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- PDB-6vfu: Crystal structure of human protocadherin 19 EC1-EC4 -

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Basic information

Entry
Database: PDB / ID: 6vfu
TitleCrystal structure of human protocadherin 19 EC1-EC4
ComponentsProtocadherin-19
KeywordsCELL ADHESION / cadherin extracellular region / non-clustered delta2 family / protocadherin / homophilic / adhesion/recognition calcium-dependent adhesion molecule
Function / homology
Function and homology information


Formation of the nephric duct / homophilic cell-cell adhesion / cell adhesion / calcium ion binding / plasma membrane
Similarity search - Function
Cadherin, N-terminal / Cadherin-like / : / Cadherins / Cadherin conserved site / Cadherin domain signature. / Cadherin repeats. / Cadherin domain / Cadherin-like / Cadherins domain profile. ...Cadherin, N-terminal / Cadherin-like / : / Cadherins / Cadherin conserved site / Cadherin domain signature. / Cadherin repeats. / Cadherin domain / Cadherin-like / Cadherins domain profile. / Cadherin-like superfamily / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
NICKEL (II) ION / Protocadherin-19
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.5 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_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_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr2_symmetry / _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.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.ptnr1_symmetry / _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_conn.ptnr2_symmetry / _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
Revision 2.2Nov 13, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
C: Protocadherin-19
A: Protocadherin-19
B: Protocadherin-19
hetero molecules


Theoretical massNumber of molelcules
Total (without water)144,83342
Polymers141,3043
Non-polymers3,52939
Water1267
1
C: Protocadherin-19
A: Protocadherin-19
hetero molecules


Theoretical massNumber of molelcules
Total (without water)96,72530
Polymers94,2022
Non-polymers2,52328
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6770 Å2
ΔGint-130 kcal/mol
Surface area46340 Å2
MethodPISA
2
B: Protocadherin-19
hetero molecules

B: Protocadherin-19
hetero molecules


Theoretical massNumber of molelcules
Total (without water)96,21524
Polymers94,2022
Non-polymers2,01322
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation4_465y-1,x+1,-z1
Buried area4820 Å2
ΔGint-91 kcal/mol
Surface area44420 Å2
MethodPISA
Unit cell
Length a, b, c (Å)108.971, 108.971, 309.663
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number154
Space group name H-MP3221
Space group name HallP322"
Symmetry operation#1: x,y,z
#2: -y,x-y,z+2/3
#3: -x+y,-x,z+1/3
#4: x-y,-y,-z+1/3
#5: -x,-x+y,-z+2/3
#6: y,x,-z
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
31
12
22
32
13
23
33
14
24
34

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
111LEULEUASPASP(chain A and ((resid 101 and (name N or name...AB101 - 209101 - 209
211LEULEUASPASP(chain B and ((resid 101 and (name N or name...BC101 - 209101 - 209
311LEULEUASPASP(chain C and ((resid 101 and (name N or name...CA101 - 209101 - 209
112ASNASNASPASP(chain A and (resseq 211:221 or (resid 222 and (name...AB211 - 317211 - 317
212ASNASNASPASP(chain B and (resseq 211:221 or (resid 222 and (name...BC211 - 317211 - 317
312ASNASNASPASP(chain C and (resseq 211:221 or (resid 222 and (name...CA211 - 317211 - 317
113LEULEUPHEPHE(chain A and ((resid 1 and (name N or name...AB1 - 301 - 30
123ALAALASERSER(chain A and ((resid 1 and (name N or name...AB39 - 8839 - 88
133GLUGLUASPASP(chain A and ((resid 1 and (name N or name...AB90 - 10090 - 100
213LEULEUALAALA(chain B and ((resid 1 and (name N or name...BC1 - 311 - 31
223PHEPHESERSER(chain B and ((resid 1 and (name N or name...BC40 - 8840 - 88
233GLUGLUASPASP(chain B and ((resid 1 and (name N or name...BC90 - 10090 - 100
313LEULEUPHEPHE(chain C and ((resid 1 and (name N or name...CA1 - 301 - 30
323ALAALASERSER(chain C and ((resid 1 and (name N or name...CA39 - 8839 - 88
333GLUGLUASPASP(chain C and ((resid 1 and (name N or name...CA90 - 10090 - 100
114THRTHRLEULEU(chain A and (resseq 318:327 or (resid 328 and (name...AB318 - 327318 - 327
124LEULEUTHRTHR(chain A and (resseq 318:327 or (resid 328 and (name...AB334 - 423334 - 423
214THRTHRLEULEU(chain B and (resseq 318:327 or (resid 328 and (name...BC318 - 327318 - 327
224LEULEUTHRTHR(chain B and (resseq 318:327 or (resid 328 and (name...BC334 - 423334 - 423
314THRTHRLEULEU(chain C and (resseq 318:327 or (resid 328 and (name...CA318 - 327318 - 327
324LEULEUTHRTHR(chain C and (resseq 318:327 or (resid 328 and (name...CA334 - 423334 - 423

NCS ensembles :
ID
1
2
3
4

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Components

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Protein , 1 types, 3 molecules CAB

#1: Protein Protocadherin-19


Mass: 47101.223 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PCDH19, KIAA1313 / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: Q8TAB3

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Sugars , 4 types, 6 molecules

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


Type: oligosaccharide / Mass: 367.349 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
LFucpa1-6DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,2,1/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1a_1-5]/1-2/a6-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(6+1)][a-L-Fucp]{}}}LINUCSPDB-CARE
#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.: 1
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
#6: 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 , 4 types, 40 molecules

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


Mass: 40.078 Da / Num. of mol.: 27
Source method: isolated from a genetically manipulated source
Formula: Ca
#7: Chemical ChemComp-NI / NICKEL (II) ION


Mass: 58.693 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Formula: Ni
#8: Chemical
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Cl
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 7 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestN
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: 3.81 Å3/Da / Density % sol: 67.75 %
Crystal growTemperature: 296 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 7%(w/v) PEG 4000 0.2M NaCl 0.05M MES pH6.5 15% (v/v) 2R,3R-butanediol 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-C / Wavelength: 0.9792 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Jun 29, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9792 Å / Relative weight: 1
ReflectionResolution: 3.5→40 Å / Num. obs: 27770 / % possible obs: 99.9 % / Redundancy: 9.8 % / Biso Wilson estimate: 138.742878931 Å2 / CC1/2: 1 / Rmerge(I) obs: 0.14 / Rpim(I) all: 0.047 / Rrim(I) all: 0.15 / Net I/σ(I): 9.4
Reflection shellResolution: 3.5→3.71 Å / Redundancy: 10.4 % / Rmerge(I) obs: 2.5 / Mean I/σ(I) obs: 1.1 / Num. unique obs: 4378 / CC1/2: 0.72 / Rpim(I) all: 0.814 / Rrim(I) all: 2.6 / % possible all: 99.9

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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: 3.5→19.99 Å / SU ML: 0.57 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 35.89
RfactorNum. reflection% reflection
Rfree0.2915 1377 5 %
Rwork0.2648 --
obs0.2661 27515 99.8 %
Solvent computationShrinkage radii: 0.8 Å / VDW probe radii: 1 Å
Displacement parametersBiso mean: 193.423073948 Å2
Refinement stepCycle: LAST / Resolution: 3.5→19.99 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9737 0 176 7 9920
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0093566395274310249
X-RAY DIFFRACTIONf_angle_d0.79052901926513745
X-RAY DIFFRACTIONf_chiral_restr0.05378261504941617
X-RAY DIFFRACTIONf_plane_restr0.004886732036451824
X-RAY DIFFRACTIONf_dihedral_angle_d10.1093196986159
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.5-3.62440.41391360.40362550X-RAY DIFFRACTION99.6290801187
3.6244-3.76860.3813445814511360.3838780816792576X-RAY DIFFRACTION99.5960337863
3.7686-3.93890.3632621916751320.3525526600162560X-RAY DIFFRACTION99.7406446832
3.9389-4.14480.3276900392911340.3264821022782567X-RAY DIFFRACTION99.8521256932
4.1448-4.40190.3733173378831350.3025837686592602X-RAY DIFFRACTION99.8905109489
4.4019-4.73760.2956109659951350.2753158524072617X-RAY DIFFRACTION99.818643453
4.7376-5.20670.2788043866241390.244939346492592X-RAY DIFFRACTION99.817251462
5.2067-5.94280.3237048103251400.2556455682992634X-RAY DIFFRACTION99.963963964
5.9428-7.4230.3111547518751460.2870333339752664X-RAY DIFFRACTION99.9644254714
7.423-19.990.2212598020921440.2037723339052776X-RAY DIFFRACTION99.8290598291
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)
16.69877743211-0.870459308173-1.038026814452.856955104560.622875292971.40594983016-0.408665319659-0.570763871562-0.08129022233530.16964550963-0.0929322314868-0.189702709496-1.26874562242-0.4480415401640.01433430554972.14795308379-0.0404625033017-0.1000524968961.62760669080.06777039090952.00143407853-39.417972909536.15882495264.6870950697
23.14498046391-0.513907862516-1.779999656226.212588021621.802999000274.201285627390.5294752681121.342809846831.283879153950.08668086798051.01670504130.769278549826-0.43557934101-2.859633208340.01923735662491.191055419790.3397157800170.41506590452.41077032971.004896932772.1523949123-59.462279884885.0494541976-65.4368255562
35.25705006353-1.48500062452-2.046885582177.046054414582.928385301772.228946561480.5430160916650.889487308291-0.0598101870186-0.412321714147-0.181676131702-0.0858683516270.1804911265710.5910622621088.37723008902E-51.839951889460.3430660208320.02025965806352.26368498041-0.1560195171611.72868810597-47.474839620745.5103456795-69.3508470318
41.39925044266-0.1015703942530.06778254994730.0958987276911-1.336488627523.27663288791-0.0579482867595-0.1227560071820.1067411790890.106175841264-0.05990683882640.0369170647783-0.6323048024071.00784666765-0.0005638520967161.96342694462-0.132807309576-0.03675945528931.569587544570.04287612924631.7143363795-35.096905764937.992189095628.9034154877
50.9701222727560.3023191161622.241600542220.5079632998860.5052763582175.985383417460.07717101076460.2572076481370.05904956851830.016196210769-0.2579865123220.001108428190190.7401261819510.4268255385440.0002966682712791.912441453360.202378192720.007766365458371.66870641974-0.061211949871.60860997254-43.440296408929.1971605103-38.789505533
61.014835297740.719176796039-0.0352915834791-0.4863954014091.233144408143.92735312698-0.1355020709680.7503460966370.2392658229680.03278794835330.134442392914-0.207748048720.9827210138572.617921459650.009290564602932.103044726220.439732451964-0.1035018754222.38478318152-0.001048833627711.82015439423-39.717482535120.9321620088-76.7557503807
72.508698898830.20485523128-2.494094915322.604203236010.3195598238538.036038823250.4997498713360.2758711158780.456710865643-0.02237033574210.351123547728-0.05234365559370.197009139217-0.8114813932470.0001677040540611.353234283750.1322686249680.2585942116541.263399193990.206815110611.74306887224-56.941240497973.4552539529-27.05971482
8-0.4938721852111.295434942231.700445946410.463759714646-0.2850750418263.13781919220.344838912519-1.007405521790.6041899631050.01891475881570.580464231159-0.5923544866810.2789841967041.56338995569-0.01877372645361.452727049470.1200791457490.104678794392.69015678758-0.7139758411532.06157152912-49.144354952482.284864165521.1922844328
9-1.68657854782.372084101282.408536202470.0180425460807-1.65424684840.662726262050.1865013532360.00671534920121-0.4370407804830.795413382820.727047357683-0.4475200671270.225234219113-0.12188777210.00241758988512.128290067250.947803079334-0.5859147445254.22881693556-0.7682470110722.51108859455-34.866760939580.422150025867.3904994517
102.12953436883-0.5781705229291.209794977184.97491852373-4.586088637166.438620447180.202951994543-0.203823171408-0.203042401135-0.230872245493-0.0626514583635-0.2078470266040.4560954918210.523830365819-0.0004561586381751.47450956966-0.02345082412890.01126141054041.20608341295-0.006476817389861.46216563843-47.055044633452.1297880802-26.364257532
110.429075946141-0.450054012294-0.4201970697240.3216278802891.349559506273.05917146672-0.0201029285228-0.3777765188110.58839042523-0.370739055880.6216311681930.161665537215-0.538207223128-0.8915856691-0.01630571068212.086265652910.245523430179-0.03345073723162.128128045970.3300632199561.50386046497-56.799101608546.523183542823.7762649374
12-0.03366978925970.185203696416-0.622061689398-0.210658751751-0.9718994414422.390131692850.094509786515-0.01997403213020.2408401913830.2538579584970.3935969648380.0257465799752-1.39204281765-0.7937971279340.003959810900482.240044187870.3912547198240.008942400116592.18753944710.06268282458631.71687955708-60.408402641242.733785302252.1898394285
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain A and resid 1:74
2X-RAY DIFFRACTION2chain B and resid 1:96
3X-RAY DIFFRACTION3chain C and resid 1:98
4X-RAY DIFFRACTION4chain A and resid 75:212
5X-RAY DIFFRACTION5chain A and resid 213:348
6X-RAY DIFFRACTION6chain A and resid 349:428
7X-RAY DIFFRACTION7chain B and resid 97:204
8X-RAY DIFFRACTION8chain B and resid 205:308
9X-RAY DIFFRACTION9chain B and resid 309:423
10X-RAY DIFFRACTION10chain C and resid 99:212
11X-RAY DIFFRACTION11chain C and resid 213:242
12X-RAY DIFFRACTION12chain C and resid 243:428

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