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- PDB-6vft: Crystal structure of human delta protocadherin 17 EC1-EC4 -

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Basic information

Entry
Database: PDB / ID: 6vft
TitleCrystal structure of human delta protocadherin 17 EC1-EC4
ComponentsProtocadherin-17
KeywordsCELL ADHESION / cadherin extracellular region / non-clustered delta2 family / protocadherin homophilic adhesion/recognition calcium-dependent / adhesion molecule
Function / homology
Function and homology information


regulation of synaptic vesicle clustering / presynaptic active zone assembly / : / : / synaptic membrane adhesion / negative regulation of synaptic transmission / adult behavior / plasma membrane => GO:0005886 / homophilic cell adhesion via plasma membrane adhesion molecules / GABA-ergic synapse ...regulation of synaptic vesicle clustering / presynaptic active zone assembly / : / : / synaptic membrane adhesion / negative regulation of synaptic transmission / adult behavior / plasma membrane => GO:0005886 / homophilic cell adhesion via plasma membrane adhesion molecules / GABA-ergic synapse / cell adhesion / glutamatergic synapse / calcium ion binding
Similarity search - Function
Protocadherin-17 / Cadherin, N-terminal / Cadherin-like / Cadherins / Cadherin conserved site / Cadherin domain signature. / Cadherin repeats. / Cadherin domain / Cadherins domain profile. / Cadherin-like ...Protocadherin-17 / Cadherin, N-terminal / Cadherin-like / Cadherins / Cadherin conserved site / Cadherin domain signature. / Cadherin repeats. / Cadherin domain / Cadherins domain profile. / Cadherin-like / Cadherin-like superfamily / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
alpha-D-mannopyranose / Protocadherin-17
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.71 Å
AuthorsHarrison, O.J. / Brasch, J. / Shapiro, L.
Funding support United States, 3items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01MH114817 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01GM118584 United States
National Science Foundation (NSF, United States)MCB-1412472 United States
CitationJournal: Cell Rep / Year: 2020
Title: Family-wide Structural and Biophysical Analysis of Binding Interactions among Non-clustered δ-Protocadherins.
Authors: Oliver J Harrison / Julia Brasch / Phinikoula S Katsamba / Goran Ahlsen / Alex J Noble / Hanbin Dan / Rosemary V Sampogna / Clinton S Potter / Bridget Carragher / Barry Honig / Lawrence Shapiro /
Abstract: Non-clustered δ1- and δ2-protocadherins, close relatives of clustered protocadherins, function in cell adhesion and motility and play essential roles in neural patterning. To understand the ...Non-clustered δ1- and δ2-protocadherins, close relatives of clustered protocadherins, function in cell adhesion and motility and play essential roles in neural patterning. To understand the molecular interactions underlying these functions, we used solution biophysics to characterize binding of δ1- and δ2-protocadherins, determined crystal structures of ectodomain complexes from each family, and assessed ectodomain assembly in reconstituted intermembrane junctions by cryoelectron tomography (cryo-ET). Homophilic trans (cell-cell) interactions were preferred for all δ-protocadherins, with additional weaker heterophilic interactions observed exclusively within each subfamily. As expected, δ1- and δ2-protocadherin trans dimers formed through antiparallel EC1-EC4 interfaces, like clustered protocadherins. However, no ectodomain-mediated cis (same-cell) interactions were detectable in solution; consistent with this, cryo-ET of reconstituted junctions revealed dense assemblies lacking the characteristic order observed for clustered protocadherins. Our results define non-clustered protocadherin binding properties and their structural basis, providing a foundation for interpreting their functional roles in neural patterning.
History
DepositionJan 6, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 11, 2020Provider: repository / Type: Initial release
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / 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 / struct_asym / struct_conn / struct_conn_type / 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 / _chem_comp.name / _pdbx_struct_assembly_gen.asym_id_list / _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_seq_id / _pdbx_struct_conn_angle.ptnr2_label_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.conn_type_id / _struct_conn.id / _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_type.id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Oct 11, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_conn / struct_ncs_dom_lim
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Protocadherin-17
B: Protocadherin-17
C: Protocadherin-17
D: Protocadherin-17
hetero molecules


Theoretical massNumber of molelcules
Total (without water)204,43763
Polymers195,7934
Non-polymers8,64559
Water1086
1
A: Protocadherin-17
C: Protocadherin-17
hetero molecules


Theoretical massNumber of molelcules
Total (without water)102,32132
Polymers97,8962
Non-polymers4,42530
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Protocadherin-17
D: Protocadherin-17
hetero molecules


Theoretical massNumber of molelcules
Total (without water)102,11631
Polymers97,8962
Non-polymers4,22029
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)214.550, 105.838, 101.403
Angle α, β, γ (deg.)90.000, 101.038, 90.000
Int Tables number5
Space group name H-MC121
Space group name HallC2y
Symmetry operation#1: x,y,z
#2: -x,y,-z
#3: x+1/2,y+1/2,z
#4: -x+1/2,y+1/2,-z
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
31
41
12
22
32
42
13
23
33
43
14
24
34
44

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111LYSLYSPROPRO(chain A and ((resid 2 and (name N or name...AA2 - 292 - 29
121TYRTYRASPASP(chain A and ((resid 2 and (name N or name...AA47 - 10747 - 107
211LYSLYSPROPRO(chain B and ((resid 2 and (name N or name...BB2 - 292 - 29
221TYRTYRASPASP(chain B and ((resid 2 and (name N or name...BB47 - 10747 - 107
311LYSLYSPROPRO(chain C and ((resid 2 and (name N or name...CC2 - 292 - 29
321TYRTYRASPASP(chain C and ((resid 2 and (name N or name...CC47 - 10747 - 107
411LYSLYSPROPRO(chain D and ((resid 2 and (name N or name...DD2 - 292 - 29
421TYRTYRASPASP(chain D and ((resid 2 and (name N or name...DD47 - 10747 - 107
132ASPASPGLYGLY(chain A and (resseq 326:338 or (resid 339 and (name...AA326 - 376326 - 376
142PROPROLEULEU(chain A and (resseq 326:338 or (resid 339 and (name...AA394 - 446394 - 446
232ASPASPGLYGLY(chain B and (resseq 326:339 or (resid 340 and (name...BB326 - 376326 - 376
242PROPROLEULEU(chain B and (resseq 326:339 or (resid 340 and (name...BB394 - 446394 - 446
332ASPASPGLYGLY(chain C and (resseq 326:338 or (resid 339 and (name...CC326 - 376326 - 376
342PROPROLEULEU(chain C and (resseq 326:338 or (resid 339 and (name...CC394 - 446394 - 446
432ASPASPGLYGLY(chain D and (resseq 326:338 or (resid 339 and (name...DD326 - 376326 - 376
442PROPROLEULEU(chain D and (resseq 326:338 or (resid 339 and (name...DD394 - 446394 - 446
113SERSERILEILE(chain A and (resseq 219:245 or (resid 246 and (name...AA219 - 325219 - 325
213SERSERILEILE(chain B and (resseq 219:245 or (resid 246 and (name...BB219 - 325219 - 325
313SERSERILEILE(chain C and (resseq 219:245 or (resid 246 and (name...CC219 - 325219 - 325
413SERSERILEILE(chain D and (resseq 219:245 or (resid 246 and (name...DD219 - 325219 - 325
114ILEILEASPASP(chain A and (resseq 108:148 or (resid 149 and (name...AA108 - 218108 - 218
214ILEILEASPASP(chain B and (resseq 108:148 or (resid 149 and (name...BB108 - 218108 - 218
314ILEILEASPASP(chain C and (resseq 108:148 or (resid 149 and (name...CC108 - 218108 - 218
414ILEILEASPASP(chain D and (resseq 108:148 or (resid 149 and (name...DD108 - 218108 - 218

NCS ensembles :
ID
1
2
3
4

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Components

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Protein , 1 types, 4 molecules ABCD

#1: Protein
Protocadherin-17 / Protocadherin-68


Mass: 48948.176 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PCDH17, PCDH68, PCH68 / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: O14917

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Sugars , 7 types, 19 molecules

#2: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta- ...2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 570.542 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1a_1-5]/1-1-2/a4-b1_a6-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}[(6+1)][a-L-Fucp]{}}}LINUCSPDB-CARE
#3: 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: isolated from a genetically manipulated source
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
#4: Polysaccharide beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 732.682 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1221m-1a_1-5]/1-1-2-3/a4-b1_a6-d1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}[(6+1)][a-L-Fucp]{}}}LINUCSPDB-CARE
#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.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam 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
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}}LINUCSPDB-CARE
#6: Polysaccharide alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 894.823 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-6DManpb1-4DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/4,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5][a1221m-1a_1-5]/1-1-2-3-4/a4-b1_a6-e1_b4-c1_c6-d1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(6+1)][a-D-Manp]{}}}[(6+1)][a-L-Fucp]{}}}LINUCSPDB-CARE
#8: Sugar
ChemComp-MAN / alpha-D-mannopyranose / alpha-D-mannose / D-mannose / mannose


Type: D-saccharide, alpha linking / Mass: 180.156 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Formula: C6H12O6
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
#9: 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 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 , 2 types, 46 molecules

#7: Chemical...
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 40 / Source method: obtained synthetically / Formula: Ca
#10: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestN

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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: 3.09 Å3/Da / Density % sol: 60.25 %
Crystal growTemperature: 296 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 13%(w/v) PEG 4000 0.3M NaCl 0.1M MES pH 6.5 30% PEG 400 (v/v) added as cryoprotectant

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-E / Wavelength: 0.979 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jul 31, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979 Å / Relative weight: 1
ReflectionResolution: 3.7→40 Å / Num. obs: 22957 / % possible obs: 96.7 % / Redundancy: 3.5 % / Biso Wilson estimate: 92.4422118318 Å2 / CC1/2: 1 / Rmerge(I) obs: 0.211 / Rpim(I) all: 0.128 / Rrim(I) all: 0.248 / Net I/σ(I): 5.4
Reflection shellResolution: 3.7→4 Å / Redundancy: 3.4 % / Rmerge(I) obs: 0.735 / Mean I/σ(I) obs: 1.6 / Num. unique obs: 4468 / CC1/2: 0.71 / Rpim(I) all: 0.451 / Rrim(I) all: 0.866 / % possible all: 92.1

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Processing

Software
NameVersionClassification
PHENIX1.10.1_2155refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6VFQ

6vfq


Resolution: 3.71→19.94 Å / SU ML: 0.5312 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 32.69
RfactorNum. reflection% reflectionSelection details
Rfree0.3002 1133 4.97 %Random selection
Rwork0.2528 ---
obs0.2552 22795 96.33 %-
Solvent computationShrinkage radii: 0.8 Å / VDW probe radii: 1 Å
Displacement parametersBiso mean: 128.02 Å2
Refinement stepCycle: LAST / Resolution: 3.71→19.94 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12825 0 499 6 13330
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0079195968665713778
X-RAY DIFFRACTIONf_angle_d0.82110823641718462
X-RAY DIFFRACTIONf_chiral_restr0.05201801827262193
X-RAY DIFFRACTIONf_plane_restr0.004799187646352434
X-RAY DIFFRACTIONf_dihedral_angle_d11.00090987168315
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.71-3.87560.36881310.33552441X-RAY DIFFRACTION87.512759442
3.8756-4.07830.32071440.31432753X-RAY DIFFRACTION98.4035326087
4.0783-4.33140.30831470.28092747X-RAY DIFFRACTION98.33503228
4.3314-4.66190.298259078981360.2589752296022719X-RAY DIFFRACTION97.7739726027
4.6619-5.12380.2902125078061480.2390396411212757X-RAY DIFFRACTION98.0425244684
5.1238-5.84880.3437864585411450.240784155532748X-RAY DIFFRACTION97.7034785545
5.8488-7.30810.3045375783081390.2687139378312742X-RAY DIFFRACTION97.2325345933
7.3081-19.94294766370.2506936101491430.1979445067992755X-RAY DIFFRACTION95.6435643564
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)
11.39716615633-1.84632162257-0.6837841858573.28740341861-0.363199959561.47440256183-0.1843069738730.451009569920.597391401803-1.629529621480.819646742745-1.52898024578-1.409284497170.4998493196680.1788697975931.6517013215-0.3814604376910.4813617806780.903350641057-0.2849391391311.6872742705113.6702829197101.37286943144.3792637037
23.20346393077-0.679678401372-3.156483726931.292916225031.120374849083.24564811489-0.7221752984780.252936249693-0.483142226027-1.569686755840.6360494535460.545436030610.89017263689-0.4610963094350.005435510808931.56996311778-0.253934294755-0.2643250517090.8879872820760.2092821900511.20695878975-30.436361104-20.164792202333.6915998007
33.02813410207-1.78929918644-2.65069693182.59628143170.1606035114644.258624923880.0501411443551-0.2732440299250.6551798696070.285324517393-0.03235412538120.454079175854-0.329983514379-0.269958784670.005533503901610.89614345741-0.197234490351-0.05335944669891.09194829039-0.09858916319590.98509231302350.856943468286.771469511223.339554896
41.8748792016-0.089490890481-0.6019244201322.83802146947-1.364275249654.313755539980.01381930222390.2590369149760.1839529813611.01842735208-0.205746008320.2941305374250.01952005819780.0414375166034-0.01359863264721.09551602723-0.1348862032990.07022997450631.02986203471-0.06171652062921.05024643966-49.1648707668-1.36412578837-1.97417651353
52.420241397530.6694165789260.6047386699494.172139213213.158060437262.8173646741-0.0650089768211-0.4412235241930.207883198768-0.0587090856136-0.03648678971250.307328578623-0.371753317537-0.3820337880950.002466615026410.667745485832-0.04413015373060.03421244124020.756217500001-0.1090338711270.810721203933-1.2659166871862.888497225239.2244868823
63.169105876622.950860096540.5950181835455.12899402003-1.177415880971.38752022583-0.2846327854760.2681190792730.2507769812770.7121208108180.584797394910.251328344949-0.0225374873190.0212792131422-0.001199115407030.734516707043-0.02576276243580.05173354164410.876562951191-0.0002278519344640.744813217257-13.492105705319.578792185337.2656856096
72.943354376181.282304086370.06155346194261.43903206905-0.8164871965580.593445283197-0.5460408895560.87820577418-0.622807433152-0.6532249238980.443559801793-0.8071578094680.0418133621992-0.382572875421-0.008672688812520.970666731856-0.4057442894430.1826769815741.29280956972-0.2634868779371.0800042481122.87197267758.643070416315.0346521348
82.962041964070.7748085758711.013621537763.1815025121-0.3501783280383.12561765958-0.5918318216140.7194323428440.306324152617-0.6509293638260.160697839388-0.054326705924-0.2435769394670.4899865516730.01005190176651.14881546971-0.448458069772-0.1846301914771.278332574890.1231805509560.889808430042-16.609330923627.92242669264.45357259519
92.62225454962.12639269660.4684497297873.494103350631.515421151631.11082059213-0.1534533878020.2574826449290.303558841815-0.09773671517570.1386961058820.2428069641150.05287096975420.02164935226050.007776874704020.789969870418-0.114054304656-0.05206754167370.8552536355560.0649254595570.752311472624-34.343341420321.180456514624.4442638046
103.572743428910.1889587713210.6068559060121.426148655550.3514064023271.416652271070.294617766374-0.293112011269-0.380204158540.579568880056-0.365384390983-0.8350280124190.1714960898040.5181310857090.0001139400453950.778184449713-0.026780232079-0.08290163569060.972144072409-0.1308793114540.86068313351221.901422326860.022219045640.603352764
112.994409923723.12972164048-0.1714386787372.60108427709-0.6232131387082.011816914490.0454721799029-0.1161130147850.194234102322-0.140807884002-0.0683999300601-0.095185517423-1.360111305880.8448841377360.01938677788161.57213402001-0.4861684239380.08282177198711.43666924316-0.2609031399381.0870285517639.370349291193.531279795741.522954528
121.164527588872.03343996506-0.8767925858794.18144900211-0.8109983392740.330275943791-0.2992161049590.241634102149-0.764336667923-0.129815686850.632697918448-0.9422176824380.08187803800160.06046601365220.002765446299230.981193971887-0.1404441119220.04791693666841.03016777772-0.2908143758311.3190959021-8.721710869727.4673097214514.6100688525
132.82103087130.9040681028321.880693851961.46226402936-0.8049340591862.15158182525-0.1226560327470.255511204327-1.112074859070.09712539915370.31542297698-0.6264630575660.3523355604540.110187467844-0.00161540265851.45642174558-0.3392093241170.07396916283831.21601300736-0.2570836449251.79869029387-36.3218484205-27.8250926976.40124467617
140.6153666673060.6006317997231.336029683095.561873752841.098805808822.65476963588-0.8911152359810.6591294773550.749087560894-0.9783250020071.169912194541.26575038072-0.4924937609790.01458975114850.01526552412521.32476541443-0.592585570078-0.30223426071.299840705520.3545954588221.189440410366.0904167160972.787915282814.8523368893
152.63203116741-0.5961474984231.43319027721.26776940182-1.133467442121.35041909420.386951846204-0.7416421955960.536108800944-0.568095783257-0.3563228485870.389928153794-0.5394154088990.267855431472-0.003899298391471.89994909268-0.6748611051750.2599330729731.58285597086-0.05037956418641.5229589994433.1433043659112.20143111425.0037420208
160.380715101290.0919790555288-0.7140684426494.00241667566-0.8619837214323.6719581670.04617587474360.114554380633-0.274440002735-0.0302421136813-0.1111225585010.4231859389441.36892500207-0.4663675166930.007685825929451.31882633796-0.253959517633-0.04573221173161.05960762012-0.05429409467961.31275394669-54.4951002193-16.114213374718.4971825232
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain A and resid 2:122
2X-RAY DIFFRACTION2chain B and resid 2:101
3X-RAY DIFFRACTION3chain C and resid 1:97
4X-RAY DIFFRACTION4chain D and resid 1:107
5X-RAY DIFFRACTION5chain A and resid 123:223
6X-RAY DIFFRACTION6chain B and resid 102:221
7X-RAY DIFFRACTION7chain C and resid 98:216
8X-RAY DIFFRACTION8chain D and resid 108:218
9X-RAY DIFFRACTION9chain A and resid 224:344
10X-RAY DIFFRACTION10chain B and resid 222:303
11X-RAY DIFFRACTION11chain B and resid 304:446
12X-RAY DIFFRACTION12chain C and resid 217:344
13X-RAY DIFFRACTION13chain C and resid 345:449
14X-RAY DIFFRACTION14chain D and resid 219:328
15X-RAY DIFFRACTION15chain D and resid 329:447
16X-RAY DIFFRACTION16chain A and resid 345:446

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