BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 19526

Title: Solution NMR structure of SLED domain of Scml2   PubMed: 24727478

Deposition date: 2013-09-24 Original release date: 2014-04-22

Authors: Bezsonova, Irina

Citation: Bezsonova, Irina. "Solution NMR Structure of the DNA-binding Domain from Scml2 (Sex Comb onMidleg-like 2)"  J. Biol. Chem. ., .-. (2014).

Assembly members:
SLED_Scml2, polymer, 119 residues, 13112.994 Da.

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: pET28b

Entity Sequences (FASTA):
SLED_Scml2: GSHMMSTVCVYVNKHGNFGP HLDPKRIQQLPDHFGPGPVN VVLRRIVQACVDCALETKTV FGYLKPDNRGGEVITASFDG ETHSIQLPPVNSASFALRFL ENFCHSLQCDNLLSSQPFS

Data sets:
Data typeCount
13C chemical shifts468
15N chemical shifts115
1H chemical shifts759

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SLED domain of Scml21

Entities:

Entity 1, SLED domain of Scml2 119 residues - 13112.994 Da.

1   GLYSERHISMETMETSERTHRVALCYSVAL
2   TYRVALASNLYSHISGLYASNPHEGLYPRO
3   HISLEUASPPROLYSARGILEGLNGLNLEU
4   PROASPHISPHEGLYPROGLYPROVALASN
5   VALVALLEUARGARGILEVALGLNALACYS
6   VALASPCYSALALEUGLUTHRLYSTHRVAL
7   PHEGLYTYRLEULYSPROASPASNARGGLY
8   GLYGLUVALILETHRALASERPHEASPGLY
9   GLUTHRHISSERILEGLNLEUPROPROVAL
10   ASNSERALASERPHEALALEUARGPHELEU
11   GLUASNPHECYSHISSERLEUGLNCYSASP
12   ASNLEULEUSERSERGLNPROPHESER

Samples:

sample_1: SLED_Scml2, [U-100% 13C; U-100% 15N], 0.3 – 1.0 mM; HEPES 50 mM; NaCl 250 mM; DTT 2 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 250 mM; pH: 7.2; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

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

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAG61234 BAG64181
EMBL CAB38943
GB AAH51913 AAH64617 ABM54391 ABM67362 EAW98937
REF NP_001248288 NP_006080 XP_003819585 XP_003924181 XP_004063918
SP Q9UQR0
AlphaFold Q9UQR0

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