BMRB Entry 6479

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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/BMR6479
MolProbity Validation Chart

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Title:
The Structure of the Excisionase (Xis) Protein from Conjugative Transposon Tn916 Provides Insights into the Regulation of Heterobivalent Tyrosine Recombinases
Deposition date:
2005-02-02
Original release date:
2005-04-04
Authors:
Abbani, M.; Iwahara, M.; Clubb, R.
Citation:

Citation: Abbani, M.; Iwahara, M.; Clubb, R.. "The structure of the excisionase (Xis) protein from conjugative transposon Tn916 provides insights into the regulation of heterobivalent tyrosine recombinases "  J. Mol. Biol. 374, 11-25 (2005).
PubMed: 15733914

Assembly members:

Assembly members:
Excisionase from transposon Tn916, polymer, 70 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Enterococcus faecalis   Taxonomy ID: 1351   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Enterococcus faecalis

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Excisionase from transposon Tn916: AGHMKQTDIPIWERYTLTIE EASKYFRIGENKLRRLAEEN KNANWLIMNGNRIQIKRKQF EKIIDTLDAI

Data sets:
Data typeCount
1H chemical shifts458
13C chemical shifts310
15N chemical shifts77
coupling constants32

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Excisionase from transposon Tn9161

Entities:

Entity 1, Excisionase from transposon Tn916 70 residues - Formula weight is not available

1   ALAGLYHISMETLYSGLNTHRASPILEPRO
2   ILETRPGLUARGTYRTHRLEUTHRILEGLU
3   GLUALASERLYSTYRPHEARGILEGLYGLU
4   ASNLYSLEUARGARGLEUALAGLUGLUASN
5   LYSASNALAASNTRPLEUILEMETASNGLY
6   ASNARGILEGLNILELYSARGLYSGLNPHE
7   GLULYSILEILEASPTHRLEUASPALAILE

Samples:

sample_1: Excisionase from transposon Tn916, [U-13C; U-15N], 1 mM; NaOAc 30 mM; NaCl 60 mM; H2O 93%; D2O 7%

sample_cond_1: pH: 4.5 na; temperature: 303 K; ionic strength: 60 mM; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C CT-HSQCnot availablenot availablenot available
2D 1H-15N HSQCnot availablenot availablenot available
3D 1H-13C-1H HCCH-COSYnot availablenot availablenot available
3D 1H-1H-15N NOESYnot availablenot availablenot available
3D 13C-1H-1H NOESYnot availablenot availablenot available
3D 1H-1H-15N TOCSYnot availablenot availablenot available
3D 1H-13C-1H HCCH-TOCSYnot availablenot availablenot available
3D CBCA(CO)NHnot availablenot availablenot available
3D HNCACBnot availablenot availablenot available
3D HCACOnot availablenot availablenot available
3D HNCAnot availablenot availablenot available
3D HNCOnot availablenot availablenot available
3D HN(CO)CAnot availablenot availablenot available
3D HNHAnot availablenot availablenot available
3D HNHBnot availablenot availablenot available
4D 1H-15N-1H-13C NOESYnot availablenot availablenot available

Software:

XWINNMR v2.6 - collection

X-PLOR v3.1 - processing

NMRPipe vsgi6x - processing

Pipp v4.3.5 - data analysis

XPLOR-NIH - refinement

NMR spectrometers:

  • Bruker AMX 500 MHz
  • Bruker AMX 600 MHz

Related Database Links:

PDB
DBJ BAG12509 BAG80636 BAK28445 GAD37681
EMBL CAA43359 CAO82957 CAP45545 CAQ49381 CAR69111
GB AAA19426 AAB60029 AAC36981 AAM99802 AAY63949
PRF 2114402X
REF NP_687930 WP_000814511 WP_000814512 WP_006417979 WP_006730246
SP P61623 P61624
AlphaFold P61623 P61624

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