BMRBj - BMREntryMaster

Found 1 Document (1.233 seconds)

BMRB: 4183

1P92

Expression and Assignment of 1H, 15N,and 13C Resonances of the C-terminal Domain of the Diphtheria Toxin Repressor

Authors

Twigg, P.D., Wylie, G.P., Wang, G., Caspar, D.L.D., Murphy, J.R., Logan, T.M.

Assembly

DtxR subunit 3, C-terminal domain

Entity

1. DtxR subunit 3, C-terminal domain (polymer), 109 monomers, 11997.18 Da Detail

MRGSHHHHHH GSNPIPGLDE LGVGNSDAAA PGTRVIDAAT SMPRKVRIVQ INEIFQVETD QFTQLLDADI RVGSEVEIVD RDGHITLSHN GKDVELLDDL AHTIRIEEL

Formula weight

11997.18 Da

Source organism

Corynebacterium diphtheriae

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 91.7 %, Completeness: 83.0 %, Completeness (bb): 88.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	83.0 % (998 of 1203)	80.5 % (498 of 619)	84.9 % (400 of 471)	88.5 % (100 of 113)
Backbone	88.7 % (573 of 646)	87.4 % (195 of 223)	89.3 % (284 of 318)	89.5 % (94 of 105)
Sidechain	77.6 % (510 of 657)	75.8 % (300 of 396)	80.6 % (204 of 253)	75.0 % (6 of 8)
Aromatic	8.9 % (5 of 56)	17.9 % (5 of 28)	0.0 % (0 of 28)
Methyl	90.6 % (125 of 138)	88.4 % (61 of 69)	92.8 % (64 of 69)

1. DtxR subunit 3, C-terminal domain

MRGSHHHHHH GSNPIPGLDE LGVGNSDAAA PGTRVIDAAT SMPRKVRIVQ INEIFQVETD QFTQLLDADI RVGSEVEIVD RDGHITLSHN GKDVELLDDL AHTIRIEEL

Show sample condition

Sample #1

Temperature 303 (±0.5) K, pH 6.5 (±0.2)

#	Name	Isotope labeling	Type	Concentration
1	DtxR subunit 3, C-terminal domain	[U-95% 15N]		1.0 ~ 2.0 mM

Sample #2

Temperature 303 (±0.5) K, pH 6.5 (±0.2)

#	Name	Isotope labeling	Type	Concentration
2	DtxR subunit 3, C-terminal domain	[U-95% 15N; U-95% 13C]		1.0 ~ 2.0 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	null	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.26 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	null	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.26 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	null	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: -0.05 ppm, Outliers: 1 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	null	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: -0.32 ppm, Outliers: 2 Detail

Release date

1999-02-28

Citation 1

Expression and assignment of the 1H, 15N, and 13C resonances of the C-terminal domain of the diphtheria toxin repressor
Twigg, P.D., Wylie, G.P., Wang, G., Caspar, D.L.D., Murphy, J.R., Logan, T.M.
J. Biomol. NMR (1999), 13, 197-198, PubMed 10070762 , 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 10.1007/bf00211777 , Abstract

Hide non-primary 1 citaion

Related entities 1. DtxR subunit 3, C-terminal domain, : 1 : 20 : 13 entities Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4183_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: bmr4183_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_one	Warning	1117		90.8 (chain: 1, length: 109)
1	Chemical shift references	chemical_shift_reference_one	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_one
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 109, Sequence coverage: 90.8%
- Total number of assignments
  - ¹³C chemical shifts: 392
  - ¹H chemical shifts: 619
  - ¹⁵N chemical shifts: 106
- Completeness of assignments
  - Entity_assemble_ID: 1
- Peptide bond of PRO
- 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

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
84	HIS	HD1	7.24
89	HIS	HD1	7.5

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Found 1 Document (1.233 seconds)

BMRB: 4183

Sample #1

Sample #2

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. DtxR subunit 3, C-terminal domain, : 1 : 20 : 13 entities Detail

Chemical shift validation 3 contents Detail

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	471	392	83.2
¹H chemical shifts	619	495	80.0
¹⁵N chemical shifts	120	106	88.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	218	190	87.2
¹H chemical shifts	223	196	87.9
¹⁵N chemical shifts	105	94	89.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	253	202	79.8
¹H chemical shifts	396	299	75.5
¹⁵N chemical shifts	15	12	80.0