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1H and 15N Chemical Shift Assignments for ribosomal protein L7
Authors
Bocharov, E.V.
Assembly
ribosomal protein L7 from E. coli
Entity
1. ribosomal protein L7 from E. coli (polymer, Thiol state: not present), 120 monomers, 12163.84 × 2 Da Detail

SITKDQIIEA VAAMSVMDVV ELISAMEEKF GVSAAAAVAV AAGPVEAAEE KTEFDVILKA AGANKVAVIK AVRGATGLGL KEAKDLVESA PAALKEGVSK DDAEALKKAL EEAGAEVEVK


Total weight
24327.68 Da
Max. entity weight
12163.84 Da
Source organism
Escherichia coli
Exptl. method
NMR
Refine. method
simulated annealing combined with molecular dynamics in torsion angle space
Data set
assigned_chemical_shifts, coupling_constants
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 95.4 %, Completeness (bb): 97.5 % Detail

Polymer type: polypeptide(L)

Total1H15N
All95.4 % (733 of 768)95.1 % (616 of 648)97.5 % (117 of 120)
Backbone97.5 % (355 of 364)97.6 % (240 of 246)97.5 % (115 of 118)
Sidechain93.6 % (378 of 404)93.5 % (376 of 402)100.0 % (2 of 2)
Aromatic100.0 % (10 of 10)100.0 % (10 of 10)
Methyl98.9 % (90 of 91)98.9 % (90 of 91)

1. E.coli ribosomal protein L7/L12

SITKDQIIEA VAAMSVMDVV ELISAMEEKF GVSAAAAVAV AAGPVEAAEE KTEFDVILKA AGANKVAVIK AVRGATGLGL KEAKDLVESA PAALKEGVSK DDAEALKKAL EEAGAEVEVK

Sample

Temperature 303 (±0.5) K, pH 6.9 (±0.1), Details The protein L7/L12 degraded during 2-3 weeks due to spontaneous proteolysis in the hinge region.


#NameIsotope labelingTypeConcentration
1E.coli ribosomal protein L7/L12[U-95% 15N]1.0 mM

Protein Blocks Logo
Calculated from 1 models in PDB: 1RQU, Strand ID: A, B Detail


Coupling constant
118 J values in 1 lists
Temperature 303 (±0.5) K, pH 6.9 (±0.1) Detail
Release date
1999-12-22
Citation 1
Topology of the secondary structure elements of ribosomal protein L7/L12 from E.coli in solutio
Bocharov, E.V., Gudkov, A.T., Arseniev, A.S.
FEBS Lett. (1996), 379, 291-294, PubMed , DOI:
Citation 2
The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
J. Biomol. NMR (1995), 6, 1-10, PubMed 22911575 , DOI 10.1007/BF00417486 ,
Citation 3
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 ,
Related entities 1. ribosomal protein L7 from E. coli, : 1 : 28 : 3 : 3 : 134 entities Detail
Interaction partners 1. ribosomal protein L7 from E. coli, : 167 interactors Detail
Experiments performed 6 experiments Detail
nullKeywords ribosome, L7/L12 protein, sequence-specific NMR assignment, secondary structure