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

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Basic information

Entry
Database: PDB / ID: 9czf
TitleCrystal structure of integrin avb6 headpiece in complex with compound MORF-627
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 / alpha-D-mannopyranose / Integrin alpha-V / Integrin beta-6
Similarity search - Component
Biological speciesHomo sapiens (human)
Mus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.53 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 5, 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)171,37230
Polymers166,1034
Non-polymers5,26926
Water1,45981
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)95.840, 133.130, 169.550
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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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 , 5 types, 7 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)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 748.682 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3/a4-b1_b4-c1_c3-d1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}}}}LINUCSPDB-CARE
#9: Sugar ChemComp-MAN / alpha-D-mannopyranose / alpha-D-mannose / D-mannose / mannose


Type: D-saccharide, alpha linking / Mass: 180.156 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C6H12O6 / Feature type: SUBJECT OF INVESTIGATION
IdentifierTypeProgram
DManpaCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
a-D-mannopyranoseCOMMON NAMEGMML 1.0
a-D-ManpIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
ManSNFG CARBOHYDRATE SYMBOLGMML 1.0
#14: Sugar ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
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 , 7 types, 100 molecules

#8: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Formula: Ca
#10: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


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


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg
#12: Chemical ChemComp-A1A6I / (2S)-{5-fluoro-2-[(6S)-5-oxaspiro[2.5]octan-6-yl]phenyl}{(3R)-3-[4-(5,6,7,8-tetrahydro-1,8-naphthyridin-2-yl)butoxy]pyrrolidin-1-yl}acetic acid / MORF-627


Mass: 537.665 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C31H40FN3O4 / 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
#15: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#16: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 81 / 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: 3.32 Å3/Da / Density % sol: 62.93 %
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: ALBA / Beamline: XALOC / Wavelength: 0.9792 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: May 1, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9792 Å / Relative weight: 1
ReflectionResolution: 2.53→54.67 Å / Num. obs: 73086 / % possible obs: 99.91 % / Redundancy: 7.4 % / CC1/2: 0.998 / Net I/σ(I): 12.56
Reflection shellResolution: 2.53→2.6 Å / Num. unique obs: 5348 / CC1/2: 0.314

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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: 2.53→54.67 Å / SU ML: 0.38 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 26.5 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2452 3641 4.99 %0.2366
Rwork0.2129 ---
obs0.2145 72983 99.92 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.53→54.67 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11434 0 339 81 11854
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00212030
X-RAY DIFFRACTIONf_angle_d0.58916302
X-RAY DIFFRACTIONf_dihedral_angle_d17.1034444
X-RAY DIFFRACTIONf_chiral_restr0.0451846
X-RAY DIFFRACTIONf_plane_restr0.0032093
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.53-2.560.33561360.33562626X-RAY DIFFRACTION100
2.56-2.60.32781240.32782648X-RAY DIFFRACTION100
2.6-2.640.35461440.32872587X-RAY DIFFRACTION100
2.64-2.670.38891480.33112623X-RAY DIFFRACTION100
2.67-2.720.35691420.33982646X-RAY DIFFRACTION100
2.72-2.760.35221470.31922610X-RAY DIFFRACTION100
2.76-2.810.37311420.31472654X-RAY DIFFRACTION100
2.81-2.860.30571210.30572639X-RAY DIFFRACTION100
2.86-2.910.26481400.26482671X-RAY DIFFRACTION100
2.91-2.970.28311160.28122654X-RAY DIFFRACTION100
2.97-3.040.32481550.27822655X-RAY DIFFRACTION100
3.04-3.110.27811300.27072646X-RAY DIFFRACTION100
3.11-3.190.27721290.2682661X-RAY DIFFRACTION100
3.19-3.270.28811510.26992631X-RAY DIFFRACTION100
3.27-3.370.25951340.25952661X-RAY DIFFRACTION100
3.37-3.480.28431350.24622671X-RAY DIFFRACTION100
3.48-3.60.2641580.22952632X-RAY DIFFRACTION100
3.6-3.750.26971570.22112652X-RAY DIFFRACTION100
3.75-3.920.21891270.19262690X-RAY DIFFRACTION100
3.92-4.120.22761380.18192669X-RAY DIFFRACTION100
4.12-4.380.19381460.16172675X-RAY DIFFRACTION100
4.38-4.720.20071340.1482712X-RAY DIFFRACTION100
4.72-5.20.17991630.14782660X-RAY DIFFRACTION100
5.2-5.950.20971190.17642754X-RAY DIFFRACTION100
5.95-7.490.26341580.20272754X-RAY DIFFRACTION100
7.49-54.670.21371470.1882861X-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)
12.36010.64611.66410.96520.36442.59560.0873-0.47660.0220.2507-0.12230.07190.103-0.35420.05480.43550.07970.1170.5253-0.00770.503212.8838-33.62339.7052
21.66880.02450.10612.1825-0.64443.7-0.0169-0.22080.05580.19310.00730.206-0.0209-0.20340.01040.3920.0220.00720.48060.00590.44988.3319-35.6155-2.2883
36.08617.04852.07238.81532.17371.20470.1641-0.2484-0.41080.01860.0252-0.62420.07070.0093-0.21060.49790.12750.1190.68690.01910.539227.0856-31.256915.2002
43.21352.6233-0.33442.36580.34021.74660.0853-0.21870.87160.0252-0.3640.6742-0.3632-0.11290.21050.7810.15560.03340.8021-0.04480.842427.1927-8.207320.3658
54.2564-1.1214-1.27855.4503-2.44991.9480.4665-0.00870.20430.4283-0.151-0.2925-0.2977-0.1467-0.33721.23260.026-0.19720.8947-0.16061.357343.098619.790718.6992
66.02361.9343-4.57264.563-2.48496.95090.45540.83480.1325-0.7378-0.23320.92880.1658-1.2761-0.20330.8090.074-0.28090.7558-0.10690.758-4.8477-47.0766-67.9354
72.2429-1.2766-0.77943.61780.77188.7222-0.05130.4086-0.0089-0.3933-0.36160.276-0.2323-0.6220.38630.59220.0567-0.1640.6036-0.05440.5845-0.5326-42.6547-60.6806
81.8006-2.7534-2.91234.21854.50354.79761.01551.018-0.4274-1.5312-1.59340.6963-1.2406-1.54220.53381.19010.3194-0.2160.7812-0.1020.58151.6818-49.7472-83.1741
96.7063-4.31980.44223.315-1.5033.29490.29820.6214-0.7855-0.7632-0.47221.07890.3914-0.77530.19850.79060.0796-0.12930.8326-0.18880.78818.2284-71.7446-85.5013
106.0705-4.243-0.09623.05570.7153.34650.28330.7566-1.1297-1.2246-0.48882.0080.1731-0.1590.18930.72380.1077-0.16520.8332-0.1190.72698.4524-70.3385-83.8887
112.40910.92912.73396.1433-0.49058.55960.97691.2751-1.656-2.1583-1.28381.67430.257-1.00980.26630.90850.0918-0.25661.1022-0.37551.01924.5531-70.6688-94.5382
122.7648-1.2566-0.93657.82864.74515.0112-0.1926-0.1145-0.22780.15940.3603-0.3080.65690.6506-0.20080.58950.1618-0.09110.53750.01340.435617.9117-52.8104-50.2034
135.25570.19762.26052.5639-2.14568.49220.1776-0.0387-0.57510.32560.05410.38991.3601-0.2712-0.37060.90470.0533-0.020.537-0.04460.64247.2363-56.1499-47.0841
141.844-1.4235-1.5375.68814.16584.348-0.0255-0.0986-0.18420.4054-0.0447-0.17690.84310.24880.07660.66640.0797-0.09070.53230.02250.476513.6739-57.57-53.605
157.5227-1.05340.09048.0091-3.75694.38180.0411.12350.2856-0.2544-0.4934-0.5736-0.02940.68070.38950.5380.0932-0.01180.68240.00330.563221.7397-66.1424-82.7286
169.2942-2.9798-0.16257.3771-0.20035.8760.0460.83470.0387-0.4806-0.3557-0.5281-0.10940.23790.33710.61440.083-0.00030.4589-0.01110.586822.9119-66.3327-82.1403
171.74370.08530.53461.30610.27832.1485-0.09950.23260.278-0.1864-0.0710.0619-0.28620.06620.16660.45670.0019-0.08170.48230.07430.459214.3118-24.064-33.3315
181.3953-0.0089-0.07291.79830.49020.3826-0.07260.00320.33420.03110.0167-0.1759-0.26250.17370.05090.5464-0.0802-0.16460.54220.11870.55930.4353-9.1213-17.6052
194.49840.65411.82193.68990.49314.0945-0.6227-0.30121.3271-0.27720.38870.1337-0.8955-0.28050.24740.80750.0086-0.11040.7067-0.08681.167947.478718.0704-9.9313
208.44846.95860.25049.47774.42295.2142-0.0269-0.2123-1.32210.4853-0.1066-2.4203-0.07270.87920.15330.95150.0216-0.18680.75680.21191.458747.50440.809521.1945
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'B' and (resid 51 through 192 )
2X-RAY DIFFRACTION2chain 'B' and (resid 193 through 342 )
3X-RAY DIFFRACTION3chain 'B' and (resid 343 through 413 )
4X-RAY DIFFRACTION4chain 'B' and (resid 414 through 447 )
5X-RAY DIFFRACTION5chain 'B' and (resid 448 through 477 )
6X-RAY DIFFRACTION6chain 'C' and (resid 1 through 18 )
7X-RAY DIFFRACTION7chain 'C' and (resid 19 through 102 )
8X-RAY DIFFRACTION8chain 'C' and (resid 103 through 113 )
9X-RAY DIFFRACTION9chain 'C' and (resid 114 through 158 )
10X-RAY DIFFRACTION10chain 'C' and (resid 159 through 197 )
11X-RAY DIFFRACTION11chain 'C' and (resid 198 through 214 )
12X-RAY DIFFRACTION12chain 'D' and (resid 1 through 33 )
13X-RAY DIFFRACTION13chain 'D' and (resid 34 through 73 )
14X-RAY DIFFRACTION14chain 'D' and (resid 74 through 124 )
15X-RAY DIFFRACTION15chain 'D' and (resid 125 through 167 )
16X-RAY DIFFRACTION16chain 'D' and (resid 168 through 217 )
17X-RAY DIFFRACTION17chain 'A' and (resid 1 through 275 )
18X-RAY DIFFRACTION18chain 'A' and (resid 276 through 460 )
19X-RAY DIFFRACTION19chain 'A' and (resid 461 through 595 )
20X-RAY DIFFRACTION20chain 'B' and (resid 5 through 50 )

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