BMRB Entry 7122

Title:
Structural Studies of MJ1529, an O6 Methylguanine DNA Methyltransferase
Deposition date:
2006-05-18
Original release date:
2007-01-11
Authors:
Roberts, A.
Citation:

Citation: Roberts, A.; Pelton, J.; Wemmer, D.. "Structural Studies of MJ1529, an O6 Methylguanine DNA Methyltransferase"  Magn. Reson. Chem. 44, S71-S82 (2006).
PubMed: 16826543

Assembly members:

Assembly members:
Methylated-DNA--protein-cysteine methyltransferase (E.C.2.1.1.63), polymer, 167 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Methanocaldococcus jannaschii   Taxonomy ID: 2190   Superkingdom: Archaea   Kingdom: not available   Genus/species: Methanococcus jannaschii

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts580
15N chemical shifts147
1H chemical shifts920
coupling constants101

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Methylated-DNA--protein-cysteine methyltransferase1

Entities:

Entity 1, Methylated-DNA--protein-cysteine methyltransferase 167 residues - Formula weight is not available

1   METILEILEGLNILEGLUGLUTYRPHEILE
2   GLYMETILEPHELYSGLYASNGLNLEUVAL
3   ARGASNTHRILEPROLEUARGARGGLUGLU
4   ILEPHEASNPHEMETASPGLYGLUVALVAL
5   SERASNPROGLUASPGLUHISLEULYSVAL
6   ALAGLUILEILELEULYSLEUTYRPHEALA
7   GLUILEASPASPLYSLYSVALARGGLULEU
8   ILESERTYRLYSLEUGLUVALPROGLUPHE
9   THRLYSLYSVALLEUASPILEVALLYSASP
10   ILEGLUPHEGLYLYSTHRLEUTHRTYRGLY
11   ASPILEALALYSLYSLEUASNTHRSERPRO
12   ARGALAVALGLYMETALALEULYSARGASN
13   PROLEUPROLEUILEILEPROCYSHISARG
14   VALVALALALYSASNSERLEUGLYGLYTYR
15   SERTYRGLYLEUASPLYSLYSLYSPHEILE
16   LEUGLUARGGLUARGLEUASNMETVALSER
17   PHELYSPHEASNLYSVALTYR

Samples:

sample_1: Methylated-DNA--protein-cysteine methyltransferase (E.C.2.1.1.63), [U-15N], 0.8 mM; sodium phosphate 50 mM; NaCl 500 mM; H2O 95%; D2O 5%

sample_2: Methylated-DNA--protein-cysteine methyltransferase (E.C.2.1.1.63), [U-13C; U-15N], 0.8 mM; sodium phosphate 50 mM; NaCl 500 mM; H2O 95%; D2O 5%

sample_3: Methylated-DNA--protein-cysteine methyltransferase (E.C.2.1.1.63), [U-15N], 0.8 mM; sodium phosphate 50 mM; NaCl 500 mM; D2O 100%

sample_4: Methylated-DNA--protein-cysteine methyltransferase (E.C.2.1.1.63), [U-13C], 0.8 mM; sodium phosphate 50 mM; NaCl 500 mM; H2O 94%; D2O 5%

sample_cond_1: ionic strength: 550 mM; pH: 6.2; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYnot availablenot availablesample_cond_1
HNHAnot availablenot availablesample_cond_1
4D 13C Separated NOESYnot availablenot availablesample_cond_1
4D 13C/15N Separated NOESYnot availablenot availablesample_cond_1
D20 Exchangenot availablenot availablesample_cond_1
3d 13C Separated NOESYnot availablenot availablesample_cond_1

Software:

CNS v1.1 - refinement, structure solution

NMRPipe v1 - processing

NMRView v5.0.4 - data analysis

NMR spectrometers:

  • Bruker DRX 500 MHz

Related Database Links:

PDB
GB AAB99547
REF NP_248537 WP_010871053
SP Q58924
AlphaFold Q58924

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