BMRB: 5757

13C, 15N solid state NMR chemical shift assignments for the microcrystallin Crh domain swapped dimer

Authors

Bockmann, A., Lange, A., Galinier, A., Luca, S., Giraud, N., Juy, M., Heise, H., Montserret, R., Penin, F., Baldus, M.

Assembly

Crh dimer

Entity

1. Crh dimer (polymer, Thiol state: not present), 93 monomers, 10390.71 × 2 Da Detail

MVQQKVEVRL KTGLQARPAA LFVQEANRFT SDVFLEKDGK KVNAKSIMGL MSLAVSTGTE VTLIAQGEDE QEALEKLAAY VQEEVLQHHH HHH

Total weight

20781.42 Da

Max. entity weight

10390.71 Da

Source organism

Bacillus subtilis

Exptl. method

NMR

Refine. method

simulated annealing,

Data set

assigned_chemical_shifts

Chem. Shift Complete1

Sequence coverage: 90.3 %, Completeness: 79.1 %, Completeness (bb): 82.5 % Detail

Download

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

Polymer type: polypeptide(L)

	Total	13C	15N
All	79.1 % (412 of 521)	78.3 % (328 of 419)	82.4 % (84 of 102)
Backbone	82.5 % (302 of 366)	80.3 % (220 of 274)	89.1 % (82 of 92)
Sidechain	77.8 % (189 of 243)	80.3 % (187 of 233)	20.0 % (2 of 10)
Aromatic	32.3 % (10 of 31)	32.3 % (10 of 31)
Methyl	93.2 % (55 of 59)	93.2 % (55 of 59)

1. catabolite repression HPr

MVQQKVEVRL KTGLQARPAA LFVQEANRFT SDVFLEKDGK KVNAKSIMGL MSLAVSTGTE VTLIAQGEDE QEALEKLAAY VQEEVLQHHH HHH

Show sample condition

Sample

Temperature 278 (±1) K, pH 6.9 (±0.2), Details Microcrystallin solid protein obtained by slow precipitation with PEG

#	Name	Isotope labeling	Type	Concentration
1	catabolite repression HPr	[U-98% 13C; U-98% 15N]		4.0 ~ 20.0 mg

Hide sample codition

Chem. Shift Complete2

Sequence coverage: 17.2 %, Completeness: 44.0 %, Completeness (bb): 46.6 % Detail

Download

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

Polymer type: polypeptide(L)

	Total	13C	15N
All	44.0 % (458 of 1042)	43.1 % (361 of 838)	47.5 % (97 of 204)
Backbone	46.6 % (341 of 732)	44.9 % (246 of 548)	51.6 % (95 of 184)
Sidechain	42.2 % (205 of 486)	43.6 % (203 of 466)	10.0 % (2 of 20)
Aromatic	16.1 % (10 of 62)	16.1 % (10 of 62)
Methyl	49.2 % (58 of 118)	49.2 % (58 of 118)

1. catabolite repression HPr

MVQQKVEVRL KTGLQARPAA LFVQEANRFT SDVFLEKDGK KVNAKSIMGL MSLAVSTGTE VTLIAQGEDE QEALEKLAAY VQEEVLQHHH HHH

Show sample condition

Sample

Temperature 278 (±1) K, pH 6.9 (±0.2), Details Microcrystallin solid protein obtained by slow precipitation with PEG

#	Name	Isotope labeling	Type	Concentration
1	catabolite repression HPr	[U-98% 13C; U-98% 15N]		4.0 ~ 20.0 mg

Hide sample codition

Protein Blocks Logo

Calculated from 24 models in PDB: 1K1C, Strand ID: A Detail

---

Release date

2003-10-15

Citation 1

Solid state NMR sequential resonance assignments and conformational analysis of the 2x10.4 kDa dimeric form of the Bacillus subtilis protein Crh
Bockmann, A., Lange, A., Galinier, A., Luca, S., Giraud, N., Juy, M., Heise, H., Montserret, R., Penin, F., Baldus, M.
J. Biomol. NMR (2003), 27, 323-339, PubMed 14512730 , Abstract

Show more 3 citaions

Citation 2

Evidence for a dimerisation state of the Bacillus subtilis catabolite repression HPr-like protein, Crh
Penin, F., Favier, A., Montserret, R., Brutscher, B., Deutscher, J., Marion, D., Galinier, D.
J. Mol. Microbiol. Biotechnol. (2001), 3, 429-432, PubMed 11361074 , Abstract

Citation 3

Solution structure and dynamics of Crh, the Bacillus subtilis catabolite repression HPr
Favier, A., Brutscher, B., Blackledge, M., Galinier, A., Deutscher, J., Penin, F., Marion, D.
J. Mol. Biol. (2002), 317, 131-144, PubMed 11916384 , DOI 10.1006/jmbi.2002.5397 , Abstract

Citation 4

Dimerization of Crh by reversible 3D domain swapping induces structural adjustments to its monomeric homologue Hpr
Juy, M., Penin, F., Favier, A., Galinier, A., Montserret, R., Haser, R., Deutscher, J., Bockmann, A.
J. Mol. Biol. (2003), 332, 767-776, PubMed 12972249 , Abstract

Hide non-primary 3 citaions

Entries sharing articles BMRB: 1, Swiss-Prot: 1 entries Detail

Related entities 1. Crh dimer, : 1 : 6 : 100 entities Detail

Interaction partners 1. Crh dimer, : 2 interactors Detail

Experiments performed 6 experiments Detail