BMRB Entry 34256

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34256
MolProbity Validation Chart

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Title:
Solution structure of the TPR domain of the cell division coordinator, CpoB
Deposition date:
2018-03-29
Original release date:
2018-08-06
Authors:
Simorre, J.; Maya Martinez, R.; Bougault, C.; Vollmer, W.; Egan, A.
Citation:

Citation: Egan, Alexander; Maya-Martinez, Roberto; Ayala, Isabel; Bougault, Catherine; Banzhaf, Manuel; Breukink, Eefjan; Vollmer, Waldemar; Simorre, Jean-Pierre. "Induced conformational changes activate the peptidoglycan synthase PBP1B."  Mol. Microbiol. 110, 335-356 (2018).
PubMed: 30044025

Assembly members:

Assembly members:
entity_1, polymer, 146 residues, 16152.112 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 83333   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: pAJFE01

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH MSGNANTDYNAAIALVQDKS RQDDAMVAFQNFIKNYPDST YLPNANYWLGQLNYNKGKKD DAAYYFASVVKNYPKSPKAA DAMFKVGVIMQDKGDTAKAK AVYQQVISKYPGTDGAKQAQ KRLNAM

Data sets:
Data typeCount
13C chemical shifts526
15N chemical shifts122
1H chemical shifts776

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 146 residues - 16152.112 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METSERGLYASNALAASNTHRASPTYRASN
4   ALAALAILEALALEUVALGLNASPLYSSER
5   ARGGLNASPASPALAMETVALALAPHEGLN
6   ASNPHEILELYSASNTYRPROASPSERTHR
7   TYRLEUPROASNALAASNTYRTRPLEUGLY
8   GLNLEUASNTYRASNLYSGLYLYSLYSASP
9   ASPALAALATYRTYRPHEALASERVALVAL
10   LYSASNTYRPROLYSSERPROLYSALAALA
11   ASPALAMETPHELYSVALGLYVALILEMET
12   GLNASPLYSGLYASPTHRALALYSALALYS
13   ALAVALTYRGLNGLNVALILESERLYSTYR
14   PROGLYTHRASPGLYALALYSGLNALAGLN
15   LYSARGLEUASNALAMET

Samples:

sample_1: CpoB, [U-13C; U-15N], 2 ± 0.1 mM; Tris/HCl 10 mM; NaCl 200 mM

sample_conditions_1: ionic strength: 200 mM; pH: 7.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D BESTROSY-HNCACBsample_1isotropicsample_conditions_1
3D BESTROSY-HN(CO)CACBsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

Aria v2.3, Rieping W., Habeck M., Bardiaux B., Bernard A , Nilges M. - structure calculation

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CcpNmr_Analysis v2.4, CCPN - chemical shift assignment

Talos+, Yang Shen, Frank Delaglio, Gabriel Cornilescu, and Ad Bax - data analysis

Unio10 v2.0.2, Torsten Herrmann - structure calculation

nmrDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

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

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 850 MHz
  • Bruker US2 950 MHz

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