BMRB: 4917

Solution structure of a lipid transfer protein extracted from rice seeds. Comparison with homologous proteins

Authors

Poznanski, J.

Assembly

Lipid Transfer Protein

Entity

1. Lipid Transfer Protein (polymer, Thiol state: all disulfide bound), 91 monomers, 8909.102 Da Detail

ITCGQVNSAV GPCLTYARGG AGPSAACCSG VRSLKAAAST TADRRTACNC LKNAARGIKG LNAGNAASIP SKCGVSVPYT ISASIDCSRV S

Formula weight

8909.102 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

Oryza sativa

Exptl. method

NMR

Refine. method

DISTANCE GEOMETRY

Data set

assigned_chemical_shifts, coupling_constants

Chem. Shift Complete1

Sequence coverage: 100.0 %, Completeness: 98.5 %, Completeness (bb): 98.4 % Detail

Download

• NMR-STAR v3.1 (partial)
• BMRB/XML (partial)
• CSV
• TSV

Polymer type: polypeptide(L)

	Total	1H
All	98.5 % (452 of 459)	98.5 % (452 of 459)
Backbone	98.4 % (185 of 188)	98.4 % (185 of 188)
Sidechain	98.5 % (267 of 271)	98.5 % (267 of 271)
Aromatic	100.0 % (8 of 8)	100.0 % (8 of 8)
Methyl	100.0 % (52 of 52)	100.0 % (52 of 52)

1. Nonspecific Lipid Transfer Protein

ITCGQVNSAV GPCLTYARGG AGPSAACCSG VRSLKAAAST TADRRTACNC LKNAARGIKG LNAGNAASIP SKCGVSVPYT ISASIDCSRV S

Show sample condition

Sample

Temperature 298 (±1) K

#	Name	Isotope labeling	Type	Concentration
1	Nonspecific Lipid Transfer Protein			5 mM
2	phosphate buffer			50 mM

Hide sample codition

Chem. Shift Complete2

Sequence coverage: 100.0 %, Completeness: 98.3 %, Completeness (bb): 97.9 % Detail

Download

• NMR-STAR v3.1 (partial)
• BMRB/XML (partial)
• CSV
• TSV

Polymer type: polypeptide(L)

	Total	1H
All	98.3 % (902 of 918)	98.3 % (902 of 918)
Backbone	97.9 % (368 of 376)	97.9 % (368 of 376)
Sidechain	98.5 % (534 of 542)	98.5 % (534 of 542)
Aromatic	100.0 % (16 of 16)	100.0 % (16 of 16)
Methyl	100.0 % (104 of 104)	100.0 % (104 of 104)

1. Nonspecific Lipid Transfer Protein

ITCGQVNSAV GPCLTYARGG AGPSAACCSG VRSLKAAAST TADRRTACNC LKNAARGIKG LNAGNAASIP SKCGVSVPYT ISASIDCSRV S

Show sample condition

Sample

Temperature 283 (±1) K

#	Name	Isotope labeling	Type	Concentration
1	Nonspecific Lipid Transfer Protein			5 mM
2	phosphate buffer			50 mM

Hide sample codition

Protein Blocks Logo

Calculated from 14 models in PDB: 1BV2, Strand ID: A Detail

---

Coupling constant

61 J values in 1 lists
Temperature 298 (±1) K Detail

---

Temperature 298 (±1) K

List #1 J_values_rtp25

Release date

2001-01-08

Citation 1

Solution structure of a lipid transfer protein extracted from rice seeds. Comparison with homologous proteins
Poznanski, J., Sodano, P., Suh, S.WON., Lee, J.YOUNG., Ptak, M., Vovelle, F.
Eur. J. Biochem. (1999), 259, 692-708, PubMed 10092854 , DOI: , Abstract

Show more 4 citaions

Citation 2

Amino acid sequence of a probable amylase/protease inhibitor from rice seeds
Yu, Y.G., Chung, C.H., Fowler, A., Suh, S.W.
Arch. Biochem. Biophys. (1988), 265, 466-475, PubMed 2458699 , DOI: , Abstract

Citation 3

The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
Bartels, C., Xia, T., Billeter, M., Guntert, P., Wuthrich, K.
J. Biomol. NMR (1995), 6, 1-10, PubMed , DOI:

Citation 4

Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA
Guntert, P., Braun, W., Wuthrich, K.
J. Mol. Biol. (1991), 217, 517-530, PubMed 1847217 , DOI: , Abstract

Citation 5

X-PLOR, version 3.1: A system for X-ray crystallography and NMR
Brunger, A.T.

Hide non-primary 4 citaions

Related entities 1. Lipid Transfer Protein, : 1 : 6 : 1 : 211 entities Detail

Experiments performed 5 experiments Detail