BMRB Entry 34338

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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/BMR34338
MolProbity Validation Chart

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Title:
Solution NMR structure of outer membrane protein AlkL
Deposition date:
2018-12-19
Original release date:
2020-01-13
Authors:
Schubeis, T.; Andreas, L.; Pintacuda, G.
Citation:

Citation: Schubeis, Tobias; Le Marchand, Tanguy; Daday, Csaba; Kopec, Wojciech; Tekwani Movellan, Kumar; Stanek, Jan; Schwarzer, Tom; Castiglione, Kathrin; de Groot, Bert; Pintacuda, Guido; Andreas, Loren. "A beta-barrel for oil transport through lipid membranes: Dynamic NMR structures of AlkL"  Proc. Natl. Acad. Sci. U.S.A. 117, 21014-21021 (2020).
PubMed: 32817429

Assembly members:

Assembly members:
entity_1, polymer, 219 residues, 24087.912 Da.

Natural source:

Natural source:   Common Name: Pseudomonas oleovorans   Taxonomy ID: 301   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Pseudomonas oleovorans

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MNENYPAKSAGYNQGDWVAS FNFSKVYVGEELGDLNVGGG ALPNADVSIGNDTTLTFDIA YFVSSNIAVDFFVGVPARAK FQGEKSISSLGRVSEVDYGP AILSLQYHYDSFERLYPYVG VGVGRVLFFDKTDGALSSFD IKDKWAPAFQVGLRYDLGNS WMLNSDVRYIPFKTDVTGTL GPVPVSTKIEVDPFILSLGA SYVFKLAAALEHHHHHHHH

Data sets:
Data typeCount
13C chemical shifts360
15N chemical shifts127
1H chemical shifts127

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 219 residues - 24087.912 Da.

1   METASNGLUASNTYRPROALALYSSERALA
2   GLYTYRASNGLNGLYASPTRPVALALASER
3   PHEASNPHESERLYSVALTYRVALGLYGLU
4   GLULEUGLYASPLEUASNVALGLYGLYGLY
5   ALALEUPROASNALAASPVALSERILEGLY
6   ASNASPTHRTHRLEUTHRPHEASPILEALA
7   TYRPHEVALSERSERASNILEALAVALASP
8   PHEPHEVALGLYVALPROALAARGALALYS
9   PHEGLNGLYGLULYSSERILESERSERLEU
10   GLYARGVALSERGLUVALASPTYRGLYPRO
11   ALAILELEUSERLEUGLNTYRHISTYRASP
12   SERPHEGLUARGLEUTYRPROTYRVALGLY
13   VALGLYVALGLYARGVALLEUPHEPHEASP
14   LYSTHRASPGLYALALEUSERSERPHEASP
15   ILELYSASPLYSTRPALAPROALAPHEGLN
16   VALGLYLEUARGTYRASPLEUGLYASNSER
17   TRPMETLEUASNSERASPVALARGTYRILE
18   PROPHELYSTHRASPVALTHRGLYTHRLEU
19   GLYPROVALPROVALSERTHRLYSILEGLU
20   VALASPPROPHEILELEUSERLEUGLYALA
21   SERTYRVALPHELYSLEUALAALAALALEU
22   GLUHISHISHISHISHISHISHISHIS

Samples:

sample_1: Outer membrane protein AlkL, [U-13C; U-15N; U-2H], 333 uM; Sodium Phosphate 20 mM; glutamate 10 mM; arginine 10 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 20 mM; pH: 7; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D 1H-15N NOESY TROSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESY TROSYsample_1isotropicsample_conditions_1
3D 1H-15N HSQC NOESY HSQCsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_1isotropicsample_conditions_1

Software:

CcpNmr Analysis, CCPN - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE III 1000 MHz

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