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BMRB: 11546

2RVK

1H, 15N and 13C resonance assignments of the conserved domain in the middle of Schizosaccharomyces pombe SAPK-interacting protein 1

Authors

Kataoka, S., Furuita, K., Hattori, Y., Kobayashi, N., Ikegami, T., Shiozaki, K., Fujiwara, T., Kojima, C.

Assembly

sin1

Entity

1. sin1 (polymer, Thiol state: not present), 160 monomers, 17573.45 Da Detail

GPGHMGSVSN AKAPTSALRA LLEHKENSSQ NGPLAENFAT FSGHAESNAL RLNIYFPSSE SPSKPLFVEL RKNVLVSEAI GYILLQYVNQ QLVPPIEDEA QNPNYWNLRI VEDDGELDED FPALDRVGPL SKFGFDAFAL VKATPAQIKE NQAAYPFKSK

Formula weight

17573.45 Da

Source organism

Schizosaccharomyces pombe

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 96.9 %, Completeness: 78.9 %, Completeness (bb): 90.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	78.9 % (1466 of 1857)	77.3 % (748 of 968)	79.2 % (572 of 722)	87.4 % (146 of 167)
Backbone	90.8 % (848 of 934)	90.8 % (287 of 316)	89.6 % (422 of 471)	94.6 % (139 of 147)
Sidechain	70.5 % (757 of 1074)	70.7 % (461 of 652)	71.9 % (289 of 402)	35.0 % (7 of 20)
Aromatic	28.6 % (44 of 154)	42.9 % (33 of 77)	13.2 % (10 of 76)	100.0 % (1 of 1)
Methyl	83.9 % (141 of 168)	89.3 % (75 of 84)	78.6 % (66 of 84)

1. sin1

GPGHMGSVSN AKAPTSALRA LLEHKENSSQ NGPLAENFAT FSGHAESNAL RLNIYFPSSE SPSKPLFVEL RKNVLVSEAI GYILLQYVNQ QLVPPIEDEA QNPNYWNLRI VEDDGELDED FPALDRVGPL SKFGFDAFAL VKATPAQIKE NQAAYPFKSK

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Temperature 303 K, pH 6.8

#	Name	Isotope labeling	Type	Concentration
1	sin1	[U-13C; U-15N]	protein	0.5 mM
2	H2O		solvent	90 %
3	D2O		solvent	10 %
4	potassium phosphate		buffer	50 mM
5	potassium chloride		salt	50 mM
6	DTT		reducing agent	1 mM

Sample #2

Solvent system 90% H2O/10% D2O, Temperature 303 K, pH 6.8

#	Name	Isotope labeling	Type	Concentration
7	sin1	natural abundance	protein	0.5 mM
8	H2O		solvent	90 %
9	D2O		solvent	10 %
10	potassium phosphate		buffer	50 mM
11	potassium chloride		salt	50 mM
12	DTT		reducing agent	1 mM

LACS Plot; CA

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

Referencing offset: -0.11 ppm, Outliers: 3 Detail

LACS Plot; CB

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

Referencing offset: -0.11 ppm, Outliers: 3 Detail

LACS Plot; HA

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

Referencing offset: 0.03 ppm, Outliers: 4 Detail

LACS Plot; CO

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

Referencing offset: 0.17 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 10 models in PDB: 2RVK, Strand ID: A Detail

Release date

2015-07-26

Citation

Utilization of paramagnetic relaxation enhancements for high-resolution NMR structure determination of a soluble loop-rich protein with sparse NOE distance restraints
Furuita, K., Kataoka, S., Hattori, Y., Kobayashi, N., Ikegami, T., Shiozaki, K., Fujiwara, T., Kojima, C.
J. Biomol. NMR (2015), 61, 55-64, PubMed 25428765 , DOI 10.1007/s10858-014-9882-7 , Abstract

Related entities 1. sin1, : 2 : 7 entities Detail

Interaction partners 1. sin1, : 2 interactors Detail

More details for 2 interactors identified by 2 citations

Experiments performed 10 experiments Detail

1 3D HNCO