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- PDB-3p70: Structural basis of thrombin-mediated factor V activation: essent... -

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Basic information

Entry
Database: PDB / ID: 3p70
TitleStructural basis of thrombin-mediated factor V activation: essential role of the hirudin-like sequence Glu666-Glu672 for processing at the heavy chain-B domain junction
Components
  • (HUMAN ALPHA-THROMBIN, ...) x 2
  • HUMAN FACTOR V, A2-B DOMAIN LINKER
KeywordsHYDROLASE / TRYPSIN-LIKE SERINE PROTEINASE / BLOOD COAGULATION / N-GLYCOSYLATION / BLOOD PLASMA
Function / homology
Function and homology information


response to vitamin K / platelet alpha granule / Cargo concentration in the ER / blood circulation / COPII-mediated vesicle transport / cytolysis by host of symbiont cells / positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway / thrombospondin receptor activity / thrombin-activated receptor signaling pathway / Defective factor XII causes hereditary angioedema ...response to vitamin K / platelet alpha granule / Cargo concentration in the ER / blood circulation / COPII-mediated vesicle transport / cytolysis by host of symbiont cells / positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway / thrombospondin receptor activity / thrombin-activated receptor signaling pathway / Defective factor XII causes hereditary angioedema / thrombin / COPII-coated ER to Golgi transport vesicle / regulation of blood coagulation / neutrophil-mediated killing of gram-negative bacterium / Defective F8 cleavage by thrombin / ligand-gated ion channel signaling pathway / Platelet Aggregation (Plug Formation) / negative regulation of astrocyte differentiation / negative regulation of platelet activation / positive regulation of collagen biosynthetic process / negative regulation of blood coagulation / negative regulation of cytokine production involved in inflammatory response / positive regulation of blood coagulation / negative regulation of fibrinolysis / regulation of cytosolic calcium ion concentration / Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus / Gamma-carboxylation of protein precursors / Common Pathway of Fibrin Clot Formation / Removal of aminoterminal propeptides from gamma-carboxylated proteins / fibrinolysis / Intrinsic Pathway of Fibrin Clot Formation / endoplasmic reticulum-Golgi intermediate compartment membrane / Peptide ligand-binding receptors / positive regulation of release of sequestered calcium ion into cytosol / platelet alpha granule lumen / Regulation of Complement cascade / acute-phase response / negative regulation of proteolysis / Cell surface interactions at the vascular wall / positive regulation of receptor signaling pathway via JAK-STAT / Post-translational protein phosphorylation / lipopolysaccharide binding / growth factor activity / positive regulation of insulin secretion / response to wounding / platelet activation / Golgi lumen / positive regulation of protein localization to nucleus / 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 / antimicrobial humoral immune response mediated by antimicrobial peptide / blood coagulation / extracellular vesicle / Platelet degranulation / Thrombin signalling through proteinase activated receptors (PARs) / heparin binding / regulation of cell shape / positive regulation of cell growth / collagen-containing extracellular matrix / G alpha (q) signalling events / blood microparticle / positive regulation of protein phosphorylation / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / cell surface receptor signaling pathway / receptor ligand activity / copper ion binding / endoplasmic reticulum lumen / signaling receptor binding / serine-type endopeptidase activity / positive regulation of cell population proliferation / calcium ion binding / proteolysis / extracellular space / extracellular exosome / extracellular region / membrane / plasma membrane
Similarity search - Function
Coagulation factor 5/8-like / : / Coagulation factors 5/8 type C domain (FA58C) signature 2. / Multicopper oxidases, conserved site / Multicopper oxidases signature 1. / Coagulation factors 5/8 type C domain (FA58C) signature 1. / Coagulation factor 5/8 C-terminal domain, discoidin domain / Coagulation factors 5/8 type C domain (FA58C) profile. / F5/8 type C domain / Coagulation factor 5/8 C-terminal domain ...Coagulation factor 5/8-like / : / Coagulation factors 5/8 type C domain (FA58C) signature 2. / Multicopper oxidases, conserved site / Multicopper oxidases signature 1. / Coagulation factors 5/8 type C domain (FA58C) signature 1. / Coagulation factor 5/8 C-terminal domain, discoidin domain / Coagulation factors 5/8 type C domain (FA58C) profile. / F5/8 type C domain / Coagulation factor 5/8 C-terminal domain / Prothrombin/thrombin / Thrombin light chain / Thrombin light chain domain superfamily / : / Thrombin light chain / Multicopper oxidase, N-terminal / Multicopper oxidase / 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 / Cupredoxin / Galactose-binding-like domain superfamily / Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Serine proteases, trypsin family, histidine active site. / Peptidase S1A, chymotrypsin family / 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
BENZAMIDINE / beta-D-glucopyranose / Prothrombin / Coagulation factor V
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.55 Å
AuthorsCorral-Rodriguez, M.A. / Bock, P.E. / Hernandez-Carvajal, E. / Gutierrez-Gallego, R. / Fuentes-Prior, P.
CitationJournal: Blood / Year: 2011
Title: Structural basis of thrombin-mediated factor V activation: the Glu666-Glu672 sequence is critical for processing at the heavy chain-B domain junction.
Authors: Corral-Rodriguez, M.A. / Bock, P.E. / Hernandez-Carvajal, E. / Gutierrez-Gallego, R. / Fuentes-Prior, P.
History
DepositionOct 11, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 28, 2011Provider: repository / Type: Initial release
Revision 1.1Feb 29, 2012Group: Database references
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_struct_conn_angle / pdbx_validate_close_contact / struct_asym / struct_conn / struct_ref_seq_dif / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _atom_site_anisotrop.id / _atom_site_anisotrop.pdbx_auth_asym_id / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_auth_comp_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_asym_id / _atom_site_anisotrop.pdbx_label_atom_id / _atom_site_anisotrop.pdbx_label_comp_id / _atom_site_anisotrop.type_symbol / _chem_comp.name / _chem_comp.type / _pdbx_entity_nonpoly.entity_id / _pdbx_entity_nonpoly.name / _pdbx_struct_assembly_gen.asym_id_list / _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.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_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 / _pdbx_validate_close_contact.auth_asym_id_1 / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_seq_id_1 / _pdbx_validate_close_contact.auth_seq_id_2 / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _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 / _struct_conn.ptnr2_label_seq_id / _struct_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Sep 6, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 2.2Oct 9, 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
A: HUMAN ALPHA-THROMBIN, LIGHT CHAIN
B: HUMAN ALPHA-THROMBIN, HEAVY CHAIN
C: HUMAN ALPHA-THROMBIN, LIGHT CHAIN
D: HUMAN ALPHA-THROMBIN, HEAVY CHAIN
E: HUMAN ALPHA-THROMBIN, LIGHT CHAIN
F: HUMAN ALPHA-THROMBIN, HEAVY CHAIN
G: HUMAN ALPHA-THROMBIN, LIGHT CHAIN
H: HUMAN ALPHA-THROMBIN, HEAVY CHAIN
M: HUMAN FACTOR V, A2-B DOMAIN LINKER
N: HUMAN FACTOR V, A2-B DOMAIN LINKER
O: HUMAN FACTOR V, A2-B DOMAIN LINKER
P: HUMAN FACTOR V, A2-B DOMAIN LINKER
hetero molecules


Theoretical massNumber of molelcules
Total (without water)171,54830
Polymers169,07512
Non-polymers2,47318
Water43224
1
A: HUMAN ALPHA-THROMBIN, LIGHT CHAIN
B: HUMAN ALPHA-THROMBIN, HEAVY CHAIN
M: HUMAN FACTOR V, A2-B DOMAIN LINKER
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,8368
Polymers42,2693
Non-polymers5675
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3530 Å2
ΔGint-30 kcal/mol
Surface area13630 Å2
MethodPISA
2
C: HUMAN ALPHA-THROMBIN, LIGHT CHAIN
D: HUMAN ALPHA-THROMBIN, HEAVY CHAIN
N: HUMAN FACTOR V, A2-B DOMAIN LINKER
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,6567
Polymers42,2693
Non-polymers3874
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3410 Å2
ΔGint-18 kcal/mol
Surface area13440 Å2
MethodPISA
3
E: HUMAN ALPHA-THROMBIN, LIGHT CHAIN
F: HUMAN ALPHA-THROMBIN, HEAVY CHAIN
O: HUMAN FACTOR V, A2-B DOMAIN LINKER
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,0167
Polymers42,2693
Non-polymers7484
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4060 Å2
ΔGint-11 kcal/mol
Surface area13890 Å2
MethodPISA
4
G: HUMAN ALPHA-THROMBIN, LIGHT CHAIN
H: HUMAN ALPHA-THROMBIN, HEAVY CHAIN
P: HUMAN FACTOR V, A2-B DOMAIN LINKER
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,0398
Polymers42,2693
Non-polymers7715
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3990 Å2
ΔGint-11 kcal/mol
Surface area13670 Å2
MethodPISA
Unit cell
Length a, b, c (Å)62.243, 68.227, 98.972
Angle α, β, γ (deg.)72.57, 84.05, 80.45
Int Tables number1
Space group name H-MP1

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Components

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HUMAN ALPHA-THROMBIN, ... , 2 types, 8 molecules ACEGBDFH

#1: Protein/peptide
HUMAN ALPHA-THROMBIN, LIGHT CHAIN / Coagulation factor II / Thrombin light chain


Mass: 4096.534 Da / Num. of mol.: 4 / Fragment: THROMBIN LIGHT CHAIN / Source method: isolated from a natural source / Details: PURIFIED FROM BLOOD PLASMA / Source: (natural) Homo sapiens (human) / References: UniProt: P00734, thrombin
#2: Protein
HUMAN ALPHA-THROMBIN, HEAVY CHAIN / Coagulation factor II / Thrombin heavy chain


Mass: 29780.219 Da / Num. of mol.: 4 / Fragment: THROMBIN HEAVY CHAIN / Source method: isolated from a natural source / Details: PURIFIED FROM BLOOD PLASMA / Source: (natural) Homo sapiens (human) / References: UniProt: P00734, thrombin

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Protein , 1 types, 4 molecules MNOP

#3: Protein
HUMAN FACTOR V, A2-B DOMAIN LINKER / Activated protein C cofactor


Mass: 8391.935 Da / Num. of mol.: 4 / Fragment: FACTOR V, A2-B DOMAIN LINKER
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: F5 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P12259

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Sugars , 3 types, 7 molecules

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


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 2 / Source method: obtained synthetically
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE
#5: 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: obtained synthetically / 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
#8: Sugar ChemComp-BGC / beta-D-glucopyranose / beta-D-glucose / D-glucose / glucose


Type: D-saccharide, beta linking / Mass: 180.156 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Formula: C6H12O6
IdentifierTypeProgram
DGlcpbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
b-D-glucopyranoseCOMMON NAMEGMML 1.0
b-D-GlcpIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 3 types, 35 molecules

#6: Chemical
ChemComp-BEN / BENZAMIDINE


Mass: 120.152 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C7H8N2
#7: Chemical
ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: Na
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 24 / 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: 2.34 Å3/Da / Density % sol: 47.32 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 100 mM MOPS/HEPES-Na, pH 7.5, 12.5% (w/v) PEG 1000, 12.5% (w/v) PEG 3350, 12.5% (v/v) 2-methylpentane-2,4-diol (MPD), 20 mM D-glucose, 20 mM D-mannose, 20 mM D-galactose, 20 mM L-fucose, 20 ...Details: 100 mM MOPS/HEPES-Na, pH 7.5, 12.5% (w/v) PEG 1000, 12.5% (w/v) PEG 3350, 12.5% (v/v) 2-methylpentane-2,4-diol (MPD), 20 mM D-glucose, 20 mM D-mannose, 20 mM D-galactose, 20 mM L-fucose, 20 mM D-xylose, 20 mM N-acetyl-D-glucosamine , VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 298 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-2 / Wavelength: 0.8726 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Feb 19, 2010
RadiationMonochromator: Si 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.8726 Å / Relative weight: 1
ReflectionResolution: 2.55→64.42 Å / Num. all: 49833 / Num. obs: 47142 / % possible obs: 94.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.6 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 10.8
Reflection shellResolution: 2.55→2.69 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.426 / Mean I/σ(I) obs: 2.7 / Num. unique all: 6841 / % possible all: 94.1

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Processing

Software
NameVersionClassification
MxCuBEdata collection
MOLREPphasing
REFMAC5.5.0072refinement
MOSFLMdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1PPB

1ppb


Resolution: 2.55→61.28 Å / Cor.coef. Fo:Fc: 0.948 / Cor.coef. Fo:Fc free: 0.905 / SU B: 27.032 / SU ML: 0.267 / Cross valid method: THROUGHOUT / ESU R Free: 0.339 / Stereochemistry target values: MAXIMUM LIKELIHOOD
RfactorNum. reflection% reflectionSelection details
Rfree0.27881 2384 5.1 %RANDOM
Rwork0.20685 ---
obs0.2105 44784 94.64 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 54.748 Å2
Baniso -1Baniso -2Baniso -3
1--0.02 Å20.03 Å2-0.01 Å2
2--0.1 Å20 Å2
3----0.09 Å2
Refinement stepCycle: LAST / Resolution: 2.55→61.28 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9282 0 163 24 9469
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0160.0229694
X-RAY DIFFRACTIONr_angle_refined_deg1.8411.9813085
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.40851126
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.01523.245453
X-RAY DIFFRACTIONr_dihedral_angle_3_deg20.398151708
X-RAY DIFFRACTIONr_dihedral_angle_4_deg18.5491582
X-RAY DIFFRACTIONr_chiral_restr0.1170.21372
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.0217316
X-RAY DIFFRACTIONr_mcbond_it0.6361.55693
X-RAY DIFFRACTIONr_mcangle_it1.18629169
X-RAY DIFFRACTIONr_scbond_it1.99634001
X-RAY DIFFRACTIONr_scangle_it3.0914.53915
LS refinement shellResolution: 2.55→2.616 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.359 178 -
Rwork0.273 3279 -
obs--94.09 %
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)
15.1303-1.64982.300210.1929-2.28153.9064-0.4006-0.55860.30790.83820.41020.2587-0.52970.024-0.00960.13280.00860.05170.1353-0.06640.09729.02141.395106.658
23.6326-2.3661-0.28025.49460.51073.5080.06420.0584-0.2757-0.38520.070.23160.21560.0545-0.13420.1062-0.0733-0.01670.1010.02060.095811.52327.62593.222
34.9821-4.10580.561311.4509-2.61793.5226-0.2663-0.65810.2490.74630.48340.261-0.0610.2894-0.21720.09460.00980.03740.191-0.05930.06379.17160.60159.149
45.1347-4.48160.03747.28230.61833.57830.25710.2891-0.9949-0.5543-0.23090.89250.22410.0461-0.02620.106-0.0488-0.0620.1425-0.0250.230512.66447.54745.259
57.2153-2.8177-5.57947.63293.80869.7429-0.4382-0.3749-0.79550.64920.48230.51520.6661-0.2194-0.04410.14390.04810.07110.15620.11880.375544.9112.45362.695
63.9595-2.8045-0.6425.29341.03493.9838-0.0392-0.30940.31560.06040.25020.0116-0.38170.1347-0.2110.0835-0.0430.02810.17110.00770.127842.04521.9362.981
77.2536-3.534-4.89725.1095-0.37426.6232-0.7405-0.7169-1.12260.43610.65130.57090.7053-0.03650.08920.2249-0.0178-0.03760.22250.20710.618544.856-16.458110.827
84.0246-2.6523-0.26585.33860.4164.5246-0.0315-0.35370.42390.15180.2803-0.1762-0.4711-0.023-0.24880.1074-0.04620.03690.1046-0.02020.129141.9632.939109.995
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A-10 - 9999
2X-RAY DIFFRACTION2B-10 - 9999
3X-RAY DIFFRACTION3C-10 - 9999
4X-RAY DIFFRACTION4D-10 - 9999
5X-RAY DIFFRACTION5E-10 - 9999
6X-RAY DIFFRACTION6F-10 - 9999
7X-RAY DIFFRACTION7G-10 - 9999
8X-RAY DIFFRACTION8H-10 - 9999

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