BMRB Entry 30210

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30210
MolProbity Validation Chart

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Title:
Solution structure of the zinc fingers 1 and 2 of MBNL1 in complex with human cardiac troponin T pre-mRNA
Deposition date:
2016-12-15
Original release date:
2017-07-25
Authors:
Phukan, P.; Park, S.; Martinez-Yamout, M.; Zeeb, M.; Dyson, H.; Wright, P.
Citation:

Citation: Park, Sangho; Phukan, Priti Deka; Zeeb, Markus; Martinez-Yamout, Maria; Dyson, Helen Jane; Wright, Peter. "Structural basis for interaction of the tandem zinc finger domains of human muscleblind with cognate RNA from human cardiac troponin T"  Biochemistry 56, 4154-4168 (2017).
PubMed: 28718627

Assembly members:

Assembly members:
Muscleblind-like protein 1, polymer, 92 residues, 10577.180 Da.
RNA (5'-R(P*GP*UP*CP*UP*CP*GP*CP*UP*UP*UP*UP*CP*CP*CP*C)-3'), polymer, 15 residues, 4618.721 Da.
ZINC ION, non-polymer, 65.409 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Muscleblind-like protein 1: MAVSVTPIRDTKWLTLEVCR EFQRGTCSRPDTECKFAHPS KSCQVENGRVIACFDSLKGR CSRENCKYLHPPPHLKTQLE INGRNNLIQQKN
RNA (5'-R(P*GP*UP*CP*UP*CP*GP*CP*UP*UP*UP*UP*CP*CP*CP*C)-3'): GUCUCGCUUUUCCCC

Data sets:
Data typeCount
13C chemical shifts300
15N chemical shifts85
1H chemical shifts554

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22
3ZINC ION, 13
4ZINC ION, 23

Entities:

Entity 1, entity_1 92 residues - 10577.180 Da.

1   METALAVALSERVALTHRPROILEARGASP
2   THRLYSTRPLEUTHRLEUGLUVALCYSARG
3   GLUPHEGLNARGGLYTHRCYSSERARGPRO
4   ASPTHRGLUCYSLYSPHEALAHISPROSER
5   LYSSERCYSGLNVALGLUASNGLYARGVAL
6   ILEALACYSPHEASPSERLEULYSGLYARG
7   CYSSERARGGLUASNCYSLYSTYRLEUHIS
8   PROPROPROHISLEULYSTHRGLNLEUGLU
9   ILEASNGLYARGASNASNLEUILEGLNGLN
10   LYSASN

Entity 2, entity_2 15 residues - 4618.721 Da.

1   GUCUCGCUUU
2   UCCCC

Entity 3, ZINC ION, 1 - 65.409 Da.

1   ZNZN

Samples:

sample_1: RNA (5'-R(P*GP*UP*CP*UP*CP*GP*CP*UP*UP*UP*UP*CP*CP*CP*C)-3'), unlabeled, 0.4 mM; Zinc fingers 1 and 2 of MBNL1, [U-98% 13C; U-98% 15N], 0.4 mM; H2O 90%; D2O 10%; NaCl 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 13C,15N-filtered NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - structure calculation

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

SPARKY, Goddard - data analysis

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz

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