BMRBj - BMREntryMaster

Found 1 Document (1.481 seconds)

BMRB: 6142

4AL2

1H 13C and 15N resonance assignments for peptide deformylase-actinonin complex

Authors

LARUE, V., BOULAROT, A., ARTAUD, I., MEINNEL, T., DARDEL, F.

Assembly

PDF 147

Entity

1. PDF 147 (polymer, Thiol state: free and other bound), 147 monomers, 16623.94 Da Detail

AVLQVLHIPD ERLRKVAKPV EEVNAEIQRI VDDMFETMYA EEGIGLAATQ VDIHQRIIVI DVSENRDERL VLINPELLEK SGETGIEEGC LSIPEQRALV PRAEKVKIRA LDRDGKPFEL EADGLLAICI QHEMDHLVGK LFMDYLS

Formula weight

16623.94 Da

Source organism

Escherichia coli

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 98.6 %, Completeness: 77.9 %, Completeness (bb): 82.3 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	77.9 % (1339 of 1718)	84.3 % (755 of 896)	66.8 % (449 of 672)	90.0 % (135 of 150)
Backbone	82.3 % (716 of 870)	95.6 % (283 of 296)	68.8 % (298 of 433)	95.7 % (135 of 141)
Sidechain	76.9 % (759 of 987)	78.7 % (472 of 600)	75.9 % (287 of 378)	0.0 % (0 of 9)
Aromatic	16.1 % (10 of 62)	32.3 % (10 of 31)	0.0 % (0 of 31)
Methyl	78.9 % (161 of 204)	80.4 % (82 of 102)	77.5 % (79 of 102)

1. Peptide Deformylase-actinonin complex

AVLQVLHIPD ERLRKVAKPV EEVNAEIQRI VDDMFETMYA EEGIGLAATQ VDIHQRIIVI DVSENRDERL VLINPELLEK SGETGIEEGC LSIPEQRALV PRAEKVKIRA LDRDGKPFEL EADGLLAICI QHEMDHLVGK LFMDYLS

Show sample condition

Sample

Temperature 310 (±0.1) K, pH 7 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Peptide Deformylase-actinonin complex	[U-13C; U-15N]		0.001 M
2	Actinonin			0.001 M

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹H	TMSP	methyl protons	internal	indirect	1.0
¹³C	TMSP	methyl carbons	internal	indirect	1.0
¹⁵N	TMSP	nitrogen	internal	indirect	1.0

Referencing offset: 0.21 ppm, Outliers: 3 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹H	TMSP	methyl protons	internal	indirect	1.0
¹³C	TMSP	methyl carbons	internal	indirect	1.0
¹⁵N	TMSP	nitrogen	internal	indirect	1.0

Referencing offset: 0.21 ppm, Outliers: 3 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹H	TMSP	methyl protons	internal	indirect	1.0
¹³C	TMSP	methyl carbons	internal	indirect	1.0
¹⁵N	TMSP	nitrogen	internal	indirect	1.0

Referencing offset: -0.15 ppm, Outliers: 1 Detail

Release date

2006-01-11

Citation

Discovery and refinement of a new structural class of potent peptide deformylase inhibitors
Boularot, A., Giglione, C., Petit, S., Duroc, Y., de Sousa, R.A., Larue, V., Cresteil, T., Dardel, F., Artaud, I., Meinnel, T.
J. Med. Chem. (2007), 50, 10-20, PubMed 17201406 , DOI 10.1021/jm060910c , Abstract

Related entities 1. PDF 147, : 1 : 1 : 37 : 186 entities Detail

Interaction partners 1. PDF 147, : 15 interactors Detail

More details for 15 interactors identified by 4 citations

Experiments performed 7 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr6142_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: bmr6142_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts	Warning	1459		98.6 (chain: 1, length: 147)
1	Chemical shift references	chemical_shift_reference	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 147, Sequence coverage: 98.6%
- Total number of assignments
  - ¹H chemical shifts: 903
  - ¹⁵N chemical shifts: 135
  - ¹³C chemical shifts: 421
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- 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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	106	81	76.4
¹³C chemical shifts	106	75	70.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	896	741	82.7
¹⁵N chemical shifts	160	135	84.4
¹³C chemical shifts	672	421	62.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	296	282	95.3
¹⁵N chemical shifts	141	135	95.7
¹³C chemical shifts	294	144	49.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	600	459	76.5
¹⁵N chemical shifts	19	0	0.0
¹³C chemical shifts	378	277	73.3

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Found 1 Document (1.481 seconds)

BMRB: 6142

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. PDF 147, : 1 : 1 : 37 : 186 entities Detail

Interaction partners 1. PDF 147, : 15 interactors Detail

Experiments performed 7 experiments Detail

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Chemical shift validation 3 contents Detail