BMRB Entry 18051

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18051
MolProbity Validation Chart

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Title:
Solution NMR structure of the N-terminal myb-like 1 domain of the human cyclin-D-binding transcription factor 1 (hDMP1). Northeast Structural Genomics Consortium (NESG) target ID hr8011a.
Deposition date:
2011-11-10
Original release date:
2012-01-06
Authors:
Montecchio, Meri; Lemak, Alexander; Yee, Adelinda; Xu, Chao; Garcia, Maite; Houliston, Scott; Min, Jinrong; Bellanda, Massimo; Montelione, Gaetano; Arrowsmith, Cheryl
Citation:

Citation: Montecchio, Meri; Lemak, Alexander; Yee, Adelinda; Xu, Chao; Garcia, Maite; Houliston, Scott; Min, Jinrong; Bellanda, Massimo; Arrowsmith, Cheryl; Montelione, Gaetano. "Solution NMR structure of the N-terminal myb-like 1 domain of the human cyclin-D-binding transcription factor 1 (hDMP1)."  .

Assembly members:

Assembly members:
entity_1, polymer, 73 residues, 6184.080 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: pET28-MHL

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MHHHHHHSSGRENLYFQGDR NHVGKYTPEEIEKLKELRIK HGNDWATIGAALGRSASSVK DRCRLMKDTCNTG

Data sets:
Data typeCount
13C chemical shifts230
15N chemical shifts57
1H chemical shifts372

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1myb-like1 domain of hDMP11

Entities:

Entity 1, myb-like1 domain of hDMP1 73 residues - 6184.080 Da.

1   METHISHISHISHISHISHISSERSERGLY
2   ARGGLUASNLEUTYRPHEGLNGLYASPARG
3   ASNHISVALGLYLYSTYRTHRPROGLUGLU
4   ILEGLULYSLEULYSGLULEUARGILELYS
5   HISGLYASNASPTRPALATHRILEGLYALA
6   ALALEUGLYARGSERALASERSERVALLYS
7   ASPARGCYSARGLEUMETLYSASPTHRCYS
8   ASNTHRGLY

Samples:

sample_1: entity 1, [U-13C; U-15N], 1 mM; sodium phosphate 10 mM; NaCl 400 mM; ZnSO4 0.01 mM; DTT 10 mM; benzamidine 1 mM; NaN3 0.01%; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 400 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D H(C)CH-TOCSYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1

Software:

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

TALOS, Cornilescu, Delaglio and Bax - data analysis

SPARKY, Goddard - peak picking

MDDGUI, Gutmanas A., Orekhov V. - processing

FMCGUI, Lemak A., Steren C., Llinas M., Arrowsmith C. - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

PSVS, Bhattacharya and Montelione - structure validation

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
GB KFO03472
REF XP_010296009

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