BMRB Entry 50270

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50270

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Title:
Cre Recombinase Catalytic Domain
Deposition date:
2020-05-12
Original release date:
2021-08-11
Authors:
Unnikrishnan, Aparna; Foster, Mark
Citation:

Citation: Unnikrishnan, Aparna; Amero, Carlos; Yadav, Deepak Kumar; Stachowski, Kye; Potter, Devante; Foster, Mark. "DNA binding induces a cis-to- trans switch in Cre recombinase to enable intasome assembly"  Proc. Natl. Acad. Sci. U. S. A. 117, 24849-24858 (2020).
PubMed: 32968014

Assembly members:

Assembly members:
entity_1, polymer, 217 residues, 23814.1 Da.

Natural source:

Natural source:   Common Name: Escherichia virus P1   Taxonomy ID: 10678   Superkingdom: Viruses   Kingdom: not available   Genus/species: Punavirus Bacteriophage P1

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: AGERAKQALAFERTDFDQVR SLMENSDRCQDIRNLAFLGI AYNTLLRIAEIARIRVKDIS RTDGGRMLIHIGRTKTLVST AGVEKALSLGVTKLVERWIS VSGVADDPNNYLFCRVRKNG VAAPSATSQLSTRALEGIFE ATHRLIYGAKDDSGQRYLAW SGHSARVGAARDMARAGVSI PEIMQAGGWTNVNIVMNYIR NLDSETGAMVRLLEDGD

Data sets:
Data typeCount
13C chemical shifts595
15N chemical shifts196
1H chemical shifts362

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Cre Recombinase Catalytic DomainCre Recombinase Catalytic Domain1

Entities:

Entity 1, Cre Recombinase Catalytic DomainCre Recombinase Catalytic Domain 217 residues - 23814.1 Da.

Residue numbers 127 to 343 in Cre Recombinase

1   ALAGLYGLUARGALALYSGLNALALEUALA
2   PHEGLUARGTHRASPPHEASPGLNVALARG
3   SERLEUMETGLUASNSERASPARGCYSGLN
4   ASPILEARGASNLEUALAPHELEUGLYILE
5   ALATYRASNTHRLEULEUARGILEALAGLU
6   ILEALAARGILEARGVALLYSASPILESER
7   ARGTHRASPGLYGLYARGMETLEUILEHIS
8   ILEGLYARGTHRLYSTHRLEUVALSERTHR
9   ALAGLYVALGLULYSALALEUSERLEUGLY
10   VALTHRLYSLEUVALGLUARGTRPILESER
11   VALSERGLYVALALAASPASPPROASNASN
12   TYRLEUPHECYSARGVALARGLYSASNGLY
13   VALALAALAPROSERALATHRSERGLNLEU
14   SERTHRARGALALEUGLUGLYILEPHEGLU
15   ALATHRHISARGLEUILETYRGLYALALYS
16   ASPASPSERGLYGLNARGTYRLEUALATRP
17   SERGLYHISSERALAARGVALGLYALAALA
18   ARGASPMETALAARGALAGLYVALSERILE
19   PROGLUILEMETGLNALAGLYGLYTRPTHR
20   ASNVALASNILEVALMETASNTYRILEARG
21   ASNLEUASPSERGLUTHRGLYALAMETVAL
22   ARGLEULEUGLUASPGLYASP

Samples:

sample_1: Cre Recombinase Catalytic Domain, [U-100% 13C; U-100% 15N], 750 uM; TRIS, [U-100% 2H], 10 mM; sodium chloride 100 mM; DSS 0.66 mM; sodium azide 0.02%; H2O 95%; D2O, [U-99% 2H], 5%

sample_conditions_1: pH: 7; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D Tr HNCOsample_1isotropicsample_conditions_1
3D Tr HN(CO)CAsample_1isotropicsample_conditions_1
3D Tr HN(CA)COsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HA(CO)NHsample_1isotropicsample_conditions_1

Software:

NMRViewJ - chemical shift assignment, data analysis, processing

NMRFx Processor - chemical shift assignment, data analysis, processing

CARA - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

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