BMRB Entry 34552

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PDB ID: 7a2d
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34552
MolProbity Validation Chart

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Title:
Structure-function analyses of dual-BON domain protein DolP identifies phospholipid binding as a new mechanism for protein localisation to the cell division site
Deposition date:
2020-08-17
Original release date:
2020-12-26
Authors:
Morris, F.; Knowles, T.; Maderbocus, R.; Jeeves, M.; Kirwan, J.; Heinz, E.; Wells, T.; Browning, D.; Sevastsyanovich, Y.; Leyton, D.; Rossiter, A.; Bavro, V.; Sridhar, P.; Ward, D.; Shimwell, N.; Martin, A.; Sahl, J.; Wardius, C.; Walker, D.; Lithgow, T.; Viant, M.; Rasko, D.; Cunningham, A.; Overduin, M.; Henderson, I.
Citation:

Citation: Bryant, Jack Alfred; Morris, Faye; Knowles, Timothy; Maderbocus, Riyaz; Heinz, Eva; Boelter, Gabriela; Alodaini, Dema; Colyer, Adam; Wotherspoon, Peter; Staunton, Kara; Jeeves, Mark; Browning, Douglas; Sevastsyanovich, Yanina; Wells, Timothy; Rossiter, Amanda; Bavro, Vassiliy; Sridhar, Pooja; Ward, Douglas; Chong, Zhi-Soon; Goodall, Emily Ca; Icke, Christopher; Teo, Alvin Ck; Chng, Shu-Sin; Roper, David; Lithgow, Trevor; Cunningham, Adam; Banzhaf, Manuel; Overduin, Michael; Henderson, Ian. "Structure of dual BON-domain protein DolP identifies phospholipid binding as a new mechanism for protein localisation"  Elife 9, .-. (2020).
PubMed: 33315009

Assembly members:

Assembly members:
entity_1, polymer, 182 residues, 19324.738 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 1169330   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: PET26B

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: IAAAVVGTAAVGTKAATDPR SVGTQVDDGTLEVRVNSALS KDEQIKKEARINVTAYQGKV LLVGQSPNAELSARAKQIAM GVDGANEVYNEIRQGQPIGL GEASNDTWITTKVRSQLLTS DLVKSSNVKVTTENGEVFLM GLVTEREAKAAADIASRVSG VKRVTTAFTFIKGGLEHHHH HH

Data typeCount
13C chemical shifts686
15N chemical shifts172
1H chemical shifts1023

Additional metadata:

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Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 182 residues - 19324.738 Da.

1   ILEALAALAALAVALVALGLYTHRALAALA
2   VALGLYTHRLYSALAALATHRASPPROARG
3   SERVALGLYTHRGLNVALASPASPGLYTHR
4   LEUGLUVALARGVALASNSERALALEUSER
5   LYSASPGLUGLNILELYSLYSGLUALAARG
6   ILEASNVALTHRALATYRGLNGLYLYSVAL
7   LEULEUVALGLYGLNSERPROASNALAGLU
8   LEUSERALAARGALALYSGLNILEALAMET
9   GLYVALASPGLYALAASNGLUVALTYRASN
10   GLUILEARGGLNGLYGLNPROILEGLYLEU
11   GLYGLUALASERASNASPTHRTRPILETHR
12   THRLYSVALARGSERGLNLEULEUTHRSER
13   ASPLEUVALLYSSERSERASNVALLYSVAL
14   THRTHRGLUASNGLYGLUVALPHELEUMET
15   GLYLEUVALTHRGLUARGGLUALALYSALA
16   ALAALAASPILEALASERARGVALSERGLY
17   VALLYSARGVALTHRTHRALAPHETHRPHE
18   ILELYSGLYGLYLEUGLUHISHISHISHIS
19   HISHIS

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