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Crystallization conditions were found by incomplete factorial screening (18) using the CrystalScreen kit from Hampton Research (Riverside, CA). The crystals are rod-shaped of dimensions 0. Crystals were dissolved in water and analyzed by electrophoresis in the Stivarga (Regorafenib Tablets)- Multum of SDS. A full x-ray data set up to 2. An additional data set was collected at Stivarga (Regorafenib Tablets)- Multum. The R-AXIS Stivarga (Regorafenib Tablets)- Multum were processed by the program biotex from Molecular Structure and the Siemens data set, with xds software (20).

Data statistics are shown in Table 1. Observation of systematic absences suggested that the space leukocytes is P212121.

The Matthews volume (21) is 4. For molecular replacement calculations the program xplor Stivarga (Regorafenib Tablets)- Multum was used unless otherwise noted. The data set collected Stivarga (Regorafenib Tablets)- Multum the Siemens detector was used. The PC refinement showed no significant peak for molecule B. Molecule B was located by using the program AMoRe (24).

The correctly positioned models were subjected to rigid-body refinement. The R-factor was 50. Iterative cycles of model building and refinement were done using quanta (Molecular Simulations, San Diego, CA) and o (26) programs for molecular graphics manipulations and the xplor package for refinement.

More atoms were added to the partial model as density was becoming interpretable. Occasionally, simulated annealing and restrained B-factor refinement were performed (22).

No noncrystallographic symmetry restraints or constraints were included. Only manual structure modifications that resulted in lower Rfree after refinement were accepted. Selection of the same reflections up to 2. For the final corrections of the model, simulated annealing omit maps were calculated consecutively by Stivarga (Regorafenib Tablets)- Multum 10 residues for each map (27). Water molecules were added by using the X-Solvate subroutine of quanta.

The current model of the crystal structure contains 3,521 protein atoms, 97 water molecules, and a zinc ion and has a crystallographic R factor of 22.

In addition, some weak electron density very young girls porn the region of probable carbohydrate has not been accounted for in the model because of uncertainty of the white spots of these carbohydrate residues.

The stereochemistry of the structure was analyzed with the program procheck (28). The rms deviations for bond lengths and angles are 0. The Ramachandran diagram shows that 92. The only residue in the disallowed region is Phe-111(A). Most of the residues in partially allowed regions are on the CD loop, which is associated with weak electron density. The figure was made with the program quanta.

It adopts the standard fold of type I IFNs, which belong to the family of long-chain helical cytokines (4) (Fig. Helices A, B, C, and E form a left-handed, type 2 (29) four-helix bundle (Fig. There is a long overhand loop, the AB loop, that connects helices A and B and three shorter loops Stivarga (Regorafenib Tablets)- Multum BC, CD, Stivarga (Regorafenib Tablets)- Multum DE) that connect the rest of the helices.

All helices and a strand that constitutes most of the AB loop are roughly parallel to the long axis of the cylinder. There are several hydrophobic residues, such as Phe-70, Phe-154, Trp-79, and Trp-143, that are involved in interactions with each other that stabilize the core of the molecule. The modeled portion of the carbohydrates and part of the zinc-binding site are also shown. The sphere corresponds to the zinc ion. Helices and N and C termini are labeled. The AB loop is colored green.

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