+Open data
-Basic information
Entry | Database: PDB / ID: 1mzl | ||||||
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Title | MAIZE NONSPECIFIC LIPID TRANSFER PROTEIN | ||||||
Components | MAIZE NONSPECIFIC LIPID TRANSFER PROTEIN | ||||||
Keywords | LIPID TRANSPORT / ALPHA-HELICAL STRUCTURE | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Zea mays (maize) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.9 Å | ||||||
Authors | Shin, D.H. / Lee, J.Y. / Hwang, K.Y. / Kim, K.K. / Suh, S.W. | ||||||
Citation | Journal: Structure / Year: 1995 Title: High-resolution crystal structure of the non-specific lipid-transfer protein from maize seedlings. Authors: Shin, D.H. / Lee, J.Y. / Hwang, K.Y. / Kim, K.K. / Suh, S.W. #1: Journal: Proteins / Year: 1994 Title: Crystallization and Preliminary X-Ray Crystallographic Analysis of Phospholipid Transfer Protein from Maize Seedlings Authors: Shin, D.H. / Hwang, K.Y. / Kim, K.K. / Kim, S. / Sweet, R.M. / Suh, S.W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1mzl.cif.gz | 26.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1mzl.ent.gz | 17.4 KB | Display | PDB format |
PDBx/mmJSON format | 1mzl.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1mzl_validation.pdf.gz | 414.1 KB | Display | wwPDB validaton report |
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Full document | 1mzl_full_validation.pdf.gz | 415.8 KB | Display | |
Data in XML | 1mzl_validation.xml.gz | 6.5 KB | Display | |
Data in CIF | 1mzl_validation.cif.gz | 8.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mz/1mzl ftp://data.pdbj.org/pub/pdb/validation_reports/mz/1mzl | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 9062.161 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Zea mays (maize) / References: UniProt: P19656 |
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#2: Water | ChemComp-HOH / |
Has protein modification | Y |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.36 Å3/Da / Density % sol: 48 % |
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Crystal | *PLUS |
Crystal grow | *PLUS Temperature: 24.5-25.5 ℃ / Method: vapor diffusion, hanging dropDetails: Shin, D.H., (1994) Proteins: Struct.,Funct., Genet., 19, 80. |
Components of the solutions | *PLUS Common name: 24-well tissue culture plates / Details: flow laboratories |
-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Detector: AREA DETECTOR |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 7765 / % possible obs: 97.5 % / Observed criterion σ(I): 0.5 / Redundancy: 9.9 % / Rmerge(I) obs: 0.036 |
Reflection | *PLUS Highest resolution: 1.9 Å / Num. measured all: 76774 |
-Processing
Software |
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Refinement | Resolution: 1.9→8 Å / σ(F): 0
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Displacement parameters | Biso mean: 23 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.25 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→8 Å
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Refine LS restraints |
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