From owner-structural-nmr@net.bio.net Tue Sep 01 23:00:00 1998 Path: biosci!biosci!not-for-mail From: Lakshmikanth Newsgroups: bionet.structural-nmr Subject: 2D nmr difference spectrum Date: 2 Sep 1998 15:32:16 -0700 Organization: TIFR Lines: 4 Sender: daemon@net.bio.net Approved: raman@hemebase.bio.uci.edu Distribution: world Message-ID: <01bdd65c$b47f0340$0e1a909e@micro.tifr.res.in> NNTP-Posting-Host: net.bio.net I want to substract one 2-D spectra from another 2-D spectra. I want to know if there is any program availabe or is it possible. lakshmi From owner-structural-nmr@net.bio.net Tue Sep 01 23:00:00 1998 Path: biosci!biosci!not-for-mail From: Kara Bren Newsgroups: bionet.structural-nmr Subject: POSTDOCTORAL POSITION IN METALLOPROTEIN NMR Date: 2 Sep 1998 10:19:12 -0700 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 42 Sender: daemon@net.bio.net Approved: raman@hemebase.bio.uci.edu Distribution: world Message-ID: NNTP-Posting-Host: net.bio.net Postdoctoral position in metalloprotein NMR An immediate opening for a post-doctoral researcher exists in our laboratory for a motivated individual with a strong background in protein NMR spectroscopy. Experience with NMR of paramagnetic metalloproteins is desirable but not required. Preference will be given to individuals with experience in solution structure determination. Possible projects are (1) the investigation of conformations of partially unfolded metalloproteins using paramagnetic NMR and (2) the study of solution structure and dynamics of metalloproteins from extremely thermophilic organisms. For both projects, there is the opportunity to employ site-directed mutagenesis and protein expression as well as NMR, CD, and UV/vis spectroscopy. Interested individuals should submit a curriculum vitae including research interests and the names, phone numbers, and e-mail addresses of three references by mail, e-mail, or fax to: Professor Kara L. Bren Department of Chemistry University of Rochester Rochester, NY 14627-0216 bren@chem.rochester.edu phone: (716) 275-4335 fax: (716) 473-6889 To obtain further information, inquiries by phone or e-mail are encouraged. _______________________________ Kara L. Bren Assistant Professor Department of Chemistry University of Rochester Rochester, NY 14627 (716) 275-4335 voice (716) 473-6889 fax bren@chem.rochester.edu _______________________________ From owner-structural-nmr@net.bio.net Tue Sep 01 23:00:00 1998 Path: biosci!biosci!not-for-mail From: Istvan Pelczer Newsgroups: bionet.structural-nmr Subject: Re: 2D nmr difference spectrum Date: 2 Sep 1998 16:08:22 -0700 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 24 Sender: daemon@net.bio.net Approved: raman@hemebase.bio.uci.edu Distribution: world Message-ID: NNTP-Posting-Host: net.bio.net Dear Lakshmi, It may not be a unique feature of it, but NMRPipe has a straightforward option to do such things. All the best, Istvan wwww,wwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwww Istvan Pelczer, Ph.D. Email: ipelczer@princeton.edu Senior NMR Spectroscopist Princeton University Department of Chemistry, Frick Lab., ph# (609) 258 2342 Washington Road fax# (609) 258 6746 Princeton, NJ 08544, USA On 2 Sep 1998, Lakshmikanth wrote: > I want to substract one 2-D spectra from another 2-D spectra. I want to > know if there is any program availabe or is it possible. > lakshmi > > From owner-structural-nmr@net.bio.net Thu Sep 03 23:00:00 1998 Path: biosci!biosci!not-for-mail From: David Eliezer Newsgroups: bionet.structural-nmr Subject: NMR Spectroscopist Position Date: 3 Sep 1998 17:53:47 -0700 Organization: The Scripps Research Institute, La Jolla, CA Lines: 31 Sender: daemon@net.bio.net Approved: raman@hemebase.bio.uci.edu Distribution: world Message-ID: <35EF0596.481232BF@scripps.edu> NNTP-Posting-Host: net.bio.net Research Associate or Assistant Professor position at Cornell University Medical College for an NMR spectroscopist to operate an Institutional biomolecular NMR core facility. Primary responsibilities include active participation in research collaborations with CUMC faculty (including spectrometer operation and data analysis and interpretation), training, scheduling and supervision of users and routine maintenance of the NMR instrumentation. Candidates should have a Ph.D. and post-doctoral experience in biochemistry, biophysics, chemistry, physics, or a related discipline, extensive experience with the day-to-day operation of high field NMR spectrometers, and demonstrated experience with the application of NMR to problems in structural biology. Additional familiarity with NMR methods and software development and/or spectrometer hardware and electronics is a plus. The current facility includes a new 600 MHz four- channel instrument. Send a curriculum vitae, including list of publications, and names of three references to: Fred Maxfield, Ph.D. Department of Biochemistry Cornell University Medical College 1300 York Avenue New York, NY 10021 Fax: 212 746 8875 Salary and rank will be commensurate with experience and qualifications. Cornell University Medical College is an Equal Opportunity/ Affirmative Action Employer. From owner-structural-nmr@net.bio.net Sun Sep 06 23:00:00 1998 Path: biosci!biosci!not-for-mail From: Brian Smith Newsgroups: bionet.structural-nmr Subject: Re: 2D nmr difference spectrum Date: 7 Sep 1998 10:14:22 -0700 Organization: Edinburgh University Lines: 17 Sender: daemon@net.bio.net Approved: raman@hemebase.bio.uci.edu Distribution: world Message-ID: References: <01bdd65c$b47f0340$0e1a909e@micro.tifr.res.in> NNTP-Posting-Host: net.bio.net On 2 Sep 1998, Lakshmikanth wrote: > I want to substract one 2-D spectra from another 2-D spectra. I want to > know if there is any program availabe or is it possible. > lakshmi Azara includes a utility "combine" which allows you to add or subtract spectra see http:www-ccmr-nmr.bioc.cam.ac.uk Brian Brian O. Smith Room 209 ICMB/Chemistry Dept. of Chemistry email: brian@chem.ed.ac.uk Joseph Black Building Tel: 0131 650 4704 West Mains Road Fax: 0131 650 4743 (probably) Edinburgh EH9 3JJ From owner-structural-nmr@net.bio.net Wed Sep 09 23:00:00 1998 Path: biosci!biosci!not-for-mail From: Guillaume Chapdelaine Newsgroups: bionet.structural-nmr Subject: Broad NMR peaks Date: 10 Sep 1998 08:00:11 -0700 Organization: NMR LABORATORY - University of Rouen - France Lines: 32 Sender: daemon@net.bio.net Approved: raman@hemebase.bio.uci.edu Distribution: world Message-ID: <35F7DA5E.41C6@univ-rouen.fr> NNTP-Posting-Host: net.bio.net Dear Members, I study a 19 kDa-protein by NMR spectroscopy. This protein has been expressed in E.coli in minimal medium (15N) and solubilized in Tris buffer 10mM, pH 7.5. It is not soluble in phosphate buffer and with pH below 6.5. The NMR spectra (1D 1H & 2D HSQC) show broad peaks and 15N nuclear relaxation measurements give me T1=795ms, T2=54ms and tau_c=13ns (Tris 10mM, protein 2mM, pH 7.2, 303K). I think that the T2 value is weak even if the protein seems to be monomeric according to the tau_c value. I have added 5mM EDTA and 0.5 mM PMSF to avoid paramagnetic ions and degradation. I do not observe any changement in NMR spectra after temperature variations (from 297K to 321K) and dilutions (from 2mM to 0.5mM). The different hypothesis could be : (1) conformational exchange, (2) dimer/monomer exchange, (3) aggregation. How can I underline these hypothesis? I think that I could use 15N nuclear relaxation measurements at different fields and at different temperatures, measurement of the translational diffusion coefficient by PFG, addition of CHAPS, and so on. Is the methodology correct? What are the other solutions? Could you send me some advice or protocol to analyse this problem? Thank you for your precious help. Yours faithfully, Guillaume Chapdelaine -- Guillaume CHAPDELAINE - Univ. Rouen - NMR LABORATORY CNRS UPRES-A 6014 76821 MONT-SAINT-AIGNAN Cedex FRANCE 33.2.35.52/29.47 (phone) /24.41 (fax) Email:Guillaume.Chapdelaine@univ-rouen.fr * http://www.mygale.org/08/gchapdel/ From owner-structural-nmr@net.bio.net Wed Sep 09 23:00:00 1998 Path: biosci!biosci!not-for-mail From: David Eliezer Newsgroups: bionet.structural-nmr Subject: Structural Biology Postdoctoral Position Date: 10 Sep 1998 16:11:20 -0700 Organization: The Scripps Research Institute, La Jolla, CA Lines: 25 Sender: daemon@net.bio.net Approved: raman@hemebase.bio.uci.edu Distribution: world Message-ID: <35F85544.5F34666B@scripps.edu> NNTP-Posting-Host: net.bio.net Postdoctoral Position: Structural transitions in cytoskeletal proteins. Department of Biochemistry, Cornell University Medical College. A postdoctoral position is available to characterize structure and dynamics in native and partially folded forms of actin binding proteins using NMR. Specific goals address the biological function of conformational transitions and of partially folded proteins, the pathways for protein aggregation and amyloid formation, and the role of folding intermediates in directing the protein folding process. Resources include a new 4 channel 600 MHz spectrometer and newly renovated laboratory space. The New York City area boasts a vibrant structural biology community. Ideal candidates should have experience in protein biophysics or biochemistry, protein structure determination, and/or protein folding. Experience with protein expression and purification, modern triple-resonance NMR techniques and a general familiarity with software tools are also helpful. Interested applicants should send a C.V. and letters from two references to David Eliezer, Department of Molecular Biology/MB2, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA 92037. Email inquiries are also welcome at Eliezer@Scripps.Edu. From owner-structural-nmr@net.bio.net Thu Sep 10 23:00:00 1998 Path: biosci!biosci!not-for-mail From: "clive delmonte" Newsgroups: bionet.structural-nmr Subject: Triple-stranded DNA Structure Date: 11 Sep 1998 08:36:40 -0700 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 43 Sender: daemon@net.bio.net Approved: raman@hemebase.bio.uci.edu Distribution: world Message-ID: <6tbg28$gt3@net.bio.net> NNTP-Posting-Host: net.bio.net The formation and properties of triple-stranded DNA are now described in a substantial body of literature. However, I have been searching for early research reports identifying triple-stranded DNA and I have come upon a problem. I would be grateful to hear what thoughts others have had about it. Leslie et al.(J Mol Biol 143 (1980) 49-72) reported that a fibre of poly(dI).poly(dC) which gave sharp X-ray diffraction spots shortly after being drawn was unstable and transformed irreversibly after a few days into poly(dC).poly(dI).poly(dC+). This new molecule also gave sharp spots in its X-ray diffraction pattern, and this new pattern did not have any of the original spots. Therefore the conversion was complete, or substantially complete. Very similar results were reported for fibres of poly(dA).poly(dT) converting to poly(dT).poly(dA).poly(dT) (J Mol Biol 88 (1974) 509-521) and for the formation of poly(U).poly(A).poly(U) (Nature New Biology 244 (1973) 99-101). The problem is evident: How and where would the torque arise inside a solid fibre that would permit one double helix to rotate so as to unwind one strand and rewind it onto an adjacent triple helix having a different diameter and rotating at a different angular velocity ? Inside the fibre, individual molecules would have a random axial translation so only very rarely would two adjacent double helices have the same axial starting point. How would there be a very high conversion of double to triple stranded molecules when any rotation of adjacent double helices would normally find the free ends of one of them axially displaced down the fibre compared to its neighbour ? None of the original workers offered any explanation as to how this conversion might be possible, nor, indeed, remarked that there might be something to explain. Naturally I have given this problem some thought, but I have been driven towards a daunting conclusion. I shall be glad to share my thoughts with anyone who lets me know they are interested, or anyone who offers their thoughts on this problem. clived@ndirect.co.uk From owner-structural-nmr@net.bio.net Sun Sep 13 23:00:00 1998 Path: biosci!biosci!not-for-mail From: "clive delmonte" Newsgroups: bionet.structural-nmr Subject: The Structure of Duplex DNA Date: 14 Sep 1998 10:54:55 -0700 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 75 Sender: daemon@net.bio.net Approved: raman@hemebase.bio.uci.edu Distribution: world Message-ID: <6tjl9f$haj@net.bio.net> NNTP-Posting-Host: net.bio.net Eric, You are right, and it is timely, to raise the topological papers by Crick, Wang & Bauer (J Mol Biol 129 (1979) 449-461), and Bauer, Crick & White (Scientific American 243 (1980) 100-113). Their treatments did not apply to every side-by-side model, however : "..This proves that the linking number is not equal to zero (at least for the great majority of those, i.e., side-by-side, molecules.), and also only to such side-by-side models "...in which the two ...chains do not coil around each other ...but instead lie side by side over most of their length, having only a few helical turns." Their treatment only applies to side-by-side models, like that of Rodley et al., for which there is a net winding because an equal number of right and left turns do not get you back to an equivalent repeat point in space because of the D chirality of asymmetric carbon in all the pentoses. The model I have come upon has exactly and identically zero plectonaemic turns in its relaxed state over any length of duplex and is therefore not covered and constrained by the two papers just cited. Thermodynamics has always been a delight to me, though I find it difficult! Chemical energy is dissipated in all directions; that is, it is not a vector, but torque is a vector. Therefore chemical energy would seem to be unable to either wind or unwind two plectonaemic strands where no breakage of covalent bonds takes place. My solution to this conundrum is to say that neither winding nor unwinding does actually take place ! But tell me - let me tease you a little - what do you make of the results of Kabata et al. (SCIENCE 262 (1993) 1561-1563) who found that RNA polymerase slides along its DNA duplex substrate and does not follow a helical path ? An absolutely crucial test of the new model offers itself, though we need someone to carry it out. Drew & Travers (J Mol Biol 186 (1985) 773-790) have constructed a 169 bp circular, covalently closed length of duplex DNA. With this length of DNA there can only be a very limited number of topoisomers present if the ring closure, of itself, could introduce only a very few superhelical turns. That is, all the 169 bp molecules would share a range of superhelical turns between about -1 and +1. Therefore in suitably mild denaturing conditions, in the absence of any strand breakage, the 169 bp sequence would be largely separable into complementary covalently closed single-stranded DNA circles interlinked at very few places according to the new model. Thus the most direct route to distinguishing between the DNA double helix and the new model is based on topology. The complementary strands in that 169 bp sequence may actually be linked by 0, or perhaps ± 1 superhelical turns due to the algebra of the enzymic closure reaction used on the 169 bp linear duplex, and the denatured covalently closed circular strands could be decorated with a suitable protein and then be examined under AFM to determine their linking number. Therefore, if the 169 bp circular DNA is denatured under mild conditions, perhaps using aqueous urea, it could then be decorated with the single-strand DNA binding protein, the product of gene 32 from phage T4 (Scanning Microscopy 9 (1995) 705-727), so as to be rendered easily visible under AFM, and the actual numbers of crossovers then counted. According to the double helix model, LK will lie in the range 16 to 18, or so, while the new model predicts LK is -1, 0 or +1. A very similar experiment could be carried out with the small circular DNAs described by Bates & Maxwell (EMBO J 8 (1989) 1861-1866), where, for the smallest, the double helix model predicts LK = 9, and the new model predicts LK = -2. Is there any research group with the interest and ability to conduct this experiment ? clive delmonte clived@ndirect.co.uk From owner-structural-nmr@net.bio.net Sun Sep 13 23:00:00 1998 Path: biosci!biosci!not-for-mail From: Guillaume Chapdelaine Newsgroups: bionet.structural-nmr Subject: T1/T2 with double-labeled protein Date: 14 Sep 1998 10:32:11 -0700 Organization: NMR LABORATORY - University of Rouen - France Lines: 19 Sender: daemon@net.bio.net Approved: raman@hemebase.bio.uci.edu Distribution: world Message-ID: <35FD459F.41C6@univ-rouen.fr> NNTP-Posting-Host: net.bio.net Dear members, Recently, I have done some 15N nuclear relaxation measurement experiments (T1, T2) with a double-labeled protein (13C/15N). According to the general bibliography, numerous 15N nuclear relaxation measurement experiments have been done with only 15N-labeled protein. Is it a problem to use 13C/15N protein to measure T1, T2 values? With a J(N,C)=11-15 Hz, is there a contribution of the carbon on the T1/T2 results? Could you give me some references about this question? Thank you for your help. Guillaume Chapdelaine -- Guillaume CHAPDELAINE - Univ. Rouen - NMR LABORATORY CNRS UPRES-A 6014 76821 MONT-SAINT-AIGNAN Cedex FRANCE 33.2.35.52/29.47 (phone) /24.41 (fax) Email:Guillaume.Chapdelaine@univ-rouen.fr * http://www.mygale.org/08/gchapdel/ From owner-structural-nmr@net.bio.net Sun Sep 13 23:00:00 1998 Path: biosci!biosci!not-for-mail From: "clive delmonte" Newsgroups: bionet.structural-nmr Subject: DNA Structure Discussion Continued Date: 14 Sep 1998 10:56:28 -0700 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 1007 Sender: daemon@net.bio.net Approved: raman@hemebase.bio.uci.edu Distribution: world Message-ID: <6tjlcc$hed@net.bio.net> NNTP-Posting-Host: net.bio.net Bill further asks whether the side-by-side structure set out in my first attachment does not contradict the structures derived from the fibres. This is a key question and requires a full answer (if you'll indulge me a little.) There are several aspects to this. First, Crick had never seen any of Franklin's (high quality) DNA fibre diffraction patterns when he and Watson proposed their structure. Watson had seen a B-DNA pattern only very briefly and could not study it at leisure. Plectonaemic winding in DNA had already been proposed by Pauling & Corey early in 1953 and Watson & Crick seem to have adopted that idea. A R Stokes, a colleague and co-worker of Crick, had deduced an important geometric ratio for the classical helical cross (Prog. Biophys. & Biophys. Chem. 5 (1955) 140-167, page 163) (see attachment) such that, for the angle from the vertical (delta), tan delta = helical pitch / (helical circumference). In Franklin's famous B-DNA diffraction pattern (see attachment), delta = 40 degrees approximately, and, as the pitch is known to be 33.4 Angstroms from the layer lines, we deduce that the major diffractors lie on a helix of diameter of about 12 to 13 Angstroms. This is close to Franklin's deduction of a diameter of 11 Angstroms from her Pattersons. I now have seventeen published DNA fibre diffraction studies in which the researchers make it explicitly clear that they chose a unit cell which would be large enough to accommodate a double helical diameter of some 19-23 Angstroms even though their patterns of systematic absences in the reflections would have allowed them to choose a smaller unit cell (into which the double helix could not be fitted.) I also have references to unpublished studies in 3 or 4 PhD theses where a larger unit cell was chosen than the raw diffraction data actually required. I should be very glad to forward the list of references to anyone interested. If you choose the smaller unit cell allowed by the dffraction pattern and recalculate the helical diameter (a simple geometric exercise, of course), you get diameters in the range 11.2 to 13.6 Angstroms. A really fascinating study in conventional chemistry is that of James & Mazia (Biochim.Biophys.Acta 10 (1953) 367-370). They discovered that 1 mg of dry calf thymus DNA could be spread in a monolayer to cover 0.28 square metres. They didn't notice that from just this result alone we can directly estimate the minor axis diameter of the duplex as 11.7 Angstroms. I would be very glad if people would like to calculate the diameter for themselves and compare their sums with mine. (James & Mazia measured the major axis diameter, that is the height of the spread film in a separate experiment as 21.6 Angstroms. Therefore their results lead us to a duplex with an elliptical section.) The new model for DNA structure leads to the presence of a "front" and a "rear" face with great implications for protein-DNA recognition, including the way such DNA would wind onto nucleosomal cores, for example. What problems would people see with this account so far, please ? 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MU]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7 MU]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7 MU]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7 MU]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7 MU]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7 MU]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7 MU]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7 MU]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7 MU]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7 MU]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7 MU]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7 MU]?7U]?7U]H"``!E```````````````````````H````( ```!4````!``@` M`````* "``"#/0``@ST````!````````V-C8V-C8V-C8V-C8V-C8V-C8V-C8 MV-C8V-C8V-C8V-CFU]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U^;7 MU]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7YM?7U]?7U]?7U]?7U]?7 MU]?7U]?7U]?7U]?7U]?7U]?FU]?7U]?7U]?7U]?7U]?7U]?7]=?7U]?7U]?7 MU]?7U^;7U]?7U]?7U]?7U]?7U]?7U]?7Y-?7U]?7U]?7U]?7YM?7U]?7U]?7 MU]?8U]?7U]?7U]?MV-CBU]?7U]?7U]?FU]? MU]?7U]?7U]?7[]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7[]?B MU]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?SXM?7U]?7U]?7U]?7 MU]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7U]?7 =U]?7U]?7U]?7U]?7U]?7U]?7U]?7LHD``%2C```` ` end From owner-structural-nmr@net.bio.net Mon Sep 14 23:00:00 1998 Path: biosci!biosci!not-for-mail From: porn@atc.atccu.chula.ac.th Newsgroups: bionet.structural-nmr Subject: deuterated glycerol Date: 15 Sep 1998 08:40:04 -0700 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 11 Sender: daemon@net.bio.net Approved: raman@hemebase.bio.uci.edu Distribution: world Message-ID: NNTP-Posting-Host: net.bio.net Dear colleagues: I would appreciate if anyone out there could provide me info about deuterated glycerol. Thank you in advance Pornthep From owner-structural-nmr@net.bio.net Mon Sep 14 23:00:00 1998 Path: biosci!biosci!not-for-mail From: Istvan Pelczer Newsgroups: bionet.structural-nmr Subject: labeled AAs Date: 15 Sep 1998 14:55:28 -0700 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 15 Sender: daemon@net.bio.net Approved: raman@hemebase.bio.uci.edu Distribution: world Message-ID: NNTP-Posting-Host: net.bio.net Dear Netters, I am looking for source of 15N and 15N/13C labeled, FMOC (preferred) or tBOC amino acid derivatives. Your help will be appreciated, All the best, Istvan wwww,wwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwww Istvan Pelczer, Ph.D. Email: ipelczer@princeton.edu Senior NMR Spectroscopist Princeton University Department of Chemistry, Frick Lab., ph# (609) 258 2342 Washington Road fax# (609) 258 6746 Princeton, NJ 08544, USA From owner-structural-nmr@net.bio.net Wed Sep 16 23:00:00 1998 Path: biosci!biosci!not-for-mail From: Jason Rife Newsgroups: bionet.structural-nmr Subject: Post-doctoral position Date: 17 Sep 1998 08:54:02 -0700 Organization: Department of Chemistry, Yale University Lines: 14 Sender: daemon@net.bio.net Approved: raman@hemebase.bio.uci.edu Distribution: world Message-ID: <36011A62.41C6@proton.chem.yale.edu> NNTP-Posting-Host: net.bio.net I am seeking a postdoctoral fellow with some experience in multi-dimensional NMR for the determination of RNA structure. The specific project is to solve the structure of two regions of 5S rRNA that are important recognition elements for protein binding. This project is being done in collaboration with a group at the Medical College of Virginia. The applicant must be a US citizen or a permanent resident. This position is available immediately and should be filled by January 1999. Dr. Paul W. Huber University of Notre Dame Department of Chemistry & Biochemistry 251 Nieuwland Science Hall Notre Dame, IN 46556-5670 From owner-structural-nmr@net.bio.net Sun Sep 20 23:00:00 1998 Path: biosci!biosci!not-for-mail From: John Tomaszewski Newsgroups: bionet.structural-nmr Subject: Linux and NMRPipe Date: 20 Sep 1998 17:13:49 -0700 Organization: University of Washington Lines: 59 Sender: daemon@net.bio.net Approved: raman@hemebase.bio.uci.edu Distribution: world Message-ID: Reply-To: John Tomaszewski NNTP-Posting-Host: net.bio.net Hi all, A month ago I installed Linus (RH5.1) and a few of the free NMR processing and analysis programs to what would best allow me to bring data between the SGIs at work and Linux at home. Among them was NMRPipe. It installed and worked fine. Then the HD crashed. So I re-installed everything (pretty much the same, but I did get some more recent graphics libraries, etc.) but this time around nmrDraw reports: Failed default color initialization; consider using option '-virt Sometimes'. NMRDraw Notice: Failed to Allocate 32 Colors and 1 Plane(s); Consider using option '-virt Sometimes'. Retrying color allocation ... NMRDraw Notice: Failed to Allocate 32 Colors and 0 Plane(s); Retrying color allocation ... NMRDraw Notice: Failed to Allocate 30 Colors and 0 Plane(s); Retrying color allocation ... .... NMRDraw Notice: Failed to Allocate 4 Colors and 0 Plane(s); Retrying color allocation ... NMRDraw Notice: Failed to Allocate 2 Colors and 0 Plane(s); Retrying color allocation ... Segmentation fault (core dumped) I read the notes on color allocation tables in the README file but none of that info. helped (ie. tried -virt always, sometimes, and never). I run at 16bpp by default but have also tried 8bpp and 24bpp to no avail. Can anyone shed any light on the problem? P.S. Here's some of the output of my X session in case it's of any use: (--) Mach64: Maximum allowed dot-clock: 230.000 MHz (**) Mach64: Mode "1280x1024": mode clock = 110.000 (**) Mach64: Mode "1024x768": mode clock = 85.000 (--) Mach64: Virtual resolution: 1280x1024 (**) Mach64: Video RAM: 4096k (--) Mach64: Using hardware cursor (--) Mach64: Using 16 MB aperture @ 0xe0000000 (--) Mach64: Using 4 KB register aperture @ 0xe1000000 (--) Mach64: Ramdac is Internal (--) Mach64: Ramdac speed: 230 MHz (**) Mach64: Color weight: 565 (--) Mach64: Pixmap cache: 1 256x256 slots, 2 128x128 slots, 8 64x64 slots (--) Mach64: Font cache: 16 fonts System: `/usr/X11R6/lib/X11/xkb/xkbcomp -w 1 -R/usr/X11R6/lib/X11/xkb -xkm -m us_microsoft -em1 "The XKEYBOARD keymap compiler (xkbcomp) reports:" -emp "> " -eml "Errors from xkbcomp are not fatal to the X server" keymap/xfree86 compiled/xfree86.xkm' waiting for X server to shut down xterm: fatal IO error 32 (Broken pipe) or KillClient on X server ":0.0" xterm: fatal IO error 32 (Broken pipe) or KillClient on X server ":0.0" xterm: fatal IO error 32 (Broken pipe) or KillClient on X server ":0.0" Thanks in advance, John Tomaszewski