Summary for 1E8L
| Entry DOI | 10.2210/pdb1e8l/pdb |
| Related | 193L 194L 1A2Y 1AKI 1AT5 1AT6 1AZF 1B0D 1BVX 1BWH 1BWI 1BWJ 1C08 1C10 1DPW 1DPX 1DQJ 1F0W 1F10 1JPO 1KIP 1KIQ 1KIR 1KXW 1KXX 1KXY 1LCN 1LKR 1LKS 1LPI 1LYO 1LZ8 1LZN 1MEL 1QTK 1RFP 1UCO 1UIA 1UIB 1UIC 1UID 1UIE 1UIF 1UIG 1UIH 1XEI 1XEJ 1XEK 2LYO 3LYO 3LZT 4LYO 4LZT |
| Descriptor | LYSOZYME (1 entity in total) |
| Functional Keywords | hydrolase |
| Biological source | GALLUS GALLUS (CHICKEN) |
| Cellular location | Secreted: P00698 |
| Total number of polymer chains | 1 |
| Total formula weight | 14331.16 |
| Authors | Schwalbe, H.,Grimshaw, S.B.,Spencer, A.,Buck, M.,Boyd, J.,Dobson, C.M.,Redfield, C.,Smith, L.J. (deposition date: 2000-09-27, release date: 2000-10-09, Last modification date: 2024-11-13) |
| Primary citation | Schwalbe, H.,Grimshaw, S.B.,Spencer, A.,Buck, M.,Boyd, J.,Dobson, C.M.,Redfield, C.,Smith, L.J. A refined solution structure of hen lysozyme determined using residual dipolar coupling data. Protein Sci., 10:677-688, 2001 Cited by PubMed Abstract: A high resolution NMR structure of hen lysozyme has been determined using 209 residual 1H-15N dipolar coupling restraints from measurements made in two different dilute liquid crystalline phases (bicelles) in conjunction with a data set of 1632 NOE distance restraints, 110 torsion angle restraints, and 60 hydrogen bond restraints. The ensemble of 50 low-energy calculated structures has an average backbone RMSD of 0.50+/-0.13A to the mean structure and of 1.49+/-0.10A to the crystal structure of hen lysozyme. To assess the importance of the dipolar coupling data in the structure determination, the final structures are compared with an ensemble calculated using an identical protocol but excluding the dipolar coupling restraints. The comparison shows that structures calculated with the dipolar coupling data are more similar to the crystal structure than those calculated without, and have better stereochemical quality. The structures also show improved quality factors when compared with additional dipolar coupling data that were not included in the structure calculations, with orientation-dependent 15N chemical shift changes measured in the bicelle solutions, and with T1/T2 values obtained from 15N relaxation measurements. Analysis of the ensemble of NMR structures and comparisons with crystal structures, 15N relaxation data, and molecular dynamics simulations of hen lysozyme provides a detailed description of the solution structure of this protein and insights into its dynamical behavior. PubMed: 11274458DOI: 10.1110/ps.43301 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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