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- PDB-3saj: Crystal Structure of glutamate receptor GluA1 Amino Terminal Domain -

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Basic information

Entry
Database: PDB / ID: 3saj
TitleCrystal Structure of glutamate receptor GluA1 Amino Terminal Domain
ComponentsGlutamate receptor 1
KeywordsTRANSPORT PROTEIN / Rossmann fold / ion channel / membrane
Function / homology
Function and homology information


Cargo concentration in the ER / cellular response to amine stimulus / axonal spine / chemical synaptic transmission, postsynaptic / COPII-mediated vesicle transport / positive regulation of membrane potential / cellular response to ammonium ion / neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration / neuron spine / myosin V binding ...Cargo concentration in the ER / cellular response to amine stimulus / axonal spine / chemical synaptic transmission, postsynaptic / COPII-mediated vesicle transport / positive regulation of membrane potential / cellular response to ammonium ion / neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration / neuron spine / myosin V binding / Trafficking of AMPA receptors / dendritic spine membrane / response to arsenic-containing substance / cellular response to dsRNA / Synaptic adhesion-like molecules / long-term synaptic depression / beta-2 adrenergic receptor binding / protein kinase A binding / cellular response to peptide hormone stimulus / neuronal cell body membrane / spinal cord development / Activation of AMPA receptors / response to lithium ion / perisynaptic space / AMPA glutamate receptor activity / Trafficking of GluR2-containing AMPA receptors / immunoglobulin binding / AMPA glutamate receptor complex / neuronal action potential / excitatory synapse / ionotropic glutamate receptor complex / adenylate cyclase binding / cellular response to organic cyclic compound / asymmetric synapse / G-protein alpha-subunit binding / regulation of postsynaptic membrane potential / regulation of receptor recycling / Unblocking of NMDA receptors, glutamate binding and activation / long-term memory / glutamate receptor binding / positive regulation of synaptic transmission / response to electrical stimulus / glutamate-gated receptor activity / presynaptic active zone membrane / response to fungicide / cellular response to brain-derived neurotrophic factor stimulus / somatodendritic compartment / synapse assembly / dendrite membrane / ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / monoatomic ion transmembrane transport / dendritic shaft / response to cocaine / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / synaptic membrane / synaptic transmission, glutamatergic / PDZ domain binding / cellular response to amino acid stimulus / postsynaptic density membrane / regulation of synaptic plasticity / modulation of chemical synaptic transmission / neuromuscular junction / receptor internalization / synaptic vesicle membrane / response to organic cyclic compound / cerebral cortex development / response to peptide hormone / response to toxic substance / cellular response to growth factor stimulus / recycling endosome / small GTPase binding / recycling endosome membrane / G-protein beta-subunit binding / cell-cell junction / synaptic vesicle / presynapse / response to estradiol / presynaptic membrane / cell body / amyloid-beta binding / chemical synaptic transmission / postsynaptic membrane / early endosome membrane / postsynapse / scaffold protein binding / dendritic spine / postsynaptic density / early endosome / neuron projection / response to xenobiotic stimulus / protein domain specific binding / dendrite / neuronal cell body / glutamatergic synapse / synapse / endoplasmic reticulum membrane / positive regulation of gene expression / protein kinase binding / cell surface / endoplasmic reticulum
Similarity search - Function
Bacterial extracellular solute-binding proteins, family 3 / Solute-binding protein family 3/N-terminal domain of MltF / Ionotropic glutamate receptor, metazoa / Ligated ion channel L-glutamate- and glycine-binding site / : / Response regulator / Ligand-gated ion channel / Ionotropic glutamate receptor, L-glutamate and glycine-binding domain / Ligated ion channel L-glutamate- and glycine-binding site / Ionotropic glutamate receptor ...Bacterial extracellular solute-binding proteins, family 3 / Solute-binding protein family 3/N-terminal domain of MltF / Ionotropic glutamate receptor, metazoa / Ligated ion channel L-glutamate- and glycine-binding site / : / Response regulator / Ligand-gated ion channel / Ionotropic glutamate receptor, L-glutamate and glycine-binding domain / Ligated ion channel L-glutamate- and glycine-binding site / Ionotropic glutamate receptor / Eukaryotic homologues of bacterial periplasmic substrate binding proteins. / Receptor, ligand binding region / Receptor family ligand binding region / Periplasmic binding protein-like I / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Glutamate receptor 1
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å
AuthorsJin, R. / Zong, Y. / Yao, G. / Gu, S.
CitationJournal: Biochem.J. / Year: 2011
Title: Crystal structure of the glutamate receptor GluA1 N-terminal domain.
Authors: Yao, G. / Zong, Y. / Gu, S. / Zhou, J. / Xu, H. / Mathews, I.I. / Jin, R.
History
DepositionJun 2, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 22, 2011Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Aug 24, 2011Group: Database references
Revision 1.3Nov 12, 2014Group: Structure summary
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / 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_validate_close_contact / struct_asym / struct_conn / struct_ref_seq_dif / 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.pdbx_label_asym_id / _chem_comp.name / _chem_comp.type / _pdbx_struct_assembly_gen.asym_id_list / _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.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_comp_id / _struct_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Glutamate receptor 1
B: Glutamate receptor 1
C: Glutamate receptor 1
D: Glutamate receptor 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)183,90619
Polymers176,8534
Non-polymers7,05415
Water2,576143
1
A: Glutamate receptor 1
C: Glutamate receptor 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)92,1679
Polymers88,4262
Non-polymers3,7407
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8180 Å2
ΔGint50 kcal/mol
Surface area34110 Å2
MethodPISA
2
B: Glutamate receptor 1
D: Glutamate receptor 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)91,74010
Polymers88,4262
Non-polymers3,3138
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6830 Å2
ΔGint40 kcal/mol
Surface area34160 Å2
MethodPISA
Unit cell
Length a, b, c (Å)92.586, 94.421, 186.367
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

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Protein / Non-polymers , 2 types, 147 molecules ABCD

#1: Protein
Glutamate receptor 1 / / GluA1 / GluR-1 / AMPA-selective glutamate receptor 1 / GluR-A / GluR-K1 / Glutamate receptor ...GluA1 / GluR-1 / AMPA-selective glutamate receptor 1 / GluR-A / GluR-K1 / Glutamate receptor ionotropic / AMPA 1


Mass: 44213.219 Da / Num. of mol.: 4 / Fragment: N-terminal domain (UNP residues 22-392) / Source method: isolated from a natural source / Source: (natural) Rattus norvegicus (Norway rat) / References: UniProt: P19490
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 143 / Source method: isolated from a natural source / Formula: H2O

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Sugars , 4 types, 15 molecules

#2: 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.: 3
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
#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.: 8
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 alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-[alpha-D- ...alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 1235.105 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-2DManpa1-3DManpa1-6[DManpa1-3]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,7,6/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3-3-3/a4-b1_b4-c1_c3-d1_c6-e1_e3-f1_f2-g1WURCSPDB2Glycan 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-D-Manp]{[(3+1)][a-D-Manp]{[(2+1)][a-D-Manp]{}}}}}}}LINUCSPDB-CARE
#5: Sugar ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine


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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Experimental details

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Experiment

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

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Sample preparation

CrystalDensity Matthews: 2.3 Å3/Da / Density % sol: 46.59 %
Crystal growTemperature: 290 K / Method: evaporation / pH: 5
Details: 22% PEG3350, 0.2 M magnesium chloride, 0.1 M sodium acetate, pH 5.0, EVAPORATION, temperature 290K

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Data collection

DiffractionMean temperature: 200 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL9-2 / Wavelength: 1
DetectorType: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Feb 3, 2011
RadiationMonochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.5→93.184 Å / Num. obs: 57222 / % possible obs: 99.7 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 5.8 % / Rmerge(I) obs: 0.066 / Rsym value: 0.066 / Net I/σ(I): 10.3
Reflection shellResolution: 2.5→2.55 Å / Redundancy: 4.8 % / Rmerge(I) obs: 0.406 / Mean I/σ(I) obs: 3.5 / Num. unique all: 2255 / % possible all: 97.5

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Processing

Software
NameVersionClassification
MAR345dtbdata collection
MOLREPphasing
REFMAC5.5.0109refinement
MOSFLMdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.5→93.18 Å / Cor.coef. Fo:Fc: 0.931 / Cor.coef. Fo:Fc free: 0.893 / SU B: 23.93 / SU ML: 0.25 / Cross valid method: THROUGHOUT / ESU R: 0.991 / ESU R Free: 0.35 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : RESIDUAL ONLY
RfactorNum. reflection% reflectionSelection details
Rfree0.28569 2886 5.1 %RANDOM
Rwork0.21815 ---
obs0.2216 54093 99.24 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 70.83 Å2
Baniso -1Baniso -2Baniso -3
1--1.79 Å20 Å20 Å2
2---0.57 Å20 Å2
3---2.36 Å2
Refinement stepCycle: LAST / Resolution: 2.5→93.18 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11914 0 466 143 12523
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0150.02212694
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.7911.98617212
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.49351471
X-RAY DIFFRACTIONr_dihedral_angle_2_deg39.75823.921630
X-RAY DIFFRACTIONr_dihedral_angle_3_deg20.776152116
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.6331598
X-RAY DIFFRACTIONr_chiral_restr0.1110.21952
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.0219574
X-RAY DIFFRACTIONr_gen_planes_other
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_it1.3551.57333
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it2.138211858
X-RAY DIFFRACTIONr_scbond_it6.13835361
X-RAY DIFFRACTIONr_scangle_it8.1144.55350
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.498→2.563 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.333 211 -
Rwork0.238 3828 -
obs--96.47 %
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)
13.0134-0.8736-0.15141.7453-0.02092.0231-0.0025-0.081-0.0851-0.00070.03690.12030.012-0.0576-0.03450.1984-0.0065-0.01250.22110.00530.3181-1.5829-5.7382-5.2243
24.03452.3415-1.24593.5908-0.05521.3680.04890.10940.2473-0.55720.0993-0.3465-0.01860.1814-0.14820.34660.08020.08070.256-0.00780.29192.288919.8491-20.0067
38.0904-1.86-0.826125.81299.14357.6388-0.6557-1.30251.7966-0.21931.7018-1.9711-1.48231.446-1.04610.5334-0.11940.32660.4525-0.34320.932910.153732.6226-11.6647
45.1201-1.4834-0.20275.36032.46163.9583-0.1478-0.44910.13010.11250.15340.01150.1180.0771-0.00560.26280.04990.05570.1622-0.05870.3186-2.204326.624-6.1652
53.2427-0.1426-0.47452.3841-0.03981.193-0.073-0.1353-0.23520.20680.10160.6986-0.0487-0.2664-0.02870.18220.0103-0.00590.26160.05660.3786-12.2083-3.0114-7.0553
61.8329-1.05410.11735.2966-0.85810.93980.18810.08850.1086-0.52-0.12860.4837-0.1593-0.1765-0.05950.23290.0294-0.08030.2215-0.0180.3087-11.27377.6184-18.1423
72.76680.2713-0.07822.40490.24321.5829-0.0997-0.0154-0.0617-0.01260.113-0.1614-0.00810.1023-0.01330.2062-0.0024-0.01110.2274-0.00550.320252.2701-33.1199-17.4841
85.88160.3620.40125.8141-1.28623.0765-0.46290.4991-0.608-0.70040.63320.31970.08140.1246-0.17030.3223-0.21260.02670.2228-0.11540.20246.052-49.6342-43.3386
92.73250.91982.03091.04851.46663.96040.08240.2874-0.9186-0.17030.4892-0.95140.76220.6754-0.57160.4124-0.02140.2890.3029-0.33530.894163.5695-50.9214-34.5767
103.86781.33280.40283.5202-0.32771.8075-0.1713-0.17710.01810.29670.2361-0.59640.00890.2176-0.06490.2204-0.003-0.02980.3813-0.0390.389163.7344-29.982-18.6994
117.958-1.7916-2.83112.8921.64482.9772-0.0017-0.19960.4467-0.23890.1798-0.1463-0.32490.28-0.17810.2139-0.0428-0.06560.1899-0.01110.332252.9608-20.899-19.2066
124.48470.5794-0.2650.90870.63565.2353-0.38260.8555-0.6988-0.64280.5177-0.34850.20280.5195-0.13510.4703-0.29780.23130.5348-0.26720.334763.0033-38.6381-40.6487
132.826-0.0948-0.14621.8973-0.18262.1860.0610.0157-0.125-0.0564-0.0014-0.15130.020.1666-0.05950.21330.0012-0.02290.2545-0.0130.334528.6874-7.4735-9.7908
146.078-3.3783.43256.0599-3.5673.3063-0.17050.08040.79580.382-0.0384-0.21-0.5748-0.13860.20880.2786-0.00250.07880.13490.00190.307522.696620.3237-19.121
1514.31813.72971.276417.1155-5.435120.64360.26040.73912.149-1.5471-0.97210.9602-1.1059-1.35040.71170.41130.94190.43861.15810.58640.485416.467424.0014-35.5839
168.1655-5.24421.53544.4524-2.59542.91710.67191.5257-0.0822-0.5632-1.0377-0.34050.10920.78140.36580.21830.01960.17680.4756-0.0080.351436.05128.6644-29.0107
174.12850.1028-1.64540.5719-0.38493.1187-0.0279-0.6276-0.56660.182-0.0671-0.22960.06660.59760.0950.15790.0073-0.0370.24170.03420.416134.5906-7.3215-2.9514
182.50070.21830.77764.3555-1.92972.2695-0.04170.21720.57030.0604-0.1265-0.3917-0.58230.56290.16820.3417-0.1495-0.03390.3528-0.0080.436837.127911.0453-9.6989
192.96540.0427-0.01121.926-0.53472.3252-0.0785-0.00620.1315-0.07380.11410.20830.0112-0.1604-0.03560.1764-0.0048-0.03690.23660.03420.348221.7188-29.3403-18.3188
202.3702-0.0516-1.89530.38191.33516.2315-0.48730.5236-0.3368-0.0820.1130.11351.3488-0.30020.37440.7299-0.2799-0.09080.32840.01430.335322.086-42.926-41.821
215.69790.05980.61454.2451-1.71115.4795-0.31060.2710.0952-0.37230.109-0.12130.3601-0.20520.20160.3549-0.1275-0.03180.2674-0.01860.228732.1404-37.1464-49.6236
224.6166-0.5759-4.38780.56510.78797.6190.05150.71980.5323-0.41220.25070.2349-0.3918-0.8974-0.30220.3613-0.2482-0.30030.44370.20160.334314.6169-28.7716-44.5974
234.77870.2987-1.16292.6084-0.56262.5537-0.2798-0.44290.23460.07570.29840.35480.0305-0.7423-0.01860.19690.0118-0.03780.36680.02250.453512.7711-32.4693-16.1705
241.94220.6079-0.46051.0997-0.30922.6626-0.25120.3583-0.3186-0.56220.37440.26360.6033-0.6852-0.12310.428-0.2093-0.11180.34010.05350.422914.1328-42.1304-30.1555
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 104
2X-RAY DIFFRACTION2A105 - 150
3X-RAY DIFFRACTION3A151 - 178
4X-RAY DIFFRACTION4A179 - 232
5X-RAY DIFFRACTION5A233 - 310
6X-RAY DIFFRACTION6A311 - 372
7X-RAY DIFFRACTION7B2 - 108
8X-RAY DIFFRACTION8B109 - 200
9X-RAY DIFFRACTION9B201 - 255
10X-RAY DIFFRACTION10B256 - 298
11X-RAY DIFFRACTION11B299 - 328
12X-RAY DIFFRACTION12B329 - 371
13X-RAY DIFFRACTION13C2 - 103
14X-RAY DIFFRACTION14C104 - 157
15X-RAY DIFFRACTION15C158 - 178
16X-RAY DIFFRACTION16C179 - 265
17X-RAY DIFFRACTION17C266 - 308
18X-RAY DIFFRACTION18C309 - 371
19X-RAY DIFFRACTION19D1 - 102
20X-RAY DIFFRACTION20D103 - 129
21X-RAY DIFFRACTION21D130 - 179
22X-RAY DIFFRACTION22D180 - 255
23X-RAY DIFFRACTION23D256 - 304
24X-RAY DIFFRACTION24D305 - 371

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