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- PDB-3sn6: Crystal structure of the beta2 adrenergic receptor-Gs protein complex -

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Basic information

Entry
Database: PDB / ID: 3sn6
TitleCrystal structure of the beta2 adrenergic receptor-Gs protein complex
Components
  • (Guanine nucleotide-binding protein ...) x 3
  • Camelid antibody VHH fragment
  • Endolysin,Beta-2 adrenergic receptor
KeywordsSIGNALING PROTEIN/Hydrolase / seven transmembrane receptor / nanobody / G protein-coupled receptor / GPCR / signal transduction / G protein signaling / SIGNALING PROTEIN-Hydrolase complex
Function / homology
Function and homology information


sensory perception of chemical stimulus / mu-type opioid receptor binding / corticotropin-releasing hormone receptor 1 binding / G-protein activation / Activation of the phototransduction cascade / : / Glucagon-type ligand receptors / Thromboxane signalling through TP receptor / Sensory perception of sweet, bitter, and umami (glutamate) taste / G beta:gamma signalling through PI3Kgamma ...sensory perception of chemical stimulus / mu-type opioid receptor binding / corticotropin-releasing hormone receptor 1 binding / G-protein activation / Activation of the phototransduction cascade / : / Glucagon-type ligand receptors / Thromboxane signalling through TP receptor / Sensory perception of sweet, bitter, and umami (glutamate) taste / G beta:gamma signalling through PI3Kgamma / G beta:gamma signalling through CDC42 / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / Ca2+ pathway / Activation of G protein gated Potassium channels / Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) / Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits / G alpha (z) signalling events / Vasopressin regulates renal water homeostasis via Aquaporins / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / Adrenaline,noradrenaline inhibits insulin secretion / ADP signalling through P2Y purinoceptor 12 / G alpha (q) signalling events / G alpha (i) signalling events / desensitization of G protein-coupled receptor signaling pathway by arrestin / beta2-adrenergic receptor activity / norepinephrine-epinephrine-mediated vasodilation involved in regulation of systemic arterial blood pressure / positive regulation of mini excitatory postsynaptic potential / Thrombin signalling through proteinase activated receptors (PARs) / Activation of G protein gated Potassium channels / G-protein activation / G beta:gamma signalling through PI3Kgamma / Prostacyclin signalling through prostacyclin receptor / G beta:gamma signalling through PLC beta / ADP signalling through P2Y purinoceptor 1 / Thromboxane signalling through TP receptor / Presynaptic function of Kainate receptors / G beta:gamma signalling through CDC42 / Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits / Glucagon-type ligand receptors / alkylglycerophosphoethanolamine phosphodiesterase activity / positive regulation of cAMP-dependent protein kinase activity / Adrenaline,noradrenaline inhibits insulin secretion / G alpha (12/13) signalling events / G beta:gamma signalling through BTK / ADP signalling through P2Y purinoceptor 12 / norepinephrine binding / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / Adrenoceptors / heat generation / positive regulation of autophagosome maturation / Thrombin signalling through proteinase activated receptors (PARs) / positive regulation of AMPA receptor activity / Ca2+ pathway / G alpha (z) signalling events / Extra-nuclear estrogen signaling / activation of transmembrane receptor protein tyrosine kinase activity / G alpha (s) signalling events / beta-2 adrenergic receptor binding / negative regulation of smooth muscle contraction / G alpha (q) signalling events / positive regulation of lipophagy / photoreceptor outer segment membrane / response to psychosocial stress / G alpha (i) signalling events / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / negative regulation of multicellular organism growth / spectrin binding / Vasopressin regulates renal water homeostasis via Aquaporins / endosome to lysosome transport / adrenergic receptor signaling pathway / diet induced thermogenesis / neuronal dense core vesicle / positive regulation of protein kinase A signaling / adenylate cyclase binding / photoreceptor outer segment / D1 dopamine receptor binding / smooth muscle contraction / potassium channel regulator activity / positive regulation of bone mineralization / positive regulation of cAMP-mediated signaling / adenylate cyclase-activating adrenergic receptor signaling pathway / brown fat cell differentiation / regulation of sodium ion transport / bone resorption / viral release from host cell by cytolysis / cardiac muscle cell apoptotic process / ionotropic glutamate receptor binding / insulin-like growth factor receptor binding / activation of adenylate cyclase activity / receptor-mediated endocytosis / photoreceptor inner segment / adenylate cyclase activator activity / response to cold / peptidoglycan catabolic process / clathrin-coated endocytic vesicle membrane / G-protein beta/gamma-subunit complex binding / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / positive regulation of protein serine/threonine kinase activity / adenylate cyclase-activating G protein-coupled receptor signaling pathway / positive regulation of GTPase activity
Similarity search - Function
Transducin (heterotrimeric G protein), gamma chain / G Protein Gi Gamma 2 / GI Alpha 1, domain 2-like / GI Alpha 1, domain 2-like / Beta 2 adrenoceptor / Adrenoceptor family / Rhopdopsin 7-helix transmembrane proteins / Rhodopsin 7-helix transmembrane proteins / G-protein alpha subunit, group S / Lysozyme - #40 ...Transducin (heterotrimeric G protein), gamma chain / G Protein Gi Gamma 2 / GI Alpha 1, domain 2-like / GI Alpha 1, domain 2-like / Beta 2 adrenoceptor / Adrenoceptor family / Rhopdopsin 7-helix transmembrane proteins / Rhodopsin 7-helix transmembrane proteins / G-protein alpha subunit, group S / Lysozyme - #40 / YVTN repeat-like/Quinoprotein amine dehydrogenase / Endolysin T4 type / T4-type lysozyme / Glycoside hydrolase, family 24 / Lysozyme domain superfamily / Phage lysozyme / 7 Propeller / Methylamine Dehydrogenase; Chain H / Serpentine type 7TM GPCR chemoreceptor Srsx / G-alpha domain profile. / Guanine nucleotide binding protein (G-protein), alpha subunit / G protein alpha subunit, helical insertion / G-protein alpha subunit / G protein alpha subunit / G-protein, gamma subunit / G-protein gamma subunit domain profile. / GGL domain / G-protein gamma-like domain superfamily / G-protein gamma-like domain / GGL domain / G protein gamma subunit-like motifs / Guanine nucleotide-binding protein, beta subunit / G-protein, beta subunit / Lysozyme / G-protein coupled receptors family 1 signature. / G protein-coupled receptor, rhodopsin-like / GPCR, rhodopsin-like, 7TM / G-protein coupled receptors family 1 profile. / 7 transmembrane receptor (rhodopsin family) / Few Secondary Structures / Irregular / Lysozyme-like domain superfamily / G-protein beta WD-40 repeat / WD40 repeat, conserved site / P-loop containing nucleotide triphosphate hydrolases / Trp-Asp (WD) repeats signature. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily / Immunoglobulins / Up-down Bundle / Immunoglobulin-like / Sandwich / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Chem-P0G / Endolysin / Guanine nucleotide-binding protein G(s) subunit alpha isoforms short / Beta-2 adrenergic receptor / Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 / Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2
Similarity search - Component
Biological speciesBos taurus (cattle)
Rattus norvegicus (Norway rat)
Enterobacteria phage T4 (virus)
Homo sapiens (human)
Lama glama (llama)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.2 Å
AuthorsRasmussen, S.G.F. / DeVree, B.T. / Zou, Y. / Kruse, A.C. / Chung, K.Y. / Kobilka, T.S. / Thian, F.S. / Chae, P.S. / Pardon, E. / Calinski, D. ...Rasmussen, S.G.F. / DeVree, B.T. / Zou, Y. / Kruse, A.C. / Chung, K.Y. / Kobilka, T.S. / Thian, F.S. / Chae, P.S. / Pardon, E. / Calinski, D. / Mathiesen, J.M. / Shah, S.T.A. / Lyons, J.A. / Caffrey, M. / Gellman, S.H. / Steyaert, J. / Skiniotis, G. / Weis, W.I. / Sunahara, R.K. / Kobilka, B.K.
CitationJournal: Nature / Year: 2011
Title: Crystal structure of the beta2 adrenergic receptor-Gs protein complex
Authors: Rasmussen, S.G. / DeVree, B.T. / Zou, Y. / Kruse, A.C. / Chung, K.Y. / Kobilka, T.S. / Thian, F.S. / Chae, P.S. / Pardon, E. / Calinski, D. / Mathiesen, J.M. / Shah, S.T. / Lyons, J.A. / ...Authors: Rasmussen, S.G. / DeVree, B.T. / Zou, Y. / Kruse, A.C. / Chung, K.Y. / Kobilka, T.S. / Thian, F.S. / Chae, P.S. / Pardon, E. / Calinski, D. / Mathiesen, J.M. / Shah, S.T. / Lyons, J.A. / Caffrey, M. / Gellman, S.H. / Steyaert, J. / Skiniotis, G. / Weis, W.I. / Sunahara, R.K. / Kobilka, B.K.
History
DepositionJun 28, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 20, 2011Provider: repository / Type: Initial release
Revision 1.1Aug 1, 2012Group: Database references
Revision 2.0Jun 21, 2017Group: Advisory / Atomic model ...Advisory / Atomic model / Database references / Derived calculations / Source and taxonomy / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / entity / entity_name_com / entity_src_gen / pdbx_unobs_or_zero_occ_atoms / pdbx_unobs_or_zero_occ_residues / struct_conf / struct_conn / struct_ref / struct_ref_seq / struct_ref_seq_dif / struct_site_gen
Item: _atom_site.auth_seq_id / _atom_site_anisotrop.pdbx_auth_seq_id ..._atom_site.auth_seq_id / _atom_site_anisotrop.pdbx_auth_seq_id / _entity.pdbx_description / _entity.pdbx_mutation / _entity_name_com.name / _pdbx_unobs_or_zero_occ_atoms.auth_seq_id / _pdbx_unobs_or_zero_occ_residues.auth_seq_id / _struct_conf.beg_auth_seq_id / _struct_conf.end_auth_seq_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr2_auth_seq_id / _struct_ref.db_code / _struct_ref.pdbx_align_begin / _struct_ref.pdbx_db_accession / _struct_ref.pdbx_db_isoform / _struct_ref.pdbx_seq_one_letter_code / _struct_ref_seq.db_align_beg / _struct_ref_seq.db_align_end / _struct_ref_seq.pdbx_auth_seq_align_beg / _struct_ref_seq.pdbx_auth_seq_align_end / _struct_ref_seq.pdbx_db_accession / _struct_ref_seq.seq_align_beg / _struct_ref_seq.seq_align_end / _struct_site_gen.auth_seq_id
Revision 3.0Jul 12, 2017Group: Advisory / Atomic model ...Advisory / Atomic model / Database references / Derived calculations / Source and taxonomy / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / entity / entity_src_gen / pdbx_unobs_or_zero_occ_atoms / pdbx_unobs_or_zero_occ_residues / struct_conf / struct_conn / struct_ref_seq / struct_ref_seq_dif / struct_site_gen
Item: _atom_site.auth_seq_id / _atom_site_anisotrop.pdbx_auth_seq_id ..._atom_site.auth_seq_id / _atom_site_anisotrop.pdbx_auth_seq_id / _entity.pdbx_mutation / _entity_src_gen.gene_src_common_name / _entity_src_gen.pdbx_gene_src_gene / _pdbx_unobs_or_zero_occ_atoms.auth_seq_id / _pdbx_unobs_or_zero_occ_residues.auth_seq_id / _struct_conf.beg_auth_seq_id / _struct_conf.end_auth_seq_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr2_auth_seq_id / _struct_ref_seq.pdbx_auth_seq_align_end / _struct_ref_seq_dif.details / _struct_ref_seq_dif.pdbx_auth_seq_num / _struct_site_gen.auth_seq_id
Revision 3.1Dec 18, 2019Group: Advisory / Database references / Structure summary
Category: entity / pdbx_poly_seq_scheme ...entity / pdbx_poly_seq_scheme / pdbx_unobs_or_zero_occ_residues / struct_ref_seq / struct_ref_seq_dif
Item: _entity.pdbx_mutation / _pdbx_poly_seq_scheme.pdb_seq_num ..._entity.pdbx_mutation / _pdbx_poly_seq_scheme.pdb_seq_num / _pdbx_unobs_or_zero_occ_residues.auth_seq_id / _struct_ref_seq.pdbx_auth_seq_align_beg / _struct_ref_seq.pdbx_auth_seq_align_end / _struct_ref_seq_dif.details
Revision 3.2Sep 13, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _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: Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
B: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
G: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2
R: Endolysin,Beta-2 adrenergic receptor
N: Camelid antibody VHH fragment
hetero molecules


Theoretical massNumber of molelcules
Total (without water)164,4936
Polymers164,1225
Non-polymers3701
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area13280 Å2
ΔGint-61 kcal/mol
Surface area59370 Å2
Unit cell
Length a, b, c (Å)119.339, 64.555, 131.240
Angle α, β, γ (deg.)90.00, 91.67, 90.00
Int Tables number4
Space group name H-MP1211

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Components

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Guanine nucleotide-binding protein ... , 3 types, 3 molecules ABG

#1: Protein Guanine nucleotide-binding protein G(s) subunit alpha isoforms short / Adenylate cyclase-stimulating G alpha protein


Mass: 44370.168 Da / Num. of mol.: 1 / Mutation: G72S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bos taurus (cattle) / Gene: GNAS, GNAS1 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P04896
#2: Protein Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 / Transducin beta chain 1


Mass: 38744.371 Da / Num. of mol.: 1 / Mutation: M1Q
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Gnb1 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P54311
#3: Protein Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 / G gamma-I


Mass: 7563.750 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bos taurus (cattle) / Gene: GNG2 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P63212

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Protein / Antibody / Non-polymers , 3 types, 3 molecules RN

#4: Protein Endolysin,Beta-2 adrenergic receptor / Lysis protein / Lysozyme / Muramidase / Beta-2 adrenoreceptor / Beta-2 adrenoceptor


Mass: 58303.109 Da / Num. of mol.: 1 / Mutation: C54T,C97A,M96T,M98T,N187E
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Enterobacteria phage T4 (virus), (gene. exp.) Homo sapiens (human)
Gene: ADRB2, ADRB2R, B2AR / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P00720, UniProt: P07550, lysozyme
#5: Antibody Camelid antibody VHH fragment


Mass: 15140.742 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Lama glama (llama) / Production host: Escherichia coli (E. coli)
#6: Chemical ChemComp-P0G / 8-[(1R)-2-{[1,1-dimethyl-2-(2-methylphenyl)ethyl]amino}-1-hydroxyethyl]-5-hydroxy-2H-1,4-benzoxazin-3(4H)-one


Mass: 370.442 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C21H26N2O4

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Details

Compound detailsCHAIN R IS A FUSION PROTEIN WITH T4 LYSOZYME FUSED TO THE N TERMINUS OF THE BETA2 ADRENERGIC RECEPTOR
Sequence detailsSEQUENCE OF CHAIN A CORRESPONDS TO ISOFORM P04896-2

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 20

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Sample preparation

CrystalDensity Matthews: 3.08 Å3/Da / Density % sol: 60.05 %
Crystal growTemperature: 293 K / Method: lipidic cubic phase / pH: 6.5
Details: 350-450 mM potassium nitrate, 100 mM MES, 1 mM TCEP, 10 mM phosphonoformate, 0.01 mM BI167107, 18-22% PEG400. Crystals were grown in a 10:1 (w:w) MAG 7.7:cholesterol lipid mix. , pH 6.5, ...Details: 350-450 mM potassium nitrate, 100 mM MES, 1 mM TCEP, 10 mM phosphonoformate, 0.01 mM BI167107, 18-22% PEG400. Crystals were grown in a 10:1 (w:w) MAG 7.7:cholesterol lipid mix. , pH 6.5, Lipidic cubic phase, temperature 293K

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Data collection

Diffraction
IDMean temperature (K)Crystal-ID
1781
2781
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-B / Wavelength: 1.033 Å
Detector
TypeIDDetectorDateDetails
MARMOSAIC 300 mm CCD1CCDApr 15, 2011Mirrors
MARMOSAIC 300 mm CCD2CCDApr 24, 2011Mirrors
Radiation
IDMonochromatorProtocolMonochromatic (M) / Laue (L)Scattering typeWavelength-ID
1Si(111) double crystalSINGLE WAVELENGTHMx-ray1
2Si(111) double crystalSINGLE WAVELENGTHMx-ray1
Radiation wavelengthWavelength: 1.033 Å / Relative weight: 1
ReflectionResolution: 3.2→50 Å / Num. obs: 31685 / % possible obs: 91.2 % / Observed criterion σ(I): -3 / Redundancy: 6.5 % / Rmerge(I) obs: 0.156
Reflection shellResolution: 3.2→3.26 Å / Redundancy: 5 % / Rmerge(I) obs: 0.553 / Mean I/σ(I) obs: 1.81 / Num. unique all: 943 / % possible all: 53.9

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Processing

Software
NameVersionClassification
Blu-Icedata collection
PHASERphasing
PHENIX(phenix.refine: 1.7_650)refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entries 3P0G, 1AZT, 1GP2, 2RH1

3p0g

1azt

1gp2

2rh1


Resolution: 3.2→40.675 Å / SU ML: 0.39 / σ(F): 1.35 / Phase error: 29.18 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2772 1557 5.01 %
Rwork0.2255 --
obs0.2282 31073 92.82 %
Solvent computationShrinkage radii: 0.04 Å / VDW probe radii: 0.4 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 52.862 Å2 / ksol: 0.32 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--7.0864 Å2-0 Å21.9451 Å2
2--2.9389 Å2-0 Å2
3---1.7946 Å2
Refinement stepCycle: LAST / Resolution: 3.2→40.675 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10247 0 27 0 10274
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00310478
X-RAY DIFFRACTIONf_angle_d0.70914209
X-RAY DIFFRACTIONf_dihedral_angle_d12.3853748
X-RAY DIFFRACTIONf_chiral_restr0.0511617
X-RAY DIFFRACTIONf_plane_restr0.0031818
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.2-3.30330.36421000.30981768X-RAY DIFFRACTION62
3.3033-3.42130.4071160.31562263X-RAY DIFFRACTION79
3.4213-3.55820.34541220.30272565X-RAY DIFFRACTION89
3.5582-3.720.35031300.28442727X-RAY DIFFRACTION95
3.72-3.9160.26661370.2232829X-RAY DIFFRACTION98
3.916-4.16110.24571530.192855X-RAY DIFFRACTION99
4.1611-4.4820.20041700.16182846X-RAY DIFFRACTION100
4.482-4.93240.22651770.16632867X-RAY DIFFRACTION100
4.9324-5.64450.25621280.20762933X-RAY DIFFRACTION100
5.6445-7.10530.31491440.25252916X-RAY DIFFRACTION99
7.1053-40.67850.28561800.22972947X-RAY DIFFRACTION99
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)
10.04460.0208-0.00730.04520.03650.0267-0.03450.0356-0.01480.00780.0006-0.0596-0.0322-0.03160.00020.8753-0.33730.12931.17970.06010.409430.234819.3723-0.4144
20.08570.0213-0.02760.03120.01660.0121-0.07830.19290.0555-0.1361-0.14560.00430.01690.0829-0.00861.1377-0.1857-0.03531.6856-0.04660.499330.00249.05321.83
30.0597-0.02950.02890.05530.01210.0091-0.05870.21690.12440.1301-0.22120.03460.1090.0035-0.02580.95960.038-0.12911.2084-0.10770.113721.21570.71756.6139
40.2507-0.18870.10270.3236-0.0760.0646-0.26220.1443-0.043-0.95370.0299-0.15860.0329-0.1479-0.40280.3358-0.3428-0.50611.1527-0.1582-0.27916.03431.27751.5531
50.0271-0.0365-0.0290.07860.0196-0.0010.03380.45370.1213-0.41650.1146-0.16170.3791-0.02850.00451.1555-0.2514-0.04011.59180.09290.751717.177113.28552.6988
60.0998-0.016-0.09020.1775-0.1020.12630.11590.04320.0981-0.15570.04810.21380.2364-0.22610.05090.2822-0.2096-0.00420.3873-0.22020.082732.0134-9.852635.8037
70.1162-0.0149-0.02620.1106-0.00080.1048-0.08210.36540.15310.02160.08670.2189-0.1203-0.3335-0.02010.7877-0.1036-0.00120.76750.3310.714824.2068-30.332533.1899
80.6381-0.0355-0.08870.25550.02240.4513-0.3510.162-0.2835-0.05340.2430.38310.4395-0.3217-0.32560.1788-0.2098-0.08530.2470.04290.29538.51655.904846.2569
90.1967-0.32820.32490.5881-0.55580.55990.1898-0.1343-0.12810.17170.19520.2415-0.0795-0.17220.47560.35070.00160.04680.3936-0.25160.297739.114623.275676.4978
100.1465-0.0478-0.07780.2093-0.17540.16690.0899-0.0277-0.0068-0.0746-0.08890.08930.0940.2411-0.01540.3929-0.0507-0.02830.4331-0.16790.511447.95754.487239.6695
110.1799-0.03010.00030.0565-0.05330.0681-0.00790.0919-0.31660.07160.1298-0.21480.47390.09690.02710.42070.214-0.0939-0.6103-0.17260.374239.4588-8.379151.2956
12-0.0028-0.02360.00930.0995-0.01710.0525-0.0918-0.14020.03360.2285-0.06060.02370.4260.31370.00110.35740.2319-0.0537-0.09830.02920.259442.99873.36962.8324
130.44590.6093-0.2621.0895-0.40460.15610.18850.11510.3163-0.22730.26790.38520.08160.2650.55130.20510.03420.05440.2317-0.09150.112946.999617.060551.0398
140.3012-0.04370.25820.1657-0.11920.22740.22370.005-0.1844-0.14880.0154-0.0578-0.0723-0.03310.19820.2598-0.07390.02440.3163-0.02720.22645.682811.168338.0581
150.00860.0113-0.00520.0087-0.00610.0001-0.0298-0.0419-0.03650.07750.08530.26020.0294-0.05820.00010.70090.09190.07220.5493-0.00780.829636.321712.86276.9112
160.05770.0507-0.03420.1215-0.0940.101-0.20090.3106-0.15-0.0542-0.0226-0.1690.1105-0.03-0.21140.12290.0330.00570.4545-0.28380.367261.247113.661148.0792
170.0143-0.03010.00370.1258-0.00640.00260.121-0.27210.07630.30450.11880.0089-0.1638-0.1909-0.02570.29440.10430.13040.6771-0.10770.650220.921729.921770.9194
180.1084-0.026-0.00170.0859-0.01140.01970.0346-0.05530.06940.0627-0.0380.06860.00140.02660.02140.22750.13880.17930.07290.06880.422421.168625.563561.6441
190.03310.0043-0.0254-0.0023-0.0060.02260.06150.0129-0.0229-0.1648-0.048-0.05220.0112-0.00740.02140.31410.14920.01280.29210.13480.298317.37830.062151.4832
200.0077-0.00650.02110.0208-0.00910.04970.0566-0.0450.04320.12980.1410.0373-0.1025-0.12730.1297-0.00590.19950.03190.20720.14580.572114.592431.610763.1253
210.34860.08370.04150.1117-0.01080.0049-0.30430.2206-0.1695-0.21230.08690.0006-0.0418-0.0324-0.01350.2994-0.04940.01480.19630.01260.265523.702121.9156.5549
220.0492-0.00370.00430.00560.00840.0127-0.0466-0.02990.0056-0.0505-0.04480.04290.0592-0.0287-0.04440.2547-0.03610.02870.0985-0.05960.373125.607417.266163.4849
230.051-0.0064-0.02680.0497-0.03190.0754-0.0335-0.01230.002-0.0165-0.03670.01490.04630.01-0.10090.07420.06610.03630.35980.41010.16612.837827.140476.5361
240.02550.0080.0128-0.0017-0.00840.0218-0.0875-0.1045-0.04080.0181-0.02710.1146-0.0659-0.05790.01340.85230.0847-0.12971.32050.20841.173429.024542.6953-37.4182
250.0109-0.00510.00740.0017-0.00280-0.0764-0.05530.0183-0.02290.00230.0209-0.09650.00840.00010.7432-0.0880.0350.99870.31631.269332.710349.4511-45.5974
26-0.00060.003-0.00390.0068-0.0080.011-0.08240.01210.0313-0.0547-0.06310.036-0.0332-0.0182-0.00720.8350.05150.071.10970.25381.363724.595947.7641-52.5553
270.00970.0263-0.00650.0835-0.01550.0078-0.09030.01730.0007-0.0833-0.105-0.21930.0975-0.01430.02870.55240.06810.00091.11440.33570.337232.337634.004-46.3973
280.00150.0016-0.00110.0046-0.00790.0053-0.01020.0598-0.04190.04860.00840.03530.12120.04080.00020.50450.0101-0.04480.74460.10430.648146.476825.4891-39.9481
290.00670.0078-0.00270.0021-0.0055-0.0022-0.0742-0.0186-0.0179-0.0382-0.01990.0660.1326-0.0268-0.00020.42380.0450.14121.23660.13531.036638.992231.8979-35.7321
300.0566-0.00570.06230.0054-0.01150.07880.0753-0.05040.0435-0.04260.0368-0.025-0.04020.11910.10920.4246-0.16260.10130.6890.37990.450150.02431.3857-34.199
31-0.00310.00020.00170.0291-0.05370.0915-0.0046-0.0872-0.0647-0.0362-0.0203-0.02720.13730.0126-0.01810.6272-0.0063-0.35171.06270.41870.263248.071726.487-24.8843
320.01520.0018-0.00270.00680.00530.01860.13790.01050.0511-0.0550.09990.0538-0.1281-0.1280.02280.6986-0.18030.22511.52250.0840.895339.22335.0259-26.0115
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'R' and (resseq 30:60)
2X-RAY DIFFRACTION2chain 'R' and (resseq 61:102)
3X-RAY DIFFRACTION3chain 'R' and (resseq 103:146)
4X-RAY DIFFRACTION4chain 'R' and (resseq 147:264)
5X-RAY DIFFRACTION5chain 'R' and (resseq 265:366)
6X-RAY DIFFRACTION6chain 'A' and (resseq 9:88)
7X-RAY DIFFRACTION7chain 'A' and (resseq 89:186)
8X-RAY DIFFRACTION8chain 'A' and (resseq 187:394)
9X-RAY DIFFRACTION9chain 'B' and (resseq 1:24)
10X-RAY DIFFRACTION10chain 'B' and (resseq 25:94)
11X-RAY DIFFRACTION11chain 'B' and (resseq 95:161)
12X-RAY DIFFRACTION12chain 'B' and (resseq 162:222)
13X-RAY DIFFRACTION13chain 'B' and (resseq 223:289)
14X-RAY DIFFRACTION14chain 'B' and (resseq 290:340)
15X-RAY DIFFRACTION15chain 'G' and (resseq 5:23)
16X-RAY DIFFRACTION16chain 'G' and (resseq 24:62)
17X-RAY DIFFRACTION17chain 'N' and (resseq 1:17)
18X-RAY DIFFRACTION18chain 'N' and (resseq 18:51)
19X-RAY DIFFRACTION19chain 'N' and (resseq 52:60)
20X-RAY DIFFRACTION20chain 'N' and (resseq 61:91)
21X-RAY DIFFRACTION21chain 'N' and (resseq 92:108)
22X-RAY DIFFRACTION22chain 'N' and (resseq 109:121)
23X-RAY DIFFRACTION23chain 'N' and (resseq 122:128)
24X-RAY DIFFRACTION24chain 'L' and (resseq 1002:1024)
25X-RAY DIFFRACTION25chain 'L' and (resseq 1025:1039)
26X-RAY DIFFRACTION26chain 'L' and (resseq 1040:1059)
27X-RAY DIFFRACTION27chain 'L' and (resseq 1060:1080)
28X-RAY DIFFRACTION28chain 'L' and (resseq 1081:1092)
29X-RAY DIFFRACTION29chain 'L' and (resseq 1093:1106)
30X-RAY DIFFRACTION30chain 'L' and (resseq 1107:1122)
31X-RAY DIFFRACTION31chain 'L' and (resseq 1123:1134)
32X-RAY DIFFRACTION32chain 'L' and (resseq 1135:1160)

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