+Open data
-Basic information
Entry | Database: PDB / ID: 1qnk | ||||||
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Title | TRUNCATED HUMAN GROB[5-73], NMR, 20 STRUCTURES | ||||||
Components | C-X-C motif chemokine 2 | ||||||
Keywords | CHEMOKINE / CHEMOKINE 15-O / HUMAN CHEMOKINE GROB[5-73] / CXC CHEMOKINE | ||||||
Function / homology | Function and homology information CXCR chemokine receptor binding / chemokine-mediated signaling pathway / Chemokine receptors bind chemokines / chemokine activity / Interleukin-10 signaling / neutrophil chemotaxis / response to molecule of bacterial origin / chemotaxis / antimicrobial humoral immune response mediated by antimicrobial peptide / G alpha (i) signalling events ...CXCR chemokine receptor binding / chemokine-mediated signaling pathway / Chemokine receptors bind chemokines / chemokine activity / Interleukin-10 signaling / neutrophil chemotaxis / response to molecule of bacterial origin / chemotaxis / antimicrobial humoral immune response mediated by antimicrobial peptide / G alpha (i) signalling events / cellular response to lipopolysaccharide / inflammatory response / extracellular space / extracellular region Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Qian, Y.Q. / Johanson, K. / McDevitt, P. | ||||||
Citation | Journal: J. Mol. Biol. / Year: 1999 Title: Nuclear magnetic resonance solution structure of truncated human GRObeta [5-73] and its structural comparison with CXC chemokine family members GROalpha and IL-8. Authors: Qian, Y.Q. / Johanson, K.O. / McDevitt, P. #1: Journal: Blood / Year: 1995 Title: Characterization and Purification of a Stromal Cell Derived Hematopoietic Synergistic Factor Induced by a Novel Hematoregulatory Compound, Sk&F 107647 Authors: King, A. / Scott, R. / Wu, D. / Strickler, J. / Mcnulty, D. / Scott, M. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR PROVIDED. | ||||||
Remark 700 | SHEET DETERMINATION METHOD: AUTHOR PROVIDED. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1qnk.cif.gz | 835.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1qnk.ent.gz | 726.5 KB | Display | PDB format |
PDBx/mmJSON format | 1qnk.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1qnk_validation.pdf.gz | 356.4 KB | Display | wwPDB validaton report |
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Full document | 1qnk_full_validation.pdf.gz | 672.7 KB | Display | |
Data in XML | 1qnk_validation.xml.gz | 61.1 KB | Display | |
Data in CIF | 1qnk_validation.cif.gz | 80.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qn/1qnk ftp://data.pdbj.org/pub/pdb/validation_reports/qn/1qnk | 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: 7553.010 Da / Num. of mol.: 2 / Fragment: Residues 5-73 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Cellular location: BLOOD / Gene: CXCL2, GRO2, GROB, MIP2A, SCYB2 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): (LW 14) / References: UniProt: P19875 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: 2D |
NMR details | Text: SEE JRNL ARTICLE FOR DETAILS THREE-DIMENSIONAL STRUCTURE IN AQUEOUS SOLUTION REPRESENTED BY 20 CONFORMERS DETERMINED BY NUCLEAR MAGNETIC RESONANCE, TORSION ANGLE DYNAMICS AND RESTRAINED ENERGY ...Text: SEE JRNL ARTICLE FOR DETAILS THREE-DIMENSIONAL STRUCTURE IN AQUEOUS SOLUTION REPRESENTED BY 20 CONFORMERS DETERMINED BY NUCLEAR MAGNETIC RESONANCE, TORSION ANGLE DYNAMICS AND RESTRAINED ENERGY REFINEMENT. DATA WERE COLLECTED AT 30 DEGREES CELSIUS AND AT PH 5.5. THEY CONSIST OF 1878 UPPER LIMITS ON DISTANCES OBTAINED FROM NOE MEASUREMENTS AND 314 ANGLE CONSTRAINTS OBTAINED FROM NOE MEASUREMENTS AND COUPLING CONSTANT MEASUREMENTS. THERE INPUT DATA ARE ALSO AVAILABLE FROM THE PROTEIN DATA BANK. TORSION ANGLE DYNAMICS CALCULATIONS WERE PERFORMED WITH THE PROGRAM DYANA (P.GUNTERT, C.MUMENTHALER, K.WUTHRICH, J.MOL.BIOL. (1997) VOL. 273, 283-298). |
-Sample preparation
Details | Contents: 90%H2O/10%D2O |
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Sample conditions | pH: 5.5 / Pressure: 1 atm / Temperature: 303 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Varian UNITYPLUS / Manufacturer: Varian / Model: UNITYPLUS / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 80 / Conformers submitted total number: 20 |