RCSB PDB Newsletter
Number 30 -- Summer 2006
Published quarterly by the
Research Collaboratory for Structural Bioinformatics Protein Data Bank
Weekly RCSB PDB news is published at www.pdb.org
To change your subscription options, please visit
lists.sdsc.edu/mailman/listinfo.cgi/rcsb-news
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TABLE OF CONTENTS
Message from the RCSB PDB
Data Deposition and Processing
pdb_extract Now Supports NMR Depositions
Deposition Statistics
Data Query, Reporting, and Access
RCSB PDB Offers Web Services
Automated Downloads of PDB Data
Website Statistics
RSS Functionality at the RCSB PDB
Outreach and Education
RCSB PDB FOCUS: Using Images from the RCSB PDB
BioSync is Alive and Growing
RCSB PDB Poster Prize at ACA, ECM, ISMB, and AsCA
Art of Science Exhibits at UCSD
Meetings and Exhibits
PDB Education Corner: Cheryl Campbell, New Providence High School
PDB Community Focus: Michael G. Rossmann, Purdue University
Molecules of the Quarter
RCSB PDB Partners, Leadership Team, and Statement of Support
Snapshot
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MESSAGE FROM THE RCSB PDB
When it was established in 2003, the Worldwide Protein Data Bank
(wwPDB) formalized a long-standing collaboration between founding
members RCSB PDB, the Macromolecular Structure Database at the
European Bioinformatics Institute (MSD-EBI), and Protein Data Bank
Japan (PDBj).
The wwPDB recognizes the international character of the PDB and
ensures that the archive will remain single and uniform.
During the past quarter, the BioMagResBank (BMRB) joined the wwPDB.
The BMRB, located at the University of Wisconsin-Madison, is the
archive for the experimental data gathered from NMR spectroscopic
investigations of biological macromolecules. The BMRB group has
created ADIT-NMR to enable authors to deposit experimental and
coordinate data using a single tool. We look forward to developing
future projects with the wwPDB.
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DATA DEPOSITION AND PROCESSING
pdb_extract NOW SUPPORTS NMR DEPOSITIONS
The program pdb_extract(1), which has simplified the deposition of
crystal structures, can now be used for NMR depositions. The latest
version supports NMR-related information from the applications
X-Plor/CNS/CNX, CYANA, and DYANA. Other enhancements made to the
pdb_extract suite are detailed in the Version Release Notes available
from the pdb_extract website.
pdb_extract minimizes errors and saves time during the deposition
process since fewer data items have to be manually entered.
The program extracts key details from the output files produced by
many X-ray crystallographic and NMR applications for use in the
deposition process. The program merges these data into macromolecular
Crystallographic Information File (mmCIF) data files that can be used
with ADIT to perform validation and to add any additional information
for PDB deposition.
pdb_extract can be used via web interface or downloadable workstation
from pdb-extract.rcsb.org.
(1)Automated and accurate deposition of structures solved by X-ray
diffraction to the Protein Data Bank. (2004) Acta Cryst. D60,
pp. 1833-1839.
DEPOSITION STATISTICS
In the first half of 2006, 3547 structures were deposited to the PDB
archive.
The entries were processed by the wwPDB teams at RCSB PDB,
MSD-EBI, and PDBj. Of the structures deposited, 70% were deposited
with a release status of "hold until publication"; 17% were released
as soon as annotation of the entry was complete; and 13% were held
until a particular date.
81% of these entries were determined by X-ray crystallographic
methods; 15% were determined by NMR methods; and 82% of all of these
depositions were deposited with experimental data.
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DATA QUERY, REPORTING, AND ACCESS
RCSB PDB OFFERS WEB SERVICES
The RCSB PDB has introduced Web Services to help the software
developer community build tools that interact more effectively with
PDB data. Instead of storing coordinate files and related data
locally, web services provide a way for software tools to interact
with the RCSB PDB remotely.
The RCSB PDB's web services were implemented using Axis
(http://ws.apache.org/axis/) and include BLAST, FASTA, PubMed, and SNP
queries. A complete list of web services and their WSDL description
(Web Services Description Language in XML Format) is available.
Web services allow the developer community to build applications that
are platform independent and require only a traditional HTTP
connection. This is especially useful for developing in environments
with relatively tight security constraints. Web services also provide
a low-overhead approach to designing workflow applications that
integrate remote services. Developers can write efficient and
manageable distributed tools without having to worry about low-level
communication details. Using web services, programmers can write
efficient workflow tools. For example, a developer could write a tool
that interoperates between local data, PDB data, and NCBI data.
For general information on web services, please visit
http://www.w3.org/2002/ws/.
AUTOMATED DOWNLOADS OF PDB DATA
The RCSB PDB FTP site provides coordinate data (in PDB, mmCIF, and
PDBML/XML formats) and experimental data. A web interface offers a way
to download multiple data files from the archive. Scripts are also
available to assist in the automated download of data from the ftp
site:
ftp://snapshots.rcsb.org/rsyncSnapshots.sh
Makes a local copy of an annual snapshot or sections of the
snapshot. This script is annotated to assist in downloading only
sections of the archive. The time required to download the entire
archive can be lengthy (18+ hours); however, the time required to
download the coordinate data in a single format should be much
less. While the amount of time depends upon network speed, our tests
show that all of the coordinate files in PDB format from a snapshot
can be downloaded in about 2 1/2 hours.
ftp://ftp.rcsb.org/pub/pdb/software/rsyncPDB.sh
Copies the current contents of the entire archive.
ftp://ftp.rcsb.org/pub/pdb/software/getPdbStructures.pl
Copies portions of the archive.
ftp://ftp.rcsb.org/pub/pdb/software/getPdbUpdate.pl
Copies the data from the weekly updates.
Questions and comments about these scripts should be sent to info@rcsb.org.
WEBSITE STATISTICS
Access statistics for www.pdb.org are given below for the second quarter of 2006.
MONTH...UNIQUE VISITORS...# OF VISITS.....BANDWITH
APR...........152465........318730........654.20GB
MAY...........157055........336815........529.67GB
JUN...........184812........398210........547.05GB
RSS FUNCTIONALITY AT THE RCSB PDB
An RSS (Really Simple Syndication) feed provides users with a list of
newly updated structures as soon as they are available. RSS pushes
information that can be read by client software (an RSS reader) that
sits on your local computer. Rather than going to look for new PDB
entries, they can come to you.
To start, download and install an RSS reader. Depending on your
reader, either drag or click on the orange RSS icon from the top of
the RCSB PDB home page (located just next to the latest release date)
to add the URL for new structures to your RSS reader.
You will now be informed of new structures as they become
available. Clicking on the update notice will take you to the list of
new structures.
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OUTREACH AND EDUCATION
RCSB PDB FOCUS: USING IMAGES FROM THE RCSB PDB
The contents of the RCSB PDB are in the public domain. Online and
printed resources are welcome to include PDB data and images from the
RCSB PDB pages as long as the images are not being sold
commercially. It is expected that the corresponding citations are
included.
For example, the prepared images available for each structure (from
the Structure Explorer pages) should cite the corresponding reference
for the entry and the RCSB PDB:
PDB ID: 1di0. B.C.Braden, C.A.Velikovsky, A.A.Cauerhff, I.Polikarpov,
F.A.Goldbaum, Divergence in Macromolecular Assembly: X-Ray
Crystallographic Structure Analysis of Lumazine Synthase from Brucella
abortus, J.Mol.Biol. 297 pp. 1031 (2000). Image from the RCSB PDB
(www.pdb.org; H.M.Berman, J.Westbrook, Z.Feng, G.Gilliland, T.N.Bhat,
H.Weissig, I.N.Shindyalov, P.E.Bourne, The Protein Data Bank, Nucleic
Acids Research, 28 pp. 235-242 (2000))
Pictures from Molecule of the Month features should also credit the
illustrator David S. Goodsell of the Scripps Research Institute:
Image of luciferase from David S. Goodsell's (The Scripps Research
Institute) Molecule of the Month series at the RCSB PDB (www.pdb.org;
H.M.Berman, J.Westbrook, Z.Feng, G.Gilliland, T.N.Bhat, H.Weissig,
I.N.Shindyalov, P.E.Bourne, The Protein Data Bank, Nucleic Acids
Research, 28 pp. 235-242 (2000); structure shown is 2d1s: T.Nakatsu,
S.Ichiyama, J.Hiratake, A.Saldanha, N.Kobashi, K.Sakata, H.Kato,
Structural basis for the spectral difference in luciferase
bioluminescence, Nature, 440 pp.372-376 (2006))
A full list of related citations is available online.
BIOSYNC IS ALIVE AND GROWING
BioSync (Structural Biology Synchrotron Users Organization) was formed
in 1990 as a grassroots organization intended to promote access to
synchrotron radiation. It established a web-based clearinghouse for
beamline information at synchrotron facilities. The BioSync resource,
originally designed and hosted by UCSD/SDSC, has been updated and is
now being maintained by the RCSB PDB at BioSync.rcsb.org.
With its new look, the BioSync website currently contains updated
descriptions of operational US synchrotron beamlines used for single
crystal macromolecular crystallography. International sites and
beamlines are listed and will go 'live' as data is added for each
one. PDB deposition statistics, grouped by site and beamline and
cross-linked to the RCSB PDB, are also available.
Comments and suggestions are welcome at BioSync@deposit.pdb.org.
RCSB PDB POSTER PRIZE AT ACA, ECM, ISMB, AND AsCA
The RCSB PDB is pleased to announce the 2006 RCSB PDB Poster Prize,
which recognizes student poster presentations at society meetings.
The prize will be awarded to the best posters related to
macromolecular crystallography by undergraduate or graduate students
at each of the meetings of the IUCr Regional Associates: the American
Crystallographic Association (ACA), the European Crystallographic
Association (ECM), and the Asian Crystallographic Association (AsCA).
At the Intelligent Systems for Molecular Biology (ISMB), the prize
will be awarded to the best student poster in the "Structural
Bioinformatics" category.
The awards consist of related educational books, and will be announced
through the RCSB PDB website and newsletter. Information about
previous winners and awards is available.
ART OF SCIENCE EXHIBITS AT UCSD
Featuring images that explore the beauty found in structural biology,
the RCSB PDBs Art of Science exhibit was on display with other
artworks at Calit2 (University of California, San Diego) from June 9
30, 2006.
Molecule of the Month writer and illustrator David S. Goodsell (The
Scripps Research Institute) provided additional watercolors, including
a cross-section of blood serum, the interaction of HIV in the blood,
and an illustration of a eukaryotic cytoplasm.
A wood carving of anthocyanidin synthatase, the natural pigment of
berries, fruits and grapes, and a sculpture of human metalloelastase
both by Edgar Meyer (Texas A&M) were also on display.
The exhibit was located in the Calit2 building on the UCSD campus,
next to the virtual reality visualization lab where PDB-in-a-CAVE
demonstrations are run. The CAVE offers a room-sized space for users
to interact with high-resolution video. Wearing stereoglasses, the
viewer can move through and around a projected biological
macromolecule.
The Art of Science traveling exhibit includes pictures available from
the RCSB PDB website and Molecule of the Month features. Since its
beginnings at Rutgers University in New Jersey, the show has traveled
to EMBL-Hamburg, Germany; University of Wisconsin-Madison; California
State University, Fullerton; Purdue University; and Hyderabad,
India. The RCSB PDB would like to see the Art of Science travel to
other places. If you would be interested in sponsoring this exhibit at
your institution, please let us know at info@rcsb.org.
David Goodsell: http://www.scripps.edu/mb/goodsell/
Edgar Meyer: http://molecular-sculpture.com
MEETINGS AND EXHIBITS
* NSTA. Jeff Milton met with teachers from around the country at the
RCSB PDBs exhibit booth at the National Science Teachers Association
54th National Conference on Science Education (April 6-9 in Anaheim,
CA).
* MAMC. Annotator Massy Rajabzadeh presented the poster "Depositing
Crystal Structures at the RCSB PDB in Five Simple Steps" and met with
depositors at the 36th Mid-Atlantic Macromolecular Crystallography
Meeting (June 1-3 at Wake Forest University in Winston-Salem, NC).
* Three-Dimensional Electron Microscopy. RCSB PDB Director Helen
M. Berman described "How the History of the Protein Data Bank can
inform the Future of Structural Biology" as one of the Keynote
Lectures at the Gordon Conference on Three-Dimensional Electron
Microscopy (June 25-30 at Il Ciocco, Barga, Italy).
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PDB EDUCATION CORNER: CHERYL CAMPBELL, NEW PROVIDENCE HIGH SCHOOL
Cheryl Campbell graduated from Boise State University in Idaho in 1982
with a Bachelor of Science degree in Biology, and received her Masters
in Teaching Natural Science from Rensselaer Polytechnic Institute in
Troy, New York in 2002. After teaching for 13 years in Idaho in a
small rural school, she moved to New Jersey and started teaching in
New Providence. Through the years, she has taught Biology, Life
Science, AP Biology, Honor's Biology, and Environmental Studies.
In October of 2005, I happened to notice a presentation on proteins
while attending a convention for science teachers in New Jersey. I
walked in and heard several people, including Christine Zardecki, talk
about protein structure. The hands-on demonstrations with modeling
kits(1) were fantastic, and I immediately knew I had to get the kits for
my students. I ordered 10 kits and after using them, each class
Biology, Honors Biology, and AP Biology seemed to understand a little
more about the three dimensional structures of proteins. The kits
were such a success in the classroom that when I heard there was a
competition on protein structure at the Science Olympiad it didn't take
much to convince the Biology Club to give the competition a try. The
students worked early and late, trying to learn how to use the RasMol
program and create a model of the TATA binding protein for the
competition in January 2006. I am proud of the students who
represented us at the Science Olympiad, and hope to participate again
next year.
After the Olympiad, we were still thirsty to learn more from the PDB.
So on Wednesday, March 22, 2006, 10 juniors and seniors from New
Providence High School (NJ) spent the day at Rutgers University
listening and watching as scientists described and demonstrated their
research projects.
We began our day with Dr. David A. Toke, our guide for a walking tour
of the Rutgers University Cell and DNA Repository. He expertly
described the steps in making cell lines that are being used to learn
more about specific genes and their function. His own studies include
taking a genetic approach to the study of addiction, longevity and
many diseases. The students were particularly amazed at the size of
the liquid nitrogen containers and the details required to insure both
the privacy of data from human subjects and accuracy of data.
Next we had a chance to sit down and listen to Dr. Cathy Lawson
(Department of Chemistry and Chemical Biology) describe how lysozyme
crystals are grown. This was a very complicated talk, and the
students were amazed at what the crystals look like and their role in
the determination of protein structures.
Dr. Helen M. Berman, the director of the RCSB PDB, gave the students a
great history of structural biology and the PDB. It is impressive to
think of how much has become understood in the past 35 years.
After lunch, the students met two graduate students in Dr. Kathryn
Uhrichs (Department of Chemistry and Chemical Biology) group Min Jung
Song and Jinzhong Wang. These students were the best. They showed us
their experiments and talked about scientific discovery. The class
saw how the process of learning by performing an experiment, and then
rethinking their hypotheses using the results, worked in this
laboratory.
The day was a great success. Each of my students gained some insight
on how real research works. Experiences like this can help energize
students to pursue science in their own college education and I would
encourage more high school teachers to take advantage of what can be
gained by interacting with the information in the PDB.
(1)Materials included the Mini-Toobers from 3D Molecular Designs
(http://www.3dmoleculardesigns.com), and the MSOE Model Lending
Library (http://www.rpc.msoe.edu/lib/how.php)
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PDB COMMUNITY FOCUS: MICHAEL G. ROSSMANN, PURDUE UNIVERSITY
Michael Rossmann was born in Frankfurt (Main), Germany in 1930. He
and his mother moved to England in 1939. He obtained a University of
London B.Sc. degree in physics and mathematics. While teaching
physics at the Royal Technical College in Glasgow (now the University
of Strathclyde), he moonlighted at the University of Glasgow,
obtaining a Ph.D. in chemical crystallography under the supervision of
John Monteath Robertson. During that time, he married Audrey Pearson.
His first two years of postdoctoral studies were in Bill Lipscomb's
laboratory at the University of Minnesota where he spent some of his
time writing some of the earliest crystallographic computer programs
for structure determination and refinement. He returned to England in
1958 to join Max Perutz in Cambridge where he participated in the
structure determination of horse oxy-hemoglobin at 5.5 Angstrom
resolution, thereby demonstrating the common evolutionary origin of
oxygen carriers, such as hemoglobin and myoglobin. While in Cambridge
and inspired by the hemoglobin results, he and David Blow established
many of the techniques of modern macromolecular crystallography,
including the molecular replacement method.
In 1964, he moved to Purdue University. Initially, he studied
dehydrogenases, discovering, in collaboration with Carl Branden in
Sweden and Len Banaszak at Washington University, that these proteins
had a common NAD binding fold and, by extrapolation, that there
existed a primordial nucleotide binding fold. He initiated his work
on virus structure with a 1971 sabbatical half year with Bror
Strandberg in Sweden. In 1985, he and his colleagues determined the
structure of a common cold virus, the first animal virus to be
determined to near atomic resolution, showing that there was a common
origin of the capsid protein and assembly for simple RNA animal and
plant viruses. This work had required the development of X-ray
diffraction data processing techniques and the use of synchrotron
methods, including the American method (still very much in favor among
American politicians) of shooting first and thinking later
(i.e. by-passing the old crystallographic technique of first setting
crystals in order to be able to index the reflections).
He has continued to study numerous viruses, including the West Nile
virus, the giant Mimivirus, and the bacteriophage T4. Currently, he
is much involved in the use of cryo-electron microscopy (cryoEM) to
extend the range of crystallography by combining low resolution
cryoEM three-dimensional images with high resolution crystal
structures of component proteins.
Q: What was it like working in Cambridge in the 1950s? What made you
decide to go to there at this time?
A: Before I went to Cambridge, my interest in crystallography was
fueled mainly by an interest in solving the phase problem for specific
structures. I had heard a talk by Dorothy Hodgkin at the 1957 IUCr
meeting in Montreal on the work in Cambridge by Perutz and Kendrew who
were trying to solve the structure of proteins. With thousands of
atoms per molecule, this seemed to be the ultimate challenge. Thus,
when my postdoctoral time with Bill Lipscomb was nearing its end, I
wrote a letter to Max Perutz asking whether he might have a job for
me. He replied positively. Later, I discovered that many
crystallographers thought that attempting to determine the structure
of proteins was an unattainable objective and, hence, Max had had
difficulty in finding helpers for his project. No doubt that was why
he was now willing to take me into his small group.
Cambridge was a very new experience for me. Max's lab was a part of
the famous Cavendish Laboratory where Rutherford, Thompson, and others
had laid the foundations of nuclear physics. However, Max's group,
initiated under the guidance of Sir Lawrence Bragg before he moved to
the Royal Institution in London, had been expelled to a small hut
outside the Austin wing of the Cavendish lab. My most important
scientific education occurred during the morning coffee breaks when
the approximately dozen occupants of the "MRC Hut" met in the crammed
entrance area of the hut. This usually included Francis Crick, Sidney
Brenner, John Kendrew, and Max. It is here that I began to realize
that science is not only about solving puzzles, but, more importantly,
recognizing what are the current significant problems susceptible to
scientific investigation. We had relatively little contact with
University activities, but Max had kindly arranged for me to be a
"supervisor" for Peterhouse College. That required meeting with pairs
of undergraduates and guiding them in their studies relevant to their
current lecture courses. Like most people in England, I had always
expected to find the best brains among Cambridge students, but I soon
found that even in Cambridge there was quite a spread in ability.
The first year in Cambridge was especially exhilarating. This was the
year that we determined the 5.5 Angstrom structure of hemoglobin and
recognized its evolutionary implications. This made an enormous
impression on me and has guided my choice of research topics ever
since. In the subsequent years, together with David Blow, I explored
crystallographic techniques required in the potential determination
of other protein structures based on my experience with the hemoglobin
structure. It was David who suggested that we should study
chymotrypsin together, a project that was subsequently brought to
fruition by David and others after I had left Cambridge. These were
exciting times, but I have been very fortunate in having experienced
many more periods of frantic activity followed by great joy and
satisfaction with new discoveries and understanding. Nevertheless,
these first true adventures on the frontiers of science made a
lasting and deep impression.
Q: You were an early pioneer in methods development for protein
crystallography. What drew you to this topic?
A: To some extent, this question has been answered above. I gradually
realized that the fun of solving crystallographic puzzles was merely a
path to major discoveries in biology and medicine. The significance
of the hemoglobin structure, recognized subsequently by a Nobel Prize
to Max and John Kendrew, gave great satisfaction. Clearly, the daily
fun of writing new computer programs and trying to solve the little
daily problems, such as how to scale data on different films, was a
fairly certain path to discoveries of major importance.
Q: You have always taken a strong interest in the PDB -- why?
A: During the important biological structure meeting at Cold Spring
Harbor in 1971, Max called a meeting of all those who had coordinates
of a protein structure. This included Fred Richards (ribonuclease),
David Phillips (lysozyme), Jan Drenth (papain), and myself (lactate
dehydrogenase). Max was concerned about the easy availability and
preservation of coordinates. Walter Hamilton, of the Brookhaven
National Lab, volunteered to be the curator, thus marking the
beginning of the PDB. Sometime later, Fred Richards formed a steering
committee that included me.
Although there were less than about a dozen structures in the early
70s, there was a tendency not to release coordinates except to
friends. When Martha Ludwig and I were assistant editors to the
Journal of Biological Chemistry (JBC), we instituted a policy that if
a paper was dependent on a new set of coordinates, then these had to
be deposited with the PDB. JBC was probably the first journal that
had this policy. However, there were still quite a few published
structures whose coordinates were unavailable in the PDB. Spurred on
by need, I wrote a program that extracted coordinates from published
stereo diagrams (Rossmann, M. G., P. Argos. 1980. Three-dimensional
coordinates from stereodiagrams of molecular structures. Acta
Crystallogr. B36:819-823). Fortunately, in those days, structural
diagrams were usually merely a set of atomic positions joined by
bonds. Ribbon diagrams had not yet become popular, although my wife
had produced the first such figures based on models of carbonic
anhydrase made by Anders Liljas and Bror Strandberg while we were on
sabbatical leave in Uppsala (Liljas, A. et al. 1972. Crystal
structure of human carbonic anhydrase C. Nat. New Biol.
235:131-137). At the 1976 Erice meeting, I made a plea for the
compulsory deposition of coordinates for any published structure.
In more recent years, I have been concerned about maintaining funding
and continuity of services by the PDB.
Q: You have used crystallography to study structures ranging from
small molecules to proteins to large viruses. Recently, you have been
studying structures using cryo-electron microscopy. What do you see
as the next challenge?
A: For the PDB, there is a challenge for appropriate archiving of data
derived from an increasing variety of physical techniques, including
not only the final inferred coordinates, but also the raw data.
More generally, I see trends to look at structures of ever-increasing
complexity to a point where the structures of equivalent objects are
no longer sufficiently similar to permit crystallization or averaging
of single particles observed by electron microscopy. Such problems
may require using single particle diffraction techniques, high
intensity synchrotron X-ray sources, and tomographic electron
microscopic imaging. I expect that we will soon be looking at frozen
vitrified single cells and, in the distant future, even observing
living cells at near atomic resolution.
Clearly, such work will require ever larger PDB resources to make the
results generally available and to avoid loss of information. I see
the task of the PDB as being ever more challenging and more essential
to all of science. I am seriously afraid of bureaucratic interference
in the smooth development and growth of the PDB, which might have
major negative impact on scientific progress.
Q: What would be your advice to someone just starting out in
structural biology?
A: Keep working in the lab. Enjoy your successes and share them with
all who want to know. Find a mentor who can teach you a fundamental
appreciation of science like I had the opportunity to learn in
Cambridge. Never hide your ignorance, because then nobody can teach
you. If you are not enjoying your studies, go and do something else.
--------------------------------------------
MOLECULES OF THE QUARTER
The Molecule of the Month series explores the functions and
significance of selected biological macromolecules for a general
audience.
The molecules featured this quarter were hemagglutinin, glucose
oxidase, luciferase. All Molecule of the Month features are accessible
from the RCSB PDB home page.
----------------------------------------
STATEMENT OF SUPPORT
The RCSB PDB is supported by funds from the National Science
Foundation, the National Institute of General Medical Sciences, the
Office of Science, Department of Energy, the National Library of
Medicine, the National Cancer Institute, the National Center for
Research Resources, the National Institute of Biomedical Imaging and
Bioengineering, and the National Institute of Neurological Disorders
and Stroke.
The RCSB PDB is managed by two partner sites of the Research
Collaboratory for Structural Bioinformatics:
RUTGERS
Rutgers, The State University of New Jersey
Department of Chemistry and Chemical Biology
610 Taylor Road
Piscataway, NJ 08854-8087
SDSC/UCSD
San Diego Supercomputer Center and the Skaggs School of Pharmacy and
Pharmaceutical Sciences
University of California, San Diego
9500 Gilman Drive
La Jolla, CA 92093-0537
RCSB PDB LEADERSHIP TEAM
Dr. Helen M. Berman - Director
Rutgers University
berman@rcsb.rutgers.edu
Dr. Philip E. Bourne - Co-Director
SDSC/SKAGGS/UCSD
bourne@sdsc.edu
A list of current RCSB PDB Team Members is available from the website.
The RCSB PDB is a member of the Worldwide PDB (www.wwpdb.org)
-----------------------------------------
SNAPSHOT July 1, 2006
37392 released atomic coordinate entries
* Molecule Type
34221 proteins, peptides, and viruses
1627 nucleic acids
1510 protein/nucleic acid complexes
34 other
* Experimental Technique
31655 X-ray
5531 NMR
126 electron microscopy
80 other
21163 structure factor files
3014 NMR restraint files