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 17323

Title: Solution NMR Structure of Med25(391-543) Comprising the Activator-Interacting Domain (ACID) of Human Mediator Subuniti 25. Northeast Structural Genomics Consortium Target HR6188A   PubMed: 21785987

Authors: Eletsky, Alexander; Ryuechan, William; Sukumaran, Dinesh; Shastry, Ritu; Ciccosanti, Colleen; Janjua, Haleema; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Szyperski, Thomas

Citation: Eletsky, Alexander; Ruyechan, William; Xiao, Rong; Acton, Thomas; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR structure of MED25(391-543) comprising the activator-interacting domain (ACID) of human mediator subunit 25."  J. Struct. Funct. Genomics 12, 159-166 (2011).

Assembly members:
HR6188A, polymer, 163 residues, 18637.756 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
HR6188A: MGHHHHHHSHGQQSVSNKLL AWSGVLEWQEKPKPASVDAN TKLTRSLPCQVYVNHGENLK TEQWPQKLIMQLIPQQLLTT LGPLFRNSRMVQFHFTNKDL ESLKGLYRIMGNGFAGCVHF PHTAPCEVRVLMLLYSSKKK IFMGLIPYDQSGFVNGIRQV ITN

Data sets:
Data typeCount
13C chemical shifts721
15N chemical shifts172
1H chemical shifts1160

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HR6188A1

Entities:

Entity 1, HR6188A 163 residues - 18637.756 Da.

residues 381-390 represent a non-native affinity tag

1   METGLYHISHISHISHISHISHISSERHIS
2   GLYGLNGLNSERVALSERASNLYSLEULEU
3   ALATRPSERGLYVALLEUGLUTRPGLNGLU
4   LYSPROLYSPROALASERVALASPALAASN
5   THRLYSLEUTHRARGSERLEUPROCYSGLN
6   VALTYRVALASNHISGLYGLUASNLEULYS
7   THRGLUGLNTRPPROGLNLYSLEUILEMET
8   GLNLEUILEPROGLNGLNLEULEUTHRTHR
9   LEUGLYPROLEUPHEARGASNSERARGMET
10   VALGLNPHEHISPHETHRASNLYSASPLEU
11   GLUSERLEULYSGLYLEUTYRARGILEMET
12   GLYASNGLYPHEALAGLYCYSVALHISPHE
13   PROHISTHRALAPROCYSGLUVALARGVAL
14   LEUMETLEULEUTYRSERSERLYSLYSLYS
15   ILEPHEMETGLYLEUILEPROTYRASPGLN
16   SERGLYPHEVALASNGLYILEARGGLNVAL
17   ILETHRASN

Samples:

HR6188A_NC: HR6188A, [U-100% 13C; U-100% 15N], 0.7 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02%; D2O 10%; H2O 90%

HR6188A_NC5: HR6188A, [U-5% 13C; U-100% 15N], 0.4 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02%; D2O 10%; H2O 90%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCHR6188A_NCisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticHR6188A_NCisotropicsample_conditions_1
3D HNCOHR6188A_NCisotropicsample_conditions_1
3D CBCA(CO)NHHR6188A_NCisotropicsample_conditions_1
3D HNCACBHR6188A_NCisotropicsample_conditions_1
3D HN(CA)COHR6188A_NCisotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYHR6188A_NCisotropicsample_conditions_1
3D HBHA(CO)NHHR6188A_NCisotropicsample_conditions_1
3D HNCAHR6188A_NCisotropicsample_conditions_1
2D 1H-13C CT-HSQC aliphaticHR6188A_NCisotropicsample_conditions_1
2D 1H-13C CT-HSQC aromaticHR6188A_NCisotropicsample_conditions_1
1D 15N T1HR6188A_NCisotropicsample_conditions_1
1D 15N T2HR6188A_NCisotropicsample_conditions_1
3D (H)CCH-TOCSY aliphaticHR6188A_NCisotropicsample_conditions_1
3D (H)CCH-COSY aliphaticHR6188A_NCisotropicsample_conditions_1
3D (H)CCH-COSY aromaticHR6188A_NCisotropicsample_conditions_1
2D 1H-15N LR-HSQC for histidinesHR6188A_NCisotropicsample_conditions_1
2D (HB)CB(CGCDCE)HDHEHR6188A_NCisotropicsample_conditions_1
2D 1H-13C CT-HSQC methylHR6188A_NC5isotropicsample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement,structure solution,geometry optimization

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis,refinement

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

XEASY v1.3.13, Bartels et al. - data analysis

TOPSPIN v2.1, Bruker Biospin - collection, processing

VNMRJ v2.2D, Varian - collection

PROSA v6.4, Guntert - processing

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

TALOS+ v1.2009.0721.18, Shen, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Varian INOVA 750 MHz

Related Database Links:

BMRB 17139
PDB
DBJ BAE29135 BAF82149 BAG51583 BAG61008
EMBL CAB66680 CAE84581
GB AAG15589 AAH21333 AAH24312 AAH31138 AAH65297
REF NP_001075914 NP_001163897 NP_083641 NP_112235 XP_001115473
SP A2VE44 Q71SY5 Q8VCB2
TPG DAA19611