BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 18051

Click here to enlarge.

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

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

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: 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)."  Not known ., .-..

Assembly members:
entity_1, polymer, 73 residues, 6184.080 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):
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
  • Hide all

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 simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts