSERLYSVALARGMET
8   VALVALILETHRGLYPROPROGLUALAGLN
9   PHELYSALAGLNGLYARGILETYRGLYLYS
10   LEULYSGLUGLUASNPHEPHEGLYPROLYS
11   GLUGLUVALLYSLEUGLUTHRHISILEARG
12   VALPROALASERALAALAGLYARGVALILE
13   GLYLYSGLYGLYLYSTHRVALASNGLULEU
14   GLNASNLEUTHRALAALAGLUVALVALVAL
15   PROARGASPGLNTHRPROASPGLUASNGLU
16   GLNVALILEVALLYSILEILEGLYHISPHE
17   TYRALASERGLNMETALAGLNARGLYSILE
18   ARGASPILELEUALAGLNVALLYSGLNGLN
19   HISGLNLYSGLYGLNSERGLYGLNLEUGLN
20   ALA

Entity 2, entity_2 8 residues - Formula weight is not available

1   UCGGACU

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 0.3 mM; entity_2 0.3 mM; phosphate buffer 20 mM; potassium phosphate 20 mM

sample_conditions_1: ionic strength: 0.02 M; pH: 6.5; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

XEASY, Bartels et al. - chemical shift assignment

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

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 950 MHz