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PDBsum entry 4cha
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Hydrolase (serine proteinase) PDB id
4cha

 

 

 

 

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Contents
Protein chains
11 a.a.
131 a.a. *
97 a.a. *
Ligands
CYS-GLY-VAL-PRO-
ALA-ILE-GLN-PRO-
VAL-LEU
Waters ×85
* Residue conservation analysis
PDB id:
4cha
Name: Hydrolase (serine proteinase)
Title: Structure of alpha- Chymotrypsin refined at 1.68 angstroms resolution
Structure: Alpha-chymotrypsin a. Chain: a, e. Alpha-chymotrypsin a. Chain: b, f. Alpha-chymotrypsin a. Chain: c, g. Ec: 3.4.21.1
Source: Bos taurus. Cattle. Organism_taxid: 9913. Organism_taxid: 9913
Biol. unit: Trimer (from PQS)
Resolution:
1.68Å     R-factor:   not given    
Authors: H.Tsukada,D.M.Blow
Key ref:
H.Tsukada and D.M.Blow (1985). Structure of alpha-chymotrypsin refined at 1.68 A resolution. J Mol Biol, 184, 703-711. PubMed id: 4046030 DOI: 10.1016/0022-2836(85)90314-6
Date:
26-Nov-84     Release date:   01-Apr-85    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00766  (CTRA_BOVIN) -  Chymotrypsinogen A from Bos taurus
Seq:
Struc: 		245 a.a.
11 a.a.
Protein chains
Pfam   ArchSchema ?
P00766  (CTRA_BOVIN) -  Chymotrypsinogen A from Bos taurus
Seq:
Struc: 		245 a.a.
131 a.a.
Protein chains
Pfam   ArchSchema ?
P00766  (CTRA_BOVIN) -  Chymotrypsinogen A from Bos taurus
Seq:
Struc: 		245 a.a.
97 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B, C, F, G: E.C.3.4.21.1  - chymotrypsin.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.

 

 
DOI no: 10.1016/0022-2836(85)90314-6 J Mol Biol 184:703-711 (1985)
PubMed id: 4046030  
 
 
Structure of alpha-chymotrypsin refined at 1.68 A resolution.
H.Tsukada, D.M.Blow.
 
  ABSTRACT  
 
Diffraction data for alpha-chymotrypsin crystals at -10 degrees C were measured at 1.68 A resolution and refined by restrained structure-factor least-squares refinement. The two independent chymotrypsin molecules in the crystallographic asymmetric unit were refined independently. The overall structure of alpha-chymotrypsin is little changed from published co-ordinates. The root-mean-square shift of C alpha co-ordinates is 0.42 A, co-ordinates for the two molecules showing a root-mean-square difference of 0.19 A. Certain regions with high disorder (residues 9 to 14, 73 to 79) remain difficult to interpret and several side-chains are disordered. Some water molecule positions have been changed. The absence of the tosyl group has made a significant difference to the refined structure at the active site. This now agrees closely with other enzymes of the trypsin family that have been refined at high resolution. There is a strong hydrogen bond between N epsilon 2 (His57) and O gamma (Ser195) in the free enzyme, in line with the published description of the charge relay system.
 
  Selected figure(s)  
 
Figure 2.
Figur 2. An example of the non-reciprocal interactions between molecles related by non-crystallographic dyad with a small screw component. The carbonyls of (a) Ser92 nd b) Tyr94 in molecule 1 form hydrogen bonds ys93 N'' in molecule 343). The side-chain f Lys93 molecule ) is free in the solvent (Table C). The broken ines show contours in the (2F,,--F,) density. 		Figure 3.
Figure 3. Electron densty 2F,-FF,) for the charge relay system. Density nd ydrogen bonds nvolving Ser214 nd Tyr146' 396) of he molecule related by 2-fold local ymmetry are shown.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (1985, 184, 703-711) copyright 1985.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21152617 P.Attri, P.Venkatesu, and A.Kumar (2011).
Activity and stability of α-chymotrypsin in biocompatible ionic liquids: enzyme refolding by triethyl ammonium acetate.
  Phys Chem Chem Phys, 13, 2788-2796.  
19408924 B.Zhang, Y.Xing, Z.Li, H.Zhou, Q.Mu, and B.Yan (2009).
Functionalized carbon nanotubes specifically bind to alpha-chymotrypsin's catalytic site and regulate its enzymatic function.
  Nano Lett, 9, 2280-2284.  
19224136 J.A.Rodríguez-Martínez, I.Rivera-Rivera, R.J.Solá, and K.Griebenow (2009).
Enzymatic activity and thermal stability of PEG-alpha-chymotrypsin conjugates.
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  18931434 A.J.da Silva, R.C.Teles, G.F.Esteves, C.R.dos Santos, J.A.Barbosa, and S.M.de Freitas (2008).
Purification, crystallization and preliminary crystallographic studies of SPCI-chymotrypsin complex at 2.8 A resolution.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 914-917.  
18751692 J.Mátrai, A.Jonckheer, E.Joris, P.Krüger, E.Carpenter, J.Tuszynski, M.De Maeyer, and Y.Engelborghs (2008).
Exploration of the activation pathway of Deltaalpha-Chymotrypsin with molecular dynamics simulations and correlation with kinetic experiments.
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18922802 K.W.Rickert, P.Kelley, N.J.Byrne, R.E.Diehl, D.L.Hall, A.M.Montalvo, J.C.Reid, J.M.Shipman, B.W.Thomas, S.K.Munshi, P.L.Darke, and H.P.Su (2008).
Structure of human prostasin, a target for the regulation of hypertension.
  J Biol Chem, 283, 34864-34872.
PDB codes: 3dfj 3dfl
18658209 N.Rezaei-Ghaleh, M.Amininasab, and M.Nemat-Gorgani (2008).
Conformational changes of alpha-chymotrypsin in a fibrillation-promoting condition: a molecular dynamics study.
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  18084102 G.F.Esteves, R.C.Teles, N.S.Cavalcante, D.Neves, M.M.Ventura, J.A.Barbosa, and S.M.de Freitas (2007).
Crystallization, data collection and processing of the chymotrypsin-BTCI-trypsin ternary complex.
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Characterizing structural features of cuticle-degrading proteases from fungi by molecular modeling.
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18458382 E.P.Ivanova, J.P.Wright, D.K.Pham, N.Brack, P.Pigram, Y.V.Alekseeva, G.M.Demyashev, and D.V.Nicolau (2006).
A comparative study between the adsorption and covalent binding of human immunoglobulin and lysozyme on surface-modified poly(tert-butyl methacrylate).
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17076704 R.J.Solá, and K.Griebenow (2006).
Influence of modulated structural dynamics on the kinetics of alpha-chymotrypsin catalysis. Insights through chemical glycosylation, molecular dynamics and domain motion analysis.
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15654079 J.R.Birtley, S.R.Knox, A.M.Jaulent, P.Brick, R.J.Leatherbarrow, and S.Curry (2005).
Crystal structure of foot-and-mouth disease virus 3C protease. New insights into catalytic mechanism and cleavage specificity.
  J Biol Chem, 280, 11520-11527.
PDB code: 2bhg
15654893 N.Singh, T.Jabeen, S.Sharma, I.Roy, M.N.Gupta, S.Bilgrami, R.K.Somvanshi, S.Dey, M.Perbandt, C.Betzel, A.Srinivasan, and T.P.Singh (2005).
Detection of native peptides as potent inhibitors of enzymes. Crystal structure of the complex formed between treated bovine alpha-chymotrypsin and an autocatalytically produced fragment, IIe-Val-Asn-Gly-Glu-Glu-Ala-Val-Pro-Gly-Ser-Trp-Pro-Trp, at 2.2 angstroms resolution.
  FEBS J, 272, 562-572.
PDB code: 1oxg
15923233 W.Ma, C.Tang, and L.Lai (2005).
Specificity of trypsin and chymotrypsin: loop-motion-controlled dynamic correlation as a determinant.
  Biophys J, 89, 1183-1193.  
15557259 J.Mátrai, G.Verheyden, P.Krüger, and Y.Engelborghs (2004).
Simulation of the activation of alpha-chymotrypsin: analysis of the pathway and role of the propeptide.
  Protein Sci, 13, 3139-3150.  
14507912 J.Pandhare, C.Dash, M.Rao, and V.Deshpande (2003).
Slow tight binding inhibition of proteinase K by a proteinaceous inhibitor: conformational alterations responsible for conferring irreversibility to the enzyme-inhibitor complex.
  J Biol Chem, 278, 48735-48744.  
17590956 J.J.Goodall, V.K.Booth, A.E.Ashcroft, and C.W.Wharton (2002).
Hydrogen-bonding in 2-aminobenzoyl-alpha-chymotrypsin formed by acylation of the enzyme with isatoic anhydride: IR and mass spectroscopic studies.
  Chembiochem, 3, 68-75.  
11856830 J.P.Turkenburg, M.B.Lamers, A.M.Brzozowski, L.M.Wright, R.E.Hubbard, S.L.Sturt, and D.H.Williams (2002).
Structure of a Cys25-->Ser mutant of human cathepsin S.
  Acta Crystallogr D Biol Crystallogr, 58, 451-455.
PDB code: 1glo
12093723 K.Anand, G.J.Palm, J.R.Mesters, S.G.Siddell, J.Ziebuhr, and R.Hilgenfeld (2002).
Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain.
  EMBO J, 21, 3213-3224.
PDB code: 1lvo
11854035 M.C.Manjabacas, E.Valero, M.Moreno-Conesa, M.García-Moreno, M.Molina-Alarcón, and R.Varón (2002).
Linear mixed irreversible inhibition of the autocatalytic activation of zymogens. Kinetic analysis checked by simulated progress curves.
  Int J Biochem Cell Biol, 34, 358-369.  
12055188 M.I.Plotnick, H.Rubin, and N.M.Schechter (2002).
The effects of reactive site location on the inhibitory properties of the serpin alpha(1)-antichymotrypsin.
  J Biol Chem, 277, 29927-29935.  
11258922 C.Betzel, S.Gourinath, P.Kumar, P.Kaur, M.Perbandt, S.Eschenburg, and T.P.Singh (2001).
Structure of a serine protease proteinase K from Tritirachium album limber at 0.98 A resolution.
  Biochemistry, 40, 3080-3088.
PDB code: 1ic6
11260254 K.Hara, M.Shiota, H.Kido, Y.Ohtsu, T.Kashiwagi, J.Iwahashi, N.Hamada, K.Mizoue, N.Tsumura, H.Kato, and T.Toyoda (2001).
Influenza virus RNA polymerase PA subunit is a novel serine protease with Ser624 at the active site.
  Genes Cells, 6, 87-97.  
11737204 N.Spreti, P.Di Profio, L.Marte, S.Bufali, L.Brinchi, and G.Savelli (2001).
Activation and stabilization of alpha-chymotrypsin by cationic additives.
  Eur J Biochem, 268, 6491-6497.  
10757995 E.S.Courtenay, M.W.Capp, C.F.Anderson, and M.T.Record (2000).
Vapor pressure osmometry studies of osmolyte-protein interactions: implications for the action of osmoprotectants in vivo and for the interpretation of "osmotic stress" experiments in vitro.
  Biochemistry, 39, 4455-4471.  
10673439 J.Zou, B.M.Hallberg, T.Bergfors, F.Oesch, M.Arand, S.L.Mowbray, and T.A.Jones (2000).
Structure of Aspergillus niger epoxide hydrolase at 1.8 A resolution: implications for the structure and function of the mammalian microsomal class of epoxide hydrolases.
  Structure, 8, 111-122.
PDB code: 1qo7
10944388 V.Z.Pletnev, T.S.Zamolodchikova, W.A.Pangborn, and W.L.Duax (2000).
Crystal structure of bovine duodenase, a serine protease, with dual trypsin and chymotrypsin-like specificities.
  Proteins, 41, 8.
PDB code: 1euf
10022823 H.Jing, K.J.Macon, D.Moore, L.J.DeLucas, J.E.Volanakis, and S.V.Narayana (1999).
Structural basis of profactor D activation: from a highly flexible zymogen to a novel self-inhibited serine protease, complement factor D.
  EMBO J, 18, 804-814.
PDB code: 1fdp
10523291 J.F.Petersen, M.M.Cherney, H.D.Liebig, T.Skern, E.Kuechler, and M.N.James (1999).
The structure of the 2A proteinase from a common cold virus: a proteinase responsible for the shut-off of host-cell protein synthesis.
  EMBO J, 18, 5463-5475.
PDB code: 2hrv
  10595562 K.S.Makarova, and N.V.Grishin (1999).
Thermolysin and mitochondrial processing peptidase: how far structure-functional convergence goes.
  Protein Sci, 8, 2537-2540.  
10497153 M.M.Krem, T.Rose, and E.Di Cera (1999).
The C-terminal sequence encodes function in serine proteases.
  J Biol Chem, 274, 28063-28066.  
10328262 T.K.Harris, and A.S.Mildvan (1999).
High-precision measurement of hydrogen bond lengths in proteins by nuclear magnetic resonance methods.
  Proteins, 35, 275-282.  
  9568890 A.R.Khan, and M.N.James (1998).
Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes.
  Protein Sci, 7, 815-836.  
9836602 S.R.Presnell, G.S.Patil, C.Mura, K.M.Jude, J.M.Conley, J.A.Bertrand, C.M.Kam, J.C.Powers, and L.D.Williams (1998).
Oxyanion-mediated inhibition of serine proteases.
  Biochemistry, 37, 17068-17081.
PDB codes: 1bju 1bjv
10076803 V.Boden, M.H.Rangeard, N.Mrabet, and M.A.Vijayalakshmi (1998).
Histidine mapping of serine protease: a synergic study by IMAC and molecular modelling.
  J Mol Recognit, 11, 32-39.  
9179777 C.Capasso, M.Rizzi, E.Menegatti, P.Ascenzi, and M.Bolognesi (1997).
Crystal structure of the bovine alpha-chymotrypsin:Kunitz inhibitor complex. An example of multiple protein:protein recognition sites.
  J Mol Recognit, 10, 26-35.
PDB code: 1mtn
  9232643 D.E.Timm (1997).
The crystal structure of the mouse glandular kallikrein-13 (prorenin converting enzyme).
  Protein Sci, 6, 1418-1425.
PDB code: 1ao5
8786411 B.Walse, M.Ullner, C.Lindbladh, L.Bülow, T.Drakenberg, and O.Teleman (1996).
Structure of a cyclic peptide with a catalytic triad, determined by computer simulation and NMR spectroscopy.
  J Comput Aided Mol Des, 10, 11-22.  
8718849 E.S.Stavridi, K.O'Malley, C.M.Lukacs, W.T.Moore, J.D.Lambris, D.W.Christianson, H.Rubin, and B.S.Cooperman (1996).
Structural change in alpha-chymotrypsin induced by complexation with alpha 1-antichymotrypsin as seen by enhanced sensitivity to proteolysis.
  Biochemistry, 35, 10608-10615.  
8808738 R.A.Buono, N.Kucharczyk, M.Neuenschwander, J.Kemmink, L.Y.Hwang, J.L.Fauchère, and C.A.Venanzi (1996).
Synthesis and conformational analysis by 1H NMR and restrained molecular dynamics simulations of the cyclic decapeptide [Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly]
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8591045 G.Spraggon, C.Phillips, U.K.Nowak, C.P.Ponting, D.Saunders, C.M.Dobson, D.I.Stuart, and E.Y.Jones (1995).
The crystal structure of the catalytic domain of human urokinase-type plasminogen activator.
  Structure, 3, 681-691.
PDB code: 1lmw
8534804 J.Antosiewicz (1995).
Computation of the dipole moments of proteins.
  Biophys J, 69, 1344-1354.  
  8563637 R.M.Stroud, and E.B.Fauman (1995).
Significance of structural changes in proteins: expected errors in refined protein structures.
  Protein Sci, 4, 2392-2404.  
  7756993 A.A.Adzhubei, and M.J.Sternberg (1994).
Conservation of polyproline II helices in homologous proteins: implications for structure prediction by model building.
  Protein Sci, 3, 2395-2410.  
  8003977 C.L.Fisher, J.S.Greengard, and J.H.Griffin (1994).
Models of the serine protease domain of the human antithrombotic plasma factor activated protein C and its zymogen.
  Protein Sci, 3, 588-599.
PDB codes: 1pcu 2pct
7523123 E.Fioretti, M.Angeletti, G.Lupidi, and M.Coletta (1994).
Heterotropic modulation of the protease-inhibitor-recognition process. Cations effect the binding properties of alpha-chymotrypsin.
  Eur J Biochem, 225, 459-465.  
7925366 G.Lange, C.Betzel, S.Branner, and K.S.Wilson (1994).
Crystallographic studies of Savinase, a subtilisin-like proteinase, at pH 10.5.
  Eur J Biochem, 224, 507-518.  
7527234 R.Oddone, D.Barra, G.Amiconi, P.Ascenzi, C.Tarricone, M.Bolognesi, F.Bortolotti, and E.Menegatti (1994).
Binding of native and [homoserine lactone-52]-52,53-seco-bovine basic pancreatic trypsin inhibitor (Kunitz inhibitor) to porcine pancreatic beta-kallikrein-B and bovine alpha-chymotrypsin: thermodynamic study.
  J Mol Recognit, 7, 39-46.  
7986566 S.Tomova, F.Cutruzzolà, D.Barra, G.Amiconi, P.Ascenzi, K.Djinović Carugo, E.Menegatti, P.Sarti, H.P.Schnebli, and M.Bolognesi (1994).
Selective oxidation of methionyl residues in the human recombinant secretory leukocyte proteinase inhibitor. Effect on the inhibitor binding properties.
  J Mol Recognit, 7, 31-37.  
8475107 C.S.Ring, E.Sun, J.H.McKerrow, G.K.Lee, P.J.Rosenthal, I.D.Kuntz, and F.E.Cohen (1993).
Structure-based inhibitor design by using protein models for the development of antiparasitic agents.
  Proc Natl Acad Sci U S A, 90, 3583-3587.  
8364156 J.H.McMinn, M.J.Sowa, S.B.Charnick, and M.E.Paulaitis (1993).
The hydration of proteins in nearly anhydrous organic solvent suspensions.
  Biopolymers, 33, 1213-1224.  
8367494 M.Z.Atassi, and T.Manshouri (1993).
Design of peptide enzymes (pepzymes): surface-simulation synthetic peptides that mimic the chymotrypsin and trypsin active sites exhibit the activity and specificity of the respective enzyme.
  Proc Natl Acad Sci U S A, 90, 8282-8286.  
8451241 N.Vtyurin (1993).
The role of local tight packing of hydrophobic groups in beta-structure.
  Proteins, 15, 62-70.  
  1304887 E.Meyer (1992).
Internal water molecules and H-bonding in biological macromolecules: a review of structural features with functional implications.
  Protein Sci, 1, 1543-1562.  
1594574 J.A.Hartsuck, G.Koelsch, and S.J.Remington (1992).
The high-resolution crystal structure of porcine pepsinogen.
  Proteins, 13, 1.
PDB code: 3psg
1557349 J.S.Finer-Moore, A.A.Kossiakoff, J.H.Hurley, T.Earnest, and R.M.Stroud (1992).
Solvent structure in crystals of trypsin determined by X-ray and neutron diffraction.
  Proteins, 12, 203-222.
PDB code: 5ptp
1317584 R.Affleck, C.A.Haynes, and D.S.Clark (1992).
Solvent dielectric effects on protein dynamics.
  Proc Natl Acad Sci U S A, 89, 5167-5170.  
1298302 S.Onesti, D.J.Matthews, P.Aducci, G.Amiconi, M.Bolognesi, E.Menegatti, and P.Ascenzi (1992).
Binding of the Kunitz-type trypsin inhibitor DE-3 from Erythrina caffra seeds to serine proteinases: a comparative study.
  J Mol Recognit, 5, 105-114.  
  1304349 W.Bode, D.Turk, and A.Karshikov (1992).
The refined 1.9-A X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human alpha-thrombin: structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships.
  Protein Sci, 1, 426-471.
PDB codes: 1ai8 1aix
1866431 D.Pathak, G.Ashley, and D.Ollis (1991).
Thiol protease-like active site found in the enzyme dienelactone hydrolase: localization using biochemical, genetic, and structural tools.
  Proteins, 9, 267-279.  
2027907 G.Vermunicht, N.Boens, and F.C.de Schryver (1991).
Global analysis of the time-resolved fluorescence of alpha- chymotrypsinogen A and alpha-chymotrypsin powders as a function of hydration.
  Photochem Photobiol, 53, 57-63.  
2006137 J.L.Scully, and D.R.Evans (1991).
Comparative modeling of mammalian aspartate transcarbamylase.
  Proteins, 9, 191-206.  
1799460 P.Ascenzi, P.Aducci, G.Amiconi, A.Ballio, A.Guaragna, E.Menegatti, H.P.Schnebli, and M.Bolognesi (1991).
Binding of the recombinant proteinase inhibitor eglin c from leech Hirudo medicinalis to serine (pro)enzymes: a comparative thermodynamic study.
  J Mol Recognit, 4, 113-119.  
2278733 M.Bolognesi, L.Pugliese, G.Gatti, F.Frigerio, A.Coda, L.Antolini, H.P.Schnebli, E.Menegatti, G.Amiconi, and P.Ascenzi (1990).
X-ray crystal structure of the bovine alpha-chymotrypsin/eglin c complex at 2.6 A resolution.
  J Mol Recognit, 3, 163-168.  
2107323 M.S.Johnson, M.J.Sutcliffe, and T.L.Blundell (1990).
Molecular anatomy: phyletic relationships derived from three-dimensional structures of proteins.
  J Mol Evol, 30, 43-59.  
  2583108 W.Bode, I.Mayr, U.Baumann, R.Huber, S.R.Stone, and J.Hofsteenge (1989).
The refined 1.9 A crystal structure of human alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment.
  EMBO J, 8, 3467-3475.
PDB code: 1ppb
3228244 L.B.Evnin, and C.S.Craik (1988).
Development of an efficient method for generating and screening active trypsin and trypsin variants.
  Ann N Y Acad Sci, 542, 61-74.  
3237717 M.E.Murphy, J.Moult, R.C.Bleackley, H.Gershenfeld, I.L.Weissman, and M.N.James (1988).
Comparative molecular model building of two serine proteinases from cytotoxic T lymphocytes.
  Proteins, 4, 190-204.  
  3366116 M.G.Grütter, G.Fendrich, R.Huber, and W.Bode (1988).
The 2.5 A X-ray crystal structure of the acid-stable proteinase inhibitor from human mucous secretions analysed in its complex with bovine alpha-chymotrypsin.
  EMBO J, 7, 345-351.  
3273224 P.Ascenzi, M.Coletta, G.Amiconi, M.Bolognesi, M.Guarneri, and E.Menegatti (1988).
Zymogen activation: effect of peptides sequentially related to the bovine beta-trypsin N-terminus on Kazal inhibitor and benzamidine binding to bovine trypsinogen.
  J Mol Recognit, 1, 130-137.  
3468505 V.T.D'Souza, X.L.Lu, R.D.Ginger, and M.L.Bender (1987).
Thermal and pH stability of "beta-benzyme".
  Proc Natl Acad Sci U S A, 84, 673-674.  
  3640709 W.Bode, A.Z.Wei, R.Huber, E.Meyer, J.Travis, and S.Neumann (1986).
X-ray crystal structure of the complex of human leukocyte elastase (PMN elastase) and the third domain of the turkey ovomucoid inhibitor.
  EMBO J, 5, 2453-2458.
PDB code: 1ppf
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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