BMRB Entry 27615

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27615

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Title:
Backbone and aliphatic side-chain NMR resonance assignments of fragment of human LSD1 (residues 100-151)
Deposition date:
2018-09-18
Original release date:
2024-04-01
Authors:
Zeng, Danyun; Brown, Benjamin; Reiter, Nicholas
Citation:

Citation: Zeng, Danyun; Brown, Benjamin; Luka, Zigmund; Martin, Bill; Moore, Khadijah; Pakhomova, Svetlana; Meiler, Jens; Reiter, Nicholas. "Transient and highly ordered structural domains exist within the N-terminus of LSD1 and contain distinct binding interactions with mononucleosomes"  Nucleic Acids Res. ., .-..

Assembly members:

Assembly members:
fragment_of_human_LSD1_(residues_100-151), polymer, 56 residues, Formula weight is not available

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: pAT109

Entity Sequences (FASTA):

Entity Sequences (FASTA):
fragment_of_human_LSD1_(residues_100-151): GPGSGIAETPEGRRTSRRKR AKVEYREMDESLANLSEDEY YSEEERNAKAEKEKKL

Data sets:
Data typeCount
13C chemical shifts212
15N chemical shifts49
1H chemical shifts339

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Fragment of human LSD1 (residues 100-151)1

Entities:

Entity 1, Fragment of human LSD1 (residues 100-151) 56 residues - Formula weight is not available

Residue No.1-4(author sequence No.-3-0)represent the reconstruction generated residues.

1   GLYPROGLYSERGLYILEALAGLUTHRPRO
2   GLUGLYARGARGTHRSERARGARGLYSARG
3   ALALYSVALGLUTYRARGGLUMETASPGLU
4   SERLEUALAASNLEUSERGLUASPGLUTYR
5   TYRSERGLUGLUGLUARGASNALALYSALA
6   GLULYSGLULYSLYSLEU

Samples:

sample_1: N-terminal fragment of Human LSD1, [U-100% 13C; U-100% 15N], 250 uM; HEPES 10 mM; potassium chloride 50 mM; DSS 50 uM; D2O, [U-99% 2H], 10 % v/v

sample_conditions_1: ionic strength: 10 mM; pH: 7.2; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

CARA v1.9.1.4, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Varian VNMRS 800 MHz
  • Bruker Avance 600 MHz
  • Varian INOVA 600 MHz

Related Database Links:

UNP KDM1A

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