(o) Space group Cell parameters (a, b, c: A) Resolution variety
(o) Space group Cell parameters (a, b, c: A) Resolution variety (A) Resolution variety outer shell No. of observed reflections No. of special reflections Typical multiplicityb Completeness ( ) I/s(I)S-SADMerged datasetBM14 CCD 225 1.771 1.0 720 720 P212121 57.9, 60.0, 77.five 20-2.0 2.03-2.0 859917 18867 18.2 (17.five) 100 (one hundred) 46.05 (9.five)ID23-1 CCD 225 0.979 0.5/2.0 360/90 180/180 P212121 55.four, 57.five, 74.six 10-1.five 1.53-1.50 2745135 38981 six.2 (6.four) 99.9 (99.9) 20.7 (2.6)B. PhasingResolution cut-off (A) No. of web pages R-anomalous C.C-anomalous Overall phasing energy Overall figure of merit Acentric reflections Centric reflections 0.406 0.116 20-2.0 13 0.02 34.five 1.C. Refinement and final structure modelPDB access code Resolution made use of in refinement (A) Reflections in: total and test set R and Rfree element ( ) Protein molecules in AU Residues in protein Non-hydrogen protein atoms Waters Residues with dual conformations Calcium atoms PEG molecule Ethylene glycol molecules N-glycosylation molecules Typical atomic B-factor (A2): general protein water calcium RMSD bond lengths from excellent (A) RMSD bond angles from excellent (u) Ramachandran outliers ( )a3ZYP 46-1.5 36753; 1951 19.1; 21.7 1 218 1698 200 18 1 1 817.9 14.five 27.4 8.7 0.009 1.31 0.Beamlines at the European Synchrotron Radiation Facility (ESRF), Grenoble, France. Numbers in parentheses are for the highest resolution bins. The table values had been calculated with O [41], [46], Refmac5 [37], CNS [47], MOLEMAN [48], and LSQMAN [49]. Calculated working with the strict boundary Ramachandran definition provided by Kleywegt and Jones [9]. doi:10.1371/RGS4 Source journal.pone.0070562.tbPLOS One | plosone.orgCrystal Structure of Cip1 from H. jecorinaFigure 2. All round view of Cip1. General view of Hypocrea jecorina Cip1 showing the structure in a) front view and B) side view. The b-strands that make up the bottom of your cleft (b-sheet B) are coloured in red, forming a b-sandwich together with b-sheet A (green). A red circle surrounds the “grip” motif where a calcium ion can also be discovered (blue). doi:ten.1371/journal.pone.0070562.gfound to become structurally homologous to Cip1, each catalytic domains and CBMs. Having said that, this calcium ion can not be viewed as a criterion for either activity or sugar binding but rather as possessing a stabilising impact around the b-jelly-roll fold. The effect of calcium around the stability of CBM proteins has been completely examined by Roske et al. [10]. As well as the 15 b-strands inside the Cip1 structure, 3 ahelices are present. The secondary-structure components from the Cip1 structure have been divided into a- and b-elements, then numberedaccording towards the order of their occurrence in the amino acid sequence of the protein and rainbow coloured (Figure three). The Cip1 structure is relatively compact without any extended loop regions, and with all round dimensions of approximately 40 A638 A637 A.The calcium binding siteAfter solving the structure, inspection from the electron density revealed the probable presence of a metal atom bound in theFigure three. PKCĪ¹ list Topology diagram of Cip1. Secondary structure of Hypocrea jecorina Cip1 coloured in rainbow from N-terminal blue to C-terminal red. The concave active web-site cleft b-sheet is on the ideal within the topology diagram (b-sheet B). The “grip” motif is around the left, in aspect consisting on the outer convex b-sheet “palm” (b-sheet A) plus the “bent fingers” formed by the loop of residues 321. The calcium ion is depicted in grey and coordinates residues from each the N-terminal and C-terminal as we.
