SUPPLEMENTARY INFORMATION

Size: px

Start display at page:

Download "SUPPLEMENTARY INFORMATION"

Emerald Sharp
5 years ago
Views:

Jhn, Supplementry Figure S1 c Supplementry Figure S1, Solvent flttened,

synptic SNARE complex with its two linker regions nd TMRs contoured t the

, Stereo-view of n nomlous difference Fourier mp (mgent mesh) contoured t

5 level, showing the selenium positions of the selenomethionines in

1 Jhn, Supplementry Figure S1 c Supplementry Figure S1, Solvent flttened, single-wvelength nomlous dispersion electron density mp (gry mesh) of the synptic SNARE complex with its two linker regions nd TMRs contoured t the 1 level, superimposed on C plot of the finl model., Stereo-view of n nomlous difference Fourier mp (mgent mesh) contoured t the 4.5 level, showing the selenium positions of the selenomethionines in syntxin 1A. Selenomethionine side chins re shown s sticks. c, Stereo-close-up view of showing the positions of the selenomethionines in the SNARE motif of syntxin 1A. 1

2 c R56 Q226 Q174 Q53 Supplementry Figure S2, Finl 2F o -F c electron density (gry mesh) of the monoclinic crystl form contoured t the 1.5 level, covering one synptic SNARE complex., Finl 2F o -F c electron density (gry mesh) round the chrcteristic zero lyer t the 1.5 level. Hydrogen onds re indicted s dshed lines. Arginine residue R56 in synptorevin 2 nd the three glutmine residues Q226 (syntxin 1A), Q53 (SN1 (N)) nd Q174 (SN2 (C)) re shown s sticks using the sme colour code s in figure 2. c, 2F o -F c electron density (gry mesh) of the orthorhomic crystl form contoured t 1.5 level, covering one synptic SNARE complex. 2

3 I IV I II III II I II III IV III C2 IV I Supplementry figure S3, X-shped ssemly of four synptic SNARE complexes (I-IV) in the C2 structure. The SNARE complexes re shown s rions using the sme colour code s in figure 2. The lower pnel is rotted 90 out the horizontl xis s indicted., X-shped ssemly of four synptic SNARE complexes (I-IV) in the I structure. Complexes II nd III re in the sme orienttion s complexes II nd III of pnel. 3

Syntxin 1A residue numer 7 206 216 226 236 246 256 266 276 286 6 5 Sy2 Sx1A Rmsd (Å) 4 3 2 1 0 35 45 55 65 75 85 95 105 115 Synptorevin 2 residue numer Supplementry figure S4, Stereo-view (C plot) of

4 Syntxin 1A residue numer Sy2 Sx1A Rmsd (Å) Synptorevin 2 residue numer Supplementry figure S4, Stereo-view (C plot) of n overly of the synptic SNARE complexes from the monoclinic form (lck nd TMRs in drk yellow) nd the orthorhomic form (light gry nd TMRs in lighter yellow). Devitions re seen only t the very C-terminus of synptorevin 2. The overly ws clculted with SSM Superpose 1., Rms devitions etween C -toms of syntxin 1A nd synptorevin 2 in the two crystl forms. 4

5 Supplementry tle 1: Crystllogrphic Dt nd Refinement Dt Collection Ntive 1 SeMet Ntive 2 Wvelength (Å) Temperture (K) Spce Group C2 C2 I Unit Cell Prmeters (Å, ) = = c = 58.7 = = c = = = c = = 96.3 = 98.6 Resolution (Å) ( ) ( ) ( ) Reflections Unique (2332) (728) (797) Completeness (%) 99.8 (100) 99.8 (99.6) 99.9 (99.9) Redundncy 6.9 (6.9) 7.7 (7.5) 7.0 (6.6) I/ (I) 15.1 (1.8) 13.6 (1.7) 11.1 (2.1) R sym (I) (0.574) (0.610) (0.510) Phsing Resolution (Å) Hevy Atom Sites 12 Correltion Coefficients c SHELXD CC/CC wek 42.5/19.6 SHELXE CC overll 34.0 CC free Left/Right Hnd 65.6/58.2 FOM d 0.58 Refinement Resolution (Å) ( ) ( ) Reflections Numer (2415) (2171) Completeness (%) 98.2 (89.0) 84.2 (74.0) Test Set (%) (0.416) (0.342) (0.485) (0.434) ESU (Å) f Contents of A.U. g Protein Molecules/Residues/Atoms 8/654/5243 8/654/5242 Lignd Molecules/Atoms 11/79 - Men B-Fctors (Å 2 ) Protein Lignd Rmchndrn Plot g (%) Fvored Outliers Rmsd i from Trget Geometry Bond Lengths (Å) Bond Angles ( ) PDB ID 3HD7 3HD9 e R work e R free c d e f g h i Dt for the highest resolution shell in prentheses R sym (I) = hkl i I i (hkl) - <I(hkl)> / hkl i I i (hkl) ; for n independent reflections nd i oservtions of given reflection; <I(hkl)> verge intensity of the i oservtions CC = [ we o E c w- we o we c ]/{[ we 2 o w -( we o ) 2 ] [ we 2 c w-( we c ) 2 ]} ½ ; w weight (see for full definitions). FOM figure of merit = F(hkl) est / F(hkl) ; F(hkl) est = P( )F hkl ( ) / P( ) R = hkl F os - F clc / hkl F os ; R work hkl T; R free hkl T; T test set ESU estimted overll coordinte error sed on mximum likelihood A.U. symmetric unit Clculted with MolProity ( Rmsd root-men-squre devition 5

6 Reference to the supplement 1 Krissinel, E. nd Henrick, K., Secondry-structure mtching (SSM), new tool for fst protein structure lignment in three dimensions. Act Crystllogr D Biol Crystllogr 60 (Pt 12 Pt 1), 2256 (2004). 6

SUPPLEMENTARY INFORMATION

SUPPLEMENTARY INFORMATION Synthesis of metl oxide with roomtemperture photoreversile phse trnsition Shin-ichi Ohkoshi 1 *, Yoshihide Tsunouchi, 1 Tomoyuki Mtsud, 1 Kzuhito Hshimoto, 2 Asuk Nmi, 1 Fumiyoshi