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 34126

Title: NMR structure and 1H, 13C and 15N signal assignments for Dictyostelium discoideum MATA protein   PubMed: 28879231

Authors: Neuhaus, D.; Hedgethorne, K.; Yang, J.-C.

Citation: Hedgethorne, Katy; Eustermann, Sebastian; Yang, Ji-Chun; Ogden, Tom; Neuhaus, David; Bloomfield, Gareth. "Homeodomain-like DNA binding proteins control the haploid-to-diploid transition in Dictyostelium."  Sci. Adv. 3, e1602937-e1602937 (2017).

Assembly members:
entity_1, polymer, 113 residues, 12510.442 Da.

Natural source:   Common Name: Slime mold   Taxonomy ID: 44689   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Dictyostelium discoideum

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

Entity Sequences (FASTA):
entity_1: GSHMASMDPLDKIINDIKKE ANDSGVTLAPLSVPKPKLEE LSEQQKIILAEYIAEVGLQN ITAITLSKKLNITVEKAKNY IKNSNRLGRTNNLKTIGILQ EEVSSMEAKSMTW

Data sets:
Data typeCount
13C chemical shifts393
15N chemical shifts120
1H chemical shifts834

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 113 residues - 12510.442 Da.

1   GLYSERHISMETALASERMETASPPROLEU
2   ASPLYSILEILEASNASPILELYSLYSGLU
3   ALAASNASPSERGLYVALTHRLEUALAPRO
4   LEUSERVALPROLYSPROLYSLEUGLUGLU
5   LEUSERGLUGLNGLNLYSILEILELEUALA
6   GLUTYRILEALAGLUVALGLYLEUGLNASN
7   ILETHRALAILETHRLEUSERLYSLYSLEU
8   ASNILETHRVALGLULYSALALYSASNTYR
9   ILELYSASNSERASNARGLEUGLYARGTHR
10   ASNASNLEULYSTHRILEGLYILELEUGLN
11   GLUGLUVALSERSERMETGLUALALYSSER
12   METTHRTRP

Samples:

sample_1: DTT, [U-2H], 1 mM; EDTA 50 uM; MATA, [U-15N], 600 ± 100 uM; TRIS, [U-2H], 50 mM; sodium chloride 100 mM

sample_2: DTT, [U-2H], 1 mM; EDTA 50 uM; MATA, [U-13C; U-15N], 600 ± 100 uM; TRIS, [U-2H], 50 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNHAHBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D [1H-13C-1H] HCCH-TOCSYsample_2isotropicsample_conditions_1
3D [13C-13C-1H] HCCH-TOCSYsample_2isotropicsample_conditions_1
3D [1H-13C-1H] HCCH-COSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESY (mix. time 150ms)sample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphatic (mix. time 150ms)sample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromatic (mix. time 150ms)sample_2isotropicsample_conditions_1

Software:

AMBER v11, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CcpNMR v2.4, CCPN - chemical shift assignment

TOPSPIN v3.1 and 3.2, Bruker Biospin - processing

UNIO v2.0.3, Herrmann - structure calculation

X-PLOR NIH v2.28, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker DMX 600 MHz

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