[English] 日本語
Yorodumi
- PDB-3v0a: 2.7 angstrom crystal structure of BoNT/Ai in complex with NTNHA -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 3v0a
Title2.7 angstrom crystal structure of BoNT/Ai in complex with NTNHA
Components
  • BoNT/A
  • Llama antibody F12
  • NTNH
KeywordsTOXIN / Botulinum neurotoxin / Neurotoxin associated protein / Progenitor toxin complex / VHH bound interlocked complex / NTNHA
Function / homology
Function and homology information


bontoxilysin / host cell presynaptic membrane / host cell cytoplasmic vesicle / host cell cytosol / protein transmembrane transporter activity / metalloendopeptidase activity / toxin activity / host cell plasma membrane / proteolysis / zinc ion binding ...bontoxilysin / host cell presynaptic membrane / host cell cytoplasmic vesicle / host cell cytosol / protein transmembrane transporter activity / metalloendopeptidase activity / toxin activity / host cell plasma membrane / proteolysis / zinc ion binding / extracellular region / membrane
Similarity search - Function
Nontoxic nonhaemagglutinin C-terminal / Nontoxic nonhaemagglutinin C-terminal / Clostridium botulinum neurotoxin B, "coiled-coil" domain / Clostridium botulinum neurotoxin b, "coiled-coil" domain / Zincin-like / Metalloproteases ("zincins"), catalytic domain like / Clostridium neurotoxin, translocation / Clostridium neurotoxin, Translocation domain / Clostridium neurotoxin, translocation domain / Clostridial neurotoxin zinc protease ...Nontoxic nonhaemagglutinin C-terminal / Nontoxic nonhaemagglutinin C-terminal / Clostridium botulinum neurotoxin B, "coiled-coil" domain / Clostridium botulinum neurotoxin b, "coiled-coil" domain / Zincin-like / Metalloproteases ("zincins"), catalytic domain like / Clostridium neurotoxin, translocation / Clostridium neurotoxin, Translocation domain / Clostridium neurotoxin, translocation domain / Clostridial neurotoxin zinc protease / Botulinum/Tetanus toxin, catalytic chain / Clostridium neurotoxin, receptor binding N-terminal / Clostridium neurotoxin, receptor-binding C-terminal / Clostridium neurotoxin, C-terminal receptor binding / Clostridium neurotoxin, N-terminal receptor binding / Kunitz inhibitor STI-like superfamily / Trefoil (Acidic Fibroblast Growth Factor, subunit A) - #50 / Trefoil (Acidic Fibroblast Growth Factor, subunit A) / Trefoil / Jelly Rolls - #200 / Neutral zinc metallopeptidases, zinc-binding region signature. / Concanavalin A-like lectin/glucanase domain superfamily / Jelly Rolls / Immunoglobulins / Alpha-Beta Complex / Up-down Bundle / Immunoglobulin-like / Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Botulinum neurotoxin type A / Non-toxic nonhemagglutinin type A / BoNT/A
Similarity search - Component
Biological speciesClostridium botulinum (bacteria)
Lama glama (llama)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.703 Å
AuthorsGu, S. / Rumpel, S. / Zhou, J. / Strotmeier, J. / Bigalke, H. / Perry, K. / Shoemaker, C.B. / Rummel, A. / Jin, R.
CitationJournal: Science / Year: 2012
Title: Botulinum neurotoxin is shielded by NTNHA in an interlocked complex.
Authors: Gu, S. / Rumpel, S. / Zhou, J. / Strotmeier, J. / Bigalke, H. / Perry, K. / Shoemaker, C.B. / Rummel, A. / Jin, R.
History
DepositionDec 7, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 14, 2012Provider: repository / Type: Initial release

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: BoNT/A
B: NTNH
C: Llama antibody F12
hetero molecules


Theoretical massNumber of molelcules
Total (without water)306,87229
Polymers304,0643
Non-polymers2,80826
Water5,296294
1


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8690 Å2
ΔGint-27 kcal/mol
Surface area101760 Å2
MethodPISA
Unit cell
Length a, b, c (Å)156.080, 156.080, 324.603
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number92
Space group name H-MP41212

-
Components

-
Protein , 2 types, 2 molecules AB

#1: Protein BoNT/A / Bont/A1 / Botulinum neurotoxin type A / Neurotoxin A / Neurotoxin BoNT


Mass: 149449.828 Da / Num. of mol.: 1 / Mutation: E224Q,R363A,Y366F
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Clostridium botulinum (bacteria) / Gene: bont/a, boNT/A, bonta / Production host: Escherichia coli (E. coli) / References: UniProt: Q7B8V4, UniProt: P0DPI1*PLUS
#2: Protein NTNH / Type A progenitor toxin nontoxic-nonHA


Mass: 138450.266 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Clostridium botulinum (bacteria) / Gene: ant, ntnh / Production host: Escherichia coli (E. coli) / References: UniProt: Q45914

-
Antibody , 1 types, 1 molecules C

#3: Antibody Llama antibody F12


Mass: 16163.727 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Lama glama (llama) / Production host: Escherichia coli (E. coli)

-
Non-polymers , 5 types, 320 molecules

#4: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn
#5: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Ca
#6: Chemical
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 20 / Source method: obtained synthetically / Formula: SO4
#7: Chemical
ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID / MES (buffer)


Mass: 195.237 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#8: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 294 / 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: 3.25 Å3/Da / Density % sol: 62.16 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.2
Details: 12% PEG MME2000, 16% pentaerythritol propoxylate(5/4 PO/OH), 0.1 M ammonium sulfate and 50mM MES, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.97918 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Mar 12, 2011
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97918 Å / Relative weight: 1
ReflectionResolution: 2.7→49.8 Å / Num. all: 109722 / Num. obs: 109570 / % possible obs: 99.9 % / Observed criterion σ(F): 13.6 / Observed criterion σ(I): 13.6 / Redundancy: 6.2 % / Rmerge(I) obs: 0.127
Reflection shellResolution: 2.7→2.85 Å / Redundancy: 6.1 % / Rmerge(I) obs: 0.768 / Mean I/σ(I) obs: 2.7 / % possible all: 99.8

-
Processing

Software
NameVersionClassification
ADSCQuantumdata collection
PHASERphasing
PHENIX(phenix.refine: 1.7.2_869)refinement
MOSFLMdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.703→49.357 Å / SU ML: 0.79 / Isotropic thermal model: RANDOM / σ(F): 1.35 / Phase error: 23.18 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2239 5474 5 %RANDOM
Rwork0.1759 ---
all0.1783 109722 --
obs0.1783 109570 99.59 %-
Solvent computationShrinkage radii: 0.73 Å / VDW probe radii: 1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 41.598 Å2 / ksol: 0.324 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-7.0759 Å20 Å2-0 Å2
2--7.0759 Å2-0 Å2
3----14.1518 Å2
Refinement stepCycle: LAST / Resolution: 2.703→49.357 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms20719 0 150 294 21163
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00621300
X-RAY DIFFRACTIONf_angle_d1.01728873
X-RAY DIFFRACTIONf_dihedral_angle_d15.347867
X-RAY DIFFRACTIONf_chiral_restr0.0763150
X-RAY DIFFRACTIONf_plane_restr0.0043704
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.7034-2.73420.31441510.28993264X-RAY DIFFRACTION95
2.7342-2.76630.34881820.28393424X-RAY DIFFRACTION100
2.7663-2.80010.35161720.27893441X-RAY DIFFRACTION99
2.8001-2.83550.32411930.26283430X-RAY DIFFRACTION100
2.8355-2.87280.33321800.2653378X-RAY DIFFRACTION100
2.8728-2.91220.30631880.25863426X-RAY DIFFRACTION100
2.9122-2.95380.31761910.25833421X-RAY DIFFRACTION100
2.9538-2.99780.3271990.24493427X-RAY DIFFRACTION100
2.9978-3.04470.29281760.22713419X-RAY DIFFRACTION100
3.0447-3.09460.26811850.23213435X-RAY DIFFRACTION100
3.0946-3.14790.29521830.22763429X-RAY DIFFRACTION100
3.1479-3.20520.26991790.22153448X-RAY DIFFRACTION100
3.2052-3.26680.2511990.21033442X-RAY DIFFRACTION100
3.2668-3.33350.30161860.20643440X-RAY DIFFRACTION100
3.3335-3.40590.25361870.20223445X-RAY DIFFRACTION100
3.4059-3.48510.24621880.19243445X-RAY DIFFRACTION100
3.4851-3.57230.24681890.18293452X-RAY DIFFRACTION100
3.5723-3.66880.22491660.17693482X-RAY DIFFRACTION100
3.6688-3.77680.20931930.16553465X-RAY DIFFRACTION100
3.7768-3.89860.19771750.15333469X-RAY DIFFRACTION100
3.8986-4.03790.1931810.14033468X-RAY DIFFRACTION100
4.0379-4.19950.18341770.12913498X-RAY DIFFRACTION100
4.1995-4.39050.17271800.1253503X-RAY DIFFRACTION100
4.3905-4.62180.14561860.1173508X-RAY DIFFRACTION100
4.6218-4.91110.15641790.11933525X-RAY DIFFRACTION100
4.9111-5.28990.18821830.1353509X-RAY DIFFRACTION100
5.2899-5.82150.19271570.16443584X-RAY DIFFRACTION100
5.8215-6.66220.23241780.18183552X-RAY DIFFRACTION100
6.6622-8.38690.19391880.15493628X-RAY DIFFRACTION100
8.3869-49.3650.19182030.17013739X-RAY DIFFRACTION98
Refinement TLS params.

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

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
10.95121.49610.08492.8822-0.48171.3067-0.16290.30730.1921-0.4760.0125-0.2574-0.18450.54640.11720.3766-0.20220.04330.6640.02710.3043110.550785.6897.2829
20.99710.17420.25631.2053-0.20291.0782-0.02140.00160.20390.1393-0.0387-0.1403-0.2330.35610.04280.2611-0.16980.03560.5247-0.06120.2437109.006581.893324.7236
30.89240.52990.78180.71910.02582.10760.1999-0.1099-0.06450.0262-0.0779-0.2559-0.13320.33180.00030.2159-0.08560.00820.5681-0.06630.2499112.260259.529429.6051
40.48120.18630.37681.25310.0490.73360.07820.01220.02630.0086-0.0167-0.10870.05210.2242-0.06220.2119-0.00360.05690.4891-0.02580.2121100.575555.36718.8927
50.25140.37621.04960.76371.223.32820.02340.02940.01170.0750.0805-0.040.04640.3455-0.11540.1795-0.03130.0230.377-0.0280.190699.85354.767537.4286
60.32740.25750.38060.40540.13891.0604-0.04-0.03460.0801-0.00790.06350.1699-0.0676-0.2004-0.02150.16780.0130.04560.39530.05880.271160.486265.74131.2473
73.48191.03473.11082.8727-1.74236.37190.268-0.09520.10320.168-0.23110.30120.2982-0.3378-0.07610.33810.09560.14730.4563-0.0420.302549.648969.126754.3207
82.34990.1414-1.08860.7061-0.02151.9320.10.2154-0.00210.07120.04980.1485-0.0263-0.3379-0.13520.2677-0.05920.0210.16150.07050.161643.828329.977957.9552
90.75450.17750.36571.21120.09351.0005-0.00170.053-0.0422-0.01930.05070.08610.0678-0.0933-0.02790.07220.0040.09070.25570.040.071964.73242.089242.9586
101.4704-0.4382-0.23462.9572-1.34192.06550.1081-0.09770.44430.24310.0714-0.0894-0.5326-0.0615-0.1090.289-0.03850.03850.2733-0.08080.264381.745979.281952.0714
113.46140.83070.7212.5378-1.28231.05630.6705-0.0811.26-0.0963-0.3288-0.2365-1.66220.6041-0.35041.2109-0.58540.24160.99660.37471.3841123.1994114.3455-9.2465
123.7567-2.30580.0912.8063-1.84982.31290.3771.36820.387-0.6255-0.7225-0.01450.4782-0.00060.27341.0203-0.18950.29711.5943-0.09551.2732127.167698.1285-28.3743
132.6754-0.1009-0.12610.67631.59375.86490.34-0.03490.5817-0.4545-0.3403-0.6351-0.85330.9549-0.1661.057-0.62540.22441.13450.14130.8508127.9415106.5982-7.6077
144.6137-1.1719-2.36662.5944-0.47068.78690.33450.8795-0.019-0.7526-0.5530.0102-0.0778-0.73230.24581.188-0.2297-0.07231.35960.05510.6559116.4608100.2188-15.4438
156.13273.24483.34593.59021.04582.3699-0.52260.715-0.132-0.55080.06690.01350.4385-0.4560.40160.577-0.40530.181.61870.08270.619123.458495.9437-5.9815
162.7239-0.52781.5261.97180.04080.9155-0.03220.6951-0.3987-1.00170.0051-0.6335-0.37041.27580.05371.0678-0.21530.31031.3577-0.14561.1647124.270689.6305-14.4307
173.60721.7616-0.63763.0153-1.51030.78030.0330.1980.1342-0.1395-0.3504-0.8523-0.62640.80810.28010.8971-0.55240.23351.58220.11180.9018133.8699104.3682-6.824
183.2380.5857-0.01522.6812-1.74471.1784-0.09740.8103-0.0436-0.4883-0.0466-0.817-0.15140.9030.17531.0783-0.53810.47751.574-0.040.8843130.6044100.5018-14.2257
190.336-0.1829-0.8170.45050.51622.2460.05660.5848-0.2266-1.1709-0.3329-0.6871-0.5170.77090.18911.2369-0.30070.13961.69520.0960.6997120.096597.9899-15.8908
202.15240.5695-1.01713.18431.27745.73690.83810.538-0.0236-0.9281-0.31970.1916-0.65190.4757-0.54931.3102-0.2632-0.16771.38890.21030.5978116.3865105.4665-13.7236
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resseq 1:99)
2X-RAY DIFFRACTION2chain 'A' and (resseq 100:412)
3X-RAY DIFFRACTION3chain 'A' and (resseq 413:495)
4X-RAY DIFFRACTION4chain 'A' and (resseq 496:628)
5X-RAY DIFFRACTION5chain 'A' and (resseq 629:825)
6X-RAY DIFFRACTION6chain 'A' and (resseq 826:1194)
7X-RAY DIFFRACTION7chain 'A' and (resseq 1195:1295)
8X-RAY DIFFRACTION8chain 'B' and (resseq 1:536)
9X-RAY DIFFRACTION9chain 'B' and (resseq 537:910)
10X-RAY DIFFRACTION10chain 'B' and (resseq 911:1194)
11X-RAY DIFFRACTION11chain 'C' and (resseq 0:7)
12X-RAY DIFFRACTION12chain 'C' and (resseq 8:16)
13X-RAY DIFFRACTION13chain 'C' and (resseq 17:33)
14X-RAY DIFFRACTION14chain 'C' and (resseq 34:44)
15X-RAY DIFFRACTION15chain 'C' and (resseq 45:59)
16X-RAY DIFFRACTION16chain 'C' and (resseq 60:67)
17X-RAY DIFFRACTION17chain 'C' and (resseq 68:76)
18X-RAY DIFFRACTION18chain 'C' and (resseq 77:83)
19X-RAY DIFFRACTION19chain 'C' and (resseq 84:101)
20X-RAY DIFFRACTION20chain 'C' and (resseq 102:118)

+
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://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