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- PDB-4ret: Crystal structure of the Na,K-ATPase E2P-digoxin complex with bou... -

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Basic information

Entry
Database: PDB / ID: 4ret
TitleCrystal structure of the Na,K-ATPase E2P-digoxin complex with bound magnesium
Components
  • (Sodium/potassium-transporting ATPase subunit ...) x 2
  • Na+/K+ ATPase gamma subunit transcript variant a
KeywordsMEMBRANE PROTEIN / HYDROLASE/INHIBITOR / alpha-helical transmembrane protein / ATPase / sodium ion transport / potassium ion transport / ATP binding / sodium binding / potassium binding / receptor for cardiotonic steroids / phosphorylation / glycosylation / plasma membrane / multisubunit complex / trimeric complex / HYDROLASE-INHIBITOR complex
Function / homology
Function and homology information


Ion homeostasis / positive regulation of P-type sodium:potassium-exchanging transporter activity / Na+/K+-exchanging ATPase / positive regulation of sodium ion export across plasma membrane / positive regulation of potassium ion import across plasma membrane / Ion transport by P-type ATPases / P-type sodium:potassium-exchanging transporter activity / membrane repolarization / sodium ion binding / sodium:potassium-exchanging ATPase complex ...Ion homeostasis / positive regulation of P-type sodium:potassium-exchanging transporter activity / Na+/K+-exchanging ATPase / positive regulation of sodium ion export across plasma membrane / positive regulation of potassium ion import across plasma membrane / Ion transport by P-type ATPases / P-type sodium:potassium-exchanging transporter activity / membrane repolarization / sodium ion binding / sodium:potassium-exchanging ATPase complex / sodium ion export across plasma membrane / regulation of calcium ion transmembrane transport / intracellular potassium ion homeostasis / establishment or maintenance of transmembrane electrochemical gradient / intracellular sodium ion homeostasis / regulation of cardiac muscle contraction by calcium ion signaling / ion channel regulator activity / relaxation of cardiac muscle / potassium ion import across plasma membrane / ATPase activator activity / potassium ion binding / organelle membrane / intercalated disc / lateral plasma membrane / sperm flagellum / ATP metabolic process / regulation of sodium ion transport / cardiac muscle contraction / T-tubule / proton transmembrane transport / protein localization to plasma membrane / sarcolemma / transmembrane transport / intracellular calcium ion homeostasis / melanosome / protein-macromolecule adaptor activity / ATPase binding / regulation of gene expression / basolateral plasma membrane / protein stabilization / cell adhesion / apical plasma membrane / axon / innate immune response / protein kinase binding / ATP hydrolysis activity / ATP binding / membrane / plasma membrane
Similarity search - Function
Na, k-atpase alpha subunit. / : / : / Ion-transport regulator, FXYD motif / ATP1G1/PLM/MAT8 family / FXYD family signature. / Calcium-transporting ATPase, transmembrane domain / Calcium-transporting ATPase, transmembrane domain / Calcium-transporting ATPase, cytoplasmic transduction domain A / Calcium-transporting ATPase, cytoplasmic transduction domain A ...Na, k-atpase alpha subunit. / : / : / Ion-transport regulator, FXYD motif / ATP1G1/PLM/MAT8 family / FXYD family signature. / Calcium-transporting ATPase, transmembrane domain / Calcium-transporting ATPase, transmembrane domain / Calcium-transporting ATPase, cytoplasmic transduction domain A / Calcium-transporting ATPase, cytoplasmic transduction domain A / Sodium/potassium-transporting ATPase subunit beta / Sodium/potassium-transporting ATPase subunit beta superfamily / Sodium / potassium ATPase beta chain / Sodium and potassium ATPases beta subunits signature 1. / Sodium and potassium ATPases beta subunits signature 2. / Calcium-transporting ATPase, cytoplasmic domain N / Calcium-transporting ATPase, cytoplasmic domain N / P-type ATPase subfamily IIC, subunit alpha / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #170 / Cation-transporting P-type ATPase, C-terminal / Cation transporting ATPase, C-terminus / Cation transporter/ATPase, N-terminus / Cation-transporting P-type ATPase, N-terminal / Cation transporter/ATPase, N-terminus / Cation transport ATPase (P-type) / E1-E2 ATPase / P-type ATPase, haloacid dehalogenase domain / P-type ATPase, phosphorylation site / P-type ATPase, cytoplasmic domain N / E1-E2 ATPases phosphorylation site. / P-type ATPase, A domain superfamily / P-type ATPase / P-type ATPase, transmembrane domain superfamily / haloacid dehalogenase-like hydrolase / HAD superfamily/HAD-like / HAD superfamily / HAD-like superfamily / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Distorted Sandwich / Up-down Bundle / Immunoglobulin-like / Sandwich / Rossmann fold / 3-Layer(aba) Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
sucrose / Chem-17F / CHOLESTEROL / DIGOXIN / Sodium/potassium-transporting ATPase subunit alpha-1 / Sodium/potassium-transporting ATPase subunit beta-1 / FXYD domain-containing ion transport regulator
Similarity search - Component
Biological speciesSus scrofa (pig)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4 Å
AuthorsGregersen, J.L. / Laursen, M. / Yatime, L. / Nissen, P. / Fedosova, N.U.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2015
Title: Structures and characterization of digoxin- and bufalin-bound Na+,K+-ATPase compared with the ouabain-bound complex.
Authors: Laursen, M. / Gregersen, J.L. / Yatime, L. / Nissen, P. / Fedosova, N.U.
History
DepositionSep 23, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 28, 2015Provider: repository / Type: Initial release
Revision 1.1Feb 11, 2015Group: Database references
Revision 1.2Feb 25, 2015Group: Database references
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Non-polymer description / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / entity / entity_name_com / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_molecule_features / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_struct_conn_angle / pdbx_unobs_or_zero_occ_atoms / pdbx_validate_close_contact / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _atom_site_anisotrop.id / _atom_site_anisotrop.pdbx_auth_asym_id / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_auth_comp_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_asym_id / _atom_site_anisotrop.pdbx_label_atom_id / _atom_site_anisotrop.pdbx_label_comp_id / _atom_site_anisotrop.type_symbol / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _pdbx_struct_assembly_gen.asym_id_list / _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.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_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 / _pdbx_unobs_or_zero_occ_atoms.label_asym_id / _pdbx_validate_close_contact.auth_asym_id_1 / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_seq_id_1 / _pdbx_validate_close_contact.auth_seq_id_2
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Sep 20, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Sodium/potassium-transporting ATPase subunit alpha-1
B: Sodium/potassium-transporting ATPase subunit beta-1
G: Na+/K+ ATPase gamma subunit transcript variant a
C: Sodium/potassium-transporting ATPase subunit alpha-1
D: Sodium/potassium-transporting ATPase subunit beta-1
E: Na+/K+ ATPase gamma subunit transcript variant a
hetero molecules


Theoretical massNumber of molelcules
Total (without water)317,96428
Polymers310,3526
Non-polymers7,61222
Water1086
1
A: Sodium/potassium-transporting ATPase subunit alpha-1
B: Sodium/potassium-transporting ATPase subunit beta-1
G: Na+/K+ ATPase gamma subunit transcript variant a
hetero molecules


Theoretical massNumber of molelcules
Total (without water)160,49816
Polymers155,1763
Non-polymers5,32113
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8870 Å2
ΔGint-51 kcal/mol
Surface area58970 Å2
MethodPISA
2
C: Sodium/potassium-transporting ATPase subunit alpha-1
D: Sodium/potassium-transporting ATPase subunit beta-1
E: Na+/K+ ATPase gamma subunit transcript variant a
hetero molecules


Theoretical massNumber of molelcules
Total (without water)157,46712
Polymers155,1763
Non-polymers2,2919
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10240 Å2
ΔGint-51 kcal/mol
Surface area59360 Å2
MethodPISA
Unit cell
Length a, b, c (Å)118.240, 118.350, 494.090
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
12
22
13
23
14
24
15
25

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111chain A and (resseq 21:80 or resseq 155:275)
211chain C and (resseq 21:80 or resseq 155:275)
112chain A and (resseq 349:376 or resseq 589:746 or resid 1101:1102)
212chain C and (resseq 349:376 or resseq 589:746 or resid 2001:2002)
113chain A and resseq 377:588
213chain C and resseq 377:588
114chain A and (resseq 81:154 or resseq 276:348 or resseq...
214chain C and (resseq 81:154 or resseq 276:348 or resseq...
115chain B and resseq 63:303
215chain D and resseq 63:303

NCS ensembles :
ID
1
2
3
4
5

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Components

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Sodium/potassium-transporting ATPase subunit ... , 2 types, 4 molecules ACBD

#1: Protein Sodium/potassium-transporting ATPase subunit alpha-1 / Na(+)/K(+) ATPase alpha-1 subunit / Sodium pump subunit alpha-1


Mass: 112877.562 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / References: UniProt: P05024, EC: 3.6.3.9
#2: Protein Sodium/potassium-transporting ATPase subunit beta-1 / Na(+) / K)(+)-ATPase beta-1 subunit / Sodium/potassium-dependent ATPase subunit beta-1


Mass: 35204.402 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / References: UniProt: P05027

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Protein , 1 types, 2 molecules GE

#3: Protein Na+/K+ ATPase gamma subunit transcript variant a / Na(+) / K)(+)-ATPase gamma subunit


Mass: 7094.115 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / References: UniProt: Q58K79

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Sugars , 3 types, 7 molecules

#4: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE
#5: Polysaccharide beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose / sucrose /


Type: oligosaccharide, Oligosaccharide / Class: Nutrient / Mass: 342.297 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: oligosaccharide with reducing-end-to-reducing-end glycosidic bond
References: sucrose
DescriptorTypeProgram
DFrufb2-1DGlcpaGlycam Condensed SequenceGMML 1.0
WURCS=2.0/2,2,1/[ha122h-2b_2-5][a2122h-1a_1-5]/1-2/a2-b1WURCSPDB2Glycan 1.1.0
[][b-D-Fruf]{[(2+1)][a-D-Glcp]{}}LINUCSPDB-CARE
#10: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE / N-Acetylglucosamine


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 5 types, 21 molecules

#6: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mg
#7: Chemical
ChemComp-CLR / CHOLESTEROL / Cholesterol


Mass: 386.654 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C27H46O
#8: Chemical ChemComp-DGX / DIGOXIN / Digoxin


Mass: 780.938 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C41H64O14 / Comment: medication*YM
#9: Chemical ChemComp-17F / O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L-serine / 1,2-Dioleoyl-sn-glycero-3-phospho-L-serine


Mass: 788.043 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C42H78NO10P / Comment: phospholipid*YM
#11: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 6 / 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: 5.57 Å3/Da / Density % sol: 77.92 %
Description: Rmeas = 0.082 (0.98 for highest resolution shell), CC-1/2 = 99.8 (62.0 for highest resolution shell)
Crystal growTemperature: 292 K / Method: vapor diffusion, hanging drop / pH: 6.2
Details: 16% PEG2000 MME, 10% glycerol, 200 mM magnesium chloride, 100 mM MES-NMDG, pH 6.2, 25 mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 292K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1 Å
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: Oct 12, 2013
RadiationMonochromator: double crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.89→50 Å / Num. all: 64928 / Num. obs: 44534 / % possible obs: 68.6 % / Observed criterion σ(F): 1.76 / Observed criterion σ(I): 1.76 / Redundancy: 5.6 % / Biso Wilson estimate: 149.72 Å2 / Net I/σ(I): 11.08
Reflection shellResolution: 3.89→3.99 Å / Redundancy: 4.8 % / Mean I/σ(I) obs: 1.76 / % possible all: 3.8

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Processing

Software
NameVersionClassification
XDSdata scaling
PHASERphasing
PHENIX(phenix.refine: dev_1593)refinement
XDSdata reduction
Diffractionanisotropy serverdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 4HYT

4hyt


Resolution: 4→49.409 Å / SU ML: 0.57 / σ(F): 2 / Phase error: 29.64 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2531 2144 4.98 %
Rwork0.2213 --
obs0.2229 43077 72.21 %
all-43077 -
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 4→49.409 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms20704 0 413 6 21123
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00921616
X-RAY DIFFRACTIONf_angle_d1.12829319
X-RAY DIFFRACTIONf_dihedral_angle_d15.3357950
X-RAY DIFFRACTIONf_chiral_restr0.0393358
X-RAY DIFFRACTIONf_plane_restr0.0043708
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A1368X-RAY DIFFRACTIONPOSITIONAL
12C1368X-RAY DIFFRACTIONPOSITIONAL0.024
21A1353X-RAY DIFFRACTIONPOSITIONAL
22C1353X-RAY DIFFRACTIONPOSITIONAL0.077
31A1668X-RAY DIFFRACTIONPOSITIONAL
32C1668X-RAY DIFFRACTIONPOSITIONAL0.007
41A3978X-RAY DIFFRACTIONPOSITIONAL
42C3978X-RAY DIFFRACTIONPOSITIONAL0.024
51B1977X-RAY DIFFRACTIONPOSITIONAL
52D1977X-RAY DIFFRACTIONPOSITIONAL0.009
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
4.0003-4.09330.3431190.3009404X-RAY DIFFRACTION11
4.0933-4.19560.3751360.2867703X-RAY DIFFRACTION19
4.1956-4.3090.3545490.27561197X-RAY DIFFRACTION32
4.309-4.43570.2982820.25841665X-RAY DIFFRACTION45
4.4357-4.57880.30341130.25382101X-RAY DIFFRACTION56
4.5788-4.74230.26931380.23712502X-RAY DIFFRACTION67
4.7423-4.9320.26061500.24242884X-RAY DIFFRACTION77
4.932-5.15630.27051840.24363269X-RAY DIFFRACTION88
5.1563-5.42780.30051710.2433645X-RAY DIFFRACTION96
5.4278-5.76740.28321850.25113632X-RAY DIFFRACTION96
5.7674-6.21190.3022150.24443665X-RAY DIFFRACTION97
6.2119-6.83560.26631950.21833681X-RAY DIFFRACTION98
6.8356-7.82130.23521890.19833778X-RAY DIFFRACTION98
7.8213-9.84120.20042010.16683860X-RAY DIFFRACTION99
9.8412-49.41270.23272170.22613947X-RAY DIFFRACTION98
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)
12.29870.4214-1.32881.1612-0.40211.9468-0.2408-0.19890.48260.18010.04390.0614-0.26230.44760.00011.42180.02960.11652.3536-0.0141.494.4966-18.26789.0615
21.23411.04320.78421.791-0.48062.28750.40850.48940.3607-0.5529-0.03910.3888-0.3487-0.12090.00071.08120.27410.11661.7945-0.01811.8615-21.9159-26.840214.0794
32.9989-0.2926-1.90275.03982.17662.0260.13221.9872-1.1826-1.84350.3942-1.49810.0513-0.05070.00152.13810.11770.66423.2829-0.55292.5335-4.7846-50.0498-8.854
41.82670.0965-1.08472.11590.53993.42070.04480.11470.15050.6091-0.08560.1875-0.08460.33850.00021.33220.0730.34611.4199-0.07371.4495-31.741-31.637958.6963
53.3571.43670.96292.7571-0.7480.89740.1805-1.73440.13331.0588-0.4755-0.13980.3218-0.5774-0.00022.4277-0.29050.42962.8152-0.451.6026-31.7373-28.3524106.4592
60.9147-0.89370.43892.03020.08961.9034-0.45930.1664-0.06120.2688-0.1940.20910.6924-0.249-0.00042.6432-0.01160.3431.81650.05442.2058-45.6106-106.0568114.6397
72.37410.23020.93062.9497-1.33851.0673-0.0422-0.23660.28640.6347-0.00440.5220.0935-0.1952-0.00012.4876-0.27860.24631.5546-0.04031.6045-54.1264-79.8605107.913
81.5524-0.36481.84880.1898-0.35291.9698-0.525-1.38690.74490.283-0.2799-0.93650.2033-1.3408-03.77710.2648-0.46323.3764-0.13562.7792-27.2761-78.8657133.4225
90.88990.61860.93813.1938-0.52543.8087-0.0006-0.0835-0.22390.308-0.04450.29230.9081-0.2948-01.8520.01970.26351.3636-0.06461.5378-52.8988-71.271762.8357
101.71570.64030.12763.6458-0.00643.66540.22830.3992-0.3342-0.1563-0.06470.22521.4952-0.3348-0.00012.2866-0.1382-0.29652.0212-0.10982.0278-52.5002-74.572915.064
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain A and (resseq 21:80 or resseq 155:275)
2X-RAY DIFFRACTION2chain A and (resseq 349:376 or resseq 589:746 or resid 1101:1102)
3X-RAY DIFFRACTION3chain A and resseq 377:588
4X-RAY DIFFRACTION4chain A and (resseq 81:154 or resseq 276:348 or resseq 747:1016 or resseq 1103 or resseq 1201:1203) or chain B and resseq 14:62 or chain G and resseq 17:48
5X-RAY DIFFRACTION5chain B and (resseq 63:303 or resseq 1001:1004)
6X-RAY DIFFRACTION6chain C and (resseq 21:80 or resseq 155:275)
7X-RAY DIFFRACTION7chain C and (resseq 349:376 or resseq 589:746 or resid 2001:2002)
8X-RAY DIFFRACTION8chain C and resseq 377:588
9X-RAY DIFFRACTION9chain C and (resseq 81:154 or resseq 276:348 or resseq 747:1016 or resseq 2003 or resseq 2101:2103) or chain D and resseq 16:62 or chain E and resseq 17:41
10X-RAY DIFFRACTION10chain D and (resseq 63:303 or resseq 2001:2003)

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