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- PDB-2rgn: Crystal Structure of p63RhoGEF complex with Galpha-q and RhoA -

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Basic information

Entry
Database: PDB / ID: 2rgn
TitleCrystal Structure of p63RhoGEF complex with Galpha-q and RhoA
Components
  • Guanine nucleotide-binding protein G(i) subunit alpha-1,Guanine nucleotide-binding protein G(q) subunit alpha
  • Rho guanine nucleotide exchange factor 25
  • Transforming protein RhoA
KeywordsSIGNALING PROTEIN complex / Heterotrimeric G-protein / small molecular weight G-protein / signaling complex / protein-protein complex / RhoGEF / RhoA / GalphaQ / Galpha-Q / p63RhoGEF / Gq / GTP-binding / Lipoprotein / Nucleotide-binding / Palmitate / Transducer / ADP-ribosylation / Cytoskeleton / Magnesium / Membrane / Methylation / Prenylation / Proto-oncogene
Function / homology
Function and homology information


guanyl-nucleotide exchange factor activity => GO:0005085 / Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion / Acetylcholine regulates insulin secretion / PLC beta mediated events / forebrain neuron development / regulation of melanocyte differentiation / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / Thromboxane signalling through TP receptor / Thrombin signalling through proteinase activated receptors (PARs) / Extra-nuclear estrogen signaling ...guanyl-nucleotide exchange factor activity => GO:0005085 / Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion / Acetylcholine regulates insulin secretion / PLC beta mediated events / forebrain neuron development / regulation of melanocyte differentiation / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / Thromboxane signalling through TP receptor / Thrombin signalling through proteinase activated receptors (PARs) / Extra-nuclear estrogen signaling / G-protein activation / Adenylate cyclase inhibitory pathway / G alpha (q) signalling events / endothelin receptor signaling pathway / ion channel modulating, G protein-coupled receptor signaling pathway / phospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway / developmental pigmentation / aortic valve formation / alpha-beta T cell lineage commitment / mitotic cleavage furrow formation / bone trabecula morphogenesis / positive regulation of lipase activity / endothelial tube lumen extension / skeletal muscle satellite cell migration / positive regulation of vascular associated smooth muscle contraction / angiotensin-mediated vasoconstriction involved in regulation of systemic arterial blood pressure / SLIT2:ROBO1 increases RHOA activity / phospholipase C-activating dopamine receptor signaling pathway / RHO GTPases Activate Rhotekin and Rhophilins / Roundabout signaling pathway / cranial skeletal system development / negative regulation of intracellular steroid hormone receptor signaling pathway / regulation of platelet activation / Axonal growth inhibition (RHOA activation) / Axonal growth stimulation / regulation of neural precursor cell proliferation / cleavage furrow formation / ADP signalling through P2Y purinoceptor 1 / regulation of modification of postsynaptic actin cytoskeleton / regulation of osteoblast proliferation / maternal behavior / forebrain radial glial cell differentiation / cell junction assembly / apical junction assembly / regulation of systemic arterial blood pressure by endothelin / regulation of Rho protein signal transduction / cellular response to chemokine / negative regulation of cell migration involved in sprouting angiogenesis / beta selection / establishment of epithelial cell apical/basal polarity / regulation of modification of postsynaptic structure / negative regulation of cell size / RHO GTPases Activate ROCKs / negative regulation of oxidative phosphorylation / negative regulation of motor neuron apoptotic process / RHO GTPases activate CIT / glutamate receptor signaling pathway / Adrenaline,noradrenaline inhibits insulin secretion / ADP signalling through P2Y purinoceptor 12 / PCP/CE pathway / Sema4D induced cell migration and growth-cone collapse / RHO GTPases activate KTN1 / G alpha (i) signalling events / apolipoprotein A-I-mediated signaling pathway / regulation of canonical Wnt signaling pathway / negative regulation of synaptic transmission / positive regulation of podosome assembly / alkylglycerophosphoethanolamine phosphodiesterase activity / negative regulation of cell-substrate adhesion / GTPase activating protein binding / Wnt signaling pathway, planar cell polarity pathway / Sema4D mediated inhibition of cell attachment and migration / ossification involved in bone maturation / positive regulation of alpha-beta T cell differentiation / odontogenesis / motor neuron apoptotic process / wound healing, spreading of cells / PI3K/AKT activation / positive regulation of leukocyte adhesion to vascular endothelial cell / apical junction complex / action potential / regulation of focal adhesion assembly / neuron remodeling / negative chemotaxis / myosin binding / embryonic digit morphogenesis / myofibril / EPHA-mediated growth cone collapse / stress fiber assembly / regulation of neuron projection development / RHOC GTPase cycle / androgen receptor signaling pathway / positive regulation of cytokinesis / cellular response to cytokine stimulus / cerebral cortex cell migration / ERBB2 Regulates Cell Motility / ligand-gated ion channel signaling pathway / cleavage furrow / negative regulation of potassium ion transport / semaphorin-plexin signaling pathway
Similarity search - Function
Rho guanine nucleotide exchange factor 25 / G-protein alpha subunit, group Q / Dbl Homology Domain; Chain A / Dbl homology (DH) domain / GI Alpha 1, domain 2-like / GI Alpha 1, domain 2-like / Small GTPase Rho / small GTPase Rho family profile. / Dbl homology (DH) domain superfamily / RhoGEF domain ...Rho guanine nucleotide exchange factor 25 / G-protein alpha subunit, group Q / Dbl Homology Domain; Chain A / Dbl homology (DH) domain / GI Alpha 1, domain 2-like / GI Alpha 1, domain 2-like / Small GTPase Rho / small GTPase Rho family profile. / Dbl homology (DH) domain superfamily / RhoGEF domain / Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases / Dbl homology (DH) domain / Dbl homology (DH) domain profile. / Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB) / PH-domain like / G-protein alpha subunit, group I / PH domain profile. / Pleckstrin homology domain / Rho (Ras homology) subfamily of Ras-like small GTPases / Ras subfamily of RAS small GTPases / Small GTPase / Ras family / 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 / Rab subfamily of small GTPases / Small GTP-binding protein domain / PH-like domain superfamily / P-loop containing nucleotide triphosphate hydrolases / Roll / Up-down Bundle / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
TETRAFLUOROALUMINATE ION / GUANOSINE-5'-DIPHOSPHATE / Guanine nucleotide-binding protein G(i) subunit alpha-1 / Guanine nucleotide-binding protein G(q) subunit alpha / Transforming protein RhoA / Rho guanine nucleotide exchange factor 25
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
Mus musculus (house mouse)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 3.5 Å
AuthorsShankaranarayanan, A. / Nance, M.R. / Tesmer, J.J.G.
CitationJournal: Science / Year: 2007
Title: Structure of Galphaq-p63RhoGEF-RhoA complex reveals a pathway for the activation of RhoA by GPCRs.
Authors: Lutz, S. / Shankaranarayanan, A. / Coco, C. / Ridilla, M. / Nance, M.R. / Vettel, C. / Baltus, D. / Evelyn, C.R. / Neubig, R.R. / Wieland, T. / Tesmer, J.J.
History
DepositionOct 4, 2007Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 15, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Refinement description / Version format compliance
Revision 1.2Jun 7, 2017Group: Database references / Structure summary
Revision 1.3Oct 25, 2017Group: Refinement description / Category: software
Revision 1.4Jan 24, 2018Group: Refinement description / Category: refine / Item: _refine.pdbx_starting_model
Revision 1.5Aug 30, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_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.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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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(i) subunit alpha-1,Guanine nucleotide-binding protein G(q) subunit alpha
B: Rho guanine nucleotide exchange factor 25
C: Transforming protein RhoA
D: Guanine nucleotide-binding protein G(i) subunit alpha-1,Guanine nucleotide-binding protein G(q) subunit alpha
E: Rho guanine nucleotide exchange factor 25
F: Transforming protein RhoA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)209,21512
Polymers208,0746
Non-polymers1,1416
Water1086
1
A: Guanine nucleotide-binding protein G(i) subunit alpha-1,Guanine nucleotide-binding protein G(q) subunit alpha
B: Rho guanine nucleotide exchange factor 25
C: Transforming protein RhoA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)104,6076
Polymers104,0373
Non-polymers5703
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7490 Å2
MethodPISA
2
D: Guanine nucleotide-binding protein G(i) subunit alpha-1,Guanine nucleotide-binding protein G(q) subunit alpha
E: Rho guanine nucleotide exchange factor 25
F: Transforming protein RhoA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)104,6076
Polymers104,0373
Non-polymers5703
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7560 Å2
MethodPISA
Unit cell
Length a, b, c (Å)67.187, 68.056, 138.018
Angle α, β, γ (deg.)80.870, 85.160, 87.090
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21D
12B
22E
32B
42E
13C
23F

NCS domain segments:

Refine code: 2

Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111ARGARGMGMGAA - H35 - 36229
211ARGARGMGMGDD - K35 - 36229
112METMETLEULEUBB162 - 30214 - 154
212METMETLEULEUEE162 - 30214 - 154
322ASPASPSERSERBB318 - 490170 - 342
422ASPASPSERSEREE318 - 490170 - 342
113ILEILEGLNGLNCC4 - 1807 - 183
213ARGARGGLNGLNFF5 - 1808 - 183

NCS ensembles :
ID
1
2
3
DetailsBiological unit is a trimer. Chains A, B, and C form one biological unit. Chains D, E, and F form a second biological unit.

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Components

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Protein , 3 types, 6 molecules ADBECF

#1: Protein Guanine nucleotide-binding protein G(i) subunit alpha-1,Guanine nucleotide-binding protein G(q) subunit alpha / Adenylate cyclase-inhibiting G alpha protein / Guanine nucleotide-binding protein alpha-q


Mass: 41298.895 Da / Num. of mol.: 2
Fragment: Chimeric protein of rat Guanine nucleotide-binding protein G(i) subunit alpha-1 N-terminal helix residues 1-28 and mouse Guanine nucleotide-binding protein G(q) subunit alpha residues 31- ...Fragment: Chimeric protein of rat Guanine nucleotide-binding protein G(i) subunit alpha-1 N-terminal helix residues 1-28 and mouse Guanine nucleotide-binding protein G(q) subunit alpha residues 31-353,Chimeric protein of rat Guanine nucleotide-binding protein G(i) subunit alpha-1 N-terminal helix residues 1-28 and mouse Guanine nucleotide-binding protein G(q) subunit alpha residues 31-353
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat), (gene. exp.) Mus musculus (house mouse)
Genus: Mus / Gene: Gnai1, Gnai-1, Gnaq / Production host: Trichoplusia ni (cabbage looper) / Strain (production host): High 5 / References: UniProt: P10824, UniProt: P21279*PLUS
#2: Protein Rho guanine nucleotide exchange factor 25 / Guanine nucleotide exchange factor GEFT / Rac/Cdc42/Rho exchange factor GEFT / RhoA/Rac/Cdc42 ...Guanine nucleotide exchange factor GEFT / Rac/Cdc42/Rho exchange factor GEFT / RhoA/Rac/Cdc42 guanine nucleotide exchange factor GEFT / p63RhoGEF


Mass: 40605.383 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ARHGEF25, GEFT / Plasmid: pMCSG9 / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta DE-3 pLysS / References: UniProt: Q86VW2
#3: Protein Transforming protein RhoA / / Rho cDNA clone 12 / h12


Mass: 22132.498 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RHOA, ARH12, ARHA, RHO12 / Plasmid: pMal c2t H10 / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta De-3 pLysS / References: UniProt: P61586

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Non-polymers , 4 types, 12 molecules

#4: Chemical ChemComp-ALF / TETRAFLUOROALUMINATE ION


Mass: 102.975 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: AlF4
#5: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#6: Chemical ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE / Guanosine diphosphate


Type: RNA linking / Mass: 443.201 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H15N5O11P2 / Comment: GDP, energy-carrying molecule*YM
#7: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 6 / 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: 2.98 Å3/Da / Density % sol: 58.75 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 100 mM HEPES pH 6.5, 14.5% PEG 3350, 400 mM KCl. Drops were microseeded to obtain large crystals, VAPOR DIFFUSION, HANGING DROP, temperature 277K

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Data collection

Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-D / Wavelength: 0.9993 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Apr 13, 2007
RadiationProtocol: SINGLE WAVELENGTH / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9993 Å / Relative weight: 1
ReflectionResolution: 3.5→30 Å / Num. all: 30174 / Num. obs: 29299 / % possible obs: 97.1 % / Observed criterion σ(I): -3 / Redundancy: 2.5 % / Rmerge(I) obs: 0.087 / Rsym value: 0.087 / Χ2: 1.038 / Net I/σ(I): 5.7
Reflection shellResolution: 3.5→3.62 Å / Redundancy: 2.4 % / Rmerge(I) obs: 0.531 / Mean I/σ(I) obs: 1.67 / Num. unique all: 2976 / Rsym value: 0.53 / Χ2: 0.929 / % possible all: 98.1

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Phasing

PhasingMethod: molecular replacement
Phasing MRModel details: Phaser MODE: MR_AUTO
Highest resolutionLowest resolution
Rotation5 Å29.66 Å
Translation5 Å29.66 Å

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
PHASERphasing
REFMACrefinement
PDB_EXTRACT3data extraction
HKL-2000data collection
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2bcj (Galpha-Q), 1lb1 (RhoA; Dbs for p63)

2bcj

1lb1


Resolution: 3.5→20 Å / Cor.coef. Fo:Fc: 0.932 / SU B: 60.302 / SU ML: 0.429 / TLS residual ADP flag: LIKELY RESIDUAL / σ(F): 0 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflection
Rfree0.299 --
Rwork0.243 --
all-30159 -
obs-29080 96.42 %
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 124.405 Å2
Baniso -1Baniso -2Baniso -3
1-3.23 Å2-5.61 Å2-1.73 Å2
2---3.53 Å24.84 Å2
3----0.37 Å2
Refinement stepCycle: LAST / Resolution: 3.5→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13455 0 68 6 13529
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.02213810
X-RAY DIFFRACTIONr_bond_other_d0.0010.029653
X-RAY DIFFRACTIONr_angle_refined_deg1.1391.96718638
X-RAY DIFFRACTIONr_angle_other_deg0.838323395
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.11451635
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.40723.975707
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.52152520
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.87215114
X-RAY DIFFRACTIONr_chiral_restr0.0640.22003
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0215175
X-RAY DIFFRACTIONr_gen_planes_other0.0010.022869
X-RAY DIFFRACTIONr_nbd_refined0.2120.23268
X-RAY DIFFRACTIONr_nbd_other0.1780.29943
X-RAY DIFFRACTIONr_nbtor_refined0.1830.26625
X-RAY DIFFRACTIONr_nbtor_other0.0840.27621
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1470.2272
X-RAY DIFFRACTIONr_xyhbond_nbd_other0.0360.21
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1370.213
X-RAY DIFFRACTIONr_symmetry_vdw_other0.1750.267
X-RAY DIFFRACTIONr_mcbond_it0.591210741
X-RAY DIFFRACTIONr_mcbond_other0.10723305
X-RAY DIFFRACTIONr_mcangle_it0.817413262
X-RAY DIFFRACTIONr_scbond_it0.94946642
X-RAY DIFFRACTIONr_scangle_it1.45865374
Refine LS restraints NCS

Dom-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Ens-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1A1921TIGHT POSITIONAL0.030.05
1A2706MEDIUM POSITIONAL0.290.5
1A1921TIGHT THERMAL0.050.5
1A2706MEDIUM THERMAL0.312
2B1762TIGHT POSITIONAL0.020.05
2B2441MEDIUM POSITIONAL0.250.5
2B1762TIGHT THERMAL0.030.5
2B2441MEDIUM THERMAL0.192
3C987TIGHT POSITIONAL0.020.05
3C1311MEDIUM POSITIONAL0.230.5
3C987TIGHT THERMAL0.020.5
3C1311MEDIUM THERMAL0.132
LS refinement shellResolution: 3.5→3.588 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.406 98 -
Rwork0.354 1953 -
obs-1953 88.73 %
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)
12.0375-1.8974-0.35432.46831.08141.48550.10210.2418-0.1604-0.1907-0.1430.13470.0480.13190.0408-0.95770.1222-0.1229-0.6002-0.0373-0.557630.539-8.701-0.562
23.8722-1.2676-0.92595.13051.19554.4320.40720.9504-0.5659-0.9962-0.1786-0.65710.47930.7408-0.22860.0030.6429-0.06590.3166-0.3465-0.349648.718-34.149-37.136
32.6142-1.9870.87142.5815-0.54451.3124-0.1592-0.23610.07680.35290.0409-0.32560.02420.08670.1183-0.95280.1044-0.1883-0.5305-0.0581-0.58155.905-32.35435.2
45.3674-1.9850.43564.5196-1.39874.9011-0.6393-1.3069-0.35711.32010.0989-0.76430.22480.58450.5405-0.14520.5167-0.58350.65020.2589-0.186730.037-51.94271.117
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A35 - 358
2X-RAY DIFFRACTION1B339 - 490
3X-RAY DIFFRACTION2B149 - 338
4X-RAY DIFFRACTION2C4 - 180
5X-RAY DIFFRACTION3D35 - 358
6X-RAY DIFFRACTION3E338 - 490
7X-RAY DIFFRACTION4E150 - 337
8X-RAY DIFFRACTION4F5 - 180

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