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- PDB-7wbq: Crystal structure of the receptor binding domain of SARS-CoV-2 De... -

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Basic information

Entry
Database: PDB / ID: 7wbq
TitleCrystal structure of the receptor binding domain of SARS-CoV-2 Delta variant spike glycoprotein in complex with its receptor human ACE2
Components
  • Angiotensin-converting enzyme 2
  • Spike protein S1
KeywordsVIRAL PROTEIN / Complex
Function / homology
Function and homology information


positive regulation of amino acid transport / angiotensin-converting enzyme 2 / positive regulation of L-proline import across plasma membrane / Hydrolases; Acting on peptide bonds (peptidases); Metallocarboxypeptidases / angiotensin-mediated drinking behavior / tryptophan transport / positive regulation of gap junction assembly / regulation of systemic arterial blood pressure by renin-angiotensin / regulation of vasoconstriction / regulation of cardiac conduction ...positive regulation of amino acid transport / angiotensin-converting enzyme 2 / positive regulation of L-proline import across plasma membrane / Hydrolases; Acting on peptide bonds (peptidases); Metallocarboxypeptidases / angiotensin-mediated drinking behavior / tryptophan transport / positive regulation of gap junction assembly / regulation of systemic arterial blood pressure by renin-angiotensin / regulation of vasoconstriction / regulation of cardiac conduction / peptidyl-dipeptidase activity / angiotensin maturation / maternal process involved in female pregnancy / Metabolism of Angiotensinogen to Angiotensins / metallocarboxypeptidase activity / Attachment and Entry / carboxypeptidase activity / negative regulation of signaling receptor activity / positive regulation of cardiac muscle contraction / regulation of cytokine production / viral life cycle / blood vessel diameter maintenance / regulation of transmembrane transporter activity / brush border membrane / negative regulation of smooth muscle cell proliferation / cilium / negative regulation of ERK1 and ERK2 cascade / endocytic vesicle membrane / metallopeptidase activity / positive regulation of reactive oxygen species metabolic process / virus receptor activity / regulation of cell population proliferation / regulation of inflammatory response / Maturation of spike protein / viral translation / Translation of Structural Proteins / Virion Assembly and Release / host cell surface / host extracellular space / endopeptidase activity / suppression by virus of host tetherin activity / Induction of Cell-Cell Fusion / structural constituent of virion / Potential therapeutics for SARS / entry receptor-mediated virion attachment to host cell / host cell endoplasmic reticulum-Golgi intermediate compartment membrane / receptor-mediated endocytosis of virus by host cell / Attachment and Entry / membrane fusion / positive regulation of viral entry into host cell / receptor-mediated virion attachment to host cell / receptor ligand activity / host cell surface receptor binding / symbiont entry into host cell / membrane raft / apical plasma membrane / fusion of virus membrane with host plasma membrane / endoplasmic reticulum lumen / fusion of virus membrane with host endosome membrane / viral envelope / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / virion attachment to host cell / SARS-CoV-2 activates/modulates innate and adaptive immune responses / host cell plasma membrane / virion membrane / cell surface / extracellular space / extracellular exosome / zinc ion binding / extracellular region / membrane / identical protein binding / plasma membrane
Similarity search - Function
Collectrin-like domain profile. / Collectrin domain / Renal amino acid transporter / Peptidase family M2 domain profile. / Peptidase M2, peptidyl-dipeptidase A / Angiotensin-converting enzyme / Neutral zinc metallopeptidases, zinc-binding region signature. / Spike (S) protein S1 subunit, receptor-binding domain, SARS-CoV-2 / Spike (S) protein S1 subunit, N-terminal domain, SARS-CoV-like / Betacoronavirus spike (S) glycoprotein S1 subunit N-terminal (NTD) domain profile. ...Collectrin-like domain profile. / Collectrin domain / Renal amino acid transporter / Peptidase family M2 domain profile. / Peptidase M2, peptidyl-dipeptidase A / Angiotensin-converting enzyme / Neutral zinc metallopeptidases, zinc-binding region signature. / Spike (S) protein S1 subunit, receptor-binding domain, SARS-CoV-2 / Spike (S) protein S1 subunit, N-terminal domain, SARS-CoV-like / Betacoronavirus spike (S) glycoprotein S1 subunit N-terminal (NTD) domain profile. / Spike glycoprotein, N-terminal domain superfamily / Betacoronavirus spike (S) glycoprotein S1 subunit C-terminal (CTD) domain profile. / Spike glycoprotein, betacoronavirus / Spike (S) protein S1 subunit, receptor-binding domain, betacoronavirus / Spike S1 subunit, receptor binding domain superfamily, betacoronavirus / Betacoronavirus spike glycoprotein S1, receptor binding / Spike glycoprotein S1, N-terminal domain, betacoronavirus-like / Betacoronavirus-like spike glycoprotein S1, N-terminal / Spike glycoprotein S2, coronavirus, heptad repeat 1 / Spike glycoprotein S2, coronavirus, heptad repeat 2 / Coronavirus spike (S) glycoprotein S2 subunit heptad repeat 2 (HR2) region profile. / Coronavirus spike (S) glycoprotein S2 subunit heptad repeat 1 (HR1) region profile. / Spike glycoprotein S2 superfamily, coronavirus / Spike glycoprotein S2, coronavirus / Coronavirus spike glycoprotein S2 / Coronavirus spike glycoprotein S1, C-terminal / Coronavirus spike glycoprotein S1, C-terminal
Similarity search - Domain/homology
Spike glycoprotein / Angiotensin-converting enzyme 2
Similarity search - Component
Biological speciesHomo sapiens (human)
Severe acute respiratory syndrome coronavirus 2
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.34 Å
AuthorsQi, J. / Han, P.
Funding support China, 1items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC) China
CitationJournal: Cell / Year: 2022
Title: Receptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2.
Authors: Pengcheng Han / Linjie Li / Sheng Liu / Qisheng Wang / Di Zhang / Zepeng Xu / Pu Han / Xiaomei Li / Qi Peng / Chao Su / Baihan Huang / Dedong Li / Rong Zhang / Mingxiong Tian / Lutang Fu / ...Authors: Pengcheng Han / Linjie Li / Sheng Liu / Qisheng Wang / Di Zhang / Zepeng Xu / Pu Han / Xiaomei Li / Qi Peng / Chao Su / Baihan Huang / Dedong Li / Rong Zhang / Mingxiong Tian / Lutang Fu / Yuanzhu Gao / Xin Zhao / Kefang Liu / Jianxun Qi / George F Gao / Peiyi Wang /
Abstract: The coronavirus disease 2019 (COVID-19) pandemic continues worldwide with many variants arising, some of which are variants of concern (VOCs). A recent VOC, omicron (B.1.1.529), which obtains a large ...The coronavirus disease 2019 (COVID-19) pandemic continues worldwide with many variants arising, some of which are variants of concern (VOCs). A recent VOC, omicron (B.1.1.529), which obtains a large number of mutations in the receptor-binding domain (RBD) of the spike protein, has risen to intense scientific and public attention. Here, we studied the binding properties between the human receptor ACE2 (hACE2) and the VOC RBDs and resolved the crystal and cryoelectron microscopy structures of the omicron RBD-hACE2 complex as well as the crystal structure of the delta RBD-hACE2 complex. We found that, unlike alpha, beta, and gamma, omicron RBD binds to hACE2 at a similar affinity to that of the prototype RBD, which might be due to compensation of multiple mutations for both immune escape and transmissibility. The complex structures of omicron RBD-hACE2 and delta RBD-hACE2 reveal the structural basis of how RBD-specific mutations bind to hACE2.
History
DepositionDec 17, 2021Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jan 19, 2022Provider: repository / Type: Initial release
Revision 1.1Feb 16, 2022Group: Database references / Category: citation
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2Mar 2, 2022Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.3Nov 29, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Angiotensin-converting enzyme 2
B: Spike protein S1
C: Angiotensin-converting enzyme 2
D: Spike protein S1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)192,02519
Polymers188,4664
Non-polymers3,55915
Water0
1
A: Angiotensin-converting enzyme 2
B: Spike protein S1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)95,9759
Polymers94,2332
Non-polymers1,7427
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
C: Angiotensin-converting enzyme 2
D: Spike protein S1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)96,05010
Polymers94,2332
Non-polymers1,8178
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)89.773, 143.654, 106.414
Angle α, β, γ (deg.)90.000, 95.290, 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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Protein , 2 types, 4 molecules ACBD

#1: Protein Angiotensin-converting enzyme 2 / / ACE-related carboxypeptidase / Angiotensin-converting enzyme homolog


Mass: 69038.578 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ACE2
Production host: Insect cell expression vector pTIE1 (others)
References: UniProt: Q9BYF1, angiotensin-converting enzyme 2, Hydrolases; Acting on peptide bonds (peptidases); Metallocarboxypeptidases
#2: Protein Spike protein S1


Mass: 25194.447 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Severe acute respiratory syndrome coronavirus 2
Gene: S, 2 / Production host: Homo sapiens (human) / References: UniProt: P0DTC2

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Sugars , 3 types, 13 molecules

#3: 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.: 2 / Source method: obtained synthetically
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam 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
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}LINUCSPDB-CARE
#4: Polysaccharide beta-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 367.349 Da / Num. of mol.: 1 / Source method: obtained synthetically
DescriptorTypeProgram
LFucpb1-6DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/2,2,1/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1b_1-5]/1-2/a6-b1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(6+1)][b-L-Fucp]{}}LINUCSPDB-CARE
#5: 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.: 10 / Source method: obtained synthetically / Formula: C8H15NO6 / Feature type: SUBJECT OF INVESTIGATION
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 , 1 types, 2 molecules

#6: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn / Feature type: SUBJECT OF INVESTIGATION

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Details

Has ligand of interestY

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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: 3.75 Å3/Da / Density % sol: 67.24 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 0.1M MES pH 6.5,10%w/v PEG 5000 MME,12% v/v 1-propanol

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL02U1 / Wavelength: 0.97918 Å
DetectorType: DECTRIS EIGER2 X 9M / Detector: PIXEL / Date: Sep 24, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97918 Å / Relative weight: 1
ReflectionResolution: 3.34→50 Å / Num. obs: 38716 / % possible obs: 100 % / Redundancy: 7 % / Biso Wilson estimate: 106.3 Å2 / CC1/2: 0.992 / Rmerge(I) obs: 0.162 / Rsym value: 0.162 / Net I/σ(I): 9.4
Reflection shellResolution: 3.34→3.47 Å / Redundancy: 7.2 % / Rmerge(I) obs: 1.307 / Mean I/σ(I) obs: 1.1 / Num. unique obs: 3873 / CC1/2: 0.825 / Rsym value: 1.307 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX1.19rc3_4028refinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6LZG

6lzg


Resolution: 3.34→44.7 Å / SU ML: 0.5127 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 27.6848
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2264 1986 5.16 %
Rwork0.1974 36504 -
obs0.1989 38490 98.78 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 120.42 Å2
Refinement stepCycle: LAST / Resolution: 3.34→44.7 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12803 0 222 0 13025
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00313398
X-RAY DIFFRACTIONf_angle_d0.628818212
X-RAY DIFFRACTIONf_chiral_restr0.04421949
X-RAY DIFFRACTIONf_plane_restr0.00452344
X-RAY DIFFRACTIONf_dihedral_angle_d7.84461842
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.34-3.430.43751250.37042301X-RAY DIFFRACTION87.23
3.43-3.520.38211410.33362598X-RAY DIFFRACTION99.31
3.52-3.620.31171390.29932591X-RAY DIFFRACTION99.06
3.62-3.740.31031430.26162618X-RAY DIFFRACTION99.68
3.74-3.870.28161430.22542618X-RAY DIFFRACTION99.64
3.87-4.030.24881440.20432637X-RAY DIFFRACTION99.96
4.03-4.210.21421420.18752625X-RAY DIFFRACTION99.96
4.21-4.430.21460.17792654X-RAY DIFFRACTION100
4.43-4.710.22861430.15712622X-RAY DIFFRACTION99.89
4.71-5.070.17771430.15482633X-RAY DIFFRACTION99.96
5.07-5.580.21191450.17422658X-RAY DIFFRACTION100
5.58-6.390.22811440.18792636X-RAY DIFFRACTION99.96
6.39-8.040.18751440.18972661X-RAY DIFFRACTION100
8.04-44.70.19241440.17932652X-RAY DIFFRACTION98.31
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)
13.229849916971.431381506871.199272898065.582307090050.7814513113660.629848666679-0.2206299157750.3407040236970.08909202827780.2814972084810.2973595563030.700828859326-0.232929730458-0.0843478041995-0.07586428697341.111504734230.0231786585479-0.1068449758730.9349860633250.02841568778230.92740369438217.28642.26256.751
26.429665317332.13960749021.865680463237.002874246083.367912411894.95894174430.700824572289-0.843448402722-0.01639837889091.65267141069-0.7792251815060.8224391983550.777417569752-1.15451655051-0.028324726710.884175266096-0.04188438385230.0960388843331.03431076618-0.07385966217030.736396967154-13.42222.26353.82
33.691261997420.9262764593191.295145392332.496733119840.4497700050062.961275448880.04726195770360.49346712195-0.3994840370930.04803950884440.0594832353127-0.1495610528130.1103088493350.238734813344-0.09225487748070.7103881257520.0632463624777-0.01936158599360.735704522276-0.1530576655210.6079170075862.26919.81240.094
42.460064220441.694748527240.3409199226337.019338116440.8298089192294.401262601890.3044876155850.388825931883-0.8610557972380.441344658746-0.0867648514011-0.1775560355890.8090896461980.461114579006-0.2084611333440.8176654964120.203798729246-0.2556531576580.908089802256-0.124578727480.97151868367618.63915.65552.665
54.878044520240.5607611893120.8972758742712.56422542410.8582216469782.93047062981-0.009494920539840.759722111469-0.791453998043-0.1938800407160.05547374768180.00411395694320.07782488603730.29332101087-0.03897833163070.7010684337540.0144061436303-0.03598762953940.757179873435-0.09735738378660.6277394285853.9120.16535.113
68.84217264842-0.8608541768763.772059457975.89250885917-0.9730519593917.44965293905-0.348683152001-0.4127987880610.4052311179290.09427087159550.250103339014-0.9081490903430.2346324921870.7996230998660.03104714564621.028754444880.210654502921-0.2914003058871.09087523353-0.3108495099631.0387711691953.04936.75976.079
72.01135417209-4.447116868746.27239052442.62841865291-0.1541387411027.012571884130.308859068535-0.581350643767-2.94417214429-0.03196551485620.192305589169-0.4441649260311.657859213540.67437120618-0.2657923892481.626510377330.104363311328-0.3750067719061.467751430270.1781242243812.0124916822954.43423.33469.43
86.44893360015-2.47760313565-0.9680487211043.926015711560.04848932310224.564396549710.114040460250.459561577738-0.419146958197-0.303228505630.270947490174-0.8761747110440.04433404945970.841814933755-0.3239533108860.909847620059-0.030370862195-0.1246794439351.03599904433-0.1705438689050.84625337467147.02236.78664.059
95.94654958089-1.931985649492.494065541763.83685816977-0.1750059057053.434633022240.06191901943270.4498346605481.87388908859-0.8956339045980.2912339844310.104330115156-0.4109887193440.03232303917280.03038940946520.944636100649-0.150765699697-0.1071421803551.081267011550.2741741635651.2044255901640.11454.67961.306
104.38661993204-1.935230771791.729952446945.34245979024-1.273011826111.76891196309-0.27097921882-0.174902554010.158726167235-0.05957291619620.619333094394-0.334296272315-0.0282009107910.328684494816-0.304111891950.9159992330780.064928076571-0.07356126912420.970390745713-0.1392080694560.59266297626542.15841.08466.304
111.95391472844-2.089736803260.07280916777495.77302118544.756586705182.59939643778-0.121894579488-1.18868420936-0.1169282664941.710564729090.5007461314430.1672579700341.234694904770.258288984532-0.3451777541051.244072152450.0086863714813-0.05397919118861.58910848120.2558572262370.91461406803148.66746.32415.522
124.093457017160.557340760280.2155496746021.05360894858-1.46110979151.733771296580.0632152692086-1.40497580460.8610374921690.3841644519360.1095954592750.401767275320.290481758785-0.332370592805-0.1277153224351.413692253940.31076949244-0.2086057644111.977089478430.02125312909991.0702226230137.58258.11618.862
133.6252465413-0.6477939800871.095571345341.783085951150.03929442880685.6292773320.294262535415-0.638561439269-0.9247923238520.03742317891970.562470891020.7817944938460.693611502939-1.28305957696-0.7625555712321.40335982554-0.00646201435259-0.2779237102741.317250734820.5560482714491.4568436701817.21254.551-1.841
143.51204665418-1.172905884210.9315114366131.75766471618-0.974375322423.96122581038-0.271429123032-0.6573715480770.2637948734690.5509963833280.5689846539910.103167739858-0.00672038126456-0.820985963734-0.3130187156650.7737722010640.0429995353743-0.07145429902110.8741894732750.1382991291590.83520873830830.86869.737-7.905
155.14171074471-0.359910005621.244852931415.530452413540.03985904000297.061232058740.584791073984-0.793338764367-0.6361260101140.0230111027244-0.10452198287-0.08472992637530.712291335911-0.288421042049-0.4496855417840.7213448873360.0490986776419-0.07456391774580.978988409680.07450917106240.84066037615951.6645.665-12.428
164.4372248978-0.503946625082-1.16644622262.748605699531.36252089561.91540332413-0.027039505837-0.3678667860280.1129480438880.06475578152750.3256831390150.07063171296670.116461012406-0.399007146307-0.295640095750.731847189362-0.000746645191817-0.1993815290540.788782168986-0.00450819348470.66986563772250.1956.075-10.659
175.31696290084-0.3971493609430.08338401632652.82338036711-0.02489790552642.832589557070.065668881267-0.7949599474490.09162918005560.3852373573460.4417615100250.272536643222-0.160509625373-0.515857604804-0.4323394529240.9004340634440.113643870035-0.1194204859680.8873252656770.1404022343410.81866738947634.00367.788-5.675
186.45707469155-1.593576461313.07153966883.37050506673-1.317053892714.53350781423-0.560347531989-0.9473469794330.9689383156250.4806504088920.331587313219-0.109612516408-0.431936375779-0.5432238844920.2999785357030.7599747305590.0831915698534-0.05260864837580.76387818432-0.04270725303730.74438834607637.2574.932-10.553
195.68159487871-0.10837473542-0.5831887072914.753816221040.7152087634945.615892892660.375501080812-0.250976479012-0.7369223910740.0552619407434-0.0653546292677-0.8837162679670.8708693705210.45737540647-0.07005966113051.020694280910.177991740805-0.1471473855081.444458199260.2323945574491.1117131318284.87232.22614.481
205.750974119260.5401592949020.2309609031832.848057982050.3572310548693.60107334151-0.150634862644-0.803652021374-0.14215113843-0.2966960300180.0622299090436-0.0575227954843-0.04681786552310.3601974681330.1093485150541.11474017170.0681607445902-0.2377096611841.214219824750.1973729503580.89645655752979.18343.2911.663
213.9807470728-1.74053943826-0.6004865660822.59857637434-0.7171663700220.880798008673-0.045573296502-1.68137762058-0.09977671692420.798117316890.2410758637760.014392508878-0.453514316489-0.0647535374254-0.1151838944791.086712274510.0609432881189-0.1051714541261.728576988880.1203190384570.81958094793265.07245.9324.573
227.327390375590.9957288573622.37787170856.879279682181.168251873025.776168569230.1666416775010.304947601405-0.7815014731260.2397485368570.274813875742-0.78164233848-0.4011914566481.16827594197-0.5380706387721.0413572278-0.0570516094443-0.09477066670491.541259950480.09691276940590.87845279301790.69139.42314.213
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND RESID 19:109 )A19 - 109
2X-RAY DIFFRACTION2( CHAIN A AND RESID 110:172 )A110 - 172
3X-RAY DIFFRACTION3( CHAIN A AND RESID 173:318 )A173 - 318
4X-RAY DIFFRACTION4( CHAIN A AND RESID 319:431 )A319 - 431
5X-RAY DIFFRACTION5( CHAIN A AND RESID 432:614 )A432 - 614
6X-RAY DIFFRACTION6( CHAIN B AND RESID 333:364 )B333 - 364
7X-RAY DIFFRACTION7( CHAIN B AND RESID 365:375 )B365 - 375
8X-RAY DIFFRACTION8( CHAIN B AND RESID 376:459 )B376 - 459
9X-RAY DIFFRACTION9( CHAIN B AND RESID 460:479 )B460 - 479
10X-RAY DIFFRACTION10( CHAIN B AND RESID 480:527 )B480 - 527
11X-RAY DIFFRACTION11( CHAIN C AND RESID 19:82 )C19 - 82
12X-RAY DIFFRACTION12( CHAIN C AND RESID 83:129 )C83 - 129
13X-RAY DIFFRACTION13( CHAIN C AND RESID 130:193 )C130 - 193
14X-RAY DIFFRACTION14( CHAIN C AND RESID 194:293 )C194 - 293
15X-RAY DIFFRACTION15( CHAIN C AND RESID 294:352 )C294 - 352
16X-RAY DIFFRACTION16( CHAIN C AND RESID 353:431 )C353 - 431
17X-RAY DIFFRACTION17( CHAIN C AND RESID 432:558 )C432 - 558
18X-RAY DIFFRACTION18( CHAIN C AND RESID 559:614 )C559 - 614
19X-RAY DIFFRACTION19( CHAIN D AND RESID 333:364 )D333 - 364
20X-RAY DIFFRACTION20( CHAIN D AND RESID 365:459 )D365 - 459
21X-RAY DIFFRACTION21( CHAIN D AND RESID 460:506 )D460 - 506
22X-RAY DIFFRACTION22( CHAIN D AND RESID 507:526 )D507 - 526

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