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- PDB-5u8r: Structure of the ectodomain of the human Type 1 insulin-like grow... -

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Basic information

Entry
Database: PDB / ID: 5u8r
TitleStructure of the ectodomain of the human Type 1 insulin-like growth factor receptor
Components
  • Fv 24-60 heavy chain
  • Fv 24-60 light chain
  • Insulin-like growth factor 1 receptor
KeywordsTRANSFERASE/IMMUNE SYSTEM / Receptor / tyrosine kinase / Type 1 insulin-like / growth factor receptor / TRANSFERASE-IMMUNE SYSTEM complex
Function / homology
Function and homology information


cardiac atrium development / negative regulation of cholangiocyte apoptotic process / insulin-like growth factor receptor activity / positive regulation of steroid hormone biosynthetic process / protein kinase complex / protein transporter activity / Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R) / IRS-related events triggered by IGF1R / insulin-like growth factor binding / negative regulation of muscle cell apoptotic process ...cardiac atrium development / negative regulation of cholangiocyte apoptotic process / insulin-like growth factor receptor activity / positive regulation of steroid hormone biosynthetic process / protein kinase complex / protein transporter activity / Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R) / IRS-related events triggered by IGF1R / insulin-like growth factor binding / negative regulation of muscle cell apoptotic process / cellular response to progesterone stimulus / positive regulation of DNA metabolic process / cellular response to zinc ion starvation / cellular response to aldosterone / insulin receptor complex / negative regulation of hepatocyte apoptotic process / cellular response to testosterone stimulus / insulin-like growth factor I binding / insulin receptor activity / transcytosis / alphav-beta3 integrin-IGF-1-IGF1R complex / response to alkaloid / positive regulation of protein-containing complex disassembly / cellular response to angiotensin / cellular response to insulin-like growth factor stimulus / response to L-glutamate / dendritic spine maintenance / insulin binding / establishment of cell polarity / negative regulation of MAPK cascade / positive regulation of axon regeneration / amyloid-beta clearance / positive regulation of cytokinesis / positive regulation of osteoblast proliferation / regulation of JNK cascade / estrous cycle / insulin receptor substrate binding / G-protein alpha-subunit binding / response to vitamin E / SHC-related events triggered by IGF1R / phosphatidylinositol 3-kinase binding / peptidyl-tyrosine autophosphorylation / cellular response to transforming growth factor beta stimulus / T-tubule / cerebellum development / cellular response to dexamethasone stimulus / axonogenesis / insulin-like growth factor receptor signaling pathway / response to nicotine / phosphatidylinositol 3-kinase/protein kinase B signal transduction / cellular response to estradiol stimulus / caveola / hippocampus development / cellular response to glucose stimulus / positive regulation of smooth muscle cell proliferation / insulin receptor binding / receptor protein-tyrosine kinase / cellular response to mechanical stimulus / cellular response to amyloid-beta / cellular senescence / insulin receptor signaling pathway / positive regulation of cold-induced thermogenesis / protein tyrosine kinase activity / response to ethanol / Extra-nuclear estrogen signaling / positive regulation of MAPK cascade / protein autophosphorylation / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / receptor complex / positive regulation of cell migration / immune response / axon / intracellular membrane-bounded organelle / neuronal cell body / positive regulation of cell population proliferation / protein-containing complex binding / negative regulation of apoptotic process / signal transduction / ATP binding / membrane / identical protein binding / plasma membrane
Similarity search - Function
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 ...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 / Protein tyrosine and serine/threonine kinase / Serine-threonine/tyrosine-protein kinase, catalytic domain / Immunoglobulins / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Immunoglobulin-like fold / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
IMIDAZOLE / D-MALATE / Insulin-like growth factor 1 receptor
Similarity search - Component
Biological speciesHomo sapiens (human)
Mus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.00001618041 Å
AuthorsLawrence, M. / Xu, Y.
Funding support Australia, 4items
OrganizationGrant numberCountry
National Health and Medical Research Council (NHMRC, Australia)APP1070526 Australia
National Health and Medical Research Council (NHMRC, Australia)APP1128553 Australia
National Health and Medical Research Council (NHMRC, Australia)IRIISS Australia
Victorian State GovernmentVictorian State Government Operational Infrastructure Support Australia
CitationJournal: Nat Commun / Year: 2018
Title: How ligand binds to the type 1 insulin-like growth factor receptor.
Authors: Xu, Y. / Kong, G.K. / Menting, J.G. / Margetts, M.B. / Delaine, C.A. / Jenkin, L.M. / Kiselyov, V.V. / De Meyts, P. / Forbes, B.E. / Lawrence, M.C.
History
DepositionDec 14, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 28, 2018Provider: repository / Type: Initial release
Revision 1.1Mar 14, 2018Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2Jan 8, 2020Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _chem_comp.name / _chem_comp.type / _pdbx_entity_nonpoly.entity_id / _pdbx_entity_nonpoly.name / _pdbx_struct_assembly_gen.asym_id_list / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Oct 4, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
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: Insulin-like growth factor 1 receptor
H: Fv 24-60 heavy chain
L: Fv 24-60 light chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)128,93513
Polymers126,7683
Non-polymers2,16710
Water0
1
A: Insulin-like growth factor 1 receptor
H: Fv 24-60 heavy chain
L: Fv 24-60 light chain
hetero molecules

A: Insulin-like growth factor 1 receptor
H: Fv 24-60 heavy chain
L: Fv 24-60 light chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)257,87026
Polymers253,5366
Non-polymers4,33420
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-x,-y,z1
Unit cell
Length a, b, c (Å)95.030, 201.730, 117.750
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number18
Space group name H-MP21212
Space group name HallP22ab
DetailsAssembly determined by non-denaturing gel

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Components

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Protein , 1 types, 1 molecules A

#1: Protein Insulin-like growth factor 1 receptor / / Insulin-like growth factor I receptor / IGF-I receptor


Mass: 101085.461 Da / Num. of mol.: 1
Mutation: residues 718-741 are replaced with the sequence AGNN
Source method: isolated from a genetically manipulated source
Details: A17delta-beta construct, see Whitten et al., J. Mol. Biol., v394, pp878-92 (2009).
Source: (gene. exp.) Homo sapiens (human) / Gene: IGF1R / Plasmid: FIII-IGFR.ECD
Details (production host): see Whitten et al., J. Mol. Biol., v394, pp878-92 (2009).
Cell line (production host): Lec8 / Production host: Cricetulus griseus (Chinese hamster)
References: UniProt: P08069, receptor protein-tyrosine kinase

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Antibody , 2 types, 2 molecules HL

#2: Antibody Fv 24-60 heavy chain


Mass: 13948.477 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: hybridoma / Source: (gene. exp.) Mus musculus (house mouse) / Plasmid: pgpHFT-SUMO-scFV / Production host: Spodoptera frugiperda (fall armyworm)
#3: Antibody Fv 24-60 light chain


Mass: 11733.944 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: hybridoma / Source: (gene. exp.) Mus musculus (house mouse) / Plasmid: pgpHFT-SUMO-scFV / Production host: Spodoptera frugiperda (fall armyworm)

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Sugars , 2 types, 6 molecules

#4: 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: 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
#7: 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.: 4
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

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Non-polymers , 3 types, 4 molecules

#5: Chemical ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: SO4
#6: Chemical ChemComp-MLT / D-MALATE / (2R)-2-HYDROXYBUTANEDIOIC ACID / 2-HYDROXY-SUCCINIC ACID / Malic acid


Mass: 134.087 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C4H6O5
#8: Chemical ChemComp-IMD / IMIDAZOLE / Imidazole


Mass: 69.085 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H5N2

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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: 4.46 Å3/Da / Density % sol: 72.4 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7
Details: 1.2 M ammonium sulfate, 0.1 M imidazole-malate pH 7.0

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.9537 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Oct 21, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9537 Å / Relative weight: 1
ReflectionResolution: 3→50 Å / Num. obs: 45844 / % possible obs: 99.7 % / Redundancy: 8.9 % / Biso Wilson estimate: 92.4253334113 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.25 / Net I/σ(I): 8.3
Reflection shellResolution: 3→3.13 Å / Redundancy: 7.2 % / Rmerge(I) obs: 3.47 / Mean I/σ(I) obs: 0.6 / Num. unique all: 5400 / CC1/2: 0.551 / % possible all: 99.5

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Processing

Software
NameVersionClassification
phenix.refine1.11.1-2575_1692refinement
PHENIX1.11.1-2575_1692refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: domains from 1IGR, 4ZXB, 3UMT

1igr

4zxb

3umt


Resolution: 3.00001618041→46.3593115758 Å / SU ML: 0.559199999756 / Cross valid method: FREE R-VALUE / σ(F): 1.33687173502 / Phase error: 37.3303485675
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.285297793528 2166 4.72874140378 %
Rwork0.255836800495 43639 -
obs0.257283021028 45805 99.3040801283 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 133.915230855 Å2
Refinement stepCycle: LAST / Resolution: 3.00001618041→46.3593115758 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8186 0 140 0 8326
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00173317964498551
X-RAY DIFFRACTIONf_angle_d0.48115750144711618
X-RAY DIFFRACTIONf_chiral_restr0.04316738331351270
X-RAY DIFFRACTIONf_plane_restr0.00286020846721488
X-RAY DIFFRACTIONf_dihedral_angle_d11.4275554375136
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3-3.06980.4780741453161380.4522889967912882X-RAY DIFFRACTION99.0163934426
3.0698-3.14650.47940283281460.4215416341372849X-RAY DIFFRACTION98.5845951284
3.1465-3.23160.4101630716391430.4020475144372818X-RAY DIFFRACTION98.3720930233
3.2316-3.32670.4137798243021400.3695619402032848X-RAY DIFFRACTION99.1044776119
3.3267-3.4340.3582712065711540.3514461993052867X-RAY DIFFRACTION98.5966057441
3.434-3.55670.3297820326271500.3299723493912847X-RAY DIFFRACTION99.1399272246
3.5567-3.6990.3308440046641420.3027380316072872X-RAY DIFFRACTION98.8845144357
3.699-3.86730.3214577255591180.2756074741672900X-RAY DIFFRACTION99.0482441746
3.8673-4.07110.3164689417091480.2668742925172901X-RAY DIFFRACTION99.5104438642
4.0711-4.3260.3245665161941410.2263364448892934X-RAY DIFFRACTION99.8376623377
4.326-4.65970.2348842271291320.1982007234952919X-RAY DIFFRACTION99.9672346003
4.6597-5.12810.2346176008381390.1958669286652944X-RAY DIFFRACTION99.9675745785
5.1281-5.86890.2829920357981580.2100868607752957X-RAY DIFFRACTION99.9037844772
5.8689-7.38930.2718984370091470.2529857335942992X-RAY DIFFRACTION99.9363260108
7.3893-46.36480.2230194420971700.2354501217883109X-RAY DIFFRACTION99.6051032807
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)
13.91479687416-0.659652716422-1.166591930381.328114066141.329970088394.22354821083-0.146238303961-1.035165772750.2820650771670.8903469205510.244568849442-0.3546151402790.09239619378780.208181127162-0.145138843071.601774063090.19221054237-0.1048376023920.812260718324-0.2167702775110.79484489855315.8497906692-31.203652242840.4523083838
25.65265697415-1.038464135340.6306974190884.11057638718-1.901723733556.174724292410.0318090942420.5522088676840.220718124492-0.068699073611-0.257372257616-1.12714141037-0.12179157457-0.1948619023730.2619186978791.27042866999-0.2706888559050.1188090201540.71012210703-0.0474744923980.96534437609814.9679050411-12.2245329461-8.62803710557
32.2608035379-0.742512933890.9173093540072.082336363690.469319508492.1555483366-0.1991476077980.384374413152-0.300969480074-0.1634829989470.08289503439490.01617818733020.9616761731680.5772059147920.09600534951551.50206949422-0.258975392961-0.05335855232390.9009963685020.1639666724890.53139374307611.467756612818.57651422420.947867910162
40.145164537571.189180179281.44328170194-0.3810847861571.261159485157.341220360340.2752955137660.06809948847650.09686284439170.00494446484358-0.03840732820620.1814828888510.8106626163530.998377307246-0.1696835146992.003927330860.322451293035-0.1259526174461.636567162320.01906834966880.57870378469817.703921961525.845190883859.573991367
53.70080699492-0.1126240770682.881142870446.20142683840.9407482730922.763883198690.945907288-0.275499156905-2.423492063421.139036703440.3378147009840.7663623995611.180189621080.214336435635-1.262672224460.8898350320460.1536926168240.1311373565110.689232115476-0.003163724354650.62644936315613.5979394413-59.439417186512.7971290368
66.561953669461.33730145543-1.996587324617.713955880971.895779170816.472338244130.0234791159854-1.6625361995-0.6017242849141.85044714467-0.222853024221-0.6709358288750.6424929677151.06418259691-0.1290397201480.5433584244050.3246207185240.09044503154830.291342948067-0.1381412812670.2900554637122.1219418893-51.433221206118.3955737728
78.9816506217-2.98710622854-5.455321525481.98215016547-3.981595109716.34207187402-0.2668161869322.22203771321-1.70064797386-2.86274904881-1.449580122850.7014566597830.850624553305-0.9071220345210.8972453209770.394300370058-0.0607299401633-0.06558191884360.848161582950.01153755874890.44042679773819.9616744615-49.69872825673.23516984681
86.032579686920.3681241082762.04487472929.657527727774.786440587696.58389066702-0.7986243330990.8678826545611.29634455822-1.01979136815-1.155248015881.531308853-0.821441269498-0.6787616327111.297390460350.7022544394560.173917641492-0.01542748757890.6782617387760.1802577769080.82545889665316.4427951554-41.29904082213.3420741254
93.368020377940.4015192079743.562826054284.87614745127-1.281657828336.84301339191-0.0141702872393-0.01431514486720.2755395117830.440960617578-1.131740755910.4781420458560.00762265046418-1.641228776880.7687552921290.9705352847680.2675734364630.2279111314450.664283661361-0.1634748899020.69943109192911.7836784238-49.499657917616.6244332677
103.047692045841.714545565642.937516186442.630114493681.164793155152.972553213080.8385192324230.7406944980041.12546934803-2.66844073172-1.40475782493-1.067361611360.3765012956550.1169240977650.3563438010471.415544849790.354044181507-0.4126512912540.8141763375670.2103583957730.9810191302057.58319822723-53.12313596410.409958204005
119.287534411382.075466268283.409125164864.355171867640.8968859119186.669236131650.196768659034-0.825970839089-0.4634168776870.6542593352480.08399152266640.343017568279-0.3611345852530.111249106496-0.1375074557920.7406298668610.1423757385640.0597751230750.4171612093390.07856442695390.43742679436222.3611389005-53.936365703810.8286601716
123.97148206276-4.27296580836-0.5900207216679.457263316354.574268024487.295241643170.4584480872650.5320757741730.524909186144-2.237835435230.140378835146-1.17001629047-0.6421013797250.32898084278-0.5664645319391.1707598149-0.05367641101060.1721516594181.089524241080.06575682057960.57855812571436.3945287838-48.3013911298-3.76287395979
133.289843731214.24058898178-1.058151471946.07597482312-0.4993426731447.63732682992-0.5805212133810.596385783648-0.786277483869-0.3796717636680.332205026216-0.4250925250470.50812114224-0.001804855902210.2066376874980.5661991371730.1601063846860.101592583680.4192701666970.01059639053940.44286298358433.8846657672-53.79328037096.86614239565
144.205187493170.369976618687-0.6213469810357.6779772777-5.46628367799.200576667230.251930409122-0.08891820214420.157310186510.6065707677570.0731970098995-0.989922044659-0.8485459036450.31386179395-0.3672057889230.9305881838170.03915188340130.1122121969361.09064111094-0.1842987104410.68358832754642.5536350303-49.94581535724.79786120898
152.570078396891.130822707320.5408818965244.5821810659-3.212224050583.087006120491.18748865848-1.781135993390.5794046267671.68851989646-0.059306058133-0.9382741538652.150581095171.35990447145-1.251058594071.530145165340.330055879793-0.05154664604181.36369553332-0.3139974617830.76920858065942.5215006922-63.64044475931.43061088823
166.41504281125-2.91961981813-0.4873658527885.56498170293.115704575861.993327325030.5300784151181.539601562920.389863801334-2.493357514-0.1030074626330.3398467810320.7123337589090.73618933113-0.2112494205331.183910850730.315994532786-0.1258477947960.5878922161610.170341556070.20618306713430.6948866674-50.20750782890.46285760271
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 307 )
2X-RAY DIFFRACTION2chain 'A' and (resid 308 through 456 )
3X-RAY DIFFRACTION3chain 'A' and (resid 457 through 600 )
4X-RAY DIFFRACTION4chain 'A' and (resid 601 through 897 )
5X-RAY DIFFRACTION5chain 'H' and (resid 0 through 21 )
6X-RAY DIFFRACTION6chain 'H' and (resid 22 through 39 )
7X-RAY DIFFRACTION7chain 'H' and (resid 40 through 51 )
8X-RAY DIFFRACTION8chain 'H' and (resid 52 through 64 )
9X-RAY DIFFRACTION9chain 'H' and (resid 65 through 83 )
10X-RAY DIFFRACTION10chain 'H' and (resid 84 through 91 )
11X-RAY DIFFRACTION11chain 'H' and (resid 92 through 117 )
12X-RAY DIFFRACTION12chain 'L' and (resid 0 through 32 )
13X-RAY DIFFRACTION13chain 'L' and (resid 33 through 52 )
14X-RAY DIFFRACTION14chain 'L' and (resid 53 through 75 )
15X-RAY DIFFRACTION15chain 'L' and (resid 76 through 84 )
16X-RAY DIFFRACTION16chain 'L' and (resid 85 through 107 )

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