BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 30691

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: Mahler, B.; Bujalowski, P.; Mao, H.; Dill, E.; Choi, K.; Jardine, P.; Morais, M.. "NMR Solution Structure and Dynamics of the C-terminal Domain of a Viral dsDNA Packaging ATPase"  . ., .-..

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

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

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

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 simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts