<p> Supplementary Table 4 Crystallographic Data and Refinement Statistics</p><p>X-ray diffraction data statistics</p><p>Data set Resolution Unique Redundancy* Completeness I/* Rsym(%)*† range reflections* (%)*</p><p>Native 20-3.2 51973 (3446) 8.4 (7.1) 99.8 (99.8) 23.6 (8.8) 5.7 (12.0) Selenium Peak 15-3.5 39618 (2600) 20.3 (20.7) 100.0 (100.0) 25.7 (11.5) 11.3 (31.2) Inflection 15-3.7 33794 (2213) 16.0 (16.4) 99.9 (100.0) 23.2 (8.5) 10.4 (33.9) Remote 15-4.0 26680 (1738) 9.6 (9.9) 100.0 (100.0) 17.3 (5.73) 10.7 (37.1)</p><p>Phasing statistics</p><p>Wavelength Isomorphous Anomalous Centric Acentric</p><p>Rcullis‡ Phasing Rcullis‡ Phasing Rcullis║ Phasing power§ power§ power¶ Peak 0.90 0.48 0.90 0.66 0.89 0.59 Inflection ND ND ND ND 0.94 0.40 Remote 0.93 0.52 0.95 0.72 0.97 0.25</p><p>Refinement statistics</p><p>Protein atoms 12,772 R.m.s. bond lengths (Å) 0.0107 R.m.s. bond angles (o) 1.59 Average B 91.5 R.m.s. main chain B (Å2) 16.9 Resolution range (Å) 20-3.2 R-factor# 0.308 Free R-factor# 0.338</p><p>1 *Last shell values in parentheses.</p><p>†Rsym = ∑(I-I) / ∑I. I is the average intensity over symmetry equivalent measurements.</p><p>‡Isomorphous Rcullis = (∑║FPH± FP│- FHcalc│) / ∑│FPH± FP│.</p><p>§Isomorphous phasing power = ∑│FH│/ ∑║FPHobs│-│FPHcalc║.</p><p>║Anomalous Rcullis = (∑║FPH+(obs) - FPH-(obs)│- │FPH+(calc) - FPH-(calc) ║) / ∑│FPH+</p><p>(obs) - FPH-(obs)│.</p><p>¶Anomalous phasing power = (∑│FHimaginary│)/ (∑║FPH+(obs) - FPH-(obs)│- </p><p>│FPH+(calc) - FPH-(calc) ║).</p><p>#R-factor = ∑(║Fobs│-│Fcalc║) / ∑│Fobs│, where the summation is over the working set of reflections. For the free R-factor, the summation is over the test set (5% of the total reflections).</p><p>2</p>