BMRB Entry 15325

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15325
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
C-terminal domain of ORF1p from mouse LINE-1
Deposition date:
2007-06-21
Original release date:
2007-07-24
Authors:
Januszyk, Kurt; Clubb, Robert
Citation:

Citation: Januszyk, Kurt; Li, Patrick; Villareal, Valerie; Branciforte, Dan; Wu, Haihong; Xie, Yongming; Feigon, Juli; Loo, Joseph; Martin, Sandra; Clubb, Robert. "Identification and solution structure of a highly conserved C-terminal domain within ORF1p required for retrotransposition of long interspersed nuclear element-1"  J. Biol. Chem. 282, 24893-24904 (2007).
PubMed: 17569664

Assembly members:

Assembly members:
CTD, polymer, 88 residues, 7649.985 Da.

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CTD: MQVTYKGRPIRITPDFSPET MKARRAWTDVIQTLREHKCQ PRLLYPAKLSITIDGETKVF HDKTKFTQYLSTNPALQRII TEKKQYKD

Data sets:
Data typeCount
13C chemical shifts413
15N chemical shifts84
1H chemical shifts630

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CTD1

Entities:

Entity 1, CTD 88 residues - 7649.985 Da.

1   METGLNVALTHRTYRLYSGLYARGPROILE
2   ARGILETHRPROASPPHESERPROGLUTHR
3   METLYSALAARGARGALATRPTHRASPVAL
4   ILEGLNTHRLEUARGGLUHISLYSCYSGLN
5   PROARGLEULEUTYRPROALALYSLEUSER
6   ILETHRILEASPGLYGLUTHRLYSVALPHE
7   HISASPLYSTHRLYSPHETHRGLNTYRLEU
8   SERTHRASNPROALALEUGLNARGILEILE
9   THRGLULYSLYSGLNTYRLYSASP

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 1 mM; Phosphate buffer 50 mM; NaCl 200 mM; DTT 5 mM; D2O 7%

sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker DRX 500 MHz

Related Database Links:

PDB
EMBL CAA27362 CAI02523 CRH42983 CRH55784 CRH56877
GB AAA39397 AAA66023 AAA67726 AAL17969 AAL17971
REF WP_057184893 WP_057247702 WP_057256795 XP_676702 XP_727753
SP P11260
AlphaFold P11260

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