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- PDB-1nsb: THE 2.2 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF INFLUENZA B NEU... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1nsb | ||||||
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Title | THE 2.2 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF INFLUENZA B NEURAMINIDASE AND ITS COMPLEX WITH SIALIC ACID | ||||||
![]() | 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: The 2.2 A resolution crystal structure of influenza B neuraminidase and its complex with sialic acid. Authors: Burmeister, W.P. / Ruigrok, R.W. / Cusack, S. #1: ![]() 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 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE ...SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. STRANDS 2, 3, AND 4 OF 3A AND 3B ARE IDENTICAL. STRAND 4 OF SHEETS 3A AND 3B IS IRREGULAR. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 215.5 KB | Display | ![]() |
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PDB format | ![]() | 175.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar 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: RESIDUES PRO A 138, PRO A 325, PRO B 138, AND PRO B 325 ARE CIS PROLINES. | |||||||||||||||
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: Chemical | #4: 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 method / Details: microseeding | ||||||||||||||||||||||||||||||
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: 2.2 Å / Num. obs: 48764 / % possible obs: 92 % / Num. measured all: 120666 / Rmerge(I) obs: 0.071 |
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Processing
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Refinement | Resolution: 2.2→7 Å / Rfactor Rwork: 0.148 / Rfactor obs: 0.148 / σ(F): 0 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→7 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.2 Å / Lowest resolution: 7 Å / σ(F): 0 / Rfactor all: 0.148 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d |