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- PDB-9cz7: Crystal structure of integrin avb6 headpiece in complex with comp... -

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Basic information

Entry
Database: PDB / ID: 9cz7
TitleCrystal structure of integrin avb6 headpiece in complex with compound 12
Components
  • 17E6 Fab heavy chain
  • 17E6 Fab light chain
  • Integrin alpha-V heavy chain
  • Integrin beta-6
KeywordsCELL ADHESION/IMMUNE SYSTEM / avb6 integrin / fibrosis / idiopathic pulmonary fibrosis / free energy perturbation / CELL ADHESION / CELL ADHESION-IMMUNE SYSTEM complex
Function / homology
Function and homology information


hard palate development / Langerhans cell differentiation / integrin alphav-beta8 complex / integrin alphav-beta6 complex / transforming growth factor beta production / negative regulation of entry of bacterium into host cell / integrin alphav-beta5 complex / extracellular matrix protein binding / opsonin binding / enamel mineralization ...hard palate development / Langerhans cell differentiation / integrin alphav-beta8 complex / integrin alphav-beta6 complex / transforming growth factor beta production / negative regulation of entry of bacterium into host cell / integrin alphav-beta5 complex / extracellular matrix protein binding / opsonin binding / enamel mineralization / integrin alphav-beta1 complex / bronchiole development / Cross-presentation of particulate exogenous antigens (phagosomes) / Laminin interactions / negative regulation of lipoprotein metabolic process / integrin alphav-beta3 complex / entry into host cell by a symbiont-containing vacuole / alphav-beta3 integrin-PKCalpha complex / phospholipid homeostasis / alphav-beta3 integrin-HMGB1 complex / negative regulation of lipid transport / regulation of phagocytosis / : / Elastic fibre formation / alphav-beta3 integrin-IGF-1-IGF1R complex / surfactant homeostasis / transforming growth factor beta binding / positive regulation of small GTPase mediated signal transduction / filopodium membrane / extracellular matrix binding / apolipoprotein A-I-mediated signaling pathway / apoptotic cell clearance / wound healing, spreading of epidermal cells / integrin complex / heterotypic cell-cell adhesion / Molecules associated with elastic fibres / Mechanical load activates signaling by PIEZO1 and integrins in osteocytes / negative chemotaxis / cell adhesion mediated by integrin / Syndecan interactions / microvillus membrane / skin development / lung alveolus development / cell-substrate adhesion / positive regulation of osteoblast proliferation / endodermal cell differentiation / PECAM1 interactions / TGF-beta receptor signaling activates SMADs / positive regulation of intracellular signal transduction / lamellipodium membrane / fibronectin binding / negative regulation of macrophage derived foam cell differentiation / negative regulation of lipid storage / ECM proteoglycans / Integrin cell surface interactions / voltage-gated calcium channel activity / vasculogenesis / specific granule membrane / coreceptor activity / extrinsic apoptotic signaling pathway in absence of ligand / phagocytic vesicle / ERK1 and ERK2 cascade / positive regulation of cell adhesion / transforming growth factor beta receptor signaling pathway / substrate adhesion-dependent cell spreading / molecular function activator activity / protein kinase C binding / Turbulent (oscillatory, disturbed) flow shear stress activates signaling by PIEZO1 and integrins in endothelial cells / cell-matrix adhesion / Signal transduction by L1 / integrin-mediated signaling pathway / cellular response to ionizing radiation / negative regulation of extrinsic apoptotic signaling pathway / wound healing / cell morphogenesis / bone development / calcium ion transmembrane transport / cell-cell adhesion / response to virus / VEGFA-VEGFR2 Pathway / ruffle membrane / integrin binding / cell migration / virus receptor activity / positive regulation of cytosolic calcium ion concentration / protease binding / angiogenesis / receptor complex / cell adhesion / immune response / positive regulation of cell migration / inflammatory response / symbiont entry into host cell / external side of plasma membrane / focal adhesion / positive regulation of cell population proliferation / Neutrophil degranulation / cell surface / extracellular exosome / metal ion binding
Similarity search - Function
Integrin beta, epidermal growth factor-like domain 1 / Integrin beta epidermal growth factor like domain 1 / Integrin beta subunit, cytoplasmic domain / Integrin beta cytoplasmic domain / Integrin_b_cyt / Integrin beta tail domain / : / Integrin alpha Ig-like domain 3 / Integrin EGF domain / Integrin beta subunit, tail ...Integrin beta, epidermal growth factor-like domain 1 / Integrin beta epidermal growth factor like domain 1 / Integrin beta subunit, cytoplasmic domain / Integrin beta cytoplasmic domain / Integrin_b_cyt / Integrin beta tail domain / : / Integrin alpha Ig-like domain 3 / Integrin EGF domain / Integrin beta subunit, tail / Integrin beta tail domain superfamily / Integrin_B_tail / EGF-like domain, extracellular / EGF-like domain / Integrins beta chain EGF (I-EGF) domain profile. / Integrin alpha cytoplasmic region / Integrin beta subunit, VWA domain / Integrin beta subunit / Integrin beta N-terminal / Integrin beta chain VWA domain / Integrin plexin domain / Integrins beta chain EGF (I-EGF) domain signature. / Integrin beta subunits (N-terminal portion of extracellular region) / Integrin alpha-2 / Integrin alpha Ig-like domain 1 / Integrin alpha chain / Integrin alpha beta-propellor / Integrin alpha chain, C-terminal cytoplasmic region, conserved site / : / Integrin alpha Ig-like domain 2 / Integrins alpha chain signature. / FG-GAP repeat profile. / Integrin alpha (beta-propellor repeats). / FG-GAP repeat / FG-GAP repeat / Integrin domain superfamily / Integrin alpha, N-terminal / PSI domain / domain found in Plexins, Semaphorins and Integrins / von Willebrand factor A-like domain superfamily / EGF-like domain signature 1. / EGF-like domain signature 2.
Similarity search - Domain/homology
: / ACETATE ION / Integrin alpha-V / Integrin beta-6
Similarity search - Component
Biological speciesHomo sapiens (human)
Mus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.57 Å
AuthorsMonroy, M.F. / Qiao, Q. / Lin, F.Y.
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: J.Med.Chem. / Year: 2024
Title: The Discovery of MORF-627, a Highly Selective Conformationally-Biased Zwitterionic Integrin alpha v beta 6 Inhibitor for Fibrosis.
Authors: Harrison, B.A. / Dowling, J.E. / Bursavich, M.G. / Troast, D.M. / Chong, K.M. / Hahn, K.N. / Zhong, C. / Mulvihill, K.M. / Nguyen, H. / Monroy, M.F. / Qiao, Q. / Sosa, B. / Mostafavi, S. / ...Authors: Harrison, B.A. / Dowling, J.E. / Bursavich, M.G. / Troast, D.M. / Chong, K.M. / Hahn, K.N. / Zhong, C. / Mulvihill, K.M. / Nguyen, H. / Monroy, M.F. / Qiao, Q. / Sosa, B. / Mostafavi, S. / Smukste, I. / Lee, D. / Cappellucci, L. / Konopka, E.H. / Nowakowski, P. / Stawski, L. / Senices, M. / Nguyen, M.H. / Kapoor, P.S. / Luus, L. / Sullivan, A. / Bortolato, A. / Svensson, M. / Hickey, E.R. / Konze, K.D. / Day, T. / Kim, B. / Negri, A. / Gerasyuto, A.I. / Moy, T.I. / Lu, M. / Ray, A.S. / Wang, L. / Cui, D. / Lin, F.Y. / Lippa, B. / Rogers, B.N.
History
DepositionAug 4, 2024Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 13, 2024Provider: repository / Type: Initial release
Revision 1.1Nov 27, 2024Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Integrin alpha-V heavy chain
B: Integrin beta-6
C: 17E6 Fab light chain
D: 17E6 Fab heavy chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)171,23228
Polymers166,1034
Non-polymers5,12824
Water1,02757
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)96.494, 132.501, 168.366
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Symmetry operation#1: x,y,z
#2: x+1/2,-y+1/2,-z
#3: -x,y+1/2,-z+1/2
#4: -x+1/2,-y,z+1/2

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Components

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Protein , 2 types, 2 molecules AB

#1: Protein Integrin alpha-V heavy chain


Mass: 66456.484 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ITGAV, MSK8, VNRA, VTNR / Production host: Homo sapiens (human) / References: UniProt: P06756
#2: Protein Integrin beta-6


Mass: 52714.875 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ITGB6 / Production host: Homo sapiens (human) / References: UniProt: P18564

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Antibody , 2 types, 2 molecules CD

#3: Antibody 17E6 Fab light chain


Mass: 23722.037 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Production host: Homo sapiens (human)
#4: Antibody 17E6 Fab heavy chain


Mass: 23209.912 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Production host: Homo sapiens (human)

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Sugars , 4 types, 6 molecules

#5: Polysaccharide beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 586.542 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}LINUCSPDB-CARE
#6: Polysaccharide alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-beta-D- ...alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]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: 1072.964 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3[DManpa1-6]DManpa1-6DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam 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_c6-d1_d3-e1_d6-f1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(6+1)][a-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}}LINUCSPDB-CARE
#7: 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-ROHGlycam 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
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}LINUCSPDB-CARE
#12: Sugar ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 6 types, 75 molecules

#8: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Ca
#9: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C3H8O3
#10: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg
#11: Chemical ChemComp-A1A6A / (2S)-phenyl{(3S)-3-[4-(5,6,7,8-tetrahydro-1,8-naphthyridin-2-yl)butoxy]pyrrolidin-1-yl}acetic acid


Mass: 409.521 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C24H31N3O3 / Feature type: SUBJECT OF INVESTIGATION
#13: Chemical ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H3O2
#14: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 57 / 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: 3.3 Å3/Da / Density % sol: 62.72 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop
Details: 13% PEG 3350, 100 mM HEPES pH 7.1, 200 mM ammonium citrate

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: NSLS-II / Beamline: 17-ID-1 / Wavelength: 0.920105 Å
DetectorType: DECTRIS EIGER X 9M / Detector: PIXEL / Date: May 28, 2022
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.920105 Å / Relative weight: 1
ReflectionResolution: 2.57→52.06 Å / Num. obs: 69516 / % possible obs: 99.88 % / Redundancy: 7.5 % / Biso Wilson estimate: 62.27 Å2 / CC1/2: 0.996 / Net I/σ(I): 8.36
Reflection shellResolution: 2.57→2.662 Å / Num. unique obs: 5073 / CC1/2: 0.369

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Processing

Software
NameVersionClassification
PHENIX1.17.1_3660refinement
DIALS3.13.0data reduction
Aimless0.7.9data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.57→52.06 Å / SU ML: 0.36 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 25.52 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2342 3422 4.93 %
Rwork0.2161 --
obs0.217 69369 99.81 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.57→52.06 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11434 0 332 57 11823
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00312022
X-RAY DIFFRACTIONf_angle_d0.6516287
X-RAY DIFFRACTIONf_dihedral_angle_d18.5694435
X-RAY DIFFRACTIONf_chiral_restr0.0471846
X-RAY DIFFRACTIONf_plane_restr0.0042094
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.57-2.610.35241350.35242663X-RAY DIFFRACTION97
2.61-2.640.39231430.34832695X-RAY DIFFRACTION100
2.64-2.690.38431380.32482731X-RAY DIFFRACTION100
2.69-2.730.32661400.32632716X-RAY DIFFRACTION100
2.73-2.780.30891390.30892729X-RAY DIFFRACTION100
2.78-2.830.32391570.30612708X-RAY DIFFRACTION100
2.83-2.880.32841270.29172721X-RAY DIFFRACTION100
2.88-2.940.29121420.29122734X-RAY DIFFRACTION100
2.94-30.32941350.3012722X-RAY DIFFRACTION100
3-3.070.29461440.28982711X-RAY DIFFRACTION100
3.07-3.150.26821570.26822732X-RAY DIFFRACTION100
3.15-3.240.28431250.26762745X-RAY DIFFRACTION100
3.24-3.330.26611410.2592731X-RAY DIFFRACTION100
3.33-3.440.26321320.24592743X-RAY DIFFRACTION100
3.44-3.560.2681530.24232754X-RAY DIFFRACTION100
3.56-3.70.26691430.22422727X-RAY DIFFRACTION100
3.7-3.870.24181420.20352751X-RAY DIFFRACTION100
3.87-4.080.21641570.18572732X-RAY DIFFRACTION100
4.08-4.330.20381460.17432774X-RAY DIFFRACTION100
4.33-4.670.15631390.15562772X-RAY DIFFRACTION100
4.67-5.140.17851480.15582794X-RAY DIFFRACTION100
5.14-5.880.18481410.18032794X-RAY DIFFRACTION100
5.88-7.40.22831410.2022844X-RAY DIFFRACTION100
7.4-52.060.20131570.18542924X-RAY DIFFRACTION99
Refinement TLS params.

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

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
16.27293.05490.00722.97010.17431.9414-0.14310.58240.7971-0.219-0.04550.3537-0.796-0.03980.16550.7790.1053-0.21080.48760.11560.732511.316-6.3423-30.6992
23.42481.07430.05583.09940.41292.8174-0.25280.35140.1646-0.3190.13610.1784-0.3028-0.30870.10630.43160.0425-0.08870.44350.0250.42055.3537-25.6875-37.1898
32.1280.31510.6871.1590.43341.9215-0.10770.2330.0827-0.0815-0.0619-0.1436-0.01730.37140.16850.39150.0202-0.04760.41370.08550.431323.8004-29.5572-29.9903
43.110.3229-3.12161.6304-0.97578.6576-0.274-0.6528-0.21190.2997-0.1514-0.1725-0.09851.17710.37120.4798-0.0879-0.16610.52070.09880.510631.6628-20.6727-12.6477
57.64891.159-2.78183.1811-0.35824.69520.0188-0.16890.64620.2135-0.1529-0.096-0.74670.31380.12440.6439-0.0668-0.18060.43060.10390.53325.0798-8.5465-17.5724
64.34941.03280.79271.2680.48940.7891-0.23710.0640.8627-0.10820.13790.0215-0.16650.19650.20840.745-0.0251-0.14580.41310.06610.815935.83345.1167-20.0838
74.62690.74212.6034.14942.44238.885-0.4223-0.18271.2372-0.17640.4263-0.0556-0.77270.00010.02970.7492-0.0185-0.11360.6171-0.03741.088548.193820.747-11.2039
83.72911.81894.45322.93150.58086.1691-0.4453-0.9860.7794-0.32180.2560.0867-0.4541-0.74330.30120.79880.0407-0.01530.839-0.12450.939147.874614.9942-8.9617
93.8432.9783-0.44846.6101-1.31852.25910.1228-0.41750.50790.9199-0.4536-0.9795-0.82880.13340.26280.94720.0644-0.28940.70230.00280.893339.6489-6.558424.9956
101.96730.50910.98291.10950.28022.06030.0664-0.452-0.16380.1441-0.06360.15960.319-0.5214-0.01190.38490.03960.08730.4470.04010.45686.072-39.08272.9842
111.7251-0.37690.39142.4378-1.33314.41840.0258-0.2681-0.04090.0803-0.03570.0789-0.0549-0.09350.01560.3095-0.0053-0.00320.38730.03110.403311.4209-34.8589-0.9701
126.44334.4286-2.33758.8788-2.34115.8733-0.16820.0784-0.4552-0.03580.3139-0.52640.0043-0.0812-0.15510.44630.0747-0.01770.6104-0.14230.456128.9474-27.180114.682
135.6794.39490.1586.74730.1012.1906-0.04560.12170.24-0.12510.016-0.0701-0.3167-0.15510.07120.57780.16030.03580.7245-0.02570.439228.4286-20.903617.9892
145.8573-1.4317-1.99316.678-2.49765.07140.4557-0.1001-0.04450.3470.0657-0.0778-0.71920.4992-0.53221.06020.0579-0.20040.9894-0.23441.266542.446719.360719.473
152.2283-0.6543-2.89880.74920.56628.0669-0.14690.7381-0.3075-0.4906-0.39140.44660.372-1.64020.54370.8276-0.0237-0.15340.8867-0.19550.7547-7.0112-45.772-63.1112
164.4646-1.436-0.24295.2671.26347.3904-0.04570.81320.1552-0.7271-0.29690.4061-0.4319-0.33690.36370.6150.081-0.14310.5714-0.03640.4461.1147-40.0921-61.1421
172.53-0.97460.97413.5511-0.29387.19030.2120.37890.2657-0.4267-0.58910.07320.18190.09830.31570.57720.0635-0.09270.6046-0.04110.60130.75-45.7758-61.4867
180.1126-0.8064-1.03893.49614.94066.9530.81990.5918-0.59-1.2277-0.40380.20830.5616-0.638-0.37331.18410.2439-0.26460.7845-0.08470.68391.3815-49.8572-81.8912
193.9743-4.0392-2.80677.39283.25552.12580.23970.8909-0.5335-0.3406-0.71580.518-0.1706-0.8030.39380.83620.0608-0.06550.9429-0.19990.717614.6899-72.0574-86.3811
204.5593-0.8188-0.25722.7281-2.58812.6833-0.29990.8384-0.88630.06330.12572.45890.3669-0.95980.31650.63070.0379-0.08811.0967-0.4551.52040.9828-71.4992-84.3997
216.7308-2.53590.40519.56582.85445.8245-0.49480.6483-0.60760.67730.57870.6322-0.60350.1387-0.1020.63750.0629-0.01780.8358-0.10310.588.7292-61.7479-80.5101
229.4202-7.10647.1987.4747-7.64657.7793-0.10290.2002-1.5323-0.18150.02571.84310.038-0.89360.23090.95870.1996-0.17891.1038-0.55331.41598.4794-81.9616-88.1701
234.3649-0.45063.78587.3623-2.23916.13481.50161.0375-1.5717-2.9496-1.45341.82410.372-0.61130.1221.27560.1446-0.3051.3109-0.56241.26884.7965-70.8784-94.3216
244.64651.5096-0.73092.0162-0.38735.68380.1758-0.1732-0.6987-0.3107-0.2707-0.92240.84950.81910.0710.67050.1952-0.08910.7005-0.02170.527218.7776-57.4935-54.2969
254.5734-0.6304-1.272.3980.83684.17720.18690.3632-0.5286-0.0927-0.1908-0.17240.95060.19160.02380.66580.1045-0.05940.4784-0.01980.421312.736-51.8792-50.2197
263.1875-0.8425.20196.72561.21619.7050.223-0.5068-0.93520.97350.21540.73031.3368-0.5569-0.31710.7498-0.02180.07890.5537-0.00320.67285.3154-55.7732-43.802
276.70620.8795-2.96488.9619-2.81514.9045-0.22580.1382-0.1714-0.2670.2389-0.23750.96390.3633-0.09630.82610.23-0.15340.5691-0.11950.518116.9775-55.7167-43.7706
282.502-3.1920.6446.0294-1.61233.18960.22040.0474-0.2804-0.6997-0.36720.51070.66070.01150.18780.6190.0135-0.05880.56-0.09710.51379.0906-52.7113-53.5418
294.6679-3.05-4.3897.27247.14667.57880.1830.2116-0.1430.4837-0.0374-0.77940.1376-0.6139-0.14750.96170.1348-0.12650.6739-0.02930.793519.198-70.9505-61.5189
306.5376-1.0937-0.46298.3381-2.88088.0316-0.04350.68750.0014-0.0272-0.1477-0.17960.36290.65290.10470.55960.1597-0.04060.705-0.05820.59821.612-67.4409-81.9171
315.53030.295-4.68332.0743-0.97536.6249-0.86040.0069-0.91170.0071-0.2704-1.030.5582-0.01530.9421.11740.0747-0.06140.7945-0.01660.888516.6036-63.6541-77.9675
325.9321-2.24053.16055.078-2.37232.23450.00711.0336-0.0107-0.19210.1487-0.5195-0.2335-0.4113-0.0650.82160.00580.01640.8036-0.14250.70919.3119-64.1916-84.4416
337.0185-1.60870.9237.35260.37697.20680.08090.87750.2098-0.3575-0.051-0.9982-0.46260.46010.09770.74490.07010.14190.77820.04060.906928.8421-67.1302-83.227
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 66 )
2X-RAY DIFFRACTION2chain 'A' and (resid 67 through 149 )
3X-RAY DIFFRACTION3chain 'A' and (resid 150 through 303 )
4X-RAY DIFFRACTION4chain 'A' and (resid 304 through 342 )
5X-RAY DIFFRACTION5chain 'A' and (resid 343 through 407 )
6X-RAY DIFFRACTION6chain 'A' and (resid 408 through 460 )
7X-RAY DIFFRACTION7chain 'A' and (resid 461 through 533 )
8X-RAY DIFFRACTION8chain 'A' and (resid 534 through 595 )
9X-RAY DIFFRACTION9chain 'B' and (resid 5 through 80 )
10X-RAY DIFFRACTION10chain 'B' and (resid 81 through 224 )
11X-RAY DIFFRACTION11chain 'B' and (resid 225 through 356 )
12X-RAY DIFFRACTION12chain 'B' and (resid 357 through 380 )
13X-RAY DIFFRACTION13chain 'B' and (resid 381 through 441 )
14X-RAY DIFFRACTION14chain 'B' and (resid 442 through 477 )
15X-RAY DIFFRACTION15chain 'C' and (resid 1 through 32 )
16X-RAY DIFFRACTION16chain 'C' and (resid 33 through 75 )
17X-RAY DIFFRACTION17chain 'C' and (resid 76 through 101 )
18X-RAY DIFFRACTION18chain 'C' and (resid 102 through 113 )
19X-RAY DIFFRACTION19chain 'C' and (resid 114 through 139 )
20X-RAY DIFFRACTION20chain 'C' and (resid 140 through 158 )
21X-RAY DIFFRACTION21chain 'C' and (resid 159 through 181 )
22X-RAY DIFFRACTION22chain 'C' and (resid 182 through 197 )
23X-RAY DIFFRACTION23chain 'C' and (resid 198 through 214 )
24X-RAY DIFFRACTION24chain 'D' and (resid 1 through 16 )
25X-RAY DIFFRACTION25chain 'D' and (resid 17 through 44 )
26X-RAY DIFFRACTION26chain 'D' and (resid 45 through 67 )
27X-RAY DIFFRACTION27chain 'D' and (resid 68 through 84 )
28X-RAY DIFFRACTION28chain 'D' and (resid 85 through 111 )
29X-RAY DIFFRACTION29chain 'D' and (resid 112 through 124 )
30X-RAY DIFFRACTION30chain 'D' and (resid 125 through 162 )
31X-RAY DIFFRACTION31chain 'D' and (resid 163 through 178 )
32X-RAY DIFFRACTION32chain 'D' and (resid 179 through 192 )
33X-RAY DIFFRACTION33chain 'D' and (resid 193 through 217 )

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