+Open data
-Basic information
Entry | Database: PDB / ID: 1fmm | ||||||
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Title | SOLUTION STRUCTURE OF NFGF-1 | ||||||
Components | ACIDIC FIBROBLAST GROWTH FACTOR | ||||||
Keywords | HORMONE/GROWTH FACTOR / growth factor / triple resonance / mitogen / wound healing / HORMONE-GROWTH FACTOR COMPLEX | ||||||
Function / homology | Function and homology information mesonephric epithelium development / branch elongation involved in ureteric bud branching / positive regulation of cholesterol biosynthetic process / fibroblast growth factor receptor binding / S100 protein binding / positive regulation of intracellular signal transduction / positive regulation of cell division / fibroblast growth factor receptor signaling pathway / growth factor activity / positive regulation of angiogenesis ...mesonephric epithelium development / branch elongation involved in ureteric bud branching / positive regulation of cholesterol biosynthetic process / fibroblast growth factor receptor binding / S100 protein binding / positive regulation of intracellular signal transduction / positive regulation of cell division / fibroblast growth factor receptor signaling pathway / growth factor activity / positive regulation of angiogenesis / integrin binding / heparin binding / cell cortex / angiogenesis / cell differentiation / positive regulation of cell migration / positive regulation of cell population proliferation / positive regulation of transcription by RNA polymerase II / extracellular space / extracellular region / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Notophthalmus viridescens (eastern newt) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model type details | minimized average | ||||||
Authors | Arunkumar, A.I. / Srisailam, S. / Kumar, T.K.S. / Chiu, I.M. / Yu, C. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2002 Title: Structure and stability of an acidic fibroblast growth factor from Notophthalmus viridescens. Authors: Arunkumar, A.I. / Srisailam, S. / Kumar, T.K. / Kathir, K.M. / Chi, Y.H. / Wang, H.M. / Chang, G.G. / Chiu, I. / Yu, C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fmm.cif.gz | 57.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fmm.ent.gz | 42.7 KB | Display | PDB format |
PDBx/mmJSON format | 1fmm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1fmm_validation.pdf.gz | 242.8 KB | Display | wwPDB validaton report |
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Full document | 1fmm_full_validation.pdf.gz | 242.6 KB | Display | |
Data in XML | 1fmm_validation.xml.gz | 6.9 KB | Display | |
Data in CIF | 1fmm_validation.cif.gz | 9.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fm/1fmm ftp://data.pdbj.org/pub/pdb/validation_reports/fm/1fmm | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 15033.870 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Notophthalmus viridescens (eastern newt) Cell: FIBROBLAST / Plasmid: PET21B / Production host: Escherichia coli (E. coli) / References: UniProt: Q7SIF8 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: 3D 13C-separated NOESY |
-Sample preparation
Details | Contents: 10 mM phosphate and 100 mM sodium Chloride / Solvent system: water |
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Sample conditions | Ionic strength: 0.1 / pH: 6.0 / Pressure: ambient / Temperature: 298 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz |
-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 50 / Conformers submitted total number: 1 |