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- PDB-2w82: The structure of ArdA -

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Basic information

Entry
Database: PDB / ID: 2w82
TitleThe structure of ArdA
ComponentsORF18
KeywordsREPLICATION INHIBITOR / DNA MIMIC
Function / homology
Function and homology information


identical protein binding
Similarity search - Function
Antirestriction protein ArdA, domain 3 / Antirestriction protein ArdA, domain 2 / Antirestriction protein ArdA, domain 1 / Antirestriction / Antirestriction protein ArdA, domain 3 / Antirestriction protein ArdA, domain 1 / Antirestriction protein ArdA, domain 2 / Antirestriction protein (ArdA) / Helicase, Ruva Protein; domain 3 / Ubiquitin-like (UB roll) ...Antirestriction protein ArdA, domain 3 / Antirestriction protein ArdA, domain 2 / Antirestriction protein ArdA, domain 1 / Antirestriction / Antirestriction protein ArdA, domain 3 / Antirestriction protein ArdA, domain 1 / Antirestriction protein ArdA, domain 2 / Antirestriction protein (ArdA) / Helicase, Ruva Protein; domain 3 / Ubiquitin-like (UB roll) / Arc Repressor Mutant, subunit A / Roll / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Antirestriction protein ArdA
Similarity search - Component
Biological speciesENTEROCOCCUS FAECALIS (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SIRAS / Resolution: 2.8 Å
AuthorsMcMahon, S.A. / Roberts, G.A. / Carter, L.G. / Cooper, L.P. / Liu, H. / White, J.H. / Johnson, K.A. / Sanghvi, B. / Oke, M. / Walkinshaw, M.D. ...McMahon, S.A. / Roberts, G.A. / Carter, L.G. / Cooper, L.P. / Liu, H. / White, J.H. / Johnson, K.A. / Sanghvi, B. / Oke, M. / Walkinshaw, M.D. / Blakely, G. / Naismith, J.H. / Dryden, D.T.F.
CitationJournal: Nucleic Acids Res. / Year: 2009
Title: Extensive DNA Mimicry by the Arda Anti-Restriction Protein and its Role in the Spread of Antibiotic Resistance.
Authors: Mcmahon, S.A. / Roberts, G.A. / Johnson, K.A. / Cooper, L.P. / Liu, H. / White, J.H. / Carter, L.G. / Sanghvi, B. / Oke, M. / Walkinshaw, M.D. / Blakely, G. / Naismith, J.H. / Dryden, D.T.F.
History
DepositionJan 8, 2009Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 27, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Aug 30, 2017Group: Data collection / Category: diffrn_detector / reflns / reflns_shell
Item: _diffrn_detector.type / _reflns.d_resolution_low ..._diffrn_detector.type / _reflns.d_resolution_low / _reflns.pdbx_Rmerge_I_obs / _reflns.pdbx_redundancy / _reflns.percent_possible_obs / _reflns_shell.Rmerge_I_obs / _reflns_shell.percent_possible_all
Revision 1.3May 8, 2024Group: Data collection / Database references ...Data collection / Database references / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _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: ORF18
B: ORF18
C: ORF18
D: ORF18


Theoretical massNumber of molelcules
Total (without water)76,5444
Polymers76,5444
Non-polymers00
Water91951
1
A: ORF18
B: ORF18


Theoretical massNumber of molelcules
Total (without water)38,2722
Polymers38,2722
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1550 Å2
ΔGint-11.8 kcal/mol
Surface area23210 Å2
MethodPQS
2
C: ORF18
D: ORF18


Theoretical massNumber of molelcules
Total (without water)38,2722
Polymers38,2722
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1190 Å2
ΔGint-14.7 kcal/mol
Surface area23190 Å2
MethodPQS
Unit cell
Length a, b, c (Å)63.810, 103.440, 172.980
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21C
12A
22C
13A
23C
14B
24D
15B
25D
16B
26D
17A
27B
37D
18A
28B
38D
19A
29B
39D

NCS domain segments:

Refine code: 5

Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111GLNGLNILEILEAA5 - 375 - 37
211GLNGLNILEILECC5 - 375 - 37
121TYRTYRARGARGAA46 - 6846 - 68
221TYRTYRARGARGCC46 - 6846 - 68
112LEULEUASPASPAA69 - 10369 - 103
212LEULEUASPASPCC69 - 10369 - 103
113ILEILEVALVALAA104 - 164104 - 164
213ILEILEVALVALCC104 - 164104 - 164
114GLNGLNGLYGLYBB5 - 125 - 12
214GLNGLNGLYGLYDD5 - 125 - 12
124GLYGLYARGARGBB21 - 6821 - 68
224GLYGLYARGARGDD21 - 6821 - 68
115LEULEUASPASPBB69 - 10369 - 103
215LEULEUASPASPDD69 - 10369 - 103
116ILEILEVALVALBB104 - 164104 - 164
216ILEILEVALVALDD104 - 164104 - 164
117GLNGLNGLYGLYAA5 - 125 - 12
217GLNGLNGLYGLYBB5 - 125 - 12
317GLNGLNGLYGLYDD5 - 125 - 12
127GLYGLYILEILEAA21 - 3721 - 37
227GLYGLYILEILEBB21 - 3721 - 37
327GLYGLYILEILEDD21 - 3721 - 37
137TYRTYRARGARGAA46 - 6846 - 68
237TYRTYRARGARGBB46 - 6846 - 68
337TYRTYRARGARGDD46 - 6846 - 68
118LEULEUASPASPAA69 - 10369 - 103
218LEULEUASPASPBB69 - 10369 - 103
318LEULEUASPASPDD69 - 10369 - 103
119ILEILEGLYGLYAA104 - 128104 - 128
219ILEILEGLYGLYBB104 - 128104 - 128
319ILEILEGLYGLYDD104 - 128104 - 128
129ASPASPVALVALAA139 - 164139 - 164
229ASPASPVALVALBB139 - 164139 - 164
329ASPASPVALVALDD139 - 164139 - 164

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9

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Components

#1: Protein
ORF18 / ARDA


Mass: 19135.883 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) ENTEROCOCCUS FAECALIS (bacteria) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: Q47730
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 51 / Source method: isolated from a natural source / Formula: H2O

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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: 3.8 Å3/Da / Density % sol: 67.4 % / Description: NONE

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 1.239
DetectorType: ADSC / Detector: CCD
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.239 Å / Relative weight: 1
ReflectionResolution: 2.8→12.5 Å / Num. obs: 27101 / % possible obs: 93.3 % / Observed criterion σ(I): 0 / Redundancy: 2.5 % / Rmerge(I) obs: 0.064 / Net I/σ(I): 12.6
Reflection shellResolution: 2.8→2.87 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.565 / Mean I/σ(I) obs: 1.8 / % possible all: 93.6

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Processing

Software
NameVersionClassification
REFMAC5.2.0019refinement
XDSdata reduction
XDSdata scaling
RefinementMethod to determine structure: SIRAS
Starting model: NONE

Resolution: 2.8→29.44 Å / Cor.coef. Fo:Fc: 0.933 / Cor.coef. Fo:Fc free: 0.899 / SU B: 26.186 / SU ML: 0.242 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.675 / ESU R Free: 0.332 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.249 1377 5.1 %RANDOM
Rwork0.207 ---
obs0.209 25724 93.5 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 43.72 Å2
Baniso -1Baniso -2Baniso -3
1--0.34 Å20 Å20 Å2
2--0.19 Å20 Å2
3---0.15 Å2
Refinement stepCycle: LAST / Resolution: 2.8→29.44 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5310 0 0 51 5361
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0060.0225436
X-RAY DIFFRACTIONr_bond_other_d0.0010.023464
X-RAY DIFFRACTIONr_angle_refined_deg0.8171.9537392
X-RAY DIFFRACTIONr_angle_other_deg0.76238472
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.5855646
X-RAY DIFFRACTIONr_dihedral_angle_2_deg32.64425.806310
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.71415882
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.81512
X-RAY DIFFRACTIONr_chiral_restr0.0510.2790
X-RAY DIFFRACTIONr_gen_planes_refined0.0020.026170
X-RAY DIFFRACTIONr_gen_planes_other0.0010.021098
X-RAY DIFFRACTIONr_nbd_refined0.1840.2949
X-RAY DIFFRACTIONr_nbd_other0.1620.23334
X-RAY DIFFRACTIONr_nbtor_refined0.1790.22662
X-RAY DIFFRACTIONr_nbtor_other0.080.22726
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1190.299
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1440.221
X-RAY DIFFRACTIONr_symmetry_vdw_other0.2030.272
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1350.213
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.2251.54209
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it0.26525204
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it0.40532642
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it0.6344.52188
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
11A330medium positional0.990.5
12C330medium positional0.990.5
21A209medium positional0.080.5
22C209medium positional0.080.5
31A360medium positional0.20.5
41B330medium positional0.140.5
51B209medium positional0.170.5
52D209medium positional0.170.5
61B360medium positional0.280.5
62D360medium positional0.280.5
71A283medium positional0.150.5
72B283medium positional0.180.5
73D283medium positional0.130.5
81A209medium positional0.560.5
82B209medium positional0.340.5
83D209medium positional0.310.5
91A301medium positional0.380.5
92B301medium positional0.260.5
93D301medium positional0.350.5
11A452loose positional1.625
12C452loose positional1.625
21A263loose positional0.435
22C263loose positional0.435
31A435loose positional0.635
41B450loose positional0.65
51B263loose positional0.675
52D263loose positional0.675
61B435loose positional0.875
62D435loose positional0.875
71A388loose positional0.685
72B388loose positional0.795
73D388loose positional0.575
81A263loose positional1.015
82B263loose positional0.965
83D263loose positional0.75
91A365loose positional15
92B365loose positional0.85
93D365loose positional1.155
11A330medium thermal0.092
12C330medium thermal0.092
21A209medium thermal0.142
22C209medium thermal0.142
31A360medium thermal0.162
41B330medium thermal0.092
51B209medium thermal0.072
52D209medium thermal0.072
61B360medium thermal0.092
62D360medium thermal0.092
71A283medium thermal0.132
72B283medium thermal0.112
73D283medium thermal0.082
81A209medium thermal0.172
82B209medium thermal0.12
83D209medium thermal0.122
91A301medium thermal0.22
92B301medium thermal0.132
93D301medium thermal0.142
11A452loose thermal0.2610
12C452loose thermal0.2610
21A263loose thermal0.2810
22C263loose thermal0.2810
31A435loose thermal0.3210
41B450loose thermal0.2710
51B263loose thermal0.2710
52D263loose thermal0.2710
61B435loose thermal0.1910
62D435loose thermal0.1910
71A388loose thermal0.3310
72B388loose thermal0.3510
73D388loose thermal0.2810
81A263loose thermal0.4610
82B263loose thermal0.310
83D263loose thermal0.410
91A365loose thermal0.6410
92B365loose thermal0.410
93D365loose thermal0.3410
LS refinement shellResolution: 2.8→2.87 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.338 104
Rwork0.309 1846
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)
118.7149-2.90852.97964.52660.43885.58790.12480.013-0.288-0.163-0.11060.09380.0723-0.2344-0.0143-0.2539-0.07650.0564-0.2255-0.1033-0.160142.67235.12572.077
214.08367.04543.90729.92174.44557.80850.2718-0.3118-0.47330.2114-0.085-0.09220.3893-0.1401-0.1867-0.2437-0.0008-0.0326-0.1603-0.0795-0.272161.34939.85884.551
35.86361.6424.20943.61972.79888.95040.4402-0.719-0.48030.8423-0.109-0.28990.9167-0.2267-0.33130.04290.01-0.1376-0.2259-0.0269-0.154274.11447.573101.984
48.729-0.38731.382517.38251.76639.08540.0854-0.56170.45920.8785-0.26510.4296-0.6176-0.44710.1797-0.166-0.0505-0.0311-0.06270.0369-0.139698.79183.336157.806
57.74112.4955.16428.90815.221614.34890.28140.3837-0.9029-0.07390.1802-0.36690.78050.5517-0.4616-0.1717-0.0028-0.05160.0542-0.01-0.16998.70565.909142.421
63.52013.93677.55054.50167.849619.76250.0790.3119-0.3255-0.60460.58780.070.31161.4725-0.66680.04740.1356-0.15340.0855-0.11080.034889.79859.902120.872
711.63884.5417-0.38428.05281.59094.37330.07370.7230.3131-0.4018-0.02230.15690.1814-0.3651-0.05140.01110.03450.0666-0.22040.0531-0.164428.81167.38564.257
83.76432.2876-1.979314.17393.39474.32120.3062-0.1555-0.0275-0.02520.0064-0.34030.3060.4124-0.3126-0.0209-0.02260.044-0.2301-0.0001-0.265240.64783.17877.338
92.85840.58131.5543.62382.04136.43450.1269-0.3096-0.25320.2743-0.0505-0.31310.4572-0.1447-0.0764-0.1676-0.01130.024-0.2922-0.0473-0.210445.04496.65795.471
1015.0009-5.1909-3.65798.98354.4937.15930.0286-0.03950.24270.1742-0.20920.1329-0.3642-0.41380.1806-0.01410.0898-0.0113-0.1328-0.0103-0.178142.495139.465151.859
116.47455.17183.59889.252110.741716.88250.37980.1595-0.50210.10910.3918-0.78110.36170.7535-0.7716-0.05120.0754-0.03020.0147-0.0769-0.169552.873126.642135.357
120.5873-1.3793-2.53946.04465.291211.14020.0178-0.31370.1386-0.06260.2484-0.184-0.38280.1761-0.2661-0.1854-0.0277-0.023-0.0318-0.1366-0.153549.143115.82114.281
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A3 - 68
2X-RAY DIFFRACTION2A69 - 103
3X-RAY DIFFRACTION3A104 - 165
4X-RAY DIFFRACTION4B3 - 68
5X-RAY DIFFRACTION5B69 - 103
6X-RAY DIFFRACTION6B104 - 164
7X-RAY DIFFRACTION7C3 - 68
8X-RAY DIFFRACTION8C69 - 103
9X-RAY DIFFRACTION9C104 - 164
10X-RAY DIFFRACTION10D3 - 68
11X-RAY DIFFRACTION11D69 - 103
12X-RAY DIFFRACTION12D104 - 164

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