BMRB Entry 16424

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16424

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Title:
Solution Structure of BamE, a component of the outer membrane protein assembly machinery in Escherichia coli
Deposition date:
2009-07-24
Original release date:
2010-06-15
Authors:
Knowles, Timothy; Sridhar, Pooja; Rajesh, Sandya; Manoli, Eleni; Henderson, Ian; Overduin, Michael
Citation:

Citation: Knowles, Timothy; Sridhar, Pooja; Rajesh, Sandya; Manoli, Eleni; Overduin, Michael; Henderson, Ian. "Secondary structure and 1H, 13C and 15N resonance assignments of BamE, a component of the outer membrane protein assembly machinery in Escherichia coli."  Biomol. NMR Assignments 4, 179-181 (2010).
PubMed: 20526702

Assembly members:

Assembly members:
BamE, polymer, 102 residues, 11446.752 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: chemical synthesis   Host organism: Escherichia coli   Vector: pET24b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BamE: SSTLERVVYRPDINQGNYLT ANDVSKIRVGMTQQQVAYAL GTPLMSDPFGTNTWFYVFRQ QPGHEGVTQQTLTLTFNSSG VLTNIDNKPALSGNLEHHHH HH

Data sets:
Data typeCount
13C chemical shifts349
15N chemical shifts89
1H chemical shifts534

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BamE1

Entities:

Entity 1, BamE 102 residues - 11446.752 Da.

Residue 20 is non native (C to S mutation) so as to remove an acylation site. Residues 114+115 non native required for cloning Residues 116-121 represent a non-native affinity tag

1   SERSERTHRLEUGLUARGVALVALTYRARG
2   PROASPILEASNGLNGLYASNTYRLEUTHR
3   ALAASNASPVALSERLYSILEARGVALGLY
4   METTHRGLNGLNGLNVALALATYRALALEU
5   GLYTHRPROLEUMETSERASPPROPHEGLY
6   THRASNTHRTRPPHETYRVALPHEARGGLN
7   GLNPROGLYHISGLUGLYVALTHRGLNGLN
8   THRLEUTHRLEUTHRPHEASNSERSERGLY
9   VALLEUTHRASNILEASPASNLYSPROALA
10   LEUSERGLYASNLEUGLUHISHISHISHIS
11   HISHIS

Samples:

sample_1: BamE, [U-100% 13C; U-100% 15N], 2.0 mM; sodium phosphate 50 mM; sodium chloride 50 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D Best HNCAsample_1isotropicsample_conditions_1
3D Best HN(CO)CAsample_1isotropicsample_conditions_1
3D Best CBCA(CO)NHsample_1isotropicsample_conditions_1
3D Best HNCACBsample_1isotropicsample_conditions_1
3D Best HNCOsample_1isotropicsample_conditions_1
3D Best HN(CA)COsample_1isotropicsample_conditions_1
2D Best 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CYANA v1.0.5, Guntert, Mumenthaler and Wuthrich - peak picking, refinement, structure solution

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 900 MHz

Related Database Links:

BMRB 16926
PDB
DBJ BAA16502 BAG78424 BAI26856 BAI31942 BAI37148
EMBL CAH23267 CAP77059 CAQ32986 CAQ88015 CAQ99565
GB AAA79787 AAC75666 AAN44171 AAN81589 AAZ89390
REF NP_417107 NP_708464 WP_001203434 WP_001203436 WP_001203437
SP P0A937 P0A938 P0A939 Q32CX2
AlphaFold P0A937 P0A938 P0A939 Q32CX2

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