Supplementary Table 2 Crystallographic Data and Refinement Statistics

Supplementary Table 4 Crystallographic Data and Refinement Statistics

X-ray diffraction data statistics

Data set Resolution Unique Redundancy* Completeness I/* Rsym(%)*† range reflections* (%)*

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)

Phasing statistics

Wavelength Isomorphous Anomalous Centric Acentric

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

Refinement statistics

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

1 *Last shell values in parentheses.

†Rsym = ∑(I-I) / ∑I. I is the average intensity over symmetry equivalent measurements.

‡Isomorphous Rcullis = (∑║FPH± FP│- FHcalc│) / ∑│FPH± FP│.

§Isomorphous phasing power = ∑│FH│/ ∑║FPHobs│-│FPHcalc║.

║Anomalous Rcullis = (∑║FPH+(obs) - FPH-(obs)│- │FPH+(calc) - FPH-(calc) ║) / ∑│FPH+

(obs) - FPH-(obs)│.

¶Anomalous phasing power = (∑│FHimaginary│)/ (∑║FPH+(obs) - FPH-(obs)│-

│FPH+(calc) - FPH-(calc) ║).

#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).