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The Structure of the Hamp Domain Implies a Rotational Mechanism in Transmembrane Signalling
Authors
Coles, M., Truffault, V., Hulko, M., Martin, J., Lupas, A.N.
Assembly
hypothetical protein AF1503
Entity
1. hypothetical protein AF1503 (polymer, Thiol state: not present), 56 monomers, 6142.907 × 2 Da Detail

GSSTITRPII ELSNTADKIA EGNLEAEVPH QNRADEIGIL AKSIERLRRS LKVAME


Total weight
12285.814 Da
Max. entity weight
6142.907 Da
Source organism
Archaeoglobus fulgidus
Exptl. method
NMR
Refine. method
simulated annealing
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 96.4 %, Completeness: 94.3 %, Completeness (bb): 92.5 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All94.3 % (596 of 632)94.3 % (312 of 331)94.7 % (230 of 243)93.1 % (54 of 58)
Backbone92.5 % (307 of 332)92.0 % (104 of 113)92.7 % (153 of 165)92.6 % (50 of 54)
Sidechain96.6 % (341 of 353)95.4 % (208 of 218)98.5 % (129 of 131)100.0 % (4 of 4)
Aromatic50.0 % (2 of 4)50.0 % (1 of 2)50.0 % (1 of 2)
Methyl98.6 % (73 of 74)97.3 % (36 of 37)100.0 % (37 of 37)

1. hypothetical protein AF1503

GSSTITRPII ELSNTADKIA EGNLEAEVPH QNRADEIGIL AKSIERLRRS LKVAME

Sample

Pressure 1 atm, Temperature 298 K, pH 7.2


#NameIsotope labelingTypeConcentration
1hypothetical protein AF15031.0 mM
2phosphate buffer20 mM
3NACL150 mM
4H2O90 %
5D2O10 %

Protein Blocks Logo
Calculated from 18 models in PDB: 2L7H, Strand ID: A, B Detail


Release date
2006-10-18
Citation
The HAMP domain structure implies helix rotation in transmembrane signaling
Hulko, M., Berndt, F., Gruber, M., Linder, J.U., Truffault, V., Schultz, A., Martin, J., Schultz, J.E., Lupas, A.N., Coles, M.
Cell (2006), 126, 929-940, PubMed 16959572 , DOI 10.1016/j.cell.2006.06.058 ,
Related entities 1. hypothetical protein AF1503, : 1 : 12 : 52 entities Detail
Experiments performed 6 experiments Detail
nullKeywords COMPLEMENTARY X-DA PACKING, HOMODIMER, PARALLEL COILED-COIL