BMRBj - BMREntryMaster

Found 1 Document (1.605 seconds)

BMRB: 4297

1JWE

Chemical Shifts (1H, 13C, 15N) and J-couplings (3JHNHA, 3JNHB, 3JHAHB) for the N-terminal Domain of E. coli DnaB Helicase, DnaB(24-136)

Authors

Weigelt, J., Brown, S.E., Miles, C.S., Dixon, N.E., Otting, G.

Assembly

DnaB helicase N-terminal domain

Entity

1. DnaB helicase N-terminal domain (polymer), 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

Refine. method

SIMULATED ANNEALING IN TORSION ANGLE SPACE

Data set

assigned_chemical_shifts, coupling_constants

Chem. Shift Complete

Sequence coverage: 98.2 %, Completeness: 93.0 %, Completeness (bb): 94.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	93.0 % (1196 of 1286)	94.9 % (631 of 665)	90.1 % (454 of 504)	94.9 % (111 of 117)
Backbone	94.4 % (636 of 674)	96.5 % (221 of 229)	92.9 % (312 of 336)	94.5 % (103 of 109)
Sidechain	91.8 % (661 of 720)	94.0 % (410 of 436)	88.0 % (243 of 276)	100.0 % (8 of 8)
Aromatic	75.6 % (59 of 78)	92.3 % (36 of 39)	57.9 % (22 of 38)	100.0 % (1 of 1)
Methyl	100.0 % (136 of 136)	100.0 % (68 of 68)	100.0 % (68 of 68)

1. DnaB helicase

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

Show sample condition

Sample #1

Temperature 305 (±1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Concentration
1	DnaB helicase	{U-98% 15N}	2.2 mM
2	sodium phosphate		20 mM
3	EDTA		1 mM
4	sodiumn azide		0.02 % w/v

Sample #2

Temperature 305 (±1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Concentration
5	DnaB helicase	{U-98% 13C, U-98% 15N}	2.2 mM
6	sodium phosphate		20 mM
7	EDTA		1 mM
8	sodiumn azide		0.02 % w/v

Sample #3

Temperature 305 (±1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Concentration
9	DnaB helicase	{U-10% 13C, U-98% 15N}	2.2 mM
10	sodium phosphate		20 mM
11	EDTA		1 mM
12	sodiumn azide		0.02 % w/v

LACS Plot; CA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
¹H	H2O	protons	4.683 ppm	internal	direct	100.0
¹⁵N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

Referencing offset: -0.19 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
¹H	H2O	protons	4.683 ppm	internal	direct	100.0
¹⁵N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

Referencing offset: -0.19 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
¹H	H2O	protons	4.683 ppm	internal	direct	100.0
¹⁵N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

Referencing offset: 0.05 ppm, Outliers: 2 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
¹H	H2O	protons	4.683 ppm	internal	direct	100.0
¹⁵N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

Referencing offset: -0.32 ppm, Outliers: 2 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 1JWE, Strand ID: A Detail

Coupling constant

190 J values in 1 lists
Temperature 305 (±1) K, pH 7.5 (±0.1) Detail

Release date

1999-02-21

Citation 1

NMR structure of the N-terminal domain of E. coli DnaB helicase: implications for structure rearrangements in the helicase hexamer
Weigelt, J., Brown, S.E., Miles, C.S., Dixon, N.E., Otting, G.
Structure (1999), 7, 681-690, PubMed 10404597 , DOI: , Abstract

Show more 1 citaion

Citation 2

1H, 13C and 15N chemical shift referencing in biomolecular NMR
Wishart, D.S., Bigam, C.G., Yao, J., Abildgaard, F., Dyson, H.J., Oldfield, E., Markley, J.L., Sykes, B.D.
J. Biomol. NMR (1995), 6, 135-140, PubMed 8589602 , DOI: , Abstract

Hide non-primary 1 citaion

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

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

More details for 20 interactors identified by 8 citations

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4297_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: bmr4297_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	Chemical_shifts	Warning	1336		98.2 (chain: 1, length: 114)
1	Chemical shift references	chemical_shift_reference	Warning	3		No information

Assigned chemical shifts

Saveframe: Chemical_shifts
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 114, Sequence coverage: 98.2%
- Total number of assignments
  - ¹³C chemical shifts: 453
  - ¹H chemical shifts: 771
  - ¹⁵N chemical shifts: 112
- Completeness of assignments
  - Entity_assemble_ID: 1
- Peptide bond of PRO
- Tautomeric state of HIS
- Rotameric state of ILE , LEU, and VAL
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	276	242	87.7
¹H chemical shifts	436	409	93.8
¹⁵N chemical shifts	17	9	52.9

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Found 1 Document (1.605 seconds)

BMRB: 4297

Sample #1

Sample #2

Sample #3

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

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

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

Chemical shift validation 3 contents Detail

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	504	453	89.9
¹H chemical shifts	665	630	94.7
¹⁵N chemical shifts	126	112	88.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	228	211	92.5
¹H chemical shifts	229	221	96.5
¹⁵N chemical shifts	109	103	94.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	38	22	57.9
¹H chemical shifts	39	36	92.3
¹⁵N chemical shifts	1	1	100.0