BMRB Entry 18349

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18349
MolProbity Validation Chart

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Title:
NMR structure of a LINE-1 type transposase domain-containing protein 1 (L1TD1) from HOMO SAPINES
Deposition date:
2012-03-26
Original release date:
2012-07-02
Authors:
Serrano, Pedro; Geralt, Michael; Mohanty, Biswaranjan; Wuthrich, Kurt
Citation:

Citation: Serrano, Pedro; Geralt, Michael; Mohanty, Biswaranjan; Wuthrich, Kurt. "NMR structure of a LINE-1 type transposase domain-containing protein 1 (L1TD1) from HOMO SAPINES"  .

Assembly members:

Assembly members:
L1TD1, polymer, 176 residues, 19804.965 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
L1TD1: GVLMDEGAVLTLAADLSSAT LDISKQWSNVFNILRENDFE PKFLCEVKLAFKCDGEIKTF SDLQSLRKFASQKSSMKELL KDVLPQKEGVLMDEGAVLTL AADLSSATLDISKQWSNVFN ILRENDFEPKFLCEVKLAFK CDGEIKTFSDLQSLRKFASQ KSSMKELLKDVLPQKE

Data sets:
Data typeCount
13C chemical shifts294
15N chemical shifts88
1H chemical shifts608

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1L1TD11

Entities:

Entity 1, L1TD1 176 residues - 19804.965 Da.

1   GLYVALLEUMETASPGLUGLYALAVALLEU
2   THRLEUALAALAASPLEUSERSERALATHR
3   LEUASPILESERLYSGLNTRPSERASNVAL
4   PHEASNILELEUARGGLUASNASPPHEGLU
5   PROLYSPHELEUCYSGLUVALLYSLEUALA
6   PHELYSCYSASPGLYGLUILELYSTHRPHE
7   SERASPLEUGLNSERLEUARGLYSPHEALA
8   SERGLNLYSSERSERMETLYSGLULEULEU
9   LYSASPVALLEUPROGLNLYSGLUGLYVAL
10   LEUMETASPGLUGLYALAVALLEUTHRLEU
11   ALAALAASPLEUSERSERALATHRLEUASP
12   ILESERLYSGLNTRPSERASNVALPHEASN
13   ILELEUARGGLUASNASPPHEGLUPROLYS
14   PHELEUCYSGLUVALLYSLEUALAPHELYS
15   CYSASPGLYGLUILELYSTHRPHESERASP
16   LEUGLNSERLEUARGLYSPHEALASERGLN
17   LYSSERSERMETLYSGLULEULEULYSASP
18   VALLEUPROGLNLYSGLU

Samples:

sample_1: L1TD1, [U-98% 13C; U-98% 15N], 1.2 mM; sodium azide 5 mM; sodium chloride 50 mM; sodium phosphate 25 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.185 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
APSY 5D-HACACONHsample_1isotropicsample_conditions_1
APSY 5D-CBCACONHsample_1isotropicsample_conditions_1
ASPY 4D-HACANHsample_1isotropicsample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

TOPSPIN, Bruker Biospin - collection, processing

UNIO, UNIO Herrmann and Wuthrich - chemical shift assignment, structure solution

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAA91878

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