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Found 1 Document (1.467 seconds)

BMRB: 4854

1Q36

Chemical shift assignments for the isolated N-terminal domain of EPSP synthase

Authors

Stauffer, M., Young, J., Helms, G., Evans, J.N.S.

Assembly

N-terminal domain of 5-enolpyruvyl shikimate-3-phosphate synthase

Entity

1. N-terminal domain of 5-enolpyruvyl shikimate-3-phosphate synthase (polymer, Thiol state: all free), 240 monomers, 25626.11 Da Detail

MESLTLQPIA RVDGTINLPG SKSVSNRALL LAALAHGKTV LTNLLDSDDV RHMLNALTAL GVSYTLSADR TRCEIIGNGG PLHAEGALEL FLGNAGTAMR PLAAALCLGS NDIVLTGEPR MKERPIGHLV DALRLGGAKI TYLEQENYPP LRLQGGFTGG NVDVDGSVSS QFLTALLMTA PLAPEDTVIR IKGDLVSKPY IDITLNLMKT FGVEIENQHY QQFVVKGGQS YQSPGTYLVE

Formula weight

25626.11 Da

Source organism

Escherichia coli

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 97.1 %, Completeness: 82.7 %, Completeness (bb): 87.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	82.7 % (2216 of 2679)	81.9 % (1128 of 1377)	84.3 % (889 of 1054)	80.2 % (199 of 248)
Backbone	87.4 % (1238 of 1416)	86.6 % (427 of 493)	88.6 % (616 of 695)	85.5 % (195 of 228)
Sidechain	78.9 % (1166 of 1478)	79.3 % (701 of 884)	80.3 % (461 of 574)	20.0 % (4 of 20)
Aromatic	13.5 % (17 of 126)	15.9 % (10 of 63)	11.1 % (7 of 63)
Methyl	95.5 % (315 of 330)	93.9 % (155 of 165)	97.0 % (160 of 165)

1. N-terminal EPSP synthase

Show sample condition

Sample

Temperature 295 (±1) K

#	Name	Isotope labeling	Concentration
1	N-terminal EPSP synthase	[U-15N; U-13C; U-70% 2H]	1.0 mM
2	Tris		50 mM
3	DTT		1 mM

LACS Plot; CA

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

Referencing offset: -0.1 ppm, Outliers: 3 Detail

LACS Plot; CB

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

Referencing offset: -0.1 ppm, Outliers: 3 Detail

LACS Plot; HA

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

Referencing offset: -0.07 ppm, Outliers: 3 Detail

LACS Plot; CO

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

Referencing offset: 0.29 ppm, Outliers: 7 Detail

Release date

2001-11-13

Citation

Sequential assignments of the isolated N-terminal domain of 5-enolpyruvylshikimate-3-phosphate synthase
Stauffer, M.E., Young, J.K., Helms, G.L., Evans, J.N.S.
J. Biomol. NMR (2001), 20, 387-388, PubMed 11563562 , Abstract

Related entities 1. N-terminal domain of 5-enolpyruvyl shikimate-3-phosphate synthase, : 1 : 9 : 1 : 17 : 132 entities Detail

Interaction partners 1. N-terminal domain of 5-enolpyruvyl shikimate-3-phosphate synthase, : 2 interactors Detail

More details for 2 interactors identified by 1 citations

Experiments performed 7 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4854_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: bmr4854_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	chemical_shifts	Warning	2472		97.1 (chain: 1, length: 240)
1	Chemical shift references	chemical_shift_reference	OK	3		No information

Assigned chemical shifts

Saveframe: chemical_shifts
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 240, Sequence coverage: 97.1%
- Total number of assignments
  - ¹H chemical shifts: 1410
  - ¹³C chemical shifts: 867
  - ¹⁵N chemical shifts: 195
- 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	1377	1090	79.2
¹³C chemical shifts	1054	867	82.3
¹⁵N chemical shifts	259	195	75.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	493	415	84.2
¹³C chemical shifts	480	417	86.9
¹⁵N chemical shifts	228	195	85.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	884	675	76.4
¹³C chemical shifts	574	450	78.4
¹⁵N chemical shifts	31	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	171	160	93.6
¹³C chemical shifts	171	165	96.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	63	0	0.0
¹³C chemical shifts	63	0	0.0

Keywords NMR, EPSP synthase, shikimate-3-phosphate, MurA

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Found 1 Document (1.467 seconds)

BMRB: 4854

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. N-terminal domain of 5-enolpyruvyl shikimate-3-phosphate synthase, : 1 : 9 : 1 : 17 : 132 entities Detail

Interaction partners 1. N-terminal domain of 5-enolpyruvyl shikimate-3-phosphate synthase, : 2 interactors Detail

Experiments performed 7 experiments Detail

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Chemical shift validation 3 contents Detail