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- PDB-2xb6: Revisited crystal structure of Neurexin1beta-Neuroligin4 complex -

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Basic information

Entry
Database: PDB / ID: 2xb6
TitleRevisited crystal structure of Neurexin1beta-Neuroligin4 complex
Components
  • NEUREXIN-1-BETA
  • NEUROLIGIN-4, X-LINKED
KeywordsCELL ADHESION / ALPHA-BETA-HYDROLASE FOLD / AUTISM / CONFORMATIONAL REARRANGEMENT
Function / homology
Function and homology information


asymmetric, glutamatergic, excitatory synapse / protein-containing complex assembly involved in synapse maturation / symmetric, GABA-ergic, inhibitory synapse / regulation of trans-synaptic signaling by endocannabinoid, modulating synaptic transmission / positive regulation of presynaptic active zone assembly / cell-cell adhesion involved in synapse maturation / gephyrin clustering involved in postsynaptic density assembly / regulation of postsynaptic specialization assembly / protein complex involved in cell-cell adhesion / positive regulation of neuromuscular synaptic transmission ...asymmetric, glutamatergic, excitatory synapse / protein-containing complex assembly involved in synapse maturation / symmetric, GABA-ergic, inhibitory synapse / regulation of trans-synaptic signaling by endocannabinoid, modulating synaptic transmission / positive regulation of presynaptic active zone assembly / cell-cell adhesion involved in synapse maturation / gephyrin clustering involved in postsynaptic density assembly / regulation of postsynaptic specialization assembly / protein complex involved in cell-cell adhesion / positive regulation of neuromuscular synaptic transmission / guanylate kinase-associated protein clustering / type 1 fibroblast growth factor receptor binding / neuron to neuron synapse / neuroligin clustering involved in postsynaptic membrane assembly / postsynaptic density protein 95 clustering / cerebellar granule cell differentiation / postsynaptic membrane assembly / gamma-aminobutyric acid receptor clustering / presynaptic membrane assembly / synapse maturation / NMDA glutamate receptor clustering / maintenance of synapse structure / negative regulation of filopodium assembly / neuroligin family protein binding / vocal learning / positive regulation of synapse maturation / positive regulation of fibroblast growth factor receptor signaling pathway / regulation of postsynaptic density assembly / synaptic membrane adhesion / synaptic vesicle clustering / receptor localization to synapse / inhibitory synapse / regulation of grooming behavior / brainstem development / neuron cell-cell adhesion / neurexin family protein binding / negative regulation of excitatory postsynaptic potential / presynapse assembly / protein localization to synapse / regulation of synaptic vesicle cycle / vocalization behavior / calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules / neurotransmitter secretion / cell-cell junction organization / regulation of AMPA receptor activity / filopodium assembly / neuron maturation / acetylcholine receptor binding / Neurexins and neuroligins / positive regulation of synapse assembly / chloride ion binding / heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules / organ growth / adult behavior / positive regulation of protein kinase A signaling / regulation of NMDA receptor activity / social behavior / positive regulation of excitatory postsynaptic potential / calcium channel regulator activity / neuromuscular process controlling balance / excitatory synapse / regulation of presynapse assembly / synaptic vesicle endocytosis / endocytic vesicle / GABA-ergic synapse / prepulse inhibition / axonal growth cone / presynaptic active zone membrane / synapse assembly / cellular response to calcium ion / cell adhesion molecule binding / cerebellum development / positive regulation of synaptic transmission, glutamatergic / neuron projection morphogenesis / learning / positive regulation of synaptic transmission, GABAergic / postsynaptic density membrane / synapse organization / positive regulation of protein localization to plasma membrane / modulation of chemical synaptic transmission / neuromuscular junction / Schaffer collateral - CA1 synapse / establishment of protein localization / positive regulation of neuron projection development / neuron differentiation / circadian rhythm / neuron projection development / calcium-dependent protein binding / transmembrane signaling receptor activity / presynapse / signaling receptor activity / presynaptic membrane / positive regulation of peptidyl-serine phosphorylation / chemical synaptic transmission / scaffold protein binding / angiogenesis / nuclear membrane / vesicle / positive regulation of ERK1 and ERK2 cascade / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
Similarity search - Function
Neuroligin / Syndecan/Neurexin domain / Syndecan domain / Neurexin/syndecan/glycophorin C / putative band 4.1 homologues' binding motif / Laminin G domain / Laminin G domain profile. / Laminin G domain / Laminin G domain / Carboxylesterase type B, conserved site ...Neuroligin / Syndecan/Neurexin domain / Syndecan domain / Neurexin/syndecan/glycophorin C / putative band 4.1 homologues' binding motif / Laminin G domain / Laminin G domain profile. / Laminin G domain / Laminin G domain / Carboxylesterase type B, conserved site / Carboxylesterases type-B signature 2. / Carboxylesterase, type B / Carboxylesterase family / Jelly Rolls - #200 / Alpha/Beta hydrolase fold, catalytic domain / Concanavalin A-like lectin/glucanase domain superfamily / Alpha/Beta hydrolase fold / Jelly Rolls / Sandwich / Rossmann fold / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Neurexin-1-beta / Neuroligin-4, X-linked
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
RATTUS NORVEGICUS (Norway rat)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.6 Å
AuthorsLeone, P. / Comoletti, D. / Ferracci, G. / Conrod, S. / Garcia, S.U. / Taylor, P. / Bourne, Y. / Marchot, P.
CitationJournal: Embo J. / Year: 2010
Title: Structural Insights Into the Exquisite Selectivity of Neurexin-Neuroligin Synaptic Interactions
Authors: Leone, P. / Comoletti, D. / Ferracci, G. / Conrod, S. / Garcia, S.U. / Taylor, P. / Bourne, Y. / Marchot, P.
History
DepositionApr 7, 2010Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 23, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Refinement description / Version format compliance
Revision 1.2Apr 3, 2019Group: Data collection / Derived calculations ...Data collection / Derived calculations / Other / Source and taxonomy
Category: entity_src_gen / pdbx_database_proc ...entity_src_gen / pdbx_database_proc / pdbx_database_status / struct_biol / struct_conn
Item: _entity_src_gen.pdbx_host_org_cell_line / _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id ..._entity_src_gen.pdbx_host_org_cell_line / _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id / _entity_src_gen.pdbx_host_org_scientific_name / _entity_src_gen.pdbx_host_org_variant / _pdbx_database_status.recvd_author_approval / _struct_conn.pdbx_leaving_atom_flag
Revision 1.3Jul 29, 2020Group: Data collection / Derived calculations ...Data collection / Derived calculations / Other / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_database_status / pdbx_entity_nonpoly / pdbx_struct_conn_angle / struct_conn / struct_site / struct_site_gen
Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_database_status.status_code_sf / _pdbx_entity_nonpoly.name / _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.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.pdbx_dist_value / _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
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.4Dec 20, 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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: NEUROLIGIN-4, X-LINKED
B: NEUROLIGIN-4, X-LINKED
C: NEUREXIN-1-BETA
D: NEUREXIN-1-BETA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)174,39546
Polymers171,1964
Non-polymers3,20042
Water6,287349
1
A: NEUROLIGIN-4, X-LINKED
C: NEUREXIN-1-BETA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)87,34024
Polymers85,5982
Non-polymers1,74222
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: NEUROLIGIN-4, X-LINKED
D: NEUREXIN-1-BETA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)87,05622
Polymers85,5982
Non-polymers1,45820
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)136.307, 198.779, 85.896
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12C
22D

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1112A43 - 62
2112B43 - 62
1212A69 - 110
2212B69 - 110
1312A143 - 407
2312B143 - 407
1412A414 - 598
2412B414 - 598
1122C82 - 101
2122D82 - 101
1222C105 - 131
2222D105 - 131
1322C137 - 258
2322D137 - 258

NCS ensembles :
ID
1
2

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Components

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Protein , 2 types, 4 molecules ABCD

#1: Protein NEUROLIGIN-4, X-LINKED / / NEUROLIGIN-4 / NEUROLIGIN X / HNLX


Mass: 66230.203 Da / Num. of mol.: 2 / Fragment: CHOLINESTERASE-LIKE DOMAIN, RESIDUES 43-619
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Cell line (production host): HEK293 / Production host: HOMO SAPIENS (human) / References: UniProt: Q8N0W4
#2: Protein NEUREXIN-1-BETA / NEUREXIN I-BETA


Mass: 19367.713 Da / Num. of mol.: 2 / Fragment: LNS DOMAIN, RESIDUES 80-258
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) RATTUS NORVEGICUS (Norway rat) / Production host: ESCHERICHIA COLI BL21(DE3) (bacteria) / Variant (production host): Rosetta / References: UniProt: Q63373

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Sugars , 1 types, 4 molecules

#3: 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 / N-Acetylglucosamine


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 4
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 , 5 types, 387 molecules

#4: Chemical...
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 30 / Source method: obtained synthetically / Formula: C2H6O2
#5: Chemical
ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Cl
#6: Chemical ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID / MES (buffer)


Mass: 195.237 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#7: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ca
#8: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 349 / Source method: isolated from a natural source / Formula: H2O

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Details

Sequence detailsR561K IS A SPONTANEOUS MUTAGENESIS OF CDNA CLONE

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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: 3.2 Å3/Da / Density % sol: 59 % / Description: NONE
Crystal growpH: 6.3 / Details: 100MM MES PH6.3,10% PEG 20000, 2MM CACL2

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.9834
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Apr 25, 2008
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9834 Å / Relative weight: 1
ReflectionResolution: 2.6→30 Å / Num. obs: 72526 / % possible obs: 99.9 % / Observed criterion σ(I): 2 / Redundancy: 4.7 % / Rmerge(I) obs: 0.1 / Net I/σ(I): 10.7
Reflection shellResolution: 2.6→2.74 Å / Redundancy: 4.8 % / Rmerge(I) obs: 0.55 / Mean I/σ(I) obs: 2.8 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.5.0102refinement
MOSFLMdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2WQZ

2wqz


Resolution: 2.6→30 Å / Cor.coef. Fo:Fc: 0.935 / Cor.coef. Fo:Fc free: 0.917 / SU B: 16.938 / SU ML: 0.182 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.394 / ESU R Free: 0.258 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.236 3658 5 %RANDOM
Rwork0.204 ---
obs0.205 68827 99.99 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 20.92 Å2
Baniso -1Baniso -2Baniso -3
1-3.65 Å20 Å20 Å2
2---1.76 Å20 Å2
3----1.89 Å2
Refinement stepCycle: LAST / Resolution: 2.6→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11176 0 195 349 11720
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0150.02211634
X-RAY DIFFRACTIONr_bond_other_d0.0040.027785
X-RAY DIFFRACTIONr_angle_refined_deg1.5261.95715758
X-RAY DIFFRACTIONr_angle_other_deg1.168318926
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.25451411
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.22424.481540
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.316151804
X-RAY DIFFRACTIONr_dihedral_angle_4_deg21.4261554
X-RAY DIFFRACTIONr_chiral_restr0.0970.21717
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.02112884
X-RAY DIFFRACTIONr_gen_planes_other0.0020.022326
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.6861.57070
X-RAY DIFFRACTIONr_mcbond_other0.0961.52889
X-RAY DIFFRACTIONr_mcangle_it1.258211409
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it2.11934564
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it3.354.54349
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
11A2852tight positional0.040.05
12B2852tight positional0.040.05
21C812tight positional0.030.05
22D812tight positional0.030.05
11A3607medium positional0.080.5
12B3607medium positional0.080.5
21C1026medium positional0.10.5
22D1026medium positional0.10.5
11A2852tight thermal0.090.5
12B2852tight thermal0.090.5
21C812tight thermal0.080.5
22D812tight thermal0.080.5
11A3607medium thermal0.092
12B3607medium thermal0.092
21C1026medium thermal0.072
22D1026medium thermal0.072
LS refinement shellResolution: 2.6→2.67 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.351 265 -
Rwork0.359 4984 -
obs--100 %
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)
10.8677-0.0293-0.13062.18510.05741.0805-0.11920.1391-0.1969-0.05180.0834-0.00760.23470.06940.03580.13660.07880.02020.1308-0.04710.0513-39.651-48.213-33.839
21.8328-3.6763-0.8498.91210.36882.2703-0.2549-0.31160.00240.76330.2077-0.14580.24860.35390.04720.41290.0488-0.04520.3160.06030.0665-34.649-48.279-13.869
34.8499-2.21950.04374.23871.54242.684-0.039-0.0187-0.00440.67170.07-0.89970.16780.596-0.03090.27980.1487-0.2030.42050.08550.4133-15.516-49.82-21.942
41.3039-0.1031-0.5913.1141-1.04193.84280.0424-0.01560.05180.2893-0.0685-0.4499-0.15810.28950.0260.10450.0411-0.06160.0861-0.0010.0828-33.71-20.385-17.153
51.58320.6813-0.13082.71140.62051.8373-0.06570.0773-0.13650.26940.0750.44950.16820.0103-0.00930.10090.06420.05140.0729-0.00570.1379-53.204-39.876-23.182
60.5307-0.4025-0.17082.49840.50990.8918-0.0221-0.07030.00260.10680.01250.1510.03880.03880.00950.0474-0.04030.01010.08090.01610.0315-47.18624.922-16.964
70.7281.98330.832510.1591.27483.21980.06190.113-0.1108-1.2939-0.1239-0.0065-0.1539-0.05220.0620.57430.1211-0.07790.2862-0.02130.1736-40.22225.139-36.378
83.20971.53360.37295.81761.17353.05830.08660.1897-0.0174-0.56820.2364-1.3049-0.11390.4488-0.3230.1226-0.0760.17450.2573-0.01680.3721-22.0929.752-27.418
91.16980.32340.44544.49580.12772.82920.0680.1737-0.096-0.22690.0215-0.52710.08680.2318-0.08950.07030.01360.04950.0930.00720.0906-34.731-2.303-32.924
101.4663-1.2081-0.76843.91170.16642.41710.14440.1858-0.105-0.3544-0.21030.8329-0.0628-0.23490.06590.0722-0.0314-0.06950.1414-0.03110.2123-57.5513.728-28.059
114.50240.03441.07835.26051.83257.35940.1586-0.0104-0.3051-0.6232-0.43221.26890.5279-2.14670.27360.2256-0.1249-0.17020.6761-0.07360.3293-48.891-39.795-73.07
124.1095-0.47550.42912.12410.94285.1635-0.0542-0.19650.1272-0.2889-0.0966-0.013-0.2631-0.28520.15080.10120.05160.00920.0415-0.00190.0153-34.361-35.957-67.588
135.15561.1355-0.03383.63170.90115.2497-0.0612-0.26850.39910.9896-0.14120.85230.1926-1.38590.20240.53290.04470.22870.67320.01860.2155-53.93314.08523.037
142.880.8563-0.09842.57220.98686.3891-0.0475-0.0337-0.03850.56520.0663-0.31190.2603-0.1673-0.01880.39370.0453-0.03090.19030.04180.0634-39.19413.48517.037
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A44 - 110
2X-RAY DIFFRACTION1A143 - 291
3X-RAY DIFFRACTION1A340 - 373
4X-RAY DIFFRACTION1A449 - 472
5X-RAY DIFFRACTION1A561 - 582
6X-RAY DIFFRACTION2A111 - 142
7X-RAY DIFFRACTION3A292 - 339
8X-RAY DIFFRACTION4A374 - 448
9X-RAY DIFFRACTION4A583 - 598
10X-RAY DIFFRACTION5A473 - 560
11X-RAY DIFFRACTION6B44 - 110
12X-RAY DIFFRACTION6B143 - 291
13X-RAY DIFFRACTION6B340 - 373
14X-RAY DIFFRACTION6B449 - 472
15X-RAY DIFFRACTION6B561 - 582
16X-RAY DIFFRACTION7B111 - 142
17X-RAY DIFFRACTION8B292 - 339
18X-RAY DIFFRACTION9B374 - 448
19X-RAY DIFFRACTION9B583 - 598
20X-RAY DIFFRACTION10B473 - 560
21X-RAY DIFFRACTION11C82 - 94
22X-RAY DIFFRACTION11C231 - 258
23X-RAY DIFFRACTION12C95 - 200
24X-RAY DIFFRACTION13D82 - 94
25X-RAY DIFFRACTION13D231 - 258
26X-RAY DIFFRACTION14D95 - 200

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