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M-Box 2 Lösung Mechanical Box (M-Box): Walkthrough Guide and Solutions Video

M BOX 2 Mechanical BOX 2 level 14 walkthrough

M-Box 2 Lösung
M-Box 2 Lösung

Drag the battery to the slot the lightning bolt was covering. Next, you need to get all three buttons pressed at once.

To do that, first press the button to the left of the battery. Then, remove the battery. Press the top right button, then the bottom right button.

Now all three buttons should be down and a panel will open, revealing a grid with blue, red, and green boxes.

Notice where they are on the grid. Count the boxes. Now, order them according to the rainbow ROYGBIV , so it goes Red, Green, Blue — or Enter that into the keypad to clear the level.

Drag it to the cut wire to fix it. This next part is super annoying. You have to press the big green power button until the first dial lines up with the light.

Then continue and go through each one. Yeah, frustrating. Once you do it, the numbers for the code is hidden in plain sight. Enter and press the small green button to complete the level.

Level 8: Drag the gear on the lower left to the slot on the upper right and press the red button to turn on the screen. It says RANDOMIZE. Just punch in random numbers and eventually it should work and show you the numbers So the key is the word RANDOMIZE.

Give each letter a number from 1 to 9. Enter Now the 0 button appears and you can enter ! You need to figure out which buttons to press to power up the keypad.

Once the keypad is powered on, slide the home button back down and reveal the numbers Enter those into the keypad to complete the level.

Level This is like a memory game. You need to match all the pairs of icons. Previously, we searched for randomly substituted phosphorothioates that prevented magnesium-mediated compaction of the M-box RNA, 32 and observed remarkable agreement between sites of phosphorothioate interferences and the six magnesium sites observed in the prior structural model.

However, we also observed a small collection of phosphorothioate interferences within electronegative pockets that resembled cation sites, but which lacked metals in the structural model.

Based on this observation, we proposed a role for these sites as putative metal sites, perhaps operative during folding of the M-box RNA.

An additional method for investigating magnesium sites is through substitution with manganese. Typically, manganese can substitute for magnesium; however, the ability of manganese to bind to a particular RNA site may not necessarily prove it to be a magnesium site as the two ions exhibit different chemical characteristics 33 , 34 , 35 , These data also reveal a higher resolution structural model, at 1.

From the sum of all of these data we gain a more thorough understanding of the specific magnesium sites that are formed within the M-box tertiary structure, which are likely to play a critical role during metal-responsive regulation by M-box RNAs.

Divalent metal ions associate closely with RNA, occupying specific sites and serving to neutralize negatively charged pockets in the RNA. This charge neutralization likely stabilizes tertiary contacts and folding of the RNA.

However, in this study we wanted to compare the folding characteristics of M-box in the presence of different ions and elaborate on the interactions of other divalent ions with the M-box using structural probing techniques.

This compares to a value of 0. The Hill coefficients for these fits, however, showed similar values ranging from 4. This suggests that the M-box may bind different metal ions with similar degrees of cooperativity but with varying affinity.

Circles that are yellow, green, red, and blue correspond to C, U, A, and G, respectively. Dashed lines indicate key tertiary contacts.

Reactions are shown for d physiological mM and e high 2. Curve-fitting analysis indicates an EC 50 value of 0. This difference is eliminated in the presence of high concentrations of monovalent ions.

These data show that in the presence of molar concentration of monovalents, all three divalents induce compaction of the M-box RNA at nearly identical concentrations.

Together, these results suggest that the M-box compacted state can be induced by multiple divalent ions, albeit at different concentrations.

However, metal-induced folding of the M-box RNA was similar for the different divalents in the context of high monovalent ions, suggesting that a common minimal number of divalent cation sites were required when low affinity metal interactions could be outcompeted by monovalent ions.

While this substitution resulted in the formation of crystals, the addition of 50 mM ammonium sulfate as an additive significantly improved diffraction quality.

The previously reported 2. This compacted native state appeared to be stabilized by multiple long-range nucleoside and base stacking interactions.

Four of these cation sites Mg1-Mg4 are located within a common region at the base of the molecule where the three helical elements converge.

The remaining two cation sites were located within an internal bulge of the P4 helix. Core 1 appears to stabilize key interhelical interactions at the portion where the three helices converged.

Core 2 may assist orientation of the L4 terminal loop to permit key long-range interactions. However, additional phosphorothioate interferences were identified at positions other than within the binding sites for M1-M6.

Several of these sites, which exhibited a similar overall strength of phosphorothioate interference, were found to be located within electronegative cavities reminiscent of the other cation binding pockets.

From these data we proposed the presence of three additional metal binding sites M7-M9. It is possible that these electronegative cavities represent relatively low occupancy sites and therefore were not observed in the 2.

This latter feature permitted the unequivocal identification of divalent ion binding sites. Representative electron density for these data is shown in Fig.

The asymmetric unit was composed of two molecules hereon referred to as chain A and chain X that exhibited subtle structural differences.

This region of the M-box is involved in multiple long-range contacts that are centered around M5 and M6 in Core 2.

The apparent flexibility of M-box backbone in this region may support the previous observation that metal sites in Core 2 show relatively weaker phosphorothioate interference Symmetry related molecules form an inter-molecular kissing loops interaction to stabilize the P6 helix in this crystal form.

The P6 helix region of the molecule was disordered in the previous structural model. Intermolecular kissing loop interactions between symmetry related molecules appeared to stabilize the L6 loop Fig.

The loop-loop interaction involves 6 nucleotides G, C, U, U, G and U where G-U and G-C base pairs flank the central uridines and allow them to be stabilized by N3-O4 and O2-N3 interactions, respectively.

While it is likely that the relative orientation of these nucleotides with respect to the native M-box structure may be affected by this crystal contact, the increased order in this region resulted in improved electron density of the entire P6 helix region.

Guided by difference density calculated from 1. The two chains also differed modestly in the number of occupied metal sites Fig.

Three out of four sites in Core 1 M1, M2 and M3 showed nearly identical occupancies in both chains. Mn1 was coordinated via interactions to the RNA backbone with the non-bridging phosphate oxygens of G, C and A, at an average distance of 2.

Again, distances from the remaining coordinating water molecules averaged around 2. This interaction is likely to be functionally significant as previous phosphorothioate interference experiments had inferred the importance of this outer—sphere interaction Finally, the last remaining Core 1 cation site, Mn4, was coordinated by a single inner-sphere contact to a nonbridging phosphate oxygen of A72, and an outer-sphere contact to the N7 of A It is noteworthy that this site is likely to represent the weakest specific cation site in Core 1 since the anomalous density ranged from 3.

Consistent with this, position A72 had previously exhibited only moderate phosphorothioate interference. Red positions denote sites of phosphorothioate interferences.

Dashed lines denote key tertiary interactions. There are negligible structural differences in the backbone as well as individual nucleotide orientations.

Mn5 contacts the RNA though one inner-sphere interaction with the phosphate oxygen of A63 and multiple outer-sphere interactions with nucleobases of C77 and U Similarly, Mn6 is coordinated by a backbone phosphate oxygen of A80 and the O4 of U The two metal-coordinating atoms are 3.

In chain X however, this distance is 4. Previously, we had observed phosphorothioate interferences at positions C35, C36, C89, G91 and U in the M-box aptamer.

These positions together appeared to represent three putative metal sites, which we designated M7 through M9. One possible explanation is that they exhibit relatively low-affinity for metal ligand and therefore were unoccupied in the final crystal structure.

Alternatively, the putative M7-M9 sites might occupied with metals only during folding. Key coordinating functional groups are shown along with metal coordinating water molecules black.

Cation binding sites are visible as patches of relatively higher electronegativity. Closer examination of Mn7 Fig. Of these, the interaction with U alone is via the pro-Rp oxygen and was previously seen as a position of phosphorothioate interference.

Metal-ligand distances are in the range of 2. Three water molecules, at an average distance of 2. The combined orientations of the A, A, and U phosphates, towards formation of an electronegative cavity, appeared to help position adjacent nucleosides for key long-range interactions at the apex of the molecule.

For example, the nucleobase ring of A stacks against the GU85 base pair located in the backbone U-turn separating the P4 and P5 helices.

Similarly, A stacks against the AU base pair at the apex of the P5 helix and also forms an A-minor motif interaction with the P4 GC57 base pair, again stabilizing distant regions of the RNA.

Mn9 is coordinated by inner-sphere interactions with the pro-Rp oxygens of C35 and C36 Fig. Outer-sphere interactions with the phosphate oxygens of C from the adjacent turn of the P2 helix further stabilize this coordination.

C35 not only makes direct inner-sphere contacts with Mn9, but also stacks against A88, which is involved in an A-minor interaction to a P2 G:C base pair.

These different metal sites exhibit a concentration of electronegative charge as would be expected for specific cation binding sites Fig.

Most were observed in both RNA chains, although Mn11 was present only in chain A and Mn14 was only in chain X. The most interesting of these metal sites, Mn10, is present in the L5 loop and is coordinated via one backbone interaction with the pro-Rp oxygen of A and the N7 of G Fig.

Two outer-sphere interactions with pro-Rp oxygen of A and G further stabilize the coordination. Notably, A had previously shown to exhibit moderate phosphorothioate interference.

Also, O2 of A on the non-metal binding face coordinates a potassium ion. The ribose oxygen of G further interacts with N1 of A from the P2 helix.

The adenine rings of A and A stack against each other and interact on opposite faces with elements from L4 and P2. While the A nucleobase interacts with the C68 ribose oxygen from the L4 loop, the N6 of A lies within 2.

The G ribose oxygen further interacts with N1 of A, also located within the P2 helix. Mn11 is present in the P4 helix of the M-box aptamer, making one inner-sphere contact with the A60 phosphate oxygen Fig.

The remaining coordinations are satisfied by water molecules. Outer-sphere coordinations are also seen with the N7 groups of A60 and A61 and the phosphate oxygen of A In chain X, the altered backbone conformation in the P4 helix alters the placement of the nucleotides involved in coordinating Mn11, placing them too far away to be able to create a compact metal-coordinating pocket.

Mn12 lies at one end of the P2 helix, close to the L6 turn in the M-box aptamer. The N7 of G45 also makes an outer sphere contact with Mn The remaining coordinations are satisfied via water molecules, though only four of the five metal-chelating water molecules were modeled due to lack of clear density for one water molecule.

With its 'Pro' label, I hoped that the M Box 2 Pro might deliver a pro-level output, so I checked with my audio level meter and found that it didn't.

For a test tone of dBFS, the M Box 2 produced an analogue output level of dB. The original M Box produced an output of dB, whereas the R did produce an output level of 0dB.

I can only assume that the higher-level output cannot be achieved because of limitations on the amount of power the M Box 2 Pro can receive from the host down the Firewire cable.

I also wanted to see if the Pro label meant any improvements in the mic preamps, so I ran a test with speech.

This can be quite telling on a mic preamp, especially in revealing its noise floor — you often need high gain settings for speech, especially in radio, when you often want to create a more intimate sound.

I first recorded using my original M Box with its Focusrite preamps, and then, without changing the mic position, swapped over to the M Box 2 Pro and recorded the same voice again.

To my ears, the M Box 2 Pro sounded smoother and fuller, and the 'silence' sounded less grainy. I don't own an M Box 2 so I was unable to compare the preamps in that model.

The headphone outputs are satisfactory, and I had no problems driving both low-impedance and high-impedance headphones with them.

Whilst recording I noticed a nice feature of the input section's peak level lights. The peak level lights go green at around dBFS, so acting as a 'signal present' indicator.

Then comes the clever bit: the lights go orange at around This is a very neat touch. You can use the conventional TRS balanced jack inputs, but the M Box 2 Pro also includes an RIAA phono preamp, with two phono sockets for connecting a turntable.

You select the phono preamp by pressing the Phono button on the front panel to the right of the Aux input level. Digi have also thoughtfully included an earth terminal, which most turntables need to stop them from humming.

The Startup Guide is a little confusing here, in that it states 'Plug in your turntable, mixer, or similar outputs into the Aux In Phono inputs L and R '.

However, taking a mixer output into the phono inputs would overload the inputs, which are specifically designed to accommodate the output straight from the turntable cartridge and process it via the RIAA EQ curve as well.

Unlike any of the other interfaces in the current Pro Tools LE range, the M Box 2 Pro has the facility to use word clock, both in and out, so it is now possible to lock up a Pro Tools LE system to external word clock, which is not available even on the or R.

Both of these do limit the flexibility of the M Box 2 Pro, but the external word clock feature is nevertheless a major step forward in the Pro Tools LE product range.

This is a new feature in the software, and offered only when the M Box 2 Pro is in use. Digidesign have finally released the portable Firewire-based interface that many people felt the M Box 2 should have been.

The M Box 2 Pro packs a lot into a small box, and Digi have tried to please a broad range of users with this new version. My only real disappointment is that there aren't four mic preamps.

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