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- PDB-4tnw: C. elegans glutamate-gated chloride channel (GluCl) in complex wi... -

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Basic information

Entry
Database: PDB / ID: 4tnw
TitleC. elegans glutamate-gated chloride channel (GluCl) in complex with Fab and POPC in a lipid-modulated conformation
Components
  • (Mouse monoclonal Fab fragment, ...) x 2
  • Avermectin-sensitive glutamate-gated chloride channel GluCl alpha
KeywordsTRANSPORT PROTEIN/IMMUNE SYSTEM / membrane protein / ligand-gated ion channel / neurotransmitter receptor / Cys-loop receptor / TRANSPORT PROTEIN-IMMUNE SYSTEM complex
Function / homology
Function and homology information


extracellularly glutamate-gated chloride channel activity / Neurotransmitter receptors and postsynaptic signal transmission / locomotion involved in locomotory behavior / glutamate binding / chloride transmembrane transport / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / transmembrane signaling receptor activity / protein complex oligomerization / postsynaptic membrane / neuron projection ...extracellularly glutamate-gated chloride channel activity / Neurotransmitter receptors and postsynaptic signal transmission / locomotion involved in locomotory behavior / glutamate binding / chloride transmembrane transport / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / transmembrane signaling receptor activity / protein complex oligomerization / postsynaptic membrane / neuron projection / synapse / identical protein binding / plasma membrane
Similarity search - Function
Glutamate gated chloride channel, transmembrane domain / Neurotransmitter-gated ion-channel transmembrane domain / Acetylcholine Binding Protein; Chain: A, / Neurotransmitter-gated ion-channel ligand-binding domain / Gamma-aminobutyric acid A receptor/Glycine receptor alpha / Neurotransmitter-gated ion-channel, conserved site / Neurotransmitter-gated ion-channels signature. / Neurotransmitter-gated ion-channel transmembrane domain / Neurotransmitter-gated ion-channel transmembrane region / Neurotransmitter-gated ion-channel transmembrane domain superfamily ...Glutamate gated chloride channel, transmembrane domain / Neurotransmitter-gated ion-channel transmembrane domain / Acetylcholine Binding Protein; Chain: A, / Neurotransmitter-gated ion-channel ligand-binding domain / Gamma-aminobutyric acid A receptor/Glycine receptor alpha / Neurotransmitter-gated ion-channel, conserved site / Neurotransmitter-gated ion-channels signature. / Neurotransmitter-gated ion-channel transmembrane domain / Neurotransmitter-gated ion-channel transmembrane region / Neurotransmitter-gated ion-channel transmembrane domain superfamily / Neuronal acetylcholine receptor / Neurotransmitter-gated ion-channel / Neurotransmitter-gated ion-channel ligand-binding domain / Neurotransmitter-gated ion-channel ligand-binding domain superfamily / Neurotransmitter-gated ion-channel ligand binding domain / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Distorted Sandwich / Immunoglobulins / Up-down Bundle / Immunoglobulin-like / Sandwich / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
Chem-POV / Glutamate-gated chloride channel alpha
Similarity search - Component
Biological speciesCaenorhabditis elegans (invertebrata)
Mus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.2 Å
AuthorsAlthoff, T. / Hibbs, R.E. / Banerjee, S. / Gouaux, E.
Funding support United States, Germany, 3items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)5 R01 GM100400 United States
German Research Foundation (DFG)AL 1725-1/1 Germany
National Institutes of Health/National Institute of Neurological Disorders and Stroke (NIH/NINDS)F32NS061404 United States
Citation
Journal: Nature / Year: 2014
Title: X-ray structures of GluCl in apo states reveal a gating mechanism of Cys-loop receptors.
Authors: Althoff, T. / Hibbs, R.E. / Banerjee, S. / Gouaux, E.
#1: Journal: Nature / Year: 2011
Title: Principles of activation and permeation in an anion-selective Cys-loop receptor.
Authors: Hibbs, R.E. / Gouaux, E.
History
DepositionJun 5, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 13, 2014Provider: repository / Type: Initial release
Revision 1.1Sep 3, 2014Group: Database references
Revision 1.2Sep 27, 2017Group: Author supporting evidence / Database references ...Author supporting evidence / Database references / Derived calculations / Other / Source and taxonomy / Structure summary
Category: citation / entity ...citation / entity / entity_src_gen / entity_src_nat / pdbx_audit_support / pdbx_database_status / pdbx_struct_oper_list
Item: _citation.journal_id_CSD / _entity.pdbx_description ..._citation.journal_id_CSD / _entity.pdbx_description / _entity_src_gen.pdbx_alt_source_flag / _entity_src_nat.pdbx_alt_source_flag / _pdbx_audit_support.funding_organization / _pdbx_database_status.pdb_format_compatible / _pdbx_struct_oper_list.symmetry_operation
Revision 1.3Dec 18, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.4Jul 29, 2020Group: Data collection / Derived calculations ...Data collection / Derived calculations / Refinement description / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / refine_hist / struct_conn / struct_site / struct_site_gen
Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _struct_conn.pdbx_role
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.5Sep 27, 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 / 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_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: Avermectin-sensitive glutamate-gated chloride channel GluCl alpha
B: Avermectin-sensitive glutamate-gated chloride channel GluCl alpha
C: Avermectin-sensitive glutamate-gated chloride channel GluCl alpha
D: Avermectin-sensitive glutamate-gated chloride channel GluCl alpha
E: Avermectin-sensitive glutamate-gated chloride channel GluCl alpha
F: Mouse monoclonal Fab fragment, heavy chain
G: Mouse monoclonal Fab fragment, heavy chain
H: Mouse monoclonal Fab fragment, heavy chain
I: Mouse monoclonal Fab fragment, heavy chain
K: Mouse monoclonal Fab fragment, light chain
L: Mouse monoclonal Fab fragment, light chain
N: Mouse monoclonal Fab fragment, light chain
O: Mouse monoclonal Fab fragment, light chain
P: Avermectin-sensitive glutamate-gated chloride channel GluCl alpha
Q: Avermectin-sensitive glutamate-gated chloride channel GluCl alpha
R: Avermectin-sensitive glutamate-gated chloride channel GluCl alpha
S: Avermectin-sensitive glutamate-gated chloride channel GluCl alpha
T: Avermectin-sensitive glutamate-gated chloride channel GluCl alpha
U: Mouse monoclonal Fab fragment, heavy chain
V: Mouse monoclonal Fab fragment, heavy chain
W: Mouse monoclonal Fab fragment, heavy chain
X: Mouse monoclonal Fab fragment, heavy chain
Y: Mouse monoclonal Fab fragment, heavy chain
Z: Mouse monoclonal Fab fragment, light chain
f: Mouse monoclonal Fab fragment, light chain
g: Mouse monoclonal Fab fragment, light chain
h: Mouse monoclonal Fab fragment, light chain
i: Mouse monoclonal Fab fragment, light chain
J: Mouse monoclonal Fab fragment, heavy chain
M: Mouse monoclonal Fab fragment, light chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)881,90456
Polymers870,85530
Non-polymers11,04926
Water0
1
A: Avermectin-sensitive glutamate-gated chloride channel GluCl alpha
B: Avermectin-sensitive glutamate-gated chloride channel GluCl alpha
C: Avermectin-sensitive glutamate-gated chloride channel GluCl alpha
D: Avermectin-sensitive glutamate-gated chloride channel GluCl alpha
E: Avermectin-sensitive glutamate-gated chloride channel GluCl alpha
F: Mouse monoclonal Fab fragment, heavy chain
G: Mouse monoclonal Fab fragment, heavy chain
H: Mouse monoclonal Fab fragment, heavy chain
I: Mouse monoclonal Fab fragment, heavy chain
K: Mouse monoclonal Fab fragment, light chain
L: Mouse monoclonal Fab fragment, light chain
N: Mouse monoclonal Fab fragment, light chain
O: Mouse monoclonal Fab fragment, light chain
J: Mouse monoclonal Fab fragment, heavy chain
M: Mouse monoclonal Fab fragment, light chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)440,22428
Polymers435,42815
Non-polymers4,79613
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
P: Avermectin-sensitive glutamate-gated chloride channel GluCl alpha
Q: Avermectin-sensitive glutamate-gated chloride channel GluCl alpha
R: Avermectin-sensitive glutamate-gated chloride channel GluCl alpha
S: Avermectin-sensitive glutamate-gated chloride channel GluCl alpha
T: Avermectin-sensitive glutamate-gated chloride channel GluCl alpha
U: Mouse monoclonal Fab fragment, heavy chain
V: Mouse monoclonal Fab fragment, heavy chain
W: Mouse monoclonal Fab fragment, heavy chain
X: Mouse monoclonal Fab fragment, heavy chain
Y: Mouse monoclonal Fab fragment, heavy chain
Z: Mouse monoclonal Fab fragment, light chain
f: Mouse monoclonal Fab fragment, light chain
g: Mouse monoclonal Fab fragment, light chain
h: Mouse monoclonal Fab fragment, light chain
i: Mouse monoclonal Fab fragment, light chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)441,68028
Polymers435,42815
Non-polymers6,25313
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)453.750, 192.870, 196.140
Angle α, β, γ (deg.)90.00, 92.27, 90.00
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11chain A and (resid 1:340 )
21chain B and (resid 1:340 )
31chain C and (resid 1:340 )
41chain D and (resid 1:340 )
51chain E and (resid 1:340 )
61chain P and (resid 1:340 )
71chain Q and (resid 1:340 )
81chain R and (resid 1:340 )
91chain S and (resid 1:340 )
101chain T and (resid 1:340 )
12chain F and (resid 1:120 )
22chain G and (resid 1:120 )
32chain H and (resid 1:120 )
42chain I and (resid 1:120 )
52chain J and (resid 1:120 )
62chain U and (resid 1:120 )
72chain V and (resid 1:120 )
82chain W and (resid 1:120 )
92chain X and (resid 1:120 )
102chain Y and (resid 1:120 )
13chain K and (resid 1:108 )
23chain L and (resid 1:108 )
33chain M and (resid 1:108 )
43chain N and (resid 1:108 )
53chain O and (resid 1:108 )
63chain Z and (resid 1:108 )
73chain f and (resid 1:108 )
83chain g and (resid 1:108 )
93chain h and (resid 1:108 )
103chain i and (resid 1:108 )

NCS domain segments:

Component-ID: 1

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11SERSERHISHISchain A and (resid 1:340 )AA1 - 3401 - 340
21SERSERHISHISchain B and (resid 1:340 )BB1 - 3401 - 340
31SERSERHISHISchain C and (resid 1:340 )CC1 - 3401 - 340
41SERSERHISHISchain D and (resid 1:340 )DD1 - 3401 - 340
51SERSERHISHISchain E and (resid 1:340 )EE1 - 3401 - 340
61SERSERHISHISchain P and (resid 1:340 )PN1 - 3401 - 340
71SERSERHISHISchain Q and (resid 1:340 )QO1 - 3401 - 340
81SERSERHISHISchain R and (resid 1:340 )RP1 - 3401 - 340
91SERSERHISHISchain S and (resid 1:340 )SQ1 - 3401 - 340
101SERSERHISHISchain T and (resid 1:340 )TR1 - 3401 - 340
12GLUGLUVALVALchain F and (resid 1:120 )FF1 - 1201 - 120
22GLUGLUVALVALchain G and (resid 1:120 )GG1 - 1201 - 120
32GLUGLUVALVALchain H and (resid 1:120 )HH1 - 1201 - 120
42GLUGLUVALVALchain I and (resid 1:120 )II1 - 1201 - 120
52GLUGLUVALVALchain J and (resid 1:120 )JCA1 - 1201 - 120
62GLUGLUVALVALchain U and (resid 1:120 )US1 - 1201 - 120
72GLUGLUVALVALchain V and (resid 1:120 )VT1 - 1201 - 120
82GLUGLUVALVALchain W and (resid 1:120 )WU1 - 1201 - 120
92GLUGLUVALVALchain X and (resid 1:120 )XV1 - 1201 - 120
102GLUGLUVALVALchain Y and (resid 1:120 )YW1 - 1201 - 120
13GLNGLNVALVALchain K and (resid 1:108 )KJ1 - 1081 - 108
23GLNGLNVALVALchain L and (resid 1:108 )LK1 - 1081 - 108
33GLNGLNVALVALchain M and (resid 1:108 )MDA1 - 1081 - 108
43GLNGLNVALVALchain N and (resid 1:108 )NL1 - 1081 - 108
53GLNGLNVALVALchain O and (resid 1:108 )OM1 - 1081 - 108
63GLNGLNVALVALchain Z and (resid 1:108 )ZX1 - 1081 - 108
73GLNGLNVALVALchain f and (resid 1:108 )fY1 - 1081 - 108
83GLNGLNVALVALchain g and (resid 1:108 )gZ1 - 1081 - 108
93GLNGLNVALVALchain h and (resid 1:108 )hAA1 - 1081 - 108
103GLNGLNVALVALchain i and (resid 1:108 )iBA1 - 1081 - 108

NCS ensembles :
ID
1
2
3

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Components

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Protein , 1 types, 10 molecules ABCDEPQRST

#1: Protein
Avermectin-sensitive glutamate-gated chloride channel GluCl alpha / Protein GLC-1


Mass: 39636.629 Da / Num. of mol.: 10 / Fragment: UNP RESIDUES 62-363,UNP RESIDUES 422-455
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Caenorhabditis elegans (invertebrata) / Gene: glc-1, CELE_F11A5.10, F11A5.10 / Plasmid: pFastBac1 / Cell line (production host): Sf9 / Organ (production host): ovary / Production host: Spodoptera frugiperda (fall armyworm) / Tissue (production host): ovary / References: UniProt: G5EBR3

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Antibody , 2 types, 20 molecules FGHIUVWXYJKLNOZfghiM

#2: Antibody
Mouse monoclonal Fab fragment, heavy chain


Mass: 24297.170 Da / Num. of mol.: 10 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse) / Cell line: Hybridoma
#3: Antibody
Mouse monoclonal Fab fragment, light chain


Mass: 23151.738 Da / Num. of mol.: 10 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse) / Cell line: Hybridoma

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Sugars , 2 types, 16 molecules

#4: 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.: 9 / Source method: obtained synthetically / 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
#8: Sugar
ChemComp-LMT / DODECYL-BETA-D-MALTOSIDE


Type: D-saccharide / Mass: 510.615 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C24H46O11 / Comment: detergent*YM

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Non-polymers , 3 types, 10 molecules

#5: Chemical
ChemComp-POV / (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate / POPC / POPC


Mass: 760.076 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C42H82NO8P / Comment: phospholipid*YM
#6: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#7: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3

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Details

Sequence detailsUNP G5EBR3 RESIDUES 364-421 ARE REPLACED WITH RESIDUES AGT

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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: 4.92 Å3/Da / Density % sol: 75.02 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 5.5
Details: 35-36% pentaerythritol propoxylate (5/4 PO/OH), 50 mM sodium citrate pH 5.5, 100 mM potassium chloride, Crystals were obtained after incubation of protein with lipid and detergent for 4 weeks at 4 degC

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.9793 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Nov 10, 2011
Details: Mirrors: bent cylinders, stripes of Pt, Rh and clear
RadiationMonochromator: Cryo-cooled double Si(111) crystal monochromator
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9793 Å / Relative weight: 1
ReflectionResolution: 3.2→58.7 Å / Num. obs: 256166 / % possible obs: 92.2 % / Redundancy: 1.92 % / Rmerge(I) obs: 0.133 / Net I/σ(I): 7.26
Reflection shellResolution: 3.2→3.24 Å / Redundancy: 1.6 % / Rmerge(I) obs: 0.638 / Mean I/σ(I) obs: 1.43 / % possible all: 83.5

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Processing

Software
NameVersionClassification
PHENIX(phenix.refine: 1.8.4_1496)refinement
ADSCdata collection
HKL-2000data reduction
HKL-2000data scaling
XDSdata reduction
XSCALEdata scaling
PHASERphasing
DMphasing
Cootmodel building
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3RHW

3rhw


Resolution: 3.2→58.7 Å / SU ML: 0.49 / Cross valid method: FREE R-VALUE / σ(F): 1.23 / Phase error: 27.36 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2506 21267 5 %Random
Rwork0.2269 ---
obs0.2281 425172 77.58 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 3.2→58.7 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms60274 0 544 0 60818
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00362464
X-RAY DIFFRACTIONf_angle_d0.73985197
X-RAY DIFFRACTIONf_dihedral_angle_d10.50722087
X-RAY DIFFRACTIONf_chiral_restr0.039864
X-RAY DIFFRACTIONf_plane_restr0.00310588
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A16369X-RAY DIFFRACTION8.489TORSIONAL
12B16369X-RAY DIFFRACTION8.489TORSIONAL
13C16369X-RAY DIFFRACTION8.489TORSIONAL
14D16369X-RAY DIFFRACTION8.489TORSIONAL
15E16369X-RAY DIFFRACTION8.489TORSIONAL
16P16369X-RAY DIFFRACTION8.489TORSIONAL
17Q16369X-RAY DIFFRACTION8.489TORSIONAL
18R16369X-RAY DIFFRACTION8.489TORSIONAL
19S16369X-RAY DIFFRACTION8.489TORSIONAL
110T16369X-RAY DIFFRACTION8.489TORSIONAL
21F5682X-RAY DIFFRACTION8.489TORSIONAL
22G5682X-RAY DIFFRACTION8.489TORSIONAL
23H5682X-RAY DIFFRACTION8.489TORSIONAL
24I5682X-RAY DIFFRACTION8.489TORSIONAL
25J5682X-RAY DIFFRACTION8.489TORSIONAL
26U5682X-RAY DIFFRACTION8.489TORSIONAL
27V5682X-RAY DIFFRACTION8.489TORSIONAL
28W5682X-RAY DIFFRACTION8.489TORSIONAL
29X5682X-RAY DIFFRACTION8.489TORSIONAL
210Y5682X-RAY DIFFRACTION8.489TORSIONAL
31K4826X-RAY DIFFRACTION8.489TORSIONAL
32L4826X-RAY DIFFRACTION8.489TORSIONAL
33M4826X-RAY DIFFRACTION8.489TORSIONAL
34N4826X-RAY DIFFRACTION8.489TORSIONAL
35O4826X-RAY DIFFRACTION8.489TORSIONAL
36Z4826X-RAY DIFFRACTION8.489TORSIONAL
37f4826X-RAY DIFFRACTION8.489TORSIONAL
38g4826X-RAY DIFFRACTION8.489TORSIONAL
39h4826X-RAY DIFFRACTION8.489TORSIONAL
310i4826X-RAY DIFFRACTION8.489TORSIONAL
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.2-3.23640.39715510.384510316X-RAY DIFFRACTION60
3.2364-3.27440.38865550.374810575X-RAY DIFFRACTION61
3.2744-3.31440.38585700.364610696X-RAY DIFFRACTION62
3.3144-3.35630.35785840.355811026X-RAY DIFFRACTION64
3.3563-3.40050.38015930.360311177X-RAY DIFFRACTION64
3.4005-3.44710.36745970.35611338X-RAY DIFFRACTION65
3.4471-3.49630.37146010.349511729X-RAY DIFFRACTION68
3.4963-3.54850.33756300.338211998X-RAY DIFFRACTION69
3.5485-3.60390.3376580.31812517X-RAY DIFFRACTION72
3.6039-3.6630.34346900.313112644X-RAY DIFFRACTION73
3.663-3.72610.33486790.317712845X-RAY DIFFRACTION74
3.7261-3.79390.31577000.305813212X-RAY DIFFRACTION76
3.7939-3.86680.3066860.279913352X-RAY DIFFRACTION77
3.8668-3.94580.28747180.269513573X-RAY DIFFRACTION79
3.9458-4.03150.26277260.262313967X-RAY DIFFRACTION80
4.0315-4.12530.26697520.235514214X-RAY DIFFRACTION82
4.1253-4.22840.24287590.21914386X-RAY DIFFRACTION83
4.2284-4.34270.2557650.222114547X-RAY DIFFRACTION84
4.3427-4.47050.22867850.202214775X-RAY DIFFRACTION85
4.4705-4.61470.21497720.194514748X-RAY DIFFRACTION85
4.6147-4.77960.19697860.18514959X-RAY DIFFRACTION86
4.7796-4.97080.21287780.175415039X-RAY DIFFRACTION87
4.9708-5.19690.19757940.167115050X-RAY DIFFRACTION87
5.1969-5.47080.20417950.174415083X-RAY DIFFRACTION87
5.4708-5.81320.21938030.193815001X-RAY DIFFRACTION87
5.8132-6.26160.21467900.208115017X-RAY DIFFRACTION87
6.2616-6.89090.26017790.215715051X-RAY DIFFRACTION87
6.8909-7.88590.24157940.200515014X-RAY DIFFRACTION87
7.8859-9.92770.18327940.16515092X-RAY DIFFRACTION87
9.9277-58.70.24087830.21714964X-RAY DIFFRACTION86
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)
11.29670.22051.31721.16620.53143.6366-0.133-0.15190.09250.1112-0.1371-0.1949-0.0890.3530.27030.57010.04240.00510.59140.09580.8052-64.3966-28.611914.3656
22.51160.2961.17481.21420.22782.01640.0758-0.305-0.22050.3777-0.0862-0.18060.04860.2625-0.0160.60890.0001-0.00070.61270.14410.6006-83.6926-28.856530.9184
33.69880.10921.79921.17850.08732.52460.2155-0.4664-0.01390.3388-0.1722-0.15720.07170.2055-0.07110.6822-0.06950.0870.64690.01420.5193-90.1195-4.801435.7933
42.4751-0.64272.00031.0123-0.66913.33350.0844-0.3820.13330.2946-0.0417-0.1811-0.03110.0725-0.04960.6646-0.12060.01860.6203-0.08860.7086-74.744310.269422.3798
51.6066-0.09221.46181.0952-0.35694.0817-0.0867-0.19850.13180.1433-0.1669-0.3281-0.14230.30840.24550.5284-0.0126-0.02180.46670.03650.7652-58.7761-4.46159.206
64.18761.4326-0.76781.0564-0.17291.45230.1846-0.9677-0.34680.4454-0.36680.18440.2654-0.050.18210.8255-0.16170.13010.78340.05760.786-133.1656-37.274347.5429
73.2481-1.9689-0.78822.49371.40352.58650.2288-0.23810.9935-0.02060.0676-0.0624-1.6496-0.4189-0.25921.75560.13910.35660.79770.02751.0962-121.705337.511936.092
81.6716-0.23220.53247.37750.52051.55070.2678-0.1473-0.38670.3081-0.06960.63440.5056-0.2347-0.1880.6628-0.0782-0.02190.66290.110.6266-80.6438-77.71772.9924
91.35121.0266-0.6523.7295-2.17672.52680.1489-0.07310.35660.2455-0.3564-0.4802-0.47670.33440.20670.7505-0.06550.07750.6975-0.02850.992-61.271344.3813-15.8701
102.2405-0.33-1.04221.59061.37653.53430.0459-0.05420.1863-0.3586-0.35230.5717-1.3853-0.83260.34271.15410.24730.05560.7759-0.05840.8388-134.765726.188639.3992
111.6285-0.37090.09564.77310.50832.84770.39280.2668-0.2847-0.7041-0.1020.16920.4868-0.0575-0.28980.70430.0809-0.07060.5540.0390.5839-72.5075-75.6646-12.3042
123.99272.1405-1.04371.2073-0.38370.5616-0.0558-0.6225-1.0550.375-0.2098-0.41460.3629-0.0410.23811.0073-0.06760.11160.74970.19381.0971-132.4167-52.497239.0958
131.59560.505-0.57263.9895-2.12481.62930.2125-0.02210.51210.6543-0.0041-0.3138-0.59870.0828-0.19950.8325-0.06590.16650.618-0.17440.9024-75.795853.4378-11.9882
142.46090.26762.18261.10550.45164.3274-0.01640.0460.0543-0.03720.02190.09310.0852-0.09410.00710.4714-0.00960.06940.68010.01290.4907-48.563999.655568.398
151.8811-0.00951.67391.0967-0.04653.5217-0.1155-0.02280.0554-0.1256-0.00370.1973-0.0634-0.23870.14560.4857-0.06220.02520.66960.01390.5395-51.448474.539270.5323
162.5789-0.18981.84521.3913-0.23112.5713-0.1733-0.060.0229-0.19370.07440.07040.149-0.26360.09060.5663-0.080.05540.5369-0.00520.4947-33.655663.38156.188
172.4356-0.37471.9320.736-0.32512.18050.2034-0.036-0.0898-0.1441-0.0983-0.03520.29440.0637-0.14370.65340.00760.04570.6849-0.03240.5701-19.938781.709545.0684
182.78970.19562.38871.13260.14832.88360.00170.01010.1136-0.0305-0.0721-0.0371-0.0148-0.02610.03220.4763-0.00580.05750.6164-0.01870.4892-28.9723104.155652.7473
191.1550.1490.283.7321-1.36592.42510.0508-0.1587-0.4785-0.18790.21340.52760.9911-0.651-0.19771.1184-0.2823-0.0360.93560.18810.8229-50.678527.461494.0602
202.1417-3.0474-1.55474.26362.14861.40830.02130.1908-0.121-0.3320.0422-0.47990.20160.314-0.07160.84510.09770.20470.8843-0.17971.108910.15935.531345.725
214.29-1.5842-3.97320.60351.62424.4838-0.29410.2325-0.41590.3161-0.1230.23930.3619-0.6080.42320.7784-0.03230.17870.8565-0.02550.6399-74.7198.5733114.3954
225.82582.7774-3.57421.3508-1.91062.76570.01690.36810.3561-0.05530.1685-0.0249-0.2479-0.1111-0.15260.6269-0.0860.18860.6393-0.02980.819222.5642110.710534.7104
231.38710.29980.30996.02690.51671.1273-0.4333-0.03940.75160.3178-0.0040.243-0.67370.04590.39751.1080.0625-0.39740.851-0.1080.9303-28.9342150.431677.6373
242.1411-2.1334-1.00583.0120.44090.7241-0.56550.0088-0.68010.2960.3040.35370.50770.25910.24710.88770.09160.14680.8144-0.13671.0984.735123.993358.0178
252.431-0.7094-2.54740.65541.34483.3860.4005-0.15620.2947-0.0244-0.07310.0442-0.5155-0.0018-0.28410.8571-0.02270.19020.83480.04270.7592-68.2823114.5443117.2431
261.31840.39960.32733.94670.71680.4805-0.4093-0.08460.51590.05150.156-0.6135-0.5736-0.25390.23271.2190.0235-0.38330.98240.03680.9901-12.3973152.510871.9797
270.2829-0.36380.27113.0839-1.90622.22380.1157-0.2991-0.44530.50510.11840.7080.3303-0.5187-0.25861.0999-0.14960.09221.240.28081.0691-58.14835.4368107.8596
284.69211.984-2.10830.9117-1.11781.4347-0.14690.1618-0.53-0.1859-0.0158-0.35310.0440.00950.14260.673-0.05480.17980.6244-0.09170.929631.626795.686635.0015
292.45090.31420.03932.15760.03132.3836-0.30.6852-0.8387-1.11580.1493-0.97850.61650.9810.15861.35330.17470.53161.0213-0.03261.3653-37.8883-26.9847-33.9331
302.91390.7424-0.58553.023-0.7292.4102-0.03160.9591-0.3978-1.21050.0856-0.6793-0.14580.3372-0.08731.1838-0.05910.26480.8970.01440.9307-38.898-11.1662-41.5215
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 340 )
2X-RAY DIFFRACTION2chain 'B' and (resid 1 through 340 )
3X-RAY DIFFRACTION3chain 'C' and (resid 1 through 340 )
4X-RAY DIFFRACTION4chain 'D' and (resid 1 through 340 )
5X-RAY DIFFRACTION5chain 'E' and (resid 1 through 340 )
6X-RAY DIFFRACTION6chain 'F' and (resid 1 through 221 )
7X-RAY DIFFRACTION7chain 'G' and (resid 1 through 221 )
8X-RAY DIFFRACTION8chain 'H' and (resid 1 through 221 )
9X-RAY DIFFRACTION9chain 'I' and (resid 1 through 221 )
10X-RAY DIFFRACTION10chain 'K' and (resid 1 through 210 )
11X-RAY DIFFRACTION11chain 'L' and (resid 1 through 210 )
12X-RAY DIFFRACTION12chain 'N' and (resid 1 through 210 )
13X-RAY DIFFRACTION13chain 'O' and (resid 1 through 210 )
14X-RAY DIFFRACTION14chain 'P' and (resid 1 through 340 )
15X-RAY DIFFRACTION15chain 'Q' and (resid 1 through 340 )
16X-RAY DIFFRACTION16chain 'R' and (resid 1 through 340 )
17X-RAY DIFFRACTION17chain 'S' and (resid 1 through 340 )
18X-RAY DIFFRACTION18chain 'T' and (resid 1 through 340 )
19X-RAY DIFFRACTION19chain 'U' and (resid 1 through 221 )
20X-RAY DIFFRACTION20chain 'V' and (resid 1 through 221 )
21X-RAY DIFFRACTION21chain 'W' and (resid 1 through 221 )
22X-RAY DIFFRACTION22chain 'X' and (resid 1 through 221 )
23X-RAY DIFFRACTION23chain 'Y' and (resid 1 through 221 )
24X-RAY DIFFRACTION24chain 'Z' and (resid 1 through 210 )
25X-RAY DIFFRACTION25chain 'f' and (resid 1 through 210 )
26X-RAY DIFFRACTION26chain 'g' and (resid 1 through 210 )
27X-RAY DIFFRACTION27chain 'h' and (resid 1 through 210 )
28X-RAY DIFFRACTION28chain 'i' and (resid 1 through 210 )
29X-RAY DIFFRACTION29chain 'J' and (resid 1 through 221 )
30X-RAY DIFFRACTION30chain 'M' and (resid 1 through 210 )

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