BMRB Entry 36119

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36119
MolProbity Validation Chart

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Title:
Solution Structure of the DISC1/Ndel1 complex
Deposition date:
2017-10-02
Original release date:
2018-02-06
Authors:
Ye, F.; Yu, C.; Yu, C.; Zhang, M.
Citation:

Citation: Ye, Fei; Kang, Eunchai; Yu, Chuan; Qian, Xuyu; Jacob, Fadi; Yu, Cong; Mao, Mao; Poon, Randy; Kim, Jieun; Song, Hongjun; Ming, Guo-Li; Zhang, Mingjie. "DISC1 Regulates Neurogenesis via Modulating Kinetochore Attachment of Ndel1/Nde1 during Mitosis."  Neuron 96, 1041-1054 (2017).
PubMed: 29103808

Assembly members:

Assembly members:
Disrupted in schizophrenia 1 homolog,Nuclear distribution protein nudE-like 1, polymer, 145 residues, 15455.417 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 'BL21-Gold(DE3)pLysS AG'

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Disrupted in schizophrenia 1 homolog,Nuclear distribution protein nudE-like 1: GSEFGPWKEDSHIVSAEVGE KCEAIGVKLLHLEDQLLGAM YSHDEALFQSLQGELQTVKE TLQAMILQLQPTKEAGEASA SYPTAGAQETEALVPRGSGF GTSPLTPSARISALNIVGDL LRKVGALESKLAACRNFAKD QASRK

Data sets:
Data typeCount
13C chemical shifts434
15N chemical shifts132
1H chemical shifts921

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 145 residues - 15455.417 Da.

1   GLYSERGLUPHEGLYPROTRPLYSGLUASP
2   SERHISILEVALSERALAGLUVALGLYGLU
3   LYSCYSGLUALAILEGLYVALLYSLEULEU
4   HISLEUGLUASPGLNLEULEUGLYALAMET
5   TYRSERHISASPGLUALALEUPHEGLNSER
6   LEUGLNGLYGLULEUGLNTHRVALLYSGLU
7   THRLEUGLNALAMETILELEUGLNLEUGLN
8   PROTHRLYSGLUALAGLYGLUALASERALA
9   SERTYRPROTHRALAGLYALAGLNGLUTHR
10   GLUALALEUVALPROARGGLYSERGLYPHE
11   GLYTHRSERPROLEUTHRPROSERALAARG
12   ILESERALALEUASNILEVALGLYASPLEU
13   LEUARGLYSVALGLYALALEUGLUSERLYS
14   LEUALAALACYSARGASNPHEALALYSASP
15   GLNALASERARGLYS

Samples:

sample_4: DISC1_Ndel1 0.8 mM; NaCl 50 mM; D2O, [U-2H], 100%

sample_1: DISC1_Ndel1, [U-99% 13C; U-99% 15N], 0.8 mM; NaCl 50 mM; D2O, U-2H, 100%

sample_2: DISC1_Ndel1, [U-99% 15N], 0.8 mM; NaCl 50 mM; H2O 90%; D2O, [U-2H], 10%

sample_3: DISC1_Ndel1, [U-99% 13C; U-99% 15N], 0.8 mM; NaCl 50 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_4anisotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1

Software:

CNS, Brunger A. T. et.al., Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure calculation

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 800 MHz

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