BMRBj - BMREntryMaster

Found 1 Document (0.971 seconds)

BMRB: 5121

1JWE

In vivo Protein Cyclization Promoted by a Circularly Permuted Synechocystis sp. PCC6803 DnaB Mini-intein

Authors

Williams, N.K., Prosselkov, P., Liepinsh, E., Line, I., Sharipo, A., Littler, D.R., Curmi, P.M.G., Otting, G., Dixon, N.E.

Assembly

N-terminal domain of DnaB helicase

Entity

1. N-terminal domain of DnaB helicase (polymer, Thiol state: not present), 114 monomers, 12701.12 Da Detail

MKVPPHSIEA EQSVLGGLML DNERWDDVAE RVVADDFYTR PHRHIFTEMA RLQESGSPID LITLAESLER QGQLDSVGGF AYLAELSKNT PSAANISAYA DIVRERAVVR EMIS

Formula weight

12701.12 Da

Source organism

Escherichia coli

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 99.1 %, Completeness: 95.0 %, Completeness (bb): 96.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	95.0 % (632 of 665)	95.0 % (632 of 665)
Backbone	96.5 % (221 of 229)	96.5 % (221 of 229)
Sidechain	92.7 % (404 of 436)	92.7 % (404 of 436)
Aromatic	94.9 % (37 of 39)	94.9 % (37 of 39)
Methyl	100.0 % (68 of 68)	100.0 % (68 of 68)

1. N-terminal Domain of E. coli DnaB Helicase

MKVPPHSIEA EQSVLGGLML DNERWDDVAE RVVADDFYTR PHRHIFTEMA RLQESGSPID LITLAESLER QGQLDSVGGF AYLAELSKNT PSAANISAYA DIVRERAVVR EMIS

Show sample condition

Sample

Temperature 304 (±1) K

#	Name	Isotope labeling	Type	Concentration
1	N-terminal Domain of E. coli DnaB Helicase			0.6 mM

Release date

2002-04-07

Citation

In vivo protein cyclization promoted by a circularly permuted Synechocystis sp. PCC6803 DnaB mini-intein
Williams, N.K., Prosselkov, P., Liepinsh, E., Line, I., Sharipo, A., Littler, D.R., Curmi, P.M.G., Otting, G., Dixon, N.E.
J. Biol. Chem. (2002), 277, 7790-7798, PubMed 11742000 , DOI 10.1074/jbc.M110303200 , Abstract

Related entities 1. N-terminal domain of DnaB helicase, : 1 : 4 : 40 entities Detail

Interaction partners 1. N-terminal domain of DnaB helicase, : 20 interactors Detail

More details for 20 interactors identified by 8 citations

Experiments performed 3 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr5121_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

None

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Content subtype: bmr5121_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	shift_set_1	Warning	774		99.1 (chain: 1, length: 114)
1	Chemical shift references	chemical_shift_reference	OK	1		No information

Assigned chemical shifts

Saveframe: shift_set_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 114, Sequence coverage: 99.1%
- Total number of assignments
  - ¹H chemical shifts: 774
- Completeness of assignments
  - Entity_assemble_ID: 1
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1

Search

Query history

Resources

Search for primary databases

Search for subsidiary databases

Display

Hits per page

Statistics

Query Changes will take effect after "OK" button is selected.

Maximum hits

Default conjunction operator

Omni-box

Search filter

Sequence search (BLAST)

E-value

Query sequence coverage

Miscellaneous

The number of previewed publications

Completeness of assigned chemical shift

Sequence chart about top aligned regions

Sequence chart about interacting regions

Hit context with highlight

Link destinations for BMRB, PDB and EMDB

Found 1 Document (0.971 seconds)

BMRB: 5121

Sample

Related entities 1. N-terminal domain of DnaB helicase, : 1 : 4 : 40 entities Detail

Interaction partners 1. N-terminal domain of DnaB helicase, : 20 interactors Detail

Experiments performed 3 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Chemical shift validation 3 contents Detail