[English] 日本語
Yorodumi
- PDB-5yw1: Crystal structure of full length NS3 protein (eD4NS2BNS3) in comp... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5yw1
TitleCrystal structure of full length NS3 protein (eD4NS2BNS3) in complex with Bovine Pancreatic Trypsin Inhibitor
Components
  • FLAVIVIRUS_NS2B
  • PTI protein
  • Peptidase S7
KeywordsVIRAL PROTEIN / SERINE PROTEASE / NON-STRUCTURAL PROTEIN 3 / DEAH HELICASE / ATPASE / DENGUE VIRUS / FLAVIVIRUS
Function / homology
Function and homology information


trypsinogen activation / negative regulation of serine-type endopeptidase activity / sulfate binding / negative regulation of platelet aggregation / potassium channel inhibitor activity / zymogen binding / molecular function inhibitor activity / negative regulation of thrombin-activated receptor signaling pathway / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of host TYK2 activity / flavivirin ...trypsinogen activation / negative regulation of serine-type endopeptidase activity / sulfate binding / negative regulation of platelet aggregation / potassium channel inhibitor activity / zymogen binding / molecular function inhibitor activity / negative regulation of thrombin-activated receptor signaling pathway / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of host TYK2 activity / flavivirin / host cell mitochondrion / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity / serine protease inhibitor complex / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity / ribonucleoside triphosphate phosphatase activity / serine-type endopeptidase inhibitor activity / double-stranded RNA binding / viral capsid / nucleoside-triphosphate phosphatase / protein complex oligomerization / monoatomic ion channel activity / clathrin-dependent endocytosis of virus by host cell / mRNA (nucleoside-2'-O-)-methyltransferase activity / protease binding / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / membrane => GO:0016020 / RNA helicase activity / host cell endoplasmic reticulum membrane / protein dimerization activity / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / RNA helicase / induction by virus of host autophagy / viral RNA genome replication / serine-type endopeptidase activity / RNA-dependent RNA polymerase activity / virus-mediated perturbation of host defense response / fusion of virus membrane with host endosome membrane / viral envelope / calcium ion binding / host cell nucleus / virion attachment to host cell / structural molecule activity / virion membrane / proteolysis / extracellular space / extracellular region / ATP binding / membrane / metal ion binding
Similarity search - Function
Pancreatic trypsin inhibitor Kunitz domain / Factor Xa Inhibitor / Proteinase inhibitor I2, Kunitz, conserved site / Pancreatic trypsin inhibitor (Kunitz) family signature. / BPTI/Kunitz family of serine protease inhibitors. / Pancreatic trypsin inhibitor Kunitz domain / Kunitz/Bovine pancreatic trypsin inhibitor domain / Pancreatic trypsin inhibitor (Kunitz) family profile. / Pancreatic trypsin inhibitor Kunitz domain superfamily / : ...Pancreatic trypsin inhibitor Kunitz domain / Factor Xa Inhibitor / Proteinase inhibitor I2, Kunitz, conserved site / Pancreatic trypsin inhibitor (Kunitz) family signature. / BPTI/Kunitz family of serine protease inhibitors. / Pancreatic trypsin inhibitor Kunitz domain / Kunitz/Bovine pancreatic trypsin inhibitor domain / Pancreatic trypsin inhibitor (Kunitz) family profile. / Pancreatic trypsin inhibitor Kunitz domain superfamily / : / Flavivirus capsid protein C superfamily / RNA-directed RNA polymerase, thumb domain, Flavivirus / Flavivirus RNA-directed RNA polymerase, thumb domain / Flavivirus non-structural protein NS2B / Flavivirus envelope glycoprotein E, stem/anchor domain / : / Flavivirus NS3 helicase, C-terminal helical domain / Genome polyprotein, Flavivirus / Flavivirus non-structural protein NS4A / Flavivirus non-structural protein NS2B / Flavivirus capsid protein C / Flavivirus non-structural protein NS4B / mRNA cap 0/1 methyltransferase / Flavivirus capsid protein C / Flavivirus non-structural protein NS4B / Flavivirus non-structural protein NS4A / Flavivirus NS2B domain profile. / mRNA cap 0 and cap 1 methyltransferase (EC 2.1.1.56 and EC 2.1.1.57) domain profile. / Flavivirus non-structural protein NS2A / Flavivirus non-structural protein NS2A / Flavivirus NS3, petidase S7 / Peptidase S7, Flavivirus NS3 serine protease / Flavivirus NS3 protease (NS3pro) domain profile. / RNA-directed RNA polymerase, flavivirus / Flavivirus RNA-directed RNA polymerase, fingers and palm domains / Flavivirus non-structural Protein NS1 / Flavivirus non-structural protein NS1 / Envelope glycoprotein M, flavivirus / Flavivirus envelope glycoprotein M / Envelope glycoprotein M superfamily, flavivirus / Flavivirus polyprotein propeptide / Flavivirus polyprotein propeptide superfamily / Flavivirus polyprotein propeptide / Flaviviral glycoprotein E, central domain, subdomain 1 / Flaviviral glycoprotein E, central domain, subdomain 2 / Flavivirus envelope glycoprotein E, Stem/Anchor domain / Flavivirus glycoprotein E, immunoglobulin-like domain / Flavivirus envelope glycoprotein E, Stem/Anchor domain superfamily / Flavivirus glycoprotein, immunoglobulin-like domain / Flavivirus glycoprotein central and dimerisation domain / Flavivirus glycoprotein, central and dimerisation domains / Ribosomal RNA methyltransferase, FtsJ domain / FtsJ-like methyltransferase / Flavivirus/Alphavirus glycoprotein, immunoglobulin-like domain superfamily / Flavivirus glycoprotein, central and dimerisation domain superfamily / Flaviviral glycoprotein E, dimerisation domain / DEAD box, Flavivirus / Flavivirus DEAD domain / Few Secondary Structures / Irregular / helicase superfamily c-terminal domain / Immunoglobulin E-set / Superfamilies 1 and 2 helicase C-terminal domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / RNA-directed RNA polymerase, catalytic domain / RdRp of positive ssRNA viruses catalytic domain profile. / S-adenosyl-L-methionine-dependent methyltransferase superfamily / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / DNA/RNA polymerase superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
PTI protein / Genome polyprotein / Pancreatic trypsin inhibitor / Core protein
Similarity search - Component
Biological speciesDengue virus 4
Bos taurus (cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.6 Å
AuthorsPhoo, W.W. / El Sahili, A.
Funding support Singapore, 4items
OrganizationGrant numberCountry
START UP GRANT Singapore
CBRG14MAY051 Singapore
CBRG/0103/2016 Singapore
National Research Foundation (Singapore)CRP001-063 Singapore
CitationJournal: To Be Published
Title: Crystal structures of unlinked full length NS3 from Dengue virus provide insights into dynamics of protease domain
Authors: Phoo, W.W. / Sahili, A.E. / Zhang, Z.Z. / Chen, M.W. / Lescar, J. / Vasudevan, S. / Luo, D.
History
DepositionNov 28, 2017Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jan 2, 2019Provider: repository / Type: Initial release
Revision 1.1Nov 22, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
B: Peptidase S7
A: FLAVIVIRUS_NS2B
I: PTI protein


Theoretical massNumber of molelcules
Total (without water)81,8203
Polymers81,8203
Non-polymers00
Water362
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4800 Å2
ΔGint-31 kcal/mol
Surface area31560 Å2
MethodPISA
Unit cell
Length a, b, c (Å)53.018, 87.493, 86.455
Angle α, β, γ (deg.)90.00, 98.25, 90.00
Int Tables number4
Space group name H-MP1211

-
Components

#1: Protein Peptidase S7


Mass: 69517.266 Da / Num. of mol.: 1 / Fragment: UNP residues 1475-2092
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Dengue virus 4 / Production host: Escherichia coli (E. coli) / References: UniProt: F8TEL4
#2: Protein FLAVIVIRUS_NS2B


Mass: 5930.479 Da / Num. of mol.: 1 / Fragment: UNP residues 1393-1439
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Dengue virus 4 / Production host: Escherichia coli (E. coli) / References: UniProt: W0LLP9
#3: Protein PTI protein / Pancreatic Trypsin Inhibitor


Mass: 6372.435 Da / Num. of mol.: 1 / Fragment: UNP residues 36-90
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bos taurus (cattle) / Gene: PTI / Production host: Escherichia coli (E. coli) / References: UniProt: A6QPK7, UniProt: P00974*PLUS
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 2.49 Å3/Da / Density % sol: 50.57 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 6 / Details: 0.1M MES pH 6.0, 12% PEG4000 / PH range: 6.0-7.0

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 2M-F / Detector: PIXEL / Date: Nov 29, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.6→45 Å / Num. obs: 24153 / % possible obs: 99.8 % / Redundancy: 3.8 % / Biso Wilson estimate: 54.01 Å2 / CC1/2: 0.997 / Rmerge(I) obs: 0.082 / Rpim(I) all: 0.075 / Rrim(I) all: 0.112 / Net I/σ(I): 10.2
Reflection shellResolution: 2.6→2.73 Å / Redundancy: 4 % / Rmerge(I) obs: 0.803 / Mean I/σ(I) obs: 1.5 / Num. unique obs: 3202 / CC1/2: 0.738 / Rpim(I) all: 0.727 / Rrim(I) all: 1.088 / % possible all: 99.9

-
Processing

Software
NameVersionClassification
PHENIX(1.14_3260: ???)refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2VBC

2vbc


Resolution: 2.6→44.998 Å / SU ML: 0.39 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 28.87 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2402 1175 4.87 %Randon Selection
Rwork0.2205 ---
obs0.2215 24103 99.63 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.6→44.998 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5276 0 0 2 5278
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0035395
X-RAY DIFFRACTIONf_angle_d0.6847327
X-RAY DIFFRACTIONf_dihedral_angle_d16.0743253
X-RAY DIFFRACTIONf_chiral_restr0.046808
X-RAY DIFFRACTIONf_plane_restr0.005959
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.6-2.71830.34961410.33292845X-RAY DIFFRACTION100
2.7183-2.86160.28981450.29662859X-RAY DIFFRACTION99
2.8616-3.04090.30861530.28132833X-RAY DIFFRACTION100
3.0409-3.27560.27211270.27522888X-RAY DIFFRACTION100
3.2756-3.60510.28671510.23492862X-RAY DIFFRACTION100
3.6051-4.12650.23871460.20772876X-RAY DIFFRACTION100
4.1265-5.19770.19791590.17892850X-RAY DIFFRACTION100
5.1977-45.00450.20651530.18882915X-RAY DIFFRACTION99
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
11.93390.2839-0.59972.1043-1.9623.7134-0.03710.4578-0.11450.05770.2304-0.0952-0.4841-1.8408-0.14180.67240.00830.01691.19360.12570.527263.3057-1.0851.875
22.2973-0.77430.04781.25870.73790.97340.0888-0.2877-0.33850.1441-0.05990.04980.1011-0.1138-0.04520.3595-0.0478-0.01220.35760.05910.403352.40884.216317.1485
31.22260.05260.40932.3671.36812.16940.13140.041-0.2169-0.4524-0.26540.2761-0.1946-0.23290.09690.38240.0472-0.00450.30980.01580.375748.4081.0281-3.8818
40.0068-0.00260.01440.0618-0.06210.07960.32350.45690.29-0.25620.02450.1879-0.0464-0.2285-0.33320.9099-0.47690.06821.2179-0.10530.878864.2817-13.446942.8208
51.72561.51680.92844.2612-0.86651.4637-0.5885-0.158-0.21020.0573-0.31910.3390.3071-0.48510.3640.8568-0.4509-0.07331.61650.03030.903955.9377-11.124555.685
61.5630.0082-1.22390.11720.07981.0280.0066-0.0067-0.2192-0.1309-0.228-0.07160.54530.23760.16131.326-0.0694-0.01251.29750.10941.053655.2136-6.304667.9539
72.0938-0.2972-0.60812.1747-0.99523.06460.42450.0383-0.10750.08030.0947-0.089-0.1649-0.1988-0.18651.1645-0.12790.05071.1256-0.00220.649268.30473.896968.6725
85.0078-0.42640.17252.2504-0.70640.2919-0.0459-0.0898-0.2957-0.11810.0107-0.50090.10810.80640.00511.4475-0.05450.29550.85230.21050.608573.987112.451750.9158
90.7124-0.5019-1.10380.95310.65232.161-0.0826-0.16970.36760.4653-0.4492-0.1524-0.45561.0770.31580.8493-0.2404-0.06191.33490.52860.774986.5766-0.253247.0147
100.5305-0.1865-0.7051.00370.9281.4174-0.60360.4715-0.1165-0.2444-0.4989-0.57990.7820.4601-0.21440.7405-0.29530.35841.41150.45320.74489.2384-8.096944.1449
112.6940.7766-0.14471.2864-1.01571.9261-0.08240.3577-0.5167-0.7141-0.4104-0.6333-0.11490.60830.41370.7612-0.02020.20361.13630.27980.809585.2994-3.554840.965
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'B' and (resid 4 through 163 )
2X-RAY DIFFRACTION2chain 'B' and (resid 164 through 429 )
3X-RAY DIFFRACTION3chain 'B' and (resid 430 through 618 )
4X-RAY DIFFRACTION4chain 'A' and (resid 50 through 54 )
5X-RAY DIFFRACTION5chain 'A' and (resid 55 through 59 )
6X-RAY DIFFRACTION6chain 'A' and (resid 60 through 64 )
7X-RAY DIFFRACTION7chain 'A' and (resid 65 through 74 )
8X-RAY DIFFRACTION8chain 'A' and (resid 75 through 86 )
9X-RAY DIFFRACTION9chain 'I' and (resid 1 through 17 )
10X-RAY DIFFRACTION10chain 'I' and (resid 18 through 31 )
11X-RAY DIFFRACTION11chain 'I' and (resid 32 through 55 )

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbjlvh1.pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more