BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 4718

Title: Assignments of amide 1H, amide 15N, and Ca, CO, Cb 13C shifts for the replication terminator protein   PubMed: 11224562

Deposition date: 2000-04-12 Original release date: 2001-05-01

Authors: Wilce, Jackie; Vivian, Julian; Hastings, Adam; Otting, Gottfried; Folmer, Rutger; Duggin, I.; Wake, R.; Wilce, Matthew

Citation: Wilce, Jackie; Vivian, Julian; Hastings, Adam; Otting, Gottfried; Folmer, Rutger; Duggin, I.; Wake, R.; Wilce, Matthew. "Structure of the RTP-DNA Complex and the Mechanism of Polar Replication Fork Arrest"  Nat. Struct. Biol. 8, 206-210 (2001).

Assembly members:
replication termination protein, polymer, 122 residues, Formula weight is not available

Natural source:   Common Name: Bacillus subtilis   Taxonomy ID: 1423   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Bacillus subtilis

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
replication termination protein: MKEEKRSSTGFLVKQRAFLK LYMITMTEQERLYGLKLLEV LRSEFKEIGFKPNHTEVYRS LHELLDDGILKQIKVKKEGA KLQEVVLYQFKDYEAAKLYK KQLKVELDRSKKLIEKALSD NF

Data sets:
Data typeCount
1H chemical shifts131
13C chemical shifts333
15N chemical shifts123

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RTP subunit 11
2RTP subunit 21

Entities:

Entity 1, RTP subunit 1 122 residues - Formula weight is not available

1   METLYSGLUGLULYSARGSERSERTHRGLY
2   PHELEUVALLYSGLNARGALAPHELEULYS
3   LEUTYRMETILETHRMETTHRGLUGLNGLU
4   ARGLEUTYRGLYLEULYSLEULEUGLUVAL
5   LEUARGSERGLUPHELYSGLUILEGLYPHE
6   LYSPROASNHISTHRGLUVALTYRARGSER
7   LEUHISGLULEULEUASPASPGLYILELEU
8   LYSGLNILELYSVALLYSLYSGLUGLYALA
9   LYSLEUGLNGLUVALVALLEUTYRGLNPHE
10   LYSASPTYRGLUALAALALYSLEUTYRLYS
11   LYSGLNLEULYSVALGLULEUASPARGSER
12   LYSLYSLEUILEGLULYSALALEUSERASP
13   ASNPHE

Samples:

sample_1: replication termination protein, [U-100% 13C; U-100% 15N; U-70% 2H], 0.25 mM

condition_1: pH: 6.0; temperature: 298 K; ionic strength: 0.11 M

Experiments:

NameSampleSample stateSample conditions
TROSY-HNCAnot availablenot availablenot available
TROSY-HNCOnot availablenot availablenot available
TROSY-HNCACBnot availablenot availablenot available
TROSY-HN(CO)CACBnot availablenot availablenot available
TROSY-HN(CA)COnot availablenot availablenot available
3D NOESY-15N-HSQCnot availablenot availablenot available

Software:

XEASY -

NMR spectrometers:

  • Bruker DRX 800 MHz
  • Bruker DMX 600 MHz

Related Database Links:

PDB
DBJ BAM52503 BAM58079 BAO93415 GAK78159
EMBL CAA29534 CAB13742 CCU58469 CEI57043 CEJ77468
GB AAA22721 AAC38659 AAC38660 AAC38662 ADM38012
REF NP_389731 WP_003220337 WP_010334473 WP_024715459 WP_041849904
SP E0TY12 P0CI76 P68733

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts