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- PDB-4rwg: Crystal structure of the CLR:RAMP1 extracellular domain heterodim... -

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Basic information

Entry
Database: PDB / ID: 4rwg
TitleCrystal structure of the CLR:RAMP1 extracellular domain heterodimer with bound high affinity CGRP analog
Components
  • CGRP analog
  • Maltose-binding periplasmic protein, Receptor activity-modifying protein 1, Calcitonin gene-related peptide type 1 receptor fusion protein
KeywordsMEMBRANE PROTEIN/HORMONE / cell surface receptor / MEMBRANE PROTEIN-HORMONE complex
Function / homology
Function and homology information


calcitonin gene-related peptide binding / cellular response to sucrose stimulus / adrenomedullin binding / CGRP receptor complex / positive regulation of protein glycosylation / adrenomedullin receptor activity / adrenomedullin receptor complex / adrenomedullin receptor signaling pathway / amylin receptor activity / calcitonin receptor activity ...calcitonin gene-related peptide binding / cellular response to sucrose stimulus / adrenomedullin binding / CGRP receptor complex / positive regulation of protein glycosylation / adrenomedullin receptor activity / adrenomedullin receptor complex / adrenomedullin receptor signaling pathway / amylin receptor activity / calcitonin receptor activity / calcitonin gene-related peptide receptor signaling pathway / vascular associated smooth muscle cell proliferation / calcitonin gene-related peptide receptor activity / amylin receptor 1 signaling pathway / amylin receptor signaling pathway / Calcitonin-like ligand receptors / regulation of G protein-coupled receptor signaling pathway / detection of maltose stimulus / maltose transport complex / carbohydrate transport / G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger / carbohydrate transmembrane transporter activity / maltose binding / maltose transport / maltodextrin transmembrane transport / cellular response to hormone stimulus / coreceptor activity / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / positive regulation of vascular associated smooth muscle cell proliferation / ATP-binding cassette (ABC) transporter complex / protein localization to plasma membrane / cell chemotaxis / intracellular protein transport / G protein-coupled receptor activity / receptor internalization / adenylate cyclase-activating G protein-coupled receptor signaling pathway / calcium ion transport / protein transport / outer membrane-bounded periplasmic space / heart development / High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR in endothelial cells / G alpha (s) signalling events / angiogenesis / periplasmic space / lysosome / receptor complex / cell surface receptor signaling pathway / endosome / G protein-coupled receptor signaling pathway / DNA damage response / cell surface / endoplasmic reticulum / membrane / 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 / G-protein coupled receptors family 2 signature 1. / : / GPCR, family 2, extracellular hormone receptor domain / G-protein coupled receptors family 2 profile 1. / Domain present in hormone receptors ...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 / G-protein coupled receptors family 2 signature 1. / : / GPCR, family 2, extracellular hormone receptor domain / G-protein coupled receptors family 2 profile 1. / Domain present in hormone receptors / Hormone receptor domain / 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 / Periplasmic binding protein-like II / D-Maltodextrin-Binding Protein; domain 2 / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
alpha-maltose / Receptor activity-modifying protein 1 / Maltose/maltodextrin-binding periplasmic protein / Calcitonin gene-related peptide type 1 receptor
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
Homo sapiens (human)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.44 Å
AuthorsBooe, J. / Pioszak, A.
CitationJournal: Mol.Cell / Year: 2015
Title: Structural Basis for Receptor Activity-Modifying Protein-Dependent Selective Peptide Recognition by a G Protein-Coupled Receptor.
Authors: Booe, J.M. / Walker, C.S. / Barwell, J. / Kuteyi, G. / Simms, J. / Jamaluddin, M.A. / Warner, M.L. / Bill, R.M. / Harris, P.W. / Brimble, M.A. / Poyner, D.R. / Hay, D.L. / Pioszak, A.A.
History
DepositionDec 3, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 20, 2015Provider: repository / Type: Initial release
Revision 1.1May 27, 2015Group: Database references / Source and taxonomy
Revision 1.2Aug 16, 2017Group: Refinement description / Source and taxonomy / Category: entity_src_gen / pdbx_entity_src_syn / software / Item: _pdbx_entity_src_syn.organism_scientific
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / 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_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.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_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_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.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_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.value / _struct_asym.entity_id / _struct_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Sep 20, 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
Revision 2.2Nov 27, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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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 fusion protein
B: Maltose-binding periplasmic protein, Receptor activity-modifying protein 1, Calcitonin gene-related peptide type 1 receptor fusion protein
C: Maltose-binding periplasmic protein, Receptor activity-modifying protein 1, Calcitonin gene-related peptide type 1 receptor fusion protein
D: CGRP analog
E: CGRP analog
F: CGRP analog
hetero molecules


Theoretical massNumber of molelcules
Total (without water)203,54810
Polymers202,4976
Non-polymers1,0514
Water1,26170
1
A: Maltose-binding periplasmic protein, Receptor activity-modifying protein 1, Calcitonin gene-related peptide type 1 receptor fusion protein
D: CGRP analog
hetero molecules


Theoretical massNumber of molelcules
Total (without water)67,8413
Polymers67,4992
Non-polymers3421
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2510 Å2
ΔGint-11 kcal/mol
Surface area25370 Å2
MethodPISA
2
B: Maltose-binding periplasmic protein, Receptor activity-modifying protein 1, Calcitonin gene-related peptide type 1 receptor fusion protein
E: CGRP analog
hetero molecules


Theoretical massNumber of molelcules
Total (without water)67,8664
Polymers67,4992
Non-polymers3672
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2360 Å2
ΔGint-16 kcal/mol
Surface area27110 Å2
MethodPISA
3
C: Maltose-binding periplasmic protein, Receptor activity-modifying protein 1, Calcitonin gene-related peptide type 1 receptor fusion protein
F: CGRP analog
hetero molecules


Theoretical massNumber of molelcules
Total (without water)67,8413
Polymers67,4992
Non-polymers3421
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2270 Å2
ΔGint-9 kcal/mol
Surface area24940 Å2
MethodPISA
Unit cell
Length a, b, c (Å)172.806, 104.623, 136.483
Angle α, β, γ (deg.)90.000, 122.430, 90.000
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11A-2302-

HOH

Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31C
12A
22B
32C
13A
23B
33C
14D
24E
34F
15D
25F
16D
26E
36F
17E
27F

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1113A6 - 49
2113B6 - 49
3113C6 - 49
1213A58 - 61
2213B58 - 61
3213C58 - 61
1313A63 - 93
2313B63 - 93
3313C63 - 93
1413A95 - 119
2413B95 - 119
3413C95 - 119
1513A121 - 124
2513B121 - 124
3513C121 - 124
1613A127 - 132
2613B127 - 132
3613C127 - 132
1713A134 - 141
2713B134 - 141
3713C134 - 141
1813A143 - 172
2813B143 - 172
3813C143 - 172
1913A183 - 202
2913B183 - 202
3913C183 - 202
1123A204 - 247
2123B204 - 247
3123C204 - 247
1223A249 - 271
2223B249 - 271
3223C249 - 271
1323A276 - 314
2323B276 - 314
3323C276 - 314
1423A316 - 322
2423B316 - 322
3423C316 - 322
1523A324 - 326
2523B324 - 326
3523C324 - 326
1623A328 - 329
2623B328 - 329
3623C328 - 329
1723A331 - 355
2723B331 - 355
3723C331 - 355
1823A357 - 363
2823B357 - 363
3823C357 - 363
1133A1035 - 1036
2133B1035 - 1036
3133C1035 - 1036
1233A1040 - 1042
2233B1040 - 1042
3233C1040 - 1042
1333A1046 - 1060
2333B1046 - 1060
3333C1046 - 1060
1433A1062 - 1064
2433B1062 - 1064
3433C1062 - 1064
1533A1068 - 1082
2533B1068 - 1082
3533C1068 - 1082
1633A1084 - 1090
2633B1084 - 1090
3633C1084 - 1090
1733A1092 - 1093
2733B1092 - 1093
3733C1092 - 1093
1833A1095 - 1109
2833B1095 - 1109
3833C1095 - 1109
1145D2040 - 2050
2145E2040 - 2050
3145F2040 - 2050
1245D2064 - 2065
2245E2064 - 2065
3245F2064 - 2065
1343D2068 - 2081
2343E2068 - 2081
3343F2068 - 2081
1443D2083 - 2099
2443E2083 - 2099
3443F2083 - 2099
1543D2101 - 2105
2543E2101 - 2105
3543F2101 - 2105
1643D2107 - 2109
2643E2107 - 2109
3643F2107 - 2109
1743D2111 - 2113
2743E2111 - 2113
3743F2111 - 2113
1845D2114 - 2118
2845E2114 - 2118
3845F2114 - 2118
1943D2120 - 2127
2943E2120 - 2127
3943F2120 - 2127
1153D2066 - 2067
2153F2066 - 2067
1253D2128
2253F2128
1163D30 - 38
2163E30 - 38
3163F30 - 38
1175E29
2175F29

NCS ensembles :
ID
1
2
3
4
5
6
7

NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.236976, -0.049529, -0.970252), (-0.127916, 0.991596, -0.019376), (0.963057, 0.11952, -0.24132)-10.98805, -55.237659, 73.27562
3given(-0.76175, 0.616604, 0.198837), (0.305608, 0.612602, -0.728919), (-0.571262, -0.494488, -0.655089)-132.911667, 60.521351, 67.121597
4given(1), (1), (1)
5given(-0.238762, -0.052804, -0.969641), (-0.127547, 0.991575, -0.022592), (0.962665, 0.118281, -0.243486)-10.78641, -55.176552, 73.412453
6given(-0.75991, 0.618793, 0.199077), (0.307718, 0.612218, -0.728354), (-0.572579, -0.492224, -0.655644)-132.94809, 60.683472, 66.871132
7given(1), (1), (1)
8given(0.054997, -0.053431, -0.997056), (0.103502, 0.993493, -0.047531), (0.993108, -0.100583, 0.06017)6.46377, -41.29961, 89.383034
9given(-0.775283, 0.587902, 0.230882), (0.255503, 0.626216, -0.736595), (-0.577628, -0.512079, -0.635706)-133.803864, 56.270512, 67.44915
10given(1), (1), (1)
11given(-0.037922, 0.004946, -0.999268), (0.051796, 0.998653, 0.002978), (0.997937, -0.051646, -0.038127)-2.81806, -44.908131, 87.158401
12given(-0.796694, 0.565686, 0.212785), (0.227897, 0.607259, -0.761117), (-0.559769, -0.557885, -0.612718)-132.120056, 57.74799, 70.720688
13given(1), (1), (1)
14given(-0.818367, 0.548764, 0.170682), (0.256226, 0.614247, -0.746357), (-0.514415, -0.567061, -0.643287)-128.581375, 57.981682, 77.694397
15given(1), (1), (1)
16given(-0.006567, 0.032456, -0.999452), (0.072842, 0.996834, 0.031893), (0.997322, -0.072592, -0.008911)-2.92739, -43.776901, 88.375603
17given(-0.793736, 0.573937, 0.201442), (0.217497, 0.577082, -0.787192), (-0.568048, -0.58101, -0.582881)-131.336075, 61.323071, 69.395218
18given(1), (1), (1)
19given(-0.378664, -0.471316, -0.796539), (0.515391, 0.607464, -0.60445), (0.768755, -0.639413, 0.012888)10.13028, 115.388268, 116.388283

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Components

#1: Protein Maltose-binding periplasmic protein, Receptor activity-modifying protein 1, Calcitonin gene-related peptide type 1 receptor fusion protein


Mass: 66304.562 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli), (gene. exp.) Homo sapiens (human)
Strain: K12 / Gene: malE, CE10_4748, RAMP1, CALCRL, CGRPR / Production host: Escherichia coli (E. coli)
References: UniProt: P0AEX9, UniProt: O60894, UniProt: Q16602
#2: Protein/peptide CGRP analog


Mass: 1194.357 Da / Num. of mol.: 3 / Source method: obtained synthetically / Details: synthetic CGRP peptide analog / Source: (synth.) synthetic construct (others)
#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-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 70 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

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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: 2.57 Å3/Da / Density % sol: 52.16 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6
Details: 16% PEG3350, 8% Tacsimate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 105 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-G / Wavelength: 0.97857 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Nov 3, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97857 Å / Relative weight: 1
ReflectionResolution: 2.44→50 Å / Num. all: 76164 / Num. obs: 76012 / % possible obs: 99.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 4.2 % / Rmerge(I) obs: 0.058 / Χ2: 1.093 / Net I/σ(I): 10.8
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allΧ2Diffraction-ID% possible all
2.45-2.493.90.64737080.748198.6
2.49-2.544.10.60638250.748199.8
2.54-2.594.20.51537580.756199.9
2.59-2.644.30.44637650.7891100
2.64-2.74.30.35938060.7971100
2.7-2.764.30.29938200.8351100
2.76-2.834.30.2637770.8791100
2.83-2.94.30.21138030.9321100
2.9-2.994.30.16937860.9581100
2.99-3.094.30.13438011.0631100
3.09-3.24.30.10437931.1251100
3.2-3.324.30.08437981.1741100
3.32-3.484.30.07137961.2861100
3.48-3.664.30.06237981.4351100
3.66-3.894.30.05338321.449199.9
3.89-4.194.30.05137951.5561100
4.19-4.614.20.04638251.654199.8
4.61-5.284.20.03838231.236199.8
5.28-6.654.20.03638431.1731100
6.65-5040.03338601.199198.6

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
SCALEPACKdata scaling
PHASERphasing
REFMAC5.8.0073refinement
PDB_EXTRACT3.15data extraction
MD2diffractometerdata collection
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3C4M and 3N7S

3c4m

3n7s


Resolution: 2.44→50 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.942 / SU B: 25.229 / SU ML: 0.255 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.434 / ESU R Free: 0.262 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED
RfactorNum. reflection% reflectionSelection details
Rfree0.2426 3827 5 %RANDOM
Rwork0.1998 ---
obs0.2019 72185 99.37 %-
all-72642 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 203.92 Å2 / Biso mean: 84.555 Å2 / Biso min: 32.59 Å2
Baniso -1Baniso -2Baniso -3
1-1.43 Å20 Å21.35 Å2
2--1.04 Å20 Å2
3----2.31 Å2
Refinement stepCycle: LAST / Resolution: 2.44→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13453 0 70 70 13593
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0130.0213895
X-RAY DIFFRACTIONr_bond_other_d0.0020.0212819
X-RAY DIFFRACTIONr_angle_refined_deg1.5161.94418894
X-RAY DIFFRACTIONr_angle_other_deg0.921329558
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.98951692
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.62125.053659
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.525152230
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.7021550
X-RAY DIFFRACTIONr_chiral_restr0.0880.22015
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.02115813
X-RAY DIFFRACTIONr_gen_planes_other0.0030.023207
X-RAY DIFFRACTIONr_mcbond_it2.613.9896807
X-RAY DIFFRACTIONr_mcbond_other2.613.9896805
X-RAY DIFFRACTIONr_mcangle_it3.9035.988490
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
11A1690LOOSE POSITIONAL0.035
12B1690LOOSE POSITIONAL0.035
13C1690LOOSE POSITIONAL0.035
11A1004TIGHT THERMAL3.780.5
12B1004TIGHT THERMAL3.880.5
13C1004TIGHT THERMAL4.090.5
11A1690LOOSE THERMAL4.3910
12B1690LOOSE THERMAL4.7510
13C1690LOOSE THERMAL4.9610
21A1340LOOSE POSITIONAL0.035
22B1340LOOSE POSITIONAL0.035
23C1340LOOSE POSITIONAL0.035
21A882TIGHT THERMAL3.120.5
22B882TIGHT THERMAL4.090.5
23C882TIGHT THERMAL3.690.5
21A1340LOOSE THERMAL3.8510
22B1340LOOSE THERMAL4.8810
23C1340LOOSE THERMAL4.4810
31A571LOOSE POSITIONAL0.055
32B571LOOSE POSITIONAL0.045
33C571LOOSE POSITIONAL0.045
31A365TIGHT THERMAL6.90.5
32B365TIGHT THERMAL4.990.5
33C365TIGHT THERMAL5.590.5
31A571LOOSE THERMAL7.3810
32B571LOOSE THERMAL5.7610
33C571LOOSE THERMAL6.0110
41D107MEDIUM POSITIONAL0.120.5
42E107MEDIUM POSITIONAL0.170.5
43F107MEDIUM POSITIONAL0.090.5
41D638LOOSE POSITIONAL0.075
42E638LOOSE POSITIONAL0.095
43F638LOOSE POSITIONAL0.055
41D295TIGHT THERMAL4.440.5
42E295TIGHT THERMAL4.560.5
43F295TIGHT THERMAL7.770.5
41D107MEDIUM THERMAL4.72
42E107MEDIUM THERMAL3.372
43F107MEDIUM THERMAL6.492
41D638LOOSE THERMAL5.1410
42E638LOOSE THERMAL5.0810
43F638LOOSE THERMAL7.7210
51D34LOOSE POSITIONAL0.15
51D18TIGHT THERMAL6.740.5
51D34LOOSE THERMAL9.2110
61D69LOOSE POSITIONAL0.285
62E69LOOSE POSITIONAL0.455
63F69LOOSE POSITIONAL0.385
61D47TIGHT THERMAL3.810.5
62E47TIGHT THERMAL12.130.5
63F47TIGHT THERMAL9.50.5
61D69LOOSE THERMAL4.2210
62E69LOOSE THERMAL12.2210
63F69LOOSE THERMAL8.7510
71E5MEDIUM POSITIONAL0.030.5
71E9LOOSE POSITIONAL0.155
71E5MEDIUM THERMAL0.912
71E9LOOSE THERMAL1.310
LS refinement shellResolution: 2.44→2.502 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.402 265 -
Rwork0.33 4962 -
all-5227 -
obs--93.19 %
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)
13.59650.1546-0.7912.6686-1.1013.03110.1214-0.30110.39210.1313-0.23920.3972-0.1777-0.14540.11780.04160.02080.02940.251-0.13130.1644-25.993445.471633.718
23.9251-0.4781-0.62193.619-0.18742.18330.3617-0.4447-0.23860.3572-0.6723-0.8862-0.25840.58780.31060.1741-0.25-0.14130.51390.40390.4538-47.386996.016222.2676
31.92360.3494-0.9653.88210.86173.7576-0.11480.15730.04950.1588-0.2076-0.0988-0.080.59650.32250.22980.05-0.07990.83170.40280.2555-67.073973.033753.9406
45.7267-0.47380.32365.24283.67666.0831-0.11-0.6189-0.96170.23320.1292-0.36220.8330.2696-0.01910.18420.1020.09050.20240.21210.30516.707213.75522.7776
56.85641.71251.7846.98450.25585.30730.07070.796-0.7796-0.27860.0967-0.74440.6911.1077-0.16740.38310.33490.1980.4963-0.11130.5414-60.893960.5609-6.7095
63.30.9152-0.96932.4604-1.30218.10670.0711-0.07220.7830.3478-0.07010.2804-0.4925-0.2394-0.0010.52480.18110.07810.3516-0.06050.5642-93.949478.835292.1284
74.6472-1.3335-0.33184.0749-1.27254.8745-0.4241-0.4941-0.66190.36810.33940.17650.2523-0.5850.08470.0780.02190.06130.16460.06020.0954-8.0822.923216.7855
82.61770.1365-0.09491.6313-0.33055.4789-0.083-0.2747-0.45710.1669-0.1227-0.41150.37930.74830.20580.08910.10140.0320.19980.15070.2492-66.604772.53413.0053
97.54471.4157-1.17523.2859-0.43733.84060.03780.29430.88420.20360.0520.0417-0.50140.2106-0.08980.40010.0727-0.0560.32060.05280.319-76.576479.006585.5975
108.2316-4.10114.03634.47772.30599.6351-0.5947-0.8243-0.57830.66470.370.57210.344-0.51720.22470.24320.2040.17820.51780.14330.1342-14.108623.059730.4228
116.2226-1.5762-2.14120.58920.5470.76760.1998-0.55660.4320.1137-0.0394-0.50780.0720.3367-0.16040.75150.4883-0.34570.96670.31330.8783-52.968870.136613.6841
126.6238-1.87114.80111.9847-0.39226.41160.24291.0874-0.1944-0.1856-0.1359-0.11810.542-0.2206-0.1070.4001-0.06680.07820.7999-0.09140.137-79.540269.144276.1267
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A3 - 374
2X-RAY DIFFRACTION1A2201
3X-RAY DIFFRACTION2B3 - 372
4X-RAY DIFFRACTION2B2201
5X-RAY DIFFRACTION3C6 - 374
6X-RAY DIFFRACTION3C2201
7X-RAY DIFFRACTION4A1024 - 1110
8X-RAY DIFFRACTION5B1027 - 1110
9X-RAY DIFFRACTION6C1024 - 1110
10X-RAY DIFFRACTION7A2033 - 2130
11X-RAY DIFFRACTION8B2033 - 2150
12X-RAY DIFFRACTION9C2036 - 2129
13X-RAY DIFFRACTION10D27 - 38
14X-RAY DIFFRACTION11E27 - 38
15X-RAY DIFFRACTION12F28 - 38

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