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- PDB-2yev: Structure of caa3-type cytochrome oxidase -

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Basic information

Entry
Database: PDB / ID: 2yev
TitleStructure of caa3-type cytochrome oxidase
Components
  • (CYTOCHROME C OXIDASE ...) x 2
  • CAA3-TYPE CYTOCHROME OXIDASE SUBUNIT IV
KeywordsELECTRON TRANSPORT
Function / homology
Function and homology information


cytochrome-c oxidase / oxidative phosphorylation / electron transport coupled proton transport / cytochrome-c oxidase activity / respirasome / aerobic respiration / respiratory electron transport chain / membrane => GO:0016020 / copper ion binding / heme binding ...cytochrome-c oxidase / oxidative phosphorylation / electron transport coupled proton transport / cytochrome-c oxidase activity / respirasome / aerobic respiration / respiratory electron transport chain / membrane => GO:0016020 / copper ion binding / heme binding / metal ion binding / plasma membrane
Similarity search - Function
Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #110 / Cytochrome oxidase Caa3-type, subunit IV / Caa3-type Cytochrome c oxidase subunit II, cupredoxin domain / Cytochrome oxidase Caa3-type, subunit IV superfamily / Cytochrome c oxidase, subunit I bacterial type / Cytochrome c oxidase, subunit III, four-helix bundle / Helix Hairpins - #90 / Cytochrome C Oxidase; Chain A / Cytochrome c oxidase-like, subunit I domain / Cytochrome c oxidase, subunit II ...Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #110 / Cytochrome oxidase Caa3-type, subunit IV / Caa3-type Cytochrome c oxidase subunit II, cupredoxin domain / Cytochrome oxidase Caa3-type, subunit IV superfamily / Cytochrome c oxidase, subunit I bacterial type / Cytochrome c oxidase, subunit III, four-helix bundle / Helix Hairpins - #90 / Cytochrome C Oxidase; Chain A / Cytochrome c oxidase-like, subunit I domain / Cytochrome c oxidase, subunit II / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Cytochrome C oxidase subunit II, transmembrane domain / Cytochrome c oxidase subunit III-like / Cytochrome c oxidase, subunit III, 4-helical bundle / Cytochrome c oxidase subunit III / Heme-copper oxidase subunit III family profile. / Cytochrome c oxidase subunit III-like superfamily / Cytochrome C oxidase subunit II, transmembrane domain / Cytochrome oxidase subunit II transmembrane region profile. / Copper centre Cu(A) / CO II and nitrous oxide reductase dinuclear copper centers signature. / Cytochrome C oxidase subunit II, transmembrane domain superfamily / Cytochrome c oxidase, subunit I, copper-binding site / Heme-copper oxidase catalytic subunit, copper B binding region signature. / Cytochrome c oxidase-like, subunit I domain / Cytochrome oxidase subunit I profile. / Cytochrome c oxidase subunit I / Cytochrome c oxidase-like, subunit I superfamily / Cytochrome C and Quinol oxidase polypeptide I / Cytochrome C oxidase subunit II, periplasmic domain / Cytochrome c oxidase subunit II-like C-terminal / Cytochrome oxidase subunit II copper A binding domain profile. / Helix Hairpins - #70 / Cytochrome c / Cupredoxins - blue copper proteins / Cytochrome c family profile. / Cytochrome c-like domain / Cytochrome c-like domain superfamily / Four Helix Bundle (Hemerythrin (Met), subunit A) / Cupredoxin / Helix non-globular / Special / Helix Hairpins / Up-down Bundle / Immunoglobulin-like / Sandwich / Orthogonal Bundle / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
(2R)-3-HYDROXYPROPANE-1,2-DIYL DIHEXADECANOATE / Chem-5PL / (2R)-2,3-DIHYDROXYPROPYL (7Z)-TETRADEC-7-ENOATE / 1,3-DIHYDROXYPROPAN-2-YL (Z)-TETRADEC-7-ENOATE / COPPER (II) ION / DINUCLEAR COPPER ION / HEME-AS / HEME C / Cytochrome c oxidase polypeptide I+III / Uncharacterized protein / Cytochrome c oxidase subunit 2
Similarity search - Component
Biological speciesTHERMUS THERMOPHILUS (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.36 Å
AuthorsLyons, J.A. / Aragao, D. / Soulimane, T. / Caffrey, M.
CitationJournal: Nature / Year: 2012
Title: Structural Insights Into Electron Transfer in Caa3-Type Cytochrome Oxidases.
Authors: Lyons, J.A. / Aragao, D. / Slattery, O. / Pisliakov, A.V. / Soulimane, T. / Caffrey, M.
History
DepositionMar 31, 2011Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 23, 2012Provider: repository / Type: Initial release
Revision 1.1Jun 27, 2012Group: Other
Revision 1.2Aug 1, 2012Group: Database references
Revision 1.3Apr 29, 2015Group: Data collection
Revision 1.4Mar 6, 2019Group: Data collection / Derived calculations ...Data collection / Derived calculations / Experimental preparation / Other
Category: exptl_crystal_grow / pdbx_database_proc ...exptl_crystal_grow / pdbx_database_proc / pdbx_database_status / struct_conn
Item: _exptl_crystal_grow.method / _pdbx_database_status.recvd_author_approval / _struct_conn.pdbx_leaving_atom_flag
Revision 1.5May 8, 2019Group: Advisory / Data collection / Derived calculations
Category: database_PDB_caveat / diffrn_source ...database_PDB_caveat / diffrn_source / pdbx_data_processing_status / pdbx_struct_conn_angle / pdbx_validate_close_contact / struct_conn
Item: _diffrn_source.pdbx_synchrotron_site
Revision 1.6Jul 10, 2019Group: Data collection / Category: diffrn_source / Item: _diffrn_source.pdbx_synchrotron_site
Revision 1.7Mar 29, 2023Group: Database references / Derived calculations ...Database references / Derived calculations / Other / Structure summary
Category: audit_author / database_2 ...audit_author / database_2 / pdbx_database_status / pdbx_struct_conn_angle / struct_conn / struct_conn_type / struct_site
Item: _audit_author.identifier_ORCID / _database_2.pdbx_DOI ..._audit_author.identifier_ORCID / _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.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.value / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _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.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_type.id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.8Feb 7, 2024Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model / pdbx_validate_chiral

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: CYTOCHROME C OXIDASE POLYPEPTIDE I+III
B: CYTOCHROME C OXIDASE SUBUNIT 2
C: CAA3-TYPE CYTOCHROME OXIDASE SUBUNIT IV
D: CYTOCHROME C OXIDASE POLYPEPTIDE I+III
E: CYTOCHROME C OXIDASE SUBUNIT 2
F: CAA3-TYPE CYTOCHROME OXIDASE SUBUNIT IV
hetero molecules


Theoretical massNumber of molelcules
Total (without water)277,44127
Polymers268,0466
Non-polymers9,39521
Water7,062392
1
D: CYTOCHROME C OXIDASE POLYPEPTIDE I+III
E: CYTOCHROME C OXIDASE SUBUNIT 2
F: CAA3-TYPE CYTOCHROME OXIDASE SUBUNIT IV
hetero molecules


Theoretical massNumber of molelcules
Total (without water)138,00312
Polymers134,0233
Non-polymers3,9809
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area17250 Å2
ΔGint-241.6 kcal/mol
Surface area39020 Å2
MethodPISA
2
A: CYTOCHROME C OXIDASE POLYPEPTIDE I+III
B: CYTOCHROME C OXIDASE SUBUNIT 2
C: CAA3-TYPE CYTOCHROME OXIDASE SUBUNIT IV
hetero molecules


Theoretical massNumber of molelcules
Total (without water)139,43815
Polymers134,0233
Non-polymers5,41512
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area19680 Å2
ΔGint-237.7 kcal/mol
Surface area39040 Å2
MethodPISA
Unit cell
Length a, b, c (Å)127.250, 76.030, 300.267
Angle α, β, γ (deg.)90.00, 92.21, 90.00
Int Tables number5
Space group name H-MI121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
12
22
13
23

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111CHAIN A AND (RESSEQ 13:149 OR RESSEQ 151:341 OR RESSEQ...
211CHAIN D AND (RESSEQ 13:149 OR RESSEQ 151:341 OR RESSEQ...
112CHAIN B AND (RESSEQ 22:49 OR RESSEQ 52:64 OR RESSEQ...
212CHAIN E AND (RESSEQ 22:49 OR RESSEQ 52:64 OR RESSEQ...
113CHAIN C AND (RESSEQ 1:35 OR RESSEQ 37:39 OR RESSEQ 41:63 )
213CHAIN F AND (RESSEQ 1:35 OR RESSEQ 37:39 OR RESSEQ 41:63 )

NCS ensembles :
ID
1
2
3

NCS oper:
IDCodeMatrixVector
1given(-0.19371, 0.77608, -0.60014), (0.76941, -0.25935, -0.58373), (-0.60867, -0.57483, -0.54689)42.19324, 25.23582, 63.46266
2given(-0.19028, 0.787, -0.58688), (0.77301, -0.24841, -0.58374), (-0.60519, -0.56473, -0.56109)41.01546, 25.30559, 64.80436
3given(-0.19782, 0.76694, -0.61047), (0.77547, -0.2585, -0.57605), (-0.5996, -0.58735, -0.5436)42.8886, 24.63366, 62.96182

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Components

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CYTOCHROME C OXIDASE ... , 2 types, 4 molecules ADBE

#1: Protein CYTOCHROME C OXIDASE POLYPEPTIDE I+III / CYTOCHROME C AA(3) SUBUNIT 1 / A-PROTEIN / CYTOCHROME CAA3CAA3-TYPE CYTOCHROME OXIDASE SUBUNIT I/III


Mass: 89281.133 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: COVALENT LINK BETWEEN HIS 250 NE2 AND TYR 254 CE2 / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Strain: HB8 / References: UniProt: P98005, cytochrome-c oxidase
#2: Protein CYTOCHROME C OXIDASE SUBUNIT 2 / / CAA3-TYPE CYTOCHROME OXIDASE SUBUNIT IIC


Mass: 37387.957 Da / Num. of mol.: 2 / Source method: isolated from a natural source
Details: COVALENT LINK BETWEEN CYS SG 247 AND HEC CAB 587 COVALENT LINK BETWEEN CYS SG 250 AND HEC CAC 587
Source: (natural) THERMUS THERMOPHILUS (bacteria) / Strain: HB8 / References: UniProt: Q5SLI2, cytochrome-c oxidase

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Protein , 1 types, 2 molecules CF

#3: Protein CAA3-TYPE CYTOCHROME OXIDASE SUBUNIT IV / UNCHARACTERIZED PROTEIN TTHA1863


Mass: 7354.026 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: N-FORMYL GROUP ON MET 1 / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Strain: HB8 / References: UniProt: Q5SH67, cytochrome-c oxidase

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Non-polymers , 11 types, 413 molecules

#4: Chemical ChemComp-5PL / (1R,4S,6R)-6-({[2-(ACETYLAMINO)-2-DEOXY-ALPHA-D-GLUCOPYRANOSYL]OXY}METHYL)-4-HYDROXY-1-{[(15-METHYLHEXADECANOYL)OXY]METHYL}-4-OXIDO-7-OXO-3,5-DIOXA-8-AZA-4-PHOSPHAHEPTACOS-1-YL 15-METHYLHEXADECANOATE


Mass: 1233.719 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C67H129N2O15P
#5: Chemical
ChemComp-HAS / HEME-AS


Mass: 920.954 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C54H64FeN4O6
#6: Chemical ChemComp-CU / COPPER (II) ION / Copper


Mass: 63.546 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cu
#7: Chemical ChemComp-4AG / (2R)-3-HYDROXYPROPANE-1,2-DIYL DIHEXADECANOATE / SN-1,2-DIPALMITOYL DIACYLGLYCEROL


Mass: 568.911 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C35H68O5
#8: Chemical ChemComp-7E8 / (2R)-2,3-DIHYDROXYPROPYL (7Z)-TETRADEC-7-ENOATE / 7.7 MAG


Mass: 300.434 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C17H32O4
#9: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#10: Chemical ChemComp-CUA / DINUCLEAR COPPER ION


Mass: 127.092 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cu2
#11: Chemical ChemComp-HEC / HEME C / Heme C


Mass: 618.503 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C34H34FeN4O4
#12: Chemical ChemComp-7E9 / 1,3-DIHYDROXYPROPAN-2-YL (Z)-TETRADEC-7-ENOATE


Mass: 300.434 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C17H32O4
#13: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Cl
#14: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 392 / Source method: isolated from a natural source / Formula: H2O

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Details

Nonpolymer detailsHEME C (HEC): THIOETHER CROSSLINKS BETWEEN ATOMS CAB AND SG OF CYS 247 IN CHAINS B AND E. THIOETHER ...HEME C (HEC): THIOETHER CROSSLINKS BETWEEN ATOMS CAB AND SG OF CYS 247 IN CHAINS B AND E. THIOETHER CROSSLINKS BETWEEN ATOMS CAC AND SG OF CYS 250 IN CHAINS B AND E.

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 21

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Sample preparation

CrystalDensity Matthews: 2.78 Å3/Da / Density % sol: 55.83 % / Description: NONE
Crystal growMethod: lipidic cubic phase / pH: 5
Details: 16-21% PEG 400, 0.1 M NA CITRATE PH 4.5-5.0, 0-0.1 M LITHIUM SULPHATE, 0.1 M NACL. CRYSTALLISED USING THE LIPIDIC CUBIC PHASE USING 7.7 MAG AS THE HOSTING LIPID.

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Data collection

Diffraction
IDMean temperature (K)Crystal-ID
11001
21001
Diffraction source
SourceSiteBeamlineIDWavelength
SYNCHROTRONAPS 23-ID-B10.97777
SYNCHROTRONDiamond I242
Detector
TypeIDDetectorDateDetails
MARRESEARCH1CCDJun 17, 2010TWO K-B PAIRS OF BIMORPH TYPE MIRRORS
MARRESEARCH2CCD
Radiation
IDMonochromatorProtocolMonochromatic (M) / Laue (L)Scattering typeWavelength-ID
1ACCEL FIXED EXIT DOUBLE CRYSTAL SI(111)SINGLE WAVELENGTHMx-ray1
2SINGLE WAVELENGTHMx-ray1
Radiation wavelengthWavelength: 0.97777 Å / Relative weight: 1
ReflectionResolution: 2.36→53.48 Å / Num. obs: 118251 / % possible obs: 100 % / Observed criterion σ(I): -3 / Redundancy: 8.4 % / Rmerge(I) obs: 0.16 / Net I/σ(I): 9.5
Reflection shellResolution: 2.36→2.49 Å / Redundancy: 8.2 % / Rmerge(I) obs: 0.98 / Mean I/σ(I) obs: 2.3 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE: 1.6.4_486)refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2OCC

2occ


Resolution: 2.36→77.179 Å / SU ML: 0.39 / σ(F): 1.37 / Phase error: 20.42 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2183 5969 5.1 %
Rwork0.1712 --
obs0.1736 118243 99.95 %
Solvent computationShrinkage radii: 1.17 Å / VDW probe radii: 1.4 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 63.021 Å2 / ksol: 0.328 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--1.392 Å20 Å2-3.4644 Å2
2--6.891 Å20 Å2
3----5.499 Å2
Refinement stepCycle: LAST / Resolution: 2.36→77.179 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms18560 0 630 392 19582
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00619884
X-RAY DIFFRACTIONf_angle_d1.08427125
X-RAY DIFFRACTIONf_dihedral_angle_d14.5326758
X-RAY DIFFRACTIONf_chiral_restr0.0632884
X-RAY DIFFRACTIONf_plane_restr0.0043316
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A5736X-RAY DIFFRACTIONPOSITIONAL
12D5736X-RAY DIFFRACTIONPOSITIONAL0.033
21B2171X-RAY DIFFRACTIONPOSITIONAL
22E2171X-RAY DIFFRACTIONPOSITIONAL0.035
31C474X-RAY DIFFRACTIONPOSITIONAL
32F474X-RAY DIFFRACTIONPOSITIONAL0.02
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.36-2.38680.29991870.24593712X-RAY DIFFRACTION100
2.3868-2.41490.27812150.23373674X-RAY DIFFRACTION100
2.4149-2.44440.31922060.24523728X-RAY DIFFRACTION100
2.4444-2.47530.33261730.26023729X-RAY DIFFRACTION100
2.4753-2.50790.32092080.24433714X-RAY DIFFRACTION100
2.5079-2.54220.27521990.2123740X-RAY DIFFRACTION100
2.5422-2.57860.30271890.22153696X-RAY DIFFRACTION100
2.5786-2.61710.25681670.20593785X-RAY DIFFRACTION100
2.6171-2.6580.25661960.193704X-RAY DIFFRACTION100
2.658-2.70150.25641950.17723741X-RAY DIFFRACTION100
2.7015-2.74810.25092220.18663680X-RAY DIFFRACTION100
2.7481-2.79810.27772110.18643733X-RAY DIFFRACTION100
2.7981-2.85190.24752050.17763694X-RAY DIFFRACTION100
2.8519-2.91010.22741920.16963763X-RAY DIFFRACTION100
2.9101-2.97340.24851950.17263719X-RAY DIFFRACTION100
2.9734-3.04260.2251940.16223742X-RAY DIFFRACTION100
3.0426-3.11870.23561900.16233708X-RAY DIFFRACTION100
3.1187-3.2030.20521930.15913754X-RAY DIFFRACTION100
3.203-3.29720.23192200.16753744X-RAY DIFFRACTION100
3.2972-3.40370.25941810.173735X-RAY DIFFRACTION100
3.4037-3.52530.23882160.16823754X-RAY DIFFRACTION100
3.5253-3.66650.2071850.16163735X-RAY DIFFRACTION100
3.6665-3.83330.22621730.16593777X-RAY DIFFRACTION100
3.8333-4.03540.20781950.16883769X-RAY DIFFRACTION100
4.0354-4.28820.2121980.17013749X-RAY DIFFRACTION100
4.2882-4.61930.18452070.16043756X-RAY DIFFRACTION100
4.6193-5.08410.18312080.14523782X-RAY DIFFRACTION100
5.0841-5.81950.1852080.15633778X-RAY DIFFRACTION100
5.8195-7.33110.18932060.17053809X-RAY DIFFRACTION100
7.3311-77.22020.19052350.16273870X-RAY DIFFRACTION99
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)
10.50540.15180.22050.21610.28710.62120.0652-0.0214-0.19440.08-0.0112-0.09140.2069-0.0164-0.05270.2056-0.025-0.02140.1139-0.00210.26828.5677-20.046496.113
20.1943-0.04590.16240.4925-0.08730.752-0.0258-0.06620.1767-0.0067-0.0605-0.2144-0.0923-0.03450.09150.12890.026-0.01760.1855-0.09490.227-5.03167.3808104.4646
30.11150.07990.21180.13280.15041.0639-0.0449-0.1386-0.0703-0.014-0.04530.1328-0.0776-0.32650.10720.20060.01170.0020.3836-0.06640.2524-20.782-6.676186.8437
41.09340.33840.06670.6547-0.35340.49010.1014-0.2486-0.0919-0.0707-0.1842-0.09490.0946-0.06370.06240.1185-0.01330.02170.1769-0.03420.088-21.3255-7.929975.6973
50.8756-0.0945-0.08040.32210.1070.3347-0.08610.25570.0048-0.0651-0.0341-0.0533-0.0538-0.00240.10280.19660.0078-0.02850.2047-0.03110.1502-17.0711-0.897257.7305
60.11090.1922-0.20440.3646-0.26820.69970.00110.0661-0.0245-0.00260.0908-0.05820.0483-0.2321-0.07450.4496-0.16940.1060.57910.05370.4879-11.8774-25.7291107.6305
70.0239-0.02030.02590.1752-0.16240.1654-0.0078-0.017-0.01920.0563-0.0092-0.0207-0.14560.01360.02090.8225-0.0713-0.12270.80330.20650.8185.6841-33.3691118.7888
80.30430.01290.30330.5991-0.62951.0039-0.038-0.1062-0.15210.0124-0.1669-0.2118-0.0607-0.03980.12540.4022-0.1532-0.03560.37750.19610.4787-9.073-32.3698101.9518
90.8472-0.00170.57230.53560.37011.2775-0.05370.3457-0.0473-0.1360.1223-0.0396-0.11160.2065-0.06320.1668-0.03480.00650.3337-0.01760.12-32.6823-19.080917.2182
100.2931-0.2071-0.4460.79190.55250.7722-0.09120.1302-0.1765-0.00910.193-0.39190.1370.2686-0.20730.46070.3115-0.15530.7764-0.49270.5815-7.6947-43.123213.3843
110.8659-0.3047-0.2130.2922-0.24760.63410.2109-0.03950.0854-0.2610.3174-0.15240.102-0.523-0.49650.6797-0.10710.10631.0225-0.07060.3667-28.3999-37.3942-16.1494
120.0670.06610.08480.08850.15340.24920.02260.0009-0.02290.07160.1507-0.13570.13120.0861-0.14830.67430.1422-0.23010.6438-0.26180.7651-22.177-49.072616.3434
130.53440.00060.12580.08990.180.4790.27740.3297-0.19780.03020.1583-0.20940.08830.5881-0.34980.17310.2071-0.16220.5075-0.20990.3485-3.2612-32.234240.6617
140.21920.00770.03530.18970.11560.06420.05490.1811-0.08270.11240.1226-0.2240.13560.3011-0.12080.29680.2863-0.19150.6333-0.31320.5188.4652-33.142242.903
150.16250.1952-0.12030.44830.04040.26230.14550.0118-0.19240.15840.0929-0.29230.12590.0126-0.20830.59850.0459-0.24790.7074-0.18420.682315.8036-13.93154.9677
160.2206-0.2570.21031.00970.49560.9770.12170.5891-0.0354-0.03430.4551-0.5640.10890.7295-0.49560.23910.0925-0.12750.8249-0.24490.44648.3574-17.883643.974
170.0219-0.09860.05940.99790.1460.57350.13590.5162-0.24990.08320.1434-0.53350.00650.8523-0.29670.29010.0671-0.07471.0164-0.29570.582213.2927-17.132142.4834
180.32170.3587-0.10890.87090.38720.59070.0689-0.0109-0.14250.3167-0.0493-0.32490.3218-0.07640.01780.564-0.0624-0.05160.41270.08630.4973-40.1977-39.926526.6871
190.0973-0.01530.07920.0412-0.03470.07750.0085-0.0023-0.0126-0.04340.0310.03050.0546-0.013-0.03970.4520.0301-0.0610.82080.06040.4384-56.3413-30.761514.5775
201.13560.1998-0.64910.80810.35380.65190.13480.31080.07590.18240.07760.02950.0972-0.56-0.1620.3246-0.06130.01630.62080.09610.3183-43.3035-32.272731.5478
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN A AND (RESSEQ 12:791)
2X-RAY DIFFRACTION2CHAIN B AND (RESSEQ 18:80)
3X-RAY DIFFRACTION3CHAIN B AND (RESSEQ 81:141)
4X-RAY DIFFRACTION4CHAIN B AND (RESSEQ 142:186)
5X-RAY DIFFRACTION5CHAIN B AND (RESSEQ 187:337)
6X-RAY DIFFRACTION6CHAIN C AND (RESSEQ 1:22)
7X-RAY DIFFRACTION7CHAIN C AND (RESSEQ 23:31)
8X-RAY DIFFRACTION8CHAIN C AND (RESSEQ 32:64)
9X-RAY DIFFRACTION9CHAIN D AND (RESSEQ 12:791)
10X-RAY DIFFRACTION10CHAIN E AND (RESSEQ 19:63)
11X-RAY DIFFRACTION11CHAIN E AND (RESSEQ 64:80)
12X-RAY DIFFRACTION12CHAIN E AND (RESSEQ 81:109)
13X-RAY DIFFRACTION13CHAIN E AND (RESSEQ 110:204)
14X-RAY DIFFRACTION14CHAIN E AND (RESSEQ 205:229)
15X-RAY DIFFRACTION15CHAIN E AND (RESSEQ 230:246)
16X-RAY DIFFRACTION16CHAIN E AND (RESSEQ 247:296)
17X-RAY DIFFRACTION17CHAIN E AND (RESSEQ 297:337)
18X-RAY DIFFRACTION18CHAIN F AND (RESSEQ 1:22)
19X-RAY DIFFRACTION19CHAIN F AND (RESSEQ 23:31)
20X-RAY DIFFRACTION20CHAIN F AND (RESSEQ 32:63)

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