BMRB: 7167

1H, 15N, 13C resonance assignments for regeneration-induced CNPase homolog (RICH) protein

Authors

Denisov, A., Kozlov, G., Gehring, K.

Assembly

RICH protein

Entity

1. RICH protein (polymer, Thiol state: all free), 222 monomers, 24587.54 Da Detail

GSHMELPLFF GWFLLPEEEE RIKCATMDFL KTLDTLEAFK EHISEFTGEA EKEVDLEQYF QNPLQLHCTT KFCDYGKAEG AKEYAELQVV KESLTKSYEL SVTALIVTPR TFGARVALTE AQVKLWPEGA DKEGVAPALL PSVEALPAGS RAHVTLGCSA GVETVQTGLD LLEILALQKE GKEGTQVEMD LGTLTYLSEG RWFLALREPI NADTTFTSFS ED

Formula weight

24587.54 Da

Source organism

Carassius auratus

Exptl. method

NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 99.5 %, Completeness: 70.5 %, Completeness (bb): 98.3 % Detail

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Polymer type: polypeptide(L)

	Total	1H	13C	15N
All	70.5 % (1801 of 2556)	68.9 % (905 of 1314)	66.9 % (680 of 1016)	95.6 % (216 of 226)
Backbone	98.3 % (1292 of 1314)	97.6 % (440 of 451)	98.6 % (641 of 650)	99.1 % (211 of 213)
Sidechain	49.4 % (715 of 1448)	53.9 % (465 of 863)	42.8 % (245 of 572)	38.5 % (5 of 13)
Aromatic	6.6 % (14 of 212)	10.4 % (11 of 106)	0.0 % (0 of 103)	100.0 % (3 of 3)
Methyl	60.7 % (165 of 272)	90.4 % (123 of 136)	30.9 % (42 of 136)

1. RICH protein

GSHMELPLFF GWFLLPEEEE RIKCATMDFL KTLDTLEAFK EHISEFTGEA EKEVDLEQYF QNPLQLHCTT KFCDYGKAEG AKEYAELQVV KESLTKSYEL SVTALIVTPR TFGARVALTE AQVKLWPEGA DKEGVAPALL PSVEALPAGS RAHVTLGCSA GVETVQTGLD LLEILALQKE GKEGTQVEMD LGTLTYLSEG RWFLALREPI NADTTFTSFS ED

Show sample condition

Sample

Temperature 307 (±0.5) K, pH 6.0 (±0.1), Details 10%/90% D2O/H2O

#	Name	Isotope labeling	Type	Concentration
1	RICH protein	[U-99% 13C; U-99% 15N]		1 mM
2	MES buffer			50 mM
3	NaCl			150 mM
4	D2O			10 %
5	H2O			90 %

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LACS Plot; CA

Referencing offset: -0.09 ppm, Outliers: 1 Detail

Show chemical shift referencing parameters

Chemical shift reference

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

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LACS Plot; CB

Referencing offset: -0.09 ppm, Outliers: 1 Detail

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Chemical shift reference

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

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LACS Plot; HA

Referencing offset: 0.04 ppm, Outliers: 1 Detail

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Chemical shift reference

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

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LACS Plot; CO

Referencing offset: -0.5 ppm, Outliers: 1 Detail

Show chemical shift referencing parameters

Chemical shift reference

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

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Protein Blocks Logo

Calculated from 10 models in PDB: 2I3E, Strand ID: A Detail

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Release date

2006-10-01

Citation 1

1H, 13C and 15N resonance assignments of the catalytic domain of the goldfish RICH protein
Denisov, A., Kozlov, G., Gravel, M., Sprules, T., Braun, P., Gehring, K.
J. Biomol. NMR (2006), 36 Suppl 1, 75-75, PubMed 17031527 , DOI 10.1007/s10858-006-9080-3 , Abstract

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Citation 2

Solution structure of the catalytic domain of RICH protein from goldfish
Denisov, A., Kozlov, G., Gravel, M., Braun, P., Gehring, K.
FEBS J. (2007), 274, 1600-1609, PubMed 17480208 , DOI 10.1111/j.1742-4658.2007.05707.x , Abstract

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Related entities 1. RICH protein, : 1 : 49 entities Detail

Experiments performed 6 experiments Detail