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- PDB-8jbm: Crystal structure of Na+,K+-ATPase in the E1.Mn2+ state -

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Basic information

Entry
Database: PDB / ID: 8jbm
TitleCrystal structure of Na+,K+-ATPase in the E1.Mn2+ state
Components
  • (Sodium/potassium-transporting ATPase subunit ...) x 2
  • FXYD domain-containing ion transport regulator
KeywordsMEMBRANE PROTEIN / ion pump / P-type ATPase
Function / homology
Function and homology information


Basigin interactions / Ion homeostasis / P-type potassium transmembrane transporter activity / 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:potassium-exchanging ATPase complex ...Basigin interactions / Ion homeostasis / P-type potassium transmembrane transporter activity / 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: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 / sodium ion transport / positive regulation of sodium ion transmembrane transport / organelle membrane / potassium ion import across plasma membrane / ATPase activator activity / sperm flagellum / intercalated disc / lateral plasma membrane / ATP metabolic process / 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
Similarity search - Function
: / Ion-transport regulator, FXYD motif / : / ATP1G1/PLM/MAT8 family / FXYD family signature. / 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. ...: / Ion-transport regulator, FXYD motif / : / ATP1G1/PLM/MAT8 family / FXYD family signature. / 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 / 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 / HAD superfamily / HAD-like superfamily
Similarity search - Domain/homology
CHOLESTEROL / : / 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE / Sodium/potassium-transporting ATPase subunit alpha / 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: 2.9 Å
AuthorsKanai, R. / Vilsen, B. / Cornelius, F. / Toyoshima, C.
Funding support Japan, 2items
OrganizationGrant numberCountry
Japan Society for the Promotion of Science (JSPS)JP19H00975 Japan
Japan Society for the Promotion of Science (JSPS)JP21K06109 Japan
CitationJournal: FEBS Lett / Year: 2023
Title: Crystal structures of Na ,K -ATPase reveal the mechanism that converts the K -bound form to Na -bound form and opens and closes the cytoplasmic gate.
Authors: Ryuta Kanai / Bente Vilsen / Flemming Cornelius / Chikashi Toyoshima /
Abstract: Na ,K -ATPase (NKA) plays a pivotal role in establishing electrochemical gradients for Na and K across the cell membrane by alternating between the E1 (showing high affinity for Na and low affinity ...Na ,K -ATPase (NKA) plays a pivotal role in establishing electrochemical gradients for Na and K across the cell membrane by alternating between the E1 (showing high affinity for Na and low affinity for K ) and E2 (low affinity to Na and high affinity to K ) forms. Presented here are two crystal structures of NKA in E1·Mg and E1·3Na states at 2.9 and 2.8 Å resolution, respectively. These two E1 structures fill a gap in our description of the NKA reaction cycle based on the atomic structures. We describe how NKA converts the K -bound E2·2K form to an E1 (E1·Mg ) form, which allows high-affinity Na binding, eventually closing the cytoplasmic gate (in E1 ~ P·ADP·3Na ) after binding three Na , while keeping the extracellular ion pathway sealed. We now understand previously unknown functional roles for several parts of NKA and that NKA uses even the lipid bilayer for gating the ion pathway.
History
DepositionMay 9, 2023Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Aug 9, 2023Provider: repository / Type: Initial release
Revision 1.1Aug 16, 2023Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.2Nov 20, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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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
B: Sodium/potassium-transporting ATPase subunit beta-1
G: FXYD domain-containing ion transport regulator
C: Sodium/potassium-transporting ATPase subunit alpha
D: Sodium/potassium-transporting ATPase subunit beta-1
E: FXYD domain-containing ion transport regulator
hetero molecules


Theoretical massNumber of molelcules
Total (without water)329,49440
Polymers310,3436
Non-polymers19,15234
Water59433
1
A: Sodium/potassium-transporting ATPase subunit alpha
B: Sodium/potassium-transporting ATPase subunit beta-1
G: FXYD domain-containing ion transport regulator
hetero molecules


Theoretical massNumber of molelcules
Total (without water)166,36021
Polymers155,1713
Non-polymers11,18918
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area19260 Å2
ΔGint-92 kcal/mol
Surface area62860 Å2
MethodPISA
2
C: Sodium/potassium-transporting ATPase subunit alpha
D: Sodium/potassium-transporting ATPase subunit beta-1
E: FXYD domain-containing ion transport regulator
hetero molecules


Theoretical massNumber of molelcules
Total (without water)163,13419
Polymers155,1713
Non-polymers7,96316
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11590 Å2
ΔGint-71 kcal/mol
Surface area60760 Å2
MethodPISA
Unit cell
Length a, b, c (Å)196.984, 74.426, 162.976
Angle α, β, γ (deg.)90.000, 116.333, 90.000
Int Tables number4
Space group name H-MP1211
Space group name HallP2yb
Symmetry operation#1: x,y,z
#2: -x,y+1/2,-z

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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


Mass: 112872.766 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / References: UniProt: D2WKD6
#2: Protein Sodium/potassium-transporting ATPase subunit beta-1 / 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 FXYD domain-containing ion transport regulator / 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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Sugars , 5 types, 5 molecules

#4: Polysaccharide alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D- ...alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 1072.964 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-6DManpa1-6[DManpa1-3]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,6,5/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3-3/a4-b1_b4-c1_c3-d1_c6-e1_e6-f1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{[(6+1)][a-D-Manp]{}}}}}}LINUCSPDB-CARE
#5: Polysaccharide alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 910.823 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3/a4-b1_b4-c1_c3-d1_c6-e1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}}LINUCSPDB-CARE
#6: 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
#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.: 1 / Source method: obtained synthetically / 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
#12: Sugar ChemComp-DMU / DECYL-BETA-D-MALTOPYRANOSIDE / DECYLMALTOSIDE


Type: D-saccharide / Mass: 482.562 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C22H42O11 / Comment: detergent*YM

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Non-polymers , 5 types, 62 molecules

#7: Chemical
ChemComp-MN / MANGANESE (II) ION


Mass: 54.938 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mn / Feature type: SUBJECT OF INVESTIGATION
#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.: 3 / Source method: obtained synthetically / Formula: C44H88NO8P / Comment: phospholipid*YM
#10: Chemical
ChemComp-PCW / 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE / (Z,Z)-4-HYDROXY-N,N,N-TRIMETHYL-10-OXO-7-[(1-OXO-9-OCTADECENYL)OXY]-3,5,9-TRIOXA-4-PHOSPHAHEPTACOS-18-EN-1-AMINIUM-4-OXIDE


Mass: 787.121 Da / Num. of mol.: 14 / Source method: obtained synthetically / Formula: C44H85NO8P / Comment: DOPC, phospholipid*YM
#13: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 33 / 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: 3.45 Å3/Da / Density % sol: 64.35 %
Crystal growTemperature: 283 K / Method: vapor diffusion, hanging drop / pH: 6.2
Details: 285 mM NaCl, 25 mM MgCl2, 15.4% (w/v) PEG2000MME, 7% (w/v) glycerol, 5 mM GSH, 0.1 mM DTT and 1 mg/ml butylhydroxytoluen, 100 mM MES

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL41XU / Wavelength: 1 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jun 9, 2019
RadiationMonochromator: Si double crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.9→30 Å / Num. obs: 54809 / % possible obs: 58 % / Redundancy: 1.5 % / Biso Wilson estimate: 83.93 Å2 / CC1/2: 0.987 / Rmerge(I) obs: 0.107 / Net I/σ(I): 7.26
Reflection shellResolution: 2.9→2.99 Å / Redundancy: 1.2 % / Rmerge(I) obs: 0.382 / Mean I/σ(I) obs: 1.17 / Num. unique obs: 218 / CC1/2: 0.502 / % possible all: 2.6

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Processing

Software
NameVersionClassification
BSSdata collection
HKL-2000data reduction
STARANISOdata scaling
PHASERphasing
PHENIX1.19.2_4158refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.9→12 Å / SU ML: 0.3918 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 32.9586
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2777 2684 5.02 %
Rwork0.2236 50823 -
obs0.2263 53507 57.44 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 88.06 Å2
Refinement stepCycle: LAST / Resolution: 2.9→12 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms20765 0 884 33 21682
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00522083
X-RAY DIFFRACTIONf_angle_d0.794229925
X-RAY DIFFRACTIONf_chiral_restr0.04783421
X-RAY DIFFRACTIONf_plane_restr0.00576391
X-RAY DIFFRACTIONf_dihedral_angle_d17.69068499
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.9-2.950.529740.348773X-RAY DIFFRACTION1.6
2.95-3.010.3978120.3327175X-RAY DIFFRACTION3.84
3.01-3.070.5063110.3482246X-RAY DIFFRACTION5.34
3.07-3.130.449190.3579338X-RAY DIFFRACTION7.36
3.13-3.210.3621300.3259512X-RAY DIFFRACTION11.2
3.21-3.280.4217400.3332723X-RAY DIFFRACTION15.71
3.28-3.370.3214630.32461044X-RAY DIFFRACTION22.53
3.37-3.470.4411680.32151401X-RAY DIFFRACTION30.35
3.47-3.580.36371150.32642093X-RAY DIFFRACTION45.13
3.58-3.70.381610.30083142X-RAY DIFFRACTION67.66
3.7-3.840.292170.2884107X-RAY DIFFRACTION88.73
3.84-4.010.34652410.26714543X-RAY DIFFRACTION97.81
4.01-4.220.29882360.24174643X-RAY DIFFRACTION99.43
4.22-4.470.27232510.21494658X-RAY DIFFRACTION99.61
4.47-4.790.25372430.19684624X-RAY DIFFRACTION99.12
4.79-5.240.25222390.2124615X-RAY DIFFRACTION98.76
5.24-5.910.29632540.22764626X-RAY DIFFRACTION98.51
5.92-7.180.28192360.22034628X-RAY DIFFRACTION97.75
7.18-120.22440.15294632X-RAY DIFFRACTION96.36
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)
10.253948851352-0.08630747410220.01470700090210.23105639035-0.9096148518291.89211722419-0.09448592269140.153484511055-0.1232818986280.01467941937120.1654173973850.1749990790890.285775403349-0.6360506225970.002901492103940.56832161116-0.07327798208140.02390511366350.502248555608-0.005083246739840.613423623977-15.003-17.039103.316
21.90124672382-0.03381034110050.5556528186610.49357362841-0.3180220312332.441608768950.0241895535605-0.531717316077-0.5254673601170.1095690077680.243655052207-0.423983257069-0.1135976744280.2017974356450.1068275356210.2770731643620.0632592900408-0.2316396996660.4495096565990.1675689442750.52575718650211.5520.501138.945
30.1408559285540.1294388570980.2734368107310.440416908310.8539967108882.66775528591-0.05672874533990.0517969958514-0.04702238056170.01719630241330.0982144676880.0711987953125-0.463235100635-0.177614862903-3.342545055690.2656708906310.04407773125270.009552607430560.2811387913580.01421205494680.3876728673-5.7147.84286.81
40.00493818018061-0.01154396882740.01124897055120.0182329257355-0.02116762471260.0203025446930.1052290131180.00264230003718-0.04215684113450.1847967908060.07705390560920.03499255650070.0608380033551-0.1464072935853.10770892178E-61.380640500290.2947920854720.08827064399461.69265887191-0.200039712331.40930551837-24.68227.58892.516
50.5808646301910.1799339682080.4423600148820.4964235632970.3185081180090.36088495591-0.3681070359450.292570371479-0.142470145553-0.1481623458950.423481810752-0.12745294652-0.9994708716660.2145835517510.04678008737691.148405141810.02964252373640.001291604061510.6352981728170.04934849669760.347870853767-8.03817.14258.975
60.1621200563170.01967409888870.2723980969980.7636282132630.1724065778870.4524652171170.411368541841-0.456598640538-0.04790810359090.290186214263-0.3563325241030.147881292957-0.7289490848240.02740489651711.94402591969E-61.026255090690.0338584668208-0.1794569529841.206997630530.1095299184030.835452118263-27.8967.50929.18
70.116228551043-0.184438436667-0.1563020134270.6954424159810.2023569741460.1886565017070.58364168545-0.09895377463370.600051533989-0.0881263443653-0.5166708076530.0106610959294-0.8717211495240.2725519645132.48560482631E-61.37969873682-0.31322136937-0.06219919393171.332708198690.07818595771110.808782018958-16.33111.17724.421
80.05107894582030.1224602218020.1267524021750.5947220621710.0638800656020.60201736112-0.06769463621280.44533016884-0.0310848326058-0.7745194393760.2217517647270.0360733432547-0.388217194939-0.1186780897250.08538237352570.8001536241230.0203835285928-0.3460531574640.9304060987710.05068890117910.62962896354-19.157-0.43629.5
90.074896279190.0909262491603-0.02810399877190.0999182444644-0.05437204845420.04634010489030.15089381692-0.268232889006-1.044117467750.0576414237791-0.14422888378-0.3384504175050.01953969925970.362119027879-2.45118786475E-50.9333600250650.0146406330964-0.06778570847391.05632051086-0.01645963862070.864887029895-13.851-11.94724.223
100.59772146558-0.694315307253-0.2240228856340.8066149117630.3733001910251.217513772120.0996764530110.117607751004-0.193153419841-0.178906328344-0.04232915556470.0948088461524-0.128010407163-0.3803662987274.30520892476E-70.835298381074-0.119110080419-0.170003152660.999490569867-0.007935838950220.498109963328-21.967-4.72130.759
110.318528801243-0.158751905839-0.02324618538580.2467626198030.03751026443420.09259492027760.1875668167010.101044454057-0.137610606358-0.4500315987020.497827519436-0.1708893577160.700394046362-0.669965190337-0.003484386651130.470667015724-0.0124898560632-0.1144647336060.661947936874-0.03838602059870.5678038486065.393-7.13659.463
120.02102571502380.0184967772383-0.004775149362020.0146141502343-0.002490619586780.0004305242013180.570699705819-0.2837698182890.03899774160910.1858775063390.1532772003950.1110247851460.3150847907390.208416642951-3.37059503725E-50.7907318981270.0793485078030.06480009652791.2988482096-0.1199537256590.89690309243714.2-10.51185.472
130.446564470116-0.0404043580688-0.6023446057210.227824303070.7603149772951.46854555615-0.111128717844-0.355517561859-0.10900468865-0.1440645174580.130206206924-0.2021682942150.2290408087780.7856225803290.03610780704130.6890300122570.09708220412380.08819027007260.686716754635-0.00609320460460.60926756561846.356-12.79934.158
141.494107650970.1859962156680.426448127688-0.01321570735570.09247395246193.16702807440.1325045596240.207961041105-0.028074745876-0.1740092934230.08525468036140.0957505330505-0.00839645574497-0.1237781615750.00166119030270.5574825368550.0148693404484-0.03313010311130.220449747028-0.08042326892920.51063266332828.318.4966.534
150.04572647068580.18230623108-0.7996103085730.19423725955-0.1005299006931.342097752920.438346038305-0.3434124704670.247641672625-0.509627422696-0.226045901503-0.0584698707246-0.576118335560.614185554402-0.01006590532710.118311816788-0.2798223649020.1401041192570.7139319123-0.2203453002230.54751934299232.34411.66360.036
16-0.0017051394333-0.000218699795615-0.000157160123982-0.002068727308750.00156396049669-0.0003595052746290.2198618804470.0214400390532-0.1848213396610.302926260928-0.0224712213457-0.1484914611890.283204563751-0.1286272327687.3031566983E-71.26552288551-0.4530147818530.2902736370161.473878339130.05685696817761.2778942765950.24136.11750.76
171.683365280680.267393174005-0.2615258819851.084418746270.380052988460.181676683305-0.0870131569124-0.8583298040460.2686649160890.0185854624468-0.02942095668080.369678906302-0.4785322573480.612702097176-0.1390366114940.822792406576-0.7140842779620.13267873420.829600979312-0.6254706707010.61863404090931.13721.60281.852
180.0325564707270.139954704286-0.03571861186360.680333573662-0.2233609794780.0711342907190.3271633767180.08290048353310.2715083167120.514828591652-0.1796444615430.330027661107-0.1417160160760.2633665141070.0754145346051.01907939159-0.267186542519-0.1498891292382.25193179868-0.3528267203080.99593346644446.37614.807113.138
190.6291963361510.841838482411-0.05559854547561.1205529681-0.06830685275350.008910563073540.078978734746-0.06076318507770.9028108408750.823512991010.08297591152540.910725084868-0.145505398296-0.3217349740970.1207292902091.2196584708-0.107057596724-0.071398060721.77254417611-0.4320060387470.85128320898823.46218.443111.893
200.196945747770.1406947198960.2581459632230.09339809531160.1712163970160.318991197626-0.151923397579-0.6259292407430.3405463517650.3851397180480.0657244453271-0.204674651421-0.07819324774010.165243209207-0.04270453696461.08607374805-0.143857668892-0.5031288743972.02434320289-0.3595122219260.6522162328249.7999.492118.057
211.3384866081-0.0202687522036-0.6127136116020.08895516432120.172244743220.569260676652-0.355880912058-0.57339835771-0.7075597301270.47370051488-0.148083226489-0.2434759642620.7672467815110.485470282448-0.09020862926181.05043356419-0.0267547297025-0.07785044779051.66422563402-0.1181559820650.7741177946929.624-2.949113.631
220.342555203420.172999566373-0.3940536007810.37748457942-0.03338644070570.5087498355770.314413058591-0.844966039057-0.06280961086880.0826301491905-0.253243416501-0.03774841832220.1492958078330.767970910925-3.72257832379E-51.0358964435-0.100842347003-0.2308442799442.10742190921-0.0705595595980.77376072424542.8730.528110.042
230.003222062608660.01337531191380.00219999568080.03851524642730.006808047793480.01146338958190.174345601446-0.554389122135-0.07506322556980.6561188280020.1198198064210.03506124456810.2428010937180.160436178154-8.32598445574E-50.657954726745-0.18058567693-0.2131243807621.29166824162-0.1330753600420.8819259949320.9480.90696.262
240.0733686173172-0.15630437706-0.07355526132150.4898004098710.1601661814020.0792199144154-0.03207564510070.184272215189-0.171969199328-0.00203000146678-0.06502037235470.2047239919670.1079282378760.309488093917-0.0004259471994960.30753655903-0.102462017057-0.0928159452240.618812629679-0.1389773944240.70256883163519.777-5.13569.508
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND RESID 22:347 )A22 - 347
2X-RAY DIFFRACTION2( CHAIN A AND RESID 348:641 )A348 - 641
3X-RAY DIFFRACTION3( CHAIN A AND RESID 642:1016 )A642 - 1016
4X-RAY DIFFRACTION4( CHAIN B AND RESID 13:28 )B13 - 28
5X-RAY DIFFRACTION5( CHAIN B AND RESID 29:80 )B29 - 80
6X-RAY DIFFRACTION6( CHAIN B AND RESID 81:132 )B81 - 132
7X-RAY DIFFRACTION7( CHAIN B AND RESID 133:168 )B133 - 168
8X-RAY DIFFRACTION8( CHAIN B AND RESID 169:192 )B169 - 192
9X-RAY DIFFRACTION9( CHAIN B AND RESID 193:217 )B193 - 217
10X-RAY DIFFRACTION10( CHAIN B AND RESID 218:303 )B218 - 303
11X-RAY DIFFRACTION11( CHAIN G AND RESID 17:45 )G17 - 45
12X-RAY DIFFRACTION12( CHAIN G AND RESID 46:51 )G46 - 51
13X-RAY DIFFRACTION13( CHAIN C AND RESID 22:305 )C22 - 305
14X-RAY DIFFRACTION14( CHAIN C AND RESID 306:700 )C306 - 700
15X-RAY DIFFRACTION15( CHAIN C AND RESID 701:1016 )C701 - 1016
16X-RAY DIFFRACTION16( CHAIN D AND RESID 13:28 )D13 - 28
17X-RAY DIFFRACTION17( CHAIN D AND RESID 29:83 )D29 - 83
18X-RAY DIFFRACTION18( CHAIN D AND RESID 84:132 )D84 - 132
19X-RAY DIFFRACTION19( CHAIN D AND RESID 133:152 )D133 - 152
20X-RAY DIFFRACTION20( CHAIN D AND RESID 153:180 )D153 - 180
21X-RAY DIFFRACTION21( CHAIN D AND RESID 181:207 )D181 - 207
22X-RAY DIFFRACTION22( CHAIN D AND RESID 208:303 )D208 - 303
23X-RAY DIFFRACTION23( CHAIN E AND RESID 16:22 )E16 - 22
24X-RAY DIFFRACTION24( CHAIN E AND RESID 23:48 )E23 - 48

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