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- PDB-3rko: Crystal structure of the membrane domain of respiratory complex I... -

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Basic information

Entry
Database: PDB / ID: 3rko
TitleCrystal structure of the membrane domain of respiratory complex I from E. coli at 3.0 angstrom resolution
Components(NADH-QUINONE OXIDOREDUCTASE SUBUNIT ...) x 6
KeywordsOXIDOREDUCTASE / complex I / proton pump / membrane protein / NADH / ubiquinone / cytoplasmic membrane
Function / homology
Function and homology information


: / NADH:ubiquinone reductase (non-electrogenic) activity / Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions / ubiquinone binding / NADH dehydrogenase (ubiquinone) activity / quinone binding / electron transport coupled proton transport / ATP synthesis coupled electron transport / membrane => GO:0016020 / plasma membrane
Similarity search - Function
NADH-ubiquinone/plastoquinone oxidoreductase chain 6, subunit NuoJ / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #2700 / NADH:ubiquinone/plastoquinone oxidoreductase, chain 3 / Helix Hairpins - #3510 / NAD(P)H-quinone oxidoreductase subunit 3, bacterial/plastid / NAD(P)H-quinone oxidoreductase, subunit N/subunit 2 / NADH-ubiquinone/plastoquinone oxidoreductase chain 6, subunit NuoJ / NADH-plastoquinone oxidoreductase, chain 5 subgroup / NADH-quinone oxidoreductase, chain M/4 / NADH-ubiquinone oxidoreductase chain 4L/K ...NADH-ubiquinone/plastoquinone oxidoreductase chain 6, subunit NuoJ / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #2700 / NADH:ubiquinone/plastoquinone oxidoreductase, chain 3 / Helix Hairpins - #3510 / NAD(P)H-quinone oxidoreductase subunit 3, bacterial/plastid / NAD(P)H-quinone oxidoreductase, subunit N/subunit 2 / NADH-ubiquinone/plastoquinone oxidoreductase chain 6, subunit NuoJ / NADH-plastoquinone oxidoreductase, chain 5 subgroup / NADH-quinone oxidoreductase, chain M/4 / NADH-ubiquinone oxidoreductase chain 4L/K / NADH:ubiquinone/plastoquinone oxidoreductase, chain 6 / NADH-ubiquinone/plastoquinone oxidoreductase chain 6 / NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminal / NADH-quinone oxidoreductase, chain 5-like / NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminus / NADH-ubiquinone oxidoreductase chain 4L/Mnh complex subunit C1-like / NADH-ubiquinone/plastoquinone oxidoreductase chain 4L / NADH:ubiquinone/plastoquinone oxidoreductase, chain 3 / NADH:ubiquinone oxidoreductase, subunit 3 superfamily / NADH-ubiquinone/plastoquinone oxidoreductase, chain 3 / NADH:ubiquinone oxidoreductase / NADH:quinone oxidoreductase/Mrp antiporter, membrane subunit / Proton-conducting membrane transporter / Four Helix Bundle (Hemerythrin (Met), subunit A) / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Helix Hairpins / Up-down Bundle / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Chem-CA7 / EICOSANE / NADH-quinone oxidoreductase subunit M / NADH-quinone oxidoreductase subunit N / NADH-quinone oxidoreductase subunit A / Proton-translocating NADH-quinone oxidoreductase, chain L / NADH-quinone oxidoreductase subunit J / NADH-quinone oxidoreductase subunit K / NADH-quinone oxidoreductase subunit A / NADH-quinone oxidoreductase subunit J ...Chem-CA7 / EICOSANE / NADH-quinone oxidoreductase subunit M / NADH-quinone oxidoreductase subunit N / NADH-quinone oxidoreductase subunit A / Proton-translocating NADH-quinone oxidoreductase, chain L / NADH-quinone oxidoreductase subunit J / NADH-quinone oxidoreductase subunit K / NADH-quinone oxidoreductase subunit A / NADH-quinone oxidoreductase subunit J / NADH-quinone oxidoreductase subunit K / NADH-quinone oxidoreductase subunit L / NADH dehydrogenase I subunit M / NADH-quinone oxidoreductase subunit N
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 3 Å
AuthorsEfremov, R.G. / Sazanov, L.A.
CitationJournal: Nature / Year: 2011
Title: Structure of the membrane domain of respiratory complex I.
Authors: Efremov, R.G. / Sazanov, L.A.
History
DepositionApr 18, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 3, 2011Provider: repository / Type: Initial release
Revision 1.1Nov 2, 2011Group: Database references
Revision 1.2Feb 28, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / 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 / _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
L: NADH-QUINONE OXIDOREDUCTASE SUBUNIT L
M: NADH-QUINONE OXIDOREDUCTASE SUBUNIT M
N: NADH-QUINONE OXIDOREDUCTASE SUBUNIT N
K: NADH-QUINONE OXIDOREDUCTASE SUBUNIT K
A: NADH-QUINONE OXIDOREDUCTASE SUBUNIT A
J: NADH-QUINONE OXIDOREDUCTASE SUBUNIT J
B: NADH-QUINONE OXIDOREDUCTASE SUBUNIT L
C: NADH-QUINONE OXIDOREDUCTASE SUBUNIT M
D: NADH-QUINONE OXIDOREDUCTASE SUBUNIT N
G: NADH-QUINONE OXIDOREDUCTASE SUBUNIT K
E: NADH-QUINONE OXIDOREDUCTASE SUBUNIT A
F: NADH-QUINONE OXIDOREDUCTASE SUBUNIT J
hetero molecules


Theoretical massNumber of molelcules
Total (without water)450,85732
Polymers444,72612
Non-polymers6,13120
Water28816
1
L: NADH-QUINONE OXIDOREDUCTASE SUBUNIT L
M: NADH-QUINONE OXIDOREDUCTASE SUBUNIT M
N: NADH-QUINONE OXIDOREDUCTASE SUBUNIT N
K: NADH-QUINONE OXIDOREDUCTASE SUBUNIT K
A: NADH-QUINONE OXIDOREDUCTASE SUBUNIT A
J: NADH-QUINONE OXIDOREDUCTASE SUBUNIT J
hetero molecules


Theoretical massNumber of molelcules
Total (without water)225,42916
Polymers222,3636
Non-polymers3,06610
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area35210 Å2
ΔGint-286 kcal/mol
Surface area61680 Å2
MethodPISA
2
B: NADH-QUINONE OXIDOREDUCTASE SUBUNIT L
C: NADH-QUINONE OXIDOREDUCTASE SUBUNIT M
D: NADH-QUINONE OXIDOREDUCTASE SUBUNIT N
G: NADH-QUINONE OXIDOREDUCTASE SUBUNIT K
E: NADH-QUINONE OXIDOREDUCTASE SUBUNIT A
F: NADH-QUINONE OXIDOREDUCTASE SUBUNIT J
hetero molecules


Theoretical massNumber of molelcules
Total (without water)225,42916
Polymers222,3636
Non-polymers3,06610
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area35190 Å2
ΔGint-285 kcal/mol
Surface area61660 Å2
MethodPISA
Unit cell
Length a, b, c (Å)94.980, 116.570, 191.370
Angle α, β, γ (deg.)98.510, 104.080, 108.510
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11L
21B
12M
22C
13N
23D
14A
24E
15J
25F
16K
26G

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111METMETLEULEUchain L and (resseq 1:612 )LA1 - 6121 - 612
211METMETLEULEUchain B and (resseq 1:612 )BG1 - 6121 - 612
112METMETVALVALchain M and (resseq 1:504 )MB1 - 5041 - 504
212METMETVALVALchain C and (resseq 1:504 )CH1 - 5041 - 504
113METMETLYSLYSchain N and (resseq 1:191 or resseq 199:439 or resseq 445:485 )NC1 - 1911 - 191
123ASNASNGLNGLNchain N and (resseq 1:191 or resseq 199:439 or resseq 445:485 )NC199 - 439199 - 439
133PROPROMETMETchain N and (resseq 1:191 or resseq 199:439 or resseq 445:485 )NC445 - 485445 - 485
213METMETLYSLYSchain D and (resseq 1:191 or resseq 199:439 or resseq 445:485 )DI1 - 1911 - 191
223ASNASNGLNGLNchain D and (resseq 1:191 or resseq 199:439 or resseq 445:485 )DI199 - 439199 - 439
233PROPROMETMETchain D and (resseq 1:191 or resseq 199:439 or resseq 445:485 )DI445 - 485445 - 485
114ALAALAALAALAchain A and (resseq 15:43 or resseq 61:126 )AE15 - 4315 - 43
124ARGARGTHRTHRchain A and (resseq 15:43 or resseq 61:126 )AE61 - 12661 - 126
214ALAALAALAALAchain E and (resseq 15:43 or resseq 61:126 )EK15 - 4315 - 43
224ARGARGTHRTHRchain E and (resseq 15:43 or resseq 61:126 )EK61 - 12661 - 126
115METMETLEULEUchain J and (resseq 1:168 )JF1 - 1681 - 168
215METMETLEULEUchain F and (resseq 1:168 )FL1 - 1681 - 168
116METMETGLYGLYchain K and (resseq 1:100 )KD1 - 1001 - 100
216METMETGLYGLYchain G and (resseq 1:100 )GJ1 - 1001 - 100

NCS ensembles :
ID
1
2
3
4
5
6

NCS oper:
IDCodeMatrixVector
1given(-0.797791, -0.602932, 0.00157), (-0.602924, 0.797789, 0.003965), (-0.003643, 0.002216, -0.999991)-17.9562, 55.493801, 1.85354
2given(-0.798078, -0.602554, 0.000982), (-0.602546, 0.798074, 0.003907), (-0.003138, 0.002526, -0.999992)-17.944599, 55.492699, 1.8457
3given(-0.798182, -0.602412, 0.00204), (-0.602406, 0.798184, 0.002899), (-0.003374, 0.001085, -0.999994)-17.958401, 55.5336, 1.81377
4given(-0.797897, -0.602788, 0.002638), (-0.602787, 0.797901, 0.001255), (-0.002861, -0.000589, -0.999996)-17.971201, 55.612301, 1.74585
5given(-0.798118, -0.602492, 0.003313), (-0.602491, 0.798124, 0.001428), (-0.003505, -0.000856, -0.999993)-18.0105, 55.606998, 1.74131
6given(-0.797822, -0.602893, 0.001113), (-0.602891, 0.797822, 0.001549), (-0.001822, 0.000565, -0.999998)-17.9515, 55.585899, 1.81225

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Components

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NADH-QUINONE OXIDOREDUCTASE SUBUNIT ... , 6 types, 12 molecules LBMCNDKGAEJF

#1: Protein NADH-QUINONE OXIDOREDUCTASE SUBUNIT L / Proton-translocating NADH-quinone oxidoreductase / chain L


Mass: 66513.633 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: cytoplasmic membrane / Source: (natural) Escherichia coli (E. coli) / Strain: BL21(DE3)
References: UniProt: C6E9S4, UniProt: A0A140N7P6*PLUS, NADH:ubiquinone reductase (H+-translocating)
#2: Protein NADH-QUINONE OXIDOREDUCTASE SUBUNIT M / Proton-translocating NADH-quinone oxidoreductase / chain M


Mass: 56560.090 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: cytoplasmic membrane / Source: (natural) Escherichia coli (E. coli) / Strain: BL21(DE3)
References: UniProt: C6E9S5, UniProt: A0A140N571*PLUS, NADH:ubiquinone reductase (H+-translocating)
#3: Protein NADH-QUINONE OXIDOREDUCTASE SUBUNIT N / NADH dehydrogenase I subunit N 1 / NDH-1 subunit N 1


Mass: 52072.672 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: cytoplasmic membrane / Source: (natural) Escherichia coli (E. coli) / Strain: BL21(DE3)
References: UniProt: C6E9S6, UniProt: A0A140N755*PLUS, NADH:ubiquinone reductase (H+-translocating)
#4: Protein NADH-QUINONE OXIDOREDUCTASE SUBUNIT K / NADH dehydrogenase I subunit K / NDH-1 subunit K


Mass: 10852.961 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: cytoplasmic membrane / Source: (natural) Escherichia coli (E. coli) / Strain: BL21(DE3)
References: UniProt: C6E9S3, UniProt: C5W716*PLUS, NADH:ubiquinone reductase (H+-translocating)
#5: Protein NADH-QUINONE OXIDOREDUCTASE SUBUNIT A


Mass: 16474.283 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: cytoplasmic membrane / Source: (natural) Escherichia coli (E. coli) / Strain: BL21(DE3)
References: UniProt: C6E9R4, UniProt: A0A140N7N4*PLUS, NADH:ubiquinone reductase (H+-translocating)
#6: Protein NADH-QUINONE OXIDOREDUCTASE SUBUNIT J / NADH dehydrogenase subunit J


Mass: 19889.551 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: cytoplasmic membrane / Source: (natural) Escherichia coli (E. coli) / Strain: BL21(DE3)
References: UniProt: C6E9S2, UniProt: A0A140N7W8*PLUS, NADH:ubiquinone reductase (H+-translocating)

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Non-polymers , 3 types, 36 molecules

#7: Chemical
ChemComp-LFA / EICOSANE / LIPID FRAGMENT


Mass: 282.547 Da / Num. of mol.: 18 / Source method: obtained synthetically / Formula: C20H42
#8: Chemical ChemComp-CA7 / 7-cyclohexylheptyl 4-O-alpha-D-glucopyranosyl-beta-D-glucopyranoside


Mass: 522.626 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C25H46O11
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 16 / 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: 4.25 Å3/Da / Density % sol: 71.05 %
Crystal growTemperature: 296 K / Method: vapor diffusion, sitting drop / pH: 4.8
Details: 0.1M sodium acetate, 0.3M sodium tartrate, 9% PEG4000, 0.15% sodium cholate, 0.1M NDSB-256, pH 4.8, VAPOR DIFFUSION, SITTING DROP, temperature 296K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.9789, 0.9790, 0.85, 1.00
DetectorType: ADSC QUANTUM 210 / Detector: CCD / Date: Jul 3, 2010 / Details: mirrors
RadiationMonochromator: Si(311) / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
IDWavelength (Å)Relative weight
10.97891
20.9791
30.851
411
ReflectionResolution: 3→29.979 Å / Num. all: 139150 / Num. obs: 139150 / % possible obs: 95.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.6 % / Biso Wilson estimate: 65.9 Å2 / Rsym value: 0.165 / Net I/σ(I): 4.2
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Mean I/σ(I) obsNum. measured allNum. unique allRsym value% possible all
3-3.162.60.852731204521.21796
3.16-3.352.61.249800193820.79296.1
3.35-3.592.61.946545181040.47596.1
3.59-3.872.62.843531169960.2896.3
3.87-4.242.54.239634155600.16796.1
4.24-4.742.56.135698140890.11396
4.74-5.482.56.931189123300.10295.4
5.48-6.712.56.825319102450.11394.1
6.71-9.492.410.81921378460.06392.9
9.49-29.9792.715.31131841460.05490.4

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Processing

Software
NameVersionClassificationNB
MOSFLMdata reduction
SCALA3.3.16data scaling
PHENIX1.6.4_486refinement
PDB_EXTRACT3.1data extraction
ADSCQuantumdata collection
SHARPphasing
RefinementMethod to determine structure: MAD / Resolution: 3→19.991 Å / Occupancy max: 1 / Occupancy min: 1 / FOM work R set: 0.7704 / SU ML: 0.46 / Isotropic thermal model: TLS and isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
Details: Before refinement, the reflection data were anisotropically scaled and truncated to 3.4, 3.0 and 3.0 angstrom along a, b and c axes, respectively, using the Anisotropy Server at http: ...Details: Before refinement, the reflection data were anisotropically scaled and truncated to 3.4, 3.0 and 3.0 angstrom along a, b and c axes, respectively, using the Anisotropy Server at http://services.mbi.ucla.edu/anisoscale/.
RfactorNum. reflection% reflectionSelection details
Rfree0.2816 2546 2.02 %RANDOM
Rwork0.2319 ---
all0.2329 126323 --
obs0.2329 126323 86.46 %-
Solvent computationShrinkage radii: 0.27 Å / VDW probe radii: 0.6 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 40.869 Å2 / ksol: 0.27 e/Å3
Displacement parametersBiso max: 348.52 Å2 / Biso mean: 76.9128 Å2 / Biso min: 2.5 Å2
Baniso -1Baniso -2Baniso -3
1--5.9953 Å20.1213 Å2-0.6214 Å2
2---4.4125 Å21.1621 Å2
3---1.7671 Å2
Refinement stepCycle: LAST / Resolution: 3→19.991 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms30002 0 292 16 30310
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01633252
X-RAY DIFFRACTIONf_angle_d1.0742196
X-RAY DIFFRACTIONf_chiral_restr0.075000
X-RAY DIFFRACTIONf_plane_restr0.0055060
X-RAY DIFFRACTIONf_dihedral_angle_d14.33510708
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11L4676X-RAY DIFFRACTIONPOSITIONAL0.013
12B4676X-RAY DIFFRACTIONPOSITIONAL0.013
21M3953X-RAY DIFFRACTIONPOSITIONAL0.016
22C3953X-RAY DIFFRACTIONPOSITIONAL0.016
31N3590X-RAY DIFFRACTIONPOSITIONAL0.016
32D3590X-RAY DIFFRACTIONPOSITIONAL0.016
41A752X-RAY DIFFRACTIONPOSITIONAL0.011
42E752X-RAY DIFFRACTIONPOSITIONAL0.011
51J1270X-RAY DIFFRACTIONPOSITIONAL0.012
52F1270X-RAY DIFFRACTIONPOSITIONAL0.012
61K760X-RAY DIFFRACTIONPOSITIONAL0.014
62G760X-RAY DIFFRACTIONPOSITIONAL0.014
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 18

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection allNum. reflection obs% reflection obs (%)
3-3.05750.4451670.388434323499343243
3.0575-3.11970.3804870.328142994386429954
3.1197-3.18730.36941070.335151405247514065
3.1873-3.26110.39621200.334458836003588374
3.2611-3.34230.37961280.305666306758663084
3.3423-3.43220.3351460.268874247570742493
3.4322-3.53270.31521650.249276257790762596
3.5327-3.6460.29481840.241776207804762096
3.646-3.77550.28281610.238776707831767096
3.7755-3.92560.27291770.224575827759758296
3.9256-4.10280.28041620.213676507812765096
4.1028-4.3170.24861280.197176737801767396
4.317-4.58450.251470.176676297776762996
4.5845-4.93350.21061500.171776057755760596
4.9335-5.4210.25711570.206875837740758396
5.421-6.1850.29161390.258875627701756294
6.185-7.71720.29641640.262672647428726492
7.7172-19.99190.22751570.203575067663750695
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)
10.28470.13870.03990.10180.03630.1645-0.2367-0.4375-0.07540.20820.03890.00010.1324-0.14760.00260.5850.18690.15140.339-0.05410.2014-24.575419.815562.4224
20.054-0.01320.05150.12510.09180.3494-0.01350.0190.02870.0919-0.08160.043-0.0755-0.2135-0.02860.70780.36810.0340.2579-0.05340.07-11.076224.841555.2265
30.14840.1404-0.04540.23030.05360.1132-0.0872-0.21120.15210.42420.04810.0551-0.0541-0.07630.16911.22640.519-0.24880.5071-0.22760.0776-7.871336.509672.0651
40.18-0.08960.11330.1579-0.02680.2962-0.1765-0.16890.10160.30.0846-0.0925-0.16080.11080.21880.95050.3245-0.27010.1722-0.14540.1011-0.403839.618248.2978
50.37130.325-0.04340.2879-0.03590.0901-0.21440.2264-0.0169-0.10310.00930.21750.0291-0.290.01610.35620.0784-0.02450.4426-0.1710.1019-31.45614.948416.1424
60.25270.2220.31740.63130.4270.46510.2198-0.0769-0.2560.25930.0179-0.17140.0630.06690.24680.1613-0.1195-0.07370.0805-0.01130.2377-16.34135.39719.8542
70.23520.09770.02580.5635-0.11310.3383-0.0615-0.0093-0.1039-0.04890.1377-0.1377-0.0122-0.2349-0.0020.0033-0.0246-0.01660.1492-0.02570.1343-20.806422.562113.476
80.43120.18490.04760.15650.05410.1005-0.042-0.02620.19320.0267-0.08050.07720.02610.0189-0.08780.0583-0.11420.00080.03180.01540.1936-5.792523.156411.328
90.2220.00770.07880.0910.09760.17080.0227-0.2020.0780.12540.0301-0.07160.1006-0.1615-0.23760.0492-0.119-0.0169-0.1869-0.11420.065-10.79823.560731.3525
100.27230.0826-0.05650.1752-0.05410.04190.03990.11040.0871-0.13380.0002-0.04790.0412-0.02390.1958-0.2033-0.13110.15350.08260.07210.1217-5.586924.6833-20.647
110.07210.0961-0.04580.1435-0.03060.0483-0.08620.1271-0.14990.0032-0.05110.13670.0021-0.0931-0.1777-0.1317-0.15510.00140.0362-0.02040.1392-11.275221.2114-4.8201
120.04230.0190.01380.0091-0.00020.0687-0.09880.07850.06140.0018-0.06050.01840.15120.208-0.00790.24830.26720.26740.65820.21120.425320.833535.5878-31.3952
130.23550.13430.00210.14750.0012-0.0008-0.0475-0.0827-0.1681-0.06560.0451-0.0861-0.02740.050.1750.05490.06780.11790.42830.24930.22549.543731.8129-36.7255
140.0063-0.0029-0.00330.00110.00210.00220.0582-0.0456-0.02-0.2392-0.01310.0084-0.1417-0.0009-0.00010.25130.07720.01260.38270.04650.674-1.683251.3728-24.5917
150.07750.0492-0.0350.0816-0.00680.0250.00170.12420.07590.0040.12330.1011-0.09030.0272-0.01060.76330.36280.21020.73290.34970.147910.316940.8086-55.2788
160.03340.00460.04170.02920.01560.05540.05320.2290.0810.00670.03240.00210.10440.14380.00040.76170.3023-0.25360.51840.07990.2033-2.986534.0837-47.9365
170.33620.1701-0.07710.2007-0.03960.10780.05430.08090.07420.04740.07170.0473-0.1284-0.05130.02310.82220.4074-0.07660.4536-0.06020.0524-7.632223.7529-49.5734
180.23280.03430.01920.17410.01370.08540.0219-0.01520.226-0.04620.0330.06510.13960.2525-0.00470.43890.08970.40790.60420.28630.369317.081538.1855-43.9181
190.140.07660.00520.04620.02490.0814-0.05520.16210.553-0.13270.09120.0934-0.3059-0.0801-0.00520.43220.076-0.06560.8188-0.04380.592820.410439.9608-29.7205
200.73050.3629-0.10130.2084-0.08270.2161-0.0339-0.03520.305-0.08820.02180.081-0.4446-0.38870.02950.780.3207-0.09580.403-0.03140.1633-4.65729.5568-40.4188
210.28270.06640.24330.36250.10260.2635-0.0250.2157-0.0535-0.4678-0.11550.1118-0.15090.1043-0.01330.47690.13850.11820.20380.0560.164226.5712-24.3408-60.7198
220.0304-0.0231-0.060.054-0.04010.22860.11220.05210.0736-0.1497-0.13160.0299-0.22080.0090.0980.65560.1895-0.16550.03310.026-0.1327.8358-28.2744-58.4033
230.09450.0425-0.00330.05540.04550.07410.170.1650.0353-0.2677-0.00410.08180.3198-0.11050.25811.19930.3144-0.26990.32880.0423-0.03843.5787-15.0961-76.006
240.09810.02990.05010.43460.05480.35310.0050.0824-0.0248-0.3553-0.16860.1123-0.0386-0.2242-0.07380.89260.4066-0.32120.2314-0.13290.1025-4.5997-23.1471-46.4794
250.34560.0922-0.07560.0262-0.03290.11940.0721-0.09140.16520.1159-0.1611-0.1203-0.13180.22720.01880.40560.0602-0.08770.42350.08990.126635.1691-24.1811-14.4682
260.36760.09680.30.4658-0.23850.48320.1850.1606-0.344-0.0340.1055-0.00780.1629-0.00520.10170.11030.1011-0.16230.2545-0.05930.241728.8494-40.9003-18.2023
270.7494-0.1567-0.02860.1767-0.02170.11010.0333-0.1326-0.1825-0.0070.07060.0573-0.09710.1008-0.0045-0.0665-0.10580.01450.1805-0.06190.111522.0887-24.5261-11.762
280.18380.04850.05460.01390.00950.0335-0.05140.11820.0566-0.0079-0.0310.0066-0.0142-0.0345-0.0413-0.0803-0.03450.00720.0872-0.00280.24829.7555-33.1043-9.5968
290.0794-0.03630.11790.12510.05080.30680.03390.1266-0.0109-0.030.05530.00210.04470.18330.1248-0.00910.02160.0150.07030.00720.081213.4444-29.7159-29.6243
300.4209-0.1083-0.09680.12140.02780.0877-0.0221-0.14860.04410.2020.0584-0.00420.03880.01950.2211-0.0486-0.09450.1190.1175-0.02040.14348.6726-32.11122.678
310.15710.0773-0.09390.0588-0.06010.06410.0685-0.18540.090.0715-0.1164-0.2747-0.06630.15990.1151-0.2038-0.16410.00760.0982-0.03610.247415.487-31.42376.2133
320.15770.04670.10720.01990.03020.1429-0.127-0.10830.0925-0.0013-0.1090.00040.1484-0.0246-0.02730.6153-0.28240.33490.42630.02020.3884-18.8247-39.357933.2202
330.1701-0.07250.07440.0879-0.06350.1056-0.0313-0.0649-0.0735-0.04160.14170.04840.0616-0.12810.2480.3428-0.22110.32820.3261-0.10360.3646-7.5344-35.564938.531
340.2635-0.21450.16040.2631-0.16240.1087-0.07660.0667-0.00190.06170.07170.0317-0.07480.0029-0.00420.2452-0.23660.0410.1814-0.01560.4104-10.3906-13.182826.4159
350.0106-0.0012-0.01470.00320.00980.0434-0.0739-0.12630.1435-0.02830.00390.0343-0.0413-0.0225-0.00011.3746-0.04530.38880.6496-0.20130.4019-13.4828-28.82957.0806
360.02110.01470.02590.01530.02340.06090.1739-0.13470.04570.0559-0.01740.04880.13010.0511-0.00011.10790.0711-0.06840.5013-0.1990.26812.2903-29.59650.5001
370.2531-0.10310.00940.1257-0.01480.06690.1395-0.07820.0308-0.04140.03880.0447-0.13370.0920.00680.94070.1210.06990.20320.04170.033311.3724-28.262650.5692
380.0026-0.002-0.00240.00860.0030.013-0.0323-0.0381-0.03950.0522-0.05490.02030.1092-0.0441-00.6352-0.11390.43940.59920.01040.3666-24.6321-41.322142.9103
390.01960.01840.00870.0380.0460.0724-0.04420.0269-0.03820.0166-0.02290.02920.0813-0.1363-0.12140.3888-0.12040.4270.67580.16760.6121-19.253-33.901145.4651
400.15780.0377-0.02730.0205-0.00730.00410.0379-0.00380.1277-0.0224-0.0023-0.01340.1295-0.0299-0.09020.7266-0.0470.50850.402-0.02350.3289-9.9326-31.079448.2302
410.00040.00010.0009-0.00010.00040.0013-0.02260.0645-0.01230.00390.03110.0365-0.0061-0.0481-0.00021.7107-0.08770.08331.74560.00241.6131-23.3853-14.871335.4498
420.0556-0.05470.06620.1086-0.05570.4477-0.1314-0.02310.2306-0.0332-0.02510.0894-0.1283-0.1262-0.00130.1905-0.2129-0.07250.4285-0.0090.5253-23.8108-36.249524.5079
430.00910.0008-0.00630.0113-0.00180.0044-0.0171-0.04470.0185-0.0509-0.0665-0.0088-0.02050.0157-0.00011.1675-0.0927-0.02621.3873-0.03051.121-13.5759-57.692940.404
440.00190.0012-0.0010.00190.00180.0044-0.03150.02040.00420.0268-0.00790.0377-0.0158-0.0018-0.00020.65050.2368-0.12380.1778-0.06080.33114.0621-49.285247.5706
450.2096-0.0183-0.01950.1851-0.02330.03830.0048-0.0546-0.06090.0005-0.003-0.0131-0.15030.0039-0.00250.6299-0.0331-0.05730.247-0.05530.03666.6262-29.529540.3987
460.00090.0006-0.00090.0002-0.00040.00160.0355-0.04550.0422-0.02590.0335-0.0053-0.04370.02230.00011.18920.0185-0.05580.8333-0.04511.09483.4664-3.392239.58
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(chain L and (resseq 1:106))L1 - 106
2X-RAY DIFFRACTION2(chain L and (resseq 107:214))L0
3X-RAY DIFFRACTION3(chain L and (resseq 215:450))L0
4X-RAY DIFFRACTION4(chain L and (resseq 451:612))L0
5X-RAY DIFFRACTION5(chain M and (resseq 1:49))M1 - 49
6X-RAY DIFFRACTION6(chain M and (resseq 50:103))M50 - 103
7X-RAY DIFFRACTION7(chain M and (resseq 104:157))M0
8X-RAY DIFFRACTION8(chain M and (resseq 158:200))M0
9X-RAY DIFFRACTION9(chain M and (resseq 201:504))M0
10X-RAY DIFFRACTION10(chain N and (resseq 1:389))N1 - 389
11X-RAY DIFFRACTION11(chain N and (resseq 390:485))N0
12X-RAY DIFFRACTION12(chain K and (resseq 1:27))K1 - 27
13X-RAY DIFFRACTION13(chain K and (resseq 28:84))K28 - 84
14X-RAY DIFFRACTION14(chain K and (resseq 85:100))K85 - 100
15X-RAY DIFFRACTION15(chain A and (resseq 15:42))A15 - 42
16X-RAY DIFFRACTION16(chain A and (resseq 43:90))A43 - 90
17X-RAY DIFFRACTION17(chain A and (resseq 91:126))A91 - 126
18X-RAY DIFFRACTION18(chain J and (resseq 1:74))J1 - 74
19X-RAY DIFFRACTION19(chain J and (resseq 75:125))J75 - 125
20X-RAY DIFFRACTION20(chain J and (resseq 126:169))J0
21X-RAY DIFFRACTION21(chain B and (resseq 1:106))B1 - 106
22X-RAY DIFFRACTION22(chain B and (resseq 107:325))B0
23X-RAY DIFFRACTION23(chain B and (resseq 326:450))B0
24X-RAY DIFFRACTION24(chain B and (resseq 451:612))B0
25X-RAY DIFFRACTION25(chain C and (resseq 1:49))C1 - 49
26X-RAY DIFFRACTION26(chain C and (resseq 50:103))C50 - 103
27X-RAY DIFFRACTION27(chain C and (resseq 104:157))C0
28X-RAY DIFFRACTION28(chain C and (resseq 158:200))C0
29X-RAY DIFFRACTION29(chain C and (resseq 201:504))C0
30X-RAY DIFFRACTION30(chain D and (resseq 1:384))D1 - 384
31X-RAY DIFFRACTION31(chain D and (resseq 385:485))D0
32X-RAY DIFFRACTION32(chain G and (resseq 1:27))G1 - 27
33X-RAY DIFFRACTION33(chain G and (resseq 28:84))G28 - 84
34X-RAY DIFFRACTION34(chain G and (resseq 85:100))G85 - 100
35X-RAY DIFFRACTION35(chain E and (resseq 15:42))E15 - 42
36X-RAY DIFFRACTION36(chain E and (resseq 43:95))E43 - 95
37X-RAY DIFFRACTION37(chain E and (resseq 96:126))E96 - 126
38X-RAY DIFFRACTION38(chain F and (resseq 1:21))F1 - 21
39X-RAY DIFFRACTION39(chain F and (resseq 22:46))F22 - 46
40X-RAY DIFFRACTION40(chain F and (resseq 47:74))F47 - 74
41X-RAY DIFFRACTION41(chain F and (resseq 75:87))F75 - 87
42X-RAY DIFFRACTION42(chain F and (resseq 88:111))F88 - 111
43X-RAY DIFFRACTION43(chain F and (resseq 112:125))F0
44X-RAY DIFFRACTION44(chain F and (resseq 126:137))F0
45X-RAY DIFFRACTION45(chain F and (resseq 138:159))F0
46X-RAY DIFFRACTION46(chain F and (resseq 160:169))F0

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