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- PDB-5dzy: Protocadherin beta 8 extracellular cadherin domains 1-4 -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 5dzy
TitleProtocadherin beta 8 extracellular cadherin domains 1-4
ComponentsPcdhb8 protein
KeywordsCELL ADHESION / Cadherin / Dimer / Extracellular
Function / homology
Function and homology information


plasma membrane => GO:0005886 / homophilic cell adhesion via plasma membrane adhesion molecules / membrane => GO:0016020 / cell adhesion / calcium ion binding / identical protein binding / plasma membrane
Similarity search - Function
Protocadherin beta-5/6/8 / Cadherin, cytoplasmic C-terminal domain / Cadherin cytoplasmic C-terminal / Cadherin, N-terminal / Cadherin-like / Cadherins / Cadherin conserved site / Cadherin domain signature. / Cadherin repeats. / Cadherin domain ...Protocadherin beta-5/6/8 / Cadherin, cytoplasmic C-terminal domain / Cadherin cytoplasmic C-terminal / 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 / Pcdhb8 protein / Protocadherin beta-8
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.9 Å
AuthorsGoodman, K.M. / Bahna, F. / Mannepalli, S. / Honig, B. / Shapiro, L.
CitationJournal: Neuron / Year: 2016
Title: Structural Basis of Diverse Homophilic Recognition by Clustered alpha- and beta-Protocadherins.
Authors: Goodman, K.M. / Rubinstein, R. / Thu, C.A. / Bahna, F. / Mannepalli, S. / Ahlsen, G. / Rittenhouse, C. / Maniatis, T. / Honig, B. / Shapiro, L.
History
DepositionSep 26, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 4, 2016Provider: repository / Type: Initial release
Revision 1.1May 25, 2016Group: Database references
Revision 1.2Jun 1, 2016Group: Database references
Revision 1.3Nov 1, 2017Group: Author supporting evidence / Database references / Derived calculations
Category: citation / pdbx_struct_assembly_auth_evidence / pdbx_struct_oper_list
Item: _citation.journal_id_CSD / _pdbx_struct_oper_list.symmetry_operation
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 / _chem_comp.type / _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_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_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 2.1Sep 27, 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
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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Pcdhb8 protein
B: Pcdhb8 protein
C: Pcdhb8 protein
D: Pcdhb8 protein
E: Pcdhb8 protein
F: Pcdhb8 protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)290,67787
Polymers280,3986
Non-polymers10,28081
Water1086
1
A: Pcdhb8 protein
B: Pcdhb8 protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)97,85030
Polymers93,4662
Non-polymers4,38428
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
C: Pcdhb8 protein
D: Pcdhb8 protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)96,22228
Polymers93,4662
Non-polymers2,75626
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
E: Pcdhb8 protein
F: Pcdhb8 protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)96,60529
Polymers93,4662
Non-polymers3,14027
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)85.140, 137.070, 326.190
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
DetailsDimer by Analytical Ultracentrifugation

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Components

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Protein , 1 types, 6 molecules ABCDEF

#1: Protein
Pcdhb8 protein


Mass: 46732.941 Da / Num. of mol.: 6 / Fragment: UNP residues 29-446
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Pcdhb8 / Cell line (production host): HEK293F / Production host: Homo sapiens (human) / References: UniProt: A8E4K6, UniProt: Q91XZ2*PLUS

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Sugars , 6 types, 27 molecules

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


Type: oligosaccharide / Mass: 367.349 Da / Num. of mol.: 3
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
#3: Polysaccharide beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-alpha-D-mannopyranose- ...beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-alpha-D-mannopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-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: 1625.490 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGalpb1-4DGlcpNAcb1-4DManpa1-3[DGlcpNAcb1-4DManpa1-6]DManpb1-4DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/5,9,8/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5][a2112h-1b_1-5][a1221m-1a_1-5]/1-1-2-3-1-4-3-1-5/a4-b1_a6-i1_b4-c1_c3-d1_c6-g1_d4-e1_e4-f1_g4-h1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Galp]{}}}[(6+1)][a-D-Manp]{[(4+1)][b-D-GlcpNAc]{}}}}[(6+1)][a-L-Fucp]{}}}LINUCSPDB-CARE
#4: 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
#5: Polysaccharide alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-3)-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
DManpa1-3DManpb1-4DGlcpNAcb1-4[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_c3-d1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}}}[(6+1)][a-L-Fucp]{}}}LINUCSPDB-CARE
#6: Sugar
ChemComp-MAN / alpha-D-mannopyranose / alpha-D-mannose / D-mannose / mannose


Type: D-saccharide, alpha linking / Mass: 180.156 Da / Num. of mol.: 18
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
#8: 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, 60 molecules

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


Mass: 40.078 Da / Num. of mol.: 54 / Source method: obtained synthetically / Formula: Ca
#9: 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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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 3.39 Å3/Da / Density % sol: 63.76 %
Crystal growTemperature: 295 K / Method: vapor diffusion, hanging drop / pH: 8.5
Details: PEG550MME, PEG20000, calcium chloride, magnesium chloride, Tris, Bicine

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.98 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Aug 7, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98 Å / Relative weight: 1
ReflectionResolution: 2.9→30 Å / Num. obs: 53465 / % possible obs: 93.6 % / Redundancy: 3.1 % / Rmerge(I) obs: 0.12 / Net I/σ(I): 5.1
Reflection shellResolution: 2.9→3.67 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.9 / Mean I/σ(I) obs: 0.8 / % possible all: 94.3

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Processing

Software
NameVersionClassification
PHENIX1.9_1692refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5DZX

5dzx


Resolution: 2.9→29.986 Å / SU ML: 0.43 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 36.37 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2829 2714 5.08 %
Rwork0.2294 --
obs0.2321 53465 62.52 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.9→29.986 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms18551 0 575 6 19132
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00219477
X-RAY DIFFRACTIONf_angle_d0.51726724
X-RAY DIFFRACTIONf_dihedral_angle_d8.0247117
X-RAY DIFFRACTIONf_chiral_restr0.0223322
X-RAY DIFFRACTIONf_plane_restr0.0033483
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.9-2.95270.4833220.2807397X-RAY DIFFRACTION9
2.9527-3.00950.5468270.28517X-RAY DIFFRACTION12
3.0095-3.07080.3766340.2586637X-RAY DIFFRACTION15
3.0708-3.13750.3154430.2515818X-RAY DIFFRACTION19
3.1375-3.21050.3206540.2429976X-RAY DIFFRACTION23
3.2105-3.29060.3366690.24771203X-RAY DIFFRACTION28
3.2906-3.37950.337640.27411482X-RAY DIFFRACTION35
3.3795-3.47880.3432900.28131846X-RAY DIFFRACTION43
3.4788-3.59090.30091060.26942290X-RAY DIFFRACTION54
3.5909-3.7190.34291990.29173040X-RAY DIFFRACTION72
3.719-3.86760.35822210.28923896X-RAY DIFFRACTION92
3.8676-4.04330.30512200.27414219X-RAY DIFFRACTION99
4.0433-4.25590.29122270.24324195X-RAY DIFFRACTION99
4.2559-4.52170.29252310.22964173X-RAY DIFFRACTION98
4.5217-4.86940.26122140.20524156X-RAY DIFFRACTION97
4.8694-5.3570.24682360.18644179X-RAY DIFFRACTION97
5.357-6.12640.27252260.22544256X-RAY DIFFRACTION98
6.1264-7.69690.31691960.2444187X-RAY DIFFRACTION95
7.6969-29.98780.23242350.19614284X-RAY DIFFRACTION94
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
13.261-1.90772.77762.9946-1.88022.38120.4231-0.30270.6677-0.4397-0.4929-0.57360.05630.3015-0.05481.7459-0.120.16111.0539-0.06370.63937.9604-59.857734.4836
24.6941-3.17972.01195.5573-4.26496.9083-0.3378-0.0080.726-0.7030.0517-0.18620.3157-1.36610.30730.6845-0.1138-0.08541.1487-0.11040.56734.478-47.7302-100.0196
34.1614-2.42863.87081.5611-2.3463.6924-0.3976-0.45210.51751.54730.19120.00981.2217-0.57720.30231.90180.178-0.02871.4773-0.01150.6479-25.9405-32.8242-11.5213
40.7381-0.61050.26790.7108-0.92681.6657-0.24251.090.217-0.7630.3876-0.57340.33660.3030.03412.7799-1.16240.29032.7485-0.19230.4977-32.6894-33.0341-146.4996
53.85842.7672.29566.87913.7682.6801-0.276-0.27020.2045-0.14470.46620.1753-0.87230.6975-0.02331.0748-0.01630.0721.47310.21510.5595-60.5913-57.11-204.7009
62.48110.4955-0.51546.48962.91073.02450.039-0.024-0.12910.15630.00920.33710.22170.7327-0.03630.7527-0.2730.01541.30430.03010.486-57.4781-39.9622-70.2615
72.62370.122-0.78181.23751.91295.65710.0204-1.0391-0.1410.73410.17160.2011-0.0868-0.5851-0.18291.24540.16330.03051.19130.09760.4608-0.4218-53.9346-8.9181
84.2287-0.966-2.69534.16750.76627.5381-0.09870.2899-0.1205-0.29350.01520.23030.2978-0.79820.15980.4855-0.0392-0.03430.523-0.01540.31449.7539-57.5093-57.1895
94.91920.1242-1.9422.83851.9069.04340.0374-0.116-0.14040.48060.1086-0.03440.2671-0.0872-0.13530.442-0.15450.06650.52030.09260.4234-36.5669-31.8909-54.3961
101.15260.7521-0.06093.08030.93615.3288-0.39770.9252-0.2026-1.07140.2551-0.00641.12510.77140.07891.1083-0.10680.06741.5629-0.21480.5732-25.8534-35.6737-102.8899
111.1893-0.1198-1.36551.6043-1.38817.2055-0.18740.4438-0.0209-0.49650.0808-0.2895-0.01781.3885-0.02930.9304-0.09220.08831.5709-0.08730.4993-52.854-46.24-162.1782
123.869-1.3616-2.60443.0223-1.85288.0008-0.07780.08670.070.1399-0.0344-0.04770.65220.25190.08780.4648-0.1129-0.03350.6361-0.07380.3655-56.8035-51.8919-112.8409
132.9064-0.32080.72612.3602-1.09353.62880.01010.3404-0.0890.04410.01310.0548-0.53040.0484-0.0050.41530.2489-0.04660.6533-0.01330.38932.7268-37.6306-56.6642
142.5836-1.25552.90950.8263-1.36263.2888-0.2170.53740.25270.8691-0.4863-0.435-1.24921.42480.60081.4185-0.1001-0.33530.86280.16440.617220.1261-56.9467-7.5283
150.7139-0.7560.27291.7314-0.85761.5345-0.41830.3518-0.1285-0.65820.3428-0.1338-0.52591.04630.04420.7651-0.4851-0.14251.00280.0680.4767-41.2066-21.1967-103.9149
163.61960.22810.91483.43630.7791.87610.1333-0.128-0.14150.3399-0.11310.1466-0.01840.0276-0.12880.39730.1825-0.0290.720.02670.4239-16.6326-26.9841-53.6107
172.4471-0.7017-1.00740.5084-0.79734.7407-0.2594-0.2560.0758-0.00390.52970.4346-1.2671-0.12370.27170.4498-0.4808-0.16320.6957-0.07350.4654-61.2161-31.4421-114.6615
181.92471.95212.36351.96772.51153.0999-0.197-0.34770.3643-0.3818-0.59810.40530.2624-1.38660.78931.07920.1642-0.06020.9551-0.25090.5494-69.9293-58.5115-161.2576
194.52550.41611.18493.49530.63243.5154-0.22570.63840.2208-0.11020.43610.0582-2.1597-1.8827-0.25281.05520.2702-0.02980.95840.10370.52980.2076-24.4686-103.9735
202.57480.5401-0.02913.6608-1.70576.6695-0.24580.10360.04710.2724-0.12250.07261.93451.48560.17971.75110.2685-0.05570.771200.531132.4308-64.098339.5891
210.1628-0.45050.41530.7156-0.42841.0169-0.61551.2052-0.2327-0.62480.08450.1037-0.4886-0.0717-0.1642.125-1.2799-0.33533.05220.01850.5397-50.7466-17.3087-152.3583
220.73840.3329-0.44310.3384-0.88722.3727-0.9293-0.97940.74881.58920.5315-1.1882-0.56970.86350.1792.23050.9482-0.49582.2112-0.30510.7334-3.8565-26.7805-6.8891
233.74080.88911.2524.58861.19697.10340.1698-0.1940.31650.647-0.22880.0589-1.5385-0.2070.07681.1648-0.0354-0.00970.8065-0.0190.6312-66.2757-18.0772-67.5924
245.1754-0.0048-1.69463.75161.05662.9038-0.27070.1908-0.3364-0.34760.03570.22951.85250.04310.06751.29540.0252-0.07750.7682-0.09430.5278-80.8504-70.9738-208.3831
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and ((resseq 3:98))
2X-RAY DIFFRACTION2chain 'B' and ((resseq 2:98))
3X-RAY DIFFRACTION3chain 'C' and ((resseq 2:98))
4X-RAY DIFFRACTION4chain 'D' and ((resseq 2:98))
5X-RAY DIFFRACTION5chain 'E' and ((resseq 3:98))
6X-RAY DIFFRACTION6chain 'F' and ((resseq 1:98))
7X-RAY DIFFRACTION7chain 'A' and ((resseq 99:206))
8X-RAY DIFFRACTION8chain 'B' and ((resseq 99:206))
9X-RAY DIFFRACTION9chain 'C' and ((resseq 99:206))
10X-RAY DIFFRACTION10chain 'D' and ((resseq 99:206))
11X-RAY DIFFRACTION11chain 'E' and ((resseq 99:206))
12X-RAY DIFFRACTION12chain 'F' and ((resseq 99:206))
13X-RAY DIFFRACTION13chain 'A' and ((resseq 207:311))
14X-RAY DIFFRACTION14chain 'B' and ((resseq 207:311))
15X-RAY DIFFRACTION15chain 'C' and ((resseq 207:311))
16X-RAY DIFFRACTION16chain 'D' and ((resseq 207:311))
17X-RAY DIFFRACTION17chain 'E' and ((resseq 207:311))
18X-RAY DIFFRACTION18chain 'F' and ((resseq 207:311))
19X-RAY DIFFRACTION19chain 'A' and ((resseq 312:416))
20X-RAY DIFFRACTION20chain 'B' and ((resseq 312:415))
21X-RAY DIFFRACTION21chain 'C' and ((resseq 312:416))
22X-RAY DIFFRACTION22chain 'D' and ((resseq 312:413))
23X-RAY DIFFRACTION23chain 'E' and ((resseq 312:415))
24X-RAY DIFFRACTION24chain 'F' and ((resseq 312:415))

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