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- PDB-3wgv: Crystal structure of a Na+-bound Na+,K+-ATPase preceding the E1P ... -

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Basic information

Entry
Database: PDB / ID: 3wgv
TitleCrystal structure of a Na+-bound Na+,K+-ATPase preceding the E1P state with oligomycin
Components
  • (Sodium/potassium-transporting ATPase subunit ...) x 2
  • Na+/K+ ATPase gamma subunit transcript variant a
KeywordsHYDROLASE/TRANSPORT PROTEIN/ANTIBIOTIC / membrane protein / ion pump / ATPase / Na+ binding / Haloacid dehydrogenease superfamily / phosphate analogue / ATP-binding / Hydrolase / Ion transport / Nucleotide-binding / Phosphoprotein / HYDROLASE-TRANSPORT PROTEIN-ANTIBIOTIC complex
Function / homology
Function and homology information


Basigin interactions / Ion homeostasis / Na+/K+-exchanging ATPase / positive regulation of sodium ion export across plasma membrane / positive regulation of potassium ion import across plasma membrane / regulation of monoatomic ion transport / Ion transport by P-type ATPases / transporter activator activity / P-type sodium:potassium-exchanging transporter activity / sodium ion binding ...Basigin interactions / Ion homeostasis / Na+/K+-exchanging ATPase / positive regulation of sodium ion export across plasma membrane / positive regulation of potassium ion import across plasma membrane / regulation of monoatomic ion transport / Ion transport by P-type ATPases / transporter activator activity / P-type sodium:potassium-exchanging transporter activity / sodium ion binding / sodium:potassium-exchanging ATPase complex / membrane repolarization / establishment or maintenance of transmembrane electrochemical gradient / sodium ion export across plasma membrane / positive regulation of potassium ion transmembrane transport / regulation of calcium ion transmembrane transport / intracellular sodium ion homeostasis / ion channel regulator activity / intracellular potassium ion homeostasis / regulation of cardiac muscle contraction by calcium ion signaling / relaxation of cardiac muscle / positive regulation of sodium ion transmembrane transport / organelle membrane / potassium ion import across plasma membrane / potassium ion binding / ATPase activator activity / sperm flagellum / intercalated disc / lateral plasma membrane / 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 / ATPase binding / regulation of gene expression / protein-macromolecule adaptor activity / basolateral plasma membrane / cell adhesion / protein stabilization / apical plasma membrane / axon / innate immune response / protein kinase binding / ATP hydrolysis activity / ATP binding / metal ion 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. / P-type ATPase subfamily IIC, subunit alpha / Calcium-transporting ATPase, cytoplasmic domain N / Calcium-transporting ATPase, cytoplasmic domain N / 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 / HAD superfamily/HAD-like / 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 superfamily / Distorted Sandwich / Up-down Bundle / Immunoglobulin-like / Sandwich / Rossmann fold / 3-Layer(aba) Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
ADENOSINE-5'-DIPHOSPHATE / TETRAFLUOROALUMINATE ION / CHOLESTEROL / Oligomycin A / 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / Sodium/potassium-transporting ATPase subunit alpha / 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: 2.8 Å
AuthorsKanai, R. / Ogawa, H. / Vilsen, B. / Cornelius, F. / Toyoshima, C.
CitationJournal: Nature / Year: 2013
Title: Crystal structure of a Na1-bound Na1,K1-ATPase preceding the E1P state
Authors: Kanai, R. / Ogawa, H. / Vilsen, B. / Cornelius, F. / Toyoshima, C.
History
DepositionAug 9, 2013Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Oct 9, 2013Provider: repository / Type: Initial release
Revision 1.1Oct 16, 2013Group: Database references
Revision 1.2Jul 29, 2020Group: Data collection / Derived calculations / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / pdbx_struct_conn_angle / struct_conn / struct_site / struct_site_gen
Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _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 / _struct_conn.pdbx_dist_value / _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
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.3Nov 20, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature
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)322,98342
Polymers309,3956
Non-polymers13,58736
Water86548
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)161,49121
Polymers154,6983
Non-polymers6,79418
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area16600 Å2
ΔGint-169 kcal/mol
Surface area58560 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)161,49121
Polymers154,6983
Non-polymers6,79418
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area14510 Å2
ΔGint-146 kcal/mol
Surface area57590 Å2
MethodPISA
Unit cell
Length a, b, c (Å)106.285, 210.183, 256.086
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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Sodium/potassium-transporting ATPase subunit ... , 2 types, 4 molecules ACBD

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


Mass: 112399.141 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 5-1020 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / Species: kidney
References: UniProt: I7HD36, UniProt: P05024*PLUS, EC: 3.6.3.9
#2: Protein Sodium/potassium-transporting ATPase subunit beta-1 / Na+ / K+-ATPase beta 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 / Sugars , 2 types, 4 molecules GE

#11: 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


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 2
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
#3: Protein Na+/K+ ATPase gamma subunit transcript variant a


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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Non-polymers , 8 types, 82 molecules

#4: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg
#5: Chemical ChemComp-ALF / TETRAFLUOROALUMINATE ION


Mass: 102.975 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: AlF4
#6: Chemical ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE


Mass: 427.201 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#7: Chemical
ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Na
#8: Chemical
ChemComp-CLR / CHOLESTEROL


Mass: 386.654 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C27H46O
#9: Chemical
ChemComp-PC1 / 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / 3-SN-PHOSPHATIDYLCHOLINE


Mass: 790.145 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C44H88NO8P / Comment: phospholipid*YM
#10: Chemical ChemComp-EFO / Oligomycin A / (1R,4E,5'S,6S,6'S,7R,8S,10R,11R,12S,14R,15S,16R,18E,20E,22R,25S,27R,28S,29R)-22-ethyl-7,11,14,15-tetrahydroxy-6'-[(2R)-2-hydroxypropyl]-5',6,8,10,12,14,16,28,29-nonamethyl-3',4',5',6'-tetrahydro-3H,9H,13H-spiro[2,26-dioxabicyclo[23.3.1]nonacosa-4,18,20-triene-27,2'-pyran]-3,9,13-trione


Mass: 791.062 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C45H74O11 / Comment: antibiotic*YM
#12: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 48 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 2

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Sample preparation

CrystalDensity Matthews: 4.62 Å3/Da / Density % sol: 73.4 %
Crystal growTemperature: 283 K / pH: 6.2
Details: 17.5% PEG 2000MME, 10% glycerol, 200mM NaCl, 50mM MES-NMDG, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 283K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL41XU / Wavelength: 0.9
DetectorType: RAYONIX MX225HE / Detector: CCD / Date: Jun 15, 2012
RadiationMonochromator: ROTATED-INCLINED DOUBLE-CRYSTAL MONOCHROMATOR , SI (111)
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9 Å / Relative weight: 1
ReflectionResolution: 2.8→50 Å / Num. obs: 139752 / % possible obs: 98.7 % / Observed criterion σ(I): 1
Reflection shellResolution: 2.8→2.88 Å / % possible all: 99.3

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Processing

Software
NameVersionClassification
BSSdata collection
PHASERphasing
PHENIX(phenix.refine: 1.8.2_1309)refinement
DENZOdata reduction
SCALEPACKdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.8→15.995 Å / SU ML: 0.67 / σ(F): 3 / Phase error: 34.68 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2982 3965 2.98 %
Rwork0.2696 --
obs0.2704 132832 94.42 %
all-140682 -
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.8→15.995 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms20937 0 924 48 21909
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00822311
X-RAY DIFFRACTIONf_angle_d1.23930174
X-RAY DIFFRACTIONf_dihedral_angle_d19.7038740
X-RAY DIFFRACTIONf_chiral_restr0.053327
X-RAY DIFFRACTIONf_plane_restr0.0063746
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.8-2.8340.41141390.39924304X-RAY DIFFRACTION90
2.834-2.86960.3741400.38174303X-RAY DIFFRACTION89
2.8696-2.90720.37151310.36574331X-RAY DIFFRACTION90
2.9072-2.94680.34991420.36694332X-RAY DIFFRACTION89
2.9468-2.98860.37111240.37844325X-RAY DIFFRACTION91
2.9886-3.03290.40781360.36824420X-RAY DIFFRACTION91
3.0329-3.080.38141390.36964439X-RAY DIFFRACTION92
3.08-3.13010.37661450.36154494X-RAY DIFFRACTION93
3.1301-3.18370.36851220.36194548X-RAY DIFFRACTION94
3.1837-3.24110.34971340.35794537X-RAY DIFFRACTION94
3.2411-3.30290.38351490.3674594X-RAY DIFFRACTION95
3.3029-3.36970.40011300.36364680X-RAY DIFFRACTION96
3.3697-3.44220.37491450.35074679X-RAY DIFFRACTION96
3.4422-3.52150.3621570.34374655X-RAY DIFFRACTION97
3.5215-3.60860.36221390.33554714X-RAY DIFFRACTION97
3.6086-3.7050.38121230.32874056X-RAY DIFFRACTION83
3.705-3.81260.32891470.28934698X-RAY DIFFRACTION97
3.8126-3.93390.30381260.2644754X-RAY DIFFRACTION97
3.9339-4.07220.27791420.24154724X-RAY DIFFRACTION98
4.0722-4.23240.29541630.22364752X-RAY DIFFRACTION98
4.2324-4.42110.2541350.19524844X-RAY DIFFRACTION98
4.4211-4.64880.24711600.17094770X-RAY DIFFRACTION98
4.6488-4.9320.20711550.17264806X-RAY DIFFRACTION98
4.932-5.29990.20331390.17324829X-RAY DIFFRACTION98
5.2999-5.810.26311510.19284861X-RAY DIFFRACTION99
5.81-6.59850.24241660.20224870X-RAY DIFFRACTION98
6.5985-8.12760.23531380.18164860X-RAY DIFFRACTION97
8.1276-15.99520.1611480.15054688X-RAY DIFFRACTION92
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)
11.59290.0916-1.54850.4634-0.28551.78390.0549-0.43610.02460.3343-0.15010.04030.1290.1615-0.01890.4835-0.26910.030.5902-0.00920.417690.118451.760442.7613
20.49530.1013-0.93440.0558-0.24631.56160-0.2259-0.06610.16320.0182-0.0149-0.2888-0.205-0.01880.1494-0.14490.0190.4584-0.01250.258589.110748.378628.5626
30.04140.1921-0.20360.0897-0.07150.01950.0864-0.1307-0.00910.2516-0.09190.0509-0.170.2328-0.12770.4053-0.05220.0460.47490.02830.388173.922851.232142.947
40.42240.1413-0.19870.3694-0.31731.1427-0.0946-0.1781-0.50320.0686-0.24960.19230.2017-0.09910.09210.2396-0.08670.04860.36790.08690.326276.630234.612522.2776
51.1193-0.47650.1522.0042-0.61481.06560.24560.30550.2648-0.3588-0.4683-0.5993-0.05050.3626-0.50760.1092-0.0483-0.1070.3097-0.2318-0.037185.561741.2499-7.0652
60.30.1232-0.19910.5779-0.20570.90490.1723-0.0334-0.34840.0637-0.15290.12290.0298-0.10930.03640.329-0.058-0.02330.228-0.00810.25663.103337.627320.3696
71.24690.0595-0.52261.1082-0.14341.88180.053-0.03950.04980.2587-0.04580.04240.31130.1398-0.01350.6088-0.13270.07990.38180.08550.334851.859529.316861.9534
80.04040.1345-0.02540.3975-0.08010.01650.2565-0.0088-0.0583-0.43370.2476-0.61150.02750.4166-0.16241.9286-0.2794-0.31151.6094-0.05471.647341.749849.2833.4578
90.49240.03350.02630.03130.24981.00520.1453-0.13190.09660.5098-0.17740.2060.1576-0.1227-0.00621.2231-0.24230.33780.74040.0030.78934.319532.321390.4496
100.42341.0411-0.01942.79040.96832.16730.2712-0.5496-0.13060.38370.2230.00090.05550.1816-0.13341.4323-0.19230.15271.20310.1560.800645.115933.8153110.3068
110.74330.1059-0.14550.394-0.24170.23580.2375-0.42040.00640.41130.1142-0.0984-0.04450.0317-0.03891.6951-0.22140.30881.1603-0.05910.667445.089135.4282103.6399
122.5855-0.683-2.64460.17780.69652.7041-0.1696-0.8326-0.97520.4946-0.0171-0.05260.78180.42160.05791.11430.14160.21471.31070.34211.02652.002314.38690.8117
131.73290.2587-1.45720.5545-0.28832.24410.0819-0.2431-0.07340.01890.01210.19180.13340.19940.06630.90290.12180.0450.8790.24260.46367.156916.354569.1274
140.3893-0.08180.03120.5350.45161.32570.0884-0.24540.1580.3405-0.24210.040.53310.07780.13640.4622-0.28850.06360.5251-0.14330.792654.828775.072116.863
150.908-0.08750.33941.51090.01030.16850.1742-0.24640.0798-0.14670.208-0.01250.023-0.2562-0.09870.8502-0.1525-0.00551.0811-0.16171.093944.623285.7760.5556
161.1836-0.00190.7831.00750.67661.58030.1949-0.46250.03840.0888-0.1921-0.4336-0.10760.0487-0.02190.3029-0.15920.03380.4493-0.03050.521765.319277.853214.4237
170.56810.03850.21591.006-0.35081.79820.2221-0.6138-0.25610.2003-0.1032-0.0277-0.1057-0.46440.08030.7157-0.0027-0.04720.3666-0.56910.685859.418586.052362.087
181.17450.257-0.54090.76720.52921.8291-0.05320.23320.3896-0.06790.0492-0.2936-0.19860.27950.0310.4007-0.00270.08460.376-0.04670.674387.027894.922513.3589
19-0.0130.0929-0.41510.55910.10041.26080.0493-0.06370.06180.0962-0.05630.0112-0.03010.31590.00880.6897-0.03670.00450.3324-0.19620.602460.5597100.233170.1807
200.85450.4199-0.00060.5827-0.27250.8789-0.0968-0.57320.0560.2644-0.11840.00410.11780.25270.20851.0277-0.0882-0.04420.6847-0.1430.70257.166894.753896.4958
211.03291.1397-0.76823.29870.09810.9625-0.09080.062-0.0947-0.1489-0.06020.79590.0117-0.49630.03761.2594-0.20470.16991.0592-0.31680.769130.869891.4808106.8709
220.3393-0.38141.30982.2499-2.28325.4151-0.0542-0.48390.36120.51420.20970.8147-0.9366-0.9829-0.07930.91420.0826-0.30891.1554-0.16930.987235.326112.118190.4521
231.23950.151-0.65081.2967-0.09944.1085-0.03710.12040.0431-0.01490.1430.0745-0.0807-0.3573-0.06250.94490.0232-0.13140.6846-00.719141.878111.073763.7181
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN A AND (RESID 23:120 )
2X-RAY DIFFRACTION2CHAIN A AND (RESID 121:245 )
3X-RAY DIFFRACTION3CHAIN A AND (RESID 246:305 )
4X-RAY DIFFRACTION4CHAIN A AND (RESID 306:430 )
5X-RAY DIFFRACTION5CHAIN A AND (RESID 431:591 )
6X-RAY DIFFRACTION6CHAIN A AND (RESID 592:788 )
7X-RAY DIFFRACTION7CHAIN A AND (RESID 789:1016 )
8X-RAY DIFFRACTION8CHAIN B AND (RESID 1:28 )
9X-RAY DIFFRACTION9CHAIN B AND (RESID 29:160 )
10X-RAY DIFFRACTION10CHAIN B AND (RESID 161:236 )
11X-RAY DIFFRACTION11CHAIN B AND (RESID 237:303 )
12X-RAY DIFFRACTION12CHAIN G AND (RESID 15:22 )
13X-RAY DIFFRACTION13CHAIN G AND (RESID 23:48 )
14X-RAY DIFFRACTION14CHAIN C AND (RESID 23:92 )
15X-RAY DIFFRACTION15CHAIN C AND (RESID 93:152 )
16X-RAY DIFFRACTION16CHAIN C AND (RESID 153:275 )
17X-RAY DIFFRACTION17CHAIN C AND (RESID 276:347 )
18X-RAY DIFFRACTION18CHAIN C AND (RESID 348:747 )
19X-RAY DIFFRACTION19CHAIN C AND (RESID 748:1016 )
20X-RAY DIFFRACTION20CHAIN D AND (RESID 1:160 )
21X-RAY DIFFRACTION21CHAIN D AND (RESID 161:303 )
22X-RAY DIFFRACTION22CHAIN E AND (RESID 15:22 )
23X-RAY DIFFRACTION23CHAIN E AND (RESID 23:49 )

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