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BMRB: 5404

4AL2

Backbone and Side Chain assignments of Peptide Deformylase complexed with Actinonin

Authors

Byerly, D.W., McElroy, C.A., Foster, M.P.

Assembly

E. coli Peptide Deformylase

Entity

1. Peptide Deformylase (polymer, Thiol state: not reported), 147 monomers, 16639.94 Da Detail

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

2. ACTINONIN (non-polymer), 385.498 Da

Total weight

17025.438 Da

Max. entity weight

16639.94 Da

Source organism

Escherichia coli

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 99.3 %, Completeness: 93.3 %, Completeness (bb): 96.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	93.3 % (1604 of 1719)	94.6 % (849 of 897)	90.6 % (609 of 672)	97.3 % (146 of 150)
Backbone	96.9 % (843 of 870)	98.0 % (290 of 296)	96.1 % (416 of 433)	97.2 % (137 of 141)
Sidechain	90.7 % (896 of 988)	93.0 % (559 of 601)	86.8 % (328 of 378)	100.0 % (9 of 9)
Aromatic	21.0 % (13 of 62)	41.9 % (13 of 31)	0.0 % (0 of 31)
Methyl	93.6 % (189 of 202)	97.0 % (98 of 101)	90.1 % (91 of 101)

1. Peptide Deformylase

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

Show sample condition

Sample

Temperature 310 (±1) K, pH 7.2 (±0.1)

#	Name	Isotope labeling	Concentration
1	Peptide Deformylase	[U-95% 13C; U-90% 15N]	0.5 ~ 1.2 mM
2	TRIS		20 mM
3	NaN3		0.02 %

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	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.24 ppm, Outliers: 3 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	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.24 ppm, Outliers: 3 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	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: -0.02 ppm, Outliers: 4 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	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.41 ppm, Outliers: 2 Detail

Release date

2005-05-19

Citation

Mapping the surface of Escherichia coli peptide deformylase by NMR with organic solvents
Byerly, D.W., McElroy, C.A., Foster, M.P.
Protein Sci. (2002), 11, 1850-1853, PubMed 12070337 , DOI 10.1110/ps.0203402 , Abstract

Related entities 1. Peptide Deformylase, : 1 : 33 : 3 : 2 : 183 entities Detail

Interaction partners 1. Peptide Deformylase, : 15 interactors Detail

More details for 15 interactors identified by 4 citations

Experiments performed 12 experiments Detail

1 15N TOCSY-HSQC