BMRB Entry 52187

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52187

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Title:
aMED25-ACID(551-680)
Deposition date:
2023-10-22
Original release date:
2024-01-09
Authors:
Xiong, Yue; Zhu, Jiang; Yang, Yunhuang
Citation:

Citation: Xiong, Yue; Zhu, Jiang; Hu, Rui; Li, Ying; Yang, Yunhuang; Liu, Maili. "Chemical shift assignments of the ACID domain of MED25, a subunit of the mediator complex in Arabidopsis thaliana"  Biomol. NMR Assign. 18, 27-31 (2024).
PubMed: 38334938

Assembly members:

Assembly members:
entity_1, polymer, 130 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Thale cress   Taxonomy ID: 3702   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Arabidopsis thaliana

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: E. coli - cell free   Vector: pET32

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SQSKYVKVWEGNLSGQRQGQ PVLITRLEGYRSASASDSLA ANWPPTMQIVRLISQDHMNN KQYVGKADFLVFRAMSQHGF LGQLQDKKLCAVIQLPSQTL LLSVSDKACRLIGMLFPGDM VVFKPQIPNQ

Data sets:
Data typeCount
13C chemical shifts544
15N chemical shifts142
1H chemical shifts878

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1aMED25-ACID1

Entities:

Entity 1, aMED25-ACID 130 residues - Formula weight is not available

1   SERGLNSERLYSTYRVALLYSVALTRPGLU
2   GLYASNLEUSERGLYGLNARGGLNGLYGLN
3   PROVALLEUILETHRARGLEUGLUGLYTYR
4   ARGSERALASERALASERASPSERLEUALA
5   ALAASNTRPPROPROTHRMETGLNILEVAL
6   ARGLEUILESERGLNASPHISMETASNASN
7   LYSGLNTYRVALGLYLYSALAASPPHELEU
8   VALPHEARGALAMETSERGLNHISGLYPHE
9   LEUGLYGLNLEUGLNASPLYSLYSLEUCYS
10   ALAVALILEGLNLEUPROSERGLNTHRLEU
11   LEULEUSERVALSERASPLYSALACYSARG
12   LEUILEGLYMETLEUPHEPROGLYASPMET
13   VALVALPHELYSPROGLNILEPROASNGLN

Samples:

sample_1: aMED25-ACID, [U-100% 13C; U-100% 15N], 0.3 mM; sodium chloride 50 mM; sodium phosphate 100 mM; DTT 5 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D (H)CCH-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:

SPARKY vv3.115, Goddard - chemical shift assignment

TOPSPIN vv3.1, Bruker Biospin - collection

NMRPipe - processing

TALOS - chemical shift calculation

CYANA - structure solution

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE III 800 MHz
  • Bruker AVANCE III 850 MHz

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