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- PDB-6d1u: Crystal structure of the human CLR:RAMP1 extracellular domain het... -

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Basic information

Entry
Database: PDB / ID: 6d1u
TitleCrystal structure of the human CLR:RAMP1 extracellular domain heterodimer in complex with adrenomedullin 2/intermedin
Components
  • ADM2
  • Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor
KeywordsPEPTIDE BINDING PROTEIN / CGRP receptor / class B GPCR / peptide hormone / amidated peptide
Function / homology
Function and homology information


calcitonin gene-related peptide binding / CGRP receptor complex / calcitonin gene-related peptide receptor signaling pathway / positive regulation of protein glycosylation / adrenomedullin binding / cellular response to sucrose stimulus / adrenomedullin receptor activity / adrenomedullin receptor complex / adrenomedullin receptor signaling pathway / amylin receptor activity ...calcitonin gene-related peptide binding / CGRP receptor complex / calcitonin gene-related peptide receptor signaling pathway / positive regulation of protein glycosylation / adrenomedullin binding / cellular response to sucrose stimulus / adrenomedullin receptor activity / adrenomedullin receptor complex / adrenomedullin receptor signaling pathway / amylin receptor activity / calcitonin receptor activity / vascular associated smooth muscle cell proliferation / calcitonin gene-related peptide receptor activity / amylin receptor signaling pathway / Calcitonin-like ligand receptors / regulation of systemic arterial blood pressure / regulation of G protein-coupled receptor signaling pathway / feeding behavior / positive regulation of heart rate / G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger / carbohydrate transmembrane transporter activity / coreceptor activity / cellular response to hormone stimulus / positive regulation of vascular associated smooth muscle cell proliferation / digestion / negative regulation of blood pressure / G protein-coupled receptor activity / protein localization to plasma membrane / intracellular protein transport / adenylate cyclase-activating G protein-coupled receptor signaling pathway / hormone activity / receptor internalization / ADORA2B mediated anti-inflammatory cytokines production / positive regulation of angiogenesis / calcium ion transport / protein transport / outer membrane-bounded periplasmic space / heart development / G alpha (s) signalling events / angiogenesis / lysosome / cell surface receptor signaling pathway / receptor complex / endosome / G protein-coupled receptor signaling pathway / protein phosphorylation / protein-containing complex binding / positive regulation of gene expression / cell surface / endoplasmic reticulum / extracellular region / plasma membrane / cytoplasm
Similarity search - Function
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 ...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 / Calcitonin gene-related peptide type 1 receptor / Protein ADM2
Similarity search - Component
Biological speciesEscherichia coli O157:H7 (bacteria)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.05 Å
AuthorsPioszak, A. / Roehrkasse, A.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01GM104251 United States
CitationJournal: J. Biol. Chem. / Year: 2018
Title: Structure-function analyses reveal a triple beta-turn receptor-bound conformation of adrenomedullin 2/intermedin and enable peptide antagonist design.
Authors: Roehrkasse, A.M. / Booe, J.M. / Lee, S.M. / Warner, M.L. / Pioszak, A.A.
History
DepositionApr 12, 2018Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 5, 2018Provider: repository / Type: Initial release
Revision 1.1Oct 24, 2018Group: Data collection / Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.2Jan 1, 2020Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 2.0Jul 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 / pdbx_struct_assembly_gen / pdbx_struct_conn_angle / struct_asym / struct_conn / struct_conn_type / 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.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.id / _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_asym_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 / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr1_symmetry / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.ptnr3_symmetry / _pdbx_struct_conn_angle.value / _struct_asym.entity_id / _struct_conn_type.id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Oct 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 / 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: 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: ADM2
E: ADM2
F: ADM2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)205,80813
Polymers204,6896
Non-polymers1,1197
Water9,548530
1
A: Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor
D: ADM2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)68,5954
Polymers68,2302
Non-polymers3652
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2530 Å2
ΔGint-14 kcal/mol
Surface area25130 Å2
MethodPISA
2
B: Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor
E: ADM2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)68,5723
Polymers68,2302
Non-polymers3421
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2690 Å2
ΔGint-7 kcal/mol
Surface area25230 Å2
MethodPISA
3
C: Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor
F: ADM2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)68,6416
Polymers68,2302
Non-polymers4114
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2680 Å2
ΔGint-35 kcal/mol
Surface area26710 Å2
MethodPISA
Unit cell
Length a, b, c (Å)172.295, 106.041, 136.911
Angle α, β, γ (deg.)90.000, 122.530, 90.000
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11A-2388-

HOH

Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12A
22C
13B
23C
14D
24E
15D
25F
16E
26F

NCS domain segments:

Component-ID: 0 / Refine code: 0

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11GLUGLUVALVALAA5 - 21295 - 572
21GLUGLUVALVALBB5 - 21295 - 572
12GLUGLUASNASNAA5 - 21285 - 571
22GLUGLUASNASNCC5 - 21285 - 571
13GLUGLUASNASNBB5 - 21285 - 571
23GLUGLUASNASNCC5 - 21285 - 571
14ASPASPSERSERDD35 - 467 - 18
24ASPASPSERSEREE35 - 467 - 18
15ASPASPTYRTYRDD35 - 477 - 19
25ASPASPTYRTYRFF35 - 477 - 19
16ASPASPSERSEREE35 - 467 - 18
26ASPASPSERSERFF35 - 467 - 18

NCS ensembles :
ID
1
2
3
4
5
6

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Components

#1: Protein Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor / MBP / MMBP / Maltodextrin-binding protein / Calcitonin-receptor-like receptor activity-modifying ...MBP / MMBP / Maltodextrin-binding protein / 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.: 3
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)
References: UniProt: P0AEY0, UniProt: O60894, UniProt: Q16602
#2: Protein/peptide ADM2 / Intermedin


Mass: 1925.002 Da / Num. of mol.: 3 / Fragment: residues 129-147 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: Q7Z4H4*PLUS
#3: Polysaccharide alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose / alpha-maltose


Type: oligosaccharide, Oligosaccharide / Class: Nutrient / Mass: 342.297 Da / Num. of mol.: 3
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: Chemical
ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Na
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 530 / 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: 2.58 Å3/Da / Density % sol: 52.25 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 13% v/v PEG 3,350 0.1 M Na cacodylate, pH 6.5 0.15 M DL-malic acid

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-G / Wavelength: 0.97857 Å
DetectorType: RAYONIX MX300-HS / Detector: CCD / Date: Apr 5, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97857 Å / Relative weight: 1
ReflectionResolution: 2.05→50 Å / Num. obs: 128678 / % possible obs: 98.9 % / Redundancy: 7.5 % / Rmerge(I) obs: 0.062 / Rpim(I) all: 0.024 / Rrim(I) all: 0.067 / Χ2: 1.136 / Net I/σ(I): 8.5 / Num. measured all: 965268
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allΧ2% possible all
2.05-2.096.51.20258870.7590.481.2960.79891
2.09-2.126.70.96560610.8580.381.0390.76793.5
2.12-2.1670.81862850.8880.3190.8790.77896.6
2.16-2.217.20.71363480.9040.2760.7650.78498
2.21-2.267.40.58964200.9440.2280.6320.8599.2
2.26-2.317.60.48764590.9580.1880.5220.8399.8
2.31-2.377.70.38564920.9730.1480.4130.823100
2.37-2.437.70.32764600.9780.1250.350.838100
2.43-2.57.70.27165120.9830.1040.290.859100
2.5-2.587.70.22264860.9870.0850.2370.912100
2.58-2.687.70.17664840.9920.0680.1891.001100
2.68-2.787.70.1465160.9940.0540.151.075100
2.78-2.917.70.11364880.9960.0430.1211.178100
2.91-3.067.70.08965350.9970.0340.0951.325100
3.06-3.257.70.07364840.9970.0280.0781.582100
3.25-3.517.70.06965230.9970.0270.0741.842100
3.51-3.867.70.06565330.9970.0250.071.851100
3.86-4.427.60.05265540.9980.020.0561.799.9
4.42-5.567.60.03565420.9990.0130.0371.49599.9
5.56-507.30.02766090.9990.0110.0291.15499.2

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Processing

Software
NameVersionClassification
HKL-2000data scaling
REFMAC5.8.0158refinement
PDB_EXTRACT3.24data extraction
HKL-2000data reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4rwg

4rwg


Resolution: 2.05→45.64 Å / Cor.coef. Fo:Fc: 0.967 / Cor.coef. Fo:Fc free: 0.956 / SU B: 11.622 / SU ML: 0.154 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.19 / ESU R Free: 0.159
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED
RfactorNum. reflection% reflectionSelection details
Rfree0.2228 6603 5.1 %RANDOM
Rwork0.194 ---
obs0.1954 121708 98.63 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso max: 158.52 Å2 / Biso mean: 66.542 Å2 / Biso min: 30.12 Å2
Baniso -1Baniso -2Baniso -3
1-1.53 Å20 Å20.34 Å2
2--1.81 Å20 Å2
3----2.08 Å2
Refinement stepCycle: final / Resolution: 2.05→45.64 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13525 0 76 530 14131
Biso mean--49.93 55.63 -
Num. residues----1715
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0130.0214003
X-RAY DIFFRACTIONr_bond_other_d0.0020.0212494
X-RAY DIFFRACTIONr_angle_refined_deg1.5191.94519050
X-RAY DIFFRACTIONr_angle_other_deg0.993329106
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.80751711
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.86925.052667
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.304152248
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.7611553
X-RAY DIFFRACTIONr_chiral_restr0.10.22025
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.02115662
X-RAY DIFFRACTIONr_gen_planes_other0.0010.022847
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A365300.05
12B365300.05
21A354280.07
22C354280.07
31B352920.07
32C352920.07
41D5240.04
42E5240.04
51D5820.09
52F5820.09
61E5260.1
62F5260.1
LS refinement shellResolution: 2.05→2.103 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.333 462 -
Rwork0.321 8050 -
all-8512 -
obs--88.94 %
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)
11.90540.1875-0.64071.2185-0.65492.25150.0393-0.23880.25740.0088-0.05290.1801-0.1672-0.13090.01360.02420.0180.00370.3785-0.08930.0932-26.21949.017633.8012
21.6383-0.1529-0.62023.2889-0.07332.8268-0.1492-0.04650.0231-0.4241-0.18310.0336-0.1097-0.35310.33230.14880.0192-0.07370.4882-0.2060.1533-6.533276.632261.4512
33.3058-0.37420.11532.4786-0.13211.70920.14180.0762-0.0550.0644-0.3478-0.724-0.1170.33450.2060.0629-0.1176-0.0760.41040.25190.4173-47.3916100.045122.3459
43.7973-0.52780.11723.44161.81645.63120.107-0.1651-0.74260.087-0.0561-0.1660.87030.0378-0.05090.14910.0207-0.00190.22080.14740.22386.123416.395122.6435
53.2057-1.9873-2.2542.85360.47486.27470.1610.18550.7399-0.3103-0.1166-0.5064-0.48290.4974-0.04440.4827-0.17450.06310.56990.12710.577620.39482.383823.1344
65.26030.63430.96518.7677-1.28967.45950.27420.4001-0.5155-0.3879-0.2383-0.87290.44481.1461-0.03590.38230.33140.03820.643-0.0870.446-60.144863.9477-6.391
72.8064-0.7628-0.07132.96980.02654.1845-0.0765-0.2028-0.4320.18480.05150.12020.3168-0.46010.0250.0355-0.03210.01310.23650.0260.0666-8.127826.155216.1507
84.1547-0.9106-0.16684.13620.91053.09930.02710.31320.5565-0.2518-0.1294-0.0733-0.5922-0.01820.10230.375-0.0612-0.08110.39050.02150.22043.021583.110129.0979
91.0076-0.19410.23670.8545-0.12065.09830.0456-0.0258-0.29720.0451-0.136-0.30680.48640.65050.09040.06270.0986-0.02040.30860.10690.255-66.630276.384413.1247
107.45923.5092-2.445712.1101-8.64046.20220.29280.2583-0.82380.76920.4521.1595-0.4237-0.3283-0.74480.4754-0.06510.24510.53260.01070.3952-13.190225.665929.0757
112.88440.19710.066611.32635.46764.978-0.0505-0.1414-0.21530.33060.07210.0980.30420.0317-0.02160.2691-0.029-0.01920.32990.00190.18766.186171.293435.8311
125.5683-7.76947.416211.7464-11.765412.1128-0.4844-0.01870.28460.4938-0.3284-0.7125-0.27310.54910.81280.50370.1405-0.13670.78660.08170.8535-53.706874.433913.0676
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A5 - 374
2X-RAY DIFFRACTION1A2201
3X-RAY DIFFRACTION2B5 - 374
4X-RAY DIFFRACTION2B2201
5X-RAY DIFFRACTION3C3 - 373
6X-RAY DIFFRACTION3C2201
7X-RAY DIFFRACTION4A1024 - 1111
8X-RAY DIFFRACTION5B1024 - 1110
9X-RAY DIFFRACTION6C1030 - 1109
10X-RAY DIFFRACTION7A2035 - 2129
11X-RAY DIFFRACTION8B2034 - 2129
12X-RAY DIFFRACTION9C2035 - 2150
13X-RAY DIFFRACTION10D35 - 48
14X-RAY DIFFRACTION11E32 - 48
15X-RAY DIFFRACTION12F35 - 48

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