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Winter Wonderland at Falls Park Kicks Off Friday in Sioux Falls
Whether you're singing 'Jingle Bells' already or are mumbling 'bah humbug', the city of Sioux Falls' Winter Wonderland will ensure everyone will be in a great mood starting this Friday at 6pm (November 21)
This Friday, Santa & Mrs Claus will be there with reindeer as drive through traffic is closed off for the opening ceremonies. There will be refreshments, wagon rides and more.
Every year we look forward to driving through the park and are so impressed with the job the workers do in decorating 271 trees, 273 light poles, and spaces in between with over 355,000 lights, 26 MILES of string lights and 2 1/2 miles of extension cords.
The park will be lit every night starting at 5pm through January 11, 2015 so you've got plenty of time to take the drive a few times.
As always, well done Sioux Falls!


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Submitted by Editor on
On Oct. 19, 2011, a USCIS Update was issued announcing processing improvements for certain naturalization and citizenship forms. USCIS has centralized intake of Forms N-336, N-600 and N-600K to the Phoenix Lockbox facility. The Dallas Lockbox facility will handle the Form N-300. This change streamlines the way forms are processed, accelerates the collection and deposit of fees and improves the consistency of our intake process.
This is a reminder that impacted forms received at local and district offices after Dec. 2, 2011, will no longer be forwarded to the appropriate USCIS Lockbox facility. Beginning Dec. 5, impacted forms received locally will be returned to the individual with instructions on how to re-file at a designated USCIS Lockbox facility.
USCIS has updated the information on our N-Form Web pages regarding filing forms at a Lockbox to clearly identify this change in procedure. Please carefully read the form instructions before filing your form to ensure that you are filing the correct form type and edition at the correct location.

subset: commoncrawl


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Among everything else going on at the Austin GDC, an interesting panel took place on the issue of changing business models in MMOs — Free To Play has an easy to read, to the point summation of the panel, which included Robert Ferrari of Turbine (LOTRO), Hilmar Veigar Petursson of CCP (EVE Online), Nicolay Nickelsen of Funcom (Age of Conan), and Min Kim of Nexon (MapleStory). Unsurprisingly, it included discussion of the revenue models — subscription versus free to play — as well as potential audiences:
Robert: F2P has a huge influence. But we have been based on subscriptions for years, with some games being around for 10+ years. Subscripitions hit a hardcore audience that is really embedded in those games. But as you expand your audience, they aren't as hardcore anymore and F2P becomes more enticing as subs only wouldn't appeal. Nicolay: Both models work. Hardcore gamers are comfortable with sub model and most of the games with microtransactions have been casual games. But it is possible to have more than one biz model in a game. Min: There is room in the market for both biz models. F2P in North America will make a large push as teenagers can't commit to $15/month, so F2P will work well with them. Nexon saw lots of success when the market went beyond core to mass market. Hilmar: Consumers are changing the business model of games - consumers making decisions. You can play Eve online through our trial program as a F2P program - users are able to "game" our trial system to play it as a F2P game. It's a challenge for companies to adopt the needs of the market rather than keeping their head in sand. People will play the game how they want. Min: We're seeing in S Korea a lot of players have a subscription-based game that is their favourite, but have a secondary game that they play f2p with microtransactions.
I can't imagine the FTP model will ever overtake subscription models in the West, but there's no doubt that there are a lot of people playing FTPs — and spending way, way more than they would on a subscription — with an ever-increasing audience. I'm curious to see if we'll get any of the crazier FTP MMOs coming out of Asia in the coming years. Evolving Business Models in MMOs - Panel [Free To Play]


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Get a head start on Passover with this great kosher chocolate cookie recipe sent in by my friend Yael over in Israel. Check out her fantastic new kosher recipe site !
"When is Passover 2011?", you ask? Chabad.org has all the updates on this year's Passover holiday dates so that you can begin preparing your Passover menus.
Start buying your Passover ingredients and add these Passover cookies to your Seder menu. Bake and freeze up to 4 weeks ahead of time. They are so delicious straight out of the freezer!
- 1 cup of sugar
- 6 ounces Passover chocolate chips
- 3 egg whites
- 1 package Passover vanilla sugar
- 1/2 cups ground nuts
- Preheat oven to 350F.
- Melt the chocolate and let it cool.
- Beat the egg whites until foamy add the vanilla and beat until stiff.
- Slowly add the sugar.
- Fold in the chocolate and the nuts.
- Drop 1 teaspoon at a time on a greased cookie sheet.
- Bake 15 minutes.
- Remove when cool. Store in freezer.
Related articles
- Warm Chickpea Salad with Arugula for Passover (thejewishhostess.com)
- Orange Shells Filled With Strawberry Sorbet (thejewishhostess.com)
- Sarah's Passover Seder- How to Make Your Table Look Like a Million! (thejewishhostess.com)
- A Down to Earth Cozy Passover Seder (thejewishhostess.com)
- Fresh Mishloach Manot Pics- Add Yours to this List and Win the New York Times Passover Cookbook! (thejewishhostess.com)
- Claudia's Passover Marshmallow-Nut Log (thejewishhostess.com)
- Passover Pizza Dough (thejewishhostess.com)


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It's hard to think of another watchmaker with a finer pedigree for craftsmanship than the Geneva-based Patek Philippe. With an annual production of about 30,000 watches, the company manufactures nearly all of the movements for its watches as well as the majority of their other components, and boasts a long and varied history for watch design and innovation. Patek sells about 6,000 timepieces each year in the U.S. market, and men's watches account for the lion's share (60 percent) of the sales.
This is why the release of some new models under its Calatrava design attracted a large amount of attention at this year's international watch show in Basel, Switzerland. The elegantly chic timepiece was first launched by Patek in 1932, but this year's rendition takes it firmly into the twenty-first century. Or, as some of Patek's representatives said at the show: "What is old becomes new again."
The Reference 5296 is clearly the best of the new Calatravas, with a timeless, contemporary look that the company says is influenced by its famous Calatrava Reference 96 from the 1930s. It shows an Art Deco sort of simplicity and look, yet its straightforward graphics and subtle two-tone white and gray face with blue-pattern time indicators give it an extremely modern touch. Its minimalist look makes it beautiful for formal use as well as casual, from black-tie to jeans and T-shirt.
The watch measures 38 millimeters in diameter (slightly larger than past Calatravas) and comes in a white-gold case with a blue alligator strap. It's a slim and easygoing watch, with a sapphire-crystal case back that reveals its self-winding mechanism (caliber 324). It has a sweeping hand for the seconds, indicates the date and is water resistant to about 80 feet. It sells for $17,400.
Patek said in Basel that it wants its "watches kept and passed on. We don't want something trendy. It has to be classic in style, which is a testament to the consistency in our customer." The Calatrava 5296 should illustrate these points nicely.
Visit www.patek.com.


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I'd like to send a big bloggin thank you to all of you; my new readers, clients, and friends! Starting this blog was very intimidating, since I've never felt that I was that strong of a writer, but it's been a fantastic process. Thank you for all your support, comments, questions and encouragement. It's been a bit of a tough year but I hope that 2010 is filled with lots of creativity, love and success!
Pictured above are Thank You cards that a made a few months ago when I was obsessing over my lined ladies (remember this post). I didn't get around to adding them to the shop until today... Perhaps one of my New Years resolutions should be to stop procrastinating so much! (Here is the set above and here is a variety pack)
Thanks again everyone and I hope you all have a FABULOUS new year!


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Add to Calendar
November 5, 2019 @ 6:00 pm – 7:30 pm
Team-Choco Heidelberg
SRH Campus Sports e.V. Bonhoefferstraße 4/1 69123 Heidelberg
SRH Campus Sports e.V. Bonhoefferstraße 4/1 69123 Heidelberg
The rationale behind our beginner class is to give absolute beginners a basic jiu jitsu vocabulary. It's to expose them to jiu jitsu ideas, give them an overall foundation, and to teach them how to be good training partners. In the Jiu Jitsu Institute curriculum, the beginner curriculum teaches a mix of sport and self-defense.
The beginner class is also a safe place. It addresses this idea of ego threat, where adult beginners may feel a threat to their self-worth, and so when surrounded by other fumbling individuals, it is okay to feel like a n00b spazz because everyone does. It's also a bonding time – classes are smaller, they can ask the "dumb" questions that they might not ask in front of a group full of advanced students.


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The federal government is doing their best X-Files impersonation after shutting down and evacuating a solar observatory and local post office in New Mexico "due to unforeseen circumstances." The weird part? No one's talking about WHY the observatory was suddenly shut down.
"We apologize for any inconvenience this may cause you; however, due to unforeseen circumstances, the Sunspot Solar Observatory, including the site, is temporarily closed, until further notice," according to a message on the observatory's website. "Thank you for your understanding."
Local police say they're just as mystified about the closure as everyone else. Otero County Sheriff Benny House told a local newspaper that his department is in the dark about what's going on and that they've been asked to remain on standby during the facility's evacuation.
"The FBI is refusing to tell us what's going on," House said. "We've got people up there that requested us to stand by while they evacuate it. Nobody would really elaborate on any of the circumstances as to why. The FBI were up there. What their purpose was, nobody will say."
House also noted the presence of a Blackhawk helicopter circling the area around the observatory.
"But for the FBI to get involved that quick and be so secretive about it, there was a lot of stuff going on up there," he said. "There was a Blackhawk helicopter, a bunch of people around antennas, and work crews on towers, but nobody would tell us anything."
House said officers were asked to go to the facility and assist with the evacuation, but were left in the dark as to the why, saying they didn't see a threat.
"They wanted us up there to help evacuate, but nobody would tell us anything," he said. "We went up there and everything was good. There was no threat. Nobody would identify any specific threat. We hung out for a little while, then we left. No reason for us to be there. Nobody would tell us what we're supposed to be watching out for."
Theories as to what's going on range from the outlandish (the aliens are here, the aliens are here!) to the mundane (gas leak). It's worth noting that Sunspot is located only a few miles away from the White Sands Missile Range, making it a prime target for foreign agents who might want to hack into the antenna array to monitor the U.S. military at their base there.
Meanwhile, the federal government and the observatory will remain closed until the security situation is resolved.


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PAUSE Of The Week: Gibril Wilson Of The Bengals Commits A Flag On The Play On Seahawks Leon Washington!
"Suspect moment during Bengals @ Seahawks game" - Kloud
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Apprentice DM
Apprentice DM
Promoted to Major DM
Moderator: Event DM
Please visit:Orleron wrote:I think it's a fun idea if you can idiot-proof it. Problem is God always builds a better idiot.
[Celedor Dedwend: [Talk] *turns around and shakes ass before giving it a sharp slap*
Celedor Dedwend: [Party] ((this is my finest RP beyond a shadow of a doubt.. my zenith if you will))
Fydonya Ivythorn: [Party] that's sad celedor..
Micah Ormane wrote:If you want potions, stand just outside the front door of the AKN, and emote *is disguised* about ever 2 minutes or so. Then, when somebody steps outside, cast wail of the banshee. Loot. Rinse. Repeat. Now that's my kind of crafting.


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Similar in size and weight to its Sigma rival, the constant f/2.8 Tamron features a layout of zoom ring at the body end and focus ring by the front element.
Available in Canon, Nikon and Sony/Minolta fit, further similarities include zoom lock and AF/Manual focus switches on the barrel. What the Tamron doesn't offer is a macro facility, though it will focus to 0.27 metres.
Image quality was disappointing, however. The Tamron suffered from wide-angle barrel distortion and was softer at all zoom lengths and aperture settings, especially wide-open.
It also caused underexposure errors on our EOS 400D when shooting with the built-in flash, which didn't happen with any other lens. The last niggle is the loud, high-pitched autofocus motor.


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JB: When did you first become interested in computing, what was your first computer and what was the first program you wrote?
BS: I learned programming in my second year of university. I was signed up to do "mathematics with computers science" from the start, but I don't really remember why. I suspect that I (erroneously) thought that computing was some sort of applied math.
My fist computer was the departmental GIER computer. It was almost exclusively programmed in Algol-60. My first semi-real program plotted lines (on paper!) between points on the edge of a superellipse to create pleasant graphical designs. That was in 1970.
JB: When you created C++, was the object oriented programming (OOP) paradigm (or programming style) obviously going to gain a lot of popularity in the future, or was it a research project to find out if OOP would catch on?
BS: Neither! My firm impression (at the time) was that all sensible people "knew" that OOP didn't work in the real world: It was too slow (by more than an order of magnitude), far too difficult for programmers to use, didn't apply to real-world problems, and couldn't interact with all the rest of the code needed in a system. Actually, I'm probably being too optimistic here: "sensible people" had never heard of OOP and didn't want to hear about it.
I designed and implemented C++ because I had some problems for which it was the right solution: I needed C-style access to hardware and Simula-style program organization. It turned out that many of my colleagues had similar needs. Actually, then it was not even obvious that C would succeed. At the time, C was gaining a following, but many people still considered serious systems programming in anything but assembler adventurous and there were several languages that—like C—provided a way of writing portable systems programs. One of those others might have become dominant instead of C.
JB: Before C++, did you "just have to create C++" because of the inadequacy of other languages, for example? In essence, why did you create C++?
BS: Yes, I created C++ in response to a real need: The languages at the time didn't support abstraction for hard systems programming tasks in the way I needed it. I was trying to separate the functions of the Unix kernel so that they could run on different processors of a multi-processor or a cluster.
JB: Personally, do you think OOP is the best programming paradigm for large scale software systems, as opposed to literate programming, functional programming, procedural programming, etc.? Why?
BS: No programming paradigm is best for everything. What you have is a problem and a solution to it; then, you try to map that solution into code for execution. You do that with resource constraints and concerns for maintainability. Sometimes, that mapping is best done with OOP, sometimes with generic programming, sometimes with functional programming, etc.
OOP is appropriate where you can organize some key concepts into a hierarchy and manipulate the resulting classes through common base classes. Please note that I equate OO with the traditional use of encapsulation, inheritance, and (run time) polymorphism. You can choose alternative definitions, but this one is well-founded in history.
I don't think that literate programming is a paradigm like the others you mention. It is more of a development method like test-driven development.


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The Associated Press, July 24, 2013
NEW YORK (AP) — The National Transportation Safety Board says the nose gear of a Southwest Airlines jet collapsed backward and into the body of the aircraft following a hard landing at New York's LaGuardia Airport.
The NTSB found the landing gear "collapsed rearward and upward into the fuselage, damaging the electronics bay that houses avionics."
The agency said on its Twitter feed the plane skidded 2,175 feet before stopping at the edge of the runway Monday.
It posted a photo showing the jet's electronics bay penetrated by the landing gear with only the right axle still attached.
Investigators recovered the flight data and cockpit voice recorders on Tuesday. They'll be analyzed by the NTSB.
Sixteen passengers suffered minor injuries during Flight 345's landing. The plane was coming from Nashville, Tenn.


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Hair Straightening Treatment: Opti Smooth Cold Wave Review
I felt that my thick and wavy hair had veered too much into Bon Jovi's Slippery When Wet territory for my liking, and I was looking for a sleeker hair profile. Less frizz. More shine. I spoke to a buddy about this, who said she'd arrange for me to get a Brazilian blow out.
It's Permanent, Not Temporary
A few days later a stylist from the Taka Salon contacted me and asked when I'd like to schedule my blowout. Sure, I thought, I've had blowouts before – takes about an hour, not too hard on the hair and is always a fun change for a few days. This was a blowout of the more permanent kind, she explained. While they can do the ubiquitous Brazilian Blowout (which lasts for 3-4 months), I learned Taka Salon are super-experts in permanent straightening.
I paused at the idea of 'permanent' anything, particularly since I knew it would involve oodles of chemicals and possibly result in a hair change that I might not like, and maybe would even loathe. Sitting in a lounge the night before, I had looked around and noticed that almost every gal – redhead, blond, brunette or raven – was sporting the same glossy head of iron-straight hair.
You Control How Straight It Is
Averse to lemming-ness when it comes to looks, I learned at the Taka Salon that there are degrees of hair straightness to be had. The stylist who did my hair is something like a master chef of hair straightening and told me she could formulate a process that would do the following: relax the frizzies; keep some of the wave at the ends, maintain the volume and increase the shine.
Four salon hours later she achieved just that with the Opti Smooth Cold Wave Treatment, which is a great option if you are looking for a smooth, straight – but not too straight – look.
There's No Heat So It's Kinder on Your Hair
Opti Smooth Cold Wave is different than the Opti Smooth Thermal Treatment or the Yuko System, which both use heat during the process and result in iron-straight hair. This absence of heat makes the Opti Smooth Cold Wave process less stressful on the condition of the hair.
Lots of chemicals are still involved though. Depending on the length and thickness of your hair, the Cold Wave will cost approximately $150 and up, and takes approximately 2-4 hours in the salon. Like other permanent hair straightening treatments, you cannot shampoo for the first 48 hours, as the chemicals are still at work.
Bottom Line: It's Awesome
For me, the Opti Smooth Cold Wave lasted about 1 year – until my hair grew out. It cost around $400 for my very long and thick hair and was worth every penny. I did not need to do anything to my hair after each washing to achieve a straight and sleek look – no hair dryer or flat iron needed, ever.


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Dinner Tonight: Roast Chicken with Spicy Hoisin Glaze Recipe
Your source for quick recipe every single week day.
The plastic guard covering the condiment shelf of my fridge burst yesterday, unleashing an avalanche of glass bottles onto the floor. They all survived, but it was a little disconcerting. I was just trying to add hoisin to my enormous collection and apparently that was one condiment too many. It was all ordered until I started seriously getting into Asian cuisine, and now with the addition of chili pastes, fish sauces, oyster sauce, chili-garlic paste, and the like, my fridge is getting out of hand. But as long as I can whip up quick meals like this one, I'll take the growing pains.
This simple recipe from Epicurious is essentially just a roast chicken covered in a very simple sauce made from standard Asian ingredients and condiments. If you have all of these ready to go, the prep work will take all of five minutes. Then it just goes into a hot oven for 25 minutes and it's done.
The glaze is a beautiful brown that covers the chicken pieces, but because it was just brushed on at the last second, most of the flavor is on top. To correct this, be sure to set aside some of the sauce for dipping at the table. You'll thank me later.
- Yield:4
- 1 chicken, cut into 8 parts
- 1/2 cup hoisin sauce
- 1 teaspoon ginger, grated
- 4 garlic cloves, minced
- 1/2 teaspoon red pepper flakes
- 1/2 teaspoon sesame oil
- 1 tablespoon soy sauce
- 1 tablespoon rice vinegar
Preheat the oven to 500°F. Whisk together the hoisin sauce, ginger, garlic, red pepper flakes, sesame oil, soy sauce, and rice vinegar. Divide the sauce into two bowls.
Brush the chicken all over with the sauce from one of the bowls. Place the chicken in roasting pan and place in the oven. Cook for 25 to 30 minutes, or until the juices run clear on the chicken.
Remove the chicken and serve with the sauce from the other bowl.
All products linked here have been independently selected by our editors. We may earn a commission on purchases, as described in our affiliate policy.


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As Gov. Maggie Hassan settles into the proverbial corner office after having been sworn in on Thursday, offers of advice and congratulations are many.
For our part, we start with the latter.
Hassan is to be congratulated on her Election Day victory and the vision she has laid out for the state. She has proved herself a capable legislator and we wish her only the best in bringing those skills and more to the challenges of being governor.
Now for the advice.
Government is a slow moving beast, especially in New Hampshire where the terms of department heads don't correspond to the governor's term in office. This proved little problem for Gov. John Lynch because he was in the job long enough to have his say on nearly all of the top jobs. On the other hand, Hassan will have to govern with the hand she has been dealt.
With that in mind, we would urge the new governor to promote a sense of purpose down through the ranks. To be specific, those who work for the state should be encouraged to find solutions rather than be consumed by process.
For example, process dictates that department heads produce maintenance budgets. This year's set of such budgets showed the state deeply in the red should the Legislature adopt the numbers presented to then Gov.-elect Hassan last month — an unrealistic expectation from the get-go.
Such a charade is not needed and is a waste of time, as now former Gov. Lynch recently told our editorial board before his departure from office.
Budget proposals should be shaped, in large part, by the knowledge and expertise of department heads and their trusted advisers. A forthright discussion with the governor and legislature should then bring these proposals into line with honest revenue projections. Unfortunately, there is often distrust of the legislative process. This has led to cooking the books so that when budgets are presented there are bones to be thrown to legislators. While this may sound like treason, there is sometimes good reason.
For example, we are told a budget hearing during which a powerful committee chair accepted a recommendation to cut several millions dollars from a portion of the juvenile justice budget. But in doing so she refused to support the legislation that would allow the cut to take place. In effect, she wanted to have her cake and eat it, too. The result was ongoing distrust of this state senator at budget hearings up until the day she left office.
If Hassan can set a no-nonsense tone early in her administration the budget process will better serve the state. And perhaps just as important, it will give state workers a greater sense of purpose knowing their honest opinions are welcome and won't somehow be used against them and their departments.
... or does it?
It doesn't bode well that one of the first headline news coming out of Concord is the reinstitution of a gun ban on the floor of the New Hampshire House, an anteroom and gallery.
It may be fine that Democrats chose to use their newly acquired majority to bring back the ban which had been overturned a couple years back under Republican leadership. But the sad truth is banning guns in the House or not banning guns makes no nevermind to the general public.
As an opening salvo of the last biennial session, voting to allow guns on the House floor allowed Democrats to hold Republicans up to ridicule for wasting precious legislative energies. It will now be tit for tat, as Democrats can rightly be accused of the same.


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Product Description
Replacement Rear Brackets for the CURVED Rear Retainer Bar (sold as set only)
Additional Information
Additional Information
|Installation Instructions
Product's Review
Write Your Own Review
- Front & Rear Cross Bars
- Center Cross Bars (two for standard models, three for long beds)
- 2 Hinged Folding Arms (left & right sides)
- Velcro Tape (hook side)
- Seamsealer - Apply before canopy installation. See seam sealer instructions on page 6.
- 2 sets of bedrails (2 pieces each)
- 4 clamps (6 for long beds)
- 4 screw-in snap studs
- Undo the snaps on the side panels, raise or unzip the rear zippers and flip the sides up and lay them nice and flat on the roof.
- Flip the rear panel up onto the roof and lay it flat.
- Stand on one side of the Softopper, and holding the front bar in place, bring the rear bar forward. You want to try and get the fabric to make even loops down in between the bars to make is as compact as possible
IMPORTANT: When retracting, especially in colder weather, it is very important to make sure that the front window folds evenly in the middle and rearward, into the bed of the truck. Failing to do so may cause the vinyl window to fold improperly and crack.
- Lower the whole unit down behind the cab. You'll notice that the pivot point is offset and the frame will move back as it's lowered forward.
IMPORTANT: When folding the Softopper forward down behind the cab it is very important to attach the rear straps (on the folding frame) to the attachment points at the front (where the front straps are attached to the bedrails). Make them snug. This will prevent the Softopper from being able to accidentally pop open when driving.
- When re-opening the Softopper...undo the rear safety straps from the front attachment points and lift the whole unit up to cab height. Now open the frame and canopy. You'll notice that as the rear part of the frame moves back, the front moves forward. Attach the rear straps, snap down the sides and rear...and you're off to the races.
- If you're going to remove the Softopper completely, retract the topper, then detach the front panel from the bed (Velcro or snaps) and wrap the front panel down under, then around the canopy into a nice little package. If you purchased the boot cover/storage bag, you can now place it over the canopy. You can remove the cotter pins and remove the folding frame and canopy as one piece.
Softopper Installation
Your Softopper contains the following pieces:
NOT SHOWN: One Fabric Canopy, two plastic snap-fit parts, two 12-inch round bars, one 40-50 inch round bar (depending on model), four #12 screws, two #20 self-drilling screws.
Select the bedrail pieces (the four (4) 1-inch square tubes). Join the two pieces of each bedrail together. They will go together so that the snaps are all on the same side. Join them by inserting the smaller square tube in the square end of its mate. Then line up the push buttons with a corner, slowly push together and carefully turn until the push button finds the hole.
There is a LEFT and RIGHT bedrail. NOTE: To tell the difference, the push button will always be forward of the split point (cab side of where the bars split in two). The angled pivot point bracket must be facing inwards, towards the bed and the snaps will be facing outwards. Place the bedrail on the top side of the truck's side rail, with the weather stripping facing down (if there is a paper-like strip on the weather stripping - remove before placing on truck. If there is a mylar coating on the weather stripping - Do Not Remove. This is to prevent it from sticking to the truck). The front end of the bedrail should be evenly aligned with the front inside corner of the bed.
It can be placed evenly with the inside edge of the truck's side rail or moved outward slightly. It is recommended that it rests within 1/2 inch from the inside.
Carefully place the clamps under the trucks side rail and then into the slots on the inner side of the Softopper bedrails. The clamps bolt will be on top. Some vehicles have ridges under the bedrail - try to avoid if possible.
NOTE: Some newer vehicles may be equipped with utility tracks beneath the bedrails. In this case you will use special utility track clamps (as shown below). To install utility track clamps, remove the track end caps (if applicable) and slide the "T" portion on the clamp into the track to the appropriate location where it lines up with the Softopper bedrail slot. Newer Nissan Frontiers with utility tracks use a C-shaped clamp that installs above the utility track, and directly onto the trucks bedrail.
Tighten down firmly...don't over-tighten. Just make sure they are snug so the Softopper bedrail is unable to move.
NOTE: You may have to re-tighten the clamps in a few minutes, after the weather stripping has had a chance to compress. Follow the same steps on the other side.
NOTE: At this point it's nice to have another person around as an extra hand to help put the folding frame together. You can do it alone . . . but it's a little awkward.
Take the hinged folding arms (left and right sides) and hold 4-5 feet apart. They should be exactly opposite of each other. The snap buttons near the connecting points will be facing inwards. One side has colored dots near the top.
Take each of the four cross bars (or five for long beds). They each have colored dots on one end. Carefully fit them together with the corresponding colors on the arm. Press the push button with your finger and carefully slide them together until the button finds the hole. You may have to wiggle them a little. HINT: Be carefully not to pinch your fingers between the pieces.
Before installing the frame onto the pivot pins on the truck bedrails, make sure to get the left and right sides correct.
NOTE: The pivot point holes in the frame are in the tubes that will be towards the rear of the truck.
EXAMPLE: If the folding frame were on the pivot pins and lying forward behind the cab, the bar with the holes in it should be on the top. Remove the cotter pin from the pivot pin in the bracket on the bedrail and carefully slide the frames' pivot hole onto the steel pivot pin. You may have to wiggle them a little or pivot it back and forth to get them on. Reinstall the cotter pin. Do the same on the other side.
NOTE: The pivot pin is designed to loosen slightly to allow for movement and flexing of the truck bed.
TIP: It is easiest to attach the canopy to the frame by working from the rear on the tailgate. Carefully lay down the frame towards the rear of the truck. Unfold the canopy a little to find the front snap flap. NOTE: The back window has zippers; the front does not...so look for the front.
Wrap the front snap flap (that has 6 or 7 female snaps) over and around the front cross bar and connect to the male snaps located on the front cross bar of the frame. Now raise the frame into a position that makes it easy to attach the rear snap flap (that has 6 or 7 female snaps) to the rear cross bar of the frame. Flip up the rear window panel onto the roof, (or climb into the back of the truck) and attach the rear snap flap snaps to the rear cross bar. Be sure to go over and around the top of bar and snap from underneath.
Now raise the entire frame up and forward. Attach the two front straps to the eyelets located on the top from ends of the bedrails. The corner fabric may bind a little this first time so you may have to help it a little. Now retract the topper towards the front of the bed.
You will now need to attach the plastic parts to the rear inside of the 1-inch square bedrails. The one marked (A) goes on the driver side and the other, marked (B) goes on the passenger side. If there are no pre-drilled holes you will need to drill two 3/16 inch holes into the rear bedrails as shown. The first hole is 1 inch from the rear of the bedrail in the center of rail, and the second hole 3 1/4 inches from the end of the rail. NOTE: Do not include the plastic end caps in these measurements. Install the adjustable snap-fit parts with the #12 screws provided.
These photos represent the rear of the driver-side bedrail
Bring the topper back up, and attach the rear straps to the rear eyelet holes on the plastic parts (make sure the straps are loose). NOTE: The topper should still be able to rock back and forth a little, as the straps should still be loose.
Flip down the front and sides of the canopy and connect the snaps along the edge of the fabric to the snaps on the side of the bedrail. It's easier to start at the front and work your way back. Snap the 2 or 3 on each side and then tighten the back straps a little. Work your way back, one snap on each side at a time.
The Canopy will be quite snug the first time it goes on. Take your time and let the fabric have time to stretch out. The roof will stretch out and everything will fit into place. It can take a few minutes or more...if it's very cold (in winter) take more time or move the truck into a warmer garage.
NOTE: If it is snug when you are nearing the last few snaps, place on hand up on top of the frame and pull down gently to help set the snaps.
Reach in and adjust the front webbings until they are snug. Don't over-tighten the straps; you just want them to be snug. They are only to hold the roof in place when the sides are rolled up.
NOTE: Test again to see if the bed rail can move. If so, retighten the clamps. After a short time the weather stripping will compress and there will be no need to retighten. Just be sure to check it once in a while.
Adjust the four corners of the Canopy with the adjustable corner Velcro to get a nice fit on your truck.
CAUTION: When removing the canopy from the frame, pull evenly on the snaps. If there is any resistance, wiggle them around under a little tension until they release. Tugging violently can cause the snaps to deform, making it very hard to re-snap.
Insert a 12-inch bar tube into each end of the longer tube, with the plastic end caps out. Press the bar assembly into the snap-fit parts on the bedrail, adjusting the total length as necessary for a tight side-to-side fit. The idea is to have the larger tube centered and have as little side-to-side movement as possible once secured in the plastic parts and have equal lengths of the smaller tubes protruding from each end. Mark the location of where the smaller tubes enter the larger tube. The longer tube has pre-drilled holes in each end. These holes will be used to guide a 1/8 inch drill bit into the smaller tube. Hold the smaller tube securely in the larger tube at the correct location and drill through. Install the #20 screw and repeat on the other end. Insert the finished tube assembly into the window panel sleeve, press into snap-fit parts on both sides and check fit.
Not to scale
Velcro... Three pieces will go on the outside of the tailgate (if you so choose), and the other two will go on the inside wall of the bed, at the front of the box near the top.
If using the velcro on the tailgate, pull down the zippers on the back flap and adjust the velcro on the back corners of the canopy so that the back flap sits nicely along the top of the tailgate. Tug gently on the back flap and find the place where it seems to sit easily. There is Velcro (loops) sewn along the bottom inside edge of the back flap. This is where the Velco tape must line up once installed on the tailgate. Not too high or too low, just right so it won't be seen when the back is zipped down and secured.
TIP: Use a washable crayon to help fiind the center and to help you line things up.
Don't pull off the sticky backing yet. Be sure to clean the area well (use a 50/50 solution of water and alcohol) where the Velcro will be installed. Plastic bed liners or tailgate protectors generally have a waxy surface, which reduces the holding strenth of the Velcro. It is best to apply the Velcro directly to the paint. Flip the back flap down and retest again for evenness. Take one piece and peel off the platic that conceals the sticky backing, and then very carefully apply it to the center of the tailgate. Now take the second piece and apply it to one side of the tailgate, leaving about an inch extending past the edge of the tailgate. This remaining inch should be wrapped around the edge of the tailgate. Now apply the 3rd piece to the other side. Now go over the three pieces and press along back and forth to make sure they are firmly attached.
NOTE: Velcro tape will reach maximum holding strength after 24 hours. Feel free to cut to shorter lengths if necessary or preferred.
You will now repeat this process with the remaining two pieces of Velcro tape, spacing them approximately 18 inches apart for the front flap along the inside front of the truck box. With bed liners you can instead install the screw-in snap studs (supplied) to attach the front inside flap.
SEAMSEALER: The seamsealer should be applied to the underside of the fabric ( as it may show if it's on the outside). It usually only needs to be applied to the seam that goes all the way around the roof, and on the upper area of the buckle webbings on the sides and rear. Be sure to shake the bottle well before applying to mix up the contents. Apply liberally to the seam, concentrating on where the needle and thread penetrated the fabric to fill the needle holes.
NOTE: Recheck the clamps again to make sure they are tight and the bedrails are secure.
Folding/Retracting the Softopper


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The university announced that the part-time employee was fired for playing "unauthorized" music at Bryant-Denny Stadium. The unauthorized music also happened to be directed at Auburn quarterback Cam Newton.
The songs in question were "Take the Money and Run" by The Steve Miller Band and "Son of a Preacher Man" by Dusty Springfield. No, hopeful souls, it is no coincidence that Newton's father, Cecil, is a pastor who is accused of soliciting $180,000 from Mississippi State for his son's services.
For those monitoring last laugh lines, of course, the undefeated Tigers took down Alabama, 28-27. Newton tossed three TDs and ran in another.
Alabama staffer terminated over Iron Bowl song choice [Tuscaloosa News]


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Express. Home of the Daily and Sunday Express.
Gartside: Youth is the future
Chairman Phil Gartside insists Bolton must invest in youth in order to flourish in the English top flight for another 10 years.
The Trotters are about to enter their 10th successive Premier League campaign and Gartside is adamant the club must live within their means to keep that run going, admitting it is futile to even try and keep pace in spending terms with the likes of Manchester City.
"To play catch-up with Manchester City, we're talking about £400million , not £10million, not £20million, not spending it on another striker. Being realistic, the youth system has got to work because we can invest in the youth and we've got to see some return for it," Gartside told the club's official website.
"That's the way (manager) Owen (Coyle) wants to move forward, he wants a younger team, he wants a team of youngsters who are going to run for him, obviously youngsters with talent. Hopefully youngsters with talent, who have been brought on by Bolton Wanderers - that's the way forward.
"I think that's true of other clubs in our circumstances. We can't go on forever tipping money into this, it won't work, it's not sustainable and we have to find a way of supplementing that talent, or supplementing the talent we've got with home-grown talent."
At the beginning of the millennium Bolton were regarded as a team which would scrap for every point under then boss Sam Allardyce at the expense of pretty football.
Gartside now wants the club to evolve into a more attractive outfit under Coyle, who took over from Gary Megson last season.
"Hopefully we can unify the whole place again, under a leader, and in football terms, under someone who can actually now express himself more on the pitch, and begin to attract the fans back as well," Gartside added.
"After seven years of playing a certain type of football, we've now got to entertain a bit more and recognise that's the business we're in."


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Ziggy, Emig, Hahn, Bowers on DMXS Radio Tonight
Factory Connection Racing was co-founded in 1998 by Rick "Ziggy" Zielfelder and has become one of the true premiere teams in the pits. The coveted ride has produced some of the sport's top riders and they continue to build the next generation of stars through their formidable amateur program. Ziggy is the "OZ" behind the curtain and rarely comes out for an interview since he's always busy in the shop tuning and tweaking suspension, or team duties at the races. We're very stoked that he has some time for us tonight to talk about his ever-growing business and race team. You can check out all the suspension goodies available for your bike at www.FactoryConnection.com.
We always love catching up with multi-time AMA champion turned SPEED TV analyst Jeff Emig to get his take on the sport off camera. He's been a frequent guest in our studio over the years and our listeners enjoy his perspective when he takes off the sport coat and regulation blue shirt and bench races with his southern crew. With the 450 season approaching the halfway point, and East coast boys heading to Atlanta for round two, we have plenty to cover tonight.
GEICO Honda's "Lil" Wil Hahn has been one of favorite riders over the years because of his never-ending positive attitude through all the adversity the sport could throw at him. It was awesome to see him podium at Dallas last weekend and see all that work pay off for the likeable Texan. I'm glad this dirt bike thing is working out, because he would starve as a rapper!
Team Babbitt Kawasaki's Tyler Bowers is synonymous with Arenacross. The multi-time champion has found his niche in the sport and is poised to make yet another run at a title this year in the popular revamped Amsoil series. We've known Tyler since he was a kid and appreciate his success and determination. You can find out more information on the series and races in your area at www.Arenacross.com.
It's that time of the year when amateur motocross ramps up and Oak Hill Raceway in Texas will be hosting a big shindig, March 13-17. We'll catch of with those folks tonight and get the latest on the 37th One Industries GNC championship in the Lone Star state. Info at www.OakHillMX.com.
Check out www.StickerApp.com and www.CaseApp.com for custom sticker sheets and iPhone cases, including cool examples of rider cases. The websites feature a web application with file upload and very simple drag and drop features with the ability to rotate, resize and change background colors and more. We will be giving away some custom iPhone cases in the next few weeks to help get the word out since they are from some of our core moto friends! Check them out now!
DMXS Radio thanks our wives, SCOTT, ONE Industries, Shades of Gray, Racer X, MX Sports, GoPro Cameras, OGIO, Concept2Rowers, Coach Robb Beams, MotoSport.com, FREEGUN Underwear, Vurb Moto and Skull Candy for their continued support!
DMXS Radio has been making Bad Billy proud since 2001!www.dmxsradio.com


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The domain within your query sequence starts at position 29 and ends at position 143; the E-value for the CH domain shown below is 2.69e-16.
CHCalponin homology domain
|SMART accession number:
|Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
|Interpro abstract (IPR001715):
A number of actin-binding proteins, including spectrin, alpha-actinin and fimbrin, contain a 250 amino acid stretch called the actin binding domain (ABD). The ABD has probably arisen from duplication of a domain which is also found in a single copy in a number of other proteins like calponin or the vav proto-oncogene and has been called calponin homology (CH) domain [(PUBMED:9708889), (PUBMED:9887274)].
A detailed analysis of The CH domain-containing proteins has shown that they can be divided in three groups [(PUBMED:9708889)]:
Each single ABD, comprising two CH domains, is able to bind one actin monomer in the filament. The amino terminal CH domain has the intrinsic ability to bind actin, albeit with lower affinity than the complete ABD, whereas the carboxy terminal CH bind actin extremely weakly or not at all. Nevertheless both CH domains are required for a fully functional ABD; the C-terminal CH domain contributing to the overall stability of the complete ABD through inter-domain helix-helix interactions [(PUBMED:9708889)]. Some of the proteins containing a single CH domain also bind to actin, although this has not been shown to be via the single CH domain alone [(PUBMED:9887274)]. In addition, the CH domain occurs also in a number of proteins not known to bind actin, a notable example being the vav protooncogene.
The resolution of the 3D structure of various CH domains has shown that the conserved core consist of four major alpha-helices [(PUBMED:9887274)].
Proteins containing a calponin domain include:
|GO function:
|protein binding (GO:0005515)
|Family alignment:
There are 66728 CH domains in 45684 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing CH domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with CH domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing CH domain in the selected taxonomic class.
- Cellular role (predicted cellular role)
Binding / catalysis: actin-binding
- Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- McCoy AJ, Fucini P, Noegel AA, Stewart M
- Structural basis for dimerization of the Dictyostelium gelation factor (ABP120) rod.
- Nat Struct Biol. 1999; 6: 836-41
- Display abstract
Gelation factor (ABP120) is one of the principal actin-cross-linking proteins of Dictyostelium discoideum. The extended molecule has an N-terminal 250-residue actin-binding domain and a rod constructed from six 100-residue repeats that have an Ig fold. The ability to dimerize is crucial to the actin cross-linking function of gelation factor and is mediated by the rod in which the two chains are arranged in an antiparallel fashion. We report the 2.2 A resolution crystal structure of rod domains 5 and 6, which shows that dimerization is mediated primarily by rod domain 6 and is the result of a double edge-to-edge extension of beta-sheets. Thus, contrary to earlier proposals, the chains of the dimeric gelation factor molecule overlap only within domain 6, and domains 1-5 do not pair with domains from the other chain. This information allows construction of a model of the gelation factor molecule and suggests how the chains in the related molecule filamin (ABP280) may interact.
- Carugo KD, Banuelos S, Saraste M
- Crystal structure of a calponin homology domain.
- Nat Struct Biol. 1997; 4: 175-9
- Display abstract
The three-dimensional structure of the calponin homology domain present in many actin binding cytoskeletal and signal-transducing proteins has been determined at 2.0 A resolution.
- Goldsmith SC, Pokala N, Shen W, Fedorov AA, Matsudaira P, Almo SC
- The structure of an actin-crosslinking domain from human fimbrin.
- Nat Struct Biol. 1997; 4: 708-12
- Hanein D, Matsudaira P, DeRosier DJ
- Evidence for a conformational change in actin induced by fimbrin (N375) binding.
- J Cell Biol. 1997; 139: 387-96
- Display abstract
Fimbrin belongs to a superfamily of actin cross-linking proteins that share a conserved 27-kD actin-binding domain. This domain contains a tandem duplication of a sequence that is homologous to calponin. Calponin homology (CH) domains not only cross-link actin filaments into bundles and networks, but they also bind intermediate filaments and some signal transduction proteins to the actin cytoskeleton. This fundamental role of CH domains as a widely used actin-binding domain underlines the necessity to understand their structural interaction with actin. Using electron cryomicroscopy, we have determined the three-dimensional structure of F-actin and F-actin decorated with the NH2-terminal CH domains of fimbrin (N375). In a difference map between actin filaments and N375-decorated actin, one end of N375 is bound to a concave surface formed between actin subdomains 1 and 2 on two neighboring actin monomers. In addition, a fit of the atomic model for the actin filament to the maps reveals the actin residues that line, the binding surface. The binding of N375 changes actin, which we interpret as a movement of subdomain 1 away from the bound N375. This change in actin structure may affect its affinity for other actin-binding proteins and may be part of the regulation of the cytoskeleton itself. Difference maps between actin and actin decorated with other proteins provides a way to look for novel structural changes in actin.
- Jiang CJ, Weeds AG, Khan S, Hussey PJ
- F-actin and G-actin binding are uncoupled by mutation of conserved tyrosine residues in maize actin depolymerizing factor (ZmADF).
- Proc Natl Acad Sci U S A. 1997; 94: 9973-8
- Display abstract
Actin depolymerizing factors (ADF) are stimulus responsive actin cytoskeleton modulating proteins. They bind both monomeric actin (G-actin) and filamentous actin (F-actin) and, under certain conditions, F-actin binding is followed by filament severing. In this paper, using mutant maize ADF3 proteins, we demonstrate that the maize ADF3 binding of F-actin can be spatially distinguished from that of G-actin. One mutant, zmadf3-1, in which Tyr-103 and Ala-104 (equivalent to destrin Tyr-117 and Ala-118) have been replaced by phenylalanine and glycine, respectively, binds more weakly to both G-actin and F-actin compared with maize ADF3. A second mutant, zmadf3-2, in which both Tyr-67 and Tyr-70 are replaced by phenylalanine, shows an affinity for G-actin similar to maize ADF3, but F-actin binding is abolished. The two tyrosines, Tyr-67 and Tyr-70, are in the equivalent position to Tyr-82 and Tyr-85 of destrin, respectively. Using the tertiary structure of destrin, yeast cofilin, and Acanthamoeba actophorin, we discuss the implications of removing the aromatic hydroxyls of Tyr-82 and Tyr-85 (i.e., the effect of substituting phenylalanine for tyrosine) and conclude that Tyr-82 plays a critical role in stabilizing the tertiary structure that is essential for F-actin binding. We propose that this tertiary structure is maintained as a result of a hydrogen bond between the hydroxyl of Tyr-82 and the carbonyl of Tyr-117, which is located in the long alpha-helix; amino acid components of this helix (Leu-111 to Phe-128) have been implicated in G-actin and F-actin binding. The structures of human destrin and yeast cofilin indicate a hydrogen distance of 2.61 and 2.77 A, respectively, with corresponding bond angles of 99.5 degrees and 113 degrees, close to the optimum for a strong hydrogen bond.
- Lappalainen P, Fedorov EV, Fedorov AA, Almo SC, Drubin DG
- Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis.
- Display abstract
Cofilin stimulates actin filament turnover in vivo. The phenotypes of twenty yeast cofilin mutants generated by systematic mutagenesis were determined. Ten grew as well as the wild type and showed no cytoskeleton defects, seven were recessive-lethal and three were conditional-lethal and caused severe actin organization defects. Biochemical characterization of interactions between nine mutant yeast cofilins and yeast actin provided evidence that F-actin binding and depolymerization are essential cofilin functions. Locating the mutated residues on the yeast cofilin molecular structure allowed several important conclusions to be drawn. First, residues required for actin monomer binding are proximal to each other. Secondly, additional residues are required for interactions with actin filaments; these residues might bind an adjacent subunit in the actin filament. Thirdly, despite striking structural similarity, cofilin interacts with actin in a different manner from gelsolin segment-1. Fourthly, a previously unrecognized cofilin function or interaction is suggested by identification of spatially proximal residues important for cofilin function in vivo, but not for actin interactions in vitro. Finally, mutation of the cofilin N-terminus suggests that its sequence is conserved because of its critical role in actin interactions, not because it is sometimes a target for protein kinases.
- Doering DS, Matsudaira P
- Cysteine scanning mutagenesis at 40 of 76 positions in villin headpiece maps the F-actin binding site and structural features of the domain.
- Biochemistry. 1996; 35: 12677-85
- Display abstract
Villin headpiece, the 76 amino acid, C-terminal domain of villin, is one of the two F-actin binding sites in villin necessary for F-actin bundling activity. Expression and study of recombinant headpiece revealed the domain to be remarkably thermostable (Tm = 74 degrees C) for a non-disulfide-bonded domain. Forty independent point mutations to cysteine of headpiece have been purified and tested for their actin binding activity, cysteine reactivity, and thermal stability. These assays identify two segments of headpiece, near amino acids 38 and 70 of headpiece, in which mutations to cysteine significantly disrupt cosedimentation of headpiece with F-actin. Assay of the thermal stability of these mutants and assay of the reactivity of the introduced cysteine show that these amino acids are mutations at the protein surface that do not perturb the overall structure of the domain. The actin binding mutants are replacements to cysteine of Lys38, Glu39, Lys65, Lys70, Lys71, Leu75, and Phe76 of headpiece. We propose that these discontinuous segments of charged amino acids define the F-actin binding contacts of the headpiece domain. The assay of mutants for effects on the thermal stability of helical structure as well as the assay of reactivity of the introduced sulfhydryl group identify candidate positions that are involved in the stabilizing core and internal structure of the domain. The cysteine scanning mutagenesis also identifies an amino-terminal subdomain (Val1-Leu35) and a predominantly helical carboxy-terminal subdomain (Pro36-Phe76).
- Hart MJ, Callow MG, Souza B, Polakis P
- IQGAP1, a calmodulin-binding protein with a rasGAP-related domain, is a potential effector for cdc42Hs.
- Display abstract
Proteins that associate with the GTP-bound forms of the Ras superfamily of proteins are potential effector targets for these molecular switches. A 195 kDa protein was purified from cell lysates by affinity chromatography on immobilized cdc42Hs-GTP and a corresponding cDNA was isolated. Sequence analysis revealed localized identities to calponin, the WW domain, unconventional myosins and to the rasGAP-related domain (GRD) contained in IRA, NF-1, SAR1 and rasGAP. p195 was found to be identical to IQGAP1, a protein previously reported to bind ras. Purified recombinant p195/IQGAP1 bound to and inhibited the GTPase activity of cdc42Hs and rac whereas no interaction with ras was detected. The C-terminal half of IQGAP1 containing the GRD bound to cdc42 and rac in a GRD-dependent fashion, but a smaller fragment containing only the GRD did not. Cdc42 was also co-immunoprecipitated from cell lysates with antibody specific to p195/IQGAP1. Calmodulin also co-immunoprecipitated with p195/IQGAP1 and was found to associate with fragments containing the IQ domain. Expression of a cDNA fragment encoding the GRD inhibited the CDC24/CDC42 pathway in yeast, but no effect on ras was observed. In mammalian cells, both endogenous and ectopically expressed p195/IQGAP1 were localized to lamellipodia and ruffling cell membranes, where co-localization with actin was apparent. These results suggest that IQGAP1 is an effector target for cdc42Hs and may mediate the effects of this GTPase on cell morphology.
- Castresana J, Saraste M
- Does Vav bind to F-actin through a CH domain?
- FEBS Lett. 1995; 374: 149-51
- Display abstract
An actin-binding protein domain we call here 'calponin-homology' or CH is present in signalling proteins such as Vav which are involved in activation and inactivation of small G-proteins. Using profile methods, we have detected two repeats of this domain in the actin-binding region of alpha-actinin and related proteins. Based on this, we propose that CH domain in Vav and other signalling proteins is employed for association with filamentous actin, and that this function correlates with their control on the G-proteins Rac and Rho which are involved in the organization of cytoskeleton.
- Pestonjamasp K, Amieva MR, Strassel CP, Nauseef WM, Furthmayr H, Luna EJ
- Moesin, ezrin, and p205 are actin-binding proteins associated with neutrophil plasma membranes.
- Mol Biol Cell. 1995; 6: 247-59
- Display abstract
Actin-binding proteins in bovine neutrophil plasma membranes were identified using blot overlays with 125I-labeled F-actin. Along with surface-biotinylated proteins, membranes were enriched in major actin-binding polypeptides of 78, 81, and 205 kDa. Binding was specific for F-actin because G-actin did not bind. Further, unlabeled F-actin blocked the binding of 125I-labeled F-actin whereas other acidic biopolymers were relatively ineffective. Binding also was specifically inhibited by myosin subfragment 1, but not by CapZ or plasma gelsolin, suggesting that the membrane proteins, like myosin, bind along the sides of the actin filaments. The 78- and 81-kDa polypeptides were identified as moesin and ezrin, respectively, by co-migration on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoprecipitation with antibodies specific for moesin and ezrin. Although not present in detectable amounts in bovine neutrophils, radixin (a third and closely related member of this gene family) also bound 125I-labeled F-actin on blot overlays. Experiments with full-length and truncated bacterial fusion proteins localized the actin-binding site in moesin to the extreme carboxy terminus, a highly conserved sequence. Immunofluorescence micrographs of permeabilized cells and cell "footprints" showed moesin co-localization with actin at the cytoplasmic surface of the plasma membrane, consistent with a role as a membrane-actin-linking protein.
- deArruda MV, Watson S, Lin CS, Leavitt J, Matsudaira P
- Fimbrin is a homologue of the cytoplasmic phosphoprotein plastin and has domains homologous with calmodulin and actin gelation proteins.
- J Cell Biol. 1990; 111: 1069-79
- Display abstract
Fimbrin is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. The complete protein sequence (630 residues) of chicken intestine fimbrin has been determined from two full-length cDNA clones. The sequence encodes a small amino-terminal domain (115 residues) that is homologous with two calcium-binding sites of calmodulin and a large carboxy-terminal domain (500 residues) consisting of a fourfold-repeated 125-residue sequence. This repeat is homologous with the actin-binding domain of alpha-actinin and the amino-terminal domains of dystrophin, actin-gelation protein, and beta-spectrin. The presence of this duplicated domain in fimbrin links actin bundling proteins and gelation proteins into a common family of actin cross-linking proteins. Fimbrin is also homologous in sequence with human L-plastin and T-plastin. L-plastin is found in only normal or transformed leukocytes where it becomes phosphorylated in response to IL 1 or phorbol myristate acetate. T-plastin is found in cells of solid tissues where it does not become phosphorylated. Neoplastic cells derived from solid tissues express both isoforms. The differences in expression, sequence, and phosphorylation suggest possible functional differences between fimbrin isoforms.
- Gorlin JB et al.
- Human endothelial actin-binding protein (ABP-280, nonmuscle filamin): a molecular leaf spring.
- J Cell Biol. 1990; 111: 1089-105
- Display abstract
Actin-binding protein (ABP-280, nonmuscle filamin) is a ubiquitous dimeric actin cross-linking phosphoprotein of peripheral cytoplasm, where it promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. The complete nucleotide sequence of human endothelial cell ABP cDNA predicts a polypeptide subunit chain of 2,647 amino acids, corresponding to 280 kD, also the mass derived from physical measurements of the native protein. The actin-binding domain is near the amino-terminus of the subunit where the amino acid sequence is similar to other actin filament binding proteins, including alpha-actinin, beta-spectrin, dystrophin, and Dictyostelium abp-120. The remaining 90% of the sequence comprises 24 repeats, each approximately 96 residues long, predicted to have stretches of beta-sheet secondary structure interspersed with turns. The first 15 repeats may have substantial intrachain hydrophobic interactions and overlap in a staggered fashion to yield a backbone with mechanical resilience. Sequence insertions immediately before repeats 16 and 24 predict two hinges in the molecule near points where rotary-shadowed molecules appear to swivel in electron micrographs. Both putative hinge regions are susceptible to cleavage by proteases and the second also contains the site that binds the platelet glycoprotein Ib/IX complex. Phosphorylation consensus sequences are also located in the hinges or near them. Degeneracy within every even-numbered repeat between 16 and 24 and the insertion before repeat 24 may convert interactions within chains to interactions between chains to account for dimer formation within a domain of 7 kD at the carboxy-terminus. The structure of ABP dimers resembles a leaf spring. Interchain interactions hold the leaves firmly together at one end, whereas intrachain hydrophobic bonds reinforce the arms of the spring where the leaves diverge, making it sufficiently stiff to promote high-angle branching of actin filaments. The large size of the leaves, their interruption by two hinges and flexible actin-binding site, facilitate cross-linking of widely dispersed actin filaments.
- Hock RS, Davis G, Speicher DW
- Purification of human smooth muscle filamin and characterization of structural domains and functional sites.
- Biochemistry. 1990; 29: 9441-51
- Display abstract
A method was developed to purify human smooth muscle filamin in high yield and structural domains were defined by using mild proteolysis to dissect the molecule into intermediate-sized peptides. Unique domains were defined and aligned by using high-resolution peptide mapping of iodinated peptides on cellulose plates. The amino- and carboxyl-terminal orientation of these domains within the molecule was determined by amino acid sequence analysis of several aligned peptides. In addition to the three unique domains which were identified, a number of smaller and larger fragments were also characterized and aligned within the intact molecule. These structural domains and related peptides provide a useful set of defined fragments for further elucidation of structure-function relationships. The two known functionally important binding sites of filamin, the self-association site and the actin-binding site, have been localized. Self-association of two monomers in a tail-to-tail orientation involves a small protease-sensitive region near the carboxyl terminal of the intact polypeptide chain. Sedimentation assays indicate that an actin-binding site is located near the blocked amino terminal of the filamin molecule. Sequences derived from large peptides mapping near the amino terminal show homology to the amino-terminal actin-binding site of alpha-actinin (chicken fibroblast and Dictyostelium), Dictyostelium 120-kDa actin gelation factor, beta-spectrin (human red cell and Drosophila), and human dystrophin. This homology is particularly interesting for two reasons. The functional form of filamin is single stranded, in contrast to alpha-actinin and spectrin which are antiparallel double-stranded actin cross-linkers. Also, no homology to the spectrin-like segments which comprise most of the mass of spectrin, alpha-actinin, and dystrophin was found. Instead, the sequence of a domain located near the center of the filamin molecule (tryptic 100-kDa peptide, T100) shows homology to the published internal repeats of the Dictyostelium 120-kDa actin gelation factor. On the basis of these results, a model of human smooth muscle filamin substructure is presented. Also, comparisons of human smooth muscle filamin, avian smooth muscle filamin, and human platelet filamin are reported.
- Disease (disease genes where sequence variants are found in this domain)
SwissProt sequences and OMIM curated human diseases associated with missense mutations within the CH domain.
Protein Disease Spectrin beta chain, erythrocytic (P11277) (SMART) OMIM:182870: Elliptocytosis-3 ; Spherocytosis-1 ; Anemia, neonatal hemolytic, fatal and near-fatal Alpha-actinin-4 (O43707) (SMART) OMIM:604638: Glomerulosclerosis, focal segmental, 1
- Metabolism (metabolic pathways involving proteins which contain this domain)
Click the image to view the interactive version of the map in iPath
% proteins involved KEGG pathway ID Description 27.53 map04510 Focal adhesion 21.91 map04810 Regulation of actin cytoskeleton 11.80 map04520 Adherens junction 10.39 map04530 Tight junction 7.30 map04010 MAPK signaling pathway 3.65 map04664 Fc epsilon RI signaling pathway 3.65 map04660 T cell receptor signaling pathway 3.65 map04662 B cell receptor signaling pathway 3.65 map04670 Leukocyte transendothelial migration 3.65 map04650 Natural killer cell mediated cytotoxicity 2.25 map05212 Pancreatic cancer 0.28 map03320 PPAR signaling pathway 0.28 map00071 Fatty acid metabolism
This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with CH domain which could be assigned to a KEGG orthologous group, and not all proteins containing CH domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.
- Structure (3D structures containing this domain)
3D Structures of CH domains in PDB
PDB code Main view Title 1aa2 CALPONIN HOMOLOGY (CH) DOMAIN FROM HUMAN BETA-SPECTRIN 1aoa N-TERMINAL ACTIN-CROSSLINKING DOMAIN FROM HUMAN FIMBRIN 1bhd SECOND CALPONIN HOMOLOGY DOMAIN FROM UTROPHIN 1bkr CALPONIN HOMOLOGY (CH) DOMAIN FROM HUMAN BETA-SPECTRIN AT 1.1 ANGSTROM RESOLUTION 1dxx N-terminal Actin-binding Domain of Human Dystrophin 1h67 NMR Structure of the CH Domain of Calponin 1mb8 Crystal Structure of the actin binding domain of plectin 1p2x CRYSTAL STRUCTURE OF THE CALPONIN-HOMOLOGY DOMAIN OF RNG2 FROM SCHIZOSACCHAROMYCES POMBE 1p5s STRUCTURE AND FUNCTION OF THE CALPONIN-HOMOLOGY DOMAIN OF AN IQGAP PROTEIN FROM SCHIZOSACCHAROMYCES POMBE 1pxy Crystal structure of the actin-crosslinking core of Arabidopsis fimbrin 1qag Actin binding region of the dystrophin homologue utrophin 1rt8 CRYSTAL STRUCTURE OF THE ACTIN-CROSSLINKING CORE OF SCHIZOSACCHAROMYCES POMBE FIMBRIN 1sh5 Crystal structure of actin-binding domain of mouse plectin 1sh6 Crystal structure of actin-binding domain of mouse plectin 1sjj Cryo-EM Structure of Chicken Gizzard Smooth Muscle alpha-Actinin 1tjt X-ray structure of the human alpha-actinin isoform 3 at 2.2A resolution 1ujo Solution Structure of the CH domain from Mouse Trangelin 1wjo Solution structure of the forth CH domain from human plastin 3 T-isoform 1wku High resolution structure of the human alpha-actinin isoform 3 1wyl Solution structure of the CH domain of human NEDD9 interacting protein with calponin homology and LIM domains 1wym Solution structure of the CH domain of human transgelin-2 1wyn Solution structure of the CH domain of human calponin-2 1wyp Solution structure of the CH domain of human Calponin 1 1wyq Solution structure of the second CH domain of human spectrin beta chain, brain 2 1wyr Solution structure of the CH domain of human Rho guanine nucleotide exchange factor 6 2d85 Solution structure of the fourth CH domain from human L-plastin 2d86 Solution structure of the CH domain from human Vav-3 protein 2d87 Solution structure of the CH domain from human Smoothelin splice isoform L2 2d88 Solution structure of the CH domain from human MICAL-3 protein 2d89 Solution structure of the CH domain from human EH domain binding protein 1 2dk9 Solution structure of Calponin Homology domain of Human MICAL-1 2e9k Solution structure of the CH domain from human MICAL-2 2eyi Crystal structure of the actin-binding domain of human alpha-actinin 1 at 1.7 Angstrom resolution 2eyn Crystal structure of the actin-binding domain of human alpha-actinin 1 at 1.8 Angstrom resolution 2jv9 The Solution Structure of Calponin Homology Domain from Smoothelin-like 1 2k2r The NMR structure of alpha-parvin CH2/paxillin LD1 complex 2k3s HADDOCK-derived structure of the CH-domain of the smoothelin-like 1 complexed with the C-domain of apocalmodulin 2l3g Solution NMR Structure of CH domain of Rho guanine nucleotide exchange factor 7 from Homo sapiens, Northeast Structural Genomics Consortium Target HR4495E 2r0o Crystal structure of the actin-binding domain of human alpha-actinin-4 mutant(K255E) 2rr8 Solution structure of calponin homology domain of IQGAP1 2vzc Crystal structure of the C-terminal calponin homology domain of alpha parvin 2vzd Crystal structure of the C-terminal calponin homology domain of alpha parvin in complex with paxillin LD1 motif 2vzg Crystal structure of the C-terminal calponin homology domain of alpha- parvin in complex with paxillin LD2 motif 2vzi Crystal structure of the C-terminal calponin homology domain of alpha- parvin in complex with paxillin LD4 motif 2wa5 Crystal structure of human filamin B actin binding domain at 1.9 Angstroms resolution 2wa6 STRUCTURE OF THE W148R MUTANT OF HUMAN FILAMIN B ACTIN BINDING DOMAIN AT 1.95 ANGSTROM RESOLUTION 2wa7 STRUCTURE OF THE M202V MUTANT OF HUMAN FILAMIN B ACTIN BINDING DOMAIN AT 1.85 ANGSTROM RESOLUTION 2wfn Filamin A actin binding domain 2yrn Solution structure of the CH domain from Human Neuron navigator 2 3byh Model of actin-fimbrin ABD2 complex 3f7p Crystal structure of a complex between integrin beta4 and plectin 3fer Crystal structure of n-terminal actin-binding domain from human filamin b (tandem ch-domains). northeast structural genomics consortium target hr5571a. 3hoc Structure of the actin-binding domain of human filamin A mutant E254K 3hop Structure of the actin-binding domain of human filamin A 3hor Structure of the actin-binding domain of human filamin A (reduced) 3i6x Crystal structure of the calponin homology domain of IQGAP1 3kmu Crystal structure of the ILK/alpha-parvin core complex (apo) 3kmw Crystal structure of the ILK/alpha-parvin core complex (MgATP) 3ky9 Autoinhibited Vav1 3lue Model of alpha-actinin CH1 bound to F-actin 3rep Crystal structure of the ILK/alpha-parvin core complex (MnATP) 4b7l Crystal Structure of Human Filamin B Actin Binding Domain with 1st Filamin Repeat 4d1e 4D1E 4edl Crystal structure of beta-parvin CH2 domain 4edm Crystal structure of beta-parvin CH2 domain 4edn Crystal structure of beta-parvin CH2 domain in complex with paxillin LD1 motif 4q57 4Q57 4q58 4Q58 4q59 4Q59 4txi 4TXI 4txk 4TXK 4z6g 4Z6G 5a36 5A36 5a37 5A37 5a38 5A38 5a4b 5A4B 5bvr 5BVR 5l0o 5L0O
- Links (links to other resources describing this domain)


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Have you experienced mold from heavy rain that has saturated the paper-covered gypsum around the units of your ventilator air intake and relief damper? Was it not a small and limited area of growth? Did it take over your home… Read More
Posts Tagged 'mold growrth'
Recovery: How to Repair a Failed Brick Rain Screen Wall
- September 16th, 2011
- Posted in Uncategorized
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Tags: 23, 25, 26, Advance Mold Remediation, area, boot, brick rain screen wall fails, cavity, cleaning and restoration, dampers, dry, eliminated, excess moisture, exterior brick, exterior walls, facebook, full containment, Growth, gypsum, heavy rain, Home, HVAC system relief, ieconnections.com, intakes, limited, living, mold, mold growrth, office, outside air, pages, paper-covered, penetration, poor flashing details, porous cellulose, primary source, Professional, professional advancemoldenv.com, rainwater, rebuild, recover, recovery how to repair a failed brick rain screen wall, redesigned, relief damper, Repair, replaced, saturated, screen wall, tips, twitter, unit ventilator, units, ventilator air intake, Warm, water intrusion, well sealed


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Wow...what a tidal wave the last few months have been! I have been working hard on getting my new business and website together and now it is ready to share with the world. However, there are only so many hours in the day and with all of the comings and goings, these pages have been sorely neglected.
It takes a pretty strong force to rip me away from my beloved blog and now, I am sad to say, this will be my last post here.
I am, however, thrilled to share my new website with you, www.desireerd.com.
The lovely Chloe Perron at Spoken Design created it for me, and I even got myself a spanky new photo, courtesy of the amazing Melia Sorenson at Lucida Photography.
My blog will continue on the new site, with plenty of great content (articles + recipes) up weekly starting February 1st. I hope you will join me there and for those of you new to this blog, here are the links to my most popular posts...enjoy!
My review of the Wheat Belly book is by far the most visited on my blog - talk about a hot button issue!
The post where I share the cake I made for my son's first birthday (from 365 Quinoa) is another good one!
My thoughts on the newest trend in Vancouver...good vegetarian restaurants.
If you are looking for a sane, measured approach to eating well - try my UnDiet!
Want to go more plant-based? Here is a simple way to get started.


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The ranking Republican on a Senate panel on Wednesday accused the Department of Homeland Security of hiding embarrassing information about its so-called "fusion" intelligence sharing centers, charging that the program has wasted hundreds of millions of dollars while contributing little to the country's counterterrorism efforts.
In a 107-page report released late Tuesday, the Senate Permanent Subcommittee on Investigations said that Homeland Security has spent up to $1.4 billion funding fusion centers -- in effect, regional intelligence sharing centers-- that have produced "useless" reports while at the same time collecting information on the innocent activities of American Muslims that may have violated a federal privacy law.
The fusion centers, created under President George W. Bush and expanded under President Barack Obama, consist of special teams of federal , state and local officials collecting and analyzing intelligence on suspicious activities throughout the country. They have been hailed by Homeland Security Secretary Janet Napolitano as "one of the centerpieces" of the nation's counterterrorism efforts.
But Sen. Tom Coburn of Oklahoma, the ranking Republican on the panel, charged Wednesday that Homeland Security had tried to bury evidence of problems at the centers.
"Unfortunately, DHS has resisted oversight of these centers," he said. "The Department opted not to inform Congress or the public of serious problems plaguing its fusion centers and broader intelligence efforts. When this subcommittee requested documents that would help it identify these issues, the department initially resisted turning them over, arguing that they were protected by privilege, too sensitive to share, were protected by confidentiality agreements, or did not exist at all. The American people deserve better. I hope this report will help generate the reforms that will help keep our country safe."
A spokesman for Homeland Security said in a statement to NBC News Tuesday that the Senate report was "out of date, inaccurate and misleading." Matt Chandler, a spokesman for Napolitano, said the Senate panel "refused to review relevant data, including important intelligence information pertinent to their findings." Another Homeland Security official, who spoke with NBC News on condition of anonymity, said the department has made improvements to the fusion centers and that the skills of officials working in them are "evolving and maturing."
The American Civil Liberties Union also issued a statement saying the report underscores problems that it and other civil liberity groups have been flagging for years. "The ACLU warned back in 2007 that fusion centers posed grave threats to Americans' privacy and civil liberties, and that they needed clear guidelines and independent oversight," said Michael German, ACLU senior policy counsel. "This report is a good first step, and we call upon Congress to hold public hearings to investigate fusion centers and their ongoing abuses."
In addition to the value of much of the fusion centers' work, the Senate panel found evidence of what it called "troubling" reports by some centers that may have violated the civil liberties and privacy of U.S. citizens. The evidence cited in the report could fuel a continuing controversy over claims that the FBI and some local police departments, notably New York City's, have spied on American Muslims without a justifiable law enforcement reason for doing so. Among the examples in the report:
- One fusion center drafted a report on a list of reading suggestions prepared by a Muslim community group, titled "Ten Book Recommendations for Every Muslim." The report noted that four of the authors were listed in a terrorism database, but a Homeland Security reviewer in Washington chastised the fusion center, saying, "We cannot report on books and other writings" simply because the authors are in a terrorism database. "The writings themselves are protected by the First Amendment unless you can establish that something in the writing indicates planning or advocates violent or other criminal activity."
- A fusion center in California prepared a report about a speaker at a Muslim center in Santa Cruz who was giving a daylong motivational talk—and a lecture on "positive parenting." No link to terrorism was alleged.
- Another fusion center drafted a report on a U.S. citizen speaking at a local mosque that speculated that -- since the speaker had been listed in a terrorism data base — he may have been attempting "to conduct fundraising and recruiting" for a foreign terrorist group.
"The number of things that scare me about this report are almost too many to write into this (form)," a Homeland Security reviewer wrote after analyzing the report. The reviewer noted that "the nature of this event is constitutionally protected activity (public speaking, freedom of assembly, freedom of religion.)"
The Senate panel found 40 reports -- including the three listed above -- that were drafted at fusion centers by Homeland Security officials, then later "nixed" by officials in Washington after reviewers "raised concerns the documents potentially endangered the civil liberties or legal privacy protections of the U.S. persons they mentioned."
Despite being scrapped, however, the Senate report concluded that "these reports should not have been drafted at all." It also noted that the reports were stored at Homeland Security headquarters in Washington, D.C., for a year or more after they had been canceled —a potential violation of the U.S. Privacy Act, which prohibits federal agencies from storing information on U.S. citizens' First Amendment-protected activities if there is no valid reason to do so.
The report said the retention of these reports also appears to contradict Homeland Security's own guidelines, which state that once a determination is made that a document should not be retained, "The U.S person identifying information is to be destroyed immediately."
The investigation was led by the Republican staff of the subcommittee but the report was approved by chairman Sen. Carl Levin, D-Mich and Coburn. It stated that much basic information about the fusion centers – including exactly how much they cost the federal government — was difficult to obtain. Although the fusion centers are overseen by Homeland Security, they are funded primarily through grants to local governments by the Federal Emergency Management Agency. Although Homeland Security "was unable to provide an accurate tally," the panel estimated the federal dollars spent on the centers between 2003 and 2011 at between $289 million and $1.4 billion.
The panel's criticism of the fusion centers was shared in part by Michael Leiter, the former director of the National National Counter-Terrorism Center and now an NBC News analyst. "Since 9/11, the growth of state and local fusion centers has been exponential and regrettably in many instances it has produced an ill-planned mishmash rather than a true national system that is well-integrated with existing organizations like the FBI-led Joint Terrorism Task Forces," Leiter wrote in an email when asked about the report.
In its response to the Senate panel , Homeland Security said that the canceled reports could still be retained "for administrative purposes such as audit and oversight."
The report cited multiple examples of what it called fusion center reports that had little if any value to counterterrorism efforts.
One fusion center report cited described how a certain model car had folding rear seats to the trunk, a feature that it said could be useful to human traffickers. This prompted a Homeland Security reviewer to note that such folding rear seats are "featured on MANY different makes and model of vehicles" and "there is nothing of any intelligence value in this report."
Another fusion center report, entitled "Possible Drug Smuggling Activity," recounted the experiences of two state wildlife officials who spotted a pair of men in a bass boat "operating suspiciously" in the body of water off the U.S.-Mexico border. The report noted that the fishermen "avoided eye contact" and that their boat appeared to be low in the water, "as if it were laden with cargo" with high winds and choppy waters.
"The fact that some guys were hanging out in a boat where people normally do not fish MIGHT be an indicator of something abnormal, but does not reach the threshold of something we should be reporting," a Homeland Security reviewer wrote, according to the Senate panel. "I … think that this should never have been nominated for production, nor passed through three reviews."
In the Homeland Security Department's response, spokesman Matt Chandler said the Senate subcommittee "refused to review relevant data, including important intelligence information pertinent to their findings."
The senior Homeland Security official who spoke to NBC News said that, while the Senate panel reviewed fusion center reports from 2009 and 2010, a more recent June 2011 case in Seattle shows that a fusion center played a key role in helping to thwart a terrorist plot against a local U.S. military processing center.
Chandler added: "The (Senate) report fundamentally misunderstands the role of the federal government in supporting fusion centers and overlooks the significant benefits of this relationship to both state and local law enforcement and the federal government. Among other benefits, fusion centers play a key role by receiving classified and unclassified information from the federal government and assessing its local implications, helping law enforcement on the frontlines better protect their communities from all threats, whether it is terrorism or other criminal activities."
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Private 2-Day Tour – Royal Marrakech
From 250 Euro per Adult / minimum 4 persons
Embark on a privileged tour and see the best of the Imperial City. Enjoy a private car and driver, selected monuments, lunch at Dar Moha, and overnight accommodation in a 5-star hotel.
|Prepare for a 2-day tour of luxury as your private car and personal driver pick you up from your Agadir hotel, and whisks you away on a journey to explore the best of Marrakech. Drive through the ever-changing scenery and landscapes, to a city filled with palm trees and a backdrop of snow-capped mountains.Explore the colorful city, and enjoy the hustle and bustle of Marrakech's streets. Travel through the former French quarters of Gueliz, and visit the El Bahia Palace and see its immaculate courtyards, and the apartments of the Sultan's concubines. Stop by the 12th Century Koutoubia Mosque and Minaret, the city's landmark, and see the white KoubbaCheck in at your 5-star hotel and freshen up, before heading to lunch at the exclusive Dar Moha for a taste of Moroccan cuisine. After lunch, visit the medina and some famous souks of Marrakech, before returning to your hotel for a chance to relax or swim in the pool. In the evening, head to Djemaa El Fnaa Square, and mingle with the local as the sun sinks below the horizon. Meet soothsayers, snake charmers, scribes, and storytellers. Watch performing monkeys, magicians, dancers, and musicians. Dine at a elegant Moroccan restaurant, while watching a live duo and exotic belly dancing performance. Return to your hotel after dinner, or ask your driver to drop you off at a trendy lounge, casino, or disco.Eat breakfast the next morning, and then visit Yves St Laurent's Majorelle Gardens. Continue through palm groves and take the road to Essaouria. Take a walking tour to see the Skala. Enjoy some free time to explore on your own, and get lunch at a restaurant. Return to Agadir via the coastal road, passing banana plantations, the Saudi Palace, isolated beaches, and tiny villages.
Inclusions :
Departure time and location:
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VW's 'transparent factory', designed by Munich architectural firm Gunther Henn, represents a new era in automotive manufacturing, a pioneering production plant – smooth, clean and transparent.
This prestigious symbol of the Free State of Saxony and the Volkswagen Group follows the strategy of combining a futuristic setting in beautifully landscaped grounds with the legend of this famous baroque city. The environmentally friendly CarGoTram transports all parts – with the exception of the bodies – from the VW logistics centre at Dresden-Friedrichstadt railway station to the factory.
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The latest version of Pokemon Go is released today. We are sharing here Pokemon Go Apk file. Download Pokémon GO 0.89.1 Apk file for Android Devices. Download apk file for Pokémon GO v0.89.1 from below link, move the file to your Android phone's SD card and then use one file manager you prefer for install it.
What's New 0.89.1:
Bug fixes
Download Pokémon GO 0.89.1 APK File
Updated: January 18, 2018
By: Niantic, Inc.
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Note: Androidfiler.com only share the original files for Pokémon GO WITHOUT ANY modification cheat, crack, unlimited gold patch. Pokémon GO is a Trademark of Niantic, Inc. If find any infringement or link not or wrong feel free to mail us at firstname.lastname@example.com


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Hey folks! I promised I would be more dedicated with my workouts and I have not let you down! I really did not want to move my body today. I woke up at 5 am and went to work. Left work at 2:30 this afternoon and immediately changed into my workout clothes. I knew that if I didn't come home […]
Posts Tagged 'lunges'
Pull-Ups? Maybe one day.
April 26th, 2012 jennifer


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In preparation for our upcoming July/August issue, we want to hear from you: What books do you, as a writer who reads deeply year-round, turn to in the warm months ahead? Perhaps you're a student who uses the break from required reading to revisit the classics. Or you're a fiction writer who chooses to pull from the neglected poetry shelf. Or, perhaps, you indulge in the best-sellers to read what everyone else is talking about.
Post a comment and let us know what's on your list.