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BMRB: 16294

2B5S

1H (NH, HA, HB, other) Chemical Shift Assignments of Peach Pru p 3, Non-Specific Lipid Transfer Protein (nsLTP) isolated from Peach fruit skin

Authors

Wijesinha-Bettoni, R., Alexeev, Y., Johnson, P.A., Marsh, J.A., Sancho, A.I., Mackie, A.R., Shewry, P.R., Smith, L.J., Mills, E.CLARE.

Assembly

Pru p 3 (nsLTP)

Entity

1. Pru p 3 (nsLTP) (polymer, Thiol state: all disulfide bound), 91 monomers, 9143.475 Da Detail

ITCGQVSSSL APCIPYVRGG GAVPPACCNG IRNVNNLART TPDRQAACNC LKQLSASVPG VNPNNAAALP GKCGVSIPYK ISASTNCATV K

Formula weight

9143.475 Da

Entity Connection

disulfide 4 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS3:SG	1:CYS50:SG
2	disulfide	sing	1:CYS13:SG	1:CYS27:SG
3	disulfide	sing	1:CYS28:SG	1:CYS73:SG
4	disulfide	sing	1:CYS48:SG	1:CYS87:SG

Source organism

Exptl. method

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 87.9 %, Completeness: 58.0 %, Completeness (bb): 90.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	58.0 % (285 of 491)	58.0 % (285 of 491)
Backbone	90.6 % (164 of 181)	90.6 % (164 of 181)
Sidechain	39.0 % (121 of 310)	39.0 % (121 of 310)
Aromatic	0.0 % (0 of 8)	0.0 % (0 of 8)
Methyl	58.5 % (31 of 53)	58.5 % (31 of 53)

1. Pru p 3 (nsLTP)

ITCGQVSSSL APCIPYVRGG GAVPPACCNG IRNVNNLART TPDRQAACNC LKQLSASVPG VNPNNAAALP GKCGVSIPYK ISASTNCATV K

Show sample condition

Sample

Solvent system 95% H2O/5% D2O, Temperature 310 (±1) K, pH 5.3 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Pru p 3 (nsLTP)	natural abundance		2.0 ~ 3.0 (±0.2) mM
2	H2O	natural abundance		95 %
3	D2O	natural abundance		5 %

Release date

2010-02-28

Citation 1

Crystal structure of peach Pru p 3, the prototypic member of the family of plant non-specific lipid transfer protein pan-allergens
Pasquato, N., Berni, R., Folli, C., Folloni, S., Cianci, M., Pantano, S., Helliwell, J.R., Zanotti, G.
J. Mol. Biol. (2006), 356, 684-694, PubMed 16388823 , DOI 10.1016/j.jmb.2005.11.063 , Abstract

Show more 1 citaion

Citation 2

The structural characteristics of nonspecific lipid transfer proteins explain their resistance to gastroduodenal proteolysis
Wijesinha-Bettoni, R., Alexeev, Y., Johnson, P., Marsh, J., Sancho, A.I., Abdullah, S.U., Mackie, A.R., Shewry, P.R., Smith, L.J., Mills, E.
Biochemistry (2010), 49, 2130-2139, PubMed 20121231 , DOI 10.1021/bi901939z , Abstract

Hide non-primary 1 citaion

Entries sharing articles Swiss-Prot: 1 entries Detail

Swiss-Prot: P81402 released on 1998-07-15
Title NLTP1_PRUPE Entity Non-specific lipid-transfer protein 1

Related entities 1. Pru p 3 (nsLTP), : 1 : 1 : 213 entities Detail

Experiments performed 14 experiments Detail

1 2D 1H-1H TOCSY

Instrument

Home-built ?,AM - 600 MHz The home-built spectrometer consists of an Oxford Instruments magnet, the GE-Omega data acquisition software and home-built probe.

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Temperature 310 (±1) K, pH 5.3 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Pru p 3 (nsLTP)	natural abundance		2.0 ~ 3.0 (±0.2) mM
2	H2O	natural abundance		95 %
3	D2O	natural abundance		5 %

2 2D 1H-1H COSY

Instrument

Home-built ?,AM - 600 MHz The home-built spectrometer consists of an Oxford Instruments magnet, the GE-Omega data acquisition software and home-built probe.

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Temperature 310 (±1) K, pH 5.3 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Pru p 3 (nsLTP)	natural abundance		2.0 ~ 3.0 (±0.2) mM
2	H2O	natural abundance		95 %
3	D2O	natural abundance		5 %

3 2D 1H-1H NOESY

Instrument

Home-built ?,AM - 600 MHz The home-built spectrometer consists of an Oxford Instruments magnet, the GE-Omega data acquisition software and home-built probe.

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Temperature 310 (±1) K, pH 5.3 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Pru p 3 (nsLTP)	natural abundance		2.0 ~ 3.0 (±0.2) mM
2	H2O	natural abundance		95 %
3	D2O	natural abundance		5 %

4 2D DQF-COSY

Instrument

Home-built ?,AM - 600 MHz The home-built spectrometer consists of an Oxford Instruments magnet, the GE-Omega data acquisition software and home-built probe.

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Temperature 310 (±1) K, pH 5.3 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Pru p 3 (nsLTP)	natural abundance		2.0 ~ 3.0 (±0.2) mM
2	H2O	natural abundance		95 %
3	D2O	natural abundance		5 %

5 2D 1H-1H TOCSY

Instrument

Home-built ?,AM - 600 MHz The home-built spectrometer consists of an Oxford Instruments magnet, the GE-Omega data acquisition software and home-built probe.

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Temperature 298 (±1) K, pH 5.3 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Pru p 3 (nsLTP)	natural abundance		2.0 ~ 3.0 (±0.2) mM
2	H2O	natural abundance		95 %
3	D2O	natural abundance		5 %

6 2D 1H-1H COSY

Instrument

Home-built ?,AM - 600 MHz The home-built spectrometer consists of an Oxford Instruments magnet, the GE-Omega data acquisition software and home-built probe.

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Temperature 298 (±1) K, pH 5.3 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Pru p 3 (nsLTP)	natural abundance		2.0 ~ 3.0 (±0.2) mM
2	H2O	natural abundance		95 %
3	D2O	natural abundance		5 %

7 2D 1H-1H NOESY

Instrument

Home-built ?,AM - 600 MHz The home-built spectrometer consists of an Oxford Instruments magnet, the GE-Omega data acquisition software and home-built probe.

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Temperature 298 (±1) K, pH 5.3 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Pru p 3 (nsLTP)	natural abundance		2.0 ~ 3.0 (±0.2) mM
2	H2O	natural abundance		95 %
3	D2O	natural abundance		5 %

8 2D 1H-1H NOESY

Instrument

Home-built ?,AM - 600 MHz The home-built spectrometer consists of an Oxford Instruments magnet, the GE-Omega data acquisition software and home-built probe.

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Temperature 298 (±1) K, pH 4 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Pru p 3 (nsLTP)	natural abundance		2.0 ~ 3.0 (±0.2) mM
2	H2O	natural abundance		95 %
3	D2O	natural abundance		5 %

9 2D 1H-1H TOCSY

Instrument

Home-built ?,AM - 600 MHz The home-built spectrometer consists of an Oxford Instruments magnet, the GE-Omega data acquisition software and home-built probe.

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Temperature 293 (±1) K, pH 6.5 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Pru p 3 (nsLTP)	natural abundance		2.0 ~ 3.0 (±0.2) mM
2	H2O	natural abundance		95 %
3	D2O	natural abundance		5 %

10 2D 1H-1H COSY

Instrument

Home-built ?,AM - 600 MHz The home-built spectrometer consists of an Oxford Instruments magnet, the GE-Omega data acquisition software and home-built probe.

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Temperature 293 (±1) K, pH 6.5 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Pru p 3 (nsLTP)	natural abundance		2.0 ~ 3.0 (±0.2) mM
2	H2O	natural abundance		95 %
3	D2O	natural abundance		5 %

11 2D 1H-1H NOESY

Instrument

Home-built ?,AM - 600 MHz The home-built spectrometer consists of an Oxford Instruments magnet, the GE-Omega data acquisition software and home-built probe.

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Temperature 293 (±1) K, pH 6.5 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Pru p 3 (nsLTP)	natural abundance		2.0 ~ 3.0 (±0.2) mM
2	H2O	natural abundance		95 %
3	D2O	natural abundance		5 %

12 2D 1H-1H TOCSY

Instrument

Home-built ?,AM - 600 MHz The home-built spectrometer consists of an Oxford Instruments magnet, the GE-Omega data acquisition software and home-built probe.

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Temperature 310 (±1) K, pH 1.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Pru p 3 (nsLTP)	natural abundance		2.0 ~ 3.0 (±0.2) mM
2	H2O	natural abundance		95 %
3	D2O	natural abundance		5 %

13 2D 1H-1H COSY

Instrument

Home-built ?,AM - 600 MHz The home-built spectrometer consists of an Oxford Instruments magnet, the GE-Omega data acquisition software and home-built probe.

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Temperature 310 (±1) K, pH 1.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Pru p 3 (nsLTP)	natural abundance		2.0 ~ 3.0 (±0.2) mM
2	H2O	natural abundance		95 %
3	D2O	natural abundance		5 %

14 2D 1H-1H NOESY

Instrument

Home-built ?,AM - 600 MHz The home-built spectrometer consists of an Oxford Instruments magnet, the GE-Omega data acquisition software and home-built probe.

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Temperature 310 (±1) K, pH 1.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	Pru p 3 (nsLTP)	natural abundance		2.0 ~ 3.0 (±0.2) mM
2	H2O	natural abundance		95 %
3	D2O	natural abundance		5 %

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr16294_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	True (see coordinates for details)
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:3:CYS:SG	1:50:CYS:SG	unknown	unknown	n/a
1:13:CYS:SG	1:27:CYS:SG	unknown	unknown	n/a
1:28:CYS:SG	1:73:CYS:SG	unknown	unknown	n/a
1:48:CYS:SG	1:87:CYS:SG	unknown	unknown	n/a

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Content subtype: bmr16294_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	332		84.6 (chain: 1, length: 91)
1	Chemical shift references	chemical_shift_reference_1	OK	1		No information

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 91, Sequence coverage: 84.6%
- Total number of assignments
  - ¹H chemical shifts: 332
- Completeness of assignments
  - Entity_assemble_ID: 1
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1