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- PDB-1hl5: The Structure of Holo Type Human Cu, Zn Superoxide Dismutase -

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Basic information

Entry
Database: PDB / ID: 1hl5
TitleThe Structure of Holo Type Human Cu, Zn Superoxide Dismutase
ComponentsSUPEROXIDE DISMUTASE
KeywordsOXIDOREDUCTASE / HUMAN CU / ZN SUPEROXIDE DISMUTASE / ANTIOXIDANT / METAL-BINDING / AMYOTROPHIC LATERAL SCLEROSIS / DISEASE MUTATION
Function / homology
Function and homology information


action potential initiation / neurofilament cytoskeleton organization / negative regulation of cholesterol biosynthetic process / anterograde axonal transport / retrograde axonal transport / positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / protein phosphatase 2B binding / regulation of organ growth / relaxation of vascular associated smooth muscle / response to superoxide ...action potential initiation / neurofilament cytoskeleton organization / negative regulation of cholesterol biosynthetic process / anterograde axonal transport / retrograde axonal transport / positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / protein phosphatase 2B binding / regulation of organ growth / relaxation of vascular associated smooth muscle / response to superoxide / peripheral nervous system myelin maintenance / superoxide anion generation / regulation of T cell differentiation in thymus / retina homeostasis / hydrogen peroxide biosynthetic process / auditory receptor cell stereocilium organization / regulation of protein kinase activity / myeloid cell homeostasis / muscle cell cellular homeostasis / regulation of GTPase activity / superoxide metabolic process / heart contraction / positive regulation of catalytic activity / superoxide dismutase / Detoxification of Reactive Oxygen Species / transmission of nerve impulse / negative regulation of reproductive process / negative regulation of developmental process / superoxide dismutase activity / neuronal action potential / regulation of multicellular organism growth / response to axon injury / ectopic germ cell programmed cell death / glutathione metabolic process / positive regulation of phagocytosis / ovarian follicle development / axon cytoplasm / embryo implantation / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / reactive oxygen species metabolic process / dendrite cytoplasm / removal of superoxide radicals / positive regulation of superoxide anion generation / thymus development / locomotory behavior / regulation of mitochondrial membrane potential / placenta development / response to organic substance / determination of adult lifespan / positive regulation of cytokine production / sensory perception of sound / response to hydrogen peroxide / mitochondrial intermembrane space / small GTPase binding / negative regulation of inflammatory response / regulation of blood pressure / peroxisome / Platelet degranulation / gene expression / response to heat / protein-folding chaperone binding / cytoplasmic vesicle / spermatogenesis / response to ethanol / negative regulation of neuron apoptotic process / intracellular iron ion homeostasis / positive regulation of MAPK cascade / mitochondrial matrix / response to xenobiotic stimulus / positive regulation of apoptotic process / copper ion binding / neuronal cell body / apoptotic process / protein-containing complex / mitochondrion / extracellular space / extracellular exosome / zinc ion binding / extracellular region / nucleoplasm / identical protein binding / nucleus / cytosol / cytoplasm
Similarity search - Function
Superoxide dismutase, copper/zinc binding domain / Copper/Zinc superoxide dismutase signature 1. / Superoxide dismutase, copper/zinc, binding site / Copper/Zinc superoxide dismutase signature 2. / Superoxide dismutase, copper/zinc binding domain / Superoxide dismutase (Cu/Zn) / superoxide dismutase copper chaperone / Copper/zinc superoxide dismutase (SODC) / Superoxide dismutase-like, copper/zinc binding domain superfamily / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
COPPER (II) ION / Superoxide dismutase [Cu-Zn]
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å
AuthorsStrange, R.W. / Antonyuk, S. / Hough, M.A. / Doucette, P. / Rodriguez, J. / Hart, P.J. / Hayward, L.J. / Valentine, J.S. / Hasnain, S.S.
CitationJournal: J.Mol.Biol. / Year: 2003
Title: The Structure of Holo and Metal-Deficient Wild-Type Human Cu, Zn Superoxide Dismutase and its Relevance to Familial Amyotrophic Lateral Sclerosis
Authors: Strange, R.W. / Antonyuk, S. / Hough, M.A. / Doucette, P. / Rodriguez, J. / Hart, P.J. / Hayward, L.J. / Valentine, J.S. / Hasnain, S.S.
History
DepositionMar 13, 2003Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 8, 2003Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Dec 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 / 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_asym_id / _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.ptnr1_symmetry / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_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.ptnr3_symmetry / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _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.ptnr1_symmetry / _struct_conn.ptnr2_auth_asym_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_conn.ptnr2_symmetry / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Remark 700 SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "FA" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "FA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "PA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: SUPEROXIDE DISMUTASE
B: SUPEROXIDE DISMUTASE
C: SUPEROXIDE DISMUTASE
D: SUPEROXIDE DISMUTASE
E: SUPEROXIDE DISMUTASE
F: SUPEROXIDE DISMUTASE
G: SUPEROXIDE DISMUTASE
H: SUPEROXIDE DISMUTASE
I: SUPEROXIDE DISMUTASE
J: SUPEROXIDE DISMUTASE
K: SUPEROXIDE DISMUTASE
L: SUPEROXIDE DISMUTASE
M: SUPEROXIDE DISMUTASE
N: SUPEROXIDE DISMUTASE
O: SUPEROXIDE DISMUTASE
P: SUPEROXIDE DISMUTASE
Q: SUPEROXIDE DISMUTASE
S: SUPEROXIDE DISMUTASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)287,33857
Polymers284,89618
Non-polymers2,44139
Water31,7601763
1
A: SUPEROXIDE DISMUTASE
H: SUPEROXIDE DISMUTASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,9136
Polymers31,6552
Non-polymers2584
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
2
B: SUPEROXIDE DISMUTASE
I: SUPEROXIDE DISMUTASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,9136
Polymers31,6552
Non-polymers2584
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
3
C: SUPEROXIDE DISMUTASE
J: SUPEROXIDE DISMUTASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,9537
Polymers31,6552
Non-polymers2985
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
4
D: SUPEROXIDE DISMUTASE
K: SUPEROXIDE DISMUTASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,9537
Polymers31,6552
Non-polymers2985
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
5
E: SUPEROXIDE DISMUTASE
L: SUPEROXIDE DISMUTASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,9136
Polymers31,6552
Non-polymers2584
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
6
F: SUPEROXIDE DISMUTASE
M: SUPEROXIDE DISMUTASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,9136
Polymers31,6552
Non-polymers2584
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
7
G: SUPEROXIDE DISMUTASE
N: SUPEROXIDE DISMUTASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,9136
Polymers31,6552
Non-polymers2584
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
8
O: SUPEROXIDE DISMUTASE
Q: SUPEROXIDE DISMUTASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,9537
Polymers31,6552
Non-polymers2985
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
9
P: SUPEROXIDE DISMUTASE
S: SUPEROXIDE DISMUTASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,9136
Polymers31,6552
Non-polymers2584
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
Unit cell
Length a, b, c (Å)76.871, 172.380, 112.450
Angle α, β, γ (deg.)90.00, 93.45, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(0.89505, -0.36885, 0.25068), (-0.37224, -0.92745, -0.03559), (0.24562, -0.06146, -0.96742)3.40235, 183.62323, 171.6217
2given(-0.98635, 0.05753, -0.15428), (-0.05773, -0.99833, -0.00323), (-0.15421, 0.00572, 0.98802)41.97392, 173.66074, 59.29191
3given(-0.91513, 0.38902, 0.10583), (0.39231, 0.91976, 0.01151), (-0.09286, 0.05205, -0.99432)4.91064, 4.10431, 115.60555
4given(0.95645, -0.19412, -0.218), (-0.08473, 0.53005, -0.84372), (0.27934, 0.82545, 0.49052)23.65226, 71.57378, -10.01044
5given(0.95793, -0.19004, 0.21505), (-0.2808, -0.46595, 0.83907), (-0.05925, -0.86416, -0.49971)8.83297, 110.49805, 183.51767
6given(-0.92535, 0.22451, -0.30548), (0.14633, -0.53182, -0.83412), (-0.34972, -0.81656, 0.45927)46.64627, 204.50653, 120.70108
7given(-0.96417, 0.22778, 0.13596), (0.22847, 0.45263, 0.86193), (0.13479, 0.86212, -0.48845)8.10633, -27.88937, 56.90441
8given(0.91156, -0.35664, -0.20462), (-0.35, -0.41187, -0.84135), (0.21578, 0.83855, -0.50026)53.72966, 211.35992, -2.85196
9given(0.99901, 0.02903, -0.03362), (0.01569, 0.47748, 0.8785), (0.04156, -0.87816, 0.47656)-13.08864, -33.34248, 175.54706
10given(0.97731, -0.03952, 0.20808), (0.16311, -0.48622, -0.85848), (0.1351, 0.87294, -0.46874)22.31427, 242.66022, 31.64304
11given(0.86263, 0.3685, 0.34653), (-0.48713, 0.42062, 0.76536), (0.13628, -0.82903, 0.54235)-44.52737, -52.29001, 133.84116
12given(-0.93287, 0.36018, 0.00567), (0.19142, 0.50897, -0.83923), (-0.30516, -0.78181, -0.54374)1.61367, 66.00793, 231.29517
13given(-0.98311, -0.02485, 0.1813), (0.16356, -0.56366, 0.80965), (0.08207, 0.82563, 0.55821)43.37927, 111.04368, -56.49068
14given(-0.91563, -0.36509, -0.16829), (0.05455, -0.52758, 0.84775), (-0.39829, 0.76705, 0.50299)137.16948, 60.4001, -44.98087
15given(-0.95028, 0.00651, -0.31132), (0.25745, 0.57881, -0.77376), (0.17515, -0.81544, -0.55171)107.0605, 86.02035, 243.4888
16given(0.53987, 0.66128, 0.52081), (-0.54485, -0.19709, 0.81504), (0.64162, -0.72378, 0.25389)-87.03172, 116.2868, 146.14423
17given(0.84456, 0.48097, 0.23536), (0.2841, -0.02992, -0.95833), (-0.45388, 0.87623, -0.16191)-70.59261, 101.88297, 1.33548

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Components

#1: Protein
SUPEROXIDE DISMUTASE /


Mass: 15827.561 Da / Num. of mol.: 18
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: SACCHAROMYCES CEREVISIAE (brewer's yeast) / Strain (production host): EG118 / Variant (production host): YEP351 / References: UniProt: P00441, superoxide dismutase
#2: Chemical
ChemComp-CU / COPPER (II) ION / Copper


Mass: 63.546 Da / Num. of mol.: 18 / Source method: obtained synthetically / Formula: Cu
#3: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 18 / Source method: obtained synthetically / Formula: Zn
#4: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Ca
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 1763 / 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: 2.6 Å3/Da / Density % sol: 52.2 %
Crystal growpH: 8 / Details: 0.2 M CA ACETATE, 15% PEG 3350, 0.1 M TRIS PH 8.0
Crystal grow
*PLUS
Method: vapor diffusion, hanging drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDDetails
16 mg/mlprotein1drop
27.5 %(w/v)PEG33501drop
3100 mMcalcium acetate1drop
450 mMTris1droppH8.0
515 %PEG33501reservoir
6200 mMcalcium acetate1reservoir
7100 mMTris-HCl1reservoirpH8.0

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SRS / Beamline: PX14.2 / Wavelength: 0.97
DetectorType: ADSC CCD / Detector: CCD / Date: Jan 15, 2002 / Details: MIRRORS
RadiationMonochromator: SI 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97 Å / Relative weight: 1
ReflectionResolution: 1.8→50 Å / Num. obs: 265996 / % possible obs: 98.6 % / Redundancy: 3.4 % / Rmerge(I) obs: 0.052 / Net I/σ(I): 20
Reflection shellResolution: 1.8→1.86 Å / Redundancy: 3 % / Rmerge(I) obs: 0.35 / Mean I/σ(I) obs: 2.7 / % possible all: 96.3
Reflection
*PLUS
Highest resolution: 1.78 Å / Num. measured all: 904897
Reflection shell
*PLUS
Highest resolution: 1.78 Å / % possible obs: 96.3 %

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Processing

Software
NameVersionClassification
REFMAC5refinement
HKL-2000data reduction
HKL-2000data scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1SOS

1sos


Resolution: 1.8→50 Å / Cor.coef. Fo:Fc: 0.957 / Cor.coef. Fo:Fc free: 0.942 / SU B: 2.732 / SU ML: 0.086 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.125 / ESU R Free: 0.12 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: DISORDERED REGIONS IN MONOMERS O AND G WERE MODELED STEREOCHEMICALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.222 13373 5 %RANDOM
Rwork0.185 ---
obs0.187 252571 98.5 %-
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: 20.08 Å2
Baniso -1Baniso -2Baniso -3
1-0.3 Å20 Å2-0.3 Å2
2---0.2 Å20 Å2
3----0.13 Å2
Refinement stepCycle: LAST / Resolution: 1.8→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms19783 0 39 1763 21585
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0140.02120321
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.6041.94527413
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.67932736
X-RAY DIFFRACTIONr_dihedral_angle_2_deg
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.312153480
X-RAY DIFFRACTIONr_dihedral_angle_4_deg
X-RAY DIFFRACTIONr_chiral_restr0.1280.23024
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.0215516
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2210.39366
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1640.52918
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined0.0860.565
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.410.3121
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2820.562
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.8351.513410
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.537221294
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it2.55836911
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it4.2764.56119
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
LS refinement shellResolution: 1.8→1.84 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.288 969
Rwork0.248 17869
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)
10.39390.3695-0.39141.7203-0.63192.45010.01550.01760.03290.0771-0.0672-0.04790.1542-0.06810.05170.2738-0.02970.02310.32680.02350.228541.99992.74577.501
20.43640.2720.46861.03340.74951.94860.01650.0149-0.0093-0.05390.02350.0374-0.0721-0.1209-0.040.2560.00480.00160.30250.02440.27841.82380.86918.236
30.34640.12930.14640.86790.35821.7061-0.0020.038-0.0468-0.03010.0157-0.05580.04730.1287-0.01380.25720.01150.00360.3237-0.00350.266740.20279.90821.039
40.4916-0.0501-0.59550.8767-0.45872.61840.05090.06620.1022-0.1570.0401-0.10.0299-0.1038-0.0910.2818-0.02060.04510.32930.03210.24943.06393.67474.837
50.46420.29420.27062.8620.57870.8262-0.0397-0.042-0.0332-0.11470.0608-0.11310.00560.049-0.02120.2553-0.0007-0.00460.2944-0.02290.274847.943120.40562.01
60.4729-0.87-0.26053.19750.69160.6928-0.0166-0.0216-0.01970.34670.1034-0.13120.18930.0453-0.08670.34670.033-0.06070.2167-0.01060.32690.456111.625110.171
71.11281.77350.81284.40670.89561.2002-0.2732-0.34410.6269-0.3784-0.27460.9741-0.3241-0.18490.54780.28540.0851-0.15760.2483-0.23250.622214.364148.39761.398
80.0761-1.0256-0.14236.0838-0.33850.87520.07460.0198-0.2476-0.27590.15270.83590.1165-0.0899-0.22730.2499-0.0187-0.07780.20390.02950.487840.118111.631105.02
94.2152-0.99060.01571.8234-1.55664.1287-0.2512-0.7339-0.19080.26980.222-0.0985-0.713-0.24690.02910.47540.05640.03420.39280.07220.174257.929121.21122.961
106.0487-1.6345-0.96486.47382.966111.4578-0.3925-1.36730.5828-0.4773-0.10790.4313-1.246-1.76860.50050.78060.8109-0.16031.2086-0.28140.06938.432139.66330.592
111.3408-2.43080.38646.2236-1.40061.1933-0.08520.0309-0.33180.1640.25460.5813-0.0673-0.076-0.16940.21630.01420.0220.25770.02370.348334.502138.856106.597
120.71270.5072-0.73181.3878-0.96282.1333-0.16790.0920.0556-0.20560.1427-0.00940.3755-0.19830.02530.3363-0.07570.02720.31160.01030.22836.31479.513101.464
130.55410.32170.12611.16160.51211.19830.0836-0.0690.010.0553-0.04860.0149-0.1109-0.0794-0.0350.2748-0.00760.03760.29880.00430.28174.35793.98242.817
140.640.22510.32161.12540.68162.08040.0013-0.01960.06830.0852-0.00390.00470.02690.02910.00260.24290.00040.00450.3125-0.00520.264643.0193.53645.222
150.49750.2732-0.35891.2445-0.43341.5452-0.01060.0381-0.0258-0.00290.1030.01640.0964-0.1063-0.09250.2647-0.0088-0.01440.29870.02710.2771-2.39680.07798.542
160.72980.84050.02572.56330.69370.6707-0.08120.03710.0803-0.29010.0942-0.0203-0.06790.049-0.0130.2947-0.0273-0.02250.2789-0.020.290852.96148.04662.403
170.5893-0.2782-0.15413.23590.36450.78570.00380.0075-0.00580.2012-0.0117-0.12680.02390.02240.00790.27640.0229-0.02360.2448-0.02130.306-4.237139.647110.609
181.93431.57710.51563.57190.38221.667-0.0159-0.36210.2038-0.1528-0.19640.29270.0223-0.16730.21220.2026-0.00360.0290.3138-0.0780.29489.336120.97659.72
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 153
2X-RAY DIFFRACTION2B1 - 153
3X-RAY DIFFRACTION3C1 - 153
4X-RAY DIFFRACTION4D1 - 153
5X-RAY DIFFRACTION5E1 - 153
6X-RAY DIFFRACTION6F3 - 153
7X-RAY DIFFRACTION7G1 - 153
8X-RAY DIFFRACTION8O1 - 153
9X-RAY DIFFRACTION9S1 - 153
10X-RAY DIFFRACTION10P1 - 153
11X-RAY DIFFRACTION11Q1 - 153
12X-RAY DIFFRACTION12H1 - 153
13X-RAY DIFFRACTION13I1 - 153
14X-RAY DIFFRACTION14J1 - 153
15X-RAY DIFFRACTION15K1 - 153
16X-RAY DIFFRACTION16L2 - 153
17X-RAY DIFFRACTION17M2 - 153
18X-RAY DIFFRACTION18N1 - 153
Refinement
*PLUS
Highest resolution: 1.78 Å / Rfactor Rfree: 0.222 / Rfactor Rwork: 0.185
Solvent computation
*PLUS
Displacement parameters
*PLUS

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