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

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Basic information

Entry
Database: PDB / ID: 3wgu
TitleCrystal structure of a Na+-bound Na+,K+-ATPase preceding the E1P state without oligomycin
Components
  • (Sodium/potassium-transporting ATPase subunit ...) x 2
  • Na+/K+ ATPase gamma subunit transcript variant a
KeywordsHYDROLASE/TRANSPORT PROTEIN / membrane protein / ion pump / ATPase / Na+ binding / Haloacid dehydrogenease superfamily / phosphate analogue / ATP-binding / Ion transport / Nucleotide-binding / Phosphoprotein / HYDROLASE-TRANSPORT PROTEIN COMPLEX
Function / homology
Function and homology information


: / Ion homeostasis / cation-transporting ATPase complex / Ion transport by P-type ATPases / Na+/K+-exchanging ATPase / regulation of monoatomic ion transport / positive regulation of sodium ion export across plasma membrane / positive regulation of potassium ion import across plasma membrane / P-type sodium:potassium-exchanging transporter activity / sodium ion binding ...: / Ion homeostasis / cation-transporting ATPase complex / Ion transport by P-type ATPases / Na+/K+-exchanging ATPase / regulation of monoatomic ion transport / positive regulation of sodium ion export across plasma membrane / positive regulation of potassium ion import across plasma membrane / 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 / plasma membrane protein complex / regulation of calcium ion transmembrane transport / positive regulation of potassium ion transmembrane transport / ion channel regulator activity / intracellular sodium ion homeostasis / relaxation of cardiac muscle / regulation of cardiac muscle contraction by calcium ion signaling / positive regulation of sodium ion transmembrane transport / organelle membrane / potassium ion binding / potassium ion import across plasma membrane / ATPase activator activity / intracellular potassium ion homeostasis / intercalated disc / lateral plasma membrane / transporter activator activity / 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 / ATPase binding / regulation of gene expression / basolateral plasma membrane / protein-macromolecule adaptor activity / cell adhesion / apical plasma membrane / protein stabilization / innate immune response / axon / 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 and potassium ATPases beta subunits signature 2. / 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. / : / 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 / P-type ATPase, cytoplasmic domain N / HAD superfamily/HAD-like / : / P-type ATPase actuator domain / 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 / 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 / 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 1.3Oct 30, 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)321,40140
Polymers309,3956
Non-polymers12,00534
Water1,04558
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)160,70020
Polymers154,6983
Non-polymers6,00317
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area16650 Å2
ΔGint-170 kcal/mol
Surface area58520 Å2
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)160,70020
Polymers154,6983
Non-polymers6,00317
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area14420 Å2
ΔGint-144 kcal/mol
Surface area57630 Å2
Unit cell
Length a, b, c (Å)106.383, 211.600, 257.124
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

#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


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 , 7 types, 90 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
#11: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 58 / 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: 1

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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 2000 MME, 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: Nov 29, 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: 143103 / % possible obs: 99.9 % / Observed criterion σ(I): 1
Reflection shellResolution: 2.8→2.9 Å / % possible all: 100

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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→15.993 Å / SU ML: 0.71 / σ(F): 3 / Phase error: 36.27 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2992 6460 5.11 %
Rwork0.2645 --
obs0.2663 126511 88.89 %
all-140690 -
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.8→15.993 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms20937 0 812 58 21807
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00922195
X-RAY DIFFRACTIONf_angle_d1.25730004
X-RAY DIFFRACTIONf_dihedral_angle_d19.1058708
X-RAY DIFFRACTIONf_chiral_restr0.0723293
X-RAY DIFFRACTIONf_plane_restr0.0063742
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.8-2.83170.39922000.37453462X-RAY DIFFRACTION78
2.8317-2.86480.40152090.37443549X-RAY DIFFRACTION79
2.8648-2.89950.35921710.37963535X-RAY DIFFRACTION79
2.8995-2.9360.40571920.373546X-RAY DIFFRACTION80
2.936-2.97440.37752060.38063565X-RAY DIFFRACTION80
2.9744-3.01490.38871880.39023605X-RAY DIFFRACTION81
3.0149-3.05770.40161920.39273629X-RAY DIFFRACTION81
3.0577-3.1030.40962060.38913618X-RAY DIFFRACTION82
3.103-3.15110.41082100.38863720X-RAY DIFFRACTION83
3.1511-3.20240.42881820.38783847X-RAY DIFFRACTION85
3.2024-3.25710.41041950.38063761X-RAY DIFFRACTION85
3.2571-3.31590.39542000.38163825X-RAY DIFFRACTION85
3.3159-3.3790.39872310.36783855X-RAY DIFFRACTION87
3.379-3.44730.38961990.35934009X-RAY DIFFRACTION88
3.4473-3.52150.39142080.35233993X-RAY DIFFRACTION89
3.5215-3.60250.36082240.34083962X-RAY DIFFRACTION89
3.6025-3.69160.34632360.32574031X-RAY DIFFRACTION90
3.6916-3.79010.36422180.29864105X-RAY DIFFRACTION91
3.7901-3.90.31652100.27484128X-RAY DIFFRACTION92
3.9-4.0240.28082040.25714175X-RAY DIFFRACTION92
4.024-4.16540.28532190.23634245X-RAY DIFFRACTION94
4.1654-4.3290.25192310.21174268X-RAY DIFFRACTION95
4.329-4.52180.23372190.19094331X-RAY DIFFRACTION96
4.5218-4.75420.22342230.17574381X-RAY DIFFRACTION96
4.7542-5.04330.25152320.17384411X-RAY DIFFRACTION97
5.0433-5.41860.2192470.18454373X-RAY DIFFRACTION97
5.4186-5.93840.26412380.19774432X-RAY DIFFRACTION97
5.9384-6.74070.24682450.20444452X-RAY DIFFRACTION97
6.7407-8.29080.25132610.17994553X-RAY DIFFRACTION99
8.2908-15.99290.18482640.16234685X-RAY DIFFRACTION99
Refinement TLS params.

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

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
12.6039-0.2694-2.78960.3580.05693.38810.5734-0.83480.74880.38190.0030.07050.04010.2458-0.27030.7196-0.39630.03881.0605-0.15380.632889.940952.100842.7502
20.9489-0.1115-1.550.3102-0.55262.2927-0.0323-0.36270.05410.36550.0014-0.12790.1932-0.0267-0.03130.4668-0.2344-0.02990.7186-0.00970.456688.85648.707628.5874
3-0.05820.176-0.20090.1394-0.0146-0.02810.3594-0.41270.39830.41840.05690.0079-0.10190.6061-0.28210.666-0.12720.17750.8282-0.02850.595973.685551.536743.0297
40.5841-0.0222-0.21420.5723-0.30481.9901-0.0018-0.1497-0.260.1425-0.10250.07280.3763-0.00160.10330.3269-0.0518-0.04850.2840.11420.403776.351134.95722.3441
51.8469-0.1374-0.14122.5989-0.49991.15460.04660.24970.1774-0.2068-0.1174-0.2952-0.05650.17740.06770.1767-0.0193-0.02730.4565-0.08440.297785.21541.5362-7.005
61.4239-0.0536-1.19440.90410.54551.38590.69561.0442-0.7232-0.2291-0.93660.4364-0.0946-0.2954-0.09980.1742-0.31090.0587-0.38320.39180.25862.790137.96120.4645
72.01440.281-1.11971.6222-0.43082.7749-0.0039-0.14380.03670.2412-0.16210.09230.32790.04190.1110.7328-0.22650.12010.49960.0910.354351.708329.718762.082
80.15420.19590.03740.8007-0.26630.18050.4235-0.08270.0529-0.46740.2398-0.865-0.01310.5225-0.44942.0037-0.1347-0.31851.6452-0.23561.993741.364649.581933.7635
90.4015-0.0274-0.2032-0.02390.30541.35520.0632-0.27540.04890.6688-0.230.29570.2441-0.40440.15661.5551-0.39380.43111.2554-0.02550.898434.228232.89990.8355
100.44471.0084-0.05282.73590.99992.13540.0749-0.5011-0.39030.61370.3092-0.05270.00920.1057-0.24371.9829-0.30140.34261.31110.21670.931245.098234.5054110.6176
111.38060.1837-0.4311.1079-0.56710.5465-0.0028-0.39410.04340.52380.0627-0.0277-0.2513-0.2006-0.12661.8901-0.33140.35841.4867-0.04670.770845.036136.0865103.9345
124.2099-1.5424-1.66882.85861.73051.2058-0.1952-0.6047-0.42690.6028-0.0139-0.08930.20590.33660.15891.49210.00070.31821.92140.11041.494452.063915.004991.0156
133.73130.4255-2.5151.507-0.62293.765-0.1063-0.5209-0.1410.15170.0578-0.11610.44360.15480.21450.88530.21730.130.98630.12590.612367.151316.903469.2962
140.60630.06260.5360.47970.63081.0310.3647-0.5683-0.00050.478-0.3320.03660.23840.0490.01570.7665-0.25550.09820.7688-0.10740.902254.580875.640316.9374
151.4443-0.05640.85592.9187-0.78760.73710.2331-0.467-0.1022-0.26730.30650.05230.3247-0.6139-0.37070.9994-0.43630.05331.4064-0.2350.906144.680286.565360.5725
161.8062-0.21931.20681.34860.95842.94610.1944-0.2462-0.1240.27230.01020.03830.19040.2112-0.11250.3253-0.10810.02550.5331-0.09270.673565.067278.41914.445
171.0449-0.0205-0.12522.182-0.7363.32530.1449-0.7254-0.09920.4328-0.30630.04760.5114-0.47160.22450.76480.10220.16120.1132-0.71350.532359.437186.871962.0492
181.83830.1489-1.10420.84960.61513.4645-0.06910.34680.3948-0.0547-0.0199-0.111-0.40850.47890.0860.4653-0.00380.10180.4622-0.09870.795486.80795.420113.2045
190.97660.2094-0.82581.2646-0.02893.12780.1317-0.06540.12280.11250.034-0.079-0.10690.1334-0.10140.5306-0.0742-0.01860.2675-0.21330.586460.673101.040970.0734
201.73360.6493-0.24561.0535-0.20151.4734-0.0744-0.57030.01440.386-0.189-0.13960.24920.20670.28110.9907-0.0931-0.10880.8117-0.09890.734257.374695.531796.5752
211.4341.4005-1.294.78930.02221.4398-0.0016-0.0035-0.16710.0743-0.05711.03750.2588-0.58270.35061.3223-0.31210.20981.3491-0.31150.92431.126292.3677107.133
220.5145-0.55891.27330.9419-1.42353.16040.1169-0.34130.17650.56680.26110.5357-0.715-0.6262-0.31981.6197-0.03490.22021.861-0.29281.206735.4773112.847290.6077
232.80390.3362-1.842.7661-0.2118.6764-0.0507-0.37070.1997-0.14480.23830.1299-0.1418-0.6368-0.2260.76960.08560.07120.8283-0.01660.78141.8643111.880863.8287
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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