BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 30080

Title: The structure of chaperone SecB in complex with unstructured proPhoA   PubMed: 27501151

Deposition date: 2016-05-09 Original release date: 2016-08-18

Authors: Huang, C.; Saio, T.; Rossi, P.; Kalodimos, C.

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

Assembly members:
Protein-export protein SecB, polymer, 155 residues, 17287.266 Da.
Alkaline phosphatase, polymer, 471 residues, 49492.367 Da.

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

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

Entity Sequences (FASTA):
Protein-export protein SecB: MSEQNNTEMTFQIQRIYTKD ISFEAPNAPHVFQKDWQPEV KLDLDTASSQLADDVYEVVL RVTVTASLGEETAFLCEVQQ GGIFSIAGIEGTQMAHCLGA YCPNILFPYARECITSMVSR GTFPQLNLAPVNFDALFMNY LQQQAGEGTEEHQDA
Alkaline phosphatase: MKQSTIALALLPLLFTPVTK ARTPEMPVLENRAAQGDITA PGGARRLTGDQTAALRDSLS DKPAKNIILLIGDGMGDSEI TAARNYAEGAGGFFKGIDAL PLTGQYTHYALNKKTGKPDY VTDSAASATAWSTGVKTYNG ALGVDIHEKDHPTILEMAKA AGLATGNVSTAELQDATPAA LVAHVTSRKCYGPSATSEKC PGNALEKGGKGSITEQLLNA RADVTLGGGAKTFAETATAG EWQGKTLREQAQARGYQLVS DAASLNSVTEANQQKPLLGL FADGNMPVRWLGPKATYHGN IDKPAVTCTPNPQRNDSVPT LAQMTDKAIELLSKNEKGFF LQVEGASIDKQDHAANPCGQ IGETVDLDEAVQRALEFAKK EGNTLVIVTADHAHASQIVA PDTKAPGLTQALNTKDGAVM VMSYGNSEEDSQEHTGSQLR IAAYGPHAANVVGLTDQTDL FYTMKAALGLK

Data typeCount
13C chemical shifts3011
15N chemical shifts926
1H chemical shifts2479

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_1, chain 11
2entity_1, chain 21
3entity_1, chain 31
4entity_1, chain 41
5entity_22

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_2 471 residues - 49492.367 Da.

1   METLYSGLNSERTHRILEALALEUALALEU
2   LEUPROLEULEUPHETHRPROVALTHRLYS
3   ALAARGTHRPROGLUMETPROVALLEUGLU
4   ASNARGALAALAGLNGLYASPILETHRALA
5   PROGLYGLYALAARGARGLEUTHRGLYASP
6   GLNTHRALAALALEUARGASPSERLEUSER
7   ASPLYSPROALALYSASNILEILELEULEU
8   ILEGLYASPGLYMETGLYASPSERGLUILE
9   THRALAALAARGASNTYRALAGLUGLYALA
10   GLYGLYPHEPHELYSGLYILEASPALALEU
11   PROLEUTHRGLYGLNTYRTHRHISTYRALA
12   LEUASNLYSLYSTHRGLYLYSPROASPTYR
13   VALTHRASPSERALAALASERALATHRALA
14   TRPSERTHRGLYVALLYSTHRTYRASNGLY
15   ALALEUGLYVALASPILEHISGLULYSASP
16   HISPROTHRILELEUGLUMETALALYSALA
17   ALAGLYLEUALATHRGLYASNVALSERTHR
18   ALAGLULEUGLNASPALATHRPROALAALA
19   LEUVALALAHISVALTHRSERARGLYSCYS
20   TYRGLYPROSERALATHRSERGLULYSCYS
21   PROGLYASNALALEUGLULYSGLYGLYLYS
22   GLYSERILETHRGLUGLNLEULEUASNALA
23   ARGALAASPVALTHRLEUGLYGLYGLYALA
24   LYSTHRPHEALAGLUTHRALATHRALAGLY
25   GLUTRPGLNGLYLYSTHRLEUARGGLUGLN
26   ALAGLNALAARGGLYTYRGLNLEUVALSER
27   ASPALAALASERLEUASNSERVALTHRGLU
28   ALAASNGLNGLNLYSPROLEULEUGLYLEU
29   PHEALAASPGLYASNMETPROVALARGTRP
30   LEUGLYPROLYSALATHRTYRHISGLYASN
31   ILEASPLYSPROALAVALTHRCYSTHRPRO
32   ASNPROGLNARGASNASPSERVALPROTHR
33   LEUALAGLNMETTHRASPLYSALAILEGLU
34   LEULEUSERLYSASNGLULYSGLYPHEPHE
35   LEUGLNVALGLUGLYALASERILEASPLYS
36   GLNASPHISALAALAASNPROCYSGLYGLN
37   ILEGLYGLUTHRVALASPLEUASPGLUALA
38   VALGLNARGALALEUGLUPHEALALYSLYS
39   GLUGLYASNTHRLEUVALILEVALTHRALA
40   ASPHISALAHISALASERGLNILEVALALA
41   PROASPTHRLYSALAPROGLYLEUTHRGLN
42   ALALEUASNTHRLYSASPGLYALAVALMET
43   VALMETSERTYRGLYASNSERGLUGLUASP
44   SERGLNGLUHISTHRGLYSERGLNLEUARG
45   ILEALAALATYRGLYPROHISALAALAASN
46   VALVALGLYLEUTHRASPGLNTHRASPLEU
47   PHETYRTHRMETLYSALAALALEUGLYLEU
48   LYS

Samples:

sample_1: E. Coli Alkaline Phosphatase (PhoA), [U-100% 13C; U-100% 15N], 300 uM; E.coli Chaperone SecB, [U-100% 13C; U-100% 15N], 300 uM; potassium chloride 150 mM; potassium phosphate 50 mM; sodium phosphate 50 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 150 mM; pH: 7; pressure: 1 atm; temperature: 301 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Bruker AvanceIII 700 MHz
  • Varian INOVA 900 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts