BMRB: 5844

ZR18 Structure determination

Authors

Baran, M.C., Aramini, J.M., Huang, Y.J., Xiao, R., Acton, T.B., Shih, L., Montelione, G.T.

Assembly

ZR18

Entity

1. ZR18 (polymer, Thiol state: not present), 91 monomers, 10471.62 Da Detail

MKIISISETP NHNTMKITLS ESREGMTSDT YTKVDDSQPA FINDILKVEG VKSIFHVMDF ISVDKENDAN WETVLPKVEA VFELEHHHHH H

Formula weight

10471.62 Da

Source organism

Staphylococcus aureus subsp. aureus Mu50

Exptl. method

NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts, coupling_constants

Chem. Shift Complete

Sequence coverage: 95.6 %, Completeness: 92.6 %, Completeness (bb): 94.1 % Detail

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Polymer type: polypeptide(L)

	Total	1H	13C	15N
All	92.6 % (987 of 1066)	92.5 % (508 of 549)	92.4 % (390 of 422)	93.7 % (89 of 95)
Backbone	94.1 % (508 of 540)	94.5 % (171 of 181)	94.1 % (255 of 271)	93.2 % (82 of 88)
Sidechain	91.7 % (564 of 615)	91.6 % (337 of 368)	91.7 % (220 of 240)	100.0 % (7 of 7)
Aromatic	60.9 % (56 of 92)	60.9 % (28 of 46)	60.0 % (27 of 45)	100.0 % (1 of 1)
Methyl	100.0 % (100 of 100)	100.0 % (50 of 50)	100.0 % (50 of 50)

1. ZR18

MKIISISETP NHNTMKITLS ESREGMTSDT YTKVDDSQPA FINDILKVEG VKSIFHVMDF ISVDKENDAN WETVLPKVEA VFELEHHHHH H

Show sample condition

Sample #1

Temperature 298 (±0.1) K, pH 6.5 (±0.5)

#	Name	Isotope labeling	Type	Concentration
1	ZR18	[U-100% 15N; U-5% 13C]		1.3 mM
2	MES			20 mM
3	NaCl			100 mM
4	CaCl2			5 mM
5	DTT			10 mM
6	NaN3			0.02 %
7	D2O			5 %

Sample #2

Temperature 298 (±0.1) K, pH 6.5 (±0.5)

#	Name	Isotope labeling	Type	Concentration
8	ZR18	[U-100% 15N; U-100% 13C]		1.15 mM
9	MES			20 mM
10	NaCl			100 mM
11	CaCl2			5 mM
12	DTT			10 mM
13	NaN3			0.02 %
14	D2O			5 %

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LACS Plot; CA

Referencing offset: -0.15 ppm, Outliers: 2 Detail

Show chemical shift referencing parameters

Chemical shift reference

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

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LACS Plot; CB

Referencing offset: -0.15 ppm, Outliers: 2 Detail

Show chemical shift referencing parameters

Chemical shift reference

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

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LACS Plot; HA

Referencing offset: -0.04 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
1H	DSS	methyl protons	0.0 ppm	internal	direct	0.0
13C	DSS	methyl protons	0.0 ppm	external	indirect	0.0
15N	DSS	methyl protons	0.0 ppm	external	indirect	0.0

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LACS Plot; CO

Referencing offset: 0.17 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
1H	DSS	methyl protons	0.0 ppm	internal	direct	0.0
13C	DSS	methyl protons	0.0 ppm	external	indirect	0.0
15N	DSS	methyl protons	0.0 ppm	external	indirect	0.0

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Protein Blocks Logo

Calculated from 10 models in PDB: 2M6Q, Strand ID: A Detail

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Coupling constant

60 J values in 1 lists
Temperature 298 (±0.1) K, pH 6.5 (±0.5) Detail

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Temperature 298 (±0.1) K, pH 6.5 (±0.5)

List #1 coupling_constant_ZR18_JNH_1

Release date

2004-07-25

Citation 1

FAST-NMR: functional annotation screening technology using NMR spectroscopy
Mercier, K.A., Baran, M., Ramanathan, V., Revesz, P., Xiao, R., Montelione, G.T., Powers, R.
J. Am. Chem. Soc. (2006), 128, 15292-15299, PubMed 17117882 , DOI 10.1021/ja0651759 , Abstract

Show more 6 citaions

Citation 2

Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3
Kawarabayasi, Y., Sawada, M., Horikawa, H., Haikawa, Y., Hino, Y., Yamamoto, S., Sekine, M., Baba, S., Kosugi, H., Hosoyama, A., Nagai, Y., Sakai, M., Ogura, K., Otsuka, R., Nakazawa, H., Takamiya, M., Ohfuku, Y., Funahashi, T., Tanaka, T., Kudoh, Y., Yamazaki, J., Kushida, N., Oguchi, A., Aoki, K., Kikuchi, H.
DNA Res. (1998), 5, 55-76, PubMed 9679194 , Abstract

Citation 3

NMRPipe: a multidimensional spectral processing system based on UNIX pipes
Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., Bax, A.
J. Biomol. NMR (1995), 6, 277-293, PubMed 8520220 , Abstract

Citation 4

Automated analysis of protein NMR assignments using methods from artificial intelligence
Zimmerman, D.E., Kulikowski, C.A., Huang, Y., Feng, W., Tashiro, M., Shimotakahara, S., Chien, C., Powers, R., Montelione, G.T.
J. Mol. Biol. (1997), 269, 592-610, PubMed 9217263 , DOI 10.1006/jmbi.1997.1052 , Abstract

Citation 5

SPINS: standardized protein NMR storage. A data dictionary and object-oriented relational database for archiving protein NMR spectra
Baran, M.C., Moseley, H.N., Sahota, G., Montelione, G.T.
J. Biomol. NMR (2002), 24, 113-121, PubMed 12495027 , Abstract

Citation 6

Protein backbone angle restraints from searching a database for chemical shift and sequence homology
Cornilescu, G., Delaglio, F., Bax, A.
J. Biomol. NMR (1999), 13, 289-302, PubMed 10212987 , Abstract

Citation 7

Torsion angle dynamics for NMR structure calculation with the new program DYANA
Guntert, P., Mumenthaler, C., Wuthrich, K.
J. Mol. Biol. (1997), 273, 283-298, PubMed 9367762 , DOI 10.1006/jmbi.1997.1284 , Abstract

Hide non-primary 6 citaions

Related entities 1. ZR18, : 1 : 2 : 2 : 37 entities Detail

Experiments performed 19 experiments Detail