PDB info file

Laura Lynn Walsh lwalsh at uxh.cso.uiuc.edu
Sat Dec 7 17:34:37 EST 1991


I have compiled a crossreference of the Brookhaven Protein Data Bank
files which may be of use to others.  If you find errors in this
listing please let me know.

/*
   This file was compiled by Laura Lynn Walsh, Beckman Institute,
   University of Illinois, 405 N. Mathews Ave., Urbana, IL 61801-2325
   (217) 244-6764   lwalsh at nemo.life.uiuc.edu

   Date begun: November, 1990
   Latest revision:  November, 1991

   This file is an annotation of all of the Brookhaven Protein Data
   Bank files with actual coordinates.  (The files beginning with
   pdb0 have been omitted until full coordinates are available.)
   The information has been taken from the Brookhaven Protein Data
   Bank and from original papers by authors listed in those files.
   Responsibility for the accuracy of the information is LLW's,
   who would welcome reports of errors and suggestions to extend
   the usefulness of the information.  This information is provided
	for your use and no warranty about the correctness of the infor-
	mation is made.

   Support from NSF-DIR90-19063 for LLW is gratefully acknowledged.

*/
/* 
   Description of Entries:

   The header line begins with the common name for the protein or 
   other molecule(s) contained in the file.I have tried to use 
   the most commonly accepted names, but in several cases, especially
   the immunoglobulin files, this has been difficult. 

   The molecule name is followed by its source.  This is the
   source of the original sequence.In several cases a protein
   is actually expressed in another organism, such as E. coli,
   but this is not noted in this file.

    DUP = duplicate entry.  This file is also listed for
         another protein or other molecule.  (E.g. the Eglin C
         and subtilisin complex is listed under both headers.)

   The file names from the Brookhaven Protein Data Bank have been
   abbreviated.  Where Brookhaven names the files pdbXXXX.ent, 
	the files are referred to here solely by the XXXX part.  Files 
	with a "w" appended to their names are files that I have 
	modified to make a "complete" protein, i.e., if the protein 
	is a tetramer and only two of the chains are given in the 
	original file, the new file would contain the tetramer and 
	conversely, if the original file contains two chains and 
   the protein is a monomer, this file contains a single chain.  
   These files are not publicly available at present.   

   The columns following the PDB file name indicate the resolution
   for the x-ray data.  If the file is an NMR file, "NMR" is in
   this field, since resolution is not applicable for these.  "CA"
   indicates that the entry contains coordinate information only
   for the alpha carbons.  "UNK" means the amino acid sequence
   is unknown.

   The body of the entry indicates how many chains are in the
   "complete" molecule (see below), how many chains are included
   in the entry, and any other information that helps distinguish
   that specific entry from another similar entry.  I have also
   included any information I had that could help in interpreting
   the data in the entry.In particular, I have attempted to
   include any possible differences between the crystallographic
   data and what is thought to be the active, "solution" structure
   of the molecule.  I am currently working on including information
	about ions and crystallization conditions, but this information
	should be considered incomplete.

*/
/*   

   "Correct" proteins are either the complete protein as seen in
   the pictures accompanying the original literature or, failing
   this, a protein that "looks ok" and which can be generated by
   both my program and Insight (Biosym) to look the same.  Failing 
   both of these, a correct protein is as close as I could come to 
   what I think is correct.  If it is not, PLEASE let me know.  
   
   The "correct" proteins were generated by one of several possible 
   methods:

   1)  If there was a matrix given in the data file itself which
   produced a "correct" protein, this was used.

   2)  If there was no applicable matrix, or if the matrix did
   not generate a correct protein, the International Table for
   Crystallography matrices were used.  If possible, these were 
   checked against the matrices and proteins produced by Insight 
   (Biosym).  Insight (Biosym) can do symmetry operations in its 
   Assembly module under the Symmetry command.  The program uses 
   a 4 X 4 matrix and is thus not the same as the program I use 
   to make symmetry related protein chains.  I use a 3 X 4 matrix. 

   I prefer my program for two reasons -- the atom numbering used 
	in the original file is retained and the symmetry related 
	chains are numbered 10000 more than the original atoms.  This 
	requires renumbering when there are several symmetry operations 
	performed, but it makes generating CONECT records much easier.  
*/


434 Cro Protein (Phage 434)
   2cro 2.35   monomer in solution - 1 chain given; dimer in crystal, 
               but dimerizes differently when bound to DNA; Insight
               can't find space group R 32; includes water
   
434 Repressor Protein - N Terminal Domain (Phage 434)
   1r69 2.0    monomer in solution - 1 chain given; includes water 
   2or1 2.5    dimer in complex with dsDNA (a2 + d2) - 4 chains given 
   
Acid Proteinase Endothiapepsin (Endothia parasitica)
   4ape 2.1    monomer; sequence numbering based on pepsin; includes water
   2er0 3.0    monomer; complex with inhibitor
   2er6 2.0    monomer; complex with inhibitor
   2er7 1.6    monomer; complex with inhibitor
   2er9 2.2    monomer; complex with inhibitor
   4er1 2.0    monomer; complex with inhibitor
   4er2 2.0    monomer; complex with inhibitor
   5er1 2.0    monomer; complex with inhibitor
   
Acid Proteinase Penicillopepsin (Penicillium janthinellum)
   2app 1.8    monomer
   3app 1.8    monomer; supersedes 2app; includes water 
   
Acid Proteinase Rhizopuspepsin (Rhizopus chinensis)
   2apr 1.8    monomer; supersedes 1apr; includes Ca++
   3apr 1.8    monomer; complex with reduced peptide inhibitor
   4apr 2.5    monomer; complex with a pepstatin-like renin inhibitor
   5apr 2.1    monomer; complex with a pepstatin-like renin inhibitor
   6apr 2.5    monomer; complex with pepstatin

Aconitase (Sus scrofa)
   5acn 2.1    monomer; inactive 3Fe-4S form
   6acn 2.5    monomer; active 4Fe-4S form; includes sulfate, tricar-
               ballylic acid and water

Actinidin (Actinidia chinensis)
   2act 1.7    monomer; supersedes 1act; includes oxygens, ammonium,
               and water
   
Actinoxanthin (Actinomyces globisporus, number 1131)
   1acx 2.0    monomer
   
Adenylate Kinase (Sus scrofa)
   3adk 2.1    monomer; supersedes 2adk; includes sulfates
  
Agarose (Rhodophycae)
   1aga 3.0    sugar polymer; NOT PROTEIN

Alamethicin (Trichoderma viride)
   1amt 1.5    3 chains given; contains many AIBs & 3 PHLs
   
Alcohol Dehydrogenase (Equus caballus)
   5adh 2.9    dimer (a2) - 1 chain given; apo; complex with ADP-ribose
   6adh 2.9    dimer (a2) - 2 chains given; holo; complex with NAD & DMSO
   7adh 3.2    dimer (a2) - 2 chains given; isonicotinamidylated
   8adh 2.4    dimer (a2) - 1 chain given; apo
   8adhw       dimerized acc to included matrix
   
Alpha-Amylase Inhibitor HOE-467A (Streptomyces tendae, 4158)
   1hoe 2.0    monomer
   
Alpha-Lytic Protease (Lysobacter enzymogenes)
   1p01 2.0    complex with substrate analogs
   1p02 2.0    complex with substrate analogs
   1p03 2.15   complex with substrate analogs
   1p04 2.55   complex with substrate analogs
   1p05 2.10   complex with substrate analogs
   1p06 2.34   complex with substrate analogs
   1p07 2.25   complex with substrate analogs
   1p08 2.25   complex with substrate analogs
   1p09 2.20   complex with substrate analogs
   1p10 2.25   complex with substrate analogs
   2alp 1.7    monomer; gaps in numbering
   
Alpha-1 Proteinase Inhibitor (Homo sapiens)
   Cleavage of original monomer yields 2 or 3 chains - 3rd "chain" is
   a single Cys residue.
   5api 3.0    2 chains given; modified; bond cleavage results in large 
               structural change; superseded by 7api
   6api 3.0    2 chains given; modified; bond cleavage results in large 
               structural change; active structure may be quite different; 
               superseded by 8api
   7api 3.0    3 chains given; modified; structural change; tetragonal form 1; 
               supersedes 5api
   8api 3.1    3 chains given; modified; structural change; hexagonal form; 
               supersedes 6api
   9api 3.0    3 chains given; modified; structural change; tetragonal form 2

Apolipoprotein D (Homo sapiens)
   1apd ---    model; non-experimental

   L-Arabinose binding protein (Escherichia coli)
   1abp 2.4    monomer
   
Aspartate Aminotransferase (Gallus gallus)
   1aat 2.8 CA complex with 2-oxo-glutaric acid
   
Aspartate Aminotransferase (Escherichia coli)
   2aat 2.8    dimer (a2) - 1 chain given; mutant K258A; complex with 
               pyridoxamine phosphate; 
   2aatw       made; checked on Iris
   
Aspartate Carbamoyltransferase (Escherichia coli)
   2atc 3.0    dodecamer (3[a2b2]) - 2 chains given; unliganded
   4atc 2.6    dodecamer (3[a2b2]) - 4 chains given; unliganded; 
               superseded by 6at1
   7atc 2.6    dodecamer (3[a2b2]) - 4 subunits; complex with CTP; 
               supersedes 5atc; superseded by 5at1
   8atc 2.5    dodecamer (3[a2b2]) - 4 chains given; R state; 
               complex with PALA
   1at1 2.8    dodecamer (3[a2b2]) - 4 chains given; R state; 
               complex with PAM & MAL
   2at1 2.8    dodecamer (3[a2b2]) - 4 chains given; R state; 
               complex with PAM & MAL
   3at1 2.8    dodecamer (3[a2b2]) - 4 chains given; T state; complex with PAM
   4at1 2.6    dodecamer (3[a2b2]) - 4 chains given; T state; complex with ATP
   5at1 2.6    dodecamer (3[a2b2]) - 4 chains given; T state; complex with CTP; 
               supersedes 7atc
   6at1 2.6    dodecamer (3[a2b2]) - 4 chains given; T state; supersedes 4atc
   7at1 2.8    dodecamer (3[a2b2]) - 4 chains given; R state; 
               complex with PAM, MAL, & ATP
   8at1 2.8    dodecamer (3[a2b2]) - 4 chains given; R state; 
               complex with PAM, MAL, & CTP

ATX 1A (Anemonia sulcata)
   1atx NMR    monomer - 8 chains given; lowest energy conformation is model 1
   
Azurin (Alcaligenes denitrificans)
   2aza 1.8    monomer - 2 chains given; oxidized
   2azaw       half of coords eliminated; monomer remains; there are a lot
               of contacts between the independent molecules in the crystal
   
Azurin (Pseudomonas aeruginosa)
   1azu 2.7    monomer 
   
Bacteriochlorophyll-A Protein (Prosthecochloris aestuarii, strain 2K)
   3bcl 1.9    monomer; many UNK residues; all ASP & ASN are ASX; 
               all GLU & GLN are GLX
   
Bacteriorhodopsin (Halobacterium halobium)
   1brd 3.5*   monomer; resolution 3.5 in x and y directions, 10.0 in z
   
BDS-1 (Anemonia sulcata)
   1bds  NMR   monomer; averaged structure
   2bds  NMR   monomer - 42 simulated annealing structures

Bean Pod Mottle Virus - Middle Component (Bountiful bean)
   1bmv  3.0   120mer + RNA (60ab + r) - 3 chains given; unusual numbering 
               system; Insight can't find space group P 2 21 21
   
Alpha Bungarotoxin (Bungarus multicinctus)
   related to Cobratoxin
   2abx 2.5    dimer (a2) - 2 chains given; due to crystal contacts, Phe 
               sticks out into solvent - near to another Phe in a neighboring
               molecule
   
Calcium-Binding Parvalbumin B (Cyprinus carpio)
   1cdp 1.6    monomer; Cadmium substituted
   1cpv 1.85   monomer
   2cpv 1.85   monomer
   3cpv 1.85   monomer
   4cpv 1.5    monomer; pI 4.25
   5cpv 1.6    monomer; supersedes 1cpv, 2cpv, 3cpv; due to crystal contacts, 
               phe sticks out into solvent - near to another phe in a 
               neighboring molecule
   
Calcium-Binding Protein (Bos taurus)
   3icb 2.3    monomer; supersedes 2icb;
   
Calmodulin (Bos taurus)
   2cln ---    trimethyl Cln complex with trifluroperazine; non-exp'l model
   3cln 2.2    monomer
   
Carbonic Anhydrase I, Form B (Carbonate Dehydratase) (Homo sapiens)
   2cab 2.0    monomer
   
Carbonic Anhydrase II (Homo sapiens)
   1ca2 2.0    monomer
   2ca2 1.9    monomer; complex with thiocyanate ion
   3ca2 2.0    monomer; complex with AMS

Carboxypeptidase A (Bos taurus)
   3cpa 2.0    monomer; alpha; complex with glycyl-L-tyrosine 
   4cpa 2.5    monomer; alpha; complex with inhibitor
   5cpa 1.54   monomer; alpha
   
Carboxypeptidase B (Bos taurus)
   1cpb 2.8 CA monomer; fraction II
   
D-Alanyl-D-Alanine Carboxypeptidase/Transpeptidase (Streptomyces r61)
   1pte 2.8 CA seq uncertain

Capsular Polysaccharide (Escherichia coli)
   1cap 3.0    from mutant; NOT PROTEIN
  
Cardiotoxin V4 (Naja mossambica mossambica)
   1cdt 2.5    2 chains given

Catabolite Gene Activator Protein (Escherichia coli)
   2gap ---    complex; model
   3gap 2.5    dimer (a2) - 2 chains given - have diff configurations; 
               complex with cyclic AMP

Catalase (Penicillium vitale)
   4cat 3.0    all residues listed as UNK

Catalase (Bos taurus)
   7cat 2.5    tetramer (a4) - 1 chain given
   8cat 2.5    tetramer (a4) - 2 chains given
   8catw       tetramerized acc. to instructions; doesn't correspond 
               to any replicate generated by Insight and matrix does
               not correspond to one in the International Tables;
               literature does not show picture of complete molecule

CD4 (Homo sapiens)
   1cd4 2.3    monomer; N-terminal fragment
   
Cellobiohydrolase I (C terminal domain) (Trichoderma reesei)
   1cbh  NMR   monomer; averaged structure
   2cbh  NMR   41 structures; simulated annealing

Cellobiohydrolase II Core Protein (Trichoderma reesei)
   3cbh 2.0 CA dimer (a2) - 1 chain given

Che-Y (Salmonella typhimurium)
   2chy 2.7 CA monomer; mutant (S56C)

Chloramphenicol Acetyltransferase - Type III (Escherichia coli)
   1cla 2.34   trimer (a3) - 1 chain given; mutant (S148A)
   2cla 2.35   trimer (a3) - 1 chain given; mutant (D199N)
   3cla 1.75   trimer (a3) - 1 chain given; complex with chloramphenicol
   3claw       trimerized acc. to included matrices; checked on Iris

Chondroitin-4-Sulfate (Bos taurus)
   1c4s 3.0    NOT PROTEIN
   2c4s        complex; NOT PROTEIN
   
Chymosin B (Bos taurus)
   1cms 2.3    monomer; crystal packing as done by Insight doesn't look
               like crystal packing in literature -- I: molecules are
               back to back; L: molecules are front to back
   
Chymotrypsin Alpha (Bos taurus)
   same seq as gamma
   1cho 1.8    monomer + inhibitor (a + b) - 2 chains given; complex with 
               ovomucoid 3rd domain (inhibitor)
   2cha 2.0    monomer; tosylated; EXC codes for excised residues
   4cha 1.68   monomer - 2 chains given; EXC codes for excised residues
   5cha 1.67   "dimeric structural unit" - 2 chains given; same as for 4cha
   6cha 1.8    "dimeric structural unit" - 2 chains given; complex with PEBA
   
Chymotrypsin Gamma (Bos taurus)
   same seq as alpha
   2gch 1.9    monomer
   3gch 1.9    monomer; with cinnamate
   4gch 1.9    monomer; with cinnamate
   5gch 2.7    monomer; photolysis product of inhibited molecule
   6gch 2.1    monomer; with inhibitor APF
   7gch 1.8    monomer; with inhibitor LF
   
Chymotrypsin Inhibitor 2 (Hordeum vulgare, hiproly strain)
   2ci2 2.0    monomer
   
Chymotrypsinogen A (Bos taurus)
   1chg 2.5    monomer; alpha; zymogen
   2cga 1.8    monomer - 2 chains given; alpha; zymogen; extensive
               contacts between monomers
   2cgaw       half of coords eliminated; monomer remains
   
Citrate Synthase (Gallus gallus)
   3cts 1.7 UNKdimer (a2) - 1 chain given; complex with CO-A & citrate; 
               residues all UNK; 
   5cts 1.9    dimer (a2) - 1 chain given; complex with oxaloacetate & 
               CO-A; seq inferred from Sus scrofa (4cts); same form
               as 2cts, presumably monoclinic, closed
   5ctsw       made; checked on Iris; has protruding N-terminus in
               contact with neighboring dimer
   6cts 2.5    dimer (a2) - 1 chain given; complex with citrylthioether 
               & CO-A; seq as 5cts

Citrate Synthase (Sus scrofa)
   1cts 2.7    dimer (a2) - 1 chain given; complex with citrate
   2cts 2.0    dimer (a2) - 1 chain given; complex with CO-A & citrate;
               monoclinic form (closed)
   2ctsw       dimer made; checked on Iris; has protruding N-terminus in
               contact with neighboring dimer
   4cts 2.9    dimer (a2) - 2 chains given; complex with oxaloacetate & CO-A;
               tetragonal form (open)
   
Alpha Cobratoxin (Naja naja siamensis)
   related to Bungarotoxin
   1ctx 2.8    monomer
   
Concanavalin A (Canavalia ensiformis)
   1cn1 3.2    dimer (a2) - 2 chains given; demetallized
   2cna 2.0    dimer or tetramer (a2 or a4) - 1 chain given 
   2cnaw       made; checked
   3cna 2.4    dimer or tetramer (a2 or a4) - 1 chain given 
   
Crambin (Crambe abyssinica)
   1crn 1.5    monomer
   
Cro Repressor Protein (Phage lambda)
   1cro 2.2 CA 4 chains in data set (O,A,B,C); O-B thought to be 
					functional unit  
   
Crystallin Gamma II (Bos taurus)
   1gcr 1.6    monomer

Crystallin Gamma IV (Bos taurus)
   2gcr 2.3    monomer; but packs tightly in vivo under some conditions
   
Cucumber Basic Protein (Cucumis sativus)
   1cbp 2.5 CA    
   
C-AMP Dependent Protein Kinase (Bos primigenius Taurus)
   1apk ---    model of Type I - Domain A
   2apk ---    model of Type I - Domain A
   1bpk ---    model of Type I - Domain B
   2bpk ---    model of Type I - Domain B

Cytochrome B5 (Bos taurus)
   membrane binding tail removed
   2b5c 2.0    monomer; oxidized
   3b5c 1.5    monomer; oxidized; supersedes 2b5c
   
Cytochrome B562 (Escherichia coli)
   156b 2.5    monomer; oxidized
   256b 1.4    monomer - 2 chains given; oxidized; supersedes 156b
   256bw       made; checked
   
Cytochrome C (Katsuwonis pelamis, linnaeus or Thunnus alalunga)
   seq same in T. alalunga & K. pelamis; Thunnus acetylated at N terminus
   1cyc 2.3    monomer; ferro; Katsuwonis
   3cyt 1.8    dimer (a2) - 2 chains given; oxidized; Thunnus
   5cyt 1.5    monomer; reduced; Thunnus

Cytochrome C (Oryza sativa l.)
   1ccr 1.5    monomer
   
Cytochrome C - Isozyme 1 (Saccharomyces cerevisiae)
   1ycc 1.23   monomer?; reduced; one residue is actually trimethyllysine

Cytochrome C Peroxidase (Saccharomyces cerevisiae)
   2cyp 1.7    monomer
   1ccp 2.2    monomer; native + two N-terminal aa's from expression in E.coli;
               sequence differs from 2cyp at 2 aa's -- strain-related
   2ccp 2.2    monomer; D235N mutant of 1ccp
   3ccp 2.2    monomer; W191F mutant of 1ccp
   4ccp 2.2    monomer; W51F mutant of 1ccp
   
Cytochrome C Prime (Rhodospirillum molischianum)
   2ccy 1.67   dimer (a2) - 2 chains given
   
Cytochrome C2 (Rhodospirillum rubrum)
   2c2c 2.0    monomer; oxidized
   3c2c 1.68   monomer; reduced
   
Cytochrome C3 (Desulfovibrio desulfuricans Norway)
   1cy3 2.5    monomer
   
Cytochrome C3 (Desulfovibrio vulgaris miyazaki iam 12604)
   2cdv 1.8    monomer
   
Cytochrome C5 (Azotobacter vinelandii)
   1cc5 2.5    monomer
   
Cytochrome C550 (Paracoccus denitrificans)
   155c 2.5    monomer; some UNK residues at C terminus
   
Cytochrome C551 (Pseudomonas aeruginosa)
   351c 1.6    monomer; oxidized
   451c 1.6    monomer; reduced
   
Cytochrome P450CAM (Camphor Monooxygenase) (Pseudomonas putida)
   2cpp 1.63   monomer; with bound camphor
   3cpp 1.9    monomer; with reduced camphor & CO
   4cpp 2.11   monomer; with adamantane
   5cpp 2.08   monomer; with adamantane
   6cpp 1.9    monomer; with camphane
   7cpp 2.0    monomer; with norcamphor
   8cpp 2.1    monomer; with thiocamphor

Cytotoxic T-Lymphocyte Proteinase I (Mus musculus)
   2cp1 ---    non-experimental model
   
Deoxyribonucleic Acid (DNA)
   1ana 2.1    tetramer
   1bd1
   1bna
   1d10 
   1d11
   1d12 
   1d13
   1d14 
   1d15
   1d16 
   1d17 
   1d18 
   1d19 
   1d20 
   1d21 
   1d22 
   1dcg 
   1dn4 
   1dn5 
   1dn6 
   1dn7 
   1dn8 
   1dn9 
   1dne 
   1dnf 
   1dnh 
   1dnm 
   1dnn
   1dns
   1zna
   2ana
   2bna
   2dcg
   2dnd 2.2    complex with distamycin
   2zna
   3ana
   3bna
   3dnb
   3zna
   4bna
   4dnb
   5ana
   5bna

Dihydrofolate reductase (Escherichia coli)
   4dfr 1.7    monomer - 2 independent chains given; chain B 
               preferred for structural comparisons; resistant 
               strain; complex with methotrexate 
   4dfrw       half of coords eliminated; monomer remains
   5dfr 2.3    monomer; apo; resistant strain
   6dfr 2.4    monomer; complex with NADP+; resistant strain
   7dfr 2.5    monomer; complex with folate & NADP+; resistant strain

Dihydrofolate reductase (Gallus gallus)
   8dfr 1.7    monomer
   
Dihydrofolate reductase (Homo sapiens)
   1dhf 2.3    monomer - 2 chains given; complex with folate; chain B
               preferred
   1dhfw       chain B; half of coords eliminated; monomer remains
   2dhf 2.3    monomer; complex with 5-deazafolate
   
Dihydrofolate reductase (Lactobacillus casei)
   3dfr 1.7    monomer; complex with NADPH & methotrexate

DNA Polymerase I Klenow Fragment (Escherichia coli)
   1dpi 2.8 CA 

Eco R1 Endonuclease (Escherichia coli)
   1r1e 2.7 CA dimer (a2) - 1 chain given; complex with DNA

Eglin C (Hirudo medicinalis)
DUP1cse 1.2    monomer; complex with subtilisin; duplicate listing
DUP1tec 2.2    monomer; complex with thermitase; duplicate listing

Elastase, Human Neutrophil (Homo sapiens)
   1hne 1.84   monomer; complex with inhibitor - Methoxysuccinyl-Ala-
             Ala-Pro-Ala-Chloromethyl ketone
   
Elastase (Sus Scrofa)
   1est 2.5    monomer; tosyl
   2est 2.5    monomer; complex with trifluoro-L-lysyl-L-alanyl-
               P-trifluoromethyl-phenylanilide
   3est 1.65   monomer; native
   
Elongation Factor TU (Escherichia coli B)
   1efm 2.7 CA trypsin modified; excised residues labeled EXC
   1etu 2.9    monomer; domain I (part of molecule not included 
               in data set); complex with guanosine diphosphate; 
               excised residues labeled EXC
   
Enolase (2-Phospho-D-Glycerate Hydrolase) (Saccharomyces cerevisiae)
   2enl 2.25CA dimer (a2) - 1 chain given
   
Erabutoxin (Laticauda semifasciata)
   1nxb 1.38   monomer; "B"; differs from 5ebx by one residue; inverted pair -
               res 6 and 7 differ from 5ebx and 3ebx
   3ebx 1.4    monomer; B; differs from 5ebx by one residue
   5ebx 2.0    monomer; A; differs from 3ebx by one residue
   
Ferredoxin (Azotobacter vinelandii)
   4fd1 1.9    monomer; supersedes 3fd1
   1fd2 1.9    monomer; mutant C20A
   2fd2 1.9    monomer; mutant C24A
   
Ferredoxin (Bacillus thermoproteolyticus)
   1fxb 2.0    monomer
   2fxb 2.3    monomer; supersedes 1fxb
   
Ferredoxin (Peptococcus aerogenes)
   1fdx 2.0    monomer
   
Ferredoxin (Spirulina platensis)
   3fxc 2.5    monomer

Ferredoxin NADP+ Oxidoreductase (Spinacia oleracea)
   1fnr 2.2    monomer?
   2fnr 3.0    monomer?; complex with 2'phospho 5' AMP

FK506 Binding Protein (Homo sapiens)
   1fkf 1.7    monomer; complex with FK506 immunosuppressant
   
Flavocytochrome B2 (Saccharomyces cerevisiae)
   1fcb 2.4    dimer? - 2 chains given; looks better as tetramer

Flavodoxin (Clostridium MP)
   3fxn 1.9    monomer; oxidized form
   4fxn 1.8    monomer; semiquinone form
   
Flavodoxin (Desulfovibrio vulgaris)
   1fx1 2.0    monomer
   
D-Galactose/D-Glucose Binding Protein (Escherichia coli B/R)
   1gbp 3.0 CA all residues UNK
   2gbp 1.9    monomer complex with beta-D-glucose and Ca++
   3gbp 2.4    monomer complex with glucose and Ca++; supersedes 1gbp

Gene 5 DNA Binding Protein (Filamentous bacteriophage FD M13)
   2gn5 2.3    dimer (a2) - 1 chain given
   2gn5w       made; checked with Insight; structures same as lit
   
Glucagon (Sus scrofa)
   related to insulin and avian pancreatic peptide
   1gcn 3.0    trimer in crystal (a3) - 1 chain given; monomer in solution; 
               high temperature factors; presumed to be in crystaline
               configuration on the receptor
   1gcnw       made; checked
   
D-Glucose 6-Phosphate Isomerase (Sus scrofa)
   1pgi 3.5 CA dimer (a2) - 1 chain given; all residues UNK
   
Glutamine Synthase (Salmonella typhimurium)
   2gls 3.5    dodecamer (a12) - 12 chains given; includes Mn++ and water
   
Glutathione Peroxidase (Bos taurus)
   1gp1 2.0    tetramer (a4) - 2 chains given
   1gp1        matrix as given in Intl Tables doesn't work -- subunits too
               far apart; Insight's matrix doesn't work either -- there is
               some overlap in the top two subunits and the bottom two are
               too far apart -- the molecule is not compact as in the lit;
               modified matrices don't seem to work either.
   
Glutathione Reductase (Homo sapiens)
   3grs 1.54   dimer (a2) - 1 chain given; oxidized; supersedes 2grs; 
   3grsw       3grs.mtx; made; checked on Iris; Insight can't find
               space group B 2
   
D-Glyceraldehyde-3-Phosphate Dehydrogenase (Bacillus Stearothermophilus)
   1gd1 1.8    tetramer (a4) - 4 chains given; holo
   2gd1 2.5    tetramer (a4) - 4 chains given; apo
   
D-Glyceraldehyde-3-Phosphate Dehydrogenase (Homarus americanus)
   1gpd 2.9    tetramer (a4) - 2 chains given; complex with NAD & phosphates
   1gpdw       made
   4gpd 2.8    tetramer (a4) - 4 chains given; apo; supersedes 2gpd
   
D-Glyceraldehyde-3-Phosphate Dehydrogenase (Homo sapiens)
   3gpd 3.5    tetramer (a4) - 2 chains given; complex with NAD & phosphates;
   3gpdw       made; checked
   
Glycolate Oxidase (Spinacia oleracea)
   1gox 2.0    octamer (a8) or tetramer (a4) (equil.) - 1 chain given
   1goxw       made; checked

Gramicidin A (Bacillus brevis)
   1gma 0.86   dimer (a2) - 2 chains given; several amino acids are in D config
   
Hannuka Factor (Homo sapiens)
   1hf1 ---    model

Heat Shock Cognate Protein (Bos taurus)
   1hsc 2.2 CA N-terminal fragment

Hemagglutinin (Influenza virus, 1968 X.31 strain)
   bromelain digested (missing hydrophobic anchor)
   1hmg 3.0    trimer of dimers (3[ab]) - 6 chains given; G146D mutant
   2hmg 3.0    trimer of dimers (3[ab]) - 6 chains given; G146D mutant
   3hmg 2.9    trimer of dimers (3[ab]) - 6 chains given; L226Q mutant
   4hmg 3.0    trimer of dimers (3[ab]) - 6 chains given; L226Q mutant; 
               complex with sialic acid
   5hmg 3.2    trimer of dimers (3[ab]) - 6 chains given; D112G (HA2) mutant; 
               complex with sialic acid
  
Hemerythrin (Siphonosoma species)
   1hr3 5.5 CA trimer (a3?) - 3 chains given; all residues UNK
   
Hemerythrin (Themiste dyscritum)
   1hmq 2.0    octamer (a8) - 4 chains given; two chains each from two
               different octamers; met
   1hmqw       made; checked with Insight -- seems to be the same
               as the one it makes, but has big holes; checked both ways;
               re-ordered literature
   1hmz 2.0    octamer (a8) - 4 chains given; azidomet
   
Hemerythrin B (Phascolopsis gouldii)
   1hrb 5.5 CA monomer
   
Hemoglobin (Equus caballus)
   2dhb 2.8    tetramer (a2b2) - 2 chains given; deoxy; supersedes 1dhb
   2dhbw       made; checked; looks ok on Iris, but Insight can't make 
					similar molecule
   2mhb 2.0    tetramer (a2b2) - 2 chains given; aquo met
   
Hemoglobin (Homo sapiens)
   1coh 2.9    tetramer (a2b2) - 4 chains given; alpha-ferrous-carbonmonoxy; 
               beta-cobaltous-deoxy; T state
   1hco 2.7    tetramer (a2b2) - 2 chains given; carbonmonoxy
   2hco 2.7    tetramer (a2b2) - 2 chains given; carbonmonoxy; energy minimized 
   2hhb 1.74   tetramer (a2b2) - 4 chains given; deoxy; "best estimate of 
               coordinates"
   3hhb 1.74   tetramer (a2b2) - 2 chains given; deoxy; "symmetry averaged"
   4hhb 1.74   tetramer (a2b2) - 4 chains given; deoxy; "unrestrained 
               refinement"
   1hho 2.1    tetramer (a2b2) - 2 chains given; A; oxy
   
Hemoglobin F (Fetal) (Homo sapiens)
   39/146 residues of subunit G are different from subunit B of H. sapiens 
   adult; other subunit is the same
   1fdh 2.5    tetramer (a2b2) - 2 chains given; deoxy
   1fdhw       made; checked
   
Hemoglobin S (Sickle Cell) (Homo sapiens)
   1hbs 3.0    tetramer (a2b2) - 8 chains given; deoxy; differs from 
               Hemoglobin A by one residue; would be useful to include 
               region around point mutation in predictions
   1hbsw       half of records eliminated; only need 4 subunits, not 8
   
Hemoglobin S (Sickle Cell) (Odocoileus virginianus)
   1hds 1.98   tetramer (a2b2) - 4 chains given
  
Hemoglobin (Scapharca inaequivalvis)
   1sdh 2.4    dimer - 2 chains given; carbonmonoxy
   2sdh 2.4    dimer - 2 chains given; deoxy

Hemoglobin III (Erythrocruorin) (Chironomous Thummi Thummi)
   1eca 1.4    monomer; aquo met
   1ecd 1.4    monomer; deoxy
   1ecn 1.4    monomer; cyano met
   1eco 1.4    monomer; carbon monoxy
   
Hemoglobin V (Petromyzon marinus)
   2lhb 2.0    monomer or dimer - 1 chain given; cyano, met; hydrogen atoms 
               added by computer
   
Hexokinase A (Saccharomyces cerevisiae)
   1hkg 3.5    monomer; complex with glucose; many UNK residues
   
Hexokinase B (Saccharomyces cerevisiae)
   2yhx 2.1    probably multimer - 1 chain given; complex with 
               orthotoluoylglucosamine; many residues UNK
   
High Potential Iron Protein (HIPIP) (Chromatium vinosum, strain D)
   1hip 2.0    monomer
   
Hirudin (Hirudo medicinalis)
   2hir  NMR   monomer; wt; multiple solutions
   4hir  NMR   monomer; K47E mutant; multiple solutions
   5hir  NMR   monomer; energy-minimized average structure
   6hir  NMR   monomer; K47E mutant; energy-minimized average structure
   
HIV-1 Protease (HIV I)
   1hvp ---    model; complex with substrate; non-experimental
   2hvp 3.0 CA dimer (a2) - 1 chain given
   3hvp 2.8    dimer (a2) - 1 chain given; 2 Cys residues replaced by ABA
   3hvpw       made; looks ok
   4hvp 2.3    dimer (a2) - 2 chains given; complex with inhibitor; 2 Cys 
               residues replaced by ABA
   
Human Class I Histocompatibility Antigen A2 (Homo sapiens)
   1hla 3.5 CA dimer (ab) - 2 chains given
   
Human Class I Histocompatibility Antigen A2.1 (Homo sapiens)
   3hla 2.6    dimer (ab) - 2 chains given
   
Human Class I Histocompatibility Antigen AW 68.1 (Homo sapiens)
   membrane anchor cleaved off with papain
   2hla 2.6    dimer (ab) - 2 chains given
   
Hyaluronic Acid (synthetic & Homo sapiens)
   1hya 3.0    NOT PROTEIN
   2hya 3.0    NOT PROTEIN
   3hya 3.0    NOT PROTEIN
   4hya 3.0    NOT PROTEIN

P-Hydroxybenzoate Hydroxylase (Pseudomonas fluorescens)
   1phh 2.3    dimer (a2) - 1 chain given; complex with FAD & DHB
   1phhw       made; no picture of dimer in lit, but same as one of
               molecules made by Insight
   2phh 2.7    dimer (a2) - 1 chain given; complex with PHBH & ADPR
   
Immunoglobulin IgA Fab Fragment Hy/Hel-10 (Mus musculus)
   1hfm ---    non-experimental
   2hfm ---    non-experimental
   
Immumoglobulin IgA FV Fragment Anti-Alpha1->6 Dextran 19.1.2 (Mus musculus)
   1fvb ---    non-experimental
   2fvb ---    non-experimental; energy minimized model
   
Immunoglobulin IgA FV Fragment Anti-Alpha 1->6 Dextran W3129 (Mus musculus)
   1fvw ---    non-experimental
   2fvw ---    non-experimental; energy minimized model
   
Immunoglobulin IgA(Kappa) Fab Fragment McPC603 (Mus musculus)
   1mcp 2.7    H & L chains; Insight makes a trimer of dimers, which looks
               like the basic crystallographic unit; re-ordered literature
   2mcp 3.1    H & L chains; complex with phosphocholine
   
Immunoglobulin IgA(Kappa) Fab Fragment J539 (Mus musculus)
   1fbj 2.6    H & L chains
   2fbj 1.95   H & L chains; supersedes 1fbj
   
Immunoglobulin IgG1 Fab Fragment (Homo sapiens)
   2fb4 1.9    H & L chains; H chain is truncated from 2ig2; some very
               close crystal contacts
   2ig2 3.0    H & L chains; some of sequence & conformation is taken from 1fc1
   
Immunoglobulin IgG1(Kappa) Fab Fragment Hy/Hel-10 (Mus musculus & Gallus gallus)
   3hfm 3.0    three chains (abx) - 2 Fab & lysozyme; similar to 2hfl, 
               not identical
   
Immunoglobulin IgG1 Fab Fragment Hy/Hel-5 (Mus musculus)
   2hfl 2.54   three chains (abx) - 2 Fab & lysozyme
   
Immunoglobulin IgG2a(Kappa) Fab Fragment (Mus musculus)
   4fab 2.7    H & L chains; complex with fluorescein (antigen)

Immunoglobulin IgG2b(Kappa) Fab R19.9 (Mus musculus)
   1f19 2.8    H & L chains; similar to 3hfm
   
Immunoglobulin IgG(Lambda) Fab New (Homo sapiens)
   3fab 2.0    H & L chains; similar to 3hfm

Immunoglobulin Fab Heterologous Light Chain Dimer (Homo sapiens)
   1mcw 3.5    dimer (ab) - 2 chains given; hybrid of Weir (H analog) & 
               MCG (L analog); chimera
   
Immunoglobulin Fab Bence/Jones Protein (Homo sapiens)
   2rhe 1.6    dimer (a2) - 1 chain given; lambda; variable domain
   2rhew       made; checked
   
Immunoglobulin Lambda Light Chain Dimer (Homo sapiens)
   1mcg 2.3 CA dimer (a2) - 2 chains given
   2mcg 2.0    dimer (a2) - 2 chains given; trigonal form (deionized water); 
               supersedes 1mcg
   3mcg 2.0    dimer (a2) - 2 chains given; orthorhombic form (ammonium 
               sulfate - high salt)
   
Immunoglobulin IgG(Kappa) Fab Bence/Jones REI (Homo sapiens)
   1rei 2.0    dimer (a2) - 2 chains given; variable portion of protein
   
Immunoglobulin IgG1 Fc Fragment (Homo sapiens)
   1fc1 2.9    dimer (a2) - 2 chains given (a2)
   1fc2 2.8    dimer (a2) - 2 chains given (a + s); half of Ig given; 
               complex with Fragment B of Protein A
   1fc2w       dimerized acc to included matrix; checked; missing piece 
               is due to assymetry of protein fragment; original lit checked; 
               protein fragment at elbow in chains
   
Immunoglobulin IgG1 pFc' Fragment (Cavia porcellus)
   1pfc 3.125  dimer (a2) - 1 chain given
   1pfcw       made; checked
   
Immunoglobulin IgE Fc' Fragment (Homo sapiens)
   1ige ---    model; should NOT be used
   
Insulin (Bos taurus)
   Insulin is produced & stored as a hexamer of dimers, but it is 
   active as a dimer.  Subunit B is the same as S. scrofa.
   2ins 2.5    dodecamer (6ab) - 4 chains given; Des-Phe B1
   
Insulin (Sus scrofa)
   Insulin is produced & stored as a hexamer of dimers, but it is 
   active as a dimer.  Subunit B is the same as B. taurus.
   1ins 1.5    dodecamer (6ab) - 4 chains given
   3ins 1.5    dodecamer - 4 chains given; joint x-ray & neutron scattering; 
               2-Zn; has hydrogens
   4ins 1.5    dodecamer - 4 chains given; supersedes 1ins
   
Insulin-like Growth Factor (Somatomedin) (Homo sapiens)
   1gf1 ---    I; non-experimental; should NOT be used
   1gf2 ---    II; non-experimental; should NOT be used

Interleukin-1 Beta (Homo sapiens)
   different structures done by different groups
   1i1b 2.0    monomer
   2i1b 2.0    monomer
   4i1b 2.0    monomer

Interleukin-8 Beta (Homo sapiens)
   1il8 NMR    dimer; energy minimized average structure
   2il8 NMR    dimer; 41 simulated annealing structures

Iota Carrageenan (Rhodophycae)
   1car 3.0    polysaccharide; NOT PROTEIN
   
Isocitrate Dehydrogenase (Escherichia coli)
   3icd 2.5    dimer - 1 chain given
   3icdw       made; checked
   4icd 2.5    dimer - 1 chain given; phosphorylated

Kallikrein A (Sus scrofa)
   related to tonin
   2kai 2.5    complex with BPTI; chain cleaved - separate identifiers
   2pka 2.05   chain cleaved - separate identifiers; 4 chains given;
               2 chains should be removed before processing
   2pkaw       half of coords eliminated; monomer remains; checked

Keratan Sulfate (Bos taurus)
   1kes 3.0    polysaccharide; NOT PROTEIN
   
   2-Keto-3-Deoxy-6-Phosphogluconate Aldolase (Pseudomona putida)
   1kga 3.5 CA trimer - 1 chain given; all residues UNK
   
L7/L12 50S Ribosomal Protein - C Terminal Domain (Escherichia coli, MRE 600)
   1ctf 1.7    "monomer" - whole protein is a dimer, but N terminus
               is thought to be required; fragment of protein
   
Alpha Lactalbumin (Papio cynocephalus)
   1alc 1.7    monomer; sequence deduced from x-ray
   
Beta Lactamase (Bacillus lichenformis 749/C)
   2blm 2.0 CA monomer; 2 chains given
  
Beta Lactamase (Staphylococcus aureus pc1)
   1blm 2.5 CA
   3blm 2.0    monomer?; supersedes 1blm; check lit
  
***********************************************************
All lactate dehydrogenases are probably tetramers, but they
seem to crystallize in unusual space groups, or else they
don't follow the crystallographic symmetry.I can't get
Insight to make a molecule that seems reasonable to me.
***********************************************************

L-Lactate Dehydrogenase (Bacillus stearothermophilus)
   1ldb 2.8    tetramer (a4) - 1 chain given; apo
   1ldbw       made from matrices given; checked; no picture in lit
               of tetramer
   2ldb 3.0    tetramer (a4) - 1 chain given; complex with NAD & F1,6P
   
L-Lactate Dehydrogenase (Lactobacillus casei)
   1llc 3.0    tetramer (a4) - 1 chain given; complex with CO2 & F1,6P
   1llcw       made from matrices given; checked; no picture from
               original lit - difficulty getting literature cited
   
Lactate Dehydrogenase (Mus musculus)
   2ldx 2.96   tetramer (a4) - 1 chain given; isoenzyme C4; apo; supersedes 1ldx
   2ldxw       made; looks ok on screen, but doesn't look like lit
   
Lactate Dehydrogenase (Squallus acanthias)
   3ldh 3.0    tetramer (a4) - 1 chain given; M4; complex with NAD & pyruvate
   6ldh 2.0    tetramer (a4) - 1 chain given; M4; apo 
   6ldhw       made; looks different from 1llc; I checked this by changing 
					the non-standard space group F 4 2 2 to I 4 2 2, which uses 
					the right-handed coordinate system.  Four of the replicates 
					used by Insight to create the tetramer are the same as those 
					mentioned in the MTRIX records.
   8ldh 2.8    tetramer (a4) - 1 chain given; M4; apo; complex with citrate
   1ldm 2.1    tetramer (a4) - 1 chain given; M4; complex with NAD & oxamate
   
Lactate Dehydrogenase (Sus scrofa)
   5ldh 2.7    tetramer (a4) - 1 chain given; H4; complex with NAD & S-Lac
   
Lambda Repressor (Phage lambda)
   1lrd 2.5    dimer (a2) - 2 chains given + dsDNA; repressor-operator complex
   1lrp 3.2 CA dimer (a2) - 1 chain given; N-terminal domain

Lectin (Pisum sativum)
   2ltn 1.7    tetramer (a2b2) - 4 chains given
   
Leghemoglobin (Lupinus luteus l)
   For these entries, the 1s & 2s of a pair were refined in diff. manners.
   1lh1 2.0    monomer; acetate, met
   2lh1 2.0    monomer; acetate, met
   1lh2 2.0    monomer; aquo, met
   2lh2 2.0    monomer; aquo, met
   1lh3 2.0    monomer; cyano, met
   2lh3 2.0    monomer; cyano, met
   1lh4 2.0    monomer; deoxy
   2lh4 2.0    monomer; deoxy
   1lh5 2.0    monomer; fluoro, met
   2lh5 2.0    monomer; fluoro, met
   1lh6 2.0    monomer; nicotinate, met
   2lh6 2.0    monomer; nicotinate, met
   1lh7 2.0    monomer; nitrosobenzene
   2lh7 2.0    monomer; nitrosobenzene

Leucine Binding Protein (Escherichia coli, strain K12)
   2lbp 2.4    monomer; similar to 2liv
   
Leucine/Isoleucine/Valine Binding Protein (Escherichia coli)
   2liv 2.4    monomer; similar to 2lbp
   
Lysozyme (Gallus Gallus)
   1lym 2.5    monomer - 2 chains given
   2lym 2.0    monomer; 1 atm; 1.4 M NaCl
   3lym 2.0    monomer; 1000 atm; 1.4 M NaCl
   1lyz 2.0    monomer; unrefined coordinates
   2lyz 2.0    monomer; after refinement 1
   3lyz 2.0    monomer; different refinement
   4lyz 2.0    monomer; different refinement
   5lyz 2.0    monomer; different refinement
   6lyz 2.0    monomer; different refinement
   7lyz 2.5    monomer; triclinic
   8lyz 2.5    monomer; iodine inactivated
   9lyz 2.5    substrate only
   1lzh 6.0 CA monoclinic
   2lzh 6.0 CA orthorhombic
   1lzt 1.97   monomer; diff refinement from 2lzt
   2lzt 1.97   monomer; diff refinement from 1lzt 
   
Lysozyme (Homo sapiens)
   1lz1 1.5    monomer
   
Lysozyme (Meleagris gallopavo)
   1lz2 2.8 CA similar to Gallus, but not identical
   2lz2 2.2    monomer; difficulty obtaining original literature
   
Lysozyme (Phage T4 in Escherichia coli)
   1lyd 2.0    monomer; synthetic coding
   2lzm 1.7    monomer; supersedes 1lzm
   3lzm 1.7    monomer; same as 2lzm, but better refinement
               use as basis for comparison of 1lxx mutants
   1l01 - 1l35 mutants of T4 lysozyme
   
Cytoplasmic Malate Dehydrogenase (Sus scrofa)
   4mdh 2.5    dimer (a2) - 2 chains given; supersedes 2mdh
   
Melittin (Apis mellifera)
   1mlt 2.0    tetramer (a4) - 2 chains given
   2mlt 2.0    tetramer (a4) - 2 chains given; supersedes 1mlt
   2mltw       made; Insight (not Intl Tables) matrix; checked; looks ok
   
Mengo Encephalomyocarditis Virus Coat Protein (Mengo virus)
   2mev 3.0    240mer - 4 chains given; supersedes 1mev

CD-7 Metallothionein-2 (Homo sapiens)
   Alpha:  one residue differs from Oryctolagus; 2 from Rattus
   Beta:  several differences
   1mhu NMR    alpha domain; 31 residues long
   2mhu NMR    beta domain; 30 residues long

CD-7 Metallothionein-2 (Oryctolagus cuniculus)
   Alpha:  one residue differs from Homo sapiens; 2 from Rattus
   Beta:  several differences
   1mrb NMR    alpha domain; 31 residues long
   2mrb NMR    beta domain; 30 residues long

CD-7 Metallothionein-2 (Rattus rattus)
   Alpha:  two residues differ each from Homo sapiens and from Oryctolagus.
   Beta:  several differences
   1mrt NMR    alpha domain; 31 residues long
   2mrt NMR    beta domain; 30 residues long

Monellin (Dioscoreophyllum cumminsii Diels)
   1mon 2.75 CA heterodimer - 8 chains given

Muconolactone Isomerase (Pseudomonas putida)
   1mli 3.3 CA decamer - 1 chain given
   
Murein Lipoproten (Escherichia coli)
   mmlp ---    non-experimental
   
Myoglobin (Aplysia limacina)
   1mba 1.6    monomer; met
   2mba 2.0    monomer; azide
   3mba 2.0    monomer; fluoride
   4mba 2.0    monomer; imidazole
   
Myoglobin (Phoca vitulina)
   1mbs 2.5    monomer; similar to Physeter; Insight can't match space
               group A 2
   
Myoglobin (Physeter catodon)
   1mb5 1.8    monomer; carbonmonoxy; neutron study; has hydrogens
   1mbc 1.5    monomer; FeII; carbonmonoxy; 260K
   1mbd 1.4    monomer; deoxy; pH 8.4
   1mbn 2.0    monomer; ferric; met
   4mbn 2.0    monomer; met; supersedes 2mbn
   5mbn 2.0    monomer; deoxy; supersedes 3mbn
   1mbo 1.6    monomer; oxy; pH 8.4
   1mbw 1.9    monomer; met; X0M & D122N mutant
   
Myoglobin (Sus scrofa)
   1pmb 2.5    monomer - 2 chains given; aquo met
   1pmbw       half of coords eliminated; monomer remains
   
Myohemerythrin (Themiste zostericola)
   2mhr 1.7/1.3 monomer; has hydrogens

Oncomodulin (Rattus norvegicus)
   1omd 1.85   monomer? 
   
Ovomucoid Third Domain (Coturnix coturnix japonica)
   similar to Lophura, but not identical
   1ovo 1.9    monomer, but crystallographically an octamer (a8) - 4 
               chains given; part of protein
   1ovow       made; checked -- It really looks like two tetramers -
               ABGH and CDEF.  N.B. C and D in the 1ovow file are NOT 
               the same CD as in the 1ovo file!!
   
Ovomucoid Third Domain (Lophura nycthemera)
   similar to Coturnix, but not identical
   2ovo 1.5    monomer - 1 chain given; part of protein
   
1-Beta-Mercaptopropionate Oxytocin (synthetic)
   1xy1 1.04   monomer - 2 chains given; 8 residues; wet form; has H's
   1xy2 1.20   monomer - 2 chains given; 8 residues; dry form; has H's
   
Avian Pancreatic Polypeptide (Meleagris gallopavo)
   related to insulin and glucagon
   1ppt 1.37   dimer (a2) - 1 chain given
   1pptw       made; checked; ok

Papain (Carica papaya)
   1pad 2.8    monomer; derivative of C25; based on 8pap
   2pad 2.8    monomer; derivative of C25; based on 8pap; supersedes 3pap
   4pad 2.8    monomer; derivative; based on 8pap; supersedes 5pap
   5pad 2.8    monomer; derivative; based on 8pap; supersedes 6pap
   6pad 2.8    monomer; derivative; based on 8pap; supersedes 7pap
   9pap 1.65   monomer; supersedes 8pap; Cys-25 oxidized
   1ppd 2.0    monomer; 2-Hydroxyethylthiopapain; C25 inhibited
   
Pepsin (Sus scrofa)
   Sequence is the same as pepsinogen, minus the leader peptide.
   3pep 2.3    monomer
   4pep 1.8    monomer; supersedes 1pep
   5pep 2.34   monomer; supersedes 2pep
   
Pepsinogen (Sus scrofa)
   Sequence is the same as pepsin, plus the leader peptide.
   1psg 1.65   monomer; propeptide residues labelled 1P - 44P; may be dimer
               in crystal; difficulty obtaining original literature

Phaseolin (Phaseolus vulgaris)
   1phs 3.0 CA dodecamer? - 3 chains given; crystallizes as tetramer of trimers
   
Phosphofructokinase (Bacillus stearothermophilus)
   3pfk 2.4    tetramer (a4) - 1 chain given; unliganded
   3pfkw       made; checked; looks ok
   4pfk 2.4    tetramer (a4) - 1 chain given; complex with F6P and ADP/Mg++
   5pfk 7.0 CA complex with inhibitor
   
Phosphofructokinase (Escherichia coli)
   1pfk 2.4    tetramer (a4) - 2 chains given; complex with F1,6P and ADP/Mg++
   2pfk 2.4    tetramer (a4) - 4 chains given, but 2 are part of one 
               tetramer & the other two are part of another; unliganded
   2pfkw       made; checked
   
Phosphoglycerate Kinase (Equus caballus)
   2pgk 3.0    all residues UNK
   
Phosphoglycerate Kinase (Saccharomyces cerevisiae)
   3pgk 2.5    monomer; complex with ATP, Mg++, and 3-Phosphoglycerate;
               some crystal contacts are very close; contacts between
               molecules are as close as contacts between domains
   
Phosphoglycerate Mutase (Saccharomyces cerevisiae)
   3pgm 2.8    tetramer (a4) - 1 chain given
   3pgmw       made; checked
   
Phospholipase A2 (Bos taurus l.)   
   1bp2 1.7    monomer
   3bp2 2.1    transaminated
   
Pro-Phospholipase A2 (Bos taurus l.)   
   2bp2 3.0    monomer; zymogen, with 7 res leader; coordinates for the
               leader peptide are not included
   
Phospholipase A2 (Crotalus atrox)
   1pp2 2.5    dimer (a2) - 2 chains given
   
Phospholipase A2 (Sus Scrofa)
   1p2p 2.6    monomer
   3p2p 2.1    mutant; surface loop deleted
   
Photoactive Yellow Protein (Ectothiorhodospira halophila)
   1phy 2.4 CA
   
Photosynthetic Reaction Center (Rhodopseudomonas viridis)
   1prc 2.3    tetramer (abcd) - 4 chains given; membrane protein - 
               solvent accessibility info will need to be re-interpreted
   
Plastocyanin (Populus nigra variant italica)
   1pcy 1.6    monomer; Cu++; pH 6.0
   2pcy 1.8    monomer; apo; pH 6.0
   3pcy 1.9    monomer; Hg++
   4pcy 2.15   monomer; crosslinked
   5pcy 1.80   monomer; Cu+; pH 7.0
   6pcy 1.90   monomer; Cu+; pH 3.8
   
Plastocyanin (Enteromorpha prolifera)
   7pcy 1.8    monomer; hydrogens included
   
Poliovirus, Type I, Mahoney Strain (Homo sapiens)
   2plv 2.88   240mer - 4 chains given
   
Prealbumin (Homo sapiens)
   2pab 1.8    tetramer (a4) - 2 chains given
   2pabw       made acc. to file; checked

Proteinase A (Streptomyces griseus, strain K1)
   2sga 1.5    monomer; sequence numbered as chymotrypsinogen - gaps;
               lots of crystal contacts; phe sticking out; see MD paper
               by Avbelj et al., Biochemistry 29 (1990)
   1sgc 1.8    complex with chymostatin; seq numbers as for 2sga
   
Proteinase B (Streptomyces griseus, strain K1)
   3sgb 1.8    monomer; complex with ovomucoid inhibitor; numbering has gaps
   4sgb 2.1    monomer; complex with potato inhibitor; inhibitor is 51 
               res long -- could be used, too
   
Proteinase K (Tritirachium album limber)
   2prk 1.5    monomer; pseudodimer in crystal

Proteinase Inhibitor IIA (Bos taurus)
   1bus NMR    monomer - 5 chains given
   2bus NMR    monomer - 1 chain given -- energy minimized structure

Pseudoazurin (Alcaligenes faecalis, strain S-6)
   1paz 1.55   monomer; oxidized Cu++ at pH 6.8
   2paz 2.0    monomer
   
Inorganic Pyrophosphatase (Saccharomyces cerevisiae)
   1pyp 3.0    dimer (a2) - 1 chain given
   1pypw       dimerized acc to included matrix; looks ok; diff from
               dimer Insight makes -- non-crystallographic symmetry
   
Pyruvate Kinase (Felis domestica)
   1pyk 2.6 CA all residues UNK
   
C-H-RAS P21 Protein Catalytic Domain (Homo sapiens)
   2p21 2.2 CA
   3p21 2.2 CA mutant (G12V)
   
Rat Mast Cell Protease II (Rattus rattus)
   3rp2 1.9    monomer - 2 chains given; residue numbering based on 
               chymotrypsin -> gaps;
   3rp2w       made; checked
   
Relaxin (Sus scrofa)
   1rlx ---    non-experimental; based on insulin
   2rlx ---    non-experimental
   3rlx ---    non-experimental
   4rlx ---    non-experimental
  
Retinol Binding Protein (Homo sapiens)
   1rbp 2.0    monomer?

Rhinovirus 14 Coat Protein (Homo sapiens)
   Icosohedral - 240mer; 4 chains given = 1 unit of icosohedron
   1r08 3.0    complex with antiviral agent
   1rmu 3.0    mutant of 1r08; otherwise same
   2r04 3.0    supersedes 1r04; complex with antiviral agent (WIN IV);
   2r06 3.0    supersedes 1r06; complex with antiviral agent (WIN VI);
   2r07 3.0    supersedes 1r07; complex with antiviral agent (WIN VII);
   2rm2 3.0    supersedes 1rm2; complex with antiviral agent (WIN II);
   2rmu 3.0    mutant (V188L in chain 1); icosohedral; 
   2rr1 3.0    supersedes 1rr1; complex with antiviral agent (WIN I[R]) 
   2rs1 3.0    supersedes 1rs1; complex with antiviral agent (WIN I[S]);
   2rs3 3.0    supersedes 1rs3; complex with antiviral agent (WIN III[S]);
   2rs5 3.0    supersedes 1rs5; complex with antiviral agent (WIN V[S]);
   4rhv 3.0    

Rhinovirus Serotype 1A Coat Protein (Homo sapiens)
   Icosohedral - 240mer; 4 chains given = 1 unit of icosohedron
   1r1a 3.2    
   
Rhodanese (Bos taurus)
   1rhd 2.5    monomer
   
Ribonuclease A (Bos taurus)
   1rbb 2.5    B; 2 identical chains given
   1rn3 1.45   monomer
   1rns 2.0    S; single chain of 1rn3 split into 2 chains
   5rsa 2.0    monomer; joint x-ray & neutron - contains hydrogens
   6rsa 2.0    monomer; complex with uridine vanadate; joint x-ray & neutron
   7rsa 1.26   monomer; phosphate-free; joint x-ray & neutron
   1rsm 2.0    monomer; cross-linked
   1srn 1.8    dimer - 2 chains given; semi-synthethic - chains are
               portions of RNase A
   
Ribonuclease T1 (Aspergillus oryzae)
   1rnt 1.9    monomer; complex with 2'guanylic acid 
   2rnt 1.8    monomer; complex with guanyl-2'6'-guanosine 
   3rnt 1.8    monomer; complex with vanadate
   
Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase (RUBISCO) 
(Rhodospirillum rubrum)
   2rub 1.7 CA dimer - 2 chains given
   
Rous Sarcoma Virus Protease (Rous Sarcoma virus, strain PR-C)
   2rsp 2.0    dimer (a2) - 2 chains given

Rubredoxin (Clostridium pasteurianum)
   4rxn 1.2    monomer; oxidized; unconstrained; supersedes 2rxn
   5rxn 1.2    monomer; oxidized; constrained; supersedes 2rxn
   
Rubredoxin (Desulfovibrio desulfuricans, strain 27774)
   6rxn 1.5    monomer
   
Rubredoxin (Desulfovibrio gigas)
   1rdg 1.4    monomer; oxidized
   
Rubredoxin (Desulfovibrio vulgaris)
   3rxn 1.5    monomer
   7rxn 1.5    monomer; supersedes 3rxn; Fe+++ and sulfate
   
Sarcoplasmic Calcium-Binding Protein (Nereis diversicolor)
   1scp 3.0 CA monomer - 2 chains given

Satellite Tobacco Necrosis Virus (STNV)
   2stv 2.5    60mer - 1 chain given
   
Scorpion Neurotoxin Variant 3 (Centruroides sculpturatus Ewing)
   1sn3 1.8    monomer
  
Southern Bean Mosaic Virus Coat Protein (SBMV)
   4sbv 2.8    540mer - 3 chains given; supersedes 3sbv

Staphylococcyl Nuclease (Staphylococcus aureus)
   1snc 1.65   monomer; complex with Ca++ & inhibitor
   1snm 1.74   monomer; E43D mutant; complex with Ca++ & deoxythymidine
               3'5'bisphosphate
   2sns 1.5    monomer; complex with 2'deoxy 3'5' diphosphothymidine;

Streptomyces Subtilisin Inhibitor (Streptomyces albogriseolus, S-3253)
   2ssi 2.6    dimer (a2) - 1 chain given; supersedes 1ssi
   2ssiw       made; checked
   
Subtilisin BPN (Novo) (Bacillus amyloliquefaciens)
   sequence very similar to Subtilisin Carlsberg
   1sbt 2.5    monomer
   2sbt 2.8    monomer
   1sic 2.0 CA BPN'; complex with inhibitor; inhibitor is a dimer & 
               binds 2 subtilisins - 1 chain of each given 
   1st2 2.0    BPN'; peroxide inactivated (Mets oxidized)
   2st1 1.8    BPN'
   1s01 1.7    monomer; mutant (M50F, N76D, G169A, Q206C, Y217K, & 
               N218S); residue 206 may be persulfide
   2sni 2.1    complex with chymotrypsin inhibitor (Hordeum vulgare)
   
Subtilisin Carlsberg (Bacillus subtilis)
   sequence very similar to Subtilisin BPN (Novo)
   1cse 1.2    monomer; complex with Eglin-C (Hirudo medicinalis)
   1sbc 2.5    monomer
   2sec 1.8    complex with N-Acetyl-Eglin-C (Hirudo medicinalis)
  
Cu, Zn Superoxide Dismutase (Bos taurus)
   2sod 2.0    dimer (a2) - 4 chains given 
   2sodw       made; checked

Taka-Amylase A (Aspergillus oryzae)
   2taa 3.0    monomer - 1 chain given

Tendamistat (Streptomyces tendae)
   2ait  NMR   monomer - 9 chains given; with hydrogens and hydrogen 
               pseudoatoms; this file messes up in Insight
   3ait  NMR   energy minimized model using AMBER
   4ait  NMR   energy minimized model using FANTOM
   
Thaumatin I (Thaumatococcus danielli Benth)
   1thi 3.2 CA monomer
   
Thermitase (Thermoactinomyces vulgaris)
   homologous to Subtilisin
   1tec 2.2    monomer; complex with Eglin C (Hirudo medicinalis) (inhibitor)
   
Thermolysin (Bacillus thermoproteolyticus)
   3tln 1.6    monomer; supersedes 1tln & 2tln
   4tln 2.3    monomer; complex with Leu-Hydroxylamine
   5tln 2.3    monomer; complex with inhibitor
   7tln 2.3    monomer; complex with inhibitor; supersedes 6tln
   1tlp 2.3    monomer; complex with phosphoramidon 
   1tmn 1.9    monomer; complex with inhibitor
   2tmn 1.6    monomer; complex with P-Leu
   3tmn 1.7    monomer; complex with Val-Trp
   4tmn 1.7    monomer; complex with CBZ-PHE-P-LEU-ALA
   5tmn 1.6    monomer; complex with CBZ-PGL-LEU-LEU
   6tmn 1.6    monomer; complex with CBZ-PGL-OLE-LEU
   7tmn ---    model of substrate GLY-TPH-LEU-LEU
   
Thioredoxin (Escherichia coli B)
   1srx 2.8 CA oxidized
   1trx NMR    monomer - 10 chains given; reduced

Thymidine Phosphorylase (Escherichia coli K12)
   1tpt 2.8 CA dimer - 1 chain given

Tobacco Mosaic Virus (TMV vulgare strain)
   2tmv 2.9    2130mer - 1 chain given; complex with RNA

Tomato Bushy Stunt Virus (TBSV)
   2tbv 2.9    180mer - 3 chains given

Tonin (Rattus rattus)
   related to Kallikrein
   1ton 1.8    monomer
   
Transfer RNAs
   1tn1
   1tn2
   1tra
   2tra
   3tra
   4tra
   4tna

Triacylglycerol Acylhydrolase (Mucor miehei)
   1tgl 1.9 CA monomer
   
Triose Phosphate Isomerase (Gallus gallus)
   1tim 2.5    dimer (a2) - 2 chains given
   
Triose Phosphate Isomerase (Saccharomyces cerevisiae)
   2ypi 2.5    dimer - 2 chains given; complex with PGA
   
Tropomyosin (Oryctolagus cuniculus)
   2tma 15.0 CA 
   
Troponin (Oryctolagus cuniculus)
   1tnc ---    non-experimental; based on parvalbumin
   
Troponin C (Gallus gallus)
   Sequence similar to M. gallopavo (5 residues differ)
   4tnc 2.0    monomer
   
Troponin C (Meleagris gallopavo)
   Sequence similar to G. gallus (5 residues differ)
   5tnc 2.0    monomer; supersedes 2tnc
   
Trypsin Beta (Bos taurus)
   1ntp 1.8    monomer; modified; monoisopropylphosphoryl inhibited; 
               neutron data
   1tld 1.5    monomer; beta; pH 5.3
   1tpa 1.9    monomer; anhydro; complex with inhibitor
   1tpo 1.7    monomer; beta; pH 5.0
   1tpp 1.4    monomer; complex with APPA
   2ptc 1.9    monomer; complex with PTI; supersedes 1ptc
   2ptn 1.55   monomer; orthorhombic crystal; supersedes 1ptn; 2.4 M
               ammonium sulfate
   3ptb 1.7    monomer; benzamidine inhibited; pH 7; supersedes 2ptb
   3ptn 1.7    monomer; trigonal; 2.4 M ammonium sulfate 
   4ptp 1.34   monomer; diisopropylphosphoryl inhibited

Trypsin (Rattus rattus)
   1trm 2.3    monomer; 2 chains given; mutant (D102N); B chain more 
               like native
   1trmw       made; checked
   2trm 2.8    monomer; mutant (D102N); complex with benzamidine; pH 8
   
Trypsin (Streptomyces griseus, strain K1)
   1sgt 1.7    monomer; sequence numbered as chymotrypsin - gaps
   
Trypsin Inhibitor (Bos taurus)
   4pti 1.5    monomer
   5pti 1.0/1.8monomer; joint x-ray & neutron - H's & D's; crystal form II
   6pti 1.7    monomer; crystal form III

Trypsinogen (Bos taurus)
   1tgb 1.8    monomer; CA form; trypsinogen; numbered acc. to 
               chymotrypsin - gaps
   1tgc 1.8    monomer; 50% methanol 50% water
   1tgn 1.65   monomer
   1tgs 1.8    monomer; complex with inhibitor
   1tgt 1.7    monomer; 173 degrees K
   2tga 1.8    monomer; 2.4 M MgSulfate
   2tgd 2.1    monomer; complex with inhibitor
   2tgp 1.9    monomer; complex with PTI
   2tgt 1.7    monomer; 103 degrees K; 70:30 = methanol:water
   2tpi 2.1    monomer; complex with PTI & Ile-Val; 2.4 MgSulfate
   3tpi 1.9    monomer; complex with PTI & Ile-Val
   4tpi 2.2    monomer; complex with PTI analog & Val-Val
   
TRP Repressor (Escherichia coli)
   1wrp 2.2    dimer (a2) - 1 chain given
   2wrp 1.65   dimer (a2) - 1 chain given; apparent error in space group in 
               PDB file - should be P 21 21 2
   2wrpw       made; checked 
   3wrp 1.8    dimer (a2) - 1 chain given; apo; apparent error in space group 
               in PDB file - should be P 21 21 2
   3wrpw       made; checked
   
Tryptophan Synthase (Salmonella typhimurium, strain TB2211/PSTH8)
   1wsy 2.5    tetramer (a2b2) - 2 chains given
   1wsyw       made; checked
   
Tumor Necrosis Factor Alpha (Homo sapiens)
   1tnf 2.6    trimer (a3) - 3 chains given

Tyrosyl-Transfer-RNA Synthetase (Bacillus stearothermophilus)
   2ts1 2.3    dimer (a2) - 1 chain given; supersedes 1ts1
   2ts1w       made; checked
   3ts1 2.7    dimer (a2) - 1 chain given; complex with tyrosinyl adenylate
   4ts1 2.5    dimer (a2) - 1 chain given; complex with tyrosine; 318 - 417
               deleted
   
Ubiquitin (Homo sapiens)
   1ubq 1.8    monomer
   
Uteroglobin (Oryctolagus cuniculus)
   1utg 1.34   dimer (a2) - 1 chain given; oxidized
   1utgw       made; checked
   2utg 1.64   dimer (a2) - 2 chains given
   
Wheat Germ Agglutinin (Triticum vulgaris)
   Two different isolectins; they differ by 5 amino acids.
   3wga 1.8    dimer - 2 chains given; isolectin 2?
   7wga 2.0    dimer - 2 chains given; isolectin 1
   9wga 1.8    dimer - 2 chains given; supersedes 3wga; isolectin 2; this
               molecule does NOT look correct - too much empty space; 
               orientation of different domains seems wrong.  Made dimers 
               by using each monomer and transforming acc to C2 matrix - 
               9wgaAC.pdb looks better and looks like one of dimers made by 
               Insight.  9wgaBD.pdb has (at least) translational problems.  
               Reordered lit - no good picture of real structure.
   1wgc 2.2    dimer - 2 chains given; complex with N-Acetylneuraminyllactose;
               isolectin 1
   2wgc 2.2    dimer - 2 chains given; complex with N-Acetylneuraminyllactose;
               isolectin 2
   
Xylose Isomerase (Arthrobacter strain B3728)
   1xia 2.3 CA tetramer - 2 chains given; all residues UNK
   4xia 2.3    tetramer - 2 chains given; complex with inhibitor sorbitol
   5xia 2.5    tetramer - 2 chains given; complex with inhibitor xylitol

Xylose Isomerase (Streptomyces rubiginosus)
   2xia 3.5 CA tetramer - 2 chains given; all residues UNK

Xylose Isomerase (Streptomyces olivochromogenes)
   3xia 3.0    dimer or tetramer - 1 chain given
   3xiaw       made; looks like one Insight makes -- no tetrameric picture
               in lit; re-ordered literature
   
Zinc Finger (Xenopus lavis)
   1znf NMR    monomer - 37 chains given; model 1 to be used for geometry



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