BMRB Entry 30101

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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/BMR30101
MolProbity Validation Chart

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Title:
Structural characterization of melanoregulin (mreg): the protein involved in regulation of cell pigmentation
Deposition date:
2016-06-03
Original release date:
2017-06-02
Authors:
Rout, A.; Bermejo, G.; Marie-Paule, S.; Hammer, J.; Tjandra, N.
Citation:

Citation: Rout, Ashok; Wu, Xufeng; Starich, Mary; Strub, Marie-Paule; Hammer, John; Tjandra, Nico. "The Structure of Melanoregulin Reveals a Role for Cholesterol Recognition in the Protein's Ability to Promote Dynein Function"  Structure 26, 1373-1383 (2018).
PubMed: 30174147

Assembly members:

Assembly members:
Melanoregulin, polymer, 217 residues, 25348.918 Da.

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli-Pichia pastoris shuttle vector pPpARG4

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Melanoregulin: EFSAGLRRWLRSACCCCPCR CLEEPARPEKEPLVSGNNPY SSFGATLERDDEKNLWSMPH DVSHTEADDDRILYNLIVIR NQQTKDSEEWQRLNYDIYTL RQIRREVRNRWRRILEDLGF QREADSLLSVTKLSTMSDSK NTRKAREMLLKLAEETSIFP ASWELSERYLLVVDRLIALD AAEDFFKIASQMYPKKPGVP CLVDGQRKLHCLPFPSP

Data sets:
Data typeCount
13C chemical shifts533
15N chemical shifts151
1H chemical shifts676

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 217 residues - 25348.918 Da.

1   GLUPHESERALAGLYLEUARGARGTRPLEU
2   ARGSERALACYSCYSCYSCYSPROCYSARG
3   CYSLEUGLUGLUPROALAARGPROGLULYS
4   GLUPROLEUVALSERGLYASNASNPROTYR
5   SERSERPHEGLYALATHRLEUGLUARGASP
6   ASPGLULYSASNLEUTRPSERMETPROHIS
7   ASPVALSERHISTHRGLUALAASPASPASP
8   ARGILELEUTYRASNLEUILEVALILEARG
9   ASNGLNGLNTHRLYSASPSERGLUGLUTRP
10   GLNARGLEUASNTYRASPILETYRTHRLEU
11   ARGGLNILEARGARGGLUVALARGASNARG
12   TRPARGARGILELEUGLUASPLEUGLYPHE
13   GLNARGGLUALAASPSERLEULEUSERVAL
14   THRLYSLEUSERTHRMETSERASPSERLYS
15   ASNTHRARGLYSALAARGGLUMETLEULEU
16   LYSLEUALAGLUGLUTHRSERILEPHEPRO
17   ALASERTRPGLULEUSERGLUARGTYRLEU
18   LEUVALVALASPARGLEUILEALALEUASP
19   ALAALAGLUASPPHEPHELYSILEALASER
20   GLNMETTYRPROLYSLYSPROGLYVALPRO
21   CYSLEUVALASPGLYGLNARGLYSLEUHIS
22   CYSLEUPROPHEPROSERPRO

Samples:

sample_1: melanoregulin, [U-99% 15N], 0.150 mM; H2O 90%; D2O 10%; L-Arginine 5 mM; L-Glutamine 5 mM

sample_2: melanoregulin, [U-99% 13C; U-99% 15N], 0.150 mM; H2O 90%; D2O 10%; L-Arginine 5 mM; L-Glutamine 5 mM

sample_3: melanoregulin, U-15;U-13C;U-2H, 0.150 mM; H2O 90%; D2O 10%; L-Arginine 5 mM; L-Glutamine 5 mM

sample_4: melanoregulin, 15N/13C/2H/ILV-CH3, 0.150 mM; D2O 100%; L-Arginine 5 mM; L-Glutamine 5 mM

sample_5: melanoregulin, [U-99% 15N], 0.150 mM; H2O 90%; D2O 10%; L-Arginine 5 mM; L-Glutamine 5 mM

sample_conditions_1: ionic strength: 10 mM; pH: 6.3; pressure: 1 atm; temperature: 303 K

sample_conditions_2: ionic strength: 10 mM; pH: 6.3; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HN(CO)CACBsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HMCMCBCAsample_4isotropicsample_conditions_1
3D ILV-CH3 NOESYsample_4isotropicsample_conditions_1
2D IPAPsample_1anisotropicsample_conditions_2
1H_T2sample_5isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - data analysis

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

PIPP, Garrett - data analysis

TOPSPIN, Bruker Biospin - collection

XPLOR, G. Marius Clore , Guillermo Bermejo, , John Kuszewski, Charles D. Schwieters, and Nico Tjandra - structure calculation

NMR spectrometers:

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

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