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 27594

Title: Backbone resonance assignments for the CsuC-CsuA/B complex.   PubMed: 30228191

Authors: McKenna, Sophie; Xu, Yingqi; Matthews, Stephen

Citation: Pakharukova, Natalia; McKenna, Sophie; Tuittila, Minna; Paavilainen, Sari; Malmi, Henri; Xu, Yingqi; Parilova, Olena; Matthews, Stephen; Zavialov, Anton. "Archaic and alternative chaperones preserve pilin folding energy by providing incomplete structural information"  J. Biol. Chem. 293, 17070-17080 (2018).

Assembly members:
CsuC, polymer, 243 residues, 26970.71 Da.
CsuA/B, polymer, 152 residues, 15915.46 Da.

Natural source:   Common Name: Acinetobacter baumannii   Taxonomy ID: 470   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Acinetobacter baumannii

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

Entity Sequences (FASTA):
CsuC: ATFLIWPIYPKIEANEKATA VWLQNTGKTDAMVQIRVFKW NQDGLKDNYSEQSEIIPSPP VAKIKAGEKHMLRLTKSVNL PDGKEQSYRLIVDELPIRLS DGNEQDASKVSFQMRYSIPL FAYGKGIGSGLTEESQKLNA KNALAKPVLQWSVRNNQQGQ SELYLKNNGQKFARLSALKT SKTGNDISLGKAAFGYVLSN STVKFAIDQSTAHELAKTSK IYGVDSSGIKQELIEITKME DPS
CsuA/B: AVTHHHHHHSTGCTVGGSQT EGNMNKFGTLNFGKTSGTWN NVLTAEVASAATGGNISVTC DGTDPVDFTVAIDGGERTDR TLKNTASADVVAYNVYRDAA RTNLYVVNQPQQFTTVSGQA TAVPIFGAIAPNTGTPKAQG DYKDTLLVTVNF

Data typeCount
13C chemical shifts834
15N chemical shifts262
1H chemical shifts262
T1 relaxation values240
T2 relaxation values240
heteronuclear NOE values259

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1CsuC1
2CsuA/B2

Entities:

Entity 1, CsuC 243 residues - 26970.71 Da.

1   ALATHRPHELEUILETRPPROILETYRPRO
2   LYSILEGLUALAASNGLULYSALATHRALA
3   VALTRPLEUGLNASNTHRGLYLYSTHRASP
4   ALAMETVALGLNILEARGVALPHELYSTRP
5   ASNGLNASPGLYLEULYSASPASNTYRSER
6   GLUGLNSERGLUILEILEPROSERPROPRO
7   VALALALYSILELYSALAGLYGLULYSHIS
8   METLEUARGLEUTHRLYSSERVALASNLEU
9   PROASPGLYLYSGLUGLNSERTYRARGLEU
10   ILEVALASPGLULEUPROILEARGLEUSER
11   ASPGLYASNGLUGLNASPALASERLYSVAL
12   SERPHEGLNMETARGTYRSERILEPROLEU
13   PHEALATYRGLYLYSGLYILEGLYSERGLY
14   LEUTHRGLUGLUSERGLNLYSLEUASNALA
15   LYSASNALALEUALALYSPROVALLEUGLN
16   TRPSERVALARGASNASNGLNGLNGLYGLN
17   SERGLULEUTYRLEULYSASNASNGLYGLN
18   LYSPHEALAARGLEUSERALALEULYSTHR
19   SERLYSTHRGLYASNASPILESERLEUGLY
20   LYSALAALAPHEGLYTYRVALLEUSERASN
21   SERTHRVALLYSPHEALAILEASPGLNSER
22   THRALAHISGLULEUALALYSTHRSERLYS
23   ILETYRGLYVALASPSERSERGLYILELYS
24   GLNGLULEUILEGLUILETHRLYSMETGLU
25   ASPPROSER

Entity 2, CsuA/B 152 residues - 15915.46 Da.

Residues 4 to 12 in the mature protein (29 to 37 in the full sequence before signal peptide removal) were replaced by a 6H-coding fragment to produce a N-terminal hexa-histag.

1   ALAVALTHRHISHISHISHISHISHISSER
2   THRGLYCYSTHRVALGLYGLYSERGLNTHR
3   GLUGLYASNMETASNLYSPHEGLYTHRLEU
4   ASNPHEGLYLYSTHRSERGLYTHRTRPASN
5   ASNVALLEUTHRALAGLUVALALASERALA
6   ALATHRGLYGLYASNILESERVALTHRCYS
7   ASPGLYTHRASPPROVALASPPHETHRVAL
8   ALAILEASPGLYGLYGLUARGTHRASPARG
9   THRLEULYSASNTHRALASERALAASPVAL
10   VALALATYRASNVALTYRARGASPALAALA
11   ARGTHRASNLEUTYRVALVALASNGLNPRO
12   GLNGLNPHETHRTHRVALSERGLYGLNALA
13   THRALAVALPROILEPHEGLYALAILEALA
14   PROASNTHRGLYTHRPROLYSALAGLNGLY
15   ASPTYRLYSASPTHRLEULEUVALTHRVAL
16   ASNPHE

Samples:

sample_1: CsuC, [U-13C; U-15N; U-2H], 500 uM; CsuA/B, [U-13C; U-15N; U-2H], 500 uM; sodium phosphate 50 mM; sodium chloride 50 mM; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 50 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D 1H-15N Trosysample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1

Software:

CCPN_Analysis v2.2, CCPN - chemical shift assignment, data analysis, peak picking

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

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 950 MHz
  • Bruker Avance 800 MHz

Related Database Links:

UniProtKB Q6XBY4 Q6XBY7