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- PDB-5v6y: Crystal structure of the human CLR:RAMP1 extracellular domain het... -

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Basic information

Entry
Database: PDB / ID: 5v6y
TitleCrystal structure of the human CLR:RAMP1 extracellular domain heterodimer with bound high-affinity and altered selectivity adrenomedullin variant
Components
  • ADM
  • Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor
KeywordsTRANSPORT PROTEIN / MEMBRANE PROTEIN / class B G protein-coupled receptor / GPCR / calcitonin family peptide / TRANSPORT PROTEIN - MEMBRANE PROTEIN complex
Function / homology
Function and homology information


adrenomedullin receptor binding / positive regulation of progesterone biosynthetic process / calcitonin gene-related peptide binding / vascular associated smooth muscle cell development / CGRP receptor complex / calcitonin gene-related peptide receptor signaling pathway / adrenomedullin binding / positive regulation of protein glycosylation / cellular response to sucrose stimulus / adrenomedullin receptor activity ...adrenomedullin receptor binding / positive regulation of progesterone biosynthetic process / calcitonin gene-related peptide binding / vascular associated smooth muscle cell development / CGRP receptor complex / calcitonin gene-related peptide receptor signaling pathway / adrenomedullin binding / positive regulation of protein glycosylation / cellular response to sucrose stimulus / adrenomedullin receptor activity / adrenomedullin receptor complex / neuron projection regeneration / adrenomedullin receptor signaling pathway / amylin receptor activity / calcitonin receptor activity / spongiotrophoblast layer development / vascular associated smooth muscle cell proliferation / calcitonin gene-related peptide receptor activity / amylin receptor signaling pathway / Calcitonin-like ligand receptors / branching involved in labyrinthine layer morphogenesis / positive regulation of vasculogenesis / regulation of systemic arterial blood pressure / regulation of the force of heart contraction / regulation of G protein-coupled receptor signaling pathway / regulation of urine volume / G protein-coupled receptor internalization / negative regulation of vascular permeability / negative regulation of vasoconstriction / positive regulation of heart rate / response to starvation / odontogenesis of dentin-containing tooth / G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger / androgen metabolic process / carbohydrate transmembrane transporter activity / maltose binding / maltose transport / developmental growth / maltodextrin transmembrane transport / vasculogenesis / animal organ regeneration / coreceptor activity / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / response to glucocorticoid / cellular response to hormone stimulus / positive regulation of vascular associated smooth muscle cell proliferation / cAMP-mediated signaling / neural tube closure / protein localization to plasma membrane / G protein-coupled receptor activity / female pregnancy / intracellular protein transport / response to insulin / adenylate cyclase-activating G protein-coupled receptor signaling pathway / hormone activity / receptor internalization / positive regulation of angiogenesis / calcium ion transport / protein transport / heart development / positive regulation of cytosolic calcium ion concentration / outer membrane-bounded periplasmic space / G alpha (s) signalling events / angiogenesis / cell population proliferation / response to lipopolysaccharide / cell surface receptor signaling pathway / lysosome / receptor complex / response to hypoxia / endosome / inflammatory response / positive regulation of apoptotic process / G protein-coupled receptor signaling pathway / negative regulation of cell population proliferation / signaling receptor binding / positive regulation of cell population proliferation / cell surface / endoplasmic reticulum / signal transduction / extracellular space / extracellular region / plasma membrane / cytoplasm
Similarity search - Function
Pro-adrenomedullin / GPCR, family 2, calcitonin gene-related peptide, type 1 receptor / Receptor activity modifying protein / RAMP domain superfamily / Receptor activity modifying family / GPCR, family 2, calcitonin receptor family / Calcitonin/adrenomedullin / Calcitonin / CGRP / IAPP family / G-protein coupled receptors family 2 signature 1. / Hormone receptor domain ...Pro-adrenomedullin / GPCR, family 2, calcitonin gene-related peptide, type 1 receptor / Receptor activity modifying protein / RAMP domain superfamily / Receptor activity modifying family / GPCR, family 2, calcitonin receptor family / Calcitonin/adrenomedullin / Calcitonin / CGRP / IAPP family / G-protein coupled receptors family 2 signature 1. / Hormone receptor domain / GPCR, family 2, extracellular hormone receptor domain / G-protein coupled receptors family 2 profile 1. / Domain present in hormone receptors / GPCR family 2, extracellular hormone receptor domain superfamily / G-protein coupled receptors family 2 signature 2. / GPCR, family 2, secretin-like, conserved site / GPCR, family 2, secretin-like / 7 transmembrane receptor (Secretin family) / GPCR, family 2-like / G-protein coupled receptors family 2 profile 2. / Maltose/Cyclodextrin ABC transporter, substrate-binding protein / Solute-binding family 1, conserved site / Bacterial extracellular solute-binding proteins, family 1 signature. / Bacterial extracellular solute-binding protein / Bacterial extracellular solute-binding protein
Similarity search - Domain/homology
alpha-maltose / Receptor activity-modifying protein 1 / Maltose/maltodextrin-binding periplasmic protein / Pro-adrenomedullin / Calcitonin gene-related peptide type 1 receptor
Similarity search - Component
Biological speciesEscherichia coli O157:H7 (bacteria)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å
AuthorsPioszak, A. / Booe, J.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM104251 United States
CitationJournal: Mol. Pharmacol. / Year: 2018
Title: Probing the Mechanism of Receptor Activity-Modifying Protein Modulation of GPCR Ligand Selectivity through Rational Design of Potent Adrenomedullin and Calcitonin Gene-Related Peptide Antagonists.
Authors: Booe, J.M. / Warner, M.L. / Roehrkasse, A.M. / Hay, D.L. / Pioszak, A.A.
History
DepositionMar 17, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 31, 2018Provider: repository / Type: Initial release
Revision 1.1Feb 7, 2018Group: Database references / Category: citation / citation_author
Item: _citation.journal_abbrev / _citation.pdbx_database_id_PubMed ..._citation.journal_abbrev / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.name
Revision 1.2Mar 14, 2018Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title
Revision 1.3Jan 1, 2020Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 2.0Mar 4, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / Derived calculations / Polymer sequence / Source and taxonomy / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / entity / entity_name_com / entity_poly / entity_poly_seq / entity_src_gen / pdbx_entity_nonpoly / pdbx_entity_src_syn / pdbx_nonpoly_scheme / pdbx_poly_seq_scheme / pdbx_struct_assembly_gen / struct_asym / struct_conn / struct_ref_seq_dif
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.group_PDB / _atom_site.label_alt_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.label_seq_id / _atom_site.occupancy / _atom_site.type_symbol / _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _atom_site_anisotrop.pdbx_auth_asym_id / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_auth_comp_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_alt_id / _atom_site_anisotrop.pdbx_label_asym_id / _atom_site_anisotrop.pdbx_label_atom_id / _atom_site_anisotrop.pdbx_label_comp_id / _atom_site_anisotrop.pdbx_label_seq_id / _atom_site_anisotrop.type_symbol / _entity_name_com.name / _entity_poly.nstd_monomer / _entity_poly.pdbx_seq_one_letter_code / _entity_poly.pdbx_seq_one_letter_code_can / _entity_src_gen.pdbx_seq_type / _pdbx_entity_src_syn.pdbx_end_seq_num / _pdbx_struct_assembly_gen.asym_id_list / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_seq_id
Revision 3.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Non-polymer description / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / entity / entity_name_com / 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_molecule_features / pdbx_nonpoly_scheme / struct_conn / 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_atom_id / _atom_site.label_comp_id / _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _atom_site_anisotrop.pdbx_auth_asym_id / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_auth_comp_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_atom_id / _atom_site_anisotrop.pdbx_label_comp_id / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.type
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 3.1Oct 4, 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: Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor
B: Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor
C: Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor
D: Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor
E: ADM
F: ADM
G: ADM
H: ADM
hetero molecules


Theoretical massNumber of molelcules
Total (without water)274,19212
Polymers272,8238
Non-polymers1,3694
Water543
1
A: Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor
E: ADM
hetero molecules


Theoretical massNumber of molelcules
Total (without water)68,5483
Polymers68,2062
Non-polymers3421
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2620 Å2
ΔGint-10 kcal/mol
Surface area24950 Å2
MethodPISA
2
B: Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor
F: ADM
hetero molecules


Theoretical massNumber of molelcules
Total (without water)68,5483
Polymers68,2062
Non-polymers3421
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2710 Å2
ΔGint-9 kcal/mol
Surface area24990 Å2
MethodPISA
3
C: Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor
G: ADM
hetero molecules


Theoretical massNumber of molelcules
Total (without water)68,5483
Polymers68,2062
Non-polymers3421
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3030 Å2
ΔGint-11 kcal/mol
Surface area25130 Å2
MethodPISA
4
D: Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor
H: ADM
hetero molecules


Theoretical massNumber of molelcules
Total (without water)68,5483
Polymers68,2062
Non-polymers3421
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2320 Å2
ΔGint-8 kcal/mol
Surface area25000 Å2
MethodPISA
Unit cell
Length a, b, c (Å)195.496, 69.436, 200.000
Angle α, β, γ (deg.)90.000, 99.430, 90.000
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain F and (resseq 38:43 or (resid 44 and (name...
21(chain E and (resseq 38:44 or resseq 46:53))
12(chain H and (resseq 40:45 or (resid 46 and (name...
22(chain G and ((resid 40 and (name O or name...
13(chain A and ((resid 4 and (name O or name...
23(chain B and ((resid 4 and (name N or name...
33(chain D and ((resid 4 and (name O or name...

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111(chain F and (resseq 38:43 or (resid 44 and (name...F38 - 43
121(chain F and (resseq 38:43 or (resid 44 and (name...F44
131(chain F and (resseq 38:43 or (resid 44 and (name...F38 - 52
141(chain F and (resseq 38:43 or (resid 44 and (name...F38 - 52
151(chain F and (resseq 38:43 or (resid 44 and (name...F38 - 52
161(chain F and (resseq 38:43 or (resid 44 and (name...F38 - 52
211(chain E and (resseq 38:44 or resseq 46:53))E38 - 44
221(chain E and (resseq 38:44 or resseq 46:53))E46 - 53
112(chain H and (resseq 40:45 or (resid 46 and (name...H40 - 45
122(chain H and (resseq 40:45 or (resid 46 and (name...H46
132(chain H and (resseq 40:45 or (resid 46 and (name...H40 - 52
142(chain H and (resseq 40:45 or (resid 46 and (name...H40 - 52
152(chain H and (resseq 40:45 or (resid 46 and (name...H40 - 52
212(chain G and ((resid 40 and (name O or name...G40
222(chain G and ((resid 40 and (name O or name...G40 - 52
232(chain G and ((resid 40 and (name O or name...G40 - 52
242(chain G and ((resid 40 and (name O or name...G40 - 52
252(chain G and ((resid 40 and (name O or name...G40 - 52
113(chain A and ((resid 4 and (name O or name...A4
123(chain A and ((resid 4 and (name O or name...A2 - 2129
133(chain A and ((resid 4 and (name O or name...A2 - 2129
143(chain A and ((resid 4 and (name O or name...A2 - 2129
153(chain A and ((resid 4 and (name O or name...A2 - 2129
163(chain A and ((resid 4 and (name O or name...A2 - 2129
173(chain A and ((resid 4 and (name O or name...A2 - 2129
213(chain B and ((resid 4 and (name N or name...B4
223(chain B and ((resid 4 and (name N or name...B3 - 2129
233(chain B and ((resid 4 and (name N or name...B3 - 2129
243(chain B and ((resid 4 and (name N or name...B3 - 2129
253(chain B and ((resid 4 and (name N or name...B3 - 2129
263(chain B and ((resid 4 and (name N or name...B3 - 2129
273(chain B and ((resid 4 and (name N or name...B3 - 2129
313(chain D and ((resid 4 and (name O or name...D4
323(chain D and ((resid 4 and (name O or name...D4 - 2201
333(chain D and ((resid 4 and (name O or name...D4 - 2201
343(chain D and ((resid 4 and (name O or name...D4 - 2201
353(chain D and ((resid 4 and (name O or name...D4 - 2201
363(chain D and ((resid 4 and (name O or name...D4 - 2201
373(chain D and ((resid 4 and (name O or name...D4 - 2201

NCS ensembles :
ID
1
2
3

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Components

#1: Protein
Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor / MMBP / Maltodextrin-binding protein / Maltose-binding protein / MBP / Calcitonin-receptor-like ...MMBP / Maltodextrin-binding protein / Maltose-binding protein / MBP / Calcitonin-receptor-like receptor activity-modifying protein 1 / CRLR activity-modifying protein 1 / CGRP type 1 receptor / Calcitonin receptor-like receptor


Mass: 66304.562 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli O157:H7 (bacteria), (gene. exp.) Homo sapiens (human)
Gene: malE, Z5632, ECs5017, RAMP1, CALCRL, CGRPR / Production host: Escherichia coli (E. coli) / Strain (production host): Origami B (DE3)
References: UniProt: P0AEY0, UniProt: O60894, UniProt: Q16602
#2: Protein/peptide
ADM


Mass: 1901.152 Da / Num. of mol.: 4 / Mutation: S45W, K46L, Q50W, Y52F / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P35318
#3: Polysaccharide
alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose / alpha-maltose


Type: oligosaccharide, Oligosaccharide / Class: Nutrient / Mass: 342.297 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Details: oligosaccharide / References: alpha-maltose
DescriptorTypeProgram
DGlcpa1-4DGlcpa1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1a_1-5]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[][a-D-Glcp]{[(4+1)][a-D-Glcp]{}}LINUCSPDB-CARE
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Formula: H2O

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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: 2.63 Å3/Da / Density % sol: 53.27 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6
Details: 15% PEG3350, 0.1 M Sodium Malonate pH 6.0, 50 mM Potassium/Sodium tartrate, 1% Cadaverine

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Data collection

DiffractionMean temperature: 105 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-G / Wavelength: 0.9786 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Jun 18, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9786 Å / Relative weight: 1
ReflectionResolution: 2.8→50 Å / Num. obs: 61924 / % possible obs: 94.3 % / Redundancy: 6.8 % / Rmerge(I) obs: 0.106 / Net I/σ(I): 19.56
Reflection shellResolution: 2.8→2.85 Å / Redundancy: 6.8 % / Mean I/σ(I) obs: 1 / Num. unique obs: 2927 / CC1/2: 0.517 / % possible all: 91.4

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Processing

Software
NameVersionClassification
PHENIX1.10.1_2155refinement
PDB_EXTRACT3.22data extraction
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4RWG

4rwg


Resolution: 2.8→45.114 Å / SU ML: 0.4 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 29.56
RfactorNum. reflection% reflection
Rfree0.2445 2000 3.23 %
Rwork0.212 --
obs0.2131 61912 94.14 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 257.75 Å2 / Biso mean: 118.0399 Å2 / Biso min: 44.62 Å2
Refinement stepCycle: final / Resolution: 2.8→45.114 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17742 0 96 3 17841
Biso mean--82.64 74.97 -
Num. residues----2253
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00218348
X-RAY DIFFRACTIONf_angle_d0.44124975
X-RAY DIFFRACTIONf_chiral_restr0.0382663
X-RAY DIFFRACTIONf_plane_restr0.0033227
X-RAY DIFFRACTIONf_dihedral_angle_d13.28510809
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11F110X-RAY DIFFRACTION5.502TORSIONAL
12E110X-RAY DIFFRACTION5.502TORSIONAL
21H98X-RAY DIFFRACTION5.502TORSIONAL
22G98X-RAY DIFFRACTION5.502TORSIONAL
31A7299X-RAY DIFFRACTION5.502TORSIONAL
32B7299X-RAY DIFFRACTION5.502TORSIONAL
33D7299X-RAY DIFFRACTION5.502TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 14

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.7997-2.86970.39941330.36283977411089
2.8697-2.94730.38511380.32514143428192
2.9473-3.0340.33241390.30014151429091
3.034-3.13190.30641390.29924184432393
3.1319-3.24380.30911440.29174298444295
3.2438-3.37360.3371450.27644346449197
3.3736-3.52710.2881470.24794403455098
3.5271-3.7130.28411500.23634479462998
3.713-3.94550.27921490.21414488463799
3.9455-4.24990.24191500.19364486463699
4.2499-4.67720.1991510.17224530468199
4.6772-5.35310.2031500.16844502465299
5.3531-6.74070.24071480.20014410455896
6.7407-45.11960.19051170.18613515363274
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)
13.1187-0.02550.97192.8947-2.227.88930.0145-0.47910.42440.102-0.40080.3506-0.0139-0.26540.33240.56440.0569-0.00170.86-0.32190.6733207.10373.73892.491
24.7703-1.28730.5584.88111.88628.599-0.2897-1.5279-0.61390.19540.4417-0.19540.49750.1359-0.06460.8230.30130.13481.47140.46120.891247.037-16.506377.9324
36.08080.2436-1.19222.20270.16113.0742-0.2955-0.5688-0.24060.04730.01850.0790.3744-0.53550.26680.72630.22250.1051.28440.27680.6166229.8053-11.243371.8967
43.8465-0.6437-0.12954.36041.27789.45690.02810.31520.4559-0.0661-0.4462-0.8465-0.63421.29860.23860.54360.01-0.12190.68350.21610.7708165.9396-28.01236.7128
55.28911.21960.66962.7873-1.47937.29130.2647-0.4807-1.10310.1528-0.42550.75930.6689-0.93710.1820.8836-0.33390.09651.0142-0.1031.2211136.4841-61.025923.216
66.7652-1.15220.90768.9507-0.99884.5312-0.1044-0.3169-0.4210.90040.04470.64290.1278-0.23140.08370.7052-0.08850.04240.6264-0.07220.5108150.4948-49.585227.937
73.78731.06170.89757.56580.22893.90770.17740.1020.1210.52310.4252-0.2097-0.2190.3548-0.55210.50710.04310.12340.598-0.18540.6068182.1832-20.416270.7648
89.25061.43090.78363.7244-2.13318.8579-0.21070.2752-0.8624-0.60590.363-0.22420.77860.3017-0.12620.53980.0583-0.01130.4782-0.08290.4887165.6813-51.497141.557
94.55391.45451.13087.45041.39216.255-0.161-0.33190.23880.09890.32130.3332-0.2064-0.3359-0.13410.33460.09680.04570.62030.11890.5034156.9353-40.149253.969
108.1615-1.86040.98797.2145-1.57062.2262-0.65031.1094-0.3972-0.13490.78460.36990.6665-0.7546-0.13051.232-0.30210.11471.73060.16680.8442216.2664-18.882357.9148
112.8351.4605-0.27764.4064-1.43254.05130.5217-0.6128-0.3188-0.0093-0.34820.1707-0.08010.0965-0.21390.7981-0.3453-0.20751.45980.28630.901195.740813.782929.9655
124.3655-1.25582.46192.5155-2.35564.198-0.75362.11820.1269-0.64190.97040.45950.6422-0.6675-0.11830.9345-0.40580.03982.20750.3290.8989220.2579-5.14644.8279
132.5033-1.8193-1.41973.1185.07219.7984-0.2866-0.8707-0.4571.20210.56420.45861.2206-1.37850.4671.01130.23840.27732.18280.57630.7715225.9784-17.246584.3287
148.3233-5.04310.17069.4977-5.01198.16190.78590.6973-0.4317-2.2854-0.99460.22860.3868-0.13980.17481.05250.0208-0.08080.6277-0.16210.5743155.8621-53.826915.0464
152.17871.6793-1.38848.99022.20397.8245-0.1717-1.2285-1.16721.43820.0315-0.98120.2220.28250.05990.54650.0715-0.07020.72540.17620.7562169.5391-39.132660.4515
166.24780.2181-1.4453.6734-4.93286.8291-0.96382.88560.7368-1.43590.2601-0.07610.31161.73290.00491.2314-0.6476-0.29123.37570.72551.1619207.4937-9.241939.0522
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and ((resseq 2:374) or (resid 2201))A0
2X-RAY DIFFRACTION2chain 'A' and ((resseq 1024:1105))A0
3X-RAY DIFFRACTION3chain 'A' and ((resseq 2035:2129))A0
4X-RAY DIFFRACTION4chain 'B' and ((resseq 3:374) or (resid 2201))B0
5X-RAY DIFFRACTION5chain 'B' and ((resseq 1024:1106))B0
6X-RAY DIFFRACTION6chain 'B' and ((resseq 2034:2129))B0
7X-RAY DIFFRACTION7chain 'C' and ((resseq 5:374) or (resid 2201))C0
8X-RAY DIFFRACTION8chain 'C' and ((resseq 1024:1106))C0
9X-RAY DIFFRACTION9chain 'C' and ((resseq 2034:2129))C0
10X-RAY DIFFRACTION10chain 'D' and ((resseq 1024:1106))D0
11X-RAY DIFFRACTION11chain 'D' and ((resseq 4:374) or (resid 2201))D0
12X-RAY DIFFRACTION12chain 'D' and ((resseq 2036:2128))D0
13X-RAY DIFFRACTION13chain 'E'E38 - 52
14X-RAY DIFFRACTION14chain 'F'F38 - 52
15X-RAY DIFFRACTION15chain 'G'G40 - 52
16X-RAY DIFFRACTION16chain 'H'H40 - 52

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