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BMRB: 16503

8R5V

Ribonuclease A in 40% acetic acid and 8M urea pH 2

Authors

L pez Alonso, J., Bruix, M., Laurents, D.

Assembly

RNase A

Entity

1. RNase A (polymer, Thiol state: all disulfide bound), 124 monomers, 13690.17 Da Detail

KETAAAKFER QHMDSSTSAA SSSNYCNQMM KSRNLTKDRC KPVNTFVHES LADVQAVCSQ KNVACKNGQT NCYQSYSTMS ITDCRETGSS KYPNCAYKTT QANKHIIVAC EGNPYVPVHF DASV

Formula weight

13690.17 Da

Entity Connection

disulfide 4 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS26:SG	1:CYS84:SG
2	disulfide	sing	1:CYS40:SG	1:CYS95:SG
3	disulfide	sing	1:CYS58:SG	1:CYS110:SG
4	disulfide	sing	1:CYS65:SG	1:CYS72:SG

Source organism

Bos taurus

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete1

Sequence coverage: 100.0 %, Completeness: 55.6 %, Completeness (bb): 96.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	55.6 % (765 of 1376)	38.5 % (275 of 714)	70.9 % (372 of 525)	86.1 % (118 of 137)
Backbone	96.9 % (713 of 736)	96.0 % (237 of 247)	97.0 % (358 of 369)	98.3 % (118 of 120)
Sidechain	22.3 % (170 of 761)	8.1 % (38 of 467)	47.7 % (132 of 277)	0.0 % (0 of 17)
Aromatic	3.2 % (3 of 94)	6.4 % (3 of 47)	0.0 % (0 of 47)
Methyl	19.0 % (19 of 100)	8.0 % (4 of 50)	30.0 % (15 of 50)

1. RNase A

KETAAAKFER QHMDSSTSAA SSSNYCNQMM KSRNLTKDRC KPVNTFVHES LADVQAVCSQ KNVACKNGQT NCYQSYSTMS ITDCRETGSS KYPNCAYKTT QANKHIIVAC EGNPYVPVHF DASV

Show sample condition

Sample #1

Solvent system 40% acetic acid (deuterated), 50% H2O (milliQ), 10% D2O, Pressure 1 atm, Temperature 298 K, pH 2

#	Name	Isotope labeling	Concentration
1	RNase A	[U-13C]	1.7 mM
2	acetic acid	natural abundance	40 %
3	H2O	natural abundance	50 %
4	D2O	natural abundance	10 %

Sample #2

Solvent system 8 M urea pH 2.5 10% D2O, Pressure 1 atm, Temperature 298 K, pH 2

#	Name	Isotope labeling	Concentration
5	RNase A	[U-100% 13C; U-100% 15N]	1.7 mM
6	D2O	natural abundance	10 %
7	urea	natural abundance	8 M

Chem. Shift Complete2

Sequence coverage: 100.0 %, Completeness: 48.3 %, Completeness (bb): 83.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	48.3 % (1330 of 2752)	31.6 % (451 of 1428)	61.6 % (647 of 1050)	84.7 % (232 of 274)
Backbone	83.0 % (1222 of 1472)	74.9 % (370 of 494)	84.3 % (622 of 738)	95.8 % (230 of 240)
Sidechain	22.5 % (343 of 1522)	8.7 % (81 of 934)	46.9 % (260 of 554)	5.9 % (2 of 34)
Aromatic	3.7 % (7 of 188)	5.3 % (5 of 94)	2.1 % (2 of 94)
Methyl	21.5 % (43 of 200)	12.0 % (12 of 100)	31.0 % (31 of 100)

1. RNase A

KETAAAKFER QHMDSSTSAA SSSNYCNQMM KSRNLTKDRC KPVNTFVHES LADVQAVCSQ KNVACKNGQT NCYQSYSTMS ITDCRETGSS KYPNCAYKTT QANKHIIVAC EGNPYVPVHF DASV

Show sample condition

Sample #1

Solvent system 40% acetic acid (deuterated), 50% H2O (milliQ), 10% D2O, Pressure 1 atm, Temperature 298 K, pH 2

#	Name	Isotope labeling	Concentration
1	RNase A	[U-13C]	1.7 mM
2	acetic acid	natural abundance	40 %
3	H2O	natural abundance	50 %
4	D2O	natural abundance	10 %

Sample #2

Solvent system 8 M urea pH 2.5 10% D2O, Pressure 1 atm, Temperature 298 K, pH 2

#	Name	Isotope labeling	Concentration
5	RNase A	[U-100% 13C; U-100% 15N]	1.7 mM
6	D2O	natural abundance	10 %
7	urea	natural abundance	8 M

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	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: -0.21 ppm, Outliers: 5 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	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: -0.21 ppm, Outliers: 5 Detail

Release date

2010-01-25

Citation

NMR spectroscopy reveals that RNase A is chiefly denatured in 40% acetic acid: implications for oligomer formation by 3D domain swapping
Lopez-Alonso, J., Bruix, M., Font, J., Ribo, M., Vilanova, M., Jimenez, M., Santoro, J., Gonzalez, C., Laurents, D.V.
J. Am. Chem. Soc. (2010), 132, 1621-1630, PubMed 20085318 , DOI 10.1021/ja9081638 , Abstract

Entries sharing articles BMRB: 2 entries Detail

  BMRB: 16010 released on 2010-10-17
    Title How do Proteins Form Amyloid? Insight from the NMR Spectroscopic Characterization of 13C, 15N-labeled Ribonuclease A in 40% Acetic Acid
  BMRB: 16011 released on 2010-10-17
    Title NMR Spectroscopic Characterization of 13C, 15N-labeled Ribonuclease A in urea 8M

Related entities 1. RNase A, : 1 : 101 : 139 entities Detail

Interaction partners 1. RNase A, : 8 interactors Detail

More details for 8 interactors identified by 6 citations