protein data bank Search Results


protein data bank entry 4g0b  (Lallemand inc)
90
Lallemand inc protein data bank entry 4g0b
Protein Data Bank Entry 4g0b, supplied by Lallemand inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/protein+data+bank/protein+data+bank+entry+4g0b/pm29992670-164-11-17
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prosite data bank  (Federation of European Neuroscience Societies)
90
Federation of European Neuroscience Societies prosite data bank
Prosite Data Bank, supplied by Federation of European Neuroscience Societies, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/protein+data+bank/protein+data+bank/pm17169003-114-33-7
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prosite data bank - by Bioz Stars, 2026-09
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protein data bank  (Biomol GmbH)
90
Biomol GmbH protein data bank
Protein Data Bank, supplied by Biomol GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/protein+data+bank/protein+data+bank/pmc08244417-22-9-23
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protein data bank - by Bioz Stars, 2026-09
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protein data bank  (Symantec Corporation)
90
Symantec Corporation protein data bank
Protein Data Bank, supplied by Symantec Corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/protein+data+bank/protein+data+bank/pmc06753081__41467_2019_12199_MOESM7_ESM-11-49-52
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protein data bank - by Bioz Stars, 2026-09
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protein data bank entries 1ycr  (DeLano Scientific LLC PyMOL)
90
DeLano Scientific LLC PyMOL protein data bank entries 1ycr
p53(15–29) and RI-p53(15–29) are structurally different in solution. A, superposition of the crystal structures of synMDM2-PMI in magenta and green and recombinant MDM2(17–125)-p53(15–29) in blue and yellow. The image was created from Protein Data Bank entries <t>3EQS</t> (15) and 1YCR (14) by PyMOL (DeLano Scientific LLC). Note that only residues 25–109 of MDM2 and 17–29 of p53 are visible in the complex structure due to disordered termini. B, CD spectra of 100 μm p53(15–29) and RI-p53(15–29) in 10 mm phosphate buffer, pH 7.2, with or without 60% (v/v) TFE. The double maxima at 208 and 222 nm and a strong negative peak at 195 nm shown by RI-p53(15–29) (green) are characteristic of left-handed α-helical secondary structure. C, 20 superimposed structures of p53(15–29) (left) and of RI-p53(15–29) (right) determined at 20 °C in 50% TFE by NMR spectroscopy.
Protein Data Bank Entries 1ycr, supplied by DeLano Scientific LLC PyMOL, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/protein+data+bank/protein+data+bank+entries+1ycr/pmc02885236-264-5-20
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protein data bank entries 1ycr - by Bioz Stars, 2026-09
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protein data bank with partial charges’ q’, autodock 4 atom types, t (pdbqt) file  (AUTODOCK GmbH)
90
AUTODOCK GmbH protein data bank with partial charges’ q’, autodock 4 atom types, t (pdbqt) file
p53(15–29) and RI-p53(15–29) are structurally different in solution. A, superposition of the crystal structures of synMDM2-PMI in magenta and green and recombinant MDM2(17–125)-p53(15–29) in blue and yellow. The image was created from Protein Data Bank entries <t>3EQS</t> (15) and 1YCR (14) by PyMOL (DeLano Scientific LLC). Note that only residues 25–109 of MDM2 and 17–29 of p53 are visible in the complex structure due to disordered termini. B, CD spectra of 100 μm p53(15–29) and RI-p53(15–29) in 10 mm phosphate buffer, pH 7.2, with or without 60% (v/v) TFE. The double maxima at 208 and 222 nm and a strong negative peak at 195 nm shown by RI-p53(15–29) (green) are characteristic of left-handed α-helical secondary structure. C, 20 superimposed structures of p53(15–29) (left) and of RI-p53(15–29) (right) determined at 20 °C in 50% TFE by NMR spectroscopy.
Protein Data Bank With Partial Charges’ Q’, Autodock 4 Atom Types, T (Pdbqt) File, supplied by AUTODOCK GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/protein+data+bank/protein+data+bank+with+partial+charges%E2%80%99+q%E2%80%99++autodock+4+atom+types++t++pdbqt++file/pmc09727334-80-29-37
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protein data bank with partial charges’ q’, autodock 4 atom types, t (pdbqt) file - by Bioz Stars, 2026-09
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protein data bank  (National Institute of Standards and Technology)
90
National Institute of Standards and Technology protein data bank
p53(15–29) and RI-p53(15–29) are structurally different in solution. A, superposition of the crystal structures of synMDM2-PMI in magenta and green and recombinant MDM2(17–125)-p53(15–29) in blue and yellow. The image was created from Protein Data Bank entries <t>3EQS</t> (15) and 1YCR (14) by PyMOL (DeLano Scientific LLC). Note that only residues 25–109 of MDM2 and 17–29 of p53 are visible in the complex structure due to disordered termini. B, CD spectra of 100 μm p53(15–29) and RI-p53(15–29) in 10 mm phosphate buffer, pH 7.2, with or without 60% (v/v) TFE. The double maxima at 208 and 222 nm and a strong negative peak at 195 nm shown by RI-p53(15–29) (green) are characteristic of left-handed α-helical secondary structure. C, 20 superimposed structures of p53(15–29) (left) and of RI-p53(15–29) (right) determined at 20 °C in 50% TFE by NMR spectroscopy.
Protein Data Bank, supplied by National Institute of Standards and Technology, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/protein+data+bank/protein+data+bank/10__5530_slash_ijper__58__3__106-143-3-27
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protein data bank - by Bioz Stars, 2026-09
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protein data bank file  (OpenEye Scientific Software Inc)
90
OpenEye Scientific Software Inc protein data bank file
p53(15–29) and RI-p53(15–29) are structurally different in solution. A, superposition of the crystal structures of synMDM2-PMI in magenta and green and recombinant MDM2(17–125)-p53(15–29) in blue and yellow. The image was created from Protein Data Bank entries <t>3EQS</t> (15) and 1YCR (14) by PyMOL (DeLano Scientific LLC). Note that only residues 25–109 of MDM2 and 17–29 of p53 are visible in the complex structure due to disordered termini. B, CD spectra of 100 μm p53(15–29) and RI-p53(15–29) in 10 mm phosphate buffer, pH 7.2, with or without 60% (v/v) TFE. The double maxima at 208 and 222 nm and a strong negative peak at 195 nm shown by RI-p53(15–29) (green) are characteristic of left-handed α-helical secondary structure. C, 20 superimposed structures of p53(15–29) (left) and of RI-p53(15–29) (right) determined at 20 °C in 50% TFE by NMR spectroscopy.
Protein Data Bank File, supplied by OpenEye Scientific Software Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/protein+data+bank/protein+data+bank+file/pm23368732-86-1-25
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protein data bank file - by Bioz Stars, 2026-09
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protein data bank file 1zgu  (DeLano Scientific)
90
DeLano Scientific protein data bank file 1zgu
p53(15–29) and RI-p53(15–29) are structurally different in solution. A, superposition of the crystal structures of synMDM2-PMI in magenta and green and recombinant MDM2(17–125)-p53(15–29) in blue and yellow. The image was created from Protein Data Bank entries <t>3EQS</t> (15) and 1YCR (14) by PyMOL (DeLano Scientific LLC). Note that only residues 25–109 of MDM2 and 17–29 of p53 are visible in the complex structure due to disordered termini. B, CD spectra of 100 μm p53(15–29) and RI-p53(15–29) in 10 mm phosphate buffer, pH 7.2, with or without 60% (v/v) TFE. The double maxima at 208 and 222 nm and a strong negative peak at 195 nm shown by RI-p53(15–29) (green) are characteristic of left-handed α-helical secondary structure. C, 20 superimposed structures of p53(15–29) (left) and of RI-p53(15–29) (right) determined at 20 °C in 50% TFE by NMR spectroscopy.
Protein Data Bank File 1zgu, supplied by DeLano Scientific, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/protein+data+bank/protein+data+bank+file+1zgu/pm17964296-59-7-17
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protein data bank file 1zgu - by Bioz Stars, 2026-09
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protein data bank, partial charge (q), & atom type (t)  (AUTODOCK GmbH)
90
AUTODOCK GmbH protein data bank, partial charge (q), & atom type (t)
p53(15–29) and RI-p53(15–29) are structurally different in solution. A, superposition of the crystal structures of synMDM2-PMI in magenta and green and recombinant MDM2(17–125)-p53(15–29) in blue and yellow. The image was created from Protein Data Bank entries <t>3EQS</t> (15) and 1YCR (14) by PyMOL (DeLano Scientific LLC). Note that only residues 25–109 of MDM2 and 17–29 of p53 are visible in the complex structure due to disordered termini. B, CD spectra of 100 μm p53(15–29) and RI-p53(15–29) in 10 mm phosphate buffer, pH 7.2, with or without 60% (v/v) TFE. The double maxima at 208 and 222 nm and a strong negative peak at 195 nm shown by RI-p53(15–29) (green) are characteristic of left-handed α-helical secondary structure. C, 20 superimposed structures of p53(15–29) (left) and of RI-p53(15–29) (right) determined at 20 °C in 50% TFE by NMR spectroscopy.
Protein Data Bank, Partial Charge (Q), & Atom Type (T), supplied by AUTODOCK GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/protein+data+bank/protein+data+bank++partial+charge++q+++++atom+type++t+++pdbqt++format/pm37047270-701-12-6
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protein data bank, partial charge (q), & atom type (t) - by Bioz Stars, 2026-09
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cyp2a13 (protein data bank 2p85)  (Schrodinger LLC)
90
Schrodinger LLC cyp2a13 (protein data bank 2p85)
p53(15–29) and RI-p53(15–29) are structurally different in solution. A, superposition of the crystal structures of synMDM2-PMI in magenta and green and recombinant MDM2(17–125)-p53(15–29) in blue and yellow. The image was created from Protein Data Bank entries <t>3EQS</t> (15) and 1YCR (14) by PyMOL (DeLano Scientific LLC). Note that only residues 25–109 of MDM2 and 17–29 of p53 are visible in the complex structure due to disordered termini. B, CD spectra of 100 μm p53(15–29) and RI-p53(15–29) in 10 mm phosphate buffer, pH 7.2, with or without 60% (v/v) TFE. The double maxima at 208 and 222 nm and a strong negative peak at 195 nm shown by RI-p53(15–29) (green) are characteristic of left-handed α-helical secondary structure. C, 20 superimposed structures of p53(15–29) (left) and of RI-p53(15–29) (right) determined at 20 °C in 50% TFE by NMR spectroscopy.
Cyp2a13 (Protein Data Bank 2p85), supplied by Schrodinger LLC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/protein+data+bank/cyp2a13++protein+data+bank+2p85+/pmc02680511-114-3-40
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crystal structure protein data bank number 1s50  (DeLano Scientific)
90
DeLano Scientific crystal structure protein data bank number 1s50
p53(15–29) and RI-p53(15–29) are structurally different in solution. A, superposition of the crystal structures of synMDM2-PMI in magenta and green and recombinant MDM2(17–125)-p53(15–29) in blue and yellow. The image was created from Protein Data Bank entries <t>3EQS</t> (15) and 1YCR (14) by PyMOL (DeLano Scientific LLC). Note that only residues 25–109 of MDM2 and 17–29 of p53 are visible in the complex structure due to disordered termini. B, CD spectra of 100 μm p53(15–29) and RI-p53(15–29) in 10 mm phosphate buffer, pH 7.2, with or without 60% (v/v) TFE. The double maxima at 208 and 222 nm and a strong negative peak at 195 nm shown by RI-p53(15–29) (green) are characteristic of left-handed α-helical secondary structure. C, 20 superimposed structures of p53(15–29) (left) and of RI-p53(15–29) (right) determined at 20 °C in 50% TFE by NMR spectroscopy.
Crystal Structure Protein Data Bank Number 1s50, supplied by DeLano Scientific, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/protein+data+bank/crystal+structure+protein+data+bank+number+1s50/pmc06672684-66-2-18
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crystal structure protein data bank number 1s50 - by Bioz Stars, 2026-09
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Image Search Results


p53(15–29) and RI-p53(15–29) are structurally different in solution. A, superposition of the crystal structures of synMDM2-PMI in magenta and green and recombinant MDM2(17–125)-p53(15–29) in blue and yellow. The image was created from Protein Data Bank entries 3EQS (15) and 1YCR (14) by PyMOL (DeLano Scientific LLC). Note that only residues 25–109 of MDM2 and 17–29 of p53 are visible in the complex structure due to disordered termini. B, CD spectra of 100 μm p53(15–29) and RI-p53(15–29) in 10 mm phosphate buffer, pH 7.2, with or without 60% (v/v) TFE. The double maxima at 208 and 222 nm and a strong negative peak at 195 nm shown by RI-p53(15–29) (green) are characteristic of left-handed α-helical secondary structure. C, 20 superimposed structures of p53(15–29) (left) and of RI-p53(15–29) (right) determined at 20 °C in 50% TFE by NMR spectroscopy.

Journal: The Journal of Biological Chemistry

Article Title: Limitations of Peptide Retro-inverso Isomerization in Molecular Mimicry *

doi: 10.1074/jbc.M110.116814

Figure Lengend Snippet: p53(15–29) and RI-p53(15–29) are structurally different in solution. A, superposition of the crystal structures of synMDM2-PMI in magenta and green and recombinant MDM2(17–125)-p53(15–29) in blue and yellow. The image was created from Protein Data Bank entries 3EQS (15) and 1YCR (14) by PyMOL (DeLano Scientific LLC). Note that only residues 25–109 of MDM2 and 17–29 of p53 are visible in the complex structure due to disordered termini. B, CD spectra of 100 μm p53(15–29) and RI-p53(15–29) in 10 mm phosphate buffer, pH 7.2, with or without 60% (v/v) TFE. The double maxima at 208 and 222 nm and a strong negative peak at 195 nm shown by RI-p53(15–29) (green) are characteristic of left-handed α-helical secondary structure. C, 20 superimposed structures of p53(15–29) (left) and of RI-p53(15–29) (right) determined at 20 °C in 50% TFE by NMR spectroscopy.

Article Snippet: The image was created from Protein Data Bank entries 3EQS ( 15 ) and 1YCR ( 14 ) by PyMOL (DeLano Scientific LLC).

Techniques: Recombinant, Spectroscopy