[English] 日本語
Yorodumi
- PDB-6osv: Potent and Selective Antitumor Antibody Targeting a Membrane-Prox... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 6osv
TitlePotent and Selective Antitumor Antibody Targeting a Membrane-Proximal Epitope of ROR2
Components
  • Antibody heavy chain variable region
  • Antibody light chain variable region
  • Tyrosine-protein kinase transmembrane receptor ROR2
Keywordsimmune sytem/transferase / Single chain Fv / ScFv / Antibody / ROR2 / Kringle domain / receptor tyrosine kinase-like orphan receptor / Phage display / IMMUNE SYSTEM / immune sytem-transferase complex
Function / homology
Function and homology information


regulation of synaptic signaling by nitric oxide / macrophage migration / WNT5A-dependent internalization of FZD2, FZD5 and ROR2 / positive regulation of macrophage differentiation / Wnt-protein binding / male genitalia development / astrocyte development / mitogen-activated protein kinase kinase kinase binding / PCP/CE pathway / regulation of postsynapse organization ...regulation of synaptic signaling by nitric oxide / macrophage migration / WNT5A-dependent internalization of FZD2, FZD5 and ROR2 / positive regulation of macrophage differentiation / Wnt-protein binding / male genitalia development / astrocyte development / mitogen-activated protein kinase kinase kinase binding / PCP/CE pathway / regulation of postsynapse organization / bone mineralization / coreceptor activity / cell surface receptor protein tyrosine kinase signaling pathway / transmembrane receptor protein tyrosine kinase activity / positive regulation of synaptic transmission, glutamatergic / clathrin-coated endocytic vesicle membrane / receptor protein-tyrosine kinase / Wnt signaling pathway / positive regulation of neuron projection development / postsynapse / microtubule / receptor complex / positive regulation of cell migration / phosphorylation / neuronal cell body / glutamatergic synapse / dendrite / cell surface / signal transduction / ATP binding / metal ion binding / plasma membrane
Similarity search - Function
Tyrosine-protein kinase, receptor ROR / Plasminogen Kringle 4 / Plasminogen Kringle 4 / Frizzled domain / Frizzled cysteine-rich domain superfamily / Fz domain / Frizzled (fz) domain profile. / Kringle domain / Kringle / Kringle, conserved site ...Tyrosine-protein kinase, receptor ROR / Plasminogen Kringle 4 / Plasminogen Kringle 4 / Frizzled domain / Frizzled cysteine-rich domain superfamily / Fz domain / Frizzled (fz) domain profile. / Kringle domain / Kringle / Kringle, conserved site / Kringle superfamily / Kringle domain signature. / Kringle domain profile. / Kringle domain / Immunoglobulin I-set / Immunoglobulin I-set domain / Kringle-like fold / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Tyrosine protein kinases specific active-site signature. / Immunoglobulin subtype / Immunoglobulin / Tyrosine-protein kinase, active site / Protein tyrosine and serine/threonine kinase / Serine-threonine/tyrosine-protein kinase, catalytic domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
Tyrosine-protein kinase transmembrane receptor ROR2
Similarity search - Component
Biological speciesOryctolagus cuniculus (rabbit)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.34 Å
AuthorsPark, H. / Rader, C.
CitationJournal: J.Biol.Chem. / Year: 2020
Title: Affinity maturation, humanization, and co-crystallization of a rabbit anti-human ROR2 monoclonal antibody for therapeutic applications.
Authors: Goydel, R.S. / Weber, J. / Peng, H. / Qi, J. / Soden, J. / Freeth, J. / Park, H. / Rader, C.
History
DepositionMay 2, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 1, 2020Provider: repository / Type: Initial release
Revision 1.1May 13, 2020Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
L: Antibody light chain variable region
K: Tyrosine-protein kinase transmembrane receptor ROR2
H: Antibody heavy chain variable region


Theoretical massNumber of molelcules
Total (without water)36,1113
Polymers36,1113
Non-polymers00
Water6,089338
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3280 Å2
ΔGint-10 kcal/mol
Surface area13700 Å2
MethodPISA
Unit cell
Length a, b, c (Å)46.109, 60.105, 102.756
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

-
Components

#1: Antibody Antibody light chain variable region


Mass: 11818.117 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Oryctolagus cuniculus (rabbit) / Production host: Escherichia coli (E. coli)
#2: Protein Tyrosine-protein kinase transmembrane receptor ROR2 / Neurotrophic tyrosine kinase / receptor-related 2


Mass: 10932.098 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ROR2, NTRKR2 / Production host: Escherichia coli (E. coli)
References: UniProt: Q01974, receptor protein-tyrosine kinase
#3: Antibody Antibody heavy chain variable region


Mass: 13360.752 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Oryctolagus cuniculus (rabbit) / Production host: Escherichia coli (E. coli)
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 338 / 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: 2.13 Å3/Da / Density % sol: 37.61 %
Crystal growTemperature: 294 K / Method: vapor diffusion, hanging drop / pH: 7
Details: 0.01 M Magnesium chloride hexahydrate, 0.005 M Nickel(II) chloride 0.1 M HEPES sodium pH 7.0, 15% w/v Polyethylene glycol 3,350

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 5.0.2 / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Apr 7, 2017
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.34→51.881 Å / Num. obs: 55957 / % possible obs: 91.5 % / Redundancy: 5.9 % / CC1/2: 1 / Rmerge(I) obs: 0.03314 / Rpim(I) all: 0.01436 / Rrim(I) all: 0.0362 / Net I/σ(I): 22
Reflection shellResolution: 1.34→1.406 Å / Rmerge(I) obs: 0.6778 / Mean I/σ(I) obs: 1.23 / Num. unique obs: 2799 / CC1/2: 0.635 / Rpim(I) all: 0.4093 / Rrim(I) all: 0.7953

-
Processing

Software
NameVersionClassification
PHENIX(1.15.2_3472: ???)refinement
XDSdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.34→51.378 Å / SU ML: 0.13 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 21.95
RfactorNum. reflection% reflection
Rfree0.189 1119 2 %
Rwork0.162 --
obs0.1625 55957 86.2 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 1.34→51.378 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2362 0 0 338 2700
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0092446
X-RAY DIFFRACTIONf_angle_d1.0433323
X-RAY DIFFRACTIONf_dihedral_angle_d9.671189
X-RAY DIFFRACTIONf_chiral_restr0.085350
X-RAY DIFFRACTIONf_plane_restr0.007430
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.34-1.4010.3058490.25942419X-RAY DIFFRACTION31
1.401-1.47490.24561080.23155315X-RAY DIFFRACTION68
1.4749-1.56730.22451490.19457247X-RAY DIFFRACTION92
1.5673-1.68830.21191580.16867801X-RAY DIFFRACTION99
1.6883-1.85820.18911610.1687864X-RAY DIFFRACTION99
1.8582-2.12710.17981620.16247941X-RAY DIFFRACTION100
2.1271-2.680.18351630.17067974X-RAY DIFFRACTION100
2.68-51.41580.18451690.1498277X-RAY DIFFRACTION100
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)
11.13680.7169-1.36155.6826-0.01331.7777-0.23090.28860.4031-0.24720.00850.3624-0.0575-0.33760.09230.25390.0851-0.08530.2558-0.01160.4002-27.22834.0371.1299
20.39320.12450.34312.07451.10321.37310.0034-0.01310.0131-0.0628-0.03670.0928-0.0293-0.0387-0.01150.42550.0574-0.020.2213-0.17450.8332-17.406922.94488.7834
30.5160.65320.04181.1643-0.22340.24210.0046-0.1630.35060.0448-0.00970.2133-0.1223-0.17490.07650.22390.03630.00330.1998-0.06460.3151-25.5020.99658.6516
40.5391-0.0720.10141.1707-0.41711.41990.0421-0.02250.5626-0.1133-0.1574-0.0938-0.25720.0424-0.00420.26120.0281-0.00460.13350.01730.2927-12.69723.97695.0785
51.1929-0.1559-0.10250.9331-0.13080.845-0.0922-0.35190.38690.1418-0.0510.1268-0.2954-0.1167-0.00430.24880.0304-0.02640.2029-0.08420.267-16.48531.160715.5465
62.91512.53090.92683.68021.05531.5578-0.1044-0.07950.20350.03440.150.0712-0.2436-0.23220.01060.30970.071-0.04570.2318-0.08380.422-22.3787.675612.9768
70.54390.4055-0.29852.47950.07280.67290.0868-0.02380.35230.06-0.1089-0.2325-0.1671-0.0272-0.02960.26270.0174-0.0260.1468-0.0010.3797-15.02997.64174.9999
80.84860.66430.18331.39440.22551.09070.06570.02240.4243-0.1706-0.20490.0098-0.22890.0101-0.01180.23880.0087-0.00940.14480.0170.3346-16.53934.63222.9777
98.67882.517-1.67439.0571-2.14084.4411-0.26280.2071-0.7195-0.1004-0.01450.07170.7969-0.4001-0.1740.4377-0.072-0.07550.43660.18190.34920.1349-32.028726.8296
100.42240.1071-0.31180.18340.0830.43370.2301-0.131-0.08780.313-0.12-0.1636-0.31730.31260.5760.2535-0.00040.09250.50980.34520.2102-2.0402-26.700822.5233
110.4959-0.1709-0.86750.0590.29921.61640.0596-0.23120.04070.1225-0.07680.0282-0.039-0.0456-0.15980.65690.150.25390.49380.09060.2097-12.77-20.034529.875
120.8156-0.1451-0.00361.3306-0.22630.8023-0.012-0.276-0.26010.0132-0.06790.22030.063-0.07430.02130.16560.0080.00410.1830.01410.1722-9.1675-18.170213.1844
134.05720.48110.47232.19320.25863.0915-0.1178-0.22310.10310.2224-0.04110.1236-0.40550.4795-0.00380.2241-0.0391-0.00920.32250.10560.1733-3.3936-21.881519.4151
143.8687-1.8543-0.96682.7718-0.97531.3924-0.0494-0.42590.00290.6195-0.008-0.1859-0.15750.01160.06090.29890.0102-0.02310.33590.06040.1484-6.8888-18.002223.3445
151.62350.1775-1.25660.11510.2722.716-0.0373-0.31070.14040.38130.07030.163-0.2458-0.1708-0.050.39210.11830.06520.3758-0.02290.157-14.7153-10.559124.6411
162.4187-3.68480.70217.2848-1.14380.2019-0.037-0.2725-0.12910.31950.0263-0.2159-0.1571-0.0751-0.00440.38310.02-0.0750.36130.10090.1832-2.6656-23.717928.9305
171.75120.2257-0.82951.0854-1.58013.65490.1659-0.25580.44970.13330.024-0.1103-0.58440.09180.12580.2647-0.0190.01860.1727-0.00290.29041.3091-0.32220.6841
180.02310.08010.14720.27620.50820.93530.05080.29430.1568-0.0550.07840.1324-0.1364-0.16930.56350.24530.06380.04930.53030.18980.2505-1.4197-2.1666-21.3242
191.1998-0.24880.44411.29641.2291.5740.0970.33360.32460.0618-0.0743-0.11450.00880.1849-0.05060.19030.02110.00520.2320.05750.18821.2418-6.8243-9.4273
200.9820.019-0.36041.0673-0.02451.01830.10970.16120.24830.0004-0.0658-0.0074-0.12220.02570.03410.16330.01390.00980.17070.04440.1821-5.9688-5.5199-1.4306
211.8791-2.6733-0.11749.8915-0.41641.13790.08480.29480.3143-0.2552-0.12210.2753-0.16-0.04370.00180.19170.043-0.01190.23370.07910.2227-14.7913-3.3199-6.7828
220.65670.0187-0.2470.6028-0.07040.81120.02060.3396-0.0178-0.03560.0182-0.02030.0026-0.08960.00320.13860.0051-0.00510.23870.03020.1323-5.9421-12.4009-8.2697
231.1361-0.2701-0.6230.604-0.09110.40970.0520.18310.39630.0349-0.1015-0.1046-0.1692-0.07240.04050.17370.014-0.00950.17850.0480.2249-5.9008-3.6244-1.2272
241.12430.6039-0.05640.6109-1.16065.6775-0.0540.42170.3534-0.2884-0.0931-0.0865-0.46240.069-0.22080.30550.1320.08060.50130.29920.4381-2.96113.8539-17.5412
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(chain H and resid 0:9)
2X-RAY DIFFRACTION2(chain H and resid 10:13)
3X-RAY DIFFRACTION3(chain H and resid 14:32)
4X-RAY DIFFRACTION4(chain H and resid 33:50)
5X-RAY DIFFRACTION5(chain H and resid 51:73)
6X-RAY DIFFRACTION6(chain H and resid 74:84)
7X-RAY DIFFRACTION7(chain H and resid 85:97)
8X-RAY DIFFRACTION8(chain H and resid 98:118)
9X-RAY DIFFRACTION9(chain K and resid 314:317)
10X-RAY DIFFRACTION10(chain K and resid 318:331)
11X-RAY DIFFRACTION11(chain K and resid 332:336)
12X-RAY DIFFRACTION12(chain K and resid 337:361)
13X-RAY DIFFRACTION13(chain K and resid 362:372)
14X-RAY DIFFRACTION14(chain K and resid 373:380)
15X-RAY DIFFRACTION15(chain K and resid 381:385)
16X-RAY DIFFRACTION16(chain K and resid 386:394)
17X-RAY DIFFRACTION17(chain L and resid 0:10)
18X-RAY DIFFRACTION18(chain L and resid 11:17)
19X-RAY DIFFRACTION19(chain L and resid 18:24)
20X-RAY DIFFRACTION20(chain L and resid 25:41)
21X-RAY DIFFRACTION21(chain L and resid 42:48)
22X-RAY DIFFRACTION22(chain L and resid 49:78)
23X-RAY DIFFRACTION23(chain L and resid 79:105)
24X-RAY DIFFRACTION24(chain L and resid 106:110)

+
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