1. Volume 23, Issue 6, Pages 1028-1038 (June 2015)
Functional Dynamics in Replication Protein A DNA Binding and Protein Recruitment Domains 
Chris A. Brosey, Sarah E. Soss, Sonja Brooks, Chunli Yan, Ivaylo Ivanov, Kavita Dorai, Walter J. Chazin 
Structure 
Volume 23, Issue 6, Pages (June 2015)
DOI: /j.str
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2. Structure 2015 23, 1028-1038DOI: (10.1016/j.str.2015.04.008)
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3. Figure 1 Domain Organization of RPA
RPA is a heterotrimer of subunits RPA70, RPA32, and RPA14, which associate through interactions between domains 70C, 32D, and 14.
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4. Figure 2 15N-T1/T2 and NOE Parameters Obtained for 15N-RPA70AB
Parameters in the absence (A) and presence (B) of dT10 oligonucleotide at 800 MHz point to independent rotational motion for domains 70A and 70B in the absence of substrate and coupled motion upon binding ssDNA. Residues in the inter-domain linker are colored black. Dark horizontal lines overlayed upon 15N-T1/T2 plots represent trimmed average T1/T2 values for each domain (see Table 1). Plots are shown without error bars here for clarity; see Figures S1–S3.
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5. Figure 3
RPA70AB Rotational Diffusion Tensors Support Independent Rotational Motion for Domains 70A and 70B in the Absence of Substrate and Coupled Motion upon Binding ssDNA
Rotational diffusion is displayed with ellipsoids for RPA70AB (A), RPA70AB/dT10 (B), and HYDRONMR simulations of domains 70A and 70B and 70AB (PDB: 1FGU, chain A) (C). Ellipsoid size is scaled to the rate of diffusion, and ellipsoid alignment is referenced to the inertial frame of each domain. The primary axis of diffusion, Dpar, is indicated by a thick line highlighted by crosses along the major axis of the ellipsoid.
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6. Figure 4
RPA70AB Bound to ssDNA Substrate, but not the Free Protein, is Well Described by Classic Model-Free Analysis
Residue plots of order parameters (S2) and internal correlation times (τe) for RPA70AB (A) and RPA70AB/dT10 (B).
Error bars represent standard fitting errors reported by the relax software.
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7. Figure 5 EMF Analysis of Free RPA70AB
(A) Total goodness of fit (χ2) for EMF solutions across a range of global correlation times.
(B) EMF parameter averages.
(C) Residue plots of order parameters (S2) and internal correlation times (τe) for τm 18 ns.
Error bars represent standard fitting errors reported by the relax software.
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8. Figure 6 15N-T1/T2 and NOE Parameters Obtained for 15N-RPA70NAB
Parameters in the absence (A) and presence (B) of dT10 oligonucleotide at 800 MHz support autonomy of the 70N domain relative to 70AB. Residues in the AB inter-domain linker are colored black. Dark horizontal lines overlayed upon 15N-T1/T2 plots represent trimmed average T1/T2 values for each domain (see Table 1). Plots are shown without error bars here for clarity; see Figure S6.
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9. Figure 7
The Rotational Diffusion of RPA70N Is Unaffected by DNA Binding
(A) Overlay of 70N 15N-T1/T2 ratios in the absence (open circles) and presence of ssDNA (filled circles). 15N-T1/T2 ratios simulated from the 70N NMR structure (PDB: 1EWI) (open squares) correspond well with experimental values, indicating that the diffusion of 70N as part of RPA70NAB is similar to that of the untethered domain.
(B) Ellipsoid displays of 70N rotational diffusion in the absence (left) and presence of ssDNA substrate (right). Ellipsoid size is scaled to the rate of diffusion, and ellipsoid alignment is referenced to the inertial frame of each domain. The primary axis of diffusion, Dpar, is indicated by a thick line along the major axis of the ellipsoid.
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10. Figure 8
The Relative Orientation of Linker Attachment Corresponds to Rotational Differences between 70A and 70B Domains
(A) Comparison of linker attachment points (highlighted in red on left) and projected rotational trajectory relative to the measured diffusion tensor.
(B) Cartoon demonstrating reorientation of linked domains upon binding ssDNA.
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