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- PDB-9ikf: Bovine Heart Cytochrome c Oxidase in the Carbon Dioxide-bound Ful... -

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Basic information

Entry
Database: PDB / ID: 9ikf
TitleBovine Heart Cytochrome c Oxidase in the Carbon Dioxide-bound Fully Oxidized State
Components(Cytochrome c oxidase subunit ...) x 13
KeywordsOXIDOREDUCTASE / carbon dioxide / fully oxidized
Function / homology
Function and homology information


Complex IV assembly / TP53 Regulates Metabolic Genes / Cytoprotection by HMOX1 / respiratory chain complex IV assembly / mitochondrial respirasome assembly / Respiratory electron transport / respiratory chain complex IV / respiratory chain complex / cytochrome-c oxidase / oxidative phosphorylation ...Complex IV assembly / TP53 Regulates Metabolic Genes / Cytoprotection by HMOX1 / respiratory chain complex IV assembly / mitochondrial respirasome assembly / Respiratory electron transport / respiratory chain complex IV / respiratory chain complex / cytochrome-c oxidase / oxidative phosphorylation / mitochondrial electron transport, cytochrome c to oxygen / cytochrome-c oxidase activity / Mitochondrial protein degradation / ATP synthesis coupled electron transport / enzyme regulator activity / aerobic respiration / central nervous system development / respiratory electron transport chain / mitochondrial inner membrane / oxidoreductase activity / copper ion binding / heme binding / mitochondrion / metal ion binding
Similarity search - Function
Cytochrome c oxidase, subunit 8 / Mitochondrial cytochrome c oxidase subunit VIc/VIIs / Cytochrome c oxidase, subunit 8 superfamily / Mitochondrial cytochrome c oxidase subunit VIc/VIIs superfamily / : / Cytochrome oxidase c subunit VIII / Cytochrome c oxidase subunit VIc / Cytochrome c oxidase subunit VIIa, metazoa / Cytochrome C oxidase, subunit VIIB / Cytochrome c oxidase subunit IV ...Cytochrome c oxidase, subunit 8 / Mitochondrial cytochrome c oxidase subunit VIc/VIIs / Cytochrome c oxidase, subunit 8 superfamily / Mitochondrial cytochrome c oxidase subunit VIc/VIIs superfamily / : / Cytochrome oxidase c subunit VIII / Cytochrome c oxidase subunit VIc / Cytochrome c oxidase subunit VIIa, metazoa / Cytochrome C oxidase, subunit VIIB / Cytochrome c oxidase subunit IV / Cytochrome C oxidase, subunit VIIB domain superfamily / Cytochrome c oxidase, subunit VIIa superfamily / Cytochrome C oxidase chain VIIB / Cytochrome c oxidase, subunit VIa, conserved site / Cytochrome c oxidase subunit VIa signature. / Cytochrome c oxidase, subunit VIa / Cytochrome c oxidase, subunit VIa superfamily / Cytochrome c oxidase subunit VIa / Cytochrome c oxidase, subunit VIb / : / Cytochrome c oxidase subunit Vb, zinc binding region signature. / Cytochrome c oxidase subunit VIIc / Cytochrome c oxidase subunit IV family / Cytochrome c oxidase, subunit VIb superfamily / Cytochrome c oxidase subunit VIIc superfamily / Cytochrome c oxidase subunit IV superfamily / Cytochrome c oxidase subunit VIIc / Cytochrome c oxidase subunit IV / Cytochrome c oxidase subunit 2, C-terminal / Cytochrome oxidase c subunit VIb / Cytochrome c oxidase, subunit Va/VI / Cytochrome c oxidase, subunit Va/VI superfamily / Cytochrome c oxidase subunit Va / Cytochrome c oxidase subunit VII / Cytochrome c oxidase subunit VII / Cytochrome c oxidase, subunit Vb / Cytochrome c oxidase subunit III domain / Cytochrome c oxidase subunit Vb / Cytochrome c oxidase subunit Vb, zinc binding domain profile. / Cytochrome c oxidase, subunit II / Cytochrome c oxidase, subunit Vb superfamily / Cytochrome c oxidase subunit I domain / Cytochrome C oxidase subunit II, transmembrane domain / Cytochrome C oxidase subunit II, transmembrane domain / Cytochrome oxidase subunit II transmembrane region profile. / Cytochrome c oxidase subunit III / 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/quinol oxidase subunit II / Cytochrome C oxidase subunit II, transmembrane domain superfamily / Copper centre Cu(A) / CO II and nitrous oxide reductase dinuclear copper centers signature. / 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. / Coiled coil-helix-coiled coil-helix (CHCH) domain profile. / Cupredoxin
Similarity search - Domain/homology
CARDIOLIPIN / CHOLIC ACID / CARBON DIOXIDE / COPPER (II) ION / DINUCLEAR COPPER ION / HEME-A / EICOSANE / Chem-PEK / PEROXIDE ION / Chem-PGV ...CARDIOLIPIN / CHOLIC ACID / CARBON DIOXIDE / COPPER (II) ION / DINUCLEAR COPPER ION / HEME-A / EICOSANE / Chem-PEK / PEROXIDE ION / Chem-PGV / Cytochrome c oxidase subunit 1 / Cytochrome c oxidase subunit 3 / Cytochrome c oxidase subunit 4 isoform 1, mitochondrial / Cytochrome c oxidase subunit 5A, mitochondrial / Cytochrome c oxidase subunit 5B, mitochondrial / Cytochrome c oxidase subunit 6B1 / Cytochrome c oxidase subunit 7C, mitochondrial / Cytochrome c oxidase subunit 6C / Cytochrome c oxidase subunit 7A1, mitochondrial / Cytochrome c oxidase subunit 6A2, mitochondrial / Cytochrome c oxidase subunit 8B, mitochondrial / Cytochrome c oxidase subunit 7B, mitochondrial / Cytochrome c oxidase subunit 2
Similarity search - Component
Biological speciesBos taurus (domestic cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.75 Å
AuthorsMuramoto, K. / Shinzawa-Itoh, K.
Funding support Japan, 1items
OrganizationGrant numberCountry
Japan Society for the Promotion of Science (JSPS)22K06130 Japan
CitationJournal: J.Biol.Chem. / Year: 2025
Title: The binding sites of carbon dioxide, nitrous oxide, and xenon reveal a putative exhaust channel for bovine cytochrome c oxidase.
Authors: Muramoto, K. / Ide, T. / Shinzawa-Itoh, K.
History
DepositionJun 27, 2024Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jul 2, 2025Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Cytochrome c oxidase subunit 1
B: Cytochrome c oxidase subunit 2
C: Cytochrome c oxidase subunit 3
D: Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
E: Cytochrome c oxidase subunit 5A
F: Cytochrome c oxidase subunit 5B, mitochondrial
G: Cytochrome c oxidase subunit 6A2, mitochondrial
H: Cytochrome c oxidase subunit 6B1
I: Cytochrome c oxidase subunit 6C
J: Cytochrome c oxidase subunit 7A1
K: Cytochrome c oxidase subunit 7B, mitochondrial
L: Cytochrome c oxidase subunit 7C, mitochondrial
M: Cytochrome c oxidase subunit 8B, mitochondrial
N: Cytochrome c oxidase subunit 1
O: Cytochrome c oxidase subunit 2
P: Cytochrome c oxidase subunit 3
Q: Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
R: Cytochrome c oxidase subunit 5A
S: Cytochrome c oxidase subunit 5B, mitochondrial
T: Cytochrome c oxidase subunit 6A2, mitochondrial
U: Cytochrome c oxidase subunit 6B1
V: Cytochrome c oxidase subunit 6C
W: Cytochrome c oxidase subunit 7A1
X: Cytochrome c oxidase subunit 7B, mitochondrial
Y: Cytochrome c oxidase subunit 7C, mitochondrial
Z: Cytochrome c oxidase subunit 8B, mitochondrial
hetero molecules


Theoretical massNumber of molelcules
Total (without water)460,859161
Polymers409,97226
Non-polymers50,888135
Water36,1562007
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: native gel electrophoresis
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area191230 Å2
ΔGint-1083 kcal/mol
Surface area103150 Å2
MethodPISA
Unit cell
Length a, b, c (Å)182.500, 204.400, 177.800
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

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Cytochrome c oxidase subunit ... , 13 types, 26 molecules ANBOCPDQERFSGTHUIVJWKXLYMZ

#1: Protein Cytochrome c oxidase subunit 1 / Cytochrome c oxidase polypeptide I


Mass: 57093.852 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P00396, cytochrome-c oxidase
#2: Protein Cytochrome c oxidase subunit 2 / Cytochrome c oxidase polypeptide II


Mass: 26068.404 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P68530, cytochrome-c oxidase
#3: Protein Cytochrome c oxidase subunit 3 / Cytochrome c oxidase polypeptide III


Mass: 29957.627 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P00415, cytochrome-c oxidase
#4: Protein Cytochrome c oxidase subunit 4 isoform 1, mitochondrial / Cytochrome c oxidase polypeptide IV / Cytochrome c oxidase subunit IV isoform 1 / COX IV-1


Mass: 17179.646 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P00423
#5: Protein Cytochrome c oxidase subunit 5A / Cytochrome c oxidase polypeptide Va


Mass: 12453.081 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P00426
#6: Protein Cytochrome c oxidase subunit 5B, mitochondrial / Cytochrome c oxidase polypeptide VIa / Cytochrome c oxidase polypeptide Vb


Mass: 10684.038 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P00428
#7: Protein Cytochrome c oxidase subunit 6A2, mitochondrial / Cytochrome c oxidase polypeptide VIa-heart / COXVIAH / Cytochrome c oxidase polypeptide VIb


Mass: 9549.802 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P07471
#8: Protein Cytochrome c oxidase subunit 6B1 / Cytochrome c oxidase polypeptide VII / Cytochrome c oxidase subunit AED / Cytochrome c oxidase ...Cytochrome c oxidase polypeptide VII / Cytochrome c oxidase subunit AED / Cytochrome c oxidase subunit VIb isoform 1 / COX VIb-1


Mass: 10039.244 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P00429
#9: Protein Cytochrome c oxidase subunit 6C / Cytochrome c oxidase polypeptide VIc / Cytochrome c oxidase subunit STA


Mass: 8494.982 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P04038
#10: Protein Cytochrome c oxidase subunit 7A1 / Cytochrome c oxidase subunit VIIIc / VIIIC


Mass: 6682.726 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P07470
#11: Protein Cytochrome c oxidase subunit 7B, mitochondrial / Cytochrome c oxidase polypeptide VIIb / IHQ


Mass: 6365.217 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P13183
#12: Protein/peptide Cytochrome c oxidase subunit 7C, mitochondrial / Cytochrome c oxidase polypeptide VIIIA


Mass: 5449.396 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P00430
#13: Protein/peptide Cytochrome c oxidase subunit 8B, mitochondrial / Cytochrome c oxidase polypeptide VIII-heart / Cytochrome c oxidase subunit 8-1 / Cytochrome c ...Cytochrome c oxidase polypeptide VIII-heart / Cytochrome c oxidase subunit 8-1 / Cytochrome c oxidase subunit 8H / IX / VIIIb


Mass: 4967.756 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P10175

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Sugars , 1 types, 42 molecules

#22: Sugar...
ChemComp-DMU / DECYL-BETA-D-MALTOPYRANOSIDE / DECYLMALTOSIDE


Type: D-saccharide / Mass: 482.562 Da / Num. of mol.: 42 / Source method: obtained synthetically / Formula: C22H42O11 / Comment: detergent*YM

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Non-polymers , 16 types, 2100 molecules

#14: Chemical
ChemComp-HEA / HEME-A


Mass: 852.837 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C49H56FeN4O6
#15: Chemical ChemComp-CU / COPPER (II) ION


Mass: 63.546 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cu
#16: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#17: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Na
#18: Chemical ChemComp-PER / PEROXIDE ION


Mass: 31.999 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: O2
#19: Chemical
ChemComp-CDL / CARDIOLIPIN / DIPHOSPHATIDYL GLYCEROL / BIS-(1,2-DIACYL-SN-GLYCERO-3-PHOSPHO)-1',3'-SN-GLYCEROL


Mass: 1464.043 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C81H156O17P2 / Comment: phospholipid*YM
#20: Chemical ChemComp-CO2 / CARBON DIOXIDE


Mass: 44.010 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: CO2 / Feature type: SUBJECT OF INVESTIGATION
#21: Chemical...
ChemComp-LFA / EICOSANE / LIPID FRAGMENT


Mass: 282.547 Da / Num. of mol.: 26 / Source method: obtained synthetically / Formula: C20H42
#23: Chemical...
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 29 / Source method: obtained synthetically / Formula: C2H6O2
#24: Chemical
ChemComp-PGV / (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE / PHOSPHATIDYLGLYCEROL / 2-VACCENOYL-1-PALMITOYL-SN-GLYCEROL-3-PHOSPHOGLYCEROL


Mass: 749.007 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C40H77O10P / Comment: phospholipid*YM
#25: Chemical ChemComp-CUA / DINUCLEAR COPPER ION


Mass: 127.092 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cu2
#26: Chemical
ChemComp-CHD / CHOLIC ACID


Mass: 408.571 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C24H40O5
#27: Chemical ChemComp-UNX / UNKNOWN ATOM OR ION


Mass: 768.055 Da / Num. of mol.: 2 / Source method: obtained synthetically
#28: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Formula: Zn
#29: Chemical ChemComp-PEK / (1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(STEAROYLOXY)METHYL]ETHYL (5E,8E,11E,14E)-ICOSA-5,8,11,14-TETRAENOATE / PHOSPHATIDYLETHANOLAMINE / 2-ARACHIDONOYL-1-STEAROYL-SN-GLYCEROL-3-PHOSPHOETHANOLAMINE


Mass: 768.055 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C43H78NO8P / Comment: phospholipid*YM
#30: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 2007 / 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: 4.2 Å3/Da / Density % sol: 70.71 %
Crystal growTemperature: 277 K / Method: batch mode / pH: 6.8
Details: 40 mM sodium phosphate buffer, pH 6.8 0.2% (w/v) decyl-maltoside 1% (w/v) polyethylene glycol 4000

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Data collection

DiffractionMean temperature: 90 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL44XU / Wavelength: 0.9 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Apr 21, 2024
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9 Å / Relative weight: 1
ReflectionResolution: 1.75→200 Å / Num. obs: 1295927 / % possible obs: 100 % / Redundancy: 21.2 % / Biso Wilson estimate: 30.5 Å2 / CC1/2: 0.999 / Rrim(I) all: 0.108 / Net I/σ(I): 18.5
Reflection shellResolution: 1.75→1.8 Å / Redundancy: 21.1 % / Mean I/σ(I) obs: 1.32 / Num. unique obs: 96102 / CC1/2: 0.767 / Rrim(I) all: 2.7 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.8.0253refinement
XDSdata reduction
XSCALEdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 8H8R
Resolution: 1.75→40 Å / Cor.coef. Fo:Fc: 0.974 / Cor.coef. Fo:Fc free: 0.966 / SU B: 4.311 / SU ML: 0.055 / Cross valid method: THROUGHOUT / ESU R: 0.073 / ESU R Free: 0.068 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.16674 33113 5 %RANDOM
Rwork0.12986 ---
obs0.13171 628313 99.98 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 42.078 Å2
Baniso -1Baniso -2Baniso -3
1--1.22 Å20 Å20 Å2
2--4.63 Å2-0 Å2
3----3.4 Å2
Refinement stepCycle: 1 / Resolution: 1.75→40 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms27834 0 2596 2007 32437
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0150.01631957
X-RAY DIFFRACTIONr_bond_other_d0.0010.01730503
X-RAY DIFFRACTIONr_angle_refined_deg1.8671.66843080
X-RAY DIFFRACTIONr_angle_other_deg1.4481.58470976
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.06653573
X-RAY DIFFRACTIONr_dihedral_angle_2_deg32.721.71359
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.834154675
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.38615124
X-RAY DIFFRACTIONr_chiral_restr0.450.24065
X-RAY DIFFRACTIONr_gen_planes_refined0.010.0233225
X-RAY DIFFRACTIONr_gen_planes_other0.0050.026797
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it3.963.28814192
X-RAY DIFFRACTIONr_mcbond_other3.9583.28814191
X-RAY DIFFRACTIONr_mcangle_it4.4314.92817798
X-RAY DIFFRACTIONr_mcangle_other4.4324.92817799
X-RAY DIFFRACTIONr_scbond_it6.0373.85117765
X-RAY DIFFRACTIONr_scbond_other6.0373.85117766
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other6.8155.59825283
X-RAY DIFFRACTIONr_long_range_B_refined6.14940.82736440
X-RAY DIFFRACTIONr_long_range_B_other6.08940.45136022
X-RAY DIFFRACTIONr_rigid_bond_restr3.693362460
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.75→1.795 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.29 2494 -
Rwork0.279 46149 -
obs--99.99 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
10.2439-0.02860.0430.1636-0.0310.34720.0129-0.0296-0.0217-0.00120.00160.0128-0.0024-0.0254-0.01450.0289-0.01520.00280.01210.00420.025-29.549-0.561-20.62
20.2767-0.0502-0.00380.21560.00430.3820.017-0.0550.0398-0.00240.009-0.05980.02160.0532-0.02610.0245-0.00510.0040.0193-0.0150.079935.21-5.194-16.833
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 513
2X-RAY DIFFRACTION1A601 - 616
3X-RAY DIFFRACTION1C301
4X-RAY DIFFRACTION1D201
5X-RAY DIFFRACTION1L101
6X-RAY DIFFRACTION1M101
7X-RAY DIFFRACTION1A1801 - 2035
8X-RAY DIFFRACTION1B454 - 514
9X-RAY DIFFRACTION1C468
10X-RAY DIFFRACTION1D358 - 420
11X-RAY DIFFRACTION1F239
12X-RAY DIFFRACTION1H204 - 258
13X-RAY DIFFRACTION1L220
14X-RAY DIFFRACTION1B1 - 227
15X-RAY DIFFRACTION1B301 - 305
16X-RAY DIFFRACTION1C4 - 261
17X-RAY DIFFRACTION1A617
18X-RAY DIFFRACTION1C302 - 322
19X-RAY DIFFRACTION1G101
20X-RAY DIFFRACTION1H101
21X-RAY DIFFRACTION1P301
22X-RAY DIFFRACTION1F269
23X-RAY DIFFRACTION1D4 - 146
24X-RAY DIFFRACTION1I114
25X-RAY DIFFRACTION1E7 - 108
26X-RAY DIFFRACTION1E201 - 203
27X-RAY DIFFRACTION1E301 - 391
28X-RAY DIFFRACTION1F3 - 93
29X-RAY DIFFRACTION1F101 - 103
30X-RAY DIFFRACTION1G12 - 83
31X-RAY DIFFRACTION1C323
32X-RAY DIFFRACTION1G102 - 103
33X-RAY DIFFRACTION1O301 - 304
34X-RAY DIFFRACTION1G201 - 241
35X-RAY DIFFRACTION1H11 - 85
36X-RAY DIFFRACTION1I3 - 72
37X-RAY DIFFRACTION1J1 - 56
38X-RAY DIFFRACTION1C324
39X-RAY DIFFRACTION1J101
40X-RAY DIFFRACTION1J201 - 214
41X-RAY DIFFRACTION1K6 - 54
42X-RAY DIFFRACTION1K103 - 120
43X-RAY DIFFRACTION1L3 - 46
44X-RAY DIFFRACTION1L102
45X-RAY DIFFRACTION1L203 - 219
46X-RAY DIFFRACTION1M1 - 40
47X-RAY DIFFRACTION1M102
48X-RAY DIFFRACTION1M204 - 219
49X-RAY DIFFRACTION2N1 - 513
50X-RAY DIFFRACTION2N601 - 616
51X-RAY DIFFRACTION2P302
52X-RAY DIFFRACTION2Q201
53X-RAY DIFFRACTION2V101
54X-RAY DIFFRACTION2Y101
55X-RAY DIFFRACTION2Z101
56X-RAY DIFFRACTION2N2801 - 3023
57X-RAY DIFFRACTION2O454 - 508
58X-RAY DIFFRACTION2S229 - 281
59X-RAY DIFFRACTION2Y221
60X-RAY DIFFRACTION2O1 - 227
61X-RAY DIFFRACTION2O305 - 309
62X-RAY DIFFRACTION2U219
63X-RAY DIFFRACTION2P4 - 261
64X-RAY DIFFRACTION2C325
65X-RAY DIFFRACTION2N617
66X-RAY DIFFRACTION2P303 - 323
67X-RAY DIFFRACTION2T101
68X-RAY DIFFRACTION2U101
69X-RAY DIFFRACTION2P401 - 498
70X-RAY DIFFRACTION2Q10 - 146
71X-RAY DIFFRACTION2Q308 - 368
72X-RAY DIFFRACTION2R7 - 108
73X-RAY DIFFRACTION2R201 - 203
74X-RAY DIFFRACTION2R301 - 384
75X-RAY DIFFRACTION2S3 - 93
76X-RAY DIFFRACTION2S101 - 103
77X-RAY DIFFRACTION2Q374
78X-RAY DIFFRACTION2T12 - 83
79X-RAY DIFFRACTION2A618
80X-RAY DIFFRACTION2B306 - 308
81X-RAY DIFFRACTION2P324
82X-RAY DIFFRACTION2T102 - 103
83X-RAY DIFFRACTION2T202 - 235
84X-RAY DIFFRACTION2U11 - 85
85X-RAY DIFFRACTION2V3 - 72
86X-RAY DIFFRACTION2V205 - 219
87X-RAY DIFFRACTION2W1 - 56
88X-RAY DIFFRACTION2P325
89X-RAY DIFFRACTION2W101
90X-RAY DIFFRACTION2W201 - 213
91X-RAY DIFFRACTION2X6 - 54
92X-RAY DIFFRACTION2X102 - 118
93X-RAY DIFFRACTION2Y3 - 46
94X-RAY DIFFRACTION2Z102
95X-RAY DIFFRACTION2Y204 - 220
96X-RAY DIFFRACTION2Z1 - 40
97X-RAY DIFFRACTION2Z103
98X-RAY DIFFRACTION2Z203 - 216

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