BMRB Entry 34872

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34872
MolProbity Validation Chart

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Title:
Magic-angle spinning NMR Structure of Opa60 in Lipid Bilayers
Deposition date:
2023-10-19
Original release date:
2024-07-17
Authors:
Forster, M.; Andreas, L.
Citation:

Citation: Forster, M.; Movellan, K.; Najbauer, E.; Becker, S.; Andreas, L.. "Magic-angle spinning NMR structure of Opa60 in lipid bilayers"  J. Struct. Biol. X 9, 100098-100098 (2024).
PubMed: 39010882

Assembly members:

Assembly members:
entity_1, polymer, 252 residues, 28772.986 Da.

Natural source:

Natural source:   Common Name: Neisseria gonorrhoeae   Taxonomy ID: 485   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Neisseria gonorrhoeae

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MASEDGGRGPYVQADLAYAY EHITHDYPEPTAPNKNKIST VSDYFRNIRTRSVHPRVSVG YDFGGWRIAADYARYRKWNN NKYSVNIENVRIRKENGIRI DRKTENQENGTFHAVSSLGL SAIYDFQINDKFKPYIGARV AYGHVRHSIDSTKKTIEVTT VPSNAPNGAVTTYNTDPKTQ NDYQSNSIRRVGLGVIAGVG FDITPKLTLDAGYRYHNWGR LENTRFKTHEASLGVRYRFK LAAALEHHHHHH

Data sets:
Data typeCount
13C chemical shifts238
15N chemical shifts84
1H chemical shifts83

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 252 residues - 28772.986 Da.

1   METALASERGLUASPGLYGLYARGGLYPRO
2   TYRVALGLNALAASPLEUALATYRALATYR
3   GLUHISILETHRHISASPTYRPROGLUPRO
4   THRALAPROASNLYSASNLYSILESERTHR
5   VALSERASPTYRPHEARGASNILEARGTHR
6   ARGSERVALHISPROARGVALSERVALGLY
7   TYRASPPHEGLYGLYTRPARGILEALAALA
8   ASPTYRALAARGTYRARGLYSTRPASNASN
9   ASNLYSTYRSERVALASNILEGLUASNVAL
10   ARGILEARGLYSGLUASNGLYILEARGILE
11   ASPARGLYSTHRGLUASNGLNGLUASNGLY
12   THRPHEHISALAVALSERSERLEUGLYLEU
13   SERALAILETYRASPPHEGLNILEASNASP
14   LYSPHELYSPROTYRILEGLYALAARGVAL
15   ALATYRGLYHISVALARGHISSERILEASP
16   SERTHRLYSLYSTHRILEGLUVALTHRTHR
17   VALPROSERASNALAPROASNGLYALAVAL
18   THRTHRTYRASNTHRASPPROLYSTHRGLN
19   ASNASPTYRGLNSERASNSERILEARGARG
20   VALGLYLEUGLYVALILEALAGLYVALGLY
21   PHEASPILETHRPROLYSLEUTHRLEUASP
22   ALAGLYTYRARGTYRHISASNTRPGLYARG
23   LEUGLUASNTHRARGPHELYSTHRHISGLU
24   ALASERLEUGLYVALARGTYRARGPHELYS
25   LEUALAALAALALEUGLUHISHISHISHIS
26   HISHIS

Samples:

sample_1: sodium phosphate 20 mM; sodium chloride 100 mM; magnesium chloride 20 mM; dimyristoyl-sn-glycero-3-phosphocholine 33 % w/w; protein, [U-99% 13C; U-99% 15N; U-98% 2H], 67 % w/w

sample_2: sodium phosphate 20 mM; sodium chloride 100 mM; magnesium chloride 20 mM; dimyristoyl-sn-glycero-3-phosphocholine, Acyl chain deuterated (d54), 33 % w/w; protein, [U-99% 13C; U-99% 15N; U-98% 2H], 67 % w/w

sample_conditions_1: ionic strength: 140 mM; pH: 6.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
(H)CANHsample_1isotropicsample_conditions_1
(H)(CO)CA(CO)NHsample_1isotropicsample_conditions_1
(H)(CA)CB(CA)NHsample_1isotropicsample_conditions_1
(H)(CA)CB(CA)(CO)NHsample_1isotropicsample_conditions_1
(H)CONHsample_1isotropicsample_conditions_1
(H)CO(CA)NHsample_1isotropicsample_conditions_1
(H)N(CA)(CO)NHsample_1isotropicsample_conditions_1
HN(H)(H)NHsample_1isotropicsample_conditions_1
(H)CANHsample_2isotropicsample_conditions_1
(H)NCAHAsample_2isotropicsample_conditions_1
HC(H)(H)CHsample_2isotropicsample_conditions_1
(H)NHsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, structure calculation

NMRFAM-SPARKY, Lee W, Tonelli M, Markley JL - data analysis, peak picking

NMR spectrometers:

  • Bruker AVANCE III HD 800 MHz
  • Bruker AVANCE III HD 600 MHz
  • Bruker AVANCE III HD 950 MHz

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