BMRB Entry 5863

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5863

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Title:
Backbone HN, N, Ca, C and Cb chemical shift assignments and Secondary Structure of FkpA, a 245-residue peptidyl- prolyl cis/trans isomerase with chaperone activity
Deposition date:
2003-07-08
Original release date:
2004-02-13
Authors:
Hu, Kaifeng; Pluckthun, Andreas; Pervushin, Konstantin
Citation:

Citation: Hu, Kaifeng; Pluckthun, Andreas; Pervushin, Konstantin. "Letter to the Editor: Backbone HN, N, CA, C' and CB chemical shift assignments and Secondary Structure of FkpA, a 245-residue peptidyl- prolyl cis/trans isomerase with chaperone activity "  J. Biomol. NMR 28, 405-406 (2004).
PubMed: 14872134

Assembly members:

Assembly members:
FkpA, polymer, 245 residues, 26223 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   Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FkpA: AEAAKPATAADSKAAFKNDD QKSAYALGASLGRYMENSLK EQEKLGIKLDKDQLIAGVQD AFADKSKLSDQEIEQTLQAF EARVKSSAQAKMEKDAADNE AKGKEYREKFAKEKGVKTSS TGLVYQVVEAGKGEAPKDSD TVVVNYKGTLIDGKEFDNSY TRGEPLSFRLDGVIPGWTEG LKNIKKGGKIKLVIPPELAY GKAGVPGIPPNSTLVFDVEL LDVKPAPKADAKPEADAKAA DSAKK

Data sets:
Data typeCount
1H chemical shifts219
13C chemical shifts685
15N chemical shifts219

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FkpA, chain 11
2FkpA, chain 21

Entities:

Entity 1, FkpA, chain 1 245 residues - 26223 Da.

1   ALAGLUALAALALYSPROALATHRALAALA
2   ASPSERLYSALAALAPHELYSASNASPASP
3   GLNLYSSERALATYRALALEUGLYALASER
4   LEUGLYARGTYRMETGLUASNSERLEULYS
5   GLUGLNGLULYSLEUGLYILELYSLEUASP
6   LYSASPGLNLEUILEALAGLYVALGLNASP
7   ALAPHEALAASPLYSSERLYSLEUSERASP
8   GLNGLUILEGLUGLNTHRLEUGLNALAPHE
9   GLUALAARGVALLYSSERSERALAGLNALA
10   LYSMETGLULYSASPALAALAASPASNGLU
11   ALALYSGLYLYSGLUTYRARGGLULYSPHE
12   ALALYSGLULYSGLYVALLYSTHRSERSER
13   THRGLYLEUVALTYRGLNVALVALGLUALA
14   GLYLYSGLYGLUALAPROLYSASPSERASP
15   THRVALVALVALASNTYRLYSGLYTHRLEU
16   ILEASPGLYLYSGLUPHEASPASNSERTYR
17   THRARGGLYGLUPROLEUSERPHEARGLEU
18   ASPGLYVALILEPROGLYTRPTHRGLUGLY
19   LEULYSASNILELYSLYSGLYGLYLYSILE
20   LYSLEUVALILEPROPROGLULEUALATYR
21   GLYLYSALAGLYVALPROGLYILEPROPRO
22   ASNSERTHRLEUVALPHEASPVALGLULEU
23   LEUASPVALLYSPROALAPROLYSALAASP
24   ALALYSPROGLUALAASPALALYSALAALA
25   ASPSERALALYSLYS

Samples:

sample_1: FkpA, [U-99% 13C; U-99% 15N; U-98% 2H], 0.6 mM; Mes buffer 20 mM; NaCl 50 mM

sample_2: FkpA, [U-99% 13C; U-99% 15N; U-98% 2H], 0.5 mM; Mes buffer 20 mM; NaCl 20 mM

Ex-cond_1: pH: 6.0; temperature: 310 K; ionic strength: 0.02 M

Experiments:

NameSampleSample stateSample conditions
Bruker Avance 600 MHz spectrometer equipped with a TXI cryogenic probehead.not availablenot availableEx-cond_1
3D TROSY-versions of HNCA, HNCACB, HNCO and HN(CA)CO run in the highnot availablenot availableEx-cond_1
resolution mode, utilizing both N->C and C->N polarization transfer periods tonot availablenot availableEx-cond_1
maximize spectral resolution along the 15N dimension.not availablenot availableEx-cond_1

Software:

XEASY -

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz

Related Database Links:

PDB
DBJ BAB37621 BAE77944 BAG79132 BAI27605 BAI32775
EMBL CAP77799 CAQ33666 CAR00285 CAR04951 CAR10001
GB AAA58144 AAC41459 AAC76372 AAG58454 AAN44828
REF NP_289894 NP_312225 NP_417806 NP_709121 NP_755985
SP P45523 P65764 P65765
AlphaFold P45523 P65764 P65765

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