BMRBj - BMREntryMaster

Found 1 Document (1.308 seconds)

BMRB: 4848

1Q36

Conformational Changes in the Isolated N-terminal Domain of 5-Enolpyruvylshikimate-3-phosphate Synthase upon Shikimate-3-phosphate Binding

Authors

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

Assembly

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

Entity

1. EPSP 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

2. shikimate-3-phosphate (non-polymer), 1 monomers, 254.131 Da

Total weight

25880.24 Da

Max. entity weight

25626.11 Da

Source organism

Escherichia coli

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 97.5 %, Completeness: 88.7 %, Completeness (bb): 93.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	88.7 % (2375 of 2679)	89.3 % (1230 of 1377)	87.6 % (923 of 1054)	89.5 % (222 of 248)
Backbone	93.1 % (1319 of 1416)	94.5 % (466 of 493)	91.5 % (636 of 695)	95.2 % (217 of 228)
Sidechain	85.3 % (1261 of 1478)	86.4 % (764 of 884)	85.7 % (492 of 574)	25.0 % (5 of 20)
Aromatic	19.0 % (24 of 126)	27.0 % (17 of 63)	11.1 % (7 of 63)
Methyl	99.7 % (329 of 330)	100.0 % (165 of 165)	99.4 % (164 of 165)

1. EPSP synthase

Show sample condition

Sample

Temperature 295 (±1) K

#	Name	Isotope labeling	Concentration
1	EPSP synthase	[U-15N; U-13C; U70%-2H]	1.0 mM
2	shikimate-3-phosphate		1.5 mM
3	Tris buffer		50 mM
4	DTT		1 mM
5	NaN3		3 mM
6	pepstatin		0.0 ~ 0.0 uM
7	leupeptin		0.0 ~ 0.0 uM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹H	H2O	water proton	4.74 ppm	internal	direct	1.0
¹⁵N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291
¹³C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495

Referencing offset: 0.33 ppm, Outliers: 6 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹H	H2O	water proton	4.74 ppm	internal	direct	1.0
¹⁵N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291
¹³C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495

Referencing offset: 0.33 ppm, Outliers: 6 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹H	H2O	water proton	4.74 ppm	internal	direct	1.0
¹⁵N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291
¹³C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495

Referencing offset: -0.07 ppm, Outliers: 1 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹H	H2O	water proton	4.74 ppm	internal	direct	1.0
¹⁵N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291
¹³C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495

Referencing offset: 0.47 ppm, Outliers: 2 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

Entries sharing articles BMRB: 1 entries Detail

BMRB: 4854 released on 2001-11-13
Title Chemical shift assignments for the isolated N-terminal domain of EPSP synthase

Related entities 1. EPSP synthase, : 1 : 9 : 1 : 17 : 132 entities Detail

Interaction partners 1. EPSP synthase, : 2 interactors Detail

More details for 2 interactors identified by 1 citations

Chemical shift validation 4 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4848_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: bmr4848_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	Nterm+S3P_cs	Warning	2670		96.7 (chain: 1, length: 240)
1	Chemical shift references	chemical_shift_reference	Warning	3		No information

Assigned chemical shifts

Saveframe: Nterm+S3P_cs
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 240, Sequence coverage: 96.7%
- Total number of assignments
  - ¹H chemical shifts: 1546
  - ¹³C chemical shifts: 906
  - ¹⁵N chemical shifts: 218
- 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	1206	87.6
¹³C chemical shifts	1054	906	86.0
¹⁵N chemical shifts	259	218	84.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	493	469	95.1
¹³C chemical shifts	480	425	88.5
¹⁵N chemical shifts	228	218	95.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	884	737	83.4
¹³C chemical shifts	574	481	83.8
¹⁵N chemical shifts	31	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	171	170	99.4
¹³C chemical shifts	171	169	98.8

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 (1.308 seconds)

BMRB: 4848

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Entries sharing articles BMRB: 1 entries Detail

Related entities 1. EPSP synthase, : 1 : 9 : 1 : 17 : 132 entities Detail

Interaction partners 1. EPSP synthase, : 2 interactors Detail

Chemical shift validation 4 contents Detail