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Open data
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Basic information
Entry | Database: PDB / ID: 1nsc | |||||||||
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Title | INFLUENZA B VIRUS NEURAMINIDASE CAN SYNTHESIZE ITS OWN INHIBITOR | |||||||||
![]() | NEURAMINIDASE | |||||||||
![]() | HYDROLASE(O-GLYCOSYL) | |||||||||
Function / homology | ![]() exo-alpha-(2->3)-sialidase activity / exo-alpha-(2->6)-sialidase activity / exo-alpha-(2->8)-sialidase activity / exo-alpha-sialidase / viral budding from plasma membrane / carbohydrate metabolic process / host cell plasma membrane / virion membrane / membrane / metal ion binding Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Burmeister, W.P. / Ruigrok, R.W.H. / Cusack, S. | |||||||||
![]() | ![]() Title: Influenza B virus neuraminidase can synthesize its own inhibitor. Authors: Burmeister, W.P. / Henrissat, B. / Bosso, C. / Cusack, S. / Ruigrok, R.W. #1: ![]() Title: The 2.2 Angstroms Resolution Crystal Structure of Influenza B Neuraminidase and its Complex with Sialic Acid Authors: Burmeister, W.P. / Ruigrok, R.W.H. / Cusack, S. #2: ![]() Title: Sequence and Crystallization of Influenza Virus B(Slash)Beijing(Slash)1(Slash)87 Neuraminidase Authors: Burmeister, W.P. / Daniels, R.S. / Dayan, S. / Gagnon, J. / Cusack, S. / Ruigrok, R.W.H. | |||||||||
History |
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Remark 700 | SHEET STRAND 4 OF SHEET RECORD *3A* AND *3B* IS IRREGULAR. STRAND 4 OF SHEET RECORD *5* IS VERY IRREGULAR. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 221 KB | Display | ![]() |
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PDB format | ![]() | 180.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 533.7 KB | Display | ![]() |
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Full document | ![]() | 548.5 KB | Display | |
Data in XML | ![]() | 18.4 KB | Display | |
Data in CIF | ![]() | 30.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Atom site foot note | 1: CA 468 BELONGS TO THE CAH SITE OF MONOMER 1. / 2: CA 469 BELONGS TO THE CAH SITE OF MONOMER 2. / 3: CA 470 BELONGS TO THE CAL SITE ON THE FOUR-FOLD AXIS. / 4: CIS PROLINE - PRO A 138 / 5: CIS PROLINE - PRO A 325 / 6: CIS PROLINE - PRO B 138 / 7: CIS PROLINE - PRO B 325 | ||||||||||||||||||
Components on special symmetry positions |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.25, 0.433, -0.866), |
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Components
#1: Protein | Mass: 43429.254 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Genus: Influenzavirus B / Species: Influenza B virus / Strain: B/Beijing/1/87 / References: UniProt: P27907, exo-alpha-sialidase #2: Sugar | #3: Sugar | #4: Chemical | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.92 Å3/Da / Density % sol: 57.95 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.9 / Method: batch methodDetails: taken from Burmeister, W.P. et al (1992). Embo J., 11, 49-56. | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 1.7 Å / Num. obs: 78825 / % possible obs: 70 % / Num. measured all: 127467 / Rmerge(I) obs: 0.088 |
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Processing
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Refinement | Rfactor Rwork: 0.18 / Rfactor obs: 0.18 / Highest resolution: 1.7 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 1.7 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 1.7 Å / Rfactor obs: 0.18 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d |