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A New Zinc Binding Fold Underlines the Versatility of Zinc Binding Modules in Protein Evolution
Authors
Sharpe, B.K., Matthews, J.M., Kwan, A.H.Y., Newton, A., Gell, D.A., Crossley, M., Mackay, J.P.
Assembly
CREB Binding Protein
Entity
1. CREB Binding Protein (polymer, Thiol state: all other bound), 27 monomers, 3065.598 Da Detail

EVRACSLPHC RTMKNVLNHM THCQAGK


2. ZN (non-polymer), 65.409 Da
Total weight
3131.0068 Da
Max. entity weight
3065.598 Da
Entity Connection
na 4 Detail

IDTypeValue orderAtom ID 1Atom ID 2
1nasing2:ZN1:ZN1:CYS5:SG
2nasing2:ZN1:ZN1:CYS10:SG
3nasing2:ZN1:ZN1:HIS19:ND1
4nasing2:ZN1:ZN1:CYS23:SG

Source organism
Homo sapiens
Exptl. method
NMR
Refine. method
distance geometry
Data set
assigned_chemical_shifts, coupling_constants
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 90.0 %, Completeness (bb): 94.4 % Detail

Polymer type: polypeptide(L)

Total1H
All90.0 % (144 of 160)90.0 % (144 of 160)
Backbone94.4 % (51 of 54)94.4 % (51 of 54)
Sidechain87.7 % (93 of 106)87.7 % (93 of 106)
Aromatic100.0 % (6 of 6)100.0 % (6 of 6)
Methyl100.0 % (12 of 12)100.0 % (12 of 12)

1. CREB Binding Protein

EVRACSLPHC RTMKNVLNHM THCQAGK

Sample

Pressure 1 atm, Temperature 275 (±1) K, pH 6.5 (±0.2)


#NameIsotope labelingTypeConcentration
1CREB Binding Protein0.4 mM
2ZINC (II) ION0.6 mM
3TCEP0.6 mM

Protein Blocks Logo
Calculated from 20 models in PDB: 1LIQ, Strand ID: A Detail


Coupling constant
10 J values in 1 lists
Pressure 1 atm, Temperature 275 (±1) K, pH 6.5 (±0.2) Detail
Release date
2002-05-29
Citation
A new zinc binding fold underlines the versatility of zinc binding modules in protein evolution
Sharpe, B.K., Matthews, J.M., Kwan, A.H.Y., Newton, A., Gell, D.A., Crossley, M., Mackay, J.P.
Structure (2002), 10, 639-648, PubMed 12015147 , DOI: ,
Related entities 1. CREB Binding Protein, : 1 : 11 : 3 : 1 : 22 entities Detail
Interaction partners 1. CREB Binding Protein, : 78 interactors Detail
Experiments performed 4 experiments Detail
nullKeywords zinc finger, protein design