DOI: 10.1006/jmbi.2001.4695. Ligand-induced structural changes to maltodextrin-binding protein as studied by solution NMR spectroscopy

Ligand-induced structural changes to maltodextrin-binding protein as studied by solution NMR spectroscopy

10.1006/jmbi.2001.4695

Crossref journal-article

Elsevier BV

Journal of Molecular Biology (78)

Bibliography

EvenÃ¤s, J., Tugarinov, V., Skrynnikov, N. R., Goto, N. K., Muhandiram, R., & Kay, L. E. (2001). Ligand-induced structural changes to maltodextrin-binding protein as studied by solution NMR spectroscopy. Journal of Molecular Biology, 309(4), 961â974.

Authors 6

Johan Evenäs (first)
Vitali Tugarinov (additional)
Nikolai R Skrynnikov (additional)
Natalie K Goto (additional)
Ranjith Muhandiram (additional)
Lewis E Kay (additional)

References 74 Referenced 125

10.1111/j.1365-2958.1996.tb02484.x / Mol. Microbiol. / Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis by Quiocho (1996)
10.1111/j.1432-1033.1974.tb03677.x / Eur. J. Biochem. / Active transport of maltose in Escherichia coli K12. Involvement of a “periplasmic” maltose binding protein by Kellermann (1974)
10.1016/S0021-9258(17)43968-8 / J. Biol. Chem. / Rates of ligand binding to periplasmic binding proteins involved in bacterial transport and chemotaxis by Miller (1983)
10.1128/MMBR.62.1.204-229.1998 / Microbiol. Mol. Biol. Rev. / Maltose/maltodextrin system of Escherichia coli by Boos (1998)
10.1073/pnas.89.6.2360 / Proc. Natl Acad. Sci. USA / Mechanism of maltose transport in Escherichia coli by Davidson (1992)
10.1128/JB.164.3.1057-1063.1985 / J. Bacteriol. / Interspecific reconstitution of maltose transport and chemotaxis in Escherichia coli with maltose-binding protein from various enteric bacteria by Dahl (1985)
10.1006/jsbi.1998.4043 / J. Struct. Biol. / Chemotaxis receptors by Mowbray (1998)
10.1016/S0021-9258(19)67774-4 / J. Biol. Chem. / The 2.3 Å resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis by Spurlino (1991)
10.1016/S0969-2126(97)00253-0 / Structure / Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor by Quiocho (1997)
10.1021/bi00159a003 / Biochemistry / Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis by Sharff (1992)
10.1021/ac00093a047 / Anal. Chem. / Engineering the maltose binding protein for reagentless fluorescence sensing by Gilardi (1994)
10.1093/protein/10.5.479 / Protein Eng. / Spectroscopic properties of an engineered maltose binding protein by Gilardi (1997)
10.1002/pro.5560060116 / Protein Sci. / Thermodynamics of maltose binding protein unfolding by Novokhatny (1997)
10.1006/jmbi.1993.1543 / J. Mol. Biol. / Genetic analysis of periplasmic binding protein dependent transport in Escherichia coli. Each lobe of maltose-binding protein interacts with a different subunit of the MalFGK2 membrane transport complex by Hor (1993)
10.1016/0022-2836(88)90560-8 / J. Mol. Biol. / Allele-specific malE mutations that restore interactions between maltose-binding protein and the inner-membrane components of the maltose transport system by Treptow (1988)
10.1074/jbc.271.30.17881 / J. Biol. Chem. / Maltose-binding protein containing an interdomain disulfide bridge confers a dominant-negative phenotype for transport and chemotaxis by Zhang (1996)
10.1002/jss.400130110 / J. Supramol. Struct. / The role of the Escherichia coli lambda receptor in the transport of maltose and maltodextrins by Ferenci (1980)
10.1016/0005-2736(86)90496-7 / Biochim. Biophys. Acta. / Substrate specificity of the Escherichia coli maltodextrin transport system and its component proteins by Ferenci (1986)
10.1021/bi00236a027 / Biochemistry / Tritium NMR spectroscopy of ligand binding to maltose-binding protein by Gehring (1991)
10.1139/o98-060 / Biochem. Cell. Biol. / An NMR study of ligand binding by maltodextrin binding protein by Gehring (1998)
10.1074/jbc.272.28.17605 / J. Biol. Chem. / Two modes of ligand binding in maltose-binding protein of Escherichia coli. Correlation with the structure of ligands and the structure of binding protein by Hall (1997)
10.1074/jbc.272.28.17615 / J. Biol. Chem. / Two modes of ligand binding in maltose-binding protein of Escherichia coli. Functional significance in active transport by Hall (1997)
10.1074/jbc.272.28.17610 / J. Biol. Chem. / Two modes of ligand binding in maltose-binding protein of Escherichia coli. Electron paramagnetic resonance study of ligand-induced global conformational changes by site-directed spin labeling by Hall (1997)
10.1021/bi00091a004 / Biochemistry / Refined 1.8-Å structure reveals the mode of binding of β-cyclodextrin to the maltodextrin binding protein by Sharff (1993)
10.1006/jmbi.1999.3430 / J. Mol. Biol. / Orienting domains in proteins using dipolar couplings measured by liquid-state NMR by Skrynnikov (2000)
10.1006/jmbi.2000.3842 / J. Mol. Biol. / Global folds of proteins with low densities of NOEs using residual dipolar couplings by Mueller (2000)
10.1146/annurev.biophys.27.1.357 / Annu. Rev. Biophys. Biomol. Struct. / The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins by Gardner (1998)
{'key': '10.1006/jmbi.2001.4695_BIB28', 'first-page': '75', 'article-title': 'NMR of perdeuterated large proteins', 'volume': 'vol. 16', 'author': 'Farmer', 'year': '1998'} / NMR of perdeuterated large proteins by Farmer (1998)
10.1038/nsb0997-732 / Nature Struct. Biol. / Using dipolar 1H-15N and 1H-13C couplings in the structure determination of magnetically oriented macromolecules in solution by Tjandra (1997)
10.1021/bi9905213 / Biochemistry / Domain orientation and dynamics in multidomain proteins from residual dipolar couplings by Fischer (1999)
10.1073/pnas.97.16.9021 / Proc. Natl Acad. Sci. USA / Accurate and rapid docking of protein-protein complexes on the basis of internuclear Overhauser enhancement data and dipolar couplings by rigid body minimization by Clore (2000)
10.1107/S0907444998003254 / Acta Crystallog. sect. D / Crystallography & NMR system by Brunger (1998)
10.1016/S0959-440X(94)90173-2 / Curr. Opin. Struct. Biol. / Multidimensional nuclear magnetic resonance methods for protein studies by Bax (1994)
10.1021/ja982019w / J. Am. Chem. Soc. / Solution NMR studies of a 42 kDa E. coli maltose binding protein/β cyclodextrin complex by Gardner (1998)
10.1007/BF00227471 / J. Biomol. NMR / 1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects by Wishart (1995)
10.1023/A:1011226512421 / J. Biomol. NMR / Domain orientation in β-cyclodextrin-loaded maltose binding protein by Hwang (2001)
10.1038/nsb0298-156 / Nature Struct. Biol. / Correlation between binding and dynamics at SH2 domain interfaces by Kay (1998)
10.1073/pnas.96.3.939 / Proc. Natl Acad. Sci. USA / Model of maltose-binding protein/chemoreceptor complex supports intrasubunit signaling mechanism by Zhang (1999)
10.1073/pnas.92.20.9279 / Proc. Natl Acad. Sci. USA / Nuclear magnetic dipole interactions in field-oriented proteins by Tolman (1995)
10.1038/4176 / Nature Struct. Biol. / Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions by Hansen (1998)
10.1023/A:1008314803561 / J. Biomol. NMR / TROSY-based HNCO pulse sequences for the measurement of 1HN-15N, 15N-13CO, 1HN-13CO, 13CO-13Cα dipolar couplings in 15N,13C,2H-labeled proteins by Yang (1999)
10.1021/ja003833y / J. Am. Chem. Soc. / Measurement of 13Cα-13Cβ dipolar couplings in 15N,13C,2H-labeled proteins by Evenäs (2001)
10.1002/(SICI)1097-0134(199703)27:3<425::AID-PROT10>3.0.CO;2-N / Proteins: Struct. Funct. Genet. / Model-free methods of analyzing domain motions in proteins from simulation by Hayward (1997)
10.1016/S0006-3495(97)78317-6 / Biophys. J. / Protein dynamics derived from clusters of crystal structures by Van Alten (1997)
10.1006/jmbi.2001.4614 / J. Mol. Biol. / What is the average conformation of bacteriophage T4 lysozyme in solution? A domain orientation study using dipolar couplings measured by solution NMR by Goto (2001)
10.1002/(SICI)1097-0134(199703)27:3<410::AID-PROT9>3.0.CO;2-G / Proteins: Struct. Funct. Genet. / A new method for modeling large-scale rearrangements of protein domains by Maiorov (1997)
10.1126/science.7754375 / Science / Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling by Brüschweiler (1995)
10.1006/jmbi.1998.1785 / J. Mol. Biol. / Multiple open forms of ribose-binding protein trace the path of its conformational change by Björkman (1998)
10.1016/S0021-9258(17)37057-6 / J. Biol. Chem. / The 1.9 Å X-ray structure of a closed unliganded form of the periplasmic glucose/galactose receptor from Salmonella typhimurium by Flocco (1994)
10.1006/jmbi.1995.0396 / J. Mol. Biol. / Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme by Zhang (1995)
{'key': '10.1006/jmbi.2001.4695_BIB51', 'first-page': '477', 'article-title': 'AQUA and PROCHECK-NMR', 'volume': '8', 'author': 'Laskowski', 'year': '1998', 'journal-title': 'J. Biomol. NMR'} / J. Biomol. NMR / AQUA and PROCHECK-NMR by Laskowski (1998)
10.1023/A:1008395916985 / J. Biomol. NMR / Bicelle-based liquid crystals for NMR-measurement of dipolar couplings at acidic and basic pH values by Ottiger (1999)
10.1023/A:1008392405740 / J. Biomol. NMR / Protein backbone angle restraints from searching a database for chemical shift and sequence homology by Cornilescu (1999)
10.1021/ja984056t / J. Am. Chem. Soc. / TROSY triple resonance four-dimensional NMR spectroscopy of a 46 ns tumbling protein by Yang (1999)
10.1021/ja00105a005 / J. Am. Chem. Soc. / A suite of triple resonance NMR experiments for the backbone assignment of 15N, 13C, 2H labeled proteins with high sensitivity by Yamazaki (1994)
10.1021/ja960627a / J. Am. Chem. Soc. / Assignment of 15N, 13Cα, 13Cβ and HN resonances in an 15N, 13C, 2H labeled 64 kDa trp repressor-operator complex using triple resonance NMR spectroscopy and 2H-decoupling by Shan (1996)
10.1021/ja00093a069 / J. Am. Chem. Soc. / An HNCA pulse scheme for the backbone assignment of 15N, 13C, 2H labeled proteins by Yamazaki (1994)
10.1073/pnas.94.23.12366 / Proc. Natl Acad. Sci. USA / Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution by Pervushin (1997)
10.1021/bi00185a040 / Biochemistry / Backbone dynamics of a free and phosphopeptide-complexed src homology 2 domain studied by 15N NMR relaxation by Farrow (1994)
10.1007/BF00197809 / J. Biomol. NMR / NMRPipe by Delaglio (1995)
10.1007/BF00404272 / J. Biomol. NMR / NMRView by Johnson (1994)
10.1006/jmra.1994.1145 / J. Magn. Reson. ser. A / Enhanced-sensitivity triple-resonance spectroscopy with minimal H2O saturation by Kay (1994)
10.1006/jmbi.1996.0699 / J. Mol. Biol. / Characterizing the use of perdeuteration in NMR studies of large proteins by Venters (1996)
10.1021/bi9624806 / Biochemistry / Global folds of highly deuterated, methyl protonated proteins by multidimensional NMR by Gardner (1997)
{'key': '10.1006/jmbi.2001.4695_BIB65', 'series-title': 'NMR relaxation studies of protein dynamics in solution', 'author': 'Mulder', 'year': '1998'} / NMR relaxation studies of protein dynamics in solution by Mulder (1998)
10.1006/jmbi.1999.3034 / J. Mol. Biol. / Altered flexibility in the substrate-binding site of related native and engineered high-alkaline Bacillus subtilisins by Mulder (1999)
10.1021/ja981546c / J. Am. Chem. Soc. / Using amide 1H and 15N transverse relaxation to detect millisecond time-scale motions in perdeuterated proteins by Ishima (1998)
{'key': '10.1006/jmbi.2001.4695_BIB68', 'first-page': '214', 'article-title': 'A common sense approach to peak picking in two-, three-, and four-dimensional spectra using automatic computer analysis of contour diagrams', 'volume': '95', 'author': 'Garrett', 'year': '1991', 'journal-title': 'J. Magn. Reson.'} / J. Magn. Reson. / A common sense approach to peak picking in two-, three-, and four-dimensional spectra using automatic computer analysis of contour diagrams by Garrett (1991)
10.1016/S0066-4103(08)60245-8 / Annu. Rep. NMR Spectrosc. / High resolution NMR of liquids and gases by Bastiaan (1987)
10.1126/science.278.5340.1111 / Science / Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium by Tjandra (1997)
10.1016/0263-7855(96)00009-4 / J. Mol. Graph. / MOLMOL by Koradi (1996)
10.1006/jmre.1997.1345 / J. Magn. Reson. / Direct structure refinement against residual dipolar couplings in the presence of rhombicity of unknown magnitude by Clore (1998)
10.1006/jmre.1996.1027 / J. Magn. Reson. / Torsion-angle molecular dynamics as a new efficient tool for NMR structure calculation by Stein (1997)
10.1023/A:1026563923774 / J. Biomol. NMR / Study of conformational rearrangement and refinement of structural homology models by the use of heteronuclear dipolar couplings by Chou (2000)

Dates

Type	When
Created	22 years, 11 months ago (Sept. 18, 2002, 11:51 a.m.)
Deposited	4 years, 3 months ago (May 3, 2021, 12:54 a.m.)
Indexed	2 months ago (June 26, 2025, 9:28 a.m.)
Issued	24 years, 2 months ago (June 1, 2001)
Published	24 years, 2 months ago (June 1, 2001)
Published Print	24 years, 2 months ago (June 1, 2001)

Funders 0

None

BibTeX

@article{Even_s_2001, title={Ligand-induced structural changes to maltodextrin-binding protein as studied by solution NMR spectroscopy}, volume={309}, ISSN={0022-2836}, url={http://dx.doi.org/10.1006/jmbi.2001.4695}, DOI={10.1006/jmbi.2001.4695}, number={4}, journal={Journal of Molecular Biology}, publisher={Elsevier BV}, author={Evenäs, Johan and Tugarinov, Vitali and Skrynnikov, Nikolai R and Goto, Natalie K and Muhandiram, Ranjith and Kay, Lewis E}, year={2001}, month=jun, pages={961–974} }

JSON

{
  "indexed": {
    "date-parts": [
      [
        2025,
        6,
        26
      ]
    ],
    "date-time": "2025-06-26T13:28:49Z",
    "timestamp": 1750944529144
  },
  "reference-count": 74,
  "publisher": "Elsevier BV",
  "issue": "4",
  "license": [
    {
      "start": {
        "date-parts": [
          [
            2001,
            6,
            1
          ]
        ],
        "date-time": "2001-06-01T00:00:00Z",
        "timestamp": 991353600000
      },
      "content-version": "tdm",
      "delay-in-days": 0,
      "URL": "https://www.elsevier.com/tdm/userlicense/1.0/"
    }
  ],
  "content-domain": {
    "domain": [],
    "crossmark-restriction": false
  },
  "published-print": {
    "date-parts": [
      [
        2001,
        6
      ]
    ]
  },
  "DOI": "10.1006/jmbi.2001.4695",
  "type": "journal-article",
  "created": {
    "date-parts": [
      [
        2002,
        9,
        18
      ]
    ],
    "date-time": "2002-09-18T15:51:29Z",
    "timestamp": 1032364289000
  },
  "page": "961-974",
  "source": "Crossref",
  "is-referenced-by-count": 125,
  "title": "Ligand-induced structural changes to maltodextrin-binding protein as studied by solution NMR spectroscopy",
  "prefix": "10.1006",
  "volume": "309",
  "author": [
    {
      "given": "Johan",
      "family": "Even\u00e4s",
      "sequence": "first",
      "affiliation": []
    },
    {
      "given": "Vitali",
      "family": "Tugarinov",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Nikolai R",
      "family": "Skrynnikov",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Natalie K",
      "family": "Goto",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Ranjith",
      "family": "Muhandiram",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Lewis E",
      "family": "Kay",
      "sequence": "additional",
      "affiliation": []
    }
  ],
  "member": "78",
  "reference": [
    {
      "key": "10.1006/jmbi.2001.4695_BIB1",
      "doi-asserted-by": "crossref",
      "first-page": "17",
      "DOI": "10.1111/j.1365-2958.1996.tb02484.x",
      "article-title": "Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis",
      "volume": "20",
      "author": "Quiocho",
      "year": "1996",
      "journal-title": "Mol. Microbiol."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB2",
      "doi-asserted-by": "crossref",
      "first-page": "139",
      "DOI": "10.1111/j.1432-1033.1974.tb03677.x",
      "article-title": "Active transport of maltose in Escherichia coli K12. Involvement of a \u201cperiplasmic\u201d maltose binding protein",
      "volume": "47",
      "author": "Kellermann",
      "year": "1974",
      "journal-title": "Eur. J. Biochem."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB3",
      "doi-asserted-by": "crossref",
      "first-page": "13193",
      "DOI": "10.1016/S0021-9258(17)43968-8",
      "article-title": "Rates of ligand binding to periplasmic binding proteins involved in bacterial transport and chemotaxis",
      "volume": "258",
      "author": "Miller",
      "year": "1983",
      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB4",
      "doi-asserted-by": "crossref",
      "first-page": "204",
      "DOI": "10.1128/MMBR.62.1.204-229.1998",
      "article-title": "Maltose/maltodextrin system of Escherichia coli",
      "volume": "62",
      "author": "Boos",
      "year": "1998",
      "journal-title": "Microbiol. Mol. Biol. Rev."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB5",
      "doi-asserted-by": "crossref",
      "first-page": "2360",
      "DOI": "10.1073/pnas.89.6.2360",
      "article-title": "Mechanism of maltose transport in Escherichia coli",
      "volume": "89",
      "author": "Davidson",
      "year": "1992",
      "journal-title": "Proc. Natl Acad. Sci. USA"
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB6",
      "doi-asserted-by": "crossref",
      "first-page": "1057",
      "DOI": "10.1128/JB.164.3.1057-1063.1985",
      "article-title": "Interspecific reconstitution of maltose transport and chemotaxis in Escherichia coli with maltose-binding protein from various enteric bacteria",
      "volume": "164",
      "author": "Dahl",
      "year": "1985",
      "journal-title": "J. Bacteriol."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB7",
      "doi-asserted-by": "crossref",
      "first-page": "257",
      "DOI": "10.1006/jsbi.1998.4043",
      "article-title": "Chemotaxis receptors",
      "volume": "124",
      "author": "Mowbray",
      "year": "1998",
      "journal-title": "J. Struct. Biol."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB8",
      "doi-asserted-by": "crossref",
      "first-page": "5202",
      "DOI": "10.1016/S0021-9258(19)67774-4",
      "article-title": "The 2.3 \u00c5 resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis",
      "volume": "266",
      "author": "Spurlino",
      "year": "1991",
      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB9",
      "doi-asserted-by": "crossref",
      "first-page": "997",
      "DOI": "10.1016/S0969-2126(97)00253-0",
      "article-title": "Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor",
      "volume": "5",
      "author": "Quiocho",
      "year": "1997",
      "journal-title": "Structure"
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB10",
      "doi-asserted-by": "crossref",
      "first-page": "10657",
      "DOI": "10.1021/bi00159a003",
      "article-title": "Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis",
      "volume": "31",
      "author": "Sharff",
      "year": "1992",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB11",
      "doi-asserted-by": "crossref",
      "first-page": "3840",
      "DOI": "10.1021/ac00093a047",
      "article-title": "Engineering the maltose binding protein for reagentless fluorescence sensing",
      "volume": "66",
      "author": "Gilardi",
      "year": "1994",
      "journal-title": "Anal. Chem."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB12",
      "doi-asserted-by": "crossref",
      "first-page": "479",
      "DOI": "10.1093/protein/10.5.479",
      "article-title": "Spectroscopic properties of an engineered maltose binding protein",
      "volume": "10",
      "author": "Gilardi",
      "year": "1997",
      "journal-title": "Protein Eng."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB13",
      "doi-asserted-by": "crossref",
      "first-page": "141",
      "DOI": "10.1002/pro.5560060116",
      "article-title": "Thermodynamics of maltose binding protein unfolding",
      "volume": "6",
      "author": "Novokhatny",
      "year": "1997",
      "journal-title": "Protein Sci."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB14",
      "doi-asserted-by": "crossref",
      "first-page": "659",
      "DOI": "10.1006/jmbi.1993.1543",
      "article-title": "Genetic analysis of periplasmic binding protein dependent transport in Escherichia coli. Each lobe of maltose-binding protein interacts with a different subunit of the MalFGK2 membrane transport complex",
      "volume": "233",
      "author": "Hor",
      "year": "1993",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB15",
      "doi-asserted-by": "crossref",
      "first-page": "809",
      "DOI": "10.1016/0022-2836(88)90560-8",
      "article-title": "Allele-specific malE mutations that restore interactions between maltose-binding protein and the inner-membrane components of the maltose transport system",
      "volume": "202",
      "author": "Treptow",
      "year": "1988",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB16",
      "doi-asserted-by": "crossref",
      "first-page": "17881",
      "DOI": "10.1074/jbc.271.30.17881",
      "article-title": "Maltose-binding protein containing an interdomain disulfide bridge confers a dominant-negative phenotype for transport and chemotaxis",
      "volume": "271",
      "author": "Zhang",
      "year": "1996",
      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB17",
      "doi-asserted-by": "crossref",
      "first-page": "101",
      "DOI": "10.1002/jss.400130110",
      "article-title": "The role of the Escherichia coli lambda receptor in the transport of maltose and maltodextrins",
      "volume": "13",
      "author": "Ferenci",
      "year": "1980",
      "journal-title": "J. Supramol. Struct."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB18",
      "doi-asserted-by": "crossref",
      "first-page": "44",
      "DOI": "10.1016/0005-2736(86)90496-7",
      "article-title": "Substrate specificity of the Escherichia coli maltodextrin transport system and its component proteins",
      "volume": "860",
      "author": "Ferenci",
      "year": "1986",
      "journal-title": "Biochim. Biophys. Acta."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB19",
      "doi-asserted-by": "crossref",
      "first-page": "5524",
      "DOI": "10.1021/bi00236a027",
      "article-title": "Tritium NMR spectroscopy of ligand binding to maltose-binding protein",
      "volume": "30",
      "author": "Gehring",
      "year": "1991",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB20",
      "doi-asserted-by": "crossref",
      "first-page": "189",
      "DOI": "10.1139/o98-060",
      "article-title": "An NMR study of ligand binding by maltodextrin binding protein",
      "volume": "76",
      "author": "Gehring",
      "year": "1998",
      "journal-title": "Biochem. Cell. Biol."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB21",
      "doi-asserted-by": "crossref",
      "first-page": "17605",
      "DOI": "10.1074/jbc.272.28.17605",
      "article-title": "Two modes of ligand binding in maltose-binding protein of Escherichia coli. Correlation with the structure of ligands and the structure of binding protein",
      "volume": "272",
      "author": "Hall",
      "year": "1997",
      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB22",
      "doi-asserted-by": "crossref",
      "first-page": "17615",
      "DOI": "10.1074/jbc.272.28.17615",
      "article-title": "Two modes of ligand binding in maltose-binding protein of Escherichia coli. Functional significance in active transport",
      "volume": "272",
      "author": "Hall",
      "year": "1997",
      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB23",
      "doi-asserted-by": "crossref",
      "first-page": "17610",
      "DOI": "10.1074/jbc.272.28.17610",
      "article-title": "Two modes of ligand binding in maltose-binding protein of Escherichia coli. Electron paramagnetic resonance study of ligand-induced global conformational changes by site-directed spin labeling",
      "volume": "272",
      "author": "Hall",
      "year": "1997",
      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB24",
      "doi-asserted-by": "crossref",
      "first-page": "10553",
      "DOI": "10.1021/bi00091a004",
      "article-title": "Refined 1.8-\u00c5 structure reveals the mode of binding of \u03b2-cyclodextrin to the maltodextrin binding protein",
      "volume": "32",
      "author": "Sharff",
      "year": "1993",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB25",
      "doi-asserted-by": "crossref",
      "first-page": "1265",
      "DOI": "10.1006/jmbi.1999.3430",
      "article-title": "Orienting domains in proteins using dipolar couplings measured by liquid-state NMR",
      "volume": "295",
      "author": "Skrynnikov",
      "year": "2000",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB26",
      "doi-asserted-by": "crossref",
      "first-page": "197",
      "DOI": "10.1006/jmbi.2000.3842",
      "article-title": "Global folds of proteins with low densities of NOEs using residual dipolar couplings",
      "volume": "300",
      "author": "Mueller",
      "year": "2000",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB27",
      "doi-asserted-by": "crossref",
      "first-page": "357",
      "DOI": "10.1146/annurev.biophys.27.1.357",
      "article-title": "The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins",
      "volume": "27",
      "author": "Gardner",
      "year": "1998",
      "journal-title": "Annu. Rev. Biophys. Biomol. Struct."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB28",
      "first-page": "75",
      "article-title": "NMR of perdeuterated large proteins",
      "volume": "vol. 16",
      "author": "Farmer",
      "year": "1998"
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB29",
      "doi-asserted-by": "crossref",
      "first-page": "732",
      "DOI": "10.1038/nsb0997-732",
      "article-title": "Using dipolar 1H-15N and 1H-13C couplings in the structure determination of magnetically oriented macromolecules in solution",
      "volume": "4",
      "author": "Tjandra",
      "year": "1997",
      "journal-title": "Nature Struct. Biol."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB30",
      "doi-asserted-by": "crossref",
      "first-page": "9013",
      "DOI": "10.1021/bi9905213",
      "article-title": "Domain orientation and dynamics in multidomain proteins from residual dipolar couplings",
      "volume": "38",
      "author": "Fischer",
      "year": "1999",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB31",
      "doi-asserted-by": "crossref",
      "first-page": "9021",
      "DOI": "10.1073/pnas.97.16.9021",
      "article-title": "Accurate and rapid docking of protein-protein complexes on the basis of internuclear Overhauser enhancement data and dipolar couplings by rigid body minimization",
      "volume": "97",
      "author": "Clore",
      "year": "2000",
      "journal-title": "Proc. Natl Acad. Sci. USA"
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB32",
      "doi-asserted-by": "crossref",
      "first-page": "905",
      "DOI": "10.1107/S0907444998003254",
      "article-title": "Crystallography & NMR system",
      "volume": "54",
      "author": "Brunger",
      "year": "1998",
      "journal-title": "Acta Crystallog. sect. D"
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB33",
      "doi-asserted-by": "crossref",
      "first-page": "738",
      "DOI": "10.1016/S0959-440X(94)90173-2",
      "article-title": "Multidimensional nuclear magnetic resonance methods for protein studies",
      "volume": "4",
      "author": "Bax",
      "year": "1994",
      "journal-title": "Curr. Opin. Struct. Biol."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB34",
      "doi-asserted-by": "crossref",
      "first-page": "11738",
      "DOI": "10.1021/ja982019w",
      "article-title": "Solution NMR studies of a 42 kDa E. coli maltose binding protein/\u03b2 cyclodextrin complex",
      "volume": "120",
      "author": "Gardner",
      "year": "1998",
      "journal-title": "J. Am. Chem. Soc."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB35",
      "doi-asserted-by": "crossref",
      "first-page": "67",
      "DOI": "10.1007/BF00227471",
      "article-title": "1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects",
      "volume": "5",
      "author": "Wishart",
      "year": "1995",
      "journal-title": "J. Biomol. NMR"
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB36",
      "doi-asserted-by": "crossref",
      "DOI": "10.1023/A:1011226512421",
      "article-title": "Domain orientation in \u03b2-cyclodextrin-loaded maltose binding protein",
      "author": "Hwang",
      "year": "2001",
      "journal-title": "J. Biomol. NMR"
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB37",
      "doi-asserted-by": "crossref",
      "first-page": "156",
      "DOI": "10.1038/nsb0298-156",
      "article-title": "Correlation between binding and dynamics at SH2 domain interfaces",
      "volume": "5",
      "author": "Kay",
      "year": "1998",
      "journal-title": "Nature Struct. Biol."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB38",
      "doi-asserted-by": "crossref",
      "first-page": "939",
      "DOI": "10.1073/pnas.96.3.939",
      "article-title": "Model of maltose-binding protein/chemoreceptor complex supports intrasubunit signaling mechanism",
      "volume": "96",
      "author": "Zhang",
      "year": "1999",
      "journal-title": "Proc. Natl Acad. Sci. USA"
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB39",
      "doi-asserted-by": "crossref",
      "first-page": "9279",
      "DOI": "10.1073/pnas.92.20.9279",
      "article-title": "Nuclear magnetic dipole interactions in field-oriented proteins",
      "volume": "92",
      "author": "Tolman",
      "year": "1995",
      "journal-title": "Proc. Natl Acad. Sci. USA"
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB40",
      "doi-asserted-by": "crossref",
      "first-page": "1065",
      "DOI": "10.1038/4176",
      "article-title": "Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions",
      "volume": "5",
      "author": "Hansen",
      "year": "1998",
      "journal-title": "Nature Struct. Biol."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB41",
      "doi-asserted-by": "crossref",
      "first-page": "333",
      "DOI": "10.1023/A:1008314803561",
      "article-title": "TROSY-based HNCO pulse sequences for the measurement of 1HN-15N, 15N-13CO, 1HN-13CO, 13CO-13C\u03b1 dipolar couplings in 15N,13C,2H-labeled proteins",
      "volume": "14",
      "author": "Yang",
      "year": "1999",
      "journal-title": "J. Biomol. NMR"
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB42",
      "doi-asserted-by": "crossref",
      "first-page": "2858",
      "DOI": "10.1021/ja003833y",
      "article-title": "Measurement of 13C\u03b1-13C\u03b2 dipolar couplings in 15N,13C,2H-labeled proteins",
      "volume": "123",
      "author": "Even\u00e4s",
      "year": "2001",
      "journal-title": "J. Am. Chem. Soc."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB43",
      "doi-asserted-by": "crossref",
      "first-page": "425",
      "DOI": "10.1002/(SICI)1097-0134(199703)27:3<425::AID-PROT10>3.0.CO;2-N",
      "article-title": "Model-free methods of analyzing domain motions in proteins from simulation",
      "volume": "27",
      "author": "Hayward",
      "year": "1997",
      "journal-title": "Proteins: Struct. Funct. Genet."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB44",
      "doi-asserted-by": "crossref",
      "first-page": "2891",
      "DOI": "10.1016/S0006-3495(97)78317-6",
      "article-title": "Protein dynamics derived from clusters of crystal structures",
      "volume": "73",
      "author": "Van Alten",
      "year": "1997",
      "journal-title": "Biophys. J."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB45",
      "doi-asserted-by": "crossref",
      "first-page": "745",
      "DOI": "10.1006/jmbi.2001.4614",
      "article-title": "What is the average conformation of bacteriophage T4 lysozyme in solution? A domain orientation study using dipolar couplings measured by solution NMR",
      "volume": "308",
      "author": "Goto",
      "year": "2001",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB46",
      "doi-asserted-by": "crossref",
      "first-page": "410",
      "DOI": "10.1002/(SICI)1097-0134(199703)27:3<410::AID-PROT9>3.0.CO;2-G",
      "article-title": "A new method for modeling large-scale rearrangements of protein domains",
      "volume": "27",
      "author": "Maiorov",
      "year": "1997",
      "journal-title": "Proteins: Struct. Funct. Genet."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB47",
      "doi-asserted-by": "crossref",
      "first-page": "886",
      "DOI": "10.1126/science.7754375",
      "article-title": "Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling",
      "volume": "268",
      "author": "Br\u00fcschweiler",
      "year": "1995",
      "journal-title": "Science"
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB48",
      "doi-asserted-by": "crossref",
      "first-page": "651",
      "DOI": "10.1006/jmbi.1998.1785",
      "article-title": "Multiple open forms of ribose-binding protein trace the path of its conformational change",
      "volume": "279",
      "author": "Bj\u00f6rkman",
      "year": "1998",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB49",
      "doi-asserted-by": "crossref",
      "first-page": "8931",
      "DOI": "10.1016/S0021-9258(17)37057-6",
      "article-title": "The 1.9 \u00c5 X-ray structure of a closed unliganded form of the periplasmic glucose/galactose receptor from Salmonella typhimurium",
      "volume": "269",
      "author": "Flocco",
      "year": "1994",
      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB50",
      "doi-asserted-by": "crossref",
      "first-page": "527",
      "DOI": "10.1006/jmbi.1995.0396",
      "article-title": "Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme",
      "volume": "250",
      "author": "Zhang",
      "year": "1995",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB51",
      "first-page": "477",
      "article-title": "AQUA and PROCHECK-NMR",
      "volume": "8",
      "author": "Laskowski",
      "year": "1998",
      "journal-title": "J. Biomol. NMR"
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB52",
      "doi-asserted-by": "crossref",
      "first-page": "187",
      "DOI": "10.1023/A:1008395916985",
      "article-title": "Bicelle-based liquid crystals for NMR-measurement of dipolar couplings at acidic and basic pH values",
      "volume": "13",
      "author": "Ottiger",
      "year": "1999",
      "journal-title": "J. Biomol. NMR"
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB53",
      "doi-asserted-by": "crossref",
      "first-page": "289",
      "DOI": "10.1023/A:1008392405740",
      "article-title": "Protein backbone angle restraints from searching a database for chemical shift and sequence homology",
      "volume": "13",
      "author": "Cornilescu",
      "year": "1999",
      "journal-title": "J. Biomol. NMR"
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB54",
      "doi-asserted-by": "crossref",
      "first-page": "2571",
      "DOI": "10.1021/ja984056t",
      "article-title": "TROSY triple resonance four-dimensional NMR spectroscopy of a 46 ns tumbling protein",
      "volume": "121",
      "author": "Yang",
      "year": "1999",
      "journal-title": "J. Am. Chem. Soc."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB55",
      "doi-asserted-by": "crossref",
      "first-page": "11655",
      "DOI": "10.1021/ja00105a005",
      "article-title": "A suite of triple resonance NMR experiments for the backbone assignment of 15N, 13C, 2H labeled proteins with high sensitivity",
      "volume": "116",
      "author": "Yamazaki",
      "year": "1994",
      "journal-title": "J. Am. Chem. Soc."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB56",
      "doi-asserted-by": "crossref",
      "first-page": "6570",
      "DOI": "10.1021/ja960627a",
      "article-title": "Assignment of 15N, 13C\u03b1, 13C\u03b2 and HN resonances in an 15N, 13C, 2H labeled 64 kDa trp repressor-operator complex using triple resonance NMR spectroscopy and 2H-decoupling",
      "volume": "118",
      "author": "Shan",
      "year": "1996",
      "journal-title": "J. Am. Chem. Soc."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB57",
      "doi-asserted-by": "crossref",
      "first-page": "6464",
      "DOI": "10.1021/ja00093a069",
      "article-title": "An HNCA pulse scheme for the backbone assignment of 15N, 13C, 2H labeled proteins",
      "volume": "116",
      "author": "Yamazaki",
      "year": "1994",
      "journal-title": "J. Am. Chem. Soc."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB58",
      "doi-asserted-by": "crossref",
      "first-page": "12366",
      "DOI": "10.1073/pnas.94.23.12366",
      "article-title": "Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution",
      "volume": "94",
      "author": "Pervushin",
      "year": "1997",
      "journal-title": "Proc. Natl Acad. Sci. USA"
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB59",
      "doi-asserted-by": "crossref",
      "first-page": "5984",
      "DOI": "10.1021/bi00185a040",
      "article-title": "Backbone dynamics of a free and phosphopeptide-complexed src homology 2 domain studied by 15N NMR relaxation",
      "volume": "33",
      "author": "Farrow",
      "year": "1994",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB60",
      "doi-asserted-by": "crossref",
      "first-page": "277",
      "DOI": "10.1007/BF00197809",
      "article-title": "NMRPipe",
      "volume": "6",
      "author": "Delaglio",
      "year": "1995",
      "journal-title": "J. Biomol. NMR"
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB61",
      "doi-asserted-by": "crossref",
      "first-page": "603",
      "DOI": "10.1007/BF00404272",
      "article-title": "NMRView",
      "volume": "4",
      "author": "Johnson",
      "year": "1994",
      "journal-title": "J. Biomol. NMR"
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB62",
      "doi-asserted-by": "crossref",
      "first-page": "129",
      "DOI": "10.1006/jmra.1994.1145",
      "article-title": "Enhanced-sensitivity triple-resonance spectroscopy with minimal H2O saturation",
      "volume": "109",
      "author": "Kay",
      "year": "1994",
      "journal-title": "J. Magn. Reson. ser. A"
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB63",
      "doi-asserted-by": "crossref",
      "first-page": "1101",
      "DOI": "10.1006/jmbi.1996.0699",
      "article-title": "Characterizing the use of perdeuteration in NMR studies of large proteins",
      "volume": "264",
      "author": "Venters",
      "year": "1996",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB64",
      "doi-asserted-by": "crossref",
      "first-page": "1389",
      "DOI": "10.1021/bi9624806",
      "article-title": "Global folds of highly deuterated, methyl protonated proteins by multidimensional NMR",
      "volume": "36",
      "author": "Gardner",
      "year": "1997",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB65",
      "series-title": "NMR relaxation studies of protein dynamics in solution",
      "author": "Mulder",
      "year": "1998"
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB66",
      "doi-asserted-by": "crossref",
      "first-page": "111",
      "DOI": "10.1006/jmbi.1999.3034",
      "article-title": "Altered flexibility in the substrate-binding site of related native and engineered high-alkaline Bacillus subtilisins",
      "volume": "292",
      "author": "Mulder",
      "year": "1999",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB67",
      "doi-asserted-by": "crossref",
      "first-page": "10534",
      "DOI": "10.1021/ja981546c",
      "article-title": "Using amide 1H and 15N transverse relaxation to detect millisecond time-scale motions in perdeuterated proteins",
      "volume": "120",
      "author": "Ishima",
      "year": "1998",
      "journal-title": "J. Am. Chem. Soc."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB68",
      "first-page": "214",
      "article-title": "A common sense approach to peak picking in two-, three-, and four-dimensional spectra using automatic computer analysis of contour diagrams",
      "volume": "95",
      "author": "Garrett",
      "year": "1991",
      "journal-title": "J. Magn. Reson."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB69",
      "doi-asserted-by": "crossref",
      "first-page": "35",
      "DOI": "10.1016/S0066-4103(08)60245-8",
      "article-title": "High resolution NMR of liquids and gases",
      "volume": "9",
      "author": "Bastiaan",
      "year": "1987",
      "journal-title": "Annu. Rep. NMR Spectrosc."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB70",
      "doi-asserted-by": "crossref",
      "first-page": "1111",
      "DOI": "10.1126/science.278.5340.1111",
      "article-title": "Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium",
      "volume": "278",
      "author": "Tjandra",
      "year": "1997",
      "journal-title": "Science"
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB71",
      "doi-asserted-by": "crossref",
      "first-page": "51",
      "DOI": "10.1016/0263-7855(96)00009-4",
      "article-title": "MOLMOL",
      "volume": "14",
      "author": "Koradi",
      "year": "1996",
      "journal-title": "J. Mol. Graph."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB72",
      "doi-asserted-by": "crossref",
      "first-page": "159",
      "DOI": "10.1006/jmre.1997.1345",
      "article-title": "Direct structure refinement against residual dipolar couplings in the presence of rhombicity of unknown magnitude",
      "volume": "131",
      "author": "Clore",
      "year": "1998",
      "journal-title": "J. Magn. Reson."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB73",
      "doi-asserted-by": "crossref",
      "first-page": "154",
      "DOI": "10.1006/jmre.1996.1027",
      "article-title": "Torsion-angle molecular dynamics as a new efficient tool for NMR structure calculation",
      "volume": "124",
      "author": "Stein",
      "year": "1997",
      "journal-title": "J. Magn. Reson."
    },
    {
      "key": "10.1006/jmbi.2001.4695_BIB74",
      "doi-asserted-by": "crossref",
      "first-page": "217",
      "DOI": "10.1023/A:1026563923774",
      "article-title": "Study of conformational rearrangement and refinement of structural homology models by the use of heteronuclear dipolar couplings",
      "volume": "18",
      "author": "Chou",
      "year": "2000",
      "journal-title": "J. Biomol. NMR"
    }
  ],
  "container-title": "Journal of Molecular Biology",
  "original-title": [],
  "language": "en",
  "link": [
    {
      "URL": "https://api.elsevier.com/content/article/PII:S0022283601946959?httpAccept=text/xml",
      "content-type": "text/xml",
      "content-version": "vor",
      "intended-application": "text-mining"
    },
    {
      "URL": "https://api.elsevier.com/content/article/PII:S0022283601946959?httpAccept=text/plain",
      "content-type": "text/plain",
      "content-version": "vor",
      "intended-application": "text-mining"
    }
  ],
  "deposited": {
    "date-parts": [
      [
        2021,
        5,
        3
      ]
    ],
    "date-time": "2021-05-03T04:54:58Z",
    "timestamp": 1620017698000
  },
  "score": 1,
  "resource": {
    "primary": {
      "URL": "https://linkinghub.elsevier.com/retrieve/pii/S0022283601946959"
    }
  },
  "subtitle": [],
  "short-title": [],
  "issued": {
    "date-parts": [
      [
        2001,
        6
      ]
    ]
  },
  "references-count": 74,
  "journal-issue": {
    "issue": "4",
    "published-print": {
      "date-parts": [
        [
          2001,
          6
        ]
      ]
    }
  },
  "alternative-id": [
    "S0022283601946959"
  ],
  "URL": "http://dx.doi.org/10.1006/jmbi.2001.4695",
  "relation": {},
  "ISSN": [
    "0022-2836"
  ],
  "subject": [],
  "container-title-short": "Journal of Molecular Biology",
  "published": {
    "date-parts": [
      [
        2001,
        6
      ]
    ]
  }
}