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 30083

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PDB ID:
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   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, 40 residues, 4325.987 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: ANQQKPLLGLFADGNMPVRW LGPKATYHGNIDKPAVTCTP

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

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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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

Samples:

sample_1: E.coli Alkaline Phosphatase (PhoA) binding site d, [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-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