BMRB Entry 17686

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17686
MolProbity Validation Chart

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Title:
Solution structure of the RMM-CTD domains of human LINE-1 ORF1p
Deposition date:
2011-06-03
Original release date:
2012-02-22
Authors:
Coles, Murray; Truffault, Vincent
Citation:

Citation: Khazina, Elena; Truffault, Vincent; Buttner, Regina; Schmidt, Steffen; Coles, Murray; Weichenrieder, Oliver. "Trimeric structure and flexibility of the L1ORF1 protein in human L1 retrotransposition."  Nat. Struct. Mol. Biol. 18, 1006-1014 (2011).
PubMed: 21822284

Assembly members:

Assembly members:
L1ORF1p, polymer, 182 residues, 20688.154 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET 15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
L1ORF1p: MGNLRLIGVPESDVENGTKL ENTLQDIIQENFPNLARQAN VQIQEIQRTPQRYSSRRATP RHIIVRFTKVEMKEKMLRAA REKGRVTLKGKPIRLTVDLS AETLQARREWGPIFNILKEK NFQPRISYPAKLSFISEGEI KYFIDKQMLRDFVTTRPALK ELLKEALNMERNNRYQHHHH HH

Data sets:
Data typeCount
13C chemical shifts697
15N chemical shifts153
1H chemical shifts1236

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1L1ORF1p1

Entities:

Entity 1, L1ORF1p 182 residues - 20688.154 Da.

Mutations R255M and P156G were for cloning purposes. Residues 331-336 are a hexahistidine purification tag

1   METGLYASNLEUARGLEUILEGLYVALPRO
2   GLUSERASPVALGLUASNGLYTHRLYSLEU
3   GLUASNTHRLEUGLNASPILEILEGLNGLU
4   ASNPHEPROASNLEUALAARGGLNALAASN
5   VALGLNILEGLNGLUILEGLNARGTHRPRO
6   GLNARGTYRSERSERARGARGALATHRPRO
7   ARGHISILEILEVALARGPHETHRLYSVAL
8   GLUMETLYSGLULYSMETLEUARGALAALA
9   ARGGLULYSGLYARGVALTHRLEULYSGLY
10   LYSPROILEARGLEUTHRVALASPLEUSER
11   ALAGLUTHRLEUGLNALAARGARGGLUTRP
12   GLYPROILEPHEASNILELEULYSGLULYS
13   ASNPHEGLNPROARGILESERTYRPROALA
14   LYSLEUSERPHEILESERGLUGLYGLUILE
15   LYSTYRPHEILEASPLYSGLNMETLEUARG
16   ASPPHEVALTHRTHRARGPROALALEULYS
17   GLULEULEULYSGLUALALEUASNMETGLU
18   ARGASNASNARGTYRGLNHISHISHISHIS
19   HISHIS

Samples:

RMM_15N: L1ORF1p-RMM, [U-100% 15N], 0.6 mM; Tris 5 mM; sodium chloride 300 mM; H2O 90%; D2O 10%

RMM_13C_15N: L1ORF1p-RMM, [U-100% 13C; U-100% 15N], 0.8 mM; Tris 5 mM; sodium chloride 300 mM; H2O 90%; D2O 10%

CTD_15N: L1ORF1p-CTD, [U-100% 15N], 0.8 mM; Tris 5 mM; sodium chloride 300 mM; H2O 90%; D2O 10%

CTD_13C_15N: L1ORF1p-CTD, [U-100% 13C; U-100% 15N], 0.8 mM; Tris 5 mM; sodium chloride 300 mM; H2O 90%; D2O 10%

RMMCTD_15N: L1ORF1p-RMM-CTD, [U-100% 15N], 0.8 mM; Tris 5 mM; sodium chloride 300 mM; H2O 90%; D2O 10%

RMMCTD_13C_15N: L1ORF1p-RMM-CTD, [U-100% 13C; U-100% 15N], 0.8 mM; Tris 5 mM; sodium chloride 300 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 300 mM; pH: 8.0; pressure: 1 atm; temperature: 291 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYRMM_15Nisotropicsample_conditions_1
3D 1H-13C NOESYRMM_13C_15Nisotropicsample_conditions_1
3D CNH-NOESYRMM_13C_15Nisotropicsample_conditions_1
3D NNH-NOESYRMM_15Nisotropicsample_conditions_1
3D HNCACBRMM_13C_15Nisotropicsample_conditions_1
3D HBHA(CO)NHRMM_13C_15Nisotropicsample_conditions_1
3D C(CO)NHRMM_13C_15Nisotropicsample_conditions_1
3D CCH-TOCSYRMM_13C_15Nisotropicsample_conditions_1
3D HNCORMM_13C_15Nisotropicsample_conditions_1
2D 15N-filtered 1H-1H NOESYRMM_15Nisotropicsample_conditions_1
3D 1H-15N NOESYCTD_15Nisotropicsample_conditions_1
3D 1H-13C NOESYCTD_13C_15Nisotropicsample_conditions_1
3D CNH-NOESYCTD_13C_15Nisotropicsample_conditions_1
3D NNH-NOESYCTD_15Nisotropicsample_conditions_1
3D CCH-NOESYCTD_13C_15Nisotropicsample_conditions_1
3D HNCACBCTD_13C_15Nisotropicsample_conditions_1
3D CBCA(CO)NHCTD_13C_15Nisotropicsample_conditions_1
3D C(CO)NHCTD_13C_15Nisotropicsample_conditions_1
3D CCH-TOCSYCTD_13C_15Nisotropicsample_conditions_1
3D HNCOCTD_13C_15Nisotropicsample_conditions_1
2D 15N-filtered 1H-1H NOESYCTD_15Nisotropicsample_conditions_1
3D 1H-15N NOESYRMMCTD_15Nisotropicsample_conditions_1
3D 1H-13C NOESYRMMCTD_13C_15Nisotropicsample_conditions_1
3D CNH-NOESYRMMCTD_13C_15Nisotropicsample_conditions_1
3D NNH-NOESYRMMCTD_15Nisotropicsample_conditions_1
3D CCH-NOESYRMMCTD_13C_15Nisotropicsample_conditions_1
3D HNCACBRMMCTD_13C_15Nisotropicsample_conditions_1
3D CBCA(CO)NHRMMCTD_13C_15Nisotropicsample_conditions_1
3D C(CO)NHRMMCTD_13C_15Nisotropicsample_conditions_1
3D CCH-TOCSYRMMCTD_13C_15Nisotropicsample_conditions_1
3D HNCORMMCTD_13C_15Nisotropicsample_conditions_1
2D 15N-filtered 1H-1H NOESYRMMCTD_15Nisotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY v3.113, Goddard - chemical shift assignment, data analysis

X-PLOR NIH v2.21, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
EMBL CJZ86355
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PRF 1901303A
SP Q9UN81
AlphaFold Q9UN81

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