BMRB Entry 15170

Title:
Backbone assignments of DNA methyltransferase M.HhaI
Deposition date:
2007-03-09
Original release date:
2007-06-06
Authors:
Zhou, Hongjun; Shatz, Whitney; Purdy, Matthew; Fera, Nick; Dahlquist, Frederick; Reich, Norbert
Citation:

Citation: Zhou, Hongjun; Shatz, Whitney; Purdy, Matthew; Fera, Nick; Dahlquist, Frederick; Reich, Norbert. "Long-range structural and dynamical changes induced by cofactor binding in DNA methyltransferase M.HhaI."  Biochemistry 46, 7261-7268 (2007).
PubMed: 17523600

Assembly members:

Assembly members:
M.HhaI, polymer, 331 residues, Formula weight is not available
SAH, non-polymer, 384.411 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Data sets:
Data typeCount
13C chemical shifts483
15N chemical shifts242
1H chemical shifts242

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1monomer1
2SAH2

Entities:

Entity 1, monomer 331 residues - Formula weight is not available

1   METILEGLUILELYSASPLYSGLNLEUTHR
2   GLYLEUARGPHEILEASPLEUPHEALAGLY
3   LEUGLYGLYPHEARGLEUALALEUGLUSER
4   CYSGLYALAGLUCYSVALTYRSERASNGLU
5   TRPASPLYSTYRALAGLNGLUVALTYRGLU
6   METASNPHEGLYGLULYSPROGLUGLYASP
7   ILETHRGLNVALASNGLULYSTHRILEPRO
8   ASPHISASPILELEUCYSALAGLYPHEPRO
9   CYSGLNALAPHESERILESERGLYLYSGLN
10   LYSGLYPHEGLUASPSERARGGLYTHRLEU
11   PHEPHEASPILEALAARGILEVALARGGLU
12   LYSLYSPROLYSVALVALPHEMETGLUASN
13   VALLYSASNPHEALASERHISASPASNGLY
14   ASNTHRLEUGLUVALVALLYSASNTHRMET
15   ASNGLULEUASPTYRSERPHEHISALALYS
16   VALLEUASNALALEUASPTYRGLYILEPRO
17   GLNLYSARGGLUARGILETYRMETILECYS
18   PHEARGASNASPLEUASNILEGLNASNPHE
19   GLNPHEPROLYSPROPHEGLULEUASNTHR
20   PHEVALLYSASPLEULEULEUPROASPSER
21   GLUVALGLUHISLEUVALILEASPARGLYS
22   ASPLEUVALMETTHRASNGLNGLUILEGLU
23   GLNTHRTHRPROLYSTHRVALARGLEUGLY
24   ILEVALGLYLYSGLYGLYGLNGLYGLUARG
25   ILETYRSERTHRARGGLYILEALAILETHR
26   LEUSERALATYRGLYGLYGLYILEPHEALA
27   LYSTHRGLYGLYTYRLEUVALASNGLYLYS
28   THRARGLYSLEUHISPROARGGLUCYSALA
29   ARGVALMETGLYTYRPROASPSERTYRLYS
30   VALHISPROSERTHRSERGLNALATYRLYS
31   GLNPHEGLYASNSERVALVALILEASNVAL
32   LEUGLNTYRILEALATYRASNILEGLYSER
33   SERLEUASNLEUGLUHISHISHISHISHIS
34   HIS

Entity 2, SAH - C14 H20 N6 O5 S - 384.411 Da.

1   SAH

Samples:

sample_1: M.HhaI, [U-13C; U-15N; U-2H], 0.3 – 0.6 mM; sodium phosphate 50 mM; DTT 5 mM; sodium chloride 100 mM; Arg 50 mM; Glu 50 mM; sodium azide 0.02%; glycerol 0.75%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1

Software:

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

ANSIG, Kraulis - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 16395
PDB
GB AAA24989 EIJ69210
REF WP_005706946
SP P05102
AlphaFold P05102

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