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- PDB-5nhu: HUMAN ALPHA THROMBIN COMPLEXED WITH ANOPHELES GAMBIAE cE5 ANTICOA... -

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Basic information

Entry
Database: PDB / ID: 5nhu
TitleHUMAN ALPHA THROMBIN COMPLEXED WITH ANOPHELES GAMBIAE cE5 ANTICOAGULANT
Components
  • (Prothrombin) x 2
  • AGAP008004-PA
KeywordsHYDROLASE / blood clotting / anticoagulant / thrombin / inhibitor
Function / homology
Function and homology information


molecular function inhibitor activity / positive regulation of lipid kinase activity / cytolysis by host of symbiont cells / positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway / thrombospondin receptor activity / Defective factor XII causes hereditary angioedema / thrombin / regulation of blood coagulation / neutrophil-mediated killing of gram-negative bacterium / ligand-gated ion channel signaling pathway ...molecular function inhibitor activity / positive regulation of lipid kinase activity / cytolysis by host of symbiont cells / positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway / thrombospondin receptor activity / Defective factor XII causes hereditary angioedema / thrombin / regulation of blood coagulation / neutrophil-mediated killing of gram-negative bacterium / ligand-gated ion channel signaling pathway / Defective F8 cleavage by thrombin / Platelet Aggregation (Plug Formation) / negative regulation of astrocyte differentiation / negative regulation of platelet activation / positive regulation of collagen biosynthetic process / negative regulation of cytokine production involved in inflammatory response / positive regulation of blood coagulation / negative regulation of fibrinolysis / Gamma-carboxylation of protein precursors / Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus / Common Pathway of Fibrin Clot Formation / Removal of aminoterminal propeptides from gamma-carboxylated proteins / fibrinolysis / regulation of cytosolic calcium ion concentration / Intrinsic Pathway of Fibrin Clot Formation / Peptide ligand-binding receptors / positive regulation of release of sequestered calcium ion into cytosol / acute-phase response / Regulation of Complement cascade / negative regulation of proteolysis / Cell surface interactions at the vascular wall / lipopolysaccharide binding / positive regulation of receptor signaling pathway via JAK-STAT / growth factor activity / positive regulation of insulin secretion / platelet activation / response to wounding / positive regulation of protein localization to nucleus / Golgi lumen / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / positive regulation of reactive oxygen species metabolic process / blood coagulation / antimicrobial humoral immune response mediated by antimicrobial peptide / Thrombin signalling through proteinase activated receptors (PARs) / heparin binding / regulation of cell shape / positive regulation of cell growth / G alpha (q) signalling events / collagen-containing extracellular matrix / blood microparticle / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / cell surface receptor signaling pathway / positive regulation of protein phosphorylation / G protein-coupled receptor signaling pathway / endoplasmic reticulum lumen / serine-type endopeptidase activity / signaling receptor binding / positive regulation of cell population proliferation / calcium ion binding / proteolysis / extracellular space / extracellular exosome / extracellular region / plasma membrane
Similarity search - Function
Salivary thrombin inhibitor anophelin, mosquito / Thrombin inhibitor from mosquito / Prothrombin/thrombin / Thrombin light chain / Thrombin light chain domain superfamily / : / Thrombin light chain / Kringle domain / Kringle / Kringle, conserved site ...Salivary thrombin inhibitor anophelin, mosquito / Thrombin inhibitor from mosquito / Prothrombin/thrombin / Thrombin light chain / Thrombin light chain domain superfamily / : / Thrombin light chain / Kringle domain / Kringle / Kringle, conserved site / Kringle superfamily / Kringle domain signature. / Kringle domain profile. / Kringle domain / Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain / Gamma-carboxyglutamic acid-rich (GLA) domain / Gamma-carboxyglutamic acid-rich (GLA) domain superfamily / Vitamin K-dependent carboxylation domain. / Gla domain profile. / Domain containing Gla (gamma-carboxyglutamate) residues. / Kringle-like fold / Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin family, histidine active site. / Serine proteases, trypsin family, serine active site. / Serine proteases, trypsin domain profile. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Trypsin-like serine proteases / Thrombin, subunit H / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
Prothrombin / Salivary thrombin inhibitor anophelin
Similarity search - Component
Biological speciesAnopheles gambiae (African malaria mosquito)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.45 Å
AuthorsRipoll-Rozada, J. / Pereira, P.J.B.
CitationJournal: J. Biol. Chem. / Year: 2017
Title: Functional analyses yield detailed insight into the mechanism of thrombin inhibition by the antihemostatic salivary protein cE5 from Anopheles gambiae.
Authors: Pirone, L. / Ripoll-Rozada, J. / Leone, M. / Ronca, R. / Lombardo, F. / Fiorentino, G. / Andersen, J.F. / Pereira, P.J.B. / Arca, B. / Pedone, E.
History
DepositionMar 22, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 14, 2017Provider: repository / Type: Initial release
Revision 1.1Jun 21, 2017Group: Database references / Category: citation
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2Aug 9, 2017Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.3Jul 29, 2020Group: Data collection / Derived calculations / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / pdbx_struct_conn_angle / struct_conn / struct_site / struct_site_gen
Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_ptnr1_label_alt_id / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _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
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.4Jan 17, 2024Group: 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
Revision 1.5Oct 23, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
L: Prothrombin
H: Prothrombin
B: Prothrombin
A: Prothrombin
D: Prothrombin
C: Prothrombin
I: AGAP008004-PA
J: AGAP008004-PA
K: AGAP008004-PA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)129,17715
Polymers128,4449
Non-polymers7336
Water13,115728
1
L: Prothrombin
H: Prothrombin
I: AGAP008004-PA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,0595
Polymers42,8153
Non-polymers2442
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5890 Å2
ΔGint-31 kcal/mol
Surface area13540 Å2
MethodPISA
2
B: Prothrombin
A: Prothrombin
J: AGAP008004-PA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,0595
Polymers42,8153
Non-polymers2442
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5730 Å2
ΔGint-32 kcal/mol
Surface area13810 Å2
MethodPISA
3
D: Prothrombin
C: Prothrombin
K: AGAP008004-PA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,0595
Polymers42,8153
Non-polymers2442
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4240 Å2
ΔGint-26 kcal/mol
Surface area12860 Å2
MethodPISA
Unit cell
Length a, b, c (Å)110.710, 78.640, 136.109
Angle α, β, γ (deg.)90.00, 101.84, 90.00
Int Tables number5
Space group name H-MI121

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Components

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Protein , 2 types, 6 molecules HACIJK

#2: Protein Prothrombin / thrombin heavy chain / Coagulation factor II


Mass: 29780.219 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P00734, thrombin
#3: Protein AGAP008004-PA / cE5 anticoagulant


Mass: 8937.997 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Anopheles gambiae (African malaria mosquito)
Gene: AgaP_AGAP008004 / Production host: Escherichia coli BL21 (bacteria) / References: UniProt: Q7Q3R9

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Protein/peptide / Sugars , 2 types, 6 molecules LBD

#1: Protein/peptide Prothrombin / thrombin light chain / Coagulation factor II


Mass: 4096.534 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P00734, thrombin
#4: 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.: 3 / Source method: isolated from a natural source / Formula: C8H15NO6 / Source: (natural) Homo sapiens (human) / References: thrombin
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 , 2 types, 731 molecules

#5: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Na
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 728 / Source method: isolated from a natural source / Formula: H2O

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Details

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 Å3/Da / Density % sol: 59 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 5
Details: Drops consisting of equal volumes (1 microliter) of protein complex (at 6.4 mg/mL) and precipitant solution (0.1M PCTP pH 5.0, 25% w/v PEG 1500) equilibrated against a 300 microliter reservoir.

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID30B / Wavelength: 0.973 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: May 7, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.973 Å / Relative weight: 1
ReflectionResolution: 1.45→54.2 Å / Num. obs: 198548 / % possible obs: 98.4 % / Redundancy: 3.9 % / CC1/2: 0.996 / Rmerge(I) obs: 0.091 / Net I/σ(I): 6.8
Reflection shellResolution: 1.45→1.47 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.772 / Mean I/σ(I) obs: 1 / Num. unique obs: 9287 / CC1/2: 0.565 / % possible all: 93.3

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Processing

Software
NameVersionClassification
PHENIX(1.11.1_2575: ???)refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3U69

3u69


Resolution: 1.45→54.177 Å / SU ML: 0.18 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 22.01 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.203 9835 4.95 %
Rwork0.1792 --
obs0.1803 198522 98.28 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.45→54.177 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7377 0 45 728 8150
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0198612
X-RAY DIFFRACTIONf_angle_d1.66711645
X-RAY DIFFRACTIONf_dihedral_angle_d27.0623327
X-RAY DIFFRACTIONf_chiral_restr0.1681208
X-RAY DIFFRACTIONf_plane_restr0.0111516
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.45-1.46650.35363380.33115916X-RAY DIFFRACTION93
1.4665-1.48370.35463090.31535987X-RAY DIFFRACTION93
1.4837-1.50180.33783160.31045875X-RAY DIFFRACTION93
1.5018-1.52080.31523060.29296122X-RAY DIFFRACTION96
1.5208-1.54080.3052960.27646088X-RAY DIFFRACTION94
1.5408-1.56190.2723160.2576190X-RAY DIFFRACTION98
1.5619-1.58430.24533230.24086290X-RAY DIFFRACTION99
1.5843-1.60790.27393620.24076324X-RAY DIFFRACTION99
1.6079-1.6330.27053580.2316308X-RAY DIFFRACTION99
1.633-1.65980.23273240.22246346X-RAY DIFFRACTION99
1.6598-1.68840.25333370.21896308X-RAY DIFFRACTION99
1.6884-1.71910.26193120.22426347X-RAY DIFFRACTION99
1.7191-1.75220.24963150.21756356X-RAY DIFFRACTION99
1.7522-1.7880.2333200.20676342X-RAY DIFFRACTION99
1.788-1.82690.24413360.21676320X-RAY DIFFRACTION99
1.8269-1.86940.23483340.20196341X-RAY DIFFRACTION99
1.8694-1.91610.2173450.1886351X-RAY DIFFRACTION100
1.9161-1.96790.21583250.18336327X-RAY DIFFRACTION99
1.9679-2.02580.21193410.18286332X-RAY DIFFRACTION99
2.0258-2.09120.20943340.17976380X-RAY DIFFRACTION99
2.0912-2.1660.20633340.17626322X-RAY DIFFRACTION99
2.166-2.25270.19033290.176401X-RAY DIFFRACTION100
2.2527-2.35520.1993330.16646307X-RAY DIFFRACTION99
2.3552-2.47940.18053320.16736396X-RAY DIFFRACTION100
2.4794-2.63470.21643310.17176377X-RAY DIFFRACTION100
2.6347-2.83810.19223330.16996392X-RAY DIFFRACTION99
2.8381-3.12370.18783120.1756384X-RAY DIFFRACTION99
3.1237-3.57570.1973450.15996392X-RAY DIFFRACTION99
3.5757-4.50460.14353330.13396370X-RAY DIFFRACTION99
4.5046-54.21510.17883060.1666496X-RAY DIFFRACTION98
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)
16.8578-0.3193-0.40533.8871.36266.96840.0617-0.53350.8203-0.0121-0.03-0.0089-1.1577-0.1701-0.05870.30340.0532-0.00370.27330.00870.20450.569718.6233-17.7546
27.4789-5.7724-6.57474.5275.20236.0345-0.1491-0.4058-0.50290.40790.03020.16920.6352-0.12770.1020.2284-0.0133-0.01770.24250.10450.21410.82614.5209-19.1778
39.51985.13-4.73037.0593-4.32783.1148-0.08870.3239-0.6322-0.3661-0.2204-0.53920.32840.3540.33550.24280.0638-0.00330.24420.02090.197313.43472.8943-27.7792
41.69630.9666-0.00052.616-0.52876.5232-0.0112-0.1503-0.21310.0318-0.02790.050.5259-0.14080.03120.13230.0164-0.02570.17850.05620.184-3.28837.8378-30.8687
50.7601-0.10330.01420.5161-0.48942.13610.01940.04630.1059-0.05060.09450.1519-0.188-0.4118-0.12630.21220.063-0.02310.25180.06350.1801-9.860922.8781-35.8425
64.24210.4997-1.48313.5263-1.23074.09880.1520.20010.5104-0.00620.0393-0.1446-0.5405-0.1196-0.23620.22160.0333-0.04040.1480.07090.16971.001130.7977-39.1607
72.62730.5243-1.10672.2325-0.78942.80590.0806-0.1180.16380.09070.0680.0824-0.3295-0.1997-0.12020.18080.04620.00010.18130.02640.1341-4.088823.2841-23.5796
81.7797-2.2257-0.78293.04880.38833.8110.06690.00710.129-0.02760.1032-0.4205-0.07930.4863-0.17530.14880.00680.01610.20460.04580.167813.809913.4738-29.876
93.55020.2038-0.73221.2723-0.43132.16370.03790.35470.0796-0.2546-0.0211-0.0025-0.01980.0227-0.00620.20670.0291-0.01920.17910.03530.12035.479612.9721-42.9937
101.78-0.1921.25931.33360.48124.58080.07640.1556-0.0561-0.1918-0.0056-0.05190.17260.1734-0.0710.13770.023-0.00040.14130.04250.12537.699912.6635-37.8196
119.7505-6.4862-3.94898.43043.71962.225-0.0723-0.40471.29950.12770.2573-0.6807-0.74070.2834-0.20530.3786-0.0179-0.07040.22930.00730.32917.414132.792-28.4633
125.3782-3.0302-1.58941.94031.88545.9039-0.0788-0.0565-0.38920.0988-0.09510.43010.2238-0.64170.13390.17170.0421-0.01750.24110.01620.18429.12747.4724-3.8638
133.6289-4.0561-3.94456.54662.7246.9110.090.19670.8651-0.1517-0.0334-0.1901-0.611-0.38490.00090.23260.0521-0.00410.13380.03180.197115.9815.2787-8.911
145.83516.99433.06568.4533.11658.2542-0.27290.89050.0512-0.87730.5095-0.2015-0.33430.3902-0.27720.25310.03070.02310.28470.06970.192823.14866.6836-19.6483
151.2197-0.3276-0.33041.80220.15751.3294-0.0903-0.26170.01150.26830.071-0.09820.02450.10540.01490.13620.0329-0.01550.17170.00660.108422.27390.06859.12
161.7796-1.7251-0.56043.89720.86692.3576-0.1677-0.1353-0.17810.31510.08180.16440.2574-0.120.08030.1006-0.02110.01980.13290.01360.128316.1021-7.09065.1675
172.0046-0.0399-0.78754.00421.74546.33950.05190.3264-0.2093-0.3716-0.07130.20130.2128-0.20460.0470.15870.0484-0.03660.1520.0040.156919.9085-2.7347-14.0336
181.7884-0.9945-1.11892.79661.8352.79280.0275-0.24450.10640.08460.0748-0.32210.00570.3334-0.07950.1028-0.0087-0.01610.15630.01490.173832.06513.5713-1.287
197.03352.4447-3.09577.14571.14813.1785-0.178-0.018-0.56730.1610.064-0.23220.4590.21730.06220.21950.06630.01740.1374-0.00030.192731.6924-16.2992-11.1422
203.451-0.51060.28761.1384-0.06291.903-0.02070.08790.0433-0.0542-0.0226-0.1530.01380.10570.03970.11990.01310.00150.09470.01970.114127.5392-2.9201-8.1263
212.9103-1.3329-4.48568.97880.59637.5776-0.17450.3164-0.3950.3079-0.02680.69880.6696-0.92830.16590.1591-0.0653-0.00760.2905-0.01550.26649.3853-13.5239-0.749
221.50952.33250.82146.32491.29566.32440.0170.76810.2485-0.4616-0.0116-0.5642-0.07750.6887-0.00180.37360.20120.14510.46220.17120.298336.626415.5171-44.0919
235.86932.6187-0.46658.47125.2087.56130.25720.3718-0.1612-0.4752-0.3705-0.18640.72220.46130.18430.26850.13510.0360.22390.06660.200127.58710.5435-39.59
248.94434.13073.92268.6833.91938.5947-0.08430.20490.928-0.1893-0.02530.0162-0.301-0.13220.10960.15380.00770.04880.23310.05490.273723.609720.9951-32.5932
250.59310.9530.37161.44770.54320.78230.179-0.2786-0.5980.1522-0.3609-0.89690.13210.42450.08750.2390.02210.01020.46640.28930.582851.337316.4555-28.019
261.9596-0.52760.12491.5864-1.13232.5510.05270.2174-0.2202-0.2244-0.5475-0.91940.57030.5728-0.14280.41930.34020.25230.66260.48040.759751.49476.5677-32.3827
270.0186-0.1208-0.04612.20370.0380.9363-0.33330.05190.39450.3279-0.6266-0.6947-0.23290.68020.27880.4005-0.1315-0.10540.77260.48061.561255.475125.243-28.4171
282.50070.2176-0.45171.6267-0.18811.6894-0.03850.050.177-0.06160.0394-0.1562-0.14110.1204-0.0130.1795-0.04340.01090.18450.05970.275843.320320.7685-37.379
291.8778-0.52290.0813.7376-0.24761.0987-0.11390.05060.92061.0837-0.4018-1.2111-0.40890.11650.27410.3582-0.0965-0.14050.24590.1220.588637.054722.9265-23.7193
303.1611-0.0391-1.81362.06130.15482.50360.3726-0.16080.3650.3716-0.12560.0194-0.42190.0746-0.21090.3336-0.0754-0.0880.1586-0.01140.255744.878828.6284-29.9159
316.66610.48872.76976.5133-3.40654.0345-0.03220.17520.63450.47870.43660.5442-0.2567-0.4054-0.37850.43840.17940.0121.17380.23910.7305-23.053124.5551-30.6384
327.48882.2177-2.49644.9248-1.08545.1141-0.07880.88790.1403-0.41220.180.14530.057-0.3885-0.11360.28290.0371-0.060.29110.05050.146-4.619418.985-48.8419
335.7151-5.2537-4.68395.46284.54183.9448-0.2381-0.88820.30550.22370.4555-0.23780.06820.5818-0.26630.34010.0695-0.05310.3966-0.04440.221625.09774.196218.6998
348.052-4.6682-0.62513.42731.87983.7824-0.1657-0.3094-0.34490.2886-0.0145-1.18940.62281.16070.10940.29040.1317-0.01770.36610.05130.372537.6203-14.03512.9071
351.93452.410.88853.42871.23511.60670.1601-0.23880.12440.5912-0.2398-0.28520.06830.1006-0.11460.9652-0.1839-0.63690.26330.04661.260149.149922.8754-13.7056
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'L' and (resid 285 through 299 )
2X-RAY DIFFRACTION2chain 'L' and (resid 300 through 308 )
3X-RAY DIFFRACTION3chain 'L' and (resid 309 through 320 )
4X-RAY DIFFRACTION4chain 'H' and (resid 321 through 334 )
5X-RAY DIFFRACTION5chain 'H' and (resid 335 through 396 )
6X-RAY DIFFRACTION6chain 'H' and (resid 397 through 420 )
7X-RAY DIFFRACTION7chain 'H' and (resid 421 through 442 )
8X-RAY DIFFRACTION8chain 'H' and (resid 443 through 460 )
9X-RAY DIFFRACTION9chain 'H' and (resid 461 through 504 )
10X-RAY DIFFRACTION10chain 'H' and (resid 505 through 563 )
11X-RAY DIFFRACTION11chain 'H' and (resid 564 through 578 )
12X-RAY DIFFRACTION12chain 'B' and (resid 288 through 299 )
13X-RAY DIFFRACTION13chain 'B' and (resid 300 through 308 )
14X-RAY DIFFRACTION14chain 'B' and (resid 309 through 320 )
15X-RAY DIFFRACTION15chain 'A' and (resid 321 through 396 )
16X-RAY DIFFRACTION16chain 'A' and (resid 397 through 442 )
17X-RAY DIFFRACTION17chain 'A' and (resid 443 through 460 )
18X-RAY DIFFRACTION18chain 'A' and (resid 461 through 489 )
19X-RAY DIFFRACTION19chain 'A' and (resid 490 through 504 )
20X-RAY DIFFRACTION20chain 'A' and (resid 505 through 563 )
21X-RAY DIFFRACTION21chain 'A' and (resid 564 through 578 )
22X-RAY DIFFRACTION22chain 'D' and (resid 289 through 299 )
23X-RAY DIFFRACTION23chain 'D' and (resid 300 through 308 )
24X-RAY DIFFRACTION24chain 'D' and (resid 309 through 317 )
25X-RAY DIFFRACTION25chain 'C' and (resid 321 through 375 )
26X-RAY DIFFRACTION26chain 'C' and (resid 376 through 396 )
27X-RAY DIFFRACTION27chain 'C' and (resid 397 through 415 )
28X-RAY DIFFRACTION28chain 'C' and (resid 416 through 460 )
29X-RAY DIFFRACTION29chain 'C' and (resid 461 through 547 )
30X-RAY DIFFRACTION30chain 'C' and (resid 548 through 576 )
31X-RAY DIFFRACTION31chain 'I' and (resid 36 through 41 )
32X-RAY DIFFRACTION32chain 'I' and (resid 42 through 62 )
33X-RAY DIFFRACTION33chain 'J' and (resid 35 through 53 )
34X-RAY DIFFRACTION34chain 'J' and (resid 54 through 63 )
35X-RAY DIFFRACTION35chain 'K' and (resid 52 through 61 )

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