BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17171

Title: The chemical shift assignment of the SWIRM domain of LSD1

Deposition date: 2010-09-08 Original release date: 2012-08-01

Authors: LIU, Changdong; LO, Ka Ching; ZHU, Guang; SZE, Kong Hung

Citation: LIU, Changdong; LUO, Raymond; SZE, Kong Hung. "The chemical shift assignment of the SWIRM domain of LSD1"  The BMRB entry is the only known published source for the data..

Assembly members:
SWIRM, polymer, 102 residues, Formula weight is not available

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   Vector: pGex-4T

Entity Sequences (FASTA):
SWIRM: GSVEGAAFQSRLPHDRMTSQ EAACFPDIISGPQQTQKVFL FIRNRTLQLWLDNPKIQLTF EATLQQLEAPYNSDTVLVHR VHSYLERHGLINFGIYKRIK PL

Data sets:
Data typeCount
13C chemical shifts370
15N chemical shifts89
1H chemical shifts678

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SWIRM1

Entities:

Entity 1, SWIRM 102 residues - Formula weight is not available

1   GLYSERVALGLUGLYALAALAPHEGLNSER
2   ARGLEUPROHISASPARGMETTHRSERGLN
3   GLUALAALACYSPHEPROASPILEILESER
4   GLYPROGLNGLNTHRGLNLYSVALPHELEU
5   PHEILEARGASNARGTHRLEUGLNLEUTRP
6   LEUASPASNPROLYSILEGLNLEUTHRPHE
7   GLUALATHRLEUGLNGLNLEUGLUALAPRO
8   TYRASNSERASPTHRVALLEUVALHISARG
9   VALHISSERTYRLEUGLUARGHISGLYLEU
10   ILEASNPHEGLYILETYRLYSARGILELYS
11   PROLEU

Samples:

sample_1: SWIRM, [U-100% 13C; U-100% 15N], 0.8 mM; sodium phosphate 50 mM; sodium chloride 50 mM; DTT 2 mM; EDTA 1 mM; H2O 90%; D2O 10%

sample_2: SWIRM 0.8 mM; sodium phosphate 50 mM; sodium chloride 50 mM; DTT 2 mM; EDTA 1 mM; D2O 100%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - data analysis, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 750 MHz

Related Database Links:

BMRB 10011
PDB
DBJ BAA25527 BAC97980 BAF83017 BAG09773
EMBL CAH90077
GB AAH16639 AAH40194 AAH48134 AAH59885 AAI51757
REF NP_001009999 NP_001106157 NP_001123570 NP_001252568 NP_055828
SP O60341 Q6ZQ88
TPG DAA32187 DAA32188
AlphaFold O60341 Q6ZQ88

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