BMRB Entry 30083

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PDB ID: 5jto
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30083
MolProbity Validation Chart

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Title:
The structure of chaperone SecB in complex with unstructured proPhoA binding site d
Deposition date:
2016-05-09
Original release date:
2016-08-18
Authors:
Huang, C.; Saio, T.; Rossi, P.; Kalodimos, C.
Citation:

Citation: Huang, C.; Saio, T.; Rossi, P.; Kalodimos, C.. "Structural basis for the antifolding activity of a molecular chaperone"  Nature 537, 202-206 (2016).
PubMed: 27501151

Assembly members:

Assembly members:
Protein-export protein SecB, polymer, 155 residues, 17287.266 Da.
Alkaline phosphatase, polymer, 40 residues, 4325.987 Da.

Natural source:

Natural source:   Common Name: enterobacteria   Taxonomy ID: 83334   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Protein-export protein SecB: MSEQNNTEMTFQIQRIYTKD ISFEAPNAPHVFQKDWQPEV KLDLDTASSQLADDVYEVVL RVTVTASLGEETAFLCEVQQ GGIFSIAGIEGTQMAHCLGA YCPNILFPYARECITSMVSR GTFPQLNLAPVNFDALFMNY LQQQAGEGTEEHQDA
Alkaline phosphatase: ANQQKPLLGLFADGNMPVRW LGPKATYHGNIDKPAVTCTP

Data typeCount
13C chemical shifts2362
15N chemical shifts666
1H chemical shifts2050

Additional metadata:

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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_1, chain 11
2entity_1, chain 21
3entity_1, chain 31
4entity_1, chain 41
5entity_2, chain 12
6entity_2, chain 22
7entity_2, chain 32
8entity_2, chain 42

Entities:

Entity 1, entity_1, chain 1 155 residues - 17287.266 Da.

1   METSERGLUGLNASNASNTHRGLUMETTHR
2   PHEGLNILEGLNARGILETYRTHRLYSASP
3   ILESERPHEGLUALAPROASNALAPROHIS
4   VALPHEGLNLYSASPTRPGLNPROGLUVAL
5   LYSLEUASPLEUASPTHRALASERSERGLN
6   LEUALAASPASPVALTYRGLUVALVALLEU
7   ARGVALTHRVALTHRALASERLEUGLYGLU
8   GLUTHRALAPHELEUCYSGLUVALGLNGLN
9   GLYGLYILEPHESERILEALAGLYILEGLU
10   GLYTHRGLNMETALAHISCYSLEUGLYALA
11   TYRCYSPROASNILELEUPHEPROTYRALA
12   ARGGLUCYSILETHRSERMETVALSERARG
13   GLYTHRPHEPROGLNLEUASNLEUALAPRO
14   VALASNPHEASPALALEUPHEMETASNTYR
15   LEUGLNGLNGLNALAGLYGLUGLYTHRGLU
16   GLUHISGLNASPALA

Entity 2, entity_2, chain 1 40 residues - 4325.987 Da.

1   ALAASNGLNGLNLYSPROLEULEUGLYLEU
2   PHEALAASPGLYASNMETPROVALARGTRP
3   LEUGLYPROLYSALATHRTYRHISGLYASN
4   ILEASPLYSPROALAVALTHRCYSTHRPRO

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