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

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Basic information

Entry
Database: PDB / ID: 4res
TitleCrystal structure of the Na,K-ATPase E2P-bufalin complex with bound potassium
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 / bufalin / CHOLESTEROL / : / 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: 3.408 Å
AuthorsLaursen, M. / Yatime, L. / Gregersen, J.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
SupersessionJan 28, 2015ID: 3N2F
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 / 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.pdbx_formal_charge / _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.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_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_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
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)314,30023
Polymers310,3526
Non-polymers3,94817
Water0
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)157,10011
Polymers155,1763
Non-polymers1,9248
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8290 Å2
ΔGint-31 kcal/mol
Surface area57020 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)157,20012
Polymers155,1763
Non-polymers2,0249
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8340 Å2
ΔGint-29 kcal/mol
Surface area56740 Å2
MethodPISA
Unit cell
Length a, b, c (Å)65.910, 240.270, 152.700
Angle α, β, γ (deg.)90.00, 102.28, 90.00
Int Tables number4
Space group name H-MP1211
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 resseq 3003:3004)
212chain C and (resseq 349:376 or resseq 589:746 or resseq 3003:3004)
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 63:90 or resseq 92:303)
215chain D and (resseq 63:90 or resseq 92:303)

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, 4 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.: 1
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, 13 molecules

#6: Chemical ChemComp-BUF / bufalin / Bufalin


Mass: 386.524 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C24H34O4 / Comment: toxin*YM
#7: Chemical ChemComp-CLR / CHOLESTEROL / Cholesterol


Mass: 386.654 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C27H46O
#8: Chemical
ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: K
#9: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#11: 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.: 1 / Source method: obtained synthetically / Formula: C42H78NO10P / Comment: phospholipid*YM

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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: 3.81 Å3/Da / Density % sol: 67.69 %
Description: Rmeas = 0.133 (0.866 for highest resolution shell), CC-1/2 = 99.9 (75.0 for highest resolution shell)
Crystal growTemperature: 292 K / Method: vapor diffusion, hanging drop / pH: 6.2
Details: 17% PEG2000 MME, 10% glycerol, 220 mM magnesium chloride, 100 mM potassium chloride, 100 mM MES-KOH, pH 6.2, 5% MPD, 6% Jeffamine M-600, 0.02% beta-DDM, 2 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, 2009
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: 3.408→55 Å / Num. all: 63228 / Num. obs: 31754 / % possible obs: 50.2 % / Observed criterion σ(F): 2.24 / Observed criterion σ(I): 2.24 / Redundancy: 5.9 % / Biso Wilson estimate: 80.97 Å2 / Net I/σ(I): 10.4
Reflection shellResolution: 3.408→3.5 Å / Redundancy: 5.7 % / Mean I/σ(I) obs: 2.24 / % possible all: 1.4

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Processing

Software
NameVersionClassification
XDSdata scaling
PHASERphasing
PHENIX(phenix.refine: 1.8.2_1309)refinement
XDSdata reduction
Diffractionanisotropy serverdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 4HYT

4hyt


Resolution: 3.408→49.903 Å / SU ML: 0.57 / σ(F): 2 / Phase error: 34.36 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2882 1623 5.14 %RANDOM
Rwork0.2447 ---
obs0.247 31546 49.94 %-
all-31546 --
Solvent computationShrinkage radii: 0.8 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 3.408→49.903 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms20654 0 227 0 20881
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01121367
X-RAY DIFFRACTIONf_angle_d1.22528967
X-RAY DIFFRACTIONf_dihedral_angle_d15.0717903
X-RAY DIFFRACTIONf_chiral_restr0.0763287
X-RAY DIFFRACTIONf_plane_restr0.0053690
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A1368X-RAY DIFFRACTIONPOSITIONAL
12C1368X-RAY DIFFRACTIONPOSITIONAL0.016
21A1353X-RAY DIFFRACTIONPOSITIONAL
22C1353X-RAY DIFFRACTIONPOSITIONAL0.018
31A1668X-RAY DIFFRACTIONPOSITIONAL
32C1668X-RAY DIFFRACTIONPOSITIONAL0.026
41A4006X-RAY DIFFRACTIONPOSITIONAL
42C4006X-RAY DIFFRACTIONPOSITIONAL0.042
51B1966X-RAY DIFFRACTIONPOSITIONAL
52D1966X-RAY DIFFRACTIONPOSITIONAL0.022
LS refinement shell

Refine-ID: X-RAY DIFFRACTION

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection obs% reflection obs (%)
3.408-3.50820.322740.418483832
3.5082-3.62140.6606160.39282742746
3.6214-3.75080.3951220.38350950910
3.7508-3.90090.3017380.330882082016
3.9009-4.07840.3128560.3111261126125
4.0784-4.29330.34751180.26181957195740
4.2933-4.56210.32611440.23852669266954
4.5621-4.91410.29751870.22053364336467
4.9141-5.40810.29092300.2234162416283
5.4081-6.18940.30042670.26224870487098
6.1894-7.79320.27522770.27434933493399
7.7932-49.90860.25552640.22235021502199
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)
12.37180.22341.82842.17221.12481.5586-0.29520.1352-0.4920.45280.303-0.51481.44490.7572-0.02221.4520.4319-0.26611.47810.27141.109133.262212.523960.1103
21.16290.4253-1.28541.8010.07531.07210.05170.67141.0256-0.6230.2311-0.2706-0.84790.0426-0.00251.71130.0530.28081.48890.26481.215133.020296.382-57.2309
32.1129-0.07941.96052.2869-1.1752.8763-0.2932-0.95330.22250.88970.44710.3777-0.5377-0.92720.00070.83660.0375-0.06080.9994-0.01190.998813.332330.868852.1107
42.28561.162-1.82251.2356-0.57631.5634-0.57350.5986-0.3536-0.72470.56930.04350.0134-0.6758-0.00020.96290.01360.0591.15510.15110.904212.999978.1135-49.1655
51.5825-0.8372-0.58614.0081-0.2041.12290.40670.14530.3138-0.0899-0.4077-0.2341-0.94451.0051-0.00031.46290.1202-0.14951.67610.02020.894937.701543.350675.7429
61.8551.11640.06472.72521.04141.51650.19920.3309-0.40710.20220.0561-0.35330.23570.4301-0.00041.83490.01320.11851.8022-0.02651.125537.267865.6037-72.8522
70.68640.49570.43522.77710.67263.24640.1358-0.2202-0.1442-0.05220.0603-0.00250.3181-0.08550.00560.25480.1592-0.0910.5298-0.00790.69317.757633.19076.3696
80.1665-0.2247-0.3682.08230.74183.56520.11160.07360.05740.0694-0.0304-0.0066-0.6053-0.1972-0.00830.2523-0.05890.1040.5980.00610.80667.830275.7817-3.3882
92.3472-0.47060.09522.88831.44924.272-0.06960.28020.0814-0.6605-0.08510.04850.5667-0.02530.00131.3106-0.2063-0.27880.6944-0.07640.81116.117323.538-39.6726
103.25960.4231-0.79052.9714-1.03983.2218-0.1536-0.5231-0.00210.56940.0011-0.2626-0.420.29260.00031.28230.06360.13680.8476-0.11060.79136.530985.516542.8461
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND ( RESID 21:80 OR RESID 155:275 ) )A21 - 80
2X-RAY DIFFRACTION1( CHAIN A AND ( RESID 21:80 OR RESID 155:275 ) )A155 - 275
3X-RAY DIFFRACTION2( CHAIN C AND ( RESID 21:80 OR RESID 155:275 ) )C21 - 80
4X-RAY DIFFRACTION2( CHAIN C AND ( RESID 21:80 OR RESID 155:275 ) )C155 - 275
5X-RAY DIFFRACTION3( CHAIN A AND ( RESID 349:376 OR RESID 589:746 OR RESID 2005:2006 ) )A349 - 376
6X-RAY DIFFRACTION3( CHAIN A AND ( RESID 349:376 OR RESID 589:746 OR RESID 2005:2006 ) )A589 - 746
7X-RAY DIFFRACTION3( CHAIN A AND ( RESID 349:376 OR RESID 589:746 OR RESID 2005:2006 ) )A2005 - 2006
8X-RAY DIFFRACTION4( CHAIN C AND ( RESID 349:376 OR RESID 589:746 OR RESID 1106:1107 ) )C349 - 376
9X-RAY DIFFRACTION4( CHAIN C AND ( RESID 349:376 OR RESID 589:746 OR RESID 1106:1107 ) )C589 - 746
10X-RAY DIFFRACTION4( CHAIN C AND ( RESID 349:376 OR RESID 589:746 OR RESID 1106:1107 ) )C1106 - 1107
11X-RAY DIFFRACTION5( CHAIN A AND RESID 377:588 )A377 - 588
12X-RAY DIFFRACTION6( CHAIN C AND RESID 377:588 )C377 - 588
13X-RAY DIFFRACTION7( CHAIN A AND ( RESID 81:154 OR RESID 276:348 OR RESID 747:1016 OR RESID 2001:2002 OR RESID 2003:2004 ) ) OR ( CHAIN C AND RESID 1101:1101 ) OR ( CHAIN B AND RESID 16:62 ) OR ( CHAIN G AND ( RESID 17:48 OR RESID 1001:1001 ) )A81 - 154
14X-RAY DIFFRACTION7( CHAIN A AND ( RESID 81:154 OR RESID 276:348 OR RESID 747:1016 OR RESID 2001:2002 OR RESID 2003:2004 ) ) OR ( CHAIN C AND RESID 1101:1101 ) OR ( CHAIN B AND RESID 16:62 ) OR ( CHAIN G AND ( RESID 17:48 OR RESID 1001:1001 ) )A276 - 348
15X-RAY DIFFRACTION7( CHAIN A AND ( RESID 81:154 OR RESID 276:348 OR RESID 747:1016 OR RESID 2001:2002 OR RESID 2003:2004 ) ) OR ( CHAIN C AND RESID 1101:1101 ) OR ( CHAIN B AND RESID 16:62 ) OR ( CHAIN G AND ( RESID 17:48 OR RESID 1001:1001 ) )A747 - 1016
16X-RAY DIFFRACTION7( CHAIN A AND ( RESID 81:154 OR RESID 276:348 OR RESID 747:1016 OR RESID 2001:2002 OR RESID 2003:2004 ) ) OR ( CHAIN C AND RESID 1101:1101 ) OR ( CHAIN B AND RESID 16:62 ) OR ( CHAIN G AND ( RESID 17:48 OR RESID 1001:1001 ) )A2001 - 2002
17X-RAY DIFFRACTION7( CHAIN A AND ( RESID 81:154 OR RESID 276:348 OR RESID 747:1016 OR RESID 2001:2002 OR RESID 2003:2004 ) ) OR ( CHAIN C AND RESID 1101:1101 ) OR ( CHAIN B AND RESID 16:62 ) OR ( CHAIN G AND ( RESID 17:48 OR RESID 1001:1001 ) )A2003 - 2004
18X-RAY DIFFRACTION7( CHAIN A AND ( RESID 81:154 OR RESID 276:348 OR RESID 747:1016 OR RESID 2001:2002 OR RESID 2003:2004 ) ) OR ( CHAIN C AND RESID 1101:1101 ) OR ( CHAIN B AND RESID 16:62 ) OR ( CHAIN G AND ( RESID 17:48 OR RESID 1001:1001 ) )C1101
19X-RAY DIFFRACTION7( CHAIN A AND ( RESID 81:154 OR RESID 276:348 OR RESID 747:1016 OR RESID 2001:2002 OR RESID 2003:2004 ) ) OR ( CHAIN C AND RESID 1101:1101 ) OR ( CHAIN B AND RESID 16:62 ) OR ( CHAIN G AND ( RESID 17:48 OR RESID 1001:1001 ) )B16 - 62
20X-RAY DIFFRACTION7( CHAIN A AND ( RESID 81:154 OR RESID 276:348 OR RESID 747:1016 OR RESID 2001:2002 OR RESID 2003:2004 ) ) OR ( CHAIN C AND RESID 1101:1101 ) OR ( CHAIN B AND RESID 16:62 ) OR ( CHAIN G AND ( RESID 17:48 OR RESID 1001:1001 ) )G17 - 48
21X-RAY DIFFRACTION7( CHAIN A AND ( RESID 81:154 OR RESID 276:348 OR RESID 747:1016 OR RESID 2001:2002 OR RESID 2003:2004 ) ) OR ( CHAIN C AND RESID 1101:1101 ) OR ( CHAIN B AND RESID 16:62 ) OR ( CHAIN G AND ( RESID 17:48 OR RESID 1001:1001 ) )G1001
22X-RAY DIFFRACTION8( CHAIN C AND ( RESID 81:154 OR RESID 276:348 OR RESID 747:1016 OR RESID 1102:1103 OR RESID 1104:1105 ) ) OR ( CHAIN E AND ( RESID 101:101 OR RESID 17:48 ) ) OR ( CHAIN D AND RESID 19:62 )C81 - 154
23X-RAY DIFFRACTION8( CHAIN C AND ( RESID 81:154 OR RESID 276:348 OR RESID 747:1016 OR RESID 1102:1103 OR RESID 1104:1105 ) ) OR ( CHAIN E AND ( RESID 101:101 OR RESID 17:48 ) ) OR ( CHAIN D AND RESID 19:62 )C276 - 348
24X-RAY DIFFRACTION8( CHAIN C AND ( RESID 81:154 OR RESID 276:348 OR RESID 747:1016 OR RESID 1102:1103 OR RESID 1104:1105 ) ) OR ( CHAIN E AND ( RESID 101:101 OR RESID 17:48 ) ) OR ( CHAIN D AND RESID 19:62 )C747 - 1016
25X-RAY DIFFRACTION8( CHAIN C AND ( RESID 81:154 OR RESID 276:348 OR RESID 747:1016 OR RESID 1102:1103 OR RESID 1104:1105 ) ) OR ( CHAIN E AND ( RESID 101:101 OR RESID 17:48 ) ) OR ( CHAIN D AND RESID 19:62 )C1102 - 1103
26X-RAY DIFFRACTION8( CHAIN C AND ( RESID 81:154 OR RESID 276:348 OR RESID 747:1016 OR RESID 1102:1103 OR RESID 1104:1105 ) ) OR ( CHAIN E AND ( RESID 101:101 OR RESID 17:48 ) ) OR ( CHAIN D AND RESID 19:62 )C1104 - 1105
27X-RAY DIFFRACTION8( CHAIN C AND ( RESID 81:154 OR RESID 276:348 OR RESID 747:1016 OR RESID 1102:1103 OR RESID 1104:1105 ) ) OR ( CHAIN E AND ( RESID 101:101 OR RESID 17:48 ) ) OR ( CHAIN D AND RESID 19:62 )E101
28X-RAY DIFFRACTION8( CHAIN C AND ( RESID 81:154 OR RESID 276:348 OR RESID 747:1016 OR RESID 1102:1103 OR RESID 1104:1105 ) ) OR ( CHAIN E AND ( RESID 101:101 OR RESID 17:48 ) ) OR ( CHAIN D AND RESID 19:62 )E17 - 48
29X-RAY DIFFRACTION8( CHAIN C AND ( RESID 81:154 OR RESID 276:348 OR RESID 747:1016 OR RESID 1102:1103 OR RESID 1104:1105 ) ) OR ( CHAIN E AND ( RESID 101:101 OR RESID 17:48 ) ) OR ( CHAIN D AND RESID 19:62 )D19 - 62
30X-RAY DIFFRACTION9( CHAIN B AND ( RESID 63:303 OR RESID 1001:1001 ) )B63 - 303
31X-RAY DIFFRACTION9( CHAIN B AND ( RESID 63:303 OR RESID 1001:1001 ) )B1001
32X-RAY DIFFRACTION10( CHAIN D AND ( RESID 63:303 OR RESID 1001:1002 ) )D63 - 303
33X-RAY DIFFRACTION10( CHAIN D AND ( RESID 63:303 OR RESID 1001:1002 ) )D1001 - 1002

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