BMRB Entry 18095

Title:
Solution NMR Structure of Lysine-specific demethylase lid from Drosophila melanogaster, Northeast Structural Genomics Consortium Target FR824D
Deposition date:
2011-11-18
Original release date:
2011-12-01
Authors:
Mills, Jeffrey; Lee, Dan; Kohan, Eitan; Sahdev, Seema; Acton, T.; Xiao, R.; Everett, J.; Montelione, G.; Szyperski, Thomas
Citation:

Citation: Mills, Jeffrey; Lee, Dan; Kohan, Eitan; Sahdev, Seema; Acton, T.; Xiao, R.; Everett, J.; Montelione, G.; Szyperski, Thomas. "Northeast Structural Genomics Consortium Target FR824D"  To be published ., .-..

Assembly members:

Assembly members:
FR824D, polymer, 107 residues, 12493.614 Da.

Natural source:

Natural source:   Common Name: fruit fly   Taxonomy ID: 7227   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Drosophila melanogaster

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15Nano6HT_NESG

Data sets:
Data typeCount
13C chemical shifts464
15N chemical shifts112
1H chemical shifts748

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FR824D1

Entities:

Entity 1, FR824D 107 residues - 12493.614 Da.

1   PROARGVALGLNARGLEUASNGLULEUGLU
2   ALALYSTHRARGVALLYSLEUASNPHELEU
3   ASPGLNILEALALYSPHETRPGLULEUGLN
4   GLYSERSERLEULYSILEPROMETVALGLU
5   ARGLYSALALEUASPLEUTYRTHRLEUHIS
6   ARGILEVALGLNGLUGLUGLYGLYMETGLU
7   GLNTHRTHRLYSASPARGLYSTRPALALYS
8   VALALAASNARGMETGLNTYRPROSERSER
9   LYSSERVALGLYALATHRLEULYSALAHIS
10   TYRGLUARGILELEUHISPROPHEGLUVAL
11   TYRTHRSERGLYLYSVALLEU

Samples:

sampleNC: FR824D, [U-100% 13C; U-100% 15N], 1.1 mM; sodium chloride 100 mM; DTT 5 mM; sodium azide 0.02%; TRIS 10 mM

sampleNC5: FR824D, [U-5% 13C; U-100% 15N], 1.3 mM; sodium chloride 100 mM; DTT 5 mM; sodium azide 0.02%; TRIS 10 mM

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsampleNCisotropicsample_conditions_1
3D HNCOsampleNCisotropicsample_conditions_1
3D CBCA(CO)NHsampleNCisotropicsample_conditions_1
3D HNCACBsampleNCisotropicsample_conditions_1
3D HCCH-COSYsampleNCisotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYsampleNCisotropicsample_conditions_1
2D 1H-13C HSQCsampleNC5isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsampleNCisotropicsample_conditions_1
2D 1H-13C HSQC aromaticsampleNCisotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization

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

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis,refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

PROSA, Guntert - processing

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

VNMRJ, Varian - collection

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
GB AAF52319 AAM11379 AAN10569 AFH03582 AFH03583
REF NP_001245908 NP_001245909 NP_001245910 NP_001285649 NP_523486
SP Q9VMJ7
AlphaFold Q9VMJ7

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