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 17396

Title: 1H, 13C, and 15N Chemical Shift Assignments for FCS domain from human polyhomeotic homolog 1   PubMed: 21351738

Authors: Ilangovan, Udayar; Kim, Chongwoo

Citation: Wang, Renjing; Ilangovan, Udayar; Leal, Belinda; Robinson, Angela; Amann, Barbara; Tong, Corey; Berg, Jeremy; Hinck, Andrew; Kim, Chongwoo. "Identification of Nucleic Acid Binding Residues in the FCS Domain of the Polycomb Group Protein Polyhomeotic."  Biochemistry 50, 4998-5007 (2011).

Assembly members:
FCS_domain_of_hPh1, polymer, 49 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.

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):
FCS_domain_of_hPh1: GTRGVDSPSAELDKKANLLK CEYCGKYAPAEQFRGSKRFC SMTCAKRYN

Data sets:
Data typeCount
13C chemical shifts198
15N chemical shifts46
1H chemical shifts306

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Zn bound FCS domain of hPh11
2zinc ion2

Entities:

Entity 1, Zn bound FCS domain of hPh1 49 residues - Formula weight is not available

1   GLYTHRARGGLYVALASPSERPROSERALA
2   GLULEUASPLYSLYSALAASNLEULEULYS
3   CYSGLUTYRCYSGLYLYSTYRALAPROALA
4   GLUGLNPHEARGGLYSERLYSARGPHECYS
5   SERMETTHRCYSALALYSARGTYRASN

Entity 2, zinc ion - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: Zn bound FCS domain of hPh1, [U-100% 15N], 1.5 mM; H2O 95%; D2O 5%

sample_2: Zn bound FCS domain of hPh1, [U-95% 13C; U-95% 15N], 1.5 mM; H2O 95%; D2O 5%

sample_3: Zn bound FCS domain of hPh1, [U-10% 13C; U-99% 15N], 1.5 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.050 M; pH: 6.0; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - data analysis

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz

Related Database Links:

PDB
REF XP_004717481 XP_004717482 XP_006069838 XP_006069839 XP_006069840