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- PDB-7kd6: Insulin Receptor L1-CR plus alphaCT fragment in co-complex with F... -

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Basic information

Entry
Database: PDB / ID: 7kd6
TitleInsulin Receptor L1-CR plus alphaCT fragment in co-complex with Fv 83-7 and single-chain insulin SCI-b
Components
  • (Insulin receptor ...) x 2
  • Fv 83-7 Heavy chain
  • Fv 83-7 Light chain
  • Single-chain Insulin SCI-b
KeywordsSIGNALING PROTEIN / Insulin receptor Single-chain insulin Antibody Fv module Insulin micro-receptor
Function / homology
Function and homology information


regulation of female gonad development / positive regulation of meiotic cell cycle / insulin-like growth factor II binding / positive regulation of developmental growth / male sex determination / insulin receptor complex / insulin-like growth factor I binding / exocrine pancreas development / positive regulation of protein-containing complex disassembly / dendritic spine maintenance ...regulation of female gonad development / positive regulation of meiotic cell cycle / insulin-like growth factor II binding / positive regulation of developmental growth / male sex determination / insulin receptor complex / insulin-like growth factor I binding / exocrine pancreas development / positive regulation of protein-containing complex disassembly / dendritic spine maintenance / cargo receptor activity / insulin binding / neuronal cell body membrane / adrenal gland development / PTB domain binding / Signaling by Insulin receptor / IRS activation / positive regulation of respiratory burst / amyloid-beta clearance / regulation of embryonic development / positive regulation of receptor internalization / protein kinase activator activity / insulin receptor substrate binding / epidermis development / positive regulation of glycogen biosynthetic process / Signal attenuation / phosphatidylinositol 3-kinase binding / transport across blood-brain barrier / heart morphogenesis / activation of protein kinase B activity / Insulin receptor recycling / insulin-like growth factor receptor binding / dendrite membrane / neuron projection maintenance / positive regulation of MAP kinase activity / positive regulation of mitotic nuclear division / Insulin receptor signalling cascade / receptor-mediated endocytosis / positive regulation of glycolytic process / learning / positive regulation of D-glucose import / placental growth factor receptor activity / insulin receptor activity / vascular endothelial growth factor receptor activity / hepatocyte growth factor receptor activity / macrophage colony-stimulating factor receptor activity / platelet-derived growth factor alpha-receptor activity / platelet-derived growth factor beta-receptor activity / stem cell factor receptor activity / boss receptor activity / protein tyrosine kinase collagen receptor activity / brain-derived neurotrophic factor receptor activity / transmembrane-ephrin receptor activity / GPI-linked ephrin receptor activity / epidermal growth factor receptor activity / fibroblast growth factor receptor activity / insulin-like growth factor receptor activity / receptor protein-tyrosine kinase / peptidyl-tyrosine phosphorylation / caveola / receptor internalization / memory / cellular response to insulin stimulus / male gonad development / positive regulation of nitric oxide biosynthetic process / late endosome / insulin receptor signaling pathway / glucose homeostasis / amyloid-beta binding / positive regulation of protein phosphorylation / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / protein autophosphorylation / protein tyrosine kinase activity / positive regulation of canonical NF-kappaB signal transduction / lysosome / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / receptor complex / positive regulation of MAPK cascade / endosome membrane / positive regulation of cell migration / protein phosphorylation / G protein-coupled receptor signaling pathway / protein domain specific binding / symbiont entry into host cell / axon / external side of plasma membrane / positive regulation of cell population proliferation / regulation of DNA-templated transcription / protein-containing complex binding / GTP binding / positive regulation of DNA-templated transcription / extracellular exosome / ATP binding / identical protein binding / membrane / plasma membrane
Similarity search - Function
Insulin receptor, trans-membrane domain / Insulin receptor trans-membrane segment / Tyrosine-protein kinase, insulin-like receptor / Tyrosine-protein kinase, receptor class II, conserved site / Receptor tyrosine kinase class II signature. / Receptor L-domain / Furin-like cysteine-rich domain / Receptor L-domain superfamily / Furin-like cysteine rich region / Receptor L domain ...Insulin receptor, trans-membrane domain / Insulin receptor trans-membrane segment / Tyrosine-protein kinase, insulin-like receptor / Tyrosine-protein kinase, receptor class II, conserved site / Receptor tyrosine kinase class II signature. / Receptor L-domain / Furin-like cysteine-rich domain / Receptor L-domain superfamily / Furin-like cysteine rich region / Receptor L domain / Furin-like repeat / Furin-like repeats / Growth factor receptor cysteine-rich domain superfamily / Fibronectin type III domain / : / Fibronectin type 3 domain / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Tyrosine-protein kinase, catalytic domain / Tyrosine kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Tyrosine-protein kinase, active site / Serine-threonine/tyrosine-protein kinase, catalytic domain / Protein tyrosine and serine/threonine kinase / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Immunoglobulin-like fold / Protein kinase domain profile. / Protein kinase domain / Immunoglobulins / Protein kinase-like domain superfamily / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
Mus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.6 Å
AuthorsLawrence, M.C. / Menting, J.G.
Funding support Australia, United States, 2items
OrganizationGrant numberCountry
National Health and Medical Research Council (NHMRC, Australia)APP1058233 Australia
National Institutes of Health/National Institute of Diabetes and Digestive and Kidney Disease (NIH/NIDDK)R01 DK040949 United States
CitationJournal: Biophys.J. / Year: 2022
Title: Single-chain insulin analogs threaded by the insulin receptor alpha CT domain.
Authors: Smith, N.A. / Menting, J.G. / Weiss, M.A. / Lawrence, M.C. / Smith, B.J.
History
DepositionOct 8, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 13, 2021Provider: repository / Type: Initial release
Revision 1.1Nov 2, 2022Group: Database references / Category: citation / citation_author
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_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Oct 18, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model
Revision 1.3Oct 9, 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
B: Single-chain Insulin SCI-b
C: Fv 83-7 Heavy chain
D: Fv 83-7 Light chain
E: Insulin receptor subunit alpha
F: Insulin receptor isoform A alphaCT peptide
H: Single-chain Insulin SCI-b
I: Fv 83-7 Heavy chain
J: Fv 83-7 Light chain
K: Insulin receptor subunit alpha
L: Insulin receptor isoform A alphaCT peptide
N: Single-chain Insulin SCI-b
O: Fv 83-7 Heavy chain
P: Fv 83-7 Light chain
Q: Insulin receptor subunit alpha
R: Insulin receptor isoform A alphaCT peptide
T: Single-chain Insulin SCI-b
U: Fv 83-7 Heavy chain
V: Fv 83-7 Light chain
W: Insulin receptor subunit alpha
X: Insulin receptor isoform A alphaCT peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)295,39045
Polymers286,77020
Non-polymers8,62025
Water2,972165
1
B: Single-chain Insulin SCI-b
C: Fv 83-7 Heavy chain
D: Fv 83-7 Light chain
E: Insulin receptor subunit alpha
F: Insulin receptor isoform A alphaCT peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)74,56212
Polymers71,6925
Non-polymers2,8707
Water905
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
H: Single-chain Insulin SCI-b
I: Fv 83-7 Heavy chain
J: Fv 83-7 Light chain
K: Insulin receptor subunit alpha
L: Insulin receptor isoform A alphaCT peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)73,60911
Polymers71,6925
Non-polymers1,9176
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
N: Single-chain Insulin SCI-b
O: Fv 83-7 Heavy chain
P: Fv 83-7 Light chain
Q: Insulin receptor subunit alpha
R: Insulin receptor isoform A alphaCT peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)73,60911
Polymers71,6925
Non-polymers1,9176
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
T: Single-chain Insulin SCI-b
U: Fv 83-7 Heavy chain
V: Fv 83-7 Light chain
W: Insulin receptor subunit alpha
X: Insulin receptor isoform A alphaCT peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)73,60911
Polymers71,6925
Non-polymers1,9176
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)97.670, 128.430, 148.790
Angle α, β, γ (deg.)90.000, 90.180, 90.000
Int Tables number4
Space group name H-MP1211

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Components

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Protein , 1 types, 4 molecules BHNT

#1: Protein
Single-chain Insulin SCI-b


Mass: 6515.308 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Details: Single-chain insulin SCI-b / Source: (gene. exp.) Homo sapiens (human) / Production host: Komagataella pastoris (fungus)

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Insulin receptor ... , 2 types, 8 molecules EKQWFLRX

#4: Protein
Insulin receptor subunit alpha / IR


Mass: 36231.762 Da / Num. of mol.: 4 / Mutation: Y171H
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: INSR / Plasmid: pEE14 / Cell line (production host): Lec 8 mutant / Organ (production host): Ovary / Production host: Cricetulus griseus (Chinese hamster)
References: UniProt: P06213, receptor protein-tyrosine kinase
#5: Protein/peptide
Insulin receptor isoform A alphaCT peptide


Mass: 1922.143 Da / Num. of mol.: 4 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: receptor protein-tyrosine kinase

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Antibody , 2 types, 8 molecules CIOUDJPV

#2: Antibody
Fv 83-7 Heavy chain


Mass: 13655.276 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Production host: Brevibacillus brevis (bacteria)
#3: Antibody
Fv 83-7 Light chain


Mass: 13367.913 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Production host: Brevibacillus brevis (bacteria)

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Sugars , 4 types, 20 molecules

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


Type: oligosaccharide / Mass: 732.682 Da / Num. of mol.: 5
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1221m-1a_1-5]/1-1-2-3/a4-b1_a6-d1_b4-c1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}[(6+1)][a-L-Fucp]{}}LINUCSPDB-CARE
#7: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta- ...2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 570.542 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1a_1-5]/1-1-2/a4-b1_a6-c1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}[(6+1)][a-L-Fucp]{}}LINUCSPDB-CARE
#8: 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.: 4
Source method: isolated from a genetically manipulated source
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
#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.: 10 / 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

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Non-polymers , 3 types, 170 molecules

#9: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: SO4
#10: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Formula: C3H8O3
#12: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 165 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestN
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: 3.19 Å3/Da / Density % sol: 61.45 %
Crystal growTemperature: 296 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 16% PEG 3350, 0.2 M sodium thiocyanate (NaSCN), 0.02% sodium azide (NaN3)

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.9537 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Dec 3, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9537 Å / Relative weight: 1
ReflectionResolution: 2.6→45.67 Å / Num. obs: 112001 / % possible obs: 88.2 % / Redundancy: 3.8 % / CC1/2: 0.99 / Rmerge(I) obs: 0.216 / Net I/av σ(I): 6.1 / Net I/σ(I): 6.1
Reflection shellResolution: 2.6→2.7 Å / Rmerge(I) obs: 3.32 / Num. unique obs: 11764 / CC1/2: 0.168

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Processing

Software
NameVersionClassification
BUSTER2.10.3refinement
PDB_EXTRACT3.25data extraction
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4OGA

4oga


Resolution: 2.6→45.65 Å / Cor.coef. Fo:Fc: 0.932 / Cor.coef. Fo:Fc free: 0.916 / SU R Cruickshank DPI: 0.365 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.341 / SU Rfree Blow DPI: 0.231 / SU Rfree Cruickshank DPI: 0.239
RfactorNum. reflection% reflectionSelection details
Rfree0.221 5626 5.08 %RANDOM
Rwork0.189 ---
obs0.191 110844 98.2 %-
Displacement parametersBiso max: 210.94 Å2 / Biso mean: 87.37 Å2 / Biso min: 19.5 Å2
Baniso -1Baniso -2Baniso -3
1-1.4735 Å20 Å21.5052 Å2
2---17.8071 Å20 Å2
3---16.3336 Å2
Refine analyzeLuzzati coordinate error obs: 0.44 Å
Refinement stepCycle: final / Resolution: 2.6→45.65 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms18341 0 561 165 19067
Biso mean--119.48 50.06 -
Num. residues----2324
Refine LS restraints
Refine-IDTypeNumberRestraint functionWeightDev ideal
X-RAY DIFFRACTIONt_dihedral_angle_d6731SINUSOIDAL2
X-RAY DIFFRACTIONt_trig_c_planes
X-RAY DIFFRACTIONt_gen_planes3224HARMONIC5
X-RAY DIFFRACTIONt_it19441HARMONIC20
X-RAY DIFFRACTIONt_nbd
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_chiral_improper_torsion2593SEMIHARMONIC5
X-RAY DIFFRACTIONt_sum_occupancies
X-RAY DIFFRACTIONt_utility_distance
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact20835SEMIHARMONIC4
X-RAY DIFFRACTIONt_bond_d19441HARMONIC20.01
X-RAY DIFFRACTIONt_angle_deg26446HARMONIC21.19
X-RAY DIFFRACTIONt_omega_torsion3.37
X-RAY DIFFRACTIONt_other_torsion19.04
LS refinement shellResolution: 2.6→2.62 Å / Rfactor Rfree error: 0 / Total num. of bins used: 50
RfactorNum. reflection% reflection
Rfree0.3187 112 5.05 %
Rwork0.253 2105 -
all0.2564 2217 -
obs--75.66 %
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)
14.40370.82090.07980.9635-2.00146.3733-0.0341-0.5144-0.17880.43260.0167-0.17260.1294-0.04270.0174-0.02830.09130.04420.3062-0.1406-0.3069110.914410.491648.4304
22.622-0.2048-1.06680.85510.28323.46690.03720.320.14750.147-0.084-0.0444-0.10340.21770.0468-0.22460.00930.05110.2757-0.0194-0.0919137.6726-1.7476-13.3335
34.49921.35081.25032.30511.26174.46460.09680.3691-0.34180.0985-0.09480.39980.5378-0.5504-0.002-0.2791-0.05240.09440.2035-0.0575-0.0886118.3892-12.069-14.8227
41.4672-0.8866-0.80041.35510.90662.4153-0.03350.08310.19190.0756-0.10730.0525-0.02140.0160.1408-0.198-0.0290.09060.1217-0.056-0.1633113.156810.872918.7054
5-0.0007-3.74970.10640-0.59465.9553-0.005-0.0571-0.0949-0.12520.1145-0.20160.1535-0.0115-0.10950.1625-0.00760.09760.1251-0.0119-0.2251110.43016.977639.3007
65.19510.41230.58313.1454-1.65568.3164-0.01780.3133-0.4538-0.22690.17730.1152-0.1239-0.2584-0.1595-0.0192-0.14190.14920.27460.0918-0.307386.99397.2665-99.0027
72.97540.3589-0.31871.29530.73173.87320.01780.1328-0.0158-0.2129-0.23330.0564-0.086-0.47040.2155-0.18620.00520.02520.1665-0.002-0.081368.0702-11.0675-35.6082
84.3183-1.39650.45362.3195-1.41114.12350.136-0.0882-0.1435-0.2658-0.17-0.77090.21140.59130.0341-0.27990.01070.11870.08580.04480.024688.5291-18.176-36.1181
91.13971.5376-1.91362.9964-2.28084.7720.02340.02280.1268-0.2748-0.0353-0.0282-0.2106-0.21660.0119-0.09040.12620.1632-0.03670.0871-0.323586.25396.4193-68.8658
100.11160.0026-3.45930.9396-0.57574.6373-0.00770.036-0.178-0.03640.08580.1270.102-0.0124-0.07810.2464-0.14260.28640.0296-0.0091-0.232689.29913.2639-90.8301
113.1336-1.9414-1.82630.0744-0.51259.27090.0683-0.3850.14540.17070.13010.21640.09290.0849-0.19840.30560.0108-0.28180.25030.0678-0.34394.9352-16.507548.7803
123.43860.16421.64670.55650.34154.1074-0.1202-0.24010.37840.1333-0.06750.0449-0.1665-0.35570.1877-0.2437-0.0105-0.00890.2614-0.0505-0.099668.7741-2.5897-13.1927
134.73931.4361.47382.9677-1.42597.4511-0.24170.48480.42210.1359-0.0676-0.5595-0.78760.8490.3093-0.3406-0.2035-0.09450.35910.0123-0.040788.257.2549-14.4553
142.0615-0.35471.61931.82560.154.34570.3074-0.1622-0.23470.6158-0.1771-0.35250.9888-0.4108-0.1303-0.0118-0.1074-0.2774-0.09360.0123-0.314892.8428-16.821918.4077
15-0.0199-2.29383.15080.4583-0.00995.3787-0.0054-0.0610.14590.04440.05150.1914-0.0718-0.0311-0.04610.3679-0.0248-0.30180.0868-0.004-0.318495.937-12.881439.5389
161.18280.0837-2.10592.0911.09296.4446-0.01980.11360.3051-0.4209-0.0540.12890.18090.26360.07380.20650.0915-0.2010.3715-0.0688-0.3955119.2989-14.7131-99.0958
173.49471.16241.91152.60640.62174.4479-0.32130.53590.3855-0.49130.03950.0507-0.31870.72450.2818-0.2775-0.1139-0.02920.40120.1007-0.282138.47836.6578-36.1811
183.9621-0.9693-0.17623.81312.55544.7852-0.15250.19420.509-0.8227-0.24811.0859-0.6863-0.03230.4006-0.33610.0046-0.30570.06790.09270.1969118.368414.2668-36.8717
191.84371.23022.98082.14342.29318.519-0.14940.2985-0.0034-0.1561-0.27560.27170.28750.8820.425-0.08740.0993-0.1360.08380.0009-0.3843119.0959-12.3593-67.8869
200.3871-0.37833.77920.306-2.08255.0154-0.00570.08010.1318-0.0239-0.003-0.0362-0.03850.08020.00870.3482-0.1445-0.30180.1576-0.006-0.3444116.7985-9.9681-90.0496
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1{ B|1 - B|57 }B1 - 57
2X-RAY DIFFRACTION2{ C|0 - C|123 }C0 - 123
3X-RAY DIFFRACTION3{ D|-2 - D|113 }D-2 - 113
4X-RAY DIFFRACTION4{ E|6 - E|310 }E6 - 310
5X-RAY DIFFRACTION5{ F|704 - F|718 }F704 - 718
6X-RAY DIFFRACTION6{ H|1 - H|57 }H1 - 57
7X-RAY DIFFRACTION7{ I|0 - I|122 }I0 - 122
8X-RAY DIFFRACTION8{ J|-1 - J|113 }J-1 - 113
9X-RAY DIFFRACTION9{ K|5 - K|303 }K5 - 303
10X-RAY DIFFRACTION10{ L|704 - L|718 }L704 - 718
11X-RAY DIFFRACTION11{ N|1 - N|57 }N1 - 57
12X-RAY DIFFRACTION12{ O|0 - O|123 }O0 - 123
13X-RAY DIFFRACTION13{ P|-2 - P|112 }P-2 - 112
14X-RAY DIFFRACTION14{ Q|5 - Q|310 }Q5 - 310
15X-RAY DIFFRACTION15{ R|704 - R|718 }R704 - 718
16X-RAY DIFFRACTION16{ T|1 - T|57 }T1 - 57
17X-RAY DIFFRACTION17{ U|0 - U|119 }U0 - 119
18X-RAY DIFFRACTION18{ V|-1 - V|112 }V-1 - 112
19X-RAY DIFFRACTION19{ W|3 - W|303 }W3 - 303
20X-RAY DIFFRACTION20{ X|704 - X|717 }X704 - 717

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