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 25312

Title: SOLUTION STRUCTURE OF HUMAN MBD1 CXXC1 DOMAIN   PubMed: 26354109

Authors: Thomson, Ross; Smith, Brian

Citation: Thomson, Ross; Smith, Brian. "Solution structure of human MBD1 CXXC1"  J. Biomol. NMR 63, 309-314 (2015).

Assembly members:
MBD1_CXXC1, polymer, 61 residues, 6673.7301 Da.
entity_ZN, non-polymer, 65.409 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

Entity Sequences (FASTA):
MBD1_CXXC1: GPLGSEQRMFKRVGCGECAA CQVTEDCGACSTCLLQLPHD VASGLFCKCERRRCLRIVER S

Data typeCount
15N chemical shifts62
1H chemical shifts344
T1 relaxation values55
T2 relaxation values53

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MBD1 CXXC11
2ZINC ION2

Entities:

Entity 1, MBD1 CXXC1 61 residues - 6673.7301 Da.

1   GLYPROLEUGLYSERGLUGLNARGMETPHE
2   LYSARGVALGLYCYSGLYGLUCYSALAALA
3   CYSGLNVALTHRGLUASPCYSGLYALACYS
4   SERTHRCYSLEULEUGLNLEUPROHISASP
5   VALALASERGLYLEUPHECYSLYSCYSGLU
6   ARGARGARGCYSLEUARGILEVALGLUARG
7   SER

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

MBD1_CXXC1_1: MBD1_CXXC1, [U-15N], 1.0 mM; NaCl 250.0 mM; tris(hydroxymethyl)aminomethane 10.0 mM

sample_new_1: MBD1_CXXC1, [U-13C; U-15N], 0.0010000 M; NaCl 250.0 mM; tris(hydroxymethyl)aminomethane 10.0 mM

MBD1_CXXC1_2: ionic strength: 0.250 M; pH: 7.500; pressure: 1.000 atm; temperature: 293.000 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYMBD1_CXXC1_1isotropicMBD1_CXXC1_2
2D 1H-1H TOCSYMBD1_CXXC1_1isotropicMBD1_CXXC1_2
2D 1H-15N HSQC/HMQCMBD1_CXXC1_1isotropicMBD1_CXXC1_2
3D 1H-15N TOCSYMBD1_CXXC1_1isotropicMBD1_CXXC1_2
2D 1H-1H NOESYMBD1_CXXC1_1isotropicMBD1_CXXC1_2
2D 1H-1H NOESYMBD1_CXXC1_1isotropicMBD1_CXXC1_2
3D 1H-15N NOESYMBD1_CXXC1_1isotropicMBD1_CXXC1_2
T2 (H[n[T2(N)]])MBD1_CXXC1_1isotropicMBD1_CXXC1_2
T1 (H[n[T1(N)]])MBD1_CXXC1_1isotropicMBD1_CXXC1_2
HNHA (H{[N]+[HA]})MBD1_CXXC1_1isotropicMBD1_CXXC1_2
3D HNHBMBD1_CXXC1_1isotropicMBD1_CXXC1_2
2D 1H-15N HSQC/HMQCMBD1_CXXC1_1isotropicMBD1_CXXC1_2
2D 1H-15N HSQC/HMQCMBD1_CXXC1_1isotropicMBD1_CXXC1_2
HNHBsample_new_1solutionMBD1_CXXC1_2

Software:

ARIA v2.3, Bioinformatique Structurale - structure calculation

AutoDep v4.3, PDBe - collection

CCPNMR_Analysis v1.0, CCPN - assignment of spectra

CNS v1.2, BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,READ, RICE,SIMONSON,WARREN - Structure calculation

Topsin v1.3, Bruker - data collection

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz
  • Bruker AVANCE 600 MHz

Related Database Links:

UniProt CF552871.1
UNP MBD1_HUMAN