BMRB Entry 36565

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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/BMR36565
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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Title:
Solution structure of ABD3 (residues 453-561) of human MED15 isoform 2
Deposition date:
2023-05-03
Original release date:
2025-04-29
Authors:
Zhang, H.; Li, Y.
Citation:

Citation: Zhang, H.; Li, Y.. "Solution structure of ABD3 (residues 453-561) of human MED15 isoform 2"  .

Assembly members:

Assembly members:
Mediator of RNA polymerase II transcription subunit 15, polymer, 118 residues, 13405.515 Da.

Natural source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-30a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Mediator of RNA polymerase II transcription subunit 15: MHHHHHHASVTARTPQNFSV PSPGPLNTPVNPSSVMSPAG SSQAEEQQYLDKLKQLSKYI EPLRRMINKIDKNEDRKKDL SKMKSLLDILTDPSKRCPLK TLQKCEIALEKLKNDMAV

Data typeCount
13C chemical shifts391
15N chemical shifts103
1H chemical shifts492

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 118 residues - 13405.515 Da.

1   METHISHISHISHISHISHISALASERVAL
2   THRALAARGTHRPROGLNASNPHESERVAL
3   PROSERPROGLYPROLEUASNTHRPROVAL
4   ASNPROSERSERVALMETSERPROALAGLY
5   SERSERGLNALAGLUGLUGLNGLNTYRLEU
6   ASPLYSLEULYSGLNLEUSERLYSTYRILE
7   GLUPROLEUARGARGMETILEASNLYSILE
8   ASPLYSASNGLUASPARGLYSLYSASPLEU
9   SERLYSMETLYSSERLEULEUASPILELEU
10   THRASPPROSERLYSARGCYSPROLEULYS
11   THRLEUGLNLYSCYSGLUILEALALEUGLU
12   LYSLEULYSASNASPMETALAVAL

Samples:

sample_1: MED15_ABD3, [U-99% 13C; U-99% 15N], 1 mM; TCEP 1 mM; sodium chloride 200 mM; HEPES 20 mM; D2O, [U-2H], 6 % v/v; H2O 94%

sample_conditions_1: ionic strength: 200 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15N/13C_sampleisotropicsample_conditions_1
2D 1H-13C HSQC15N/13C_sampleisotropicsample_conditions_1
2D 1H-13C HSQC aromatic15N/13C_sampleisotropicsample_conditions_1
3D CBCA(CO)NH15N/13C_sampleisotropicsample_conditions_1
3D CBCANH15N/13C_sampleisotropicsample_conditions_1
3D HNCA15N/13C_sampleisotropicsample_conditions_1
3D HN(CO)CA15N/13C_sampleisotropicsample_conditions_1
3D HNCO15N/13C_sampleisotropicsample_conditions_1
3D HN(CA)CO15N/13C_sampleisotropicsample_conditions_1
3D HBHA(CO)NH15N/13C_sampleisotropicsample_conditions_1
3D C(CO)NH15N/13C_sampleisotropicsample_conditions_1
3D H(CCO)NH15N/13C_sampleisotropicsample_conditions_1
3D 1H-15N NOESY15N/13C_sampleisotropicsample_conditions_1
3D 1H-13C NOESY15N/13C_sampleisotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - collection

ARIA2alpha, Wolfgang Rieping, Michael Habeck, Benjamin Bardiaux, Aymeric Bernard, Therese E. Malliavin, Michael Nilges - structure calculation

NMRFAM-SPARKY, Lee W, Tonelli M, Markley JL - chemical shift assignment

NMRFAM-SPARKY, Lee W, Tonelli M, Markley JL - peak picking

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

ARIA2alpha, Wolfgang Rieping, Michael Habeck, Benjamin Bardiaux, Aymeric Bernard, Therese E. Malliavin, Michael Nilges - refinement

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