BMRB Entry 18147

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18147

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Title:
Assigned NMR chemical shift of Escherichia coli Ribosome binding factor A
Deposition date:
2011-12-16
Original release date:
2012-03-07
Authors:
Kobayashi, Hiroshi; Swapna, G.V.T; Wu, Kuen-Phon; Yuliya, Afinogenova; Conover, Kenith; Mao, Binchen; Montelione, Gaetano; Inouye, Masayori
Citation:

Citation: Kobayashi, Hiroshi; Swapna, G.; Wu, Kuen-Phon; Afinogenova, Yuliya; Conover, Kenith; Mao, Binchen; Montelione, Gaetano; Inouye, Masayori. "Segmental isotope labeling of proteins for NMR structural study using a protein S tag for higher expression and solubility."  J. Biomol. NMR 52, 303-313 (2012).
PubMed: 22389115

Assembly members:

Assembly members:
RbfA, polymer, 147 residues, Formula weight is not available

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RbfA: SGVHMAKEFGRPQRVAQEMQ KEIALILQREIKDPRLGMMT TVSGVEMSRDLAYAKVYVTF LNDKDEDAVKAGIKALQEAS GFIRSLLGKAMRLRIVPELT FFYDNSLVEGMRMSNLVTSV VKHDEERRVNPDDSKEDGSW SHPQFEK

Data sets:
Data typeCount
13C chemical shifts393
15N chemical shifts136
1H chemical shifts136

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RbfA1

Entities:

Entity 1, RbfA 147 residues - Formula weight is not available

First 4 residue (SGVH) and last 10 residue (GSWSHPQFEK) come from cloning site or purification tag.

1   SERGLYVALHISMETALALYSGLUPHEGLY
2   ARGPROGLNARGVALALAGLNGLUMETGLN
3   LYSGLUILEALALEUILELEUGLNARGGLU
4   ILELYSASPPROARGLEUGLYMETMETTHR
5   THRVALSERGLYVALGLUMETSERARGASP
6   LEUALATYRALALYSVALTYRVALTHRPHE
7   LEUASNASPLYSASPGLUASPALAVALLYS
8   ALAGLYILELYSALALEUGLNGLUALASER
9   GLYPHEILEARGSERLEULEUGLYLYSALA
10   METARGLEUARGILEVALPROGLULEUTHR
11   PHEPHETYRASPASNSERLEUVALGLUGLY
12   METARGMETSERASNLEUVALTHRSERVAL
13   VALLYSHISASPGLUGLUARGARGVALASN
14   PROASPASPSERLYSGLUASPGLYSERTRP
15   SERHISPROGLNPHEGLULYS

Samples:

sample_1: RbfA, [U-100% 13C; U-100% 15N], 0.5 mM; NaCl 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 4.0; pressure: 1 atm; temperature: 308 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 HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAB37471 BAE77213 BAG78977 BAH65352 BAI27447
EMBL CAA31634 CAA32020 CAP77629 CAQ33502 CAQ90639
GB AAA57970 AAC76201 AAG58303 AAL22157 AAN44675
REF NP_312075 NP_417636 NP_462198 NP_708968 WP_001040197
SP A1AG72 A6TEI6 A7ZS64 A8A4Y3 A8AQ56
AlphaFold A8AQ56 A6TEI6 A7ZS64 A8A4Y3 A1AG72

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