BMRB Entry 30532

Title:
Solution NMR Structure of DANCER3-F34A, a rigid and natively folded single mutant of the dynamic protein DANCER-3
Deposition date:
2018-10-31
Original release date:
2019-08-16
Authors:
Damry, A.; Mayer, M.; Goto, N.; Chica, R.
Citation:

Citation: Damry, Adam; Mayer, Marc; Broom, Aron; Goto, Natalie; Chica, Roberto. "Origin of conformational dynamics in a globular protein"  Commun. Biol. 2, 433-433 (2019).
PubMed: 31799435

Assembly members:

Assembly members:
entity_1, polymer, 64 residues, 7230.964 Da.

Natural source:

Natural source:   Common Name: Streptococcus sp.   Taxonomy ID: 1320   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptococcus Streptococcus sp.

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-11a

Entity Sequences (FASTA):

Data typeCount
13C chemical shifts242
15N chemical shifts62
1H chemical shifts379

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 64 residues - 7230.964 Da.

1   METHISHISHISHISHISHISGLYMETTHR
2   PHELYSLEUILEILEASNGLYLYSTHRLEU
3   LYSGLYGLUTHRTHRTHRGLUALAVALASP
4   ALAALATHRALAGLULYSVALPHELYSGLN
5   TYRALAASNASPASNGLYLEUASPGLYGLU
6   TRPTHRTYRASPASPALATHRLYSTHRPHE
7   THRILETHRGLU

Samples:

sample_1: protein (GB1), [U-98% 15N], 1.0 mM; sodium phosphate 10 mM

sample_2: protein (GB1), [U-99% 13C; U-98% 15N], 1.0 mM; sodium phosphate 10 mM

sample_3: protein (GB1), [U-99% 13C; U-98% 15N], 1.0 mM; sodium phosphate 10 mM

sample_conditions_1: ionic strength: 10 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_3isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D CCH-TOCSYsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

TOPSPIN, Bruker Biospin - collection

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

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

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