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- PDB-2vza: Type IV secretion system effector protein BepA -

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Basic information

Entry
Database: PDB / ID: 2vza
TitleType IV secretion system effector protein BepA
ComponentsCELL FILAMENTATION PROTEIN
KeywordsCELL ADHESION / T4SS / OB FOLD / FIC DOMAIN / SUBSTRATE PROTEIN / PROTEIN TRANSLOCATION
Function / homology
Function and homology information


AMPylase activity / protein adenylylation / protein adenylyltransferase / symbiont-mediated suppression of host apoptosis / regulation of cell division / extracellular region / ATP binding
Similarity search - Function
BepA, intracellular delivery domain / Intracellular delivery domain / Fido-like domain / Fic-like fold / Fido-like domain superfamily / Fic/DOC family / Fido domain / Fido domain profile. / Nucleic acid-binding proteins / OB fold (Dihydrolipoamide Acetyltransferase, E2P) ...BepA, intracellular delivery domain / Intracellular delivery domain / Fido-like domain / Fic-like fold / Fido-like domain superfamily / Fic/DOC family / Fido domain / Fido domain profile. / Nucleic acid-binding proteins / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Nucleic acid-binding, OB-fold / Beta Barrel / Orthogonal Bundle / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
Protein adenylyltransferase
Similarity search - Component
Biological speciesBARTONELLA HENSELAE (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.05 Å
AuthorsMeury, M. / Schirmer, T.
CitationJournal: Protein Sci. / Year: 2011
Title: Fic Domain Catalyzed Adenylylation: Insight Provided by the Structural Analysis of the Type Iv Secretion System Effector Bepa.
Authors: Palanivelu, D.V. / Goepfert, A. / Meury, M. / Guye, P. / Dehio, C. / Schirmer, T.
History
DepositionJul 31, 2008Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 17, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Oct 26, 2011Group: Database references / Other
Revision 1.3Dec 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / struct_ncs_dom_lim / struct_site
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 / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: CELL FILAMENTATION PROTEIN
B: CELL FILAMENTATION PROTEIN
C: CELL FILAMENTATION PROTEIN
D: CELL FILAMENTATION PROTEIN
E: CELL FILAMENTATION PROTEIN
F: CELL FILAMENTATION PROTEIN
G: CELL FILAMENTATION PROTEIN
H: CELL FILAMENTATION PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)273,04518
Polymers272,0858
Non-polymers96110
Water00
1
A: CELL FILAMENTATION PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)34,1072
Polymers34,0111
Non-polymers961
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
2
B: CELL FILAMENTATION PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)34,2033
Polymers34,0111
Non-polymers1922
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
3
C: CELL FILAMENTATION PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)34,1072
Polymers34,0111
Non-polymers961
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
4
D: CELL FILAMENTATION PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)34,1072
Polymers34,0111
Non-polymers961
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
5
E: CELL FILAMENTATION PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)34,1072
Polymers34,0111
Non-polymers961
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
6
F: CELL FILAMENTATION PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)34,2033
Polymers34,0111
Non-polymers1922
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
7
G: CELL FILAMENTATION PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)34,1072
Polymers34,0111
Non-polymers961
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
8
H: CELL FILAMENTATION PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)34,1072
Polymers34,0111
Non-polymers961
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
Unit cell
Length a, b, c (Å)229.902, 229.902, 308.994
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number155
Space group name H-MH32
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31C
41D
51E
61F
71G
81H
12A
22B
32C
42D
52E
62F
72G
82H
13A
23B
33C
43D
53E
63F
73G
83H
14A
24B
34C
44D
54E
64F
74G
84H

NCS domain segments:

Refine code: 1

Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111THRTHRPROPROAA11 - 163 - 8
211THRTHRPROPROBB11 - 163 - 8
311THRTHRPROPROCC11 - 163 - 8
411THRTHRPROPRODD11 - 163 - 8
511THRTHRPROPROEE11 - 163 - 8
611THRTHRPROPROFF11 - 163 - 8
711THRTHRPROPROGG11 - 163 - 8
811THRTHRPROPROHH11 - 163 - 8
121HISHISASNASNAA18 - 3710 - 29
221HISHISASNASNBB18 - 3710 - 29
321HISHISASNASNCC18 - 3710 - 29
421HISHISASNASNDD18 - 3710 - 29
521HISHISASNASNEE18 - 3710 - 29
621HISHISASNASNFF18 - 3710 - 29
721HISHISASNASNGG18 - 3710 - 29
821HISHISASNASNHH18 - 3710 - 29
131LEULEULYSLYSAA75 - 10567 - 97
231LEULEULYSLYSBB75 - 10567 - 97
331LEULEULYSLYSCC75 - 10567 - 97
431LEULEULYSLYSDD75 - 10567 - 97
531LEULEULYSLYSEE75 - 10567 - 97
631LEULEULYSLYSFF75 - 10567 - 97
731LEULEULYSLYSGG75 - 10567 - 97
831LEULEULYSLYSHH75 - 10567 - 97
112ALAALAGLNGLNAA38 - 7430 - 66
212ALAALAGLNGLNBB38 - 7430 - 66
312ALAALAGLNGLNCC38 - 7430 - 66
412ALAALAGLNGLNDD38 - 7430 - 66
512ALAALAGLNGLNEE38 - 7430 - 66
612ALAALAGLNGLNFF38 - 7430 - 66
712ALAALAGLNGLNGG38 - 7430 - 66
812ALAALAGLNGLNHH38 - 7430 - 66
113ALAALAPROPROAA112 - 160104 - 152
213ALAALAPROPROBB112 - 160104 - 152
313ALAALAPROPROCC112 - 160104 - 152
413ALAALAPROPRODD112 - 160104 - 152
513ALAALAPROPROEE112 - 160104 - 152
613ALAALAPROPROFF112 - 160104 - 152
713ALAALAPROPROGG112 - 160104 - 152
813ALAALAPROPROHH112 - 160104 - 152
123PHEPHEGLYGLYAA161 - 166153 - 158
223PHEPHEGLYGLYBB161 - 166153 - 158
323PHEPHEGLYGLYCC161 - 166153 - 158
423PHEPHEGLYGLYDD161 - 166153 - 158
523PHEPHEGLYGLYEE161 - 166153 - 158
623PHEPHEGLYGLYFF161 - 166153 - 158
723PHEPHEGLYGLYGG161 - 166153 - 158
823PHEPHEGLYGLYHH161 - 166153 - 158
133THRTHRHISHISAA168 - 182160 - 174
233THRTHRHISHISBB168 - 182160 - 174
333THRTHRHISHISCC168 - 182160 - 174
433THRTHRHISHISDD168 - 182160 - 174
533THRTHRHISHISEE168 - 182160 - 174
633THRTHRHISHISFF168 - 182160 - 174
733THRTHRHISHISGG168 - 182160 - 174
833THRTHRHISHISHH168 - 182160 - 174
143GLNGLNMETMETAA183 - 233175 - 225
243GLNGLNMETMETBB183 - 233175 - 225
343GLNGLNMETMETCC183 - 233175 - 225
443GLNGLNMETMETDD183 - 233175 - 225
543GLNGLNMETMETEE183 - 233175 - 225
643GLNGLNMETMETFF183 - 233175 - 225
743GLNGLNMETMETGG183 - 233175 - 225
843GLNGLNMETMETHH183 - 233175 - 225
114VALVALVALVALAA240 - 247232 - 239
214VALVALVALVALBB240 - 247232 - 239
314VALVALVALVALCC240 - 247232 - 239
414VALVALVALVALDD240 - 247232 - 239
514VALVALVALVALEE240 - 247232 - 239
614VALVALVALVALFF240 - 247232 - 239
714VALVALVALVALGG240 - 247232 - 239
814VALVALVALVALHH240 - 247232 - 239
124ALAALAHISHISAA248 - 306240 - 298
224ALAALAHISHISBB248 - 306240 - 298
324ALAALAHISHISCC248 - 306240 - 298
424ALAALAHISHISDD248 - 306240 - 298
524ALAALAHISHISEE248 - 306240 - 298
624ALAALAHISHISFF248 - 306240 - 298
724ALAALAHISHISGG248 - 306240 - 298
824ALAALAHISHISHH248 - 306240 - 298

NCS ensembles :
ID
1
2
3
4

NCS oper:
IDCodeMatrixVector
1given(0.992557, 0.117928, 0.030391), (0.118415, -0.992854, -0.014775), (0.028432, 0.018264, -0.999429)-9.287, 133.6263, 127.9978
2given(0.188564, -0.899338, 0.394506), (-0.07614, -0.413892, -0.907136), (0.979105, 0.141015, -0.14652)29.9693, 177.3464, 60.7275
3given(-0.382974, -0.527779, -0.758143), (-0.855425, -0.107166, 0.506719), (-0.348683, 0.842594, -0.410433)107.0033, 11.6916, 46.1396
4given(-0.433856, -0.535946, -0.724245), (-0.825809, -0.0849, 0.557523), (-0.360291, 0.839973, -0.405755)102.3143, 7.3174, -32.6353
5given(-0.475725, -0.496042, -0.726381), (0.804219, 0.089183, -0.587605), (0.356257, -0.863707, 0.356499)93.7869, 129.9321, 89.1448
6given(0.536022, 0.368222, -0.759666), (0.728413, -0.656591, 0.19571), (-0.426725, -0.658256, -0.620166)54.0723, 124.9574, 76.8873
7given(0.893915, -0.29754, 0.33524), (0.170868, 0.917633, 0.358822), (-0.414391, -0.263475, 0.871126)49.5209, 19.6665, -63.02
8given(0.430365, 0.516969, 0.739969), (-0.468906, -0.572424, 0.672631), (0.771305, -0.636453, -0.003941)-108.2985, 35.0402, 85.6203
9given(-0.661802, -0.187728, 0.72578), (0.43061, -0.88769, 0.16303), (0.613672, 0.420433, 0.668332)-59.0241, 114.0452, -38.248
10given(0.047474, -0.995898, 0.077008), (-0.78411, -0.084927, -0.614799), (0.618803, -0.031212, -0.784917)63.8723, 116.2178, 149.058
11given(-0.000795, -0.999415, 0.034157), (-0.768033, -0.021276, -0.640071), (0.64041, -0.026758, -0.767558)65.799, 115.5365, 69.8431
12given(-0.011463, -0.998076, -0.060951), (0.788112, -0.046522, 0.613783), (-0.615424, -0.040984, 0.787119)66.4337, 25.1714, -16.7258
13given(0.951711, -0.210971, 0.223031), (-0.211934, 0.074071, 0.974472), (-0.222104, -0.974681, 0.025759)2.6308, -7.278, 37.3313
14given(0.032279, 0.40756, 0.912617), (0.445432, 0.811525, -0.37815), (-0.894733, 0.418713, -0.155352)-62.4614, 100.1076, -11.8853
15given(0.998856, 0.036647, -0.030712), (0.036538, -0.999324, -0.004087), (-0.030841, 0.00296, -0.99952)1.4753, 133.3349, 129.015
16given(0.236282, -0.907146, 0.34822), (-0.148819, -0.387924, -0.909598), (0.960221, 0.1631, -0.22666)32.2195, 175.4079, 66.1615
17given(-0.388821, -0.614238, -0.68668), (-0.837997, -0.073941, 0.540641), (-0.382856, 0.785649, -0.48598)104.9416, 7.4133, 56.4789
18given(-0.41591, -0.629445, -0.656367), (-0.840175, -0.010259, 0.542219), (-0.348031, 0.776977, -0.524577)101.0774, 3.7226, -16.5922
19given(-0.479438, -0.593995, -0.645994), (0.794426, 0.018993, -0.607064), (0.372863, -0.804244, 0.462779)91.0253, 132.5449, 74.6117
20given(0.489207, 0.206401, -0.847393), (0.711408, -0.656507, 0.250795), (-0.504555, -0.725532, -0.468003)67.7663, 116.4881, 66.2752
21given(0.913462, -0.325948, 0.243608), (0.278317, 0.937177, 0.210331), (-0.296861, -0.124329, 0.946793)50.6918, 36.6986, -71.0233

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Components

#1: Protein
CELL FILAMENTATION PROTEIN / BEPA PROTEIN / BEPA


Mass: 34010.574 Da / Num. of mol.: 8 / Fragment: RESIDUES 10-303
Source method: isolated from a genetically manipulated source
Details: C-TERMINAL (HIS)6-TAG / Source: (gene. exp.) BARTONELLA HENSELAE (bacteria) / Plasmid: PRUN / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): PLYSS / References: UniProt: Q6G2A9
#2: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: SO4
Nonpolymer detailsSULPHATES 310 OF CHAINS A TO H ARE BOUND TO THE PUTATIVE ACTIVE SITE AT THE N-TERMINUS OF ALPHA- ...SULPHATES 310 OF CHAINS A TO H ARE BOUND TO THE PUTATIVE ACTIVE SITE AT THE N-TERMINUS OF ALPHA-HELIX 5 OF EACH CHAIN. THEY OCCUPY TWO ALTERNATIVE, MUTUALLY EXCLUSIVE POSITIONS. AN OCCUPANCY OF 0.5 IS ASSIGNED TO EACH POSITION. SULPHATE B 311 MEDIATES CRYSTAL CONTACT BETWEEN CHAINS A AND B SULPHATE F 311 MEDIATES CRYSTAL CONTACT BETWEEN CHAINS E AND F

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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: 2.86 Å3/Da / Density % sol: 56.94 % / Description: NONE
Crystal growpH: 8.25
Details: 30 MG/ML PROTEIN IN 20 MM TRIS_HCL (PH 8.0), 500 MM NACL AND 2 MM BETA-MERCAPTOETHANOL MIXED WITH 1.5 M AMMONIUM SULFATE, 10 MM TRIS-HCL (PH 8.25) AND 0.1 M LITHIUM SULFATE

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1.0001
DetectorType: MARRESEARCH / Detector: CCD / Date: Mar 16, 2007
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.0001 Å / Relative weight: 1
ReflectionResolution: 2.95→83.62 Å / Num. obs: 55048 / % possible obs: 92.6 % / Observed criterion σ(I): 0 / Redundancy: 2.91 % / Rmerge(I) obs: 0.11 / Net I/σ(I): 5.34
Reflection shellResolution: 3.05→3.21 Å / Redundancy: 1.84 % / Rmerge(I) obs: 0.45 / Mean I/σ(I) obs: 1.61 / % possible all: 75.4

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Processing

Software
NameVersionClassification
REFMAC5.2.0019refinement
MOSFLMdata reduction
SCALAdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2VY3

2vy3


Resolution: 3.05→30 Å / Cor.coef. Fo:Fc: 0.913 / Cor.coef. Fo:Fc free: 0.882 / SU B: 53.121 / SU ML: 0.424 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R Free: 0.517 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY.
RfactorNum. reflection% reflectionSelection details
Rfree0.277 2796 5.1 %RANDOM
Rwork0.244 ---
obs0.246 52197 92.1 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 60.65 Å2
Baniso -1Baniso -2Baniso -3
1-0.27 Å20.13 Å20 Å2
2--0.27 Å20 Å2
3----0.4 Å2
Refinement stepCycle: LAST / Resolution: 3.05→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms19008 0 50 0 19058
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.02118285
X-RAY DIFFRACTIONr_bond_other_d0.0020.0212029
X-RAY DIFFRACTIONr_angle_refined_deg1.0171.94524769
X-RAY DIFFRACTIONr_angle_other_deg0.821329200
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.19852290
X-RAY DIFFRACTIONr_dihedral_angle_2_deg29.77124.75880
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.492152882
X-RAY DIFFRACTIONr_dihedral_angle_4_deg12.731566
X-RAY DIFFRACTIONr_chiral_restr0.0570.22657
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0220700
X-RAY DIFFRACTIONr_gen_planes_other0.0020.023692
X-RAY DIFFRACTIONr_nbd_refined0.2230.24464
X-RAY DIFFRACTIONr_nbd_other0.1670.211897
X-RAY DIFFRACTIONr_nbtor_refined0.180.29133
X-RAY DIFFRACTIONr_nbtor_other0.0870.29200
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1420.2383
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2320.286
X-RAY DIFFRACTIONr_symmetry_vdw_other0.2350.2137
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1580.210
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.2281.514600
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it0.277218122
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it0.44837919
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it0.7094.56647
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
11A775tight positional0.070.05
12B775tight positional0.070.05
13C775tight positional0.070.05
14D775tight positional0.070.05
15E775tight positional0.080.05
16F775tight positional0.060.05
17G775tight positional0.070.05
18H775tight positional0.060.05
21A501tight positional0.050.05
22B501tight positional0.050.05
23C501tight positional0.060.05
24D501tight positional0.050.05
25E501tight positional0.050.05
26F501tight positional0.050.05
27G501tight positional0.060.05
28H501tight positional0.050.05
31A1525tight positional0.060.05
32B1525tight positional0.060.05
33C1525tight positional0.060.05
34D1525tight positional0.070.05
35E1525tight positional0.060.05
36F1525tight positional0.070.05
37G1525tight positional0.070.05
38H1525tight positional0.050.05
41A803tight positional0.050.05
42B803tight positional0.060.05
43C803tight positional0.040.05
44D803tight positional0.050.05
45E803tight positional0.040.05
46F803tight positional0.060.05
47G803tight positional0.050.05
48H803tight positional0.040.05
11A775tight thermal0.10.5
12B775tight thermal0.090.5
13C775tight thermal0.10.5
14D775tight thermal0.10.5
15E775tight thermal0.090.5
16F775tight thermal0.080.5
17G775tight thermal0.10.5
18H775tight thermal0.090.5
21A501tight thermal0.090.5
22B501tight thermal0.090.5
23C501tight thermal0.090.5
24D501tight thermal0.070.5
25E501tight thermal0.080.5
26F501tight thermal0.080.5
27G501tight thermal0.090.5
28H501tight thermal0.060.5
31A1525tight thermal0.090.5
32B1525tight thermal0.080.5
33C1525tight thermal0.090.5
34D1525tight thermal0.080.5
35E1525tight thermal0.080.5
36F1525tight thermal0.080.5
37G1525tight thermal0.10.5
38H1525tight thermal0.070.5
41A803tight thermal0.080.5
42B803tight thermal0.080.5
43C803tight thermal0.070.5
44D803tight thermal0.070.5
45E803tight thermal0.060.5
46F803tight thermal0.090.5
47G803tight thermal0.070.5
48H803tight thermal0.060.5
LS refinement shellResolution: 3.05→3.13 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.367 147
Rwork0.36 2677
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)
14.57410.5396-1.42766.33371.3716.91130.0729-0.2053-0.34810.4171-0.5021-0.7350.45840.43530.4291-0.4625-0.1278-0.0436-0.6012-0.0433-0.005520.87680.50279.464
25.30440.0706-5.67537.6518-2.00836.56030.3886-0.176-0.1815-0.425-0.5608-0.2682-0.0786-0.00650.1722-0.4217-0.0593-0.0644-0.6847-0.1083-0.134517.62687.12775.452
33.42390.33642.50018.0755-4.21698.85230.3184-0.21230.65881.02-0.31411.5277-0.227-0.7988-0.0042-0.178-0.32180.1579-0.2247-0.3296-0.0492-0.67279.04784.641
42.68354.1937-0.021110.1681-2.34432.52110.777-0.1089-0.20340.9296-0.9168-0.52090.16560.31260.13980.0057-0.33530.0511-0.3201-0.0465-0.32067.42464.28383.78
55.60817.24840.877413.892.81265.27510.6636-0.1515-0.86240.2465-0.4449-1.29780.30250.1467-0.2187-0.0195-0.2864-0.051-0.42820.0534-0.28173.21643.92183.292
65.9311-0.27390.76024.99182.49538.69490.44470.33490.3238-0.2702-0.2735-0.9692-0.6580.8538-0.1712-0.30750.06610.1518-0.51450.05410.048623.36854.99250.643
76.19680.14741.966411.1059-1.87033.97910.2088-0.00110.26770.29010.0354-0.4517-0.3392-0.3452-0.2442-0.18590.07640.1304-0.4409-0.0083-0.229720.7848.16554.656
83.941-1.6148-1.77766.8485-1.85014.23350.64210.5028-0.6994-0.7985-0.49830.95770.0978-0.9199-0.1438-0.14160.30420.0151-0.0818-0.1155-0.15962.01254.04944.793
92.3355-4.4455-1.290610.39240.43672.82640.79490.23110.3658-0.6264-0.657-0.8189-0.8408-0.109-0.1380.07070.36240.1057-0.12860.1775-0.32118.89169.37945.428
106.4894-5.85070.58216.09223.64888.27760.4401-0.21781.8313-0.6283-0.8905-1.421-0.5210.06970.45040.25260.63380.1323-0.18020.2463-0.12813.73689.14645.584
116.0537-3.55111.90869.442-0.47987.8565-0.3173-0.61890.47590.3599-0.00690.2941-0.2105-1.20860.3242-0.5697-0.1869-0.0947-0.231-0.2502-0.34284.062107.26383.076
126.8203-1.41872.51124.2482-5.41736.9857-0.2299-0.19660.6774-0.1968-0.1543-0.45070.0859-0.6140.3842-0.587-0.093-0.0832-0.5617-0.1835-0.153611.518106.75278.916
139.6781-4.32132.42785.85951.40447.0597-0.33680.41671.7641-0.7699-0.4113-0.8084-0.8279-0.45250.7481-0.29040.1269-0.0427-0.11670.0907-0.0734-2.094115.04463.161
149.7548-0.98033.68892.00421.05514.3957-0.1308-1.6627-0.12990.3636-0.1250.2041-0.0778-1.81310.2557-0.3650.2211-0.04490.6434-0.0587-0.3111-13.821106.85772.053
1517.3892-3.62032.430712.6312-8.276113.1327-0.0417-3.5992-2.05741.73830.12460.4373-0.8844-0.5432-0.0829-0.12040.01660.06471.45070.3581-0.1474-32.80498.94470.165
165.21322.2670.402411.4081-2.23086.6917-0.11560.8303-0.3889-0.26930.47270.98080.5771-0.4772-0.357-0.41170.19420.1535-0.3175-0.177-0.20669.12526.96947.081
172.34110.2462-0.99190.7617-1.85894.60430.14620.0905-0.20710.4119-0.31760.059-0.108-0.27080.1714-0.32670.08150.0352-0.4612-0.1479-0.20415.18430.32553.76
1812.89315.5674-0.66365.60060.31584.96060.2785-1.019-1.52130.2957-0.522-0.6060.33320.21290.2435-0.038-0.01720.0089-0.31210.0828-0.12212.74121.16767.042
198.4789-0.1617-2.75811.9521-0.93791.7407-0.25211.02730.0567-0.79920.29990.0990.0947-0.7826-0.0477-0.1413-0.2811-0.020.00280.0292-0.2366-8.95726.94356.788
2012.37660.3144-2.57910.5511-0.39748.17940.05912.05341.6657-0.12410.16160.4965-1.1797-0.6464-0.2206-0.2034-0.1001-0.1120.37820.37740.0005-28.15634.18256.933
216.0162-1.1107-2.18774.65240.1416.5489-0.4045-0.2045-0.26750.190.0434-0.67760.31560.16520.3612-0.39870.1357-0.1358-0.3337-0.2551-0.04920.50780.9111.355
228.17333.5578-2.59415.9976-0.86940.8385-0.1908-0.17060.2621-0.23860.1085-0.35280.03970.06080.0824-0.30590.1345-0.1485-0.4249-0.2361-0.143917.64987.67-2.576
235.28121.6359-0.12758.864-5.94377.9413-0.2765-0.68440.36550.79210.51240.7908-0.4247-0.6068-0.236-0.28080.2478-0.0082-0.0051-0.1034-0.3072-1.23980.8276.647
242.01132.52091.04157.8206-2.35243.4101-0.3299-0.4377-0.5047-0.25780.3593-0.66661.0504-0.18-0.02940.01750.12190.14160.08060.0063-0.20555.88665.5676.201
252.34250.25990.870711.2680.527210.6014-0.723-0.697-1.1555-1.01450.5266-1.04170.77510.70410.19640.5405-0.07720.328-0.11150.27570.22390.46745.496.496
265.71191.01053.80227.03312.7226.8412-0.2360.01970.17990.2379-0.05650.0039-0.00790.5380.2925-0.43580.10140.0953-0.3269-0.2202-0.084420.21957.148-28.49
274.04420.20184.004410.1062-2.51164.69310.0626-0.2581-0.15091.1314-0.28730.83280.18590.0150.2246-0.07750.05270.1951-0.3787-0.1716-0.088517.00150.296-24.781
284.50382.65750.93398.8766-2.52546.70040.0189-0.5107-0.1963-0.0828-0.03381.79220.6439-0.73420.0148-0.34930.03730.0654-0.1977-0.51080.4806-1.26757.673-34.914
291.4666-3.3807-0.885810.32450.04272.46830.17160.108-0.19790.2034-0.38860.25880.05730.38930.2169-0.29960.0554-0.0073-0.171-0.2401-0.06795.72172.805-33.054
307.6973-4.27120.11729.69392.45838.25120.06920.21560.5027-0.1976-0.1107-0.4134-0.3973-0.08330.0414-0.3560.12250.0368-0.3999-0.1394-0.20270.21292.668-31.824
316.3359-1.00221.94937.9488-3.57937.58-0.162-0.3746-0.13190.42610.50180.6342-0.5059-0.1693-0.3398-0.5087-0.0506-0.154-0.4801-0.2174-0.35724.497107.8495.482
322.1022-0.83411.74611.2707-2.24444.0122-0.22970.2710.1236-0.00590.4209-0.2510.23060.3171-0.1912-0.52570.0188-0.1341-0.2317-0.154-0.181510.884105.46-1.051
3313.613-4.35862.3845.62961.43495.79920.13950.93511.3409-0.6897-0.2679-0.4994-0.6260.26270.1284-0.34630.0089-0.045-0.33240.0387-0.281-2.009114.177-14.271
347.5725-0.24023.2911.43230.18124.8637-0.1563-1.0033-0.18170.60830.0351-0.13390.1495-0.93470.1211-0.4590.152-0.0223-0.0609-0.0079-0.3188-13.67107.079-4.755
3514.89382.77323.45188.02121.40788.99460.0898-2.2048-1.67030.2184-0.14570.4290.9171-1.58930.0559-0.5809-0.07950.05590.67930.2379-0.1963-32.61498.834-6.234
367.1141.8745-2.080810.3018-1.87525.3361-0.17940.1533-0.30910.12850.17670.95510.5442-0.18530.0027-0.1970.1430.2517-0.3412-0.1245-0.25424.09530.216-32.875
374.2902-1.5460.4872.2318-3.12285.2426-0.2538-0.3073-0.41590.96560.20720.31510.2033-0.17750.0467-0.03630.08590.129-0.3315-0.0365-0.121311.3730.732-28.547
386.02221.99461.38168.6226-0.89077.3462-0.3474-0.8592-1.3180.32120.1316-0.24140.62280.15740.21580.41620.11640.4277-0.08790.1260.1288-2.20722.221-12.826
399.46871.7307-0.20031.07250.73431.1632-0.35120.0039-0.2407-0.0953-0.0860.53490.0037-0.69910.43720.4181-0.01470.53430.0436-0.00030.1877-14.15930.305-21.575
409.54144.99011.531510.7572-0.19335.2166-0.62840.05320.4162-0.98920.8835-0.3416-0.545-0.0824-0.25510.24160.11820.40770.2765-0.0443-0.0089-33.36837.781-19.483
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A11 - 74
2X-RAY DIFFRACTION2A75 - 109
3X-RAY DIFFRACTION3A110 - 160
4X-RAY DIFFRACTION4A161 - 247
5X-RAY DIFFRACTION5A248 - 302
6X-RAY DIFFRACTION6B11 - 74
7X-RAY DIFFRACTION7B75 - 109
8X-RAY DIFFRACTION8B110 - 160
9X-RAY DIFFRACTION9B161 - 247
10X-RAY DIFFRACTION10B248 - 302
11X-RAY DIFFRACTION11C11 - 74
12X-RAY DIFFRACTION12C75 - 109
13X-RAY DIFFRACTION13C110 - 160
14X-RAY DIFFRACTION14C161 - 247
15X-RAY DIFFRACTION15C248 - 302
16X-RAY DIFFRACTION16D11 - 74
17X-RAY DIFFRACTION17D75 - 109
18X-RAY DIFFRACTION18D110 - 160
19X-RAY DIFFRACTION19D161 - 247
20X-RAY DIFFRACTION20D248 - 302
21X-RAY DIFFRACTION21E11 - 74
22X-RAY DIFFRACTION22E75 - 109
23X-RAY DIFFRACTION23E110 - 160
24X-RAY DIFFRACTION24E161 - 247
25X-RAY DIFFRACTION25E248 - 302
26X-RAY DIFFRACTION26F11 - 74
27X-RAY DIFFRACTION27F75 - 109
28X-RAY DIFFRACTION28F110 - 160
29X-RAY DIFFRACTION29F161 - 247
30X-RAY DIFFRACTION30F248 - 302
31X-RAY DIFFRACTION31G11 - 74
32X-RAY DIFFRACTION32G75 - 109
33X-RAY DIFFRACTION33G110 - 160
34X-RAY DIFFRACTION34G161 - 247
35X-RAY DIFFRACTION35G248 - 302
36X-RAY DIFFRACTION36H11 - 74
37X-RAY DIFFRACTION37H75 - 109
38X-RAY DIFFRACTION38H110 - 160
39X-RAY DIFFRACTION39H161 - 247
40X-RAY DIFFRACTION40H248 - 302

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