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- PDB-6kxk: BON1 -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 6kxk
TitleBON1
Components(Protein BONZAI ...) x 5
KeywordsLIPID BINDING PROTEIN / Copines / BON1 / C2 domain / vWA domain / Phospholipid / Membrane.
Function / homology
Function and homology information


response to humidity / plasmodesma / calcium-dependent phospholipid binding / plastid / response to temperature stimulus / positive regulation of cell size / defense response / metal ion binding / plasma membrane
Similarity search - Function
Copine, C2B domain / Copine / Copine, C-terminal / Copine / C2 domain / Protein kinase C conserved region 2 (CalB) / C2 domain / C2 domain profile. / von Willebrand factor (vWF) type A domain / VWFA domain profile. ...Copine, C2B domain / Copine / Copine, C-terminal / Copine / C2 domain / Protein kinase C conserved region 2 (CalB) / C2 domain / C2 domain profile. / von Willebrand factor (vWF) type A domain / VWFA domain profile. / von Willebrand factor, type A / von Willebrand factor A-like domain superfamily / C2 domain superfamily
Similarity search - Domain/homology
DI(HYDROXYETHYL)ETHER / TRIETHYLENE GLYCOL / Protein BONZAI 1
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å
AuthorsWang, Q.C. / Jiang, M.Q. / Isupov, M.N. / Sun, L.F. / Wu, Y.K.
CitationJournal: To be published
Title: Crystal Structure of an Arabidopsis Copine providing insights into this protein family
Authors: Wang, Q.C. / Jiang, M.Q. / Isupov, M.N. / Sun, L.F. / Wu, Y.K.
History
DepositionSep 12, 2019Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Sep 16, 2020Provider: repository / Type: Initial release
Revision 1.1Mar 27, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Protein BONZAI 1
B: Protein BONZAI 1
C: Protein BONZAI 1
D: Protein BONZAI 1
E: Protein BONZAI 1
F: Protein BONZAI 1
G: Protein BONZAI 1
H: Protein BONZAI 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)493,522144
Polymers482,9138
Non-polymers10,608136
Water10,863603
1
A: Protein BONZAI 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)63,18826
Polymers61,0601
Non-polymers2,12825
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Protein BONZAI 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)59,77018
Polymers58,4201
Non-polymers1,34917
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Protein BONZAI 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)62,55320
Polymers61,0601
Non-polymers1,49319
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: Protein BONZAI 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)63,09827
Polymers61,0601
Non-polymers2,03826
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
E: Protein BONZAI 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)61,79813
Polymers60,8151
Non-polymers98312
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
6
F: Protein BONZAI 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)62,78025
Polymers61,0601
Non-polymers1,72024
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
7
G: Protein BONZAI 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)58,7046
Polymers58,3631
Non-polymers3405
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
8
H: Protein BONZAI 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)61,6319
Polymers61,0741
Non-polymers5578
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)122.284, 118.716, 222.253
Angle α, β, γ (deg.)90.000, 90.200, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12A
22C
13A
23D
14A
24E
15A
25F
16A
26G
17A
27H
18B
28C
19B
29D
110B
210E
111B
211F
112B
212G
113B
213H
114C
214D
115C
215E
116C
216F
117C
217G
118C
218H
119D
219E
120D
220F
121D
221G
122D
222H
123E
223F
124E
224G
125E
225H
126F
226G
127F
227H
128G
228H

NCS domain segments:

Component-ID: 0 / Refine code: 0

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11GLYGLYARGARGAA16 - 54226 - 552
21GLYGLYARGARGBB16 - 5421 - 527
12GLYGLYASNASNAA-9 - 5431 - 553
22GLYGLYASNASNCC-9 - 5431 - 553
13GLYGLYASNASNAA-9 - 5431 - 553
23GLYGLYASNASNDD-9 - 5431 - 553
14SERSERASNASNAA-6 - 5434 - 553
24SERSERASNASNEE-6 - 5431 - 550
15GLYGLYASNASNAA-9 - 5431 - 553
25GLYGLYASNASNFF-9 - 5431 - 553
16LEULEUARGARGAA17 - 54227 - 552
26LEULEUARGARGGG17 - 5421 - 526
17GLYGLYASNASNAA-9 - 5431 - 553
27GLYGLYASNASNHH-9 - 5431 - 553
18GLYGLYARGARGBB16 - 5421 - 527
28GLYGLYARGARGCC16 - 54226 - 552
19GLYGLYARGARGBB16 - 5421 - 527
29GLYGLYARGARGDD16 - 54226 - 552
110GLYGLYARGARGBB16 - 5421 - 527
210GLYGLYARGARGEE16 - 54223 - 549
111GLYGLYARGARGBB16 - 5421 - 527
211GLYGLYARGARGFF16 - 54226 - 552
112LEULEUARGARGBB17 - 5422 - 527
212LEULEUARGARGGG17 - 5421 - 526
113GLYGLYARGARGBB16 - 5421 - 527
213GLYGLYARGARGHH13 - 54223 - 552
114GLYGLYASNASNCC-9 - 5431 - 553
214GLYGLYASNASNDD-9 - 5431 - 553
115SERSERASNASNCC-6 - 5434 - 553
215SERSERASNASNEE-6 - 5431 - 550
116GLYGLYASNASNCC-9 - 5431 - 553
216GLYGLYASNASNFF-9 - 5431 - 553
117LEULEUARGARGCC17 - 54227 - 552
217LEULEUARGARGGG17 - 5421 - 526
118GLYGLYASNASNCC-9 - 5431 - 553
218GLYGLYASNASNHH-9 - 5431 - 553
119SERSERASNASNDD-6 - 5434 - 553
219SERSERASNASNEE-6 - 5431 - 550
120GLYGLYASNASNDD-9 - 5431 - 553
220GLYGLYASNASNFF-9 - 5431 - 553
121LEULEUARGARGDD17 - 54227 - 552
221LEULEUARGARGGG17 - 5421 - 526
122GLYGLYASNASNDD-9 - 5431 - 553
222GLYGLYASNASNHH-9 - 5431 - 553
123SERSERASNASNEE-6 - 5431 - 550
223SERSERASNASNFF-6 - 5434 - 553
124LEULEUARGARGEE17 - 54224 - 549
224LEULEUARGARGGG17 - 5421 - 526
125SERSERARGARGEE-6 - 5421 - 549
225SERSERARGARGHH-6 - 5424 - 552
126LEULEUARGARGFF17 - 54227 - 552
226LEULEUARGARGGG17 - 5421 - 526
127GLYGLYASNASNFF-9 - 5431 - 553
227GLYGLYASNASNHH-9 - 5431 - 553
128LEULEUARGARGGG17 - 5421 - 526
228LEULEUARGARGHH17 - 54227 - 552

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15
16
17
18
19
20
21
22
23
24
25
26
27
28

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Components

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Protein BONZAI ... , 5 types, 8 molecules ACDFBEGH

#1: Protein
Protein BONZAI 1 / COPINE 1


Mass: 61060.125 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: BON1, CPN1, At5g61900, K22G18.2 / Plasmid: pET32a / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q941L3
#2: Protein Protein BONZAI 1 / COPINE 1


Mass: 58420.270 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: BON1, CPN1, At5g61900, K22G18.2 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q941L3
#3: Protein Protein BONZAI 1 / COPINE 1


Mass: 60814.898 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: BON1, CPN1, At5g61900, K22G18.2 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q941L3
#4: Protein Protein BONZAI 1 / COPINE 1


Mass: 58363.223 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: BON1, CPN1, At5g61900, K22G18.2 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q941L3
#5: Protein Protein BONZAI 1 / COPINE 1


Mass: 61074.156 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: BON1, CPN1, At5g61900, K22G18.2 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q941L3

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Non-polymers , 8 types, 739 molecules

#6: Chemical
ChemComp-PEG / DI(HYDROXYETHYL)ETHER / Diethylene glycol


Mass: 106.120 Da / Num. of mol.: 17 / Source method: obtained synthetically / Formula: C4H10O3
#7: Chemical...
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 81 / Source method: obtained synthetically / Formula: C2H6O2
#8: Chemical...
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 27 / Source method: obtained synthetically / Formula: C3H8O3
#9: Chemical
ChemComp-PGE / TRIETHYLENE GLYCOL / Polyethylene glycol


Mass: 150.173 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C6H14O4
#10: Chemical ChemComp-PG4 / TETRAETHYLENE GLYCOL / Polyethylene glycol


Mass: 194.226 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C8H18O5 / Comment: precipitant*YM
#11: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#12: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ca / Feature type: SUBJECT OF INVESTIGATION
#13: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 603 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY

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Experimental details

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Experiment

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

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Sample preparation

CrystalDensity Matthews: 3.36 Å3/Da / Density % sol: 63.39 % / Mosaicity: 0.13 °
Crystal growTemperature: 289 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: 0.05 M MES (PH 7.0), 0.05 M HEPES (PH 7.5), 7% PEG 8000

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL17U1 / Wavelength: 0.9789 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Oct 1, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9789 Å / Relative weight: 1
ReflectionResolution: 2.5→48.21 Å / Num. obs: 215443 / % possible obs: 98.2 % / Redundancy: 4 % / CC1/2: 0.997 / Rmerge(I) obs: 0.116 / Rpim(I) all: 0.065 / Rrim(I) all: 0.134 / Net I/σ(I): 8.2
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. measured allNum. unique obsCC1/2Rpim(I) allRrim(I) allNet I/σ(I) obs% possible all
2.5-2.544.10.244244256107440.2490.13640.28040.798.9
13.69-48.163.70.029506313700.9990.0170.03333.396.1

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Processing

Software
NameVersionClassification
Aimless0.7.4data scaling
REFMAC5.8.0238refinement
PDB_EXTRACT3.25data extraction
XDSdata reduction
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.5→48.21 Å / Cor.coef. Fo:Fc: 0.949 / Cor.coef. Fo:Fc free: 0.927 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.43 / ESU R Free: 0.282 / Details: U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.2662 10856 5 %RANDOM
Rwork0.2271 ---
obs0.229 204561 98.03 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso max: 228.1 Å2 / Biso mean: 68.067 Å2 / Biso min: 18.62 Å2
Baniso -1Baniso -2Baniso -3
1--1.75 Å20 Å20 Å2
2--5.31 Å20 Å2
3----3.56 Å2
Refinement stepCycle: final / Resolution: 2.5→48.21 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms33809 0 685 603 35097
Biso mean--75.51 48.5 -
Num. residues----4345
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.01235009
X-RAY DIFFRACTIONr_angle_refined_deg1.5331.62947071
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.47654331
X-RAY DIFFRACTIONr_dihedral_angle_2_deg39.09323.1551667
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.958156056
X-RAY DIFFRACTIONr_dihedral_angle_4_deg22.44715168
X-RAY DIFFRACTIONr_chiral_restr0.1180.24559
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.0225890
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A156630.11
12B156630.11
21A169580.09
22C169580.09
31A167370.1
32D167370.1
41A163380.11
42E163380.11
51A167580.1
52F167580.1
61A153830.09
62G153830.09
71A165960.1
72H165960.1
81B156510.11
82C156510.11
91B155060.11
92D155060.11
101B157800.11
102E157800.11
111B155550.11
112F155550.11
121B154590.09
122G154590.09
131B158340.11
132H158340.11
141C167540.09
142D167540.09
151C163070.11
152E163070.11
161C168290.1
162F168290.1
171C153820.09
172G153820.09
181C165540.1
182H165540.1
191D161650.11
192E161650.11
201D169460.09
202F169460.09
211D151900.1
212G151900.1
221D163890.11
222H163890.11
231E162700.11
232F162700.11
241E154450.09
242G154450.09
251E166230.1
252H166230.1
261F153200.1
262G153200.1
271F164850.11
272H164850.11
281G155000.09
282H155000.09
LS refinement shellResolution: 2.5→2.565 Å / Rfactor Rfree error: 0
RfactorNum. reflection% reflection
Rfree0.426 859 -
Rwork0.35 15064 -
obs--98.52 %

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