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- PDB-9iyk: Crystal structure of hSOD1 in C121 space group -

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Basic information

Entry
Database: PDB / ID: 9iyk
TitleCrystal structure of hSOD1 in C121 space group
ComponentsSuperoxide dismutase [Cu-Zn]
KeywordsOXIDOREDUCTASE / hSOD1 / SOD1 / superoxide dismutase (Cu-Zn)
Function / homology
Function and homology information


action potential initiation / response to antipsychotic drug / neurofilament cytoskeleton organization / response to carbon monoxide / protein phosphatase 2B binding / dense core granule / regulation of organ growth / relaxation of vascular associated smooth muscle / anterograde axonal transport / positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway ...action potential initiation / response to antipsychotic drug / neurofilament cytoskeleton organization / response to carbon monoxide / protein phosphatase 2B binding / dense core granule / regulation of organ growth / relaxation of vascular associated smooth muscle / anterograde axonal transport / positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / response to superoxide / regulation of T cell differentiation in thymus / peripheral nervous system myelin maintenance / retina homeostasis / auditory receptor cell stereocilium organization / hydrogen peroxide biosynthetic process / cellular response to potassium ion / retrograde axonal transport / superoxide anion generation / myeloid cell homeostasis / regulation of GTPase activity / response to copper ion / superoxide metabolic process / muscle cell cellular homeostasis / superoxide dismutase / heart contraction / Detoxification of Reactive Oxygen Species / cellular response to ATP / superoxide dismutase activity / negative regulation of reproductive process / negative regulation of developmental process / transmission of nerve impulse / cellular response to cadmium ion / regulation of multicellular organism growth / ectopic germ cell programmed cell death / response to axon injury / neuronal action potential / ovarian follicle development / positive regulation of superoxide anion generation / regulation of mitochondrial membrane potential / axon cytoplasm / glutathione metabolic process / embryo implantation / dendrite cytoplasm / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / removal of superoxide radicals / reactive oxygen species metabolic process / positive regulation of phagocytosis / placenta development / response to amphetamine / thymus development / positive regulation of cytokine production / determination of adult lifespan / locomotory behavior / response to nutrient levels / response to hydrogen peroxide / sensory perception of sound / regulation of blood pressure / mitochondrial intermembrane space / small GTPase binding / negative regulation of inflammatory response / peroxisome / Platelet degranulation / protein-folding chaperone binding / response to heat / cytoplasmic vesicle / response to ethanol / spermatogenesis / gene expression / negative regulation of neuron apoptotic process / intracellular iron ion homeostasis / lysosome / positive regulation of MAPK cascade / positive regulation of apoptotic process / mitochondrial matrix / response to xenobiotic stimulus / copper ion binding / neuronal cell body / apoptotic process / protein homodimerization activity / protein-containing complex / mitochondrion / extracellular space / extracellular exosome / extracellular region / zinc ion binding / nucleoplasm / identical protein binding / nucleus / cytosol / cytoplasm
Similarity search - Function
Copper/Zinc superoxide dismutase signature 1. / Superoxide dismutase (Cu/Zn) / superoxide dismutase copper chaperone / Superoxide dismutase, copper/zinc, binding site / Copper/Zinc superoxide dismutase signature 2. / Superoxide dismutase, copper/zinc binding domain / Copper/zinc superoxide dismutase (SODC) / Superoxide dismutase-like, copper/zinc binding domain superfamily
Similarity search - Domain/homology
ACETATE ION / COPPER (II) ION / Superoxide dismutase [Cu-Zn]
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.34 Å
AuthorsYapici, I. / DeMirci, H.
Funding support Turkey, 1items
OrganizationGrant numberCountry
Other government122Z429 Turkey
CitationJournal: Int J Mol Sci / Year: 2025
Title: Structural Insights into the Dynamics of Water in SOD1 Catalysis and Drug Interactions.
Authors: Yapici, I. / Tokur, A.G. / Sever, B. / Ciftci, H. / Basak, A.N. / DeMirci, H.
History
DepositionJul 30, 2024Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Aug 14, 2024Provider: repository / Type: Initial release
Revision 1.1Oct 16, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification
Revision 1.2May 7, 2025Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.title / _citation.year
Revision 1.3May 28, 2025Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Superoxide dismutase [Cu-Zn]
C: Superoxide dismutase [Cu-Zn]
K: Superoxide dismutase [Cu-Zn]
F: Superoxide dismutase [Cu-Zn]
E: Superoxide dismutase [Cu-Zn]
D: Superoxide dismutase [Cu-Zn]
B: Superoxide dismutase [Cu-Zn]
G: Superoxide dismutase [Cu-Zn]
I: Superoxide dismutase [Cu-Zn]
L: Superoxide dismutase [Cu-Zn]
J: Superoxide dismutase [Cu-Zn]
H: Superoxide dismutase [Cu-Zn]
hetero molecules


Theoretical massNumber of molelcules
Total (without water)196,44145
Polymers194,20812
Non-polymers2,23333
Water8,881493
1
A: Superoxide dismutase [Cu-Zn]
B: Superoxide dismutase [Cu-Zn]
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,90510
Polymers32,3682
Non-polymers5378
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2140 Å2
ΔGint-27 kcal/mol
Surface area14060 Å2
MethodPISA
2
C: Superoxide dismutase [Cu-Zn]
D: Superoxide dismutase [Cu-Zn]
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,8409
Polymers32,3682
Non-polymers4727
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2080 Å2
ΔGint-24 kcal/mol
Surface area14020 Å2
MethodPISA
3
K: Superoxide dismutase [Cu-Zn]
L: Superoxide dismutase [Cu-Zn]
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,6266
Polymers32,3682
Non-polymers2584
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1520 Å2
ΔGint-17 kcal/mol
Surface area13930 Å2
MethodPISA
4
F: Superoxide dismutase [Cu-Zn]
E: Superoxide dismutase [Cu-Zn]
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,7227
Polymers32,3682
Non-polymers3545
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1370 Å2
ΔGint-9 kcal/mol
Surface area13890 Å2
MethodPISA
5
G: Superoxide dismutase [Cu-Zn]
H: Superoxide dismutase [Cu-Zn]
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,6266
Polymers32,3682
Non-polymers2584
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1490 Å2
ΔGint-17 kcal/mol
Surface area13670 Å2
MethodPISA
6
I: Superoxide dismutase [Cu-Zn]
J: Superoxide dismutase [Cu-Zn]
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,7227
Polymers32,3682
Non-polymers3545
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1390 Å2
ΔGint-10 kcal/mol
Surface area13830 Å2
MethodPISA
Unit cell
Length a, b, c (Å)178.190, 138.250, 112.930
Angle α, β, γ (deg.)90.00, 129.20, 90.00
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11F-339-

HOH

21B-343-

HOH

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Components

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Protein , 1 types, 12 molecules ACKFEDBGILJH

#1: Protein
Superoxide dismutase [Cu-Zn] / Superoxide dismutase 1 / hSod1


Mass: 16183.982 Da / Num. of mol.: 12
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SOD1 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P00441, superoxide dismutase

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Non-polymers , 5 types, 526 molecules

#2: Chemical
ChemComp-CU / COPPER (II) ION


Mass: 63.546 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: Cu / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 13 / Source method: obtained synthetically / Formula: Zn / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical
ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C2H3O2 / Feature type: SUBJECT OF INVESTIGATION
#5: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: SO4 / Feature type: SUBJECT OF INVESTIGATION
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 493 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY
Has protein modificationY

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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: 2.83 Å3/Da / Density % sol: 56.46 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / Details: Ammonium sulfate, sodium acetate

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.98 Å
DetectorType: DECTRIS EIGER2 XE 16M / Detector: PIXEL / Date: Dec 1, 2023
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98 Å / Relative weight: 1
ReflectionResolution: 2.34→56.47 Å / Num. obs: 88500 / % possible obs: 99.2 % / Redundancy: 7.13 % / CC1/2: 0.939 / Net I/σ(I): 9
Reflection shellResolution: 2.34→2.38 Å / Num. unique obs: 4366 / CC1/2: 0.237

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Processing

Software
NameVersionClassification
PHENIX(1.20.1_4487: ???)refinement
xia2data reduction
xia2data scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.34→48.92 Å / SU ML: 0.41 / Cross valid method: FREE R-VALUE / σ(F): 0 / Phase error: 33.72 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2632 3831 4.98 %
Rwork0.1981 --
obs0.2014 77004 86.28 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.34→48.92 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13364 0 55 493 13912
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00414160
X-RAY DIFFRACTIONf_angle_d0.63419249
X-RAY DIFFRACTIONf_dihedral_angle_d13.3545119
X-RAY DIFFRACTIONf_chiral_restr0.052096
X-RAY DIFFRACTIONf_plane_restr0.0042624
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.34-2.370.39061100.35472022X-RAY DIFFRACTION66
2.37-2.40.42831150.36682192X-RAY DIFFRACTION68
2.4-2.430.43521210.35952140X-RAY DIFFRACTION70
2.43-2.470.45181210.34572286X-RAY DIFFRACTION72
2.47-2.510.35661220.33032318X-RAY DIFFRACTION73
2.51-2.540.4221290.31942268X-RAY DIFFRACTION74
2.54-2.590.40281220.31332374X-RAY DIFFRACTION76
2.59-2.630.39251300.3052418X-RAY DIFFRACTION76
2.63-2.680.4381190.32032325X-RAY DIFFRACTION75
2.68-2.730.35321210.29922436X-RAY DIFFRACTION79
2.73-2.790.35361460.29812598X-RAY DIFFRACTION82
2.79-2.850.34751350.2852690X-RAY DIFFRACTION86
2.85-2.910.38911440.28872745X-RAY DIFFRACTION87
2.91-2.990.30171460.26052788X-RAY DIFFRACTION90
2.99-3.070.31731460.2482834X-RAY DIFFRACTION90
3.07-3.160.28381540.23482969X-RAY DIFFRACTION94
3.16-3.260.3211530.22282966X-RAY DIFFRACTION94
3.26-3.370.29521510.22382989X-RAY DIFFRACTION95
3.37-3.510.29211560.21713008X-RAY DIFFRACTION96
3.51-3.670.25751550.19452993X-RAY DIFFRACTION96
3.67-3.860.29161450.17562971X-RAY DIFFRACTION95
3.86-4.10.21521680.163077X-RAY DIFFRACTION98
4.1-4.420.19751620.12623118X-RAY DIFFRACTION99
4.42-4.870.19351630.12113136X-RAY DIFFRACTION99
4.87-5.570.17461620.13793155X-RAY DIFFRACTION100
5.57-7.010.20911650.1593155X-RAY DIFFRACTION99
7.02-48.920.20221700.15713202X-RAY DIFFRACTION100
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)
13.48350.87842.44961.89951.70695.92850.4229-0.8880.39140.619-0.25010.09050.21190.1074-0.31190.7154-0.42350.25230.5874-0.31460.56529.9763-10.781137.1723
23.0537-0.7463-0.4194.41960.03882.27270.3467-0.70090.43960.4875-0.02590.5845-0.13720.1238-0.32490.4833-0.25760.10890.4349-0.10830.418322.3381-20.172531.7731
32.43160.11490.00371.14160.36551.19330.3368-0.67950.03470.3918-0.32770.27840.05370.0635-0.00130.5081-0.28320.12790.5379-0.13590.364324.3883-19.890732.6954
42.3464-0.1605-1.49123.4254-0.36783.8076-0.5318-0.7152-0.8697-0.2911-0.3134-0.26510.76971.35320.66810.64680.27130.29440.83270.38480.657440.8067-53.285326.6947
56.22-0.9463-0.47774.79660.62753.7251-0.1985-0.0984-0.4442-0.4708-0.1716-0.25520.20070.54690.27380.32780.02370.01150.29620.02110.194132.8194-42.499521.1979
64.9722-2.01071.30456.0095-3.88373.1978-0.15960.2151-1.5786-0.8968-0.2282-0.23111.06430.90780.33190.83990.24510.41490.59740.20770.817540.9319-54.971114.6801
72.3381-0.10252.07394.8118-1.12175.7457-0.2295-0.5633-0.51060.0011-0.20520.02650.02060.31660.3570.26920.12080.1050.49850.1190.285733.3886-44.087322.2619
84.44984.398-0.12874.37690.08774.30770.1067-0.14750.7106-0.2464-0.15540.4224-0.58850.01910.04340.44920.13580.06940.47240.03980.45259.5772-43.9416-10.8143
93.84960.35780.43675.4492.51435.4537-0.3237-0.64770.04310.2046-0.04570.1283-0.1152-0.2620.33870.28390.15870.07320.42850.05450.292853.5722-46.7237-2.8357
107.3033-6.7814-6.35866.29665.88915.8563-0.8892-2.01140.55682.03671.1828-1.13060.40251.2174-0.27090.60250.1928-0.03810.67950.00030.464265.5405-41.3064-1.0267
115.2048-0.89950.60751.6261.11611.0821-0.2133-0.3357-0.38040.29230.03120.19540.2741-0.04980.16130.44950.19290.10450.40020.17120.396752.1569-51.24920.4909
126.9931-2.44065.01871.2596-1.16435.08310.10250.71640.2808-0.4832-0.4138-0.3493-0.11030.35650.30160.82820.49620.09350.90230.16770.41820.5423-15.0275-18.8305
132.0053-1.31671.31953.6561-2.83954.4296-0.06710.06750.08240.3532-0.1117-0.1214-0.55850.03490.20790.70970.3928-0.0240.77890.13590.457415.79-9.9472-15.4107
143.1741.243-2.88.9573.09944.6606-0.2638-0.27660.79351.33630.166-0.5137-0.9528-0.28560.07381.15730.3956-0.0730.80590.1650.548112.17143.194-9.9255
154.7952-1.73082.72923.7002-2.64515.00990.22720.65060.3323-0.0383-0.1901-0.3055-0.25650.09120.13060.62130.45740.03120.67460.24860.519511.2872-3.2646-20.0265
161.87590.71562.10870.27250.81422.4712-0.32930.37550.7263-0.2797-0.2361-0.1539-0.46130.13550.61670.92840.52220.02021.11680.36760.87318.6545-5.3842-24.8437
176.5315-5.42863.13097.9212-4.45552.5082-0.6035-0.68631.61441.30620.0737-1.2834-0.73650.23840.50280.91440.3325-0.09320.71950.13470.987224.5946-2.9179-9.3673
183.4697-1.97251.49282.4469-1.34981.4289-0.0445-0.0792-0.08580.37080.17190.1773-0.2816-0.0915-0.07420.69130.55780.06460.72810.2910.44539.3402-7.9391-13.836
194.8344-2.3910.60964.0373-2.23052.7270.0730.45720.1242-0.0663-0.2065-0.0349-0.6094-0.33030.10830.5710.2941-0.04670.53620.02030.366625.5826-25.6496-3.5273
205.428-1.11320.61132.2574-1.26143.2330.09330.141-0.27550.2169-0.3949-0.3196-0.13490.34930.29750.55630.26-0.08310.45550.04150.409733.8794-30.11081.223
218.7713-7.02255.59069.0554-6.49174.9292-0.68930.09722.33120.8532-0.191-1.7978-2.43550.04940.93530.82890.1484-0.11750.49350.03560.716932.8973-15.9608-0.9041
226.4809-4.60712.33786.0084-1.73630.84930.63331.1231-0.0363-0.4219-0.6649-0.0955-0.2808-0.16240.00110.56460.3070.04950.70760.07560.335832.755-31.6208-7.0262
236.2171.8435-3.29813.4756-4.36555.6690.2193-0.8525-0.12520.4569-0.37960.1077-0.30770.39930.05830.68040.10590.25920.61550.30720.528724.091-48.04842.5466
240.69550.0403-0.22150.6579-0.57491.1739-0.028-0.3412-0.2148-0.0066-0.2179-0.21630.14370.5019-0.03150.7940.50610.29481.59181.01090.956732.018-58.685449.1998
250.40860.0835-0.55991.374-1.31731.9119-0.3669-0.708-0.60980.1993-0.2783-0.3180.44910.94610.13930.82560.3840.26931.23080.71370.703927.5029-57.579348.561
264.45810.62560.28736.37880.18072.45070.1782-0.10270.02260.1389-0.1823-0.3208-0.23870.43990.00910.304-0.15960.07190.3757-0.05250.31944.4201-13.586717.7427
273.44470.84540.18114.37870.4861.31240.074-0.29540.4280.1107-0.0499-0.4647-0.22830.3344-0.01510.515-0.31790.0760.5663-0.10730.475750.5182-7.368622.1513
285.5649-2.5768-7.23039.34762.99099.410.4277-1.89940.36541.3053-0.1954-1.04210.06371.1433-0.23180.6086-0.3134-0.02620.6493-0.07110.497949.3807-17.784728.539
292.7761.8789-0.37572.45710.33730.84940.1517-0.29450.36930.06390.0636-0.1235-0.24740.4796-0.09550.654-0.4140.17110.4574-0.23220.666649.7115-2.338222.0484
304.34522.97150.31954.30880.39451.78030.08930.0788-1.00210.0339-0.0658-0.95220.12240.3013-0.33350.7161-0.55260.02560.7243-0.32150.80452.5552-42.043625.4798
317.83513.37941.04194.97071.42692.92770.3461-0.8084-0.88940.5164-0.2548-0.32350.12170.0415-0.08490.725-0.4068-0.01740.6909-0.04870.59090.4676-36.981635.2521
324.06643.30633.11857.9465.06976.57940.3609-0.6441-0.61640.7744-0.4925-0.5590.2175-0.33550.06610.6075-0.44950.09380.8928-0.23760.6954-2.8066-36.870436.8141
334.2589-1.8189-1.89615.4706-2.81169.0299-0.4013-0.0894-0.34770.20710.14130.43461.2271-0.75530.27261.0048-0.45370.17181.2164-0.13370.4356-2.9995-21.363462.4527
345.3849-2.2272-1.85763.50540.92582.32120.44820.07740.2623-0.53850.0732-0.395-0.1584-0.2295-0.52030.8994-0.40790.24241.0722-0.16820.50497.8952-13.532157.3496
354.476-0.1367-4.74762.40050.02527.0643-0.3369-0.2571-0.2296-0.05630.1837-0.06930.8686-0.13470.13610.914-0.41810.20261.0351-0.18730.475.9921-17.901755.9719
365.3414-0.2829-0.27463.9651.5962.8102-0.1819-0.862-0.46950.35950.1925-0.41020.19040.32740.19510.49610.28050.13950.72410.26440.520575.821-59.3696-7.0364
374.8238-0.3861-0.30423.13171.10752.3704-0.06440.30680.2057-0.1918-0.253-0.5232-0.0862-0.03010.17210.47570.18360.19540.52310.23980.544377.1936-53.484-19.8284
385.8744-4.8439-0.9234.4558-0.98536.7476-0.1391-0.2160.517-0.0994-0.3322-2.2376-0.29030.8780.43090.49820.17590.16320.81790.34380.864187.299-51.075-17.6761
393.665-3.77580.10559.62730.25723.0799-0.3922-0.4435-0.96030.5397-0.03640.20030.54260.32360.40020.590.32150.28760.73430.32540.792280.9958-68.2445-14.0052
407.2507-7.259-0.20058.10551.57736.96880.08590.1871.7392-0.15470.3292-1.5547-0.57091.0146-0.39760.37920.07580.09180.67410.10280.690879.5108-47.7613-7.8166
411.659-0.441-0.37740.86810.40960.3576-0.09060.15150.1165-0.2582-0.1953-0.3155-0.02380.2568-0.12940.59610.36230.20990.73970.43980.512278.3399-56.5274-22.2089
425.9081-0.2807-3.86976.62961.20132.96430.313-0.09051.11240.1470.6709-0.213-0.73310.8004-1.02090.7499-0.21830.22511.101-0.09560.5651.5348-4.078979.8145
436.2662-0.3688-3.01835.90661.34338.8718-0.01120.0860.50290.5060.65620.00840.38540.1152-0.5730.7935-0.25820.27951.0466-0.04330.493-4.3671-9.797785.4604
445.76840.3843-6.49921.59210.09997.4986-0.00710.75310.2601-0.17080.4132-0.00410.49850.2726-0.33730.7462-0.25830.11210.9369-0.08070.4138-5.5396-10.613484.2118
455.35111.73780.91777.21270.25835.55060.349-0.3307-0.59680.4169-0.3115-0.1636-0.1654-0.0439-0.02290.7342-0.4064-0.08750.5286-0.1210.6162-16.973-51.215127.5619
465.01580.25713.04317.0649-2.34738.90290.9561-0.8936-1.4810.5441-0.5524-0.42211.39280.0477-0.43221.001-0.3748-0.17510.77240.17961.0252-17.9552-59.944232.6475
472.23641.99950.43012.7503-0.04540.4413-0.32970.5634-0.0221-0.59020.6251-0.5152-0.19480.507-0.02490.7249-0.56950.26790.887-0.3491.198-12.8406-54.54216.8349
487.86777.3997-4.36238.5941-4.57882.81010.2327-0.1924-0.55550.2406-0.2219-0.7159-0.34120.64030.00291.1219-0.3638-0.0321.3624-0.74762.8872-9.587-69.422317.9276
491.0642-0.8665-0.94391.10611.79313.45820.12620.5904-1.92480.15240.3837-1.71371.02540.2762-0.52820.7865-0.35030.2730.8235-0.61721.7711-12.1826-68.322619.4446
504.22992.86081.83386.32531.46063.4994-0.08640.1109-0.1962-0.28780.02130.36130.0241-0.17810.06350.6618-0.43420.02390.621-0.20180.9027-27.1664-57.915723.0086
513.64613.69592.15593.77162.02312.29910.34340.2257-1.78490.3690.2006-1.92810.72840.4282-0.43530.9363-0.3573-0.19630.7337-0.23531.9609-6.6257-61.939529.1135
523.62033.07883.10284.61381.77743.0243-0.38621.1202-1.0535-1.01660.7473-0.85280.03640.4201-0.3121.0085-0.66230.3050.9818-0.48120.9702-15.053-58.886814.7693
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 36 )
2X-RAY DIFFRACTION2chain 'A' and (resid 37 through 94 )
3X-RAY DIFFRACTION3chain 'A' and (resid 95 through 153 )
4X-RAY DIFFRACTION4chain 'C' and (resid 1 through 36 )
5X-RAY DIFFRACTION5chain 'C' and (resid 37 through 85 )
6X-RAY DIFFRACTION6chain 'C' and (resid 86 through 101 )
7X-RAY DIFFRACTION7chain 'C' and (resid 102 through 153 )
8X-RAY DIFFRACTION8chain 'K' and (resid 2 through 28 )
9X-RAY DIFFRACTION9chain 'K' and (resid 29 through 101 )
10X-RAY DIFFRACTION10chain 'K' and (resid 102 through 115 )
11X-RAY DIFFRACTION11chain 'K' and (resid 116 through 153 )
12X-RAY DIFFRACTION12chain 'F' and (resid 1 through 22 )
13X-RAY DIFFRACTION13chain 'F' and (resid 23 through 65 )
14X-RAY DIFFRACTION14chain 'F' and (resid 66 through 75 )
15X-RAY DIFFRACTION15chain 'F' and (resid 76 through 93 )
16X-RAY DIFFRACTION16chain 'F' and (resid 94 through 102 )
17X-RAY DIFFRACTION17chain 'F' and (resid 103 through 112 )
18X-RAY DIFFRACTION18chain 'F' and (resid 113 through 153 )
19X-RAY DIFFRACTION19chain 'E' and (resid 1 through 65 )
20X-RAY DIFFRACTION20chain 'E' and (resid 66 through 101 )
21X-RAY DIFFRACTION21chain 'E' and (resid 102 through 115 )
22X-RAY DIFFRACTION22chain 'E' and (resid 116 through 153 )
23X-RAY DIFFRACTION23chain 'D' and (resid -2 through 36 )
24X-RAY DIFFRACTION24chain 'D' and (resid 37 through 85 )
25X-RAY DIFFRACTION25chain 'D' and (resid 86 through 153 )
26X-RAY DIFFRACTION26chain 'B' and (resid -2 through 48 )
27X-RAY DIFFRACTION27chain 'B' and (resid 49 through 101 )
28X-RAY DIFFRACTION28chain 'B' and (resid 102 through 115 )
29X-RAY DIFFRACTION29chain 'B' and (resid 116 through 153 )
30X-RAY DIFFRACTION30chain 'G' and (resid 2 through 36 )
31X-RAY DIFFRACTION31chain 'G' and (resid 37 through 107 )
32X-RAY DIFFRACTION32chain 'G' and (resid 108 through 153 )
33X-RAY DIFFRACTION33chain 'I' and (resid 1 through 36 )
34X-RAY DIFFRACTION34chain 'I' and (resid 37 through 75 )
35X-RAY DIFFRACTION35chain 'I' and (resid 76 through 153 )
36X-RAY DIFFRACTION36chain 'L' and (resid 1 through 36 )
37X-RAY DIFFRACTION37chain 'L' and (resid 37 through 75 )
38X-RAY DIFFRACTION38chain 'L' and (resid 76 through 85 )
39X-RAY DIFFRACTION39chain 'L' and (resid 86 through 101 )
40X-RAY DIFFRACTION40chain 'L' and (resid 102 through 115 )
41X-RAY DIFFRACTION41chain 'L' and (resid 116 through 153 )
42X-RAY DIFFRACTION42chain 'J' and (resid 1 through 48 )
43X-RAY DIFFRACTION43chain 'J' and (resid 49 through 101 )
44X-RAY DIFFRACTION44chain 'J' and (resid 102 through 153 )
45X-RAY DIFFRACTION45chain 'H' and (resid 1 through 22 )
46X-RAY DIFFRACTION46chain 'H' and (resid 23 through 36 )
47X-RAY DIFFRACTION47chain 'H' and (resid 37 through 65 )
48X-RAY DIFFRACTION48chain 'H' and (resid 66 through 75 )
49X-RAY DIFFRACTION49chain 'H' and (resid 76 through 85 )
50X-RAY DIFFRACTION50chain 'H' and (resid 86 through 101 )
51X-RAY DIFFRACTION51chain 'H' and (resid 102 through 115 )
52X-RAY DIFFRACTION52chain 'H' and (resid 116 through 153 )

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