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- PDB-4c7u: Crystal structure of manganese superoxide dismutase from Arabidop... -

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Basic information

Entry
Database: PDB / ID: 4c7u
TitleCrystal structure of manganese superoxide dismutase from Arabidopsis thaliana
ComponentsSUPEROXIDE DISMUTASE [MN] 1, MITOCHONDRIAL
KeywordsOXIDOREDUCTASE / OXIDATIVE STRESS / OXIDATION-REDUCTION
Function / homology
Function and homology information


embryo development ending in seed dormancy / response to zinc ion / superoxide dismutase / superoxide dismutase activity / manganese ion binding / mitochondrial matrix / defense response to bacterium / copper ion binding / mitochondrion / metal ion binding / cytosol
Similarity search - Function
Iron/manganese superoxide dismutase, C-terminal domain / Fe,Mn superoxide dismutase (SOD) domain / minor pseudopilin epsh fold / 3-Layer(bab) Sandwich / Manganese/iron superoxide dismutase, binding site / Manganese and iron superoxide dismutases signature. / Manganese/iron superoxide dismutase / Manganese/iron superoxide dismutase, N-terminal / Iron/manganese superoxide dismutases, alpha-hairpin domain / Manganese/iron superoxide dismutase, C-terminal ...Iron/manganese superoxide dismutase, C-terminal domain / Fe,Mn superoxide dismutase (SOD) domain / minor pseudopilin epsh fold / 3-Layer(bab) Sandwich / Manganese/iron superoxide dismutase, binding site / Manganese and iron superoxide dismutases signature. / Manganese/iron superoxide dismutase / Manganese/iron superoxide dismutase, N-terminal / Iron/manganese superoxide dismutases, alpha-hairpin domain / Manganese/iron superoxide dismutase, C-terminal / Manganese/iron superoxide dismutase, C-terminal domain superfamily / Iron/manganese superoxide dismutases, C-terminal domain / Manganese/iron superoxide dismutase, N-terminal domain superfamily / Helix Hairpins / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
: / Superoxide dismutase [Mn] 1, mitochondrial
Similarity search - Component
Biological speciesARABIDOPSIS THALIANA (thale cress)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.951 Å
AuthorsMarques, A. / Santos, S.P. / Rosa, M. / Carrondo, M.A. / Abreu, I.A. / Romao, C.V. / Frazao, C.
CitationJournal: To be Published
Title: Crystal Structure of the Arabidopsis Thaliana Manganese Superoxide Dismutase at 1.95 A Resolution
Authors: Marques, A. / Santos, S.P. / Rosa, M. / Carrondo, M.A. / Abreu, I.A. / Romao, C.V. / Frazao, C.
History
DepositionSep 25, 2013Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 15, 2014Provider: repository / Type: Initial release
Revision 1.1Sep 6, 2017Group: Data collection / Category: diffrn_detector / Item: _diffrn_detector.type
Revision 1.2Jan 30, 2019Group: Data collection / Experimental preparation / Category: exptl_crystal_grow / Item: _exptl_crystal_grow.method
Revision 1.3Feb 6, 2019Group: Data collection / Experimental preparation / Category: exptl_crystal_grow / Item: _exptl_crystal_grow.temp
Revision 1.4Dec 20, 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 / pdbx_struct_conn_angle / struct_conn / 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 / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_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: SUPEROXIDE DISMUTASE [MN] 1, MITOCHONDRIAL
B: SUPEROXIDE DISMUTASE [MN] 1, MITOCHONDRIAL
C: SUPEROXIDE DISMUTASE [MN] 1, MITOCHONDRIAL
D: SUPEROXIDE DISMUTASE [MN] 1, MITOCHONDRIAL
E: SUPEROXIDE DISMUTASE [MN] 1, MITOCHONDRIAL
F: SUPEROXIDE DISMUTASE [MN] 1, MITOCHONDRIAL
G: SUPEROXIDE DISMUTASE [MN] 1, MITOCHONDRIAL
H: SUPEROXIDE DISMUTASE [MN] 1, MITOCHONDRIAL
hetero molecules


Theoretical massNumber of molelcules
Total (without water)201,16916
Polymers200,7308
Non-polymers4408
Water11,097616
1
F: SUPEROXIDE DISMUTASE [MN] 1, MITOCHONDRIAL
hetero molecules

B: SUPEROXIDE DISMUTASE [MN] 1, MITOCHONDRIAL
C: SUPEROXIDE DISMUTASE [MN] 1, MITOCHONDRIAL
H: SUPEROXIDE DISMUTASE [MN] 1, MITOCHONDRIAL
hetero molecules


Theoretical massNumber of molelcules
Total (without water)100,5858
Polymers100,3654
Non-polymers2204
Water724
TypeNameSymmetry operationNumber
crystal symmetry operation1_545x,y-1,z1
identity operation1_555x,y,z1
Buried area8440 Å2
ΔGint-57.7 kcal/mol
Surface area31130 Å2
MethodPISA
2
G: SUPEROXIDE DISMUTASE [MN] 1, MITOCHONDRIAL
hetero molecules

D: SUPEROXIDE DISMUTASE [MN] 1, MITOCHONDRIAL
hetero molecules

A: SUPEROXIDE DISMUTASE [MN] 1, MITOCHONDRIAL
E: SUPEROXIDE DISMUTASE [MN] 1, MITOCHONDRIAL
hetero molecules


Theoretical massNumber of molelcules
Total (without water)100,5858
Polymers100,3654
Non-polymers2204
Water724
TypeNameSymmetry operationNumber
crystal symmetry operation1_556x,y,z+11
crystal symmetry operation1_656x+1,y,z+11
identity operation1_555x,y,z1
Buried area8530 Å2
ΔGint-58.4 kcal/mol
Surface area31320 Å2
MethodPISA
3
F: SUPEROXIDE DISMUTASE [MN] 1, MITOCHONDRIAL
hetero molecules

B: SUPEROXIDE DISMUTASE [MN] 1, MITOCHONDRIAL
C: SUPEROXIDE DISMUTASE [MN] 1, MITOCHONDRIAL
H: SUPEROXIDE DISMUTASE [MN] 1, MITOCHONDRIAL
hetero molecules


Theoretical massNumber of molelcules
Total (without water)100,5858
Polymers100,3654
Non-polymers2204
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation1_565x,y+1,z1
Buried area8440 Å2
ΔGint-57.7 kcal/mol
Surface area31130 Å2
MethodPISA
4
G: SUPEROXIDE DISMUTASE [MN] 1, MITOCHONDRIAL
hetero molecules

D: SUPEROXIDE DISMUTASE [MN] 1, MITOCHONDRIAL
hetero molecules

A: SUPEROXIDE DISMUTASE [MN] 1, MITOCHONDRIAL
E: SUPEROXIDE DISMUTASE [MN] 1, MITOCHONDRIAL
hetero molecules


Theoretical massNumber of molelcules
Total (without water)100,5858
Polymers100,3654
Non-polymers2204
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation1_655x+1,y,z1
crystal symmetry operation1_554x,y,z-11
Buried area8530 Å2
ΔGint-58.4 kcal/mol
Surface area31320 Å2
MethodPISA
5
D: SUPEROXIDE DISMUTASE [MN] 1, MITOCHONDRIAL
hetero molecules

G: SUPEROXIDE DISMUTASE [MN] 1, MITOCHONDRIAL
hetero molecules

A: SUPEROXIDE DISMUTASE [MN] 1, MITOCHONDRIAL
E: SUPEROXIDE DISMUTASE [MN] 1, MITOCHONDRIAL
hetero molecules


Theoretical massNumber of molelcules
Total (without water)100,5858
Polymers100,3654
Non-polymers2204
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation1_455x-1,y,z1
crystal symmetry operation1_454x-1,y,z-11
Buried area8530 Å2
ΔGint-58.4 kcal/mol
Surface area31320 Å2
MethodPISA
Unit cell
Length a, b, c (Å)58.952, 59.181, 107.980
Angle α, β, γ (deg.)90.55, 90.51, 89.85
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(0.9999, 0.0102, 0.0121), (0.0108, -0.9985, -0.0529), (0.0115, 0.053, -0.9985)27.8429, 80.0553, 210.4719
2given(-0.0099, -0.9999, -0.0133), (0.9987, -0.0106, 0.0503), (-0.0504, -0.0128, 0.9986)100.7651, 2.6003, 56.9162
3given(0.0011, -1, 0.0008), (-1, -0.0011, -0.0007), (0.0007, -0.0008, -1)129.2488, 70.3164, 158.3873
4given(-0.9975, 0.0199, 0.0683), (-0.0162, -0.9984, 0.054), (0.0692, 0.0527, 0.9962)140.3912, 99.3857, -7.3362
5given(-0.9977, -0.0067, -0.0681), (-0.0076, 0.9999, 0.0127), (0.068, 0.0132, -0.9976)127.5917, -31.0263, 207.9614
6given(-0.0162, 0.9976, -0.067), (0.9986, 0.0128, -0.0507), (-0.0497, -0.0678, -0.9965)24.4703, -23.1504, 165.8442
7given(0.0082, 0.9974, 0.0717), (-0.9999, 0.0088, -0.0089), (-0.0095, -0.0716, 0.9974)45.4312, 99.4312, 56.548

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Components

#1: Protein
SUPEROXIDE DISMUTASE [MN] 1, MITOCHONDRIAL / MANGANESE SUPEROXIDE DISMUTASE / PROTEIN MANGANESE SUPEROXIDE ATMSD1 / PROTEIN MATERNAL EFFECT ...MANGANESE SUPEROXIDE DISMUTASE / PROTEIN MANGANESE SUPEROXIDE ATMSD1 / PROTEIN MATERNAL EFFECT EMBRYO ARREST 33


Mass: 25091.205 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) ARABIDOPSIS THALIANA (thale cress) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): ROSETTA PLYSS / References: UniProt: O81235, superoxide dismutase
#2: Chemical
ChemComp-MN / MANGANESE (II) ION


Mass: 54.938 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Mn
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 616 / 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: 2.07 Å3/Da / Density % sol: 40.7 % / Description: NONE
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop
Details: 0.2 M SODIUM FORMATE, 20 % PEG 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277 K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.9611
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jun 20, 2013 / Details: TOROIDAL MIRROR
RadiationMonochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9611 Å / Relative weight: 1
ReflectionResolution: 1.95→53.98 Å / Num. obs: 98683 / % possible obs: 92.9 % / Observed criterion σ(I): 0 / Redundancy: 1.74 % / Biso Wilson estimate: 28.14 Å2 / Rmerge(I) obs: 0.07 / Net I/σ(I): 7.64
Reflection shellResolution: 1.95→2.07 Å / Redundancy: 1.45 % / Rmerge(I) obs: 0.57 / Mean I/σ(I) obs: 1.09 / % possible all: 92.3

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRIES 3AK2 1GV3 1IX9 1LUW 1COJ

3ak2

1gv3

1ix9

1luw

1coj


Resolution: 1.951→53.985 Å / SU ML: 0.19 / σ(F): 1.96 / Phase error: 16.14 / Stereochemistry target values: ML
Details: MNSOD REFINEMENT CONVERGED TO R- -WORK AND R-FREE OF 0.1759 AND 0.2153, RESPECTIVELY, USING A THIN-SHELLS R-FREE SET WITH 2149 REFLECTIONS. THEN A LAST REFINEMENT CYCLE WAS PERFORMED USING ...Details: MNSOD REFINEMENT CONVERGED TO R- -WORK AND R-FREE OF 0.1759 AND 0.2153, RESPECTIVELY, USING A THIN-SHELLS R-FREE SET WITH 2149 REFLECTIONS. THEN A LAST REFINEMENT CYCLE WAS PERFORMED USING THE FULL DATA SET IN ORDER TO OBTAIN THE FINAL MNSOD MODEL.
RfactorNum. reflection% reflection
Rwork0.1729 --
obs0.1729 98653 92.9 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.951→53.985 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12614 0 8 616 13238
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01213032
X-RAY DIFFRACTIONf_angle_d1.1517658
X-RAY DIFFRACTIONf_dihedral_angle_d11.7864636
X-RAY DIFFRACTIONf_chiral_restr0.0541882
X-RAY DIFFRACTIONf_plane_restr0.0072270
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.9511-1.97330.295631620.29563162X-RAY DIFFRACTION88
1.9733-1.99650.286632940.28663294X-RAY DIFFRACTION94
1.9965-2.02090.269232890.26923289X-RAY DIFFRACTION93
2.0209-2.04650.272533160.27253316X-RAY DIFFRACTION92
2.0465-2.07340.246132670.24613267X-RAY DIFFRACTION94
2.0734-2.10180.239432530.23943253X-RAY DIFFRACTION91
2.1018-2.13180.240832530.24083253X-RAY DIFFRACTION92
2.1318-2.16360.234232110.23423211X-RAY DIFFRACTION92
2.1636-2.19750.21132610.2113261X-RAY DIFFRACTION90
2.1975-2.23350.195830550.19583055X-RAY DIFFRACTION88
2.2335-2.2720.195433490.19543349X-RAY DIFFRACTION93
2.272-2.31330.192932820.19293282X-RAY DIFFRACTION94
2.3133-2.35780.179133010.17913301X-RAY DIFFRACTION92
2.3578-2.40590.187332060.18733206X-RAY DIFFRACTION92
2.4059-2.45820.193833280.19383328X-RAY DIFFRACTION92
2.4582-2.51540.17931690.1793169X-RAY DIFFRACTION91
2.5154-2.57830.164632630.16463263X-RAY DIFFRACTION92
2.5783-2.6480.15632090.1563209X-RAY DIFFRACTION92
2.648-2.7260.145831990.14583199X-RAY DIFFRACTION90
2.726-2.81390.146734020.14673402X-RAY DIFFRACTION95
2.8139-2.91450.147433330.14743333X-RAY DIFFRACTION95
2.9145-3.03120.148333590.14833359X-RAY DIFFRACTION95
3.0312-3.16910.143133760.14313376X-RAY DIFFRACTION95
3.1691-3.33620.150233770.15023377X-RAY DIFFRACTION95
3.3362-3.54520.146132810.14613281X-RAY DIFFRACTION94
3.5452-3.81880.167634300.16763430X-RAY DIFFRACTION97
3.8188-4.2030.144834520.14483452X-RAY DIFFRACTION97
4.203-4.81090.150833430.15083343X-RAY DIFFRACTION96
4.8109-6.05990.164333810.16433381X-RAY DIFFRACTION95
6.0599-54.00610.184932520.18493252X-RAY DIFFRACTION92
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)
10.01330.01050.00350.0233-0.00530.01830.01540.0608-0.0204-0.08920.0153-0.05290.0052-0.01210.01680.19250.06760.03170.1355-0.01680.058179.48837.2077109.2782
20.0060.00420.00570.00740.00140.00960.0202-0.00630.0185-0.03830.0455-0.020.01130.03140.01820.10210.00490.03990.1085-0.02620.101792.546141.91129.3698
30.03860.0054-0.00860.00040.00090.010.0144-0.0142-0.0144-0.0974-0.01740.02210.06730.0076-0.00220.17830.00470.00380.08010.00310.134670.28532.1167114.0899
40.0028-0.0014-0.00090.00070.00170.00440.0442-0.05570.0063-0.00190.01570.00130.0244-0.03380.00010.0839-0.0081-0.00740.10490.02620.102756.651535.4394122.4663
50.0014-0.0065-0.00940.01590.02910.05420.0772-0.0427-0.0333-0.0010.031-0.0231-0.0008-0.04190.04570.0604-0.0106-0.00310.0480.05510.097667.045838.0551127.7822
60.01230.0058-0.00850.01760.02130.03450.06590.0031-0.0041-0.0555-0.0162-0.0209-0.0455-0.02540.03290.10350.01060.00470.0609-0.00220.059468.149142.0581117.6643
70.00650.0009-0.0040.001-0.00030.0032-0.01120.00910.00270.00550.0266-0.02070.00090.01950.00010.2508-0.0102-0.05030.17220.04340.25368.414324.4175122.6922
80.0079-0.00260.01690.0007-0.00620.040.0459-0.02270.03560.08010.0123-0.06660.01840.05330.07480.08150.0081-0.007-0.0346-0.1525-0.071650.515938.1994103.4386
90.00430.0054-0.00430.0064-0.00280.0092-0.00680.03820.00280.0280.0447-0.0028-0.00510.0330.00320.0507-0.0113-0.0040.1137-0.05070.078864.814534.828383.0238
100.0016-0.0007-0.00070.00910.00230.0030.0257-0.01980.05360.107-0.03280.0838-0.02730.00740.00260.15020.01430.02840.0472-0.01450.097743.476441.28597.126
110.0063-0.00090.00270.00130.00030.00030.03670.03250.0479-0.00710.00070.0181-0.0413-0.059700.160.02950.01890.15130.01980.214427.233740.088290.5509
120.09650.0314-0.01670.03740.03130.05590.08810.07710.04880.0768-0.0230.07220.0101-0.08680.07330.120.01490.0110.09280.00850.100938.749434.346692.7314
130.00110.00120.00150.0083-0.00620.01880.0053-0.00080.0069-0.01-0.0063-0.0077-0.0247-0.0007-0.00210.10050.01980.01640.0999-0.00660.277937.011250.748692.1648
140.0002-0.00050.0010.005-0.00540.0065-0.00090.00110.00330.0086-0.0053-0.0030.0026-0.005200.15670.0084-0.09130.15950.05450.219525.57818.110166.2622
150.0506-0.023-0.05450.01080.02360.0607-0.04680.1111-0.0818-0.03050.02120.06040.06780.0689-0.01570.08490.0061-0.07250.123-0.01410.049733.08119.317455.3832
160.16840.0778-0.00860.12730.04760.19770.0730.0828-0.0010.05180.05520.00220.121-0.02310.15530.03490.0092-0.06140.043-0.01190.006833.685813.369970.7531
170.0007-0.0011-0.0020.00280.00420.0059-0.01350.00710.01270.0018-0.02030.00680.0092-0.0077-00.13760.0569-0.06650.27980.10940.263922.310238.649554.8821
180.00940.01310.00310.0181-0.00060.0121-0.00950.03010.04150.10390.04330.0576-0.07610.02340.00930.09790.02730.01670.06760.00520.111231.897836.230470.3958
190.02870.02280.00820.0260.0040.0252-0.0410.11610.07060.02380.0877-0.0009-0.07320.05630.03670.07670.0105-0.00330.11620.0060.089337.443131.788260.6685
200.0011-0.00030.00090.0039-0.00020.00130.00030.00040.0056-0.00570.00240.0037-0.00450.00450.00130.15010.0351-0.04960.11890.03460.368819.325632.731466.7347
210.04020.0255-0.02840.05170.00790.0380.039-0.0515-0.09310.07750.0365-0.0294-0.0280.0160.01970.13220.0891-0.02870.21730.03410.069733.465750.796850.1944
220.002-0.00240.00470.00660.00010.0050.01760.011-0.06410.01160.0136-0.00230.04550.00180.01080.13610.0151-0.01520.08930.0320.116928.873737.008630.7013
230.0327-0.00890.02450.0085-0.00690.0214-0.0385-0.06990.0116-0.0072-0.0106-0.03190.01570.0298-0.02210.09290.0174-0.00550.1612-0.00140.094735.853856.184443.0354
240.00650.0082-0.00140.0069-0.00310.003-0.0002-0.01550.0609-0.03460.0187-0.0042-0.03290.0944-0.00020.147-0.01720.01610.1842-0.02680.185335.62272.596436.3461
250.0026-0.00270.00140.03920.00820.00380.0313-0.0046-0.0209-0.00190.05590.0122-0.0037-0.00570.03060.097-0.01410.02740.12740.00080.112632.598362.774130.4591
260.0104-0.0037-0.00180.07920.0310.1371-0.0065-0.0708-0.00390.03840.0977-0.0149-0.01370.00680.10610.08320.0145-0.0050.11570.00210.075727.899860.9341.0895
270.0007-0.0013-0.00020.00290.00080.00080.0189-0.0051-0.02280.0106-0.0022-0.00520.01520.01130.00020.1096-0.00120.02560.2357-0.0160.23345.771760.880135.6175
280.0091-0.00310.00170.0037-0.00160.0025-0.00650.03930.0212-0.0756-0.0501-0.02290.020.028-0.0440.35910.08350.06330.11460.09060.074571.178367.9824107.1431
290.00110.0018-0.00450.0032-0.00750.0113-0.0141-0.00970.0032-0.05290.02590.0541-0.0184-0.0503-0.00010.10650.0192-0.01090.0754-0.00720.091658.020964.2609126.3812
300.0307-0.03250.05130.0362-0.04770.08290.00460.0420.0642-0.0928-0.0767-0.0842-0.01580.0241-0.09150.10730.01280.0564-0.02050.05030.049470.95466.6029119.8516
310.03070.0105-0.02690.0025-0.00520.0168-0.0465-0.00170.0504-0.0352-0.0236-0.0082-0.05070.0783-0.0390.1633-0.09980.05930.12760.03580.312692.12871.1022116.742
320.0881-0.06340.01360.0578-0.00290.0214-0.0432-0.04440.0408-0.0157-0.0099-0.16870.03730.0299-0.07150.0859-0.01610.03240.01830.01330.142780.975163.0092121.1578
330.03140.01980.01760.01320.00390.0616-0.07770.0220.0518-0.0476-0.0521-0.02690.03580.0751-0.07970.1952-0.07790.11490.10830.0630.322385.202572.2437114.2794
340.0079-0.0029-0.00390.0034-0.00150.0039-0.0226-0.0138-0.01250.0693-0.0238-0.0083-0.00420.0085-0.05080.5252-0.0825-0.19960.09640.15270.081643.258765.6298104.9737
350.00320.0042-0.00360.0203-0.00230.00540.04150.00410.00410.10240.0388-0.0009-0.013-0.0240.02230.2151-0.07620.0280.10840.00860.161432.029670.243392.2868
360.0122-0.0026-0.00250.0089-0.00210.00120.01410.0226-0.02070.0414-0.01690.03120.0046-0.02060.0010.07280.0069-0.00890.0944-0.01060.06831.120373.685379.7247
370.013-0.0037-0.0030.0436-0.0530.07150.0854-0.0004-0.08050.09250.0629-0.08540.08350.03830.08360.35790.0318-0.1844-0.00290.00890.195654.386960.712996.6046
380.04290.0251-0.00670.04570.00360.00360.16120.0707-0.10290.041-0.0158-0.07290.11110.09670.10480.1475-0.0271-0.1752-0.1105-0.2305-0.125254.564171.64591.184
390.0019-0.0004-0.0020.01120.00280.0037-0.0003-0.0051-0.02540.0217-0.002-0.0056-0.0111-0.0043-0.02880.3370.0682-0.24980.0985-0.00740.247155.217460.33194.9587
400.03220.01330.01170.0140.01970.0387-0.1278-0.1559-0.10260.0672-0.00860.04140.04020.0241-0.12050.06350.11740.09910.18790.0280.039962.353359.927949.1723
410.00020.0011-0.00130.00150.00150.00250.0045-0.0210.02330.01590.0029-0.0206-0.0159-0.0085-00.13290.0120.01050.0791-0.01330.091564.894673.940826.7
420.00170.00310.00310.0080.00530.0079-0.0458-0.0851-0.15150.0368-0.00120.11780.0648-0.065-0.0205-0.0523-0.01120.08690.07240.04460.173358.223950.150441.0918
430.01920.010.0110.0050.00590.0033-0.0417-0.0084-0.0911-0.0176-0.00510.03950.0576-0.0184-0.05190.0168-0.04940.0464-0.00590.01590.186263.38241.404635.4438
440.0274-0.018-0.01280.04650.00620.0553-0.0694-0.0542-0.1278-0.0003-0.03440.04880.06090.0566-0.10240.0281-0.00170.05590.13920.07240.167367.55549.178739.0425
450.02720.0303-0.00530.04440.01980.0373-0.0553-0.0245-0.0340.0415-0.06420.06850.09030.0278-0.09490.188-0.0630.12430.25730.15630.445856.601144.497543.4235
460.01950.0018-0.00120.00560.00780.0149-0.01890.15180.0322-0.00670.0066-0.0051-0.02640.0112-0.03210.0434-0.16840.07250.384-0.05760.129561.466630.661656.7189
470.06740.0237-0.00630.0343-0.04810.0935-0.00730.15890.01190.02950.0691-0.0521-0.08740.08060.0634-0.0114-0.09690.00180.1887-0.05460.10459.535335.372172.4827
480.0048-0.002-0.00310.00080.00070.00170.00010.00060.0046-0.0014-0.0074-0.00610.00370.0022-0.0020.11180.08680.00460.3597-0.1520.266272.02311.390555.0246
490.028-0.02070.01560.0145-0.0130.01240.02290.0071-0.03740.04590.0376-0.07610.02960.04960.01960.14240.1066-0.06990.2108-0.19530.218663.34855.904167.1223
500.04610.01140.01640.0832-0.03170.03120.01520.0150.0110.06150.1995-0.06840.04690.06180.2010.00450.0116-0.06130.2166-0.09580.056459.156518.640370.7824
510.00320.0014-0.00160.0056-0.00430.0014-0.00470.052-0.0336-0.00570.0253-0.05350.02660.0309-0.01270.0940.0273-0.02960.3591-0.27150.147262.210115.74259.8581
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(CHAIN A AND RESID -1:35)
2X-RAY DIFFRACTION2(CHAIN A AND RESID 36:67)
3X-RAY DIFFRACTION3(CHAIN A AND RESID 68:93)
4X-RAY DIFFRACTION4(CHAIN A AND RESID 94:119)
5X-RAY DIFFRACTION5(CHAIN A AND RESID 120:137)
6X-RAY DIFFRACTION6(CHAIN A AND RESID 138:190)
7X-RAY DIFFRACTION7(CHAIN A AND RESID 191:202)
8X-RAY DIFFRACTION8(CHAIN B AND RESID -2:35)
9X-RAY DIFFRACTION9(CHAIN B AND RESID 36:62)
10X-RAY DIFFRACTION10(CHAIN B AND RESID 63:93)
11X-RAY DIFFRACTION11(CHAIN B AND RESID 94:119)
12X-RAY DIFFRACTION12(CHAIN B AND RESID 120:189)
13X-RAY DIFFRACTION13(CHAIN B AND RESID 190:200)
14X-RAY DIFFRACTION14(CHAIN C AND RESID -2:3)
15X-RAY DIFFRACTION15(CHAIN C AND RESID 4:42)
16X-RAY DIFFRACTION16(CHAIN C AND RESID 43:83)
17X-RAY DIFFRACTION17(CHAIN C AND RESID 84:93)
18X-RAY DIFFRACTION18(CHAIN C AND RESID 94:149)
19X-RAY DIFFRACTION19(CHAIN C AND RESID 150:189)
20X-RAY DIFFRACTION20(CHAIN C AND RESID 190:201)
21X-RAY DIFFRACTION21(CHAIN D AND RESID -1:30)
22X-RAY DIFFRACTION22(CHAIN D AND RESID 31:64)
23X-RAY DIFFRACTION23(CHAIN D AND RESID 65:91)
24X-RAY DIFFRACTION24(CHAIN D AND RESID 92:119)
25X-RAY DIFFRACTION25(CHAIN D AND RESID 120:139)
26X-RAY DIFFRACTION26(CHAIN D AND RESID 140:190)
27X-RAY DIFFRACTION27(CHAIN D AND RESID 191:202)
28X-RAY DIFFRACTION28(CHAIN E AND RESID -1:28)
29X-RAY DIFFRACTION29(CHAIN E AND RESID 29:59)
30X-RAY DIFFRACTION30(CHAIN E AND RESID 60:83)
31X-RAY DIFFRACTION31(CHAIN E AND RESID 84:119)
32X-RAY DIFFRACTION32(CHAIN E AND RESID 120:178)
33X-RAY DIFFRACTION33(CHAIN E AND RESID 179:200)
34X-RAY DIFFRACTION34(CHAIN F AND RESID 1:24)
35X-RAY DIFFRACTION35(CHAIN F AND RESID 25:48)
36X-RAY DIFFRACTION36(CHAIN F AND RESID 49:70)
37X-RAY DIFFRACTION37(CHAIN F AND RESID 71:102)
38X-RAY DIFFRACTION38(CHAIN F AND RESID 103:180)
39X-RAY DIFFRACTION39(CHAIN F AND RESID 181:202)
40X-RAY DIFFRACTION40(CHAIN G AND RESID -1:37)
41X-RAY DIFFRACTION41(CHAIN G AND RESID 38:60)
42X-RAY DIFFRACTION42(CHAIN G AND RESID 61:102)
43X-RAY DIFFRACTION43(CHAIN G AND RESID 103:136)
44X-RAY DIFFRACTION44(CHAIN G AND RESID 137:178)
45X-RAY DIFFRACTION45(CHAIN G AND RESID 179:201)
46X-RAY DIFFRACTION46(CHAIN H AND RESID 1:40)
47X-RAY DIFFRACTION47(CHAIN H AND RESID 41:83)
48X-RAY DIFFRACTION48(CHAIN H AND RESID 84:93)
49X-RAY DIFFRACTION49(CHAIN H AND RESID 94:119)
50X-RAY DIFFRACTION50(CHAIN H AND RESID 120:169)
51X-RAY DIFFRACTION51(CHAIN H AND RESID 170:202)

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