BMRB Entry 18267

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18267

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Title:
Substrate-dependent millisecond domain motions in DNA polymerase beta
Deposition date:
2012-02-15
Original release date:
2012-03-27
Authors:
Loria, Patrick; Swain, Monalisa; Berlowy, Rebecca; Sweasy, Joann; Dalal, Shibani
Citation:

Citation: Berlow, Rebecca; Swain, Monalisa; Dalal, Shibani; Sweasy, Joann; Loria, J. Patrick. "Substrate-Dependent Millisecond Domain Motions in DNA Polymerase ."  J. Mol. Biol. 419, 171-182 (2012).
PubMed: 22446382

Assembly members:

Assembly members:
DNA_Polymerase_beta_polypeptide, polymer, 335 residues, Formula weight is not available

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: purified from the natural source   Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
DNA_Polymerase_beta_polypeptide: MSKRKAPQETLNGGITDMLV ELANFEKNVSQAIHKYNAYR KAASVIAKYPHKIKSGAEAK KLPGVGTKIAEKIDEFLATG KLRKLEKIRQDDTSSSINFL TRVTGIGPSAARKLVDEGIK TLEDLRKNEDKLNHHQRIGL KYFEDFEKRIPREEMLQMQD IVLNEVKKLDPEYIATVCGS FRRGAESSGDMDVLLTHPNF TSESSKQPKLLHRVVEQLQK VRFITDTLSKGETKFMGVCQ LPSENDENEYPHRRIDIRLI PKDQYYCGVLYFTGSDIFNK NMRAHALEKGFTINEYTIRP LGVTGVAGEPLPVDSEQDIF DYIQWRYREPKDRSE

Data sets:
Data typeCount
13C chemical shifts802
15N chemical shifts260
1H chemical shifts260

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DNA polymerase beta1

Entities:

Entity 1, DNA polymerase beta 335 residues - Formula weight is not available

1   METSERLYSARGLYSALAPROGLNGLUTHR
2   LEUASNGLYGLYILETHRASPMETLEUVAL
3   GLULEUALAASNPHEGLULYSASNVALSER
4   GLNALAILEHISLYSTYRASNALATYRARG
5   LYSALAALASERVALILEALALYSTYRPRO
6   HISLYSILELYSSERGLYALAGLUALALYS
7   LYSLEUPROGLYVALGLYTHRLYSILEALA
8   GLULYSILEASPGLUPHELEUALATHRGLY
9   LYSLEUARGLYSLEUGLULYSILEARGGLN
10   ASPASPTHRSERSERSERILEASNPHELEU
11   THRARGVALTHRGLYILEGLYPROSERALA
12   ALAARGLYSLEUVALASPGLUGLYILELYS
13   THRLEUGLUASPLEUARGLYSASNGLUASP
14   LYSLEUASNHISHISGLNARGILEGLYLEU
15   LYSTYRPHEGLUASPPHEGLULYSARGILE
16   PROARGGLUGLUMETLEUGLNMETGLNASP
17   ILEVALLEUASNGLUVALLYSLYSLEUASP
18   PROGLUTYRILEALATHRVALCYSGLYSER
19   PHEARGARGGLYALAGLUSERSERGLYASP
20   METASPVALLEULEUTHRHISPROASNPHE
21   THRSERGLUSERSERLYSGLNPROLYSLEU
22   LEUHISARGVALVALGLUGLNLEUGLNLYS
23   VALARGPHEILETHRASPTHRLEUSERLYS
24   GLYGLUTHRLYSPHEMETGLYVALCYSGLN
25   LEUPROSERGLUASNASPGLUASNGLUTYR
26   PROHISARGARGILEASPILEARGLEUILE
27   PROLYSASPGLNTYRTYRCYSGLYVALLEU
28   TYRPHETHRGLYSERASPILEPHEASNLYS
29   ASNMETARGALAHISALALEUGLULYSGLY
30   PHETHRILEASNGLUTYRTHRILEARGPRO
31   LEUGLYVALTHRGLYVALALAGLYGLUPRO
32   LEUPROVALASPSERGLUGLNASPILEPHE
33   ASPTYRILEGLNTRPARGTYRARGGLUPRO
34   LYSASPARGSERGLU

Samples:

sample_1: DNA_Polymerase_beta, [U-13C; U-15N; U-2H], 0.6 ± 0.2 mM; HEPES 50 ± 0.1 mM; potassium chloride 100 ± 0.1 mM; sodium azide 0.002 ± 0.1 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.001 M; pH: 7.4; pressure: 1 atm; temperature: 296 K

Experiments:

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

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 900 MHz
  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAC36630 BAE27405 BAE30399
GB AAA41900 AAA41901 AAB00389 AAH60998 AAH98668
REF NP_035260 NP_058837 XP_005066593 XP_005362476
SP P06766 Q8K409
AlphaFold P06766 Q8K409

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