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- PDB-5y2z: Crystal structure of human LGI1 EPTP-ADAM22 complex -

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Basic information

Entry
Database: PDB / ID: 5y2z
TitleCrystal structure of human LGI1 EPTP-ADAM22 complex
Components
  • Disintegrin and metalloproteinase domain-containing protein 22
  • Leucine-rich glioma-inactivated protein 1
KeywordsCELL ADHESION / epilepsy / synapse / ADAM / EPTP / WD40
Function / homology
Function and homology information


LGI-ADAM interactions / axon initial segment / negative regulation of cell adhesion / neurotransmitter receptor localization to postsynaptic specialization membrane / positive regulation of synaptic transmission / synaptic cleft / axon guidance / central nervous system development / postsynaptic density membrane / metalloendopeptidase activity ...LGI-ADAM interactions / axon initial segment / negative regulation of cell adhesion / neurotransmitter receptor localization to postsynaptic specialization membrane / positive regulation of synaptic transmission / synaptic cleft / axon guidance / central nervous system development / postsynaptic density membrane / metalloendopeptidase activity / integrin binding / neuron projection development / nervous system development / positive regulation of cell growth / cell adhesion / signaling receptor binding / axon / dendrite / glutamatergic synapse / endoplasmic reticulum / Golgi apparatus / proteolysis / extracellular space / extracellular region / membrane / plasma membrane / cytoplasm
Similarity search - Function
Leucine-rich glioma-inactivated , EPTP repeat / EAR / : / EPTP domain / EAR repeat profile. / ADAM cysteine-rich / Disintegrin domain / Echistatin / ADAM, cysteine-rich domain / ADAM Cysteine-Rich Domain ...Leucine-rich glioma-inactivated , EPTP repeat / EAR / : / EPTP domain / EAR repeat profile. / ADAM cysteine-rich / Disintegrin domain / Echistatin / ADAM, cysteine-rich domain / ADAM Cysteine-Rich Domain / Disintegrin, conserved site / Disintegrins signature. / Peptidase M12B, propeptide / Reprolysin family propeptide / Reprolysin domain, adamalysin-type / Reprolysin (M12B) family zinc metalloprotease / Disintegrin / Disintegrin domain profile. / Homologues of snake disintegrins / Disintegrin domain / Disintegrin domain superfamily / Peptidase M12B, ADAM/reprolysin / ADAM type metalloprotease domain profile. / EGF-like domain, extracellular / EGF-like domain / Cysteine-rich flanking region, C-terminal / Leucine rich repeat C-terminal domain / Collagenase (Catalytic Domain) / Collagenase (Catalytic Domain) / Metallopeptidase, catalytic domain superfamily / Leucine rich repeat / Leucine-rich repeat, typical subtype / Leucine-rich repeats, typical (most populated) subfamily / EGF-like domain signature 1. / EGF-like domain / Leucine-rich repeat / Leucine-rich repeat domain superfamily / Few Secondary Structures / Irregular / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Leucine-rich glioma-inactivated protein 1 / Disintegrin and metalloproteinase domain-containing protein 22
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.67 Å
AuthorsYamagata, A. / Fukai, S.
Funding support Japan, 2items
OrganizationGrant numberCountry
JST-CREST Japan
MEXT16H04749 Japan
CitationJournal: Nat Commun / Year: 2018
Title: Structural basis of epilepsy-related ligand-receptor complex LGI1-ADAM22.
Authors: Yamagata, A. / Miyazaki, Y. / Yokoi, N. / Shigematsu, H. / Sato, Y. / Goto-Ito, S. / Maeda, A. / Goto, T. / Sanbo, M. / Hirabayashi, M. / Shirouzu, M. / Fukata, Y. / Fukata, M. / Fukai, S.
History
DepositionJul 27, 2017Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0May 2, 2018Provider: repository / Type: Initial release
Revision 1.1Oct 31, 2018Group: Data collection / Structure summary / Category: struct / Item: _struct.title
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / 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_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 / _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.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_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_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.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 2.1Nov 22, 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
Revision 2.2Oct 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
A: Disintegrin and metalloproteinase domain-containing protein 22
C: Disintegrin and metalloproteinase domain-containing protein 22
E: Disintegrin and metalloproteinase domain-containing protein 22
G: Disintegrin and metalloproteinase domain-containing protein 22
I: Disintegrin and metalloproteinase domain-containing protein 22
K: Disintegrin and metalloproteinase domain-containing protein 22
B: Leucine-rich glioma-inactivated protein 1
D: Leucine-rich glioma-inactivated protein 1
F: Leucine-rich glioma-inactivated protein 1
H: Leucine-rich glioma-inactivated protein 1
J: Leucine-rich glioma-inactivated protein 1
L: Leucine-rich glioma-inactivated protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)583,48548
Polymers576,83912
Non-polymers6,64636
Water16,466914
1
A: Disintegrin and metalloproteinase domain-containing protein 22
B: Leucine-rich glioma-inactivated protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)97,4578
Polymers96,1402
Non-polymers1,3176
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
C: Disintegrin and metalloproteinase domain-containing protein 22
D: Leucine-rich glioma-inactivated protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)97,2958
Polymers96,1402
Non-polymers1,1556
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
E: Disintegrin and metalloproteinase domain-containing protein 22
F: Leucine-rich glioma-inactivated protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)97,0928
Polymers96,1402
Non-polymers9526
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
G: Disintegrin and metalloproteinase domain-containing protein 22
H: Leucine-rich glioma-inactivated protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)97,2548
Polymers96,1402
Non-polymers1,1146
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
I: Disintegrin and metalloproteinase domain-containing protein 22
J: Leucine-rich glioma-inactivated protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)97,2958
Polymers96,1402
Non-polymers1,1556
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
6
K: Disintegrin and metalloproteinase domain-containing protein 22
L: Leucine-rich glioma-inactivated protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)97,0928
Polymers96,1402
Non-polymers9526
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)83.579, 83.608, 293.543
Angle α, β, γ (deg.)86.40, 88.17, 59.95
Int Tables number1
Space group name H-MP1

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Components

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Protein , 2 types, 12 molecules ACEGIKBDFHJL

#1: Protein
Disintegrin and metalloproteinase domain-containing protein 22 / ADAM 22 / Metalloproteinase-disintegrin ADAM22-3 / Metalloproteinase-like / disintegrin-like / and ...ADAM 22 / Metalloproteinase-disintegrin ADAM22-3 / Metalloproteinase-like / disintegrin-like / and cysteine-rich protein 2


Mass: 55761.281 Da / Num. of mol.: 6 / Fragment: UNP RESIDUES 233-729
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ADAM22, MDC2 / Production host: Mammalia (mammals) / References: UniProt: Q9P0K1
#2: Protein
Leucine-rich glioma-inactivated protein 1 / Epitempin-1


Mass: 40378.527 Da / Num. of mol.: 6 / Fragment: UNP RESIDUES 224-557
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: LGI1, EPT, UNQ775/PRO1569 / Production host: Mammalia (mammals) / References: UniProt: O95970

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Sugars , 5 types, 12 molecules

#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.: 4
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 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.: 3
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
#6: 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
#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.: 2
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, 938 molecules

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


Mass: 40.078 Da / Num. of mol.: 24
Source method: isolated from a genetically manipulated source
Formula: Ca
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 914 / 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: 3.07 Å3/Da / Density % sol: 59.96 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6
Details: 10 % PEG 8000, 0.1 M zinc acetate, 0.1 M MES-Na (pH 6.0)

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL41XU / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Jul 15, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.67→50 Å / Num. obs: 177282 / % possible obs: 90.6 % / Redundancy: 3.8 % / Rsym value: 0.12 / Net I/σ(I): 9.9
Reflection shellResolution: 2.66→2.72 Å / Redundancy: 3.7 % / CC1/2: 0.702 / Rsym value: 0.53 / % possible all: 88.4

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Processing

Software
NameVersionClassification
PHENIX1.9_1692refinement
HKL-2000data reduction
HKL-2000data scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3G5C

3g5c


Resolution: 2.67→48.827 Å / SU ML: 0.41 / Cross valid method: FREE R-VALUE / σ(F): 2.04 / Phase error: 28.42
RfactorNum. reflection% reflection
Rfree0.2792 9033 5.1 %
Rwork0.2442 --
obs0.246 177245 90.49 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.67→48.827 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms38103 0 400 914 39417
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00539615
X-RAY DIFFRACTIONf_angle_d0.77753154
X-RAY DIFFRACTIONf_dihedral_angle_d12.63214426
X-RAY DIFFRACTIONf_chiral_restr0.0365837
X-RAY DIFFRACTIONf_plane_restr0.0046810
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.6661-2.69640.35943240.30475444X-RAY DIFFRACTION86
2.6964-2.72810.31473010.29345532X-RAY DIFFRACTION92
2.7281-2.76140.33942890.29185784X-RAY DIFFRACTION93
2.7614-2.79630.34332800.27785820X-RAY DIFFRACTION92
2.7963-2.83310.31842850.27575588X-RAY DIFFRACTION92
2.8331-2.87190.31133670.27285724X-RAY DIFFRACTION91
2.8719-2.9130.34693390.28635500X-RAY DIFFRACTION91
2.913-2.95640.2983020.28535626X-RAY DIFFRACTION90
2.9564-3.00260.32822730.27985589X-RAY DIFFRACTION90
3.0026-3.05180.30613000.27725353X-RAY DIFFRACTION88
3.0518-3.10450.34292260.27255579X-RAY DIFFRACTION87
3.1045-3.16090.313030.27424970X-RAY DIFFRACTION82
3.1609-3.22170.30192200.27775983X-RAY DIFFRACTION93
3.2217-3.28740.31973100.27085678X-RAY DIFFRACTION94
3.2874-3.35890.33632280.2665928X-RAY DIFFRACTION93
3.3589-3.4370.30943370.25345619X-RAY DIFFRACTION93
3.437-3.52290.28443410.24475645X-RAY DIFFRACTION91
3.5229-3.61820.26313540.23695659X-RAY DIFFRACTION91
3.6182-3.72460.28383020.2425450X-RAY DIFFRACTION90
3.7246-3.84480.27132780.23775255X-RAY DIFFRACTION85
3.8448-3.98210.28993070.23595642X-RAY DIFFRACTION90
3.9821-4.14150.25463620.22745752X-RAY DIFFRACTION94
4.1415-4.32990.23142910.21965763X-RAY DIFFRACTION93
4.3299-4.5580.24182660.2165776X-RAY DIFFRACTION92
4.558-4.84330.22763290.2025554X-RAY DIFFRACTION90
4.8433-5.21690.24083030.2075270X-RAY DIFFRACTION84
5.2169-5.74110.25813320.22225765X-RAY DIFFRACTION95
5.7411-6.57020.26933400.22815785X-RAY DIFFRACTION93
6.5702-8.27120.23753200.23455349X-RAY DIFFRACTION87
8.2712-48.83560.27832240.24095830X-RAY DIFFRACTION93
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)
12.47260.13860.80150.36570.12511.6131-0.1271-0.15980.06640.0056-0.0410.1018-0.154-0.20450.10420.25860.0252-0.01440.2389-0.00950.25220.1197-1.3998-0.5036
22.1963-1.8866-1.28762.67030.68342.1956-0.17430.0533-0.38670.0541-0.08890.12630.3483-0.09230.05580.2115-0.00960.04020.2181-0.05280.3121-5.6881-27.0929-98.2658
32.2151.71171.30782.82740.54562.3068-0.0871-0.11720.41990.0224-0.19490.0634-0.3362-0.11740.10930.19210.0239-0.03430.212-0.04330.2904-5.626931.9235-79.4392
41.5868-1.2958-0.25523.8846-1.072.0615-0.1396-0.0032-0.24740.1968-0.1613-0.2140.04580.32860.10760.2250.0241-0.01840.22870.04990.297350.9833-31.420818.3259
53.1949-0.4531-1.27730.53510.18031.743-0.14180.2865-0.0955-0.046-0.06060.18970.2207-0.24940.06910.2429-0.0364-0.00130.2789-0.02410.2667-41.6782-65.416-177.3244
61.07740.9828-0.12013.5359-1.3342.2521-0.07150.0340.17130.0035-0.2608-0.2563-0.08490.37920.07860.2037-0.044-0.04080.27270.03350.282410.5867-35.1211-195.701
71.77070.0004-0.2161.6869-0.64312.0742-0.1-0.0406-0.02640.15480.0176-0.0906-0.0247-0.03290.03580.30190.0293-0.0670.19780.0020.173122.9616-0.314539.7481
81.53620.02480.56412.1366-0.13831.64710.0455-0.10440.0680.1733-0.0620.02620.03480.01620.01440.24360.00030.04090.2256-0.02290.1596-18.1234-8.3281-57.8773
91.67970.1942-0.33321.77780.12521.97760.1027-0.0204-0.0788-0.1212-0.14030.0485-0.12830.11210.00720.22510.0224-0.04580.2197-0.02480.2013-17.947113.5986-119.9753
102.11430.05520.10691.55040.36991.25240.04170.28810.0443-0.17520.01590.1726-0.0258-0.0978-0.04880.27440.0131-0.0160.33330.03860.190341.6493-11.4459-22.3899
111.74820.17020.21342.2486-0.29561.8942-0.06340.04860.1761-0.25510.0724-0.0858-0.077-0.0695-0.0210.3375-0.0810.07130.33660.01080.2103-19.1922-66.3361-217.6574
121.7356-0.31880.07851.81840.51361.7901-0.0683-0.3559-0.08610.1280.04450.2071-0.0705-0.1348-0.03240.2215-0.00190.04250.33450.04390.2267-0.153-55.3764-155.4519
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A'
2X-RAY DIFFRACTION2chain 'C'
3X-RAY DIFFRACTION3chain 'E'
4X-RAY DIFFRACTION4chain 'G'
5X-RAY DIFFRACTION5chain 'I'
6X-RAY DIFFRACTION6chain 'K'
7X-RAY DIFFRACTION7chain 'B'
8X-RAY DIFFRACTION8chain 'D'
9X-RAY DIFFRACTION9chain 'F'
10X-RAY DIFFRACTION10chain 'H'
11X-RAY DIFFRACTION11chain 'J'
12X-RAY DIFFRACTION12chain 'L'

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