SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.
FOR THE HETERO-ASSEMBLY DESCRIBED BY REMARK 350THIS PDB ENTRY CONSISTS OF ONE CONSTITUENT CHAIN OFA POTASSIUM CHANNEL AND THE LIGHT AND HEAVY CHAINS OF AFAB WHICH IS BOUND TO THE CHANNEL PROTEIN. THE HOMO-TETRAMERIC CHANNEL IS COMPRISED OF FOUR SYMMETRY-RELATEDCOPIES OF THE CHANNEL PROTEIN.
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Components
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Protein , 1 types, 1 molecules C
#3: Protein
POTASSIUMCHANNELKCSA
Mass: 13211.582 Da / Num. of mol.: 1 / Fragment: RESIDUES 1-124 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) STREPTOMYCES LIVIDANS (bacteria) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): NOVABLUE / References: UniProt: P0A334
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Antibody , 2 types, 2 molecules AB
#1: Antibody
ANTIBODYFABFRAGMENTHEAVYCHAIN
Mass: 23411.242 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) MUS MUSCULUS (house mouse)
#2: Antibody
ANTIBODYFABFRAGMENTLIGHTCHAIN
Mass: 23435.738 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) MUS MUSCULUS (house mouse)
Resolution: 3.01→25 Å / Cor.coef. Fo:Fc: 0.886 / Cor.coef. Fo:Fc free: 0.858 / SU B: 16.586 / SU ML: 0.288 / Cross valid method: THROUGHOUT / ESU R: 2.23 / ESU R Free: 0.38 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: MOLECULAR REPLACEMENT AND INITIAL REFINEMENT WERE PERFORMED IN CNS. A COBALT ION WAS MODELED NEAR HIS C 124 CONSISTENT WITH ANOMALOUS DATA. RESIDUAL FEATURES ON THE CRYSTALLOGRAPHIC FOUR- ...Details: MOLECULAR REPLACEMENT AND INITIAL REFINEMENT WERE PERFORMED IN CNS. A COBALT ION WAS MODELED NEAR HIS C 124 CONSISTENT WITH ANOMALOUS DATA. RESIDUAL FEATURES ON THE CRYSTALLOGRAPHIC FOUR-FOLD AXIS WERE MODELED AS LOW OCCUPANCY THALLIUM IONS PRESENT IN THE UNBLOCKED STATE OF THE CHANNEL, APPROXIMATELY 20 PERCENT.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.25
900
5.1 %
RANDOM
Rwork
0.222
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obs
0.223
16821
98.4 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK