BMRB Entry 30691

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30691
MolProbity Validation Chart

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Title:
NMR Structure of C-terminal Domain of phi29 ATPase
Deposition date:
2019-11-21
Original release date:
2020-09-28
Authors:
Mahler, B.; Mao, H.; Morais, M.
Citation:

Citation: Woodson, Michael; Pajak, Joshua; Mahler, Bryon; Zhao, Wei; Zhang, Wei; Arya, Gaurav; White, Mark; Jardine, Paul; Morais, Marc. "A viral genome packaging motor transitions between cyclic and helical symmetry to translocate dsDNA"  Sci. Adv. 7, eabc1955-eabc1955 (2021).
PubMed: 33962953

Assembly members:

Assembly members:
entity_1, polymer, 119 residues, 14195.173 Da.

Natural source:

Natural source:   Common Name: Bacillus phage phi29   Taxonomy ID: 10756   Superkingdom: Viruses   Kingdom: not available   Genus/species: Salasvirus Bacillus phage phi29

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: pET30a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MFIGDSQVFIEKRSKDSKFV FSIVYNGFTLGVWVDVNQGL MYIDTAHDPSTKNVYTLTTD DLNENMMLITNYKNNYHLRK LASAFMNGYLRFDNQVIRNI AYELFRKMRIQLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts441
15N chemical shifts103
1H chemical shifts641

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 119 residues - 14195.173 Da.

1   METPHEILEGLYASPSERGLNVALPHEILE
2   GLULYSARGSERLYSASPSERLYSPHEVAL
3   PHESERILEVALTYRASNGLYPHETHRLEU
4   GLYVALTRPVALASPVALASNGLNGLYLEU
5   METTYRILEASPTHRALAHISASPPROSER
6   THRLYSASNVALTYRTHRLEUTHRTHRASP
7   ASPLEUASNGLUASNMETMETLEUILETHR
8   ASNTYRLYSASNASNTYRHISLEUARGLYS
9   LEUALASERALAPHEMETASNGLYTYRLEU
10   ARGPHEASPASNGLNVALILEARGASNILE
11   ALATYRGLULEUPHEARGLYSMETARGILE
12   GLNLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: protein, [U-15N], 1 uM; MES 50 mM

sample_2: protein, [U-13C], 1 uM; MES, [U-2H], 50 mM

sample_3: protein, U-15N, U-13C, 1 uM; MES 50 mM

sample_conditions_1: pH: 6.0; pressure: 1013 mbar; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D 15N NOESY-HSQCsample_1isotropicsample_conditions_1
3D 13C-edited NOESY-HSQC aliphaticsample_2isotropicsample_conditions_1
3D 13C-editied NOESY-HSQC aromaticsample_2isotropicsample_conditions_1
3D HSQC-NOESY-HSQCsample_2isotropicsample_conditions_1
HD-exchangesample_1isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1

Software:

TopSpin v3.2, Bruker Biospin - collection

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

NMRView v9.2.0, Johnson, One Moon Scientific - data analysis

TALOS-N, Cornilescu, Delaglio and Bax - chemical shift calculation

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

NMR spectrometers:

  • Bruker AVANCE III 750 MHz
  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE III 800 MHz

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