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 5315

Title: 1H, 13C and 15N chemical shift assignment for ribosome-associated factor Y   PubMed: 12392550

Authors: Ye, Keqiong; Serganov, Alexander; Hu, Weidong; Patel, Dinshaw

Citation: Ye, Keqiong; Serganov, Alexander; Hu, Weidong; Patel, Dinshaw. "Ribosome-associated Factor Y adopts a Fold resembling a Double-stranded RNA Binding Domain Scaffold "  Eur. J. Biochem. 269, 5182-5191 (2002).

Assembly members:
Protein Yfia, polymer, 112 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
Protein Yfia: TMNITSKQMEITPAIRQHVA DRLAKLEKWQTHLINPHIIL SKEPQGFVADATINTPNGVL VASGKHEDMYTAINELINKL ERQLNKLQHKGEARRAATSV KDANFVEEVEEE

Data sets:
Data typeCount
1H chemical shifts818
13C chemical shifts499
15N chemical shifts120
coupling constants75

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Protein Yfia1

Entities:

Entity 1, Protein Yfia 112 residues - Formula weight is not available

1   THRMETASNILETHRSERLYSGLNMETGLU
2   ILETHRPROALAILEARGGLNHISVALALA
3   ASPARGLEUALALYSLEUGLULYSTRPGLN
4   THRHISLEUILEASNPROHISILEILELEU
5   SERLYSGLUPROGLNGLYPHEVALALAASP
6   ALATHRILEASNTHRPROASNGLYVALLEU
7   VALALASERGLYLYSHISGLUASPMETTYR
8   THRALAILEASNGLULEUILEASNLYSLEU
9   GLUARGGLNLEUASNLYSLEUGLNHISLYS
10   GLYGLUALAARGARGALAALATHRSERVAL
11   LYSASPALAASNPHEVALGLUGLUVALGLU
12   GLUGLU

Samples:

sample_1: Protein Yfia, [U-99% 15N], 2 mM; sodium phosphate 10 mM; NaCl 50 mM; D2O 7%; H2O 93%

sample_2: Protein Yfia, [U-99% 13C; U-99% 15N], 1.5 mM; sodium phosphate 10 mM; NACL 50 mM; D2O 7%; H2O 97%

Ex-cond_1: pH: 5.7; temperature: 304.5 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYnot availablenot availablenot available
2D 1H-1H TOCSYnot availablenot availablenot available
2D 1H-15N HSQCnot availablenot availablenot available
2D 1H-13C CT-HSQCnot availablenot availablenot available
3D CBCA(CO)NHnot availablenot availablenot available
3D HNCACBnot availablenot availablenot available
3D HNCOnot availablenot availablenot available
3D HN(CA)COnot availablenot availablenot available
3D 1H-13C-1H HCCH-TOCSYnot availablenot availablenot available
3D 15N NOESYnot availablenot availablenot available
3D 15N TOCSYnot availablenot availablenot available
3D 13C NOESYnot availablenot availablenot available
3D H(CCO)NHnot availablenot availablenot available
3D C(CO)NHnot availablenot availablenot available
3D HNHAnot availablenot availablenot available
3D HNHBnot availablenot availablenot available

Software:

VNMR v6.1B - data collection

FELIX v98 - data processing

NMRView v5.0 - data analysis

CNS v1.0 - Structure Calculation

NMR spectrometers:

  • Varian UnityPlus 600 MHz

Related Database Links:

BMRB 5389
PDB
DBJ BAA16481 BAB36883 BAG78406 BAI26837 BAI31922
EMBL CAA94436 CAP77041 CAQ32967 CAQ88030 CAQ99546
GB AAA24328 AAC75646 AAG57709 AAN44153 AAN81568
REF NP_289151 NP_311487 NP_417088 NP_708446 NP_755000
SP P0AD49 P0AD50 P0AD51 P0AD52