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Found 1 Document (1.155 seconds)

BMRB: 4834

Backbone (1H, 15N, 13C) Resonance Assignments of a 21 kDa construct of S. aureus Peptide Deformylase

Authors

Scahill, T.A., Kloosterman, D.A., Cialdella, J.I., Deibel, M.R., Marshall, V.P., Yem, A.W.

Assembly

S. aureus peptide deformylase

Entity

1. Staphylococcal aureus peptide deformylase (polymer, Thiol state: all free), 189 monomers, 21382.12 Da Detail

MLTMKDIIRD GHPTLRQKAA ELELPLTKEE KETLIAMREF LVNSQDEEIA KRYGLRSGVG LAAPQINISK RMIAVLIPDD GSGKSYDYML VNPKIVSHSV QEAYLPTGEG CLSVDDNVAG LVHRHNRITI KAKDIEGNDI QLRLKGYPAI VFQHEIDHLN GVMFYDHIDK DHPLQPHTDA VEVHHHHHH

2. ZN (non-polymer), 65.409 Da

Total weight

21447.527 Da

Max. entity weight

21382.12 Da

Source organism

Staphylococcus aureus

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 96.8 %, Completeness: 62.5 %, Completeness (bb): 92.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	62.5 % (1377 of 2203)	58.4 % (669 of 1146)	62.3 % (538 of 863)	87.6 % (170 of 194)
Backbone	92.7 % (1035 of 1116)	92.7 % (353 of 381)	92.4 % (513 of 555)	93.9 % (169 of 180)
Sidechain	39.7 % (502 of 1264)	40.9 % (313 of 765)	38.8 % (188 of 485)	7.1 % (1 of 14)
Aromatic	6.5 % (9 of 138)	8.7 % (6 of 69)	4.3 % (3 of 69)
Methyl	19.5 % (44 of 226)	21.2 % (24 of 113)	17.7 % (20 of 113)

1. Staphylococcal aureus peptide deformylase

Show sample condition

Sample

Temperature 310 (±0.1) K

#	Name	Isotope labeling	Type	Concentration
1	Staphylococcal aureus peptide deformylase	[95% 13C; 90% 15N]		0.3 ~ 1.0 mM
2	ZINC (II) ION			0.6 ~ 2.0 mM

LACS Plot; CA

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

Referencing offset: 0.11 ppm, Outliers: 1 Detail

LACS Plot; CB

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

Referencing offset: 0.11 ppm, Outliers: 1 Detail

LACS Plot; HA

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

Referencing offset: -0.1 ppm, Outliers: 1 Detail

LACS Plot; CO

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

Referencing offset: 0.17 ppm, Outliers: 3 Detail

Release date

2001-02-13

Citation

Letter to the Editor: Backbone (1H, 15N, 13C) resonance assignments of a 21 kDa construct of S. aureus peptide deformylase
Scahill, T.A., Kloosterman, D.A., Cialdella, J.I., Deibel, M.R., Marshall, V.P., Yem, A.W.
J. Biomol. NMR (2001), 19, 81-82, PubMed , DOI:

Related entities 1. Staphylococcal aureus peptide deformylase, : 2 : 128 entities Detail

Experiments performed 8 experiments Detail

Chemical shift validation 4 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4834_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: bmr4834_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	shift_set_1	Warning	1307		94.7 (chain: 1, length: 189)
1	Chemical shift references	chemical_shift_reference	OK	3		No information

Assigned chemical shifts

Saveframe: shift_set_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 189, Sequence coverage: 94.7%
- Total number of assignments
  - ¹H chemical shifts: 632
  - ¹³C chemical shifts: 509
  - ¹⁵N chemical shifts: 166
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- Peptide bond of PRO
- 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	1146	610	53.2
¹³C chemical shifts	863	509	59.0
¹⁵N chemical shifts	203	166	81.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	381	348	91.3
¹³C chemical shifts	378	345	91.3
¹⁵N chemical shifts	180	166	92.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	765	262	34.2
¹³C chemical shifts	485	164	33.8
¹⁵N chemical shifts	23	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	119	11	9.2
¹³C chemical shifts	119	12	10.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	69	0	0.0
¹³C chemical shifts	69	0	0.0

Keywords antibiotics, drug discovery, peptide deformylase, pdf, NMR assignment

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Found 1 Document (1.155 seconds)

BMRB: 4834

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Staphylococcal aureus peptide deformylase, : 2 : 128 entities Detail

Experiments performed 8 experiments Detail

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Chemical shift validation 4 contents Detail