BMRB Entry 5389

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5389
MolProbity Validation Chart

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Title:
1H, 13C and 15N assignments for the cold shock response protein Yfia
Deposition date:
2002-06-09
Original release date:
2002-09-25
Authors:
Kalinin, Alexander; Rak, Alexej; Shcherbakov, Dimitry; Bayer, Peter
Citation:

Citation: Kalinin, Alexander; Rak, Alexej; Shcherbakov, Dimitry; Bayer, Peter. "Letter to the Editor: 1H, 13C and 15N resonance assignments of the ribosome-associated cold shock response protein Yfia of Escherichia coli"  J. Biomol. NMR 23, 335-336 (2002).

Assembly members:

Assembly members:
cold shock response protein Yfia, polymer, 113 residues, 12784.5 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
cold shock response protein Yfia: MTMNITSKQMEITPAIRQHV ADRLAKLEKWQTHLINPHII LSKEPQGFVADATINTPNGV LVASGKHEDMYTAINELINK LERQLNKLQHKGEARRAATS VKDANFVEEVEEE

Data sets:
Data typeCount
1H chemical shifts809
13C chemical shifts490
15N chemical shifts117

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Yfia subunit 11

Entities:

Entity 1, Yfia subunit 1 113 residues - 12784.5 Da.

1   METTHRMETASNILETHRSERLYSGLNMET
2   GLUILETHRPROALAILEARGGLNHISVAL
3   ALAASPARGLEUALALYSLEUGLULYSTRP
4   GLNTHRHISLEUILEASNPROHISILEILE
5   LEUSERLYSGLUPROGLNGLYPHEVALALA
6   ASPALATHRILEASNTHRPROASNGLYVAL
7   LEUVALALASERGLYLYSHISGLUASPMET
8   TYRTHRALAILEASNGLULEUILEASNLYS
9   LEUGLUARGGLNLEUASNLYSLEUGLNHIS
10   LYSGLYGLUALAARGARGALAALATHRSER
11   VALLYSASPALAASNPHEVALGLUGLUVAL
12   GLUGLUGLU

Samples:

sample_1: cold shock response protein Yfia, [U-13C; U-15N], 0.5 – 0.8 mM

sample_2: cold shock response protein Yfia0.5 – 0.8 mM

Ex-cond_1: pH: 6.65; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
3D-HNCAnot availablenot availablenot available
3D-HNCOnot availablenot availablenot available
3D-HNCACBnot availablenot availablenot available
3D-HC(CO)NHnot availablenot availablenot available
3D-C(CO)NHnot availablenot availablenot available
3D-HCCH-TOCSYnot availablenot availablenot available
3D-1H,15N-HSQC-TOCSYnot availablenot availablenot available
3D-1H,15N-HSQC-NOESYnot availablenot availablenot available
3D-1H,13C-HSQC-NOESYnot availablenot availablenot available
2D-1H,13C-HSQCnot availablenot availablenot available
2D-1H,15N-HSQCnot availablenot availablenot available
2D-1H,1H-DQF-COSYnot availablenot availablenot available
2D-1H,1H-TOCSYnot availablenot availablenot available
2D-1H,1H-NOESYnot availablenot availablenot available

Software:

Aurelia v2.0 - Assignment of 3D-spectra

NDEE - Assignment of 2D-spectra, details, Spin-Up, Dortmund, Germany

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Varian INOVA 600 MHz

Related Database Links:

BMRB 5315
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
AlphaFold P0AD49 P0AD50 P0AD51 P0AD52

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks