Added a new Change Serial procedure, which can be used to change the serial number of your Samsung device. The procedure is available only from EUB mode for devices equipped with the following Exynos SoCs:

The Metal Geometry tool facilitates analysis of metal-binding sites. It lists potential metal-coordinating atoms (nearby nucleophilic heteroatoms) and suggests likely coordination geometries. An idealized geometry can be depicted with solid arrows, as shown in the figure for the octahedral coordination of Mn++ by six atoms, and the coordination pseudobonds in the structure can be updated to match the chosen geometry.

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As you may all know, our licenses are valid for 12 months and the allowed numbers of PCs are divided accordingly. We separate the PC usage into 4 quarters (Q1-Q4). On each quarter (Q1=3 months) you will be able to use certain amount of PCs based on your license type. Please be informed that the period of the quarters cannot be modified. It will remain 3 months/quarter.

Fluorescently labeled lectins are useful tools for in vivo and in vitro studies of the structure and function of tissues and various pathogens such as viruses, bacteria, and fungi. For the evaluation of high-mannose glycans present on various glycoproteins, a three-dimensional (3D) model of the chimera was designed from the crystal structures of recombinant banana lectin (BanLec, Protein Data Bank entry (PDB): 5EXG) and an enhanced green fluorescent protein (eGFP, PDB 4EUL) by applying molecular modeling and molecular mechanics and expressed in Escherichia coli. BanLec-eGFP, produced as a soluble cytosolic protein of about 42 kDa, revealed -sheets (41%) as the predominant secondary structures, with the emission peak maximum detected at 509 nm (excitation wavelength 488 nm). More than 65% of the primary structure was confirmed by mass spectrometry. Competitive BanLec-eGFP binding to high mannose glycans of the influenza vaccine (Vaxigrip) was shown in a fluorescence-linked lectin sorbent assay (FLLSA) with monosaccharides (mannose and glucose) and wild type BanLec and H84T BanLec mutant. BanLec-eGFP exhibited binding to mannose residues on different strains of Salmonella in flow cytometry, with especially pronounced binding to a Salmonella Typhi clinical isolate. BanLec-eGFP can be a useful tool for screening high-mannose glycosylation sites on different microorganisms.

Chimera has gathered the SYSTEM registry and ntds.dit files from target systems.[1] Chimera specifically has used the NtdsAudit tool to dump the password hashes of domain users via msadcs.exe "NTDS.dit" -s "SYSTEM" -p RecordedTV_pdmp.txt --users-csv RecordedTV_users.csv and used ntdsutil to copy the Active Directory database.[2]

Motivation:  Contact maps are a convenient method for the structural biologists to identify structural features through two-dimensional simplification. Binary (yes/no) contact maps with a single cutoff distance can be generalized to show continuous distance ranges. We have developed a UCSF Chimera tool, RRDistMaps, to compute such generalized maps in order to analyze pairwise variations in intramolecular contacts. An interactive utility, RRDistMaps, visualizes conformational changes, both local (e.g. binding-site residues) and global (e.g. hinge motion), between unbound and bound proteins through distance patterns. Users can target residue pairs in RRDistMaps for further navigation in Chimera. The interface contains the unique features of identifying long-range residue motion and aligning sequences to simultaneously compare distance maps.

The ChimeraTool PREMIUM licence is valid for 1 year and it can be used with any mobile device we currently support, including Samsung, Huawei, HTC, LG and many others. Any software updates we make to ChimeraTool are included in this licence, free of charge. The ChimeraTool PREMIUM licence allows you to perform an unlimited number of procedures (certain procedures are only available with extra ChimeraTool credits) and 20,000 phones can be connected to the Tool during the license validity. Moreover, our PREMIUM license Users will have access to our priority support hotline and their query will be handled with priority.

The ChimeraTool PREMIUM licence is the best option for professionals in the phone repair industry who work with a lot of phones from different brands.

When you purchase the PREMIUM, the credits are not included.Those have to be purchased separately.

Every NIC (Network Interface Card) has a unique MAC address (Media Access Control). This applies to all types of network cards, including Ethernet cards and WiFi cards. The MAC Address is a six-byte number or 12-digit hexadecimal number ...

To answer this questions, here is some streamlined background information about how the phones work software-wise.Every phone has a serial number (IMEI). This is a digital data that gets connected to the given phone during manufactur...

Reading and writing digitally signed certificates became necessary because in some Samsung models the serial number (IMEI) was stored and protected in this manner. Thus the manufacturer aimed to prevent one from manipulating the originally stored serial number without authorization. Sometimes this part gets damaged or overwritten by an improper tool. If this occurs, having a backup of that part can be very useful, enabling the ability to make a hassle-free restoration. In some cases, a previously saved content can also be restored to other devices by repairing them in the same way. It is important to note that in the latter situation this means that this serial number is cloned as well.

In some cases it happens that the serial number becomes overwritten or just simply damaged. If the case arises, it is possible to fix. Because this feature is not available for all devices, you should beforehand always check out our current list of supported devices.

Comparing related structures and viewing the structures in the context of sequence alignments are important tasks in protein structure-function research. While many programs exist for individual aspects of such work, there is a need for interactive visualization tools that: (a) provide a deep integration of sequence and structure, far beyond mapping where a sequence region falls in the structure and vice versa; (b) facilitate changing data of one type based on the other (for example, using only sequence-conserved residues to match structures, or adjusting a sequence alignment based on spatial fit); (c) can be used with a researcher's own data, including arbitrary sequence alignments and annotations, closely or distantly related sets of proteins, etc.; and (d) interoperate with each other and with a full complement of molecular graphics features. We describe enhancements to UCSF Chimera to achieve these goals.

The molecular graphics program UCSF Chimera includes a suite of tools for interactive analyses of sequences and structures. Structures automatically associate with sequences in imported alignments, allowing many kinds of crosstalk. A novel method is provided to superimpose structures in the absence of a pre-existing sequence alignment. The method uses both sequence and secondary structure, and can match even structures with very low sequence identity. Another tool constructs structure-based sequence alignments from superpositions of two or more proteins. Chimera is designed to be extensible, and mechanisms for incorporating user-specific data without Chimera code development are also provided.

The tools described here apply to many problems involving comparison and analysis of protein structures and their sequences. Chimera includes complete documentation and is intended for use by a wide range of scientists, not just those in the computational disciplines. UCSF Chimera is free for non-commercial use and is available for Microsoft Windows, Apple Mac OS X, Linux, and other platforms from

Integration of protein sequence and structure information is essential in many problem domains, including structural biology, protein engineering, and drug design. A suite of tools within UCSF Chimera [1] has been developed for studying sequence-structure relationships and comparing related structures.

These tools work together within Chimera to enhance the understanding of sequence information in the context of structure and vice versa. Below, we describe the tools in more detail and discuss their advantages and disadvantages relative to other programs.

The implementation of the Chimera system is described elsewhere [1]. The tools described in this paper (Multalign Viewer, MatchMaker, Match -> Align) are all implemented as extensions to Chimera and are distributed along with Chimera. They are written in the Python scripting language and their user interfaces are implemented using Tkinter, Python's interface to the Tk GUI toolkit. Chimera's normal extension mechanisms are used to make the tools available in Chimera's "Tools" menu and to register file types that the tools can open, which then appear in the list of types in Chimera's main file-opening dialog.

The Multalign Viewer, MatchMaker, and Match -> Align tools are accessed from the Structure Comparison section of the Tools menu. Descriptions of parameters refer to the default settings in Chimera version 1.2199.

Sequence alignments in several common formats (Clustal ALN, aligned FASTA, GCG MSF, GCG RSF, aligned NBRF/PIR, and Stockholm) can be opened in Chimera and shown with Multalign Viewer. When a sequence alignment and a structure have been opened in Chimera (in either order), the sequence of the structure is compared to each of the sequences in the alignment. The structure is then associated with the alignment sequence that yields the fewest mismatches, if within a user-specified tolerance. The default mismatch tolerance is 1/10 the number of residues in the structure chain. Reasons for mismatches include point mutations, portions of a structure missing due to insufficient density for coordinates to be determined, and association with a homologous protein rather than the same protein (a useful sequence alignment might not include the sequence of the structure of interest, or even any sequence for which a structure is known). For rapid automatic association, it is assumed that gaps in the structure sequence relative to the alignment sequence can only occur where residues are missing from the structure. Multiple structures can be associated with multiple sequences, or even with the same sequence. When a sequence is associated with a structure, its name is shown in bold over a rectangle of the structure's default color (or if the sequence is associated with multiple structures, a dashed outline). be457b7860

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