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- PDB-4cl7: Crystal structure of VEGFR-1 domain 2 in presence of Cobalt -

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Basic information

Entry
Database: PDB / ID: 4cl7
TitleCrystal structure of VEGFR-1 domain 2 in presence of Cobalt
ComponentsVASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 1VEGF receptor
KeywordsRECEPTOR / METAL-BINDING
Function / homology
Function and homology information


vascular endothelial growth factor receptor-1 signaling pathway / placental growth factor receptor activity / hyaloid vascular plexus regression / Neurophilin interactions with VEGF and VEGFR / VEGF binds to VEGFR leading to receptor dimerization / vascular endothelial growth factor receptor activity / embryonic morphogenesis / negative regulation of vascular endothelial cell proliferation / blood vessel morphogenesis / growth factor binding ...vascular endothelial growth factor receptor-1 signaling pathway / placental growth factor receptor activity / hyaloid vascular plexus regression / Neurophilin interactions with VEGF and VEGFR / VEGF binds to VEGFR leading to receptor dimerization / vascular endothelial growth factor receptor activity / embryonic morphogenesis / negative regulation of vascular endothelial cell proliferation / blood vessel morphogenesis / growth factor binding / monocyte chemotaxis / cellular response to vascular endothelial growth factor stimulus / vascular endothelial growth factor receptor signaling pathway / positive regulation of phospholipase C activity / transmembrane receptor protein tyrosine kinase activity / positive regulation of MAP kinase activity / receptor protein-tyrosine kinase / peptidyl-tyrosine phosphorylation / cell surface receptor protein tyrosine kinase signaling pathway / positive regulation of angiogenesis / cell migration / actin cytoskeleton / angiogenesis / positive regulation of MAPK cascade / protein autophosphorylation / cell differentiation / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / receptor complex / endosome / positive regulation of cell migration / focal adhesion / positive regulation of cell population proliferation / extracellular space / ATP binding / plasma membrane
Similarity search - Function
Vascular endothelial growth factor receptor 1 (VEGFR1) / VEGFR-2, transmembrane domain / VEGFR-2 Transmembrane domain / Vascular endothelial growth factor receptor 1-like, Ig-like domain / Tyrosine-protein kinase, receptor class III, conserved site / Receptor tyrosine kinase class III signature. / Immunoglobulin / Immunoglobulin domain / Immunoglobulin domain / Immunoglobulin I-set ...Vascular endothelial growth factor receptor 1 (VEGFR1) / VEGFR-2, transmembrane domain / VEGFR-2 Transmembrane domain / Vascular endothelial growth factor receptor 1-like, Ig-like domain / Tyrosine-protein kinase, receptor class III, conserved site / Receptor tyrosine kinase class III signature. / Immunoglobulin / Immunoglobulin domain / Immunoglobulin domain / Immunoglobulin I-set / Immunoglobulin I-set domain / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Immunoglobulin V-Type / Immunoglobulin V-set domain / Tyrosine-protein kinase, catalytic domain / Tyrosine kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Immunoglobulin subtype / Immunoglobulin / Tyrosine-protein kinase, active site / Protein tyrosine and serine/threonine kinase / Serine-threonine/tyrosine-protein kinase, catalytic domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / 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
: / Vascular endothelial growth factor receptor 1
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å
AuthorsGaucher, J.-F. / Reille-Seroussi, M. / Gagey-Eilstein, N. / Broussy, S. / Coric, P. / Seijo, B. / Lascombe, M.-B. / Gautier, B. / Liu, W.-Q. / Huguenot, F. ...Gaucher, J.-F. / Reille-Seroussi, M. / Gagey-Eilstein, N. / Broussy, S. / Coric, P. / Seijo, B. / Lascombe, M.-B. / Gautier, B. / Liu, W.-Q. / Huguenot, F. / Inguimbert, N. / Bouaziz, S. / Vidal, M. / Broutin, I.
CitationJournal: Plos One / Year: 2016
Title: Biophysical Studies of the Induced Dimerization of Human Vegf R Receptor 1 Binding Domain by Divalent Metals Competing with Vegf-A
Authors: Gaucher, J.-F. / Reille-Seroussi, M. / Gagey-Eilstein, N. / Broussy, S. / Coric, P. / Seijo, B. / Lascombe, M.-B. / Gautier, B. / Liu, W.-Q. / Huguenot, F. / Inguimbert, N. / Bouaziz, S. / ...Authors: Gaucher, J.-F. / Reille-Seroussi, M. / Gagey-Eilstein, N. / Broussy, S. / Coric, P. / Seijo, B. / Lascombe, M.-B. / Gautier, B. / Liu, W.-Q. / Huguenot, F. / Inguimbert, N. / Bouaziz, S. / Vidal, M. / Broutin, I.
History
DepositionJan 13, 2014Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 28, 2015Provider: repository / Type: Initial release
Revision 1.1Feb 1, 2017Group: Database references
Revision 1.2May 8, 2019Group: Data collection / Experimental preparation / Other
Category: database_PDB_rev / database_PDB_rev_record ...database_PDB_rev / database_PDB_rev_record / exptl_crystal_grow / pdbx_database_proc / pdbx_database_status
Item: _exptl_crystal_grow.method / _pdbx_database_status.recvd_author_approval
Revision 1.3Dec 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 1
B: VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 1
C: VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 1
D: VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,82714
Polymers43,2224
Non-polymers60510
Water5,062281
1
A: VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 1
C: VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)21,9748
Polymers21,6112
Non-polymers3636
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1610 Å2
ΔGint-28.2 kcal/mol
Surface area10910 Å2
MethodPISA
2
B: VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 1
D: VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)21,8536
Polymers21,6112
Non-polymers2424
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1550 Å2
ΔGint-22.1 kcal/mol
Surface area11160 Å2
MethodPISA
Unit cell
Length a, b, c (Å)27.746, 41.711, 94.694
Angle α, β, γ (deg.)87.05, 82.25, 73.03
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(0.99983, -0.01621, 0.00862), (-0.01604, -0.99969, -0.0191), (0.00893, 0.01896, -0.99978)0.07169, -58.84029, 60.80122
2given(-0.99996, -0.00618, -0.00677), (-0.00334, -0.44264, 0.89669), (-0.00854, 0.89668, 0.4426)19.89528, -88.1649, 15.62318
3given(-0.99943, 0.01626, -0.02954), (0.0337, 0.44868, -0.89306), (-0.00127, -0.89355, -0.44897)20.52068, 28.48222, 44.82311

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Components

#1: Protein
VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 1 / VEGF receptor / VEGFR-1 / FMS-LIKE TYROSINE KINASE 1 / FLT-1 / TYROSINE-PROTEI N KINASE FRT / TYROSINE-PROTEIN ...VEGFR-1 / FMS-LIKE TYROSINE KINASE 1 / FLT-1 / TYROSINE-PROTEI N KINASE FRT / TYROSINE-PROTEIN KINASE RECEPTOR FLT / FLT / VASCULAR PERMEABILITY FACTOR RECEPTOR


Mass: 10805.559 Da / Num. of mol.: 4 / Fragment: DOMAIN-2, RESIDUES 132-225
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PET22 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): ROSETTA-GAMI PLYSS
References: UniProt: P17948, receptor protein-tyrosine kinase
#2: Chemical
ChemComp-CO / COBALT (II) ION


Mass: 58.933 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Co
#3: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C2H6O2
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 281 / Source method: isolated from a natural source / Formula: H2O

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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: 2.36 Å3/Da / Density % sol: 47.9 % / Description: NONE
Crystal growMethod: vapor diffusion, hanging drop / pH: 7
Details: CRYSTAL WERE OBTAINED BY HANGING DROP METHOD FROM 1MM VEGFR1-D2, 5MM HEPES/NAOH PH7.0, 10MM COCL2, 100 MM BIS-TRIS/HCL PH6.5 15%(W/V) PEG3350.

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-2 / Wavelength: 0.8726
DetectorType: ADSC CCD / Detector: CCD / Date: Nov 6, 2009 / Details: KIRKPATRICK-BAEZ MIRRORSWITH PT COATING
RadiationMonochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.8726 Å / Relative weight: 1
ReflectionResolution: 2→19.47 Å / Num. obs: 26362 / % possible obs: 97.1 % / Observed criterion σ(I): 2 / Redundancy: 1.8 % / Biso Wilson estimate: 17.48 Å2 / Rmerge(I) obs: 0.07 / Net I/σ(I): 10.74
Reflection shellResolution: 2→2.07 Å / Redundancy: 1.8 % / Rmerge(I) obs: 0.33 / Mean I/σ(I) obs: 3.01 / % possible all: 96.6

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
XDSdata reduction
SCALEPACKdata scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1FLT

1flt


Resolution: 2→19.469 Å / SU ML: 0.26 / σ(F): 1.97 / Phase error: 22.75 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2332 1294 4.9 %
Rwork0.1675 --
obs0.1707 26358 97.05 %
Solvent computationShrinkage radii: 0.83 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 61.072 Å2 / ksol: 0.386 e/Å3
Displacement parametersBiso mean: 17.58 Å2
Baniso -1Baniso -2Baniso -3
1--0.2689 Å20.3828 Å2-0.1891 Å2
2--0.2025 Å2-0.0657 Å2
3---0.0664 Å2
Refinement stepCycle: LAST / Resolution: 2→19.469 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3020 0 25 281 3326
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0063107
X-RAY DIFFRACTIONf_angle_d0.9834202
X-RAY DIFFRACTIONf_dihedral_angle_d12.8261181
X-RAY DIFFRACTIONf_chiral_restr0.063488
X-RAY DIFFRACTIONf_plane_restr0.005524
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2-2.080.27161690.19632717X-RAY DIFFRACTION97
2.08-2.17450.26221390.18462826X-RAY DIFFRACTION97
2.1745-2.2890.24841370.1852807X-RAY DIFFRACTION98
2.289-2.43210.25911490.1772778X-RAY DIFFRACTION98
2.4321-2.61950.31731380.18252831X-RAY DIFFRACTION98
2.6195-2.88240.20951270.16552814X-RAY DIFFRACTION98
2.8824-3.29770.22131530.15052810X-RAY DIFFRACTION98
3.2977-4.14820.21281500.14862764X-RAY DIFFRACTION97
4.1482-19.470.19961320.16562717X-RAY DIFFRACTION94
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)
10.93220.01770.71420.2966-0.67562.25210.05470.2479-0.41530.03430.29010.16630.0416-0.4033-0.2410.0515-0.04320.02060.1789-0.00430.08613.7971-30.22167.1569
20.5014-0.64230.10361.3064-0.55140.41070.1290.524-0.80330.1236-0.07840.57560.2145-0.461-0.02450.1168-0.2003-0.00510.2121-0.09290.38845.7055-33.282656.6542
30.60320.49350.29330.4637-0.06030.4862-0.0783-0.1153-0.0586-0.2026-0.0744-0.04470.0328-0.04220.08590.0734-0.01430.00720.0543-0.01480.037515.3463-20.48256.3342
40.2491-0.0514-0.30281.54170.72691.1382-0.01930.038-0.0860.45440.3584-0.210.3141-0.10310.1037-0.0033-0.00440.0980.10170.0062-0.00728.3879-25.888975.256
52.1578-1.5185-1.34663.8392-1.11944.08340.1608-0.52850.0681-1.03220.00320.0021.04250.78770.2573-0.02590.17860.0419-0.05010.05550.051318.6312-33.684463.2935
60.8479-1.07011.08621.3084-1.43711.84860.14850.4505-0.01720.0652-0.5327-0.5118-0.12460.73050.12470.02140.00180.0220.15820.00850.110323.5907-24.645466.0864
73.20161.366-0.30770.746-0.44630.7002-0.2078-0.19380.7090.25190.15280.287-0.5127-0.1569-0.11650.0790.07440.02370.0681-0.01460.089511.3444-19.854470.958
81.3063-0.573-0.01880.92720.92071.3764-0.2830.00060.15430.11370.3250.0543-0.13870.685-0.04360.0627-0.0439-0.04230.1389-0.01650.028918.5875-19.985862.9761
90.6845-0.2421-0.03770.70610.28230.67740.09480.06320.17690.024300.03770.17810.0918-0.06510.08950.01080.02330.07790.00990.105419.4507-28.81357.8307
100.7827-0.06870.04811.7458-0.78671.4855-0.1284-0.2418-0.2083-0.25250.3555-0.03040.3111-0.12260.07740.14930.01940.04630.10510.05380.10419.0235-37.874275.2088
110.83431.1197-1.42393.0879-2.05042.8861-0.0313-0.31430.0758-0.3792-0.0919-0.17560.42480.5601-0.090.0596-0.0808-0.01880.1159-0.01870.094912.4281-28.526554.8881
121.63040.3653-1.33390.39140.38292.55080.21010.29180.1995-0.08450.42890.0438-0.3713-0.05-0.1246-0.0760.0237-0.11920.17280.05030.02824.9493-29.9943-6.837
131.8798-1.14950.27491.9155-0.65071.1660.4787-0.22080.3974-0.2749-0.15080.2992-0.4787-0.2751-0.13110.1920.07330.05330.30930.02710.15556.7175-26.69373.0938
140.7494-0.52910.20161.1017-0.54020.5128-0.3608-0.0432-0.00410.70240.18980.0394-0.4071-0.06190.10330.19610.04970.00370.13680.02440.070816.0899-39.52254.4107
150.1659-0.2373-0.05450.3688-0.04590.1568-0.17190.358-0.1187-0.13680.10330.05790.01860.01550.05150.0943-0.0394-0.02580.14560.00640.03779.4601-34.5171-14.7713
160.7030.66990.22761.6270.17960.93880.039-0.04570.73540.2204-0.22440.5922-0.50960.111-0.02530.1081-0.10950.01960.2084-0.02390.084419.7303-26.6919-2.9678
171.1714-0.2633-0.72470.6292-0.12660.57030.1909-0.53710.26660.2162-0.1653-0.51320.11420.4558-0.01770.110.0359-0.04580.2335-0.03120.169524.5548-35.6982-5.5973
185.2385-2.65870.66721.4139-0.76773.1728-0.00840.2897-0.96940.2121-0.11210.2739-0.01840.71690.08320.06540.00650.04750.14810.00050.086912.3617-40.5284-10.3294
193.8270.47451.73611.21540.79381.1586-0.5788-0.11-0.0006-0.27860.2833-0.08170.21930.47260.19760.06110.11670.05360.18720.02010.034419.5468-40.3742-2.2719
201.3753-0.94920.53491.1175-0.26541.60340.15420.21790.07820.1737-0.1649-0.4112-0.29110.42870.19950.0784-0.0514-0.10360.12220.01680.113620.4316-31.36332.446
212.47471.52250.65721.55880.63793.0657-0.4698-0.0764-0.1058-0.13150.1282-0.3195-0.5687-0.23210.1110.07920.0171-0.02040.1506-0.01210.048110.2607-22.5649-14.7962
220.5181-1.00080.88112.894-3.35655.95590.19090.0329-0.14390.42330.29580.4114-0.48720.4031-0.28390.14840.0678-0.01150.1322-0.01910.090213.2878-31.70645.3076
230.24520.49-0.04163.0551-0.39330.17890.13270.08590.0564-0.2019-0.1119-1.1453-0.0240.013-0.00060.06280.02730.06350.05960.00960.176914.1963-44.711841.6534
241.7109-0.77830.7641.8476-0.35534.2840.11690.0580.43120.0681-0.2124-0.73010.61440.50920.03440.1210.0584-0.06270.1198-0.02010.152512.452-37.644449.289
250.432-0.6496-0.1211.26680.47260.20460.07980.0273-0.1622-0.0727-0.11380.2150.0048-0.08320.00970.07160.01820.02910.07680.0270.08873.5031-30.520537.9451
261.3667-0.93830.23790.6819-0.03951.2637-0.33830.4763-0.0742-0.2779-0.31050.13960.1680.3211-0.22670.11910.0250.0838-0.0266-0.08290.06149.8083-50.043634.5243
270.61140.2118-0.13721.0178-0.70130.62670.245-0.3003-0.24020.9624-0.46980.3588-0.27140.220.07220.2745-0.10180.07650.0739-0.0360.17-0.6259-42.659546.2137
280.65010.5953-0.23590.8179-0.56030.43480.0989-0.38130.22960.01290.11330.2866-0.04560.0106-0.16090.05460.0149-0.00710.1666-0.01440.1428-5.6103-41.106637.365
294.4028-1.39331.70291.1545-0.15221.28150.31671.374-0.3043-0.50080.0729-0.0161-0.44850.575-0.20620.1335-0.01490.08570.2133-0.06790.1756.4548-43.296530.418
300.676-0.37180.71621.3966-0.85290.9545-0.0513-0.1459-0.0633-0.23540.06610.30450.0674-0.0723-0.01970.07750.0106-0.01050.0894-0.00040.086-0.1743-36.129534.3308
310.1331-0.241-0.06970.1793-0.0970.43830.0590.08750.0251-0.1102-0.0746-0.06070.11070.0811-0.0330.0661-0.0242-0.01290.0173-0.0180.1015-1.1099-35.159544.5013
320.0344-0.0351-0.04330.7194-0.29261.0447-0.10890.084-0.0827-0.4586-0.2154-0.42110.22430.12280.25420.21520.01020.08040.00880.00170.10169.3693-55.04144.9746
330.1918-0.0488-0.18831.7662-0.50760.74660.11480.0544-0.02690.2787-0.2833-0.1758-0.0665-0.02340.11510.0663-0.0086-0.03040.06840.00460.07046.0783-33.177245.517
341.34031.15730.23931.02280.19520.8972-0.15930.11540.1235-0.25320.1546-0.5213-0.44050.4512-0.01250.0912-0.0332-0.01280.09120.00980.232615.7145-14.619618.1041
350.3482-0.00640.3540.00890.0330.5229-0.03740.65710.1224-0.50710.2633-0.2433-0.79871.0616-0.22980.344-0.18960.10460.4024-0.01720.177113.7989-22.064610.7167
360.6464-0.3268-0.06270.26530.1170.7229-0.16460.0543-0.034-0.05510.0341-0.18730.3076-0.11540.11220.137-0.0420.01380.02710.00250.08384.6791-28.55122.1208
371.07630.7926-0.77450.9916-0.43960.71120.0534-0.0037-0.1346-0.5386-0.1777-0.2647-0.36790.0404-0.00230.19710.0149-0.08730.0368-0.06730.142411.0304-9.491425.8369
380.916-0.4195-0.35631.2374-0.4620.5986-0.16180.41380.4339-0.37850.06860.1568-0.0169-0.1659-0.05240.1437-0.0028-0.06690.17670.03380.08371.0121-16.375513.2626
390.52970.17590.4210.7183-0.12720.91220.21440.3609-0.2838-0.13790.09310.37930.4335-0.0621-0.25960.1037-0.0051-0.01860.1538-0.03220.1385-4.5241-17.979322.343
403.1229-0.2462-2.66852.5029-0.28533.1042-0.2695-0.6049-0.26890.8511-0.12520.22490.1310.55450.08790.11470.0247-0.09670.002-0.02130.07378.5326-15.734128.9341
412.6922-1.092-1.61682.33381.3975.7237-0.4854-0.1791-0.2364-0.0392-0.29740.01780.4876-0.36380.1920.16160.01840.03860.0943-0.01540.0331.2026-22.846825.5601
422.79111.7187-1.45371.7355-1.18961.3278-0.06850.48180.5737-0.14270.32070.6148-0.1445-0.46420.07960.1057-0.0387-0.09830.12470.01280.07560.1913-23.514215.4174
430.26840.3444-0.01380.53110.26470.6976-0.35570.50280.35530.2712-0.4906-0.4213-0.60880.91670.60060.3316-0.1563-0.16240.03750.18990.397611.316-4.44414.922
441.49961.1597-0.16060.9822-0.14450.3482-0.0079-0.39990.30820.0986-0.22030.48550.17480.05750.0320.1673-0.01940.10550.07060.0724-0.02267.4304-26.143414.4138
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(CHAIN A AND RESID 133:139)
2X-RAY DIFFRACTION2(CHAIN A AND RESID 140:145)
3X-RAY DIFFRACTION3(CHAIN A AND RESID 146:158)
4X-RAY DIFFRACTION4(CHAIN A AND RESID 159:166)
5X-RAY DIFFRACTION5(CHAIN A AND RESID 167:173)
6X-RAY DIFFRACTION6(CHAIN A AND RESID 174:185)
7X-RAY DIFFRACTION7(CHAIN A AND RESID 186:190)
8X-RAY DIFFRACTION8(CHAIN A AND RESID 191:196)
9X-RAY DIFFRACTION9(CHAIN A AND RESID 197:208)
10X-RAY DIFFRACTION10(CHAIN A AND RESID 209:216)
11X-RAY DIFFRACTION11(CHAIN A AND RESID 217:225)
12X-RAY DIFFRACTION12(CHAIN B AND RESID 133:139)
13X-RAY DIFFRACTION13(CHAIN B AND RESID 140:145)
14X-RAY DIFFRACTION14(CHAIN B AND RESID 146:158)
15X-RAY DIFFRACTION15(CHAIN B AND RESID 159:166)
16X-RAY DIFFRACTION16(CHAIN B AND RESID 167:173)
17X-RAY DIFFRACTION17(CHAIN B AND RESID 174:185)
18X-RAY DIFFRACTION18(CHAIN B AND RESID 186:190)
19X-RAY DIFFRACTION19(CHAIN B AND RESID 191:196)
20X-RAY DIFFRACTION20(CHAIN B AND RESID 197:208)
21X-RAY DIFFRACTION21(CHAIN B AND RESID 209:216)
22X-RAY DIFFRACTION22(CHAIN B AND RESID 217:225)
23X-RAY DIFFRACTION23(CHAIN C AND RESID 133:139)
24X-RAY DIFFRACTION24(CHAIN C AND RESID 140:145)
25X-RAY DIFFRACTION25(CHAIN C AND RESID 146:158)
26X-RAY DIFFRACTION26(CHAIN C AND RESID 159:166)
27X-RAY DIFFRACTION27(CHAIN C AND RESID 167:173)
28X-RAY DIFFRACTION28(CHAIN C AND RESID 174:185)
29X-RAY DIFFRACTION29(CHAIN C AND RESID 186:190)
30X-RAY DIFFRACTION30(CHAIN C AND RESID 191:196)
31X-RAY DIFFRACTION31(CHAIN C AND RESID 197:208)
32X-RAY DIFFRACTION32(CHAIN C AND RESID 209:216)
33X-RAY DIFFRACTION33(CHAIN C AND RESID 217:225)
34X-RAY DIFFRACTION34(CHAIN D AND RESID 133:139)
35X-RAY DIFFRACTION35(CHAIN D AND RESID 140:145)
36X-RAY DIFFRACTION36(CHAIN D AND RESID 146:158)
37X-RAY DIFFRACTION37(CHAIN D AND RESID 159:166)
38X-RAY DIFFRACTION38(CHAIN D AND RESID 167:173)
39X-RAY DIFFRACTION39(CHAIN D AND RESID 174:185)
40X-RAY DIFFRACTION40(CHAIN D AND RESID 186:190)
41X-RAY DIFFRACTION41(CHAIN D AND RESID 191:196)
42X-RAY DIFFRACTION42(CHAIN D AND RESID 197:208)
43X-RAY DIFFRACTION43(CHAIN D AND RESID 209:216)
44X-RAY DIFFRACTION44(CHAIN D AND RESID 217:225)

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