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- PDB-2xtz: Crystal structure of the G alpha protein AtGPA1 from Arabidopsis ... -

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Basic information

Entry
Database: PDB / ID: 2xtz
TitleCrystal structure of the G alpha protein AtGPA1 from Arabidopsis thaliana
ComponentsGUANINE NUCLEOTIDE-BINDING PROTEIN ALPHA-1 SUBUNIT
KeywordsHYDROLASE / G-PROTEIN SIGNALING / SELF-ACTIVATION / RAS-LIKE DOMAIN
Function / homology
Function and homology information


thylakoid membrane organization / response to low fluence blue light stimulus by blue low-fluence system / blue light signaling pathway / positive regulation of abscisic acid-activated signaling pathway / gibberellic acid mediated signaling pathway / regulation of stomatal closure / response to pheromone / seed germination / tyrosine biosynthetic process / regulation of stomatal movement ...thylakoid membrane organization / response to low fluence blue light stimulus by blue low-fluence system / blue light signaling pathway / positive regulation of abscisic acid-activated signaling pathway / gibberellic acid mediated signaling pathway / regulation of stomatal closure / response to pheromone / seed germination / tyrosine biosynthetic process / regulation of stomatal movement / cell death / GTPase inhibitor activity / L-phenylalanine biosynthetic process / plasmodesma / channel regulator activity / abscisic acid-activated signaling pathway / response to glucose / reactive oxygen species metabolic process / G protein-coupled receptor binding / G-protein beta/gamma-subunit complex binding / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / peroxisome / heterotrimeric G-protein complex / GTPase binding / regulation of cell population proliferation / G protein-coupled receptor signaling pathway / GTPase activity / GTP binding / endoplasmic reticulum membrane / metal ion binding / plasma membrane
Similarity search - Function
Plant G-protein, alpha subunit / GI Alpha 1, domain 2-like / GI Alpha 1, domain 2-like / 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 / P-loop containing nucleotide triphosphate hydrolases / P-loop containing nucleoside triphosphate hydrolase ...Plant G-protein, alpha subunit / GI Alpha 1, domain 2-like / GI Alpha 1, domain 2-like / 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 / P-loop containing nucleotide triphosphate hydrolases / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE / Guanine nucleotide-binding protein alpha-1 subunit
Similarity search - Component
Biological speciesARABIDOPSIS THALIANA (thale cress)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.34 Å
AuthorsJones, J.C. / Duffy, J.W. / Machius, M. / Temple, B.R.S. / Dohlman, H.G. / Jones, A.M.
Citation
Journal: Sci.Signal. / Year: 2011
Title: The Crystal Structure of a Self-Activating G Protein Alpha Subunit Reveals its Distinct Mechanism of Signal Initiation
Authors: Jones, J.C. / Duffy, J.W. / Machius, M. / Temple, B.R.S. / Dohlman, H.G. / Jones, A.M.
#1: Journal: Proc.Natl.Acad.Sci.USA / Year: 2007
Title: Gtpase Acceleration as the Rate-Limiting Step in Arabidopsis G Protein-Coupled Sugar Signaling.
Authors: Johnston, C.A. / Taylor, J.P. / Gao, Y. / Kimple, A.J. / Grigston, J.C. / Chen, J. / Siderovski, D.P. / Jones, A.M. / Willard, F.S.
History
DepositionOct 13, 2010Deposition site: PDBE / Processing site: PDBE
Revision 1.0Feb 16, 2011Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Apr 3, 2019Group: Data collection / Derived calculations ...Data collection / Derived calculations / Experimental preparation / Other
Category: exptl_crystal_grow / pdbx_database_proc ...exptl_crystal_grow / pdbx_database_proc / pdbx_database_status / struct_conn
Item: _exptl_crystal_grow.temp / _pdbx_database_status.recvd_author_approval / _struct_conn.pdbx_leaving_atom_flag
Revision 1.4May 15, 2019Group: Data collection / Experimental preparation / Category: exptl_crystal_grow / Item: _exptl_crystal_grow.method
Revision 1.5Dec 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _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.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.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _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_conn.ptnr2_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 ALPHA-1 SUBUNIT
B: GUANINE NUCLEOTIDE-BINDING PROTEIN ALPHA-1 SUBUNIT
C: GUANINE NUCLEOTIDE-BINDING PROTEIN ALPHA-1 SUBUNIT
hetero molecules


Theoretical massNumber of molelcules
Total (without water)125,53818
Polymers123,2253
Non-polymers2,31315
Water4,486249
1
A: GUANINE NUCLEOTIDE-BINDING PROTEIN ALPHA-1 SUBUNIT
hetero molecules


Theoretical massNumber of molelcules
Total (without water)41,7705
Polymers41,0751
Non-polymers6954
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: GUANINE NUCLEOTIDE-BINDING PROTEIN ALPHA-1 SUBUNIT
hetero molecules


Theoretical massNumber of molelcules
Total (without water)41,8066
Polymers41,0751
Non-polymers7315
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: GUANINE NUCLEOTIDE-BINDING PROTEIN ALPHA-1 SUBUNIT
hetero molecules


Theoretical massNumber of molelcules
Total (without water)41,9627
Polymers41,0751
Non-polymers8876
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)67.130, 119.347, 161.725
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

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Protein , 1 types, 3 molecules ABC

#1: Protein GUANINE NUCLEOTIDE-BINDING PROTEIN ALPHA-1 SUBUNIT


Mass: 41075.090 Da / Num. of mol.: 3 / Fragment: RESIDUES 37-383
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) ARABIDOPSIS THALIANA (thale cress) / Plasmid: PPROEX-HTB / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / Variant (production host): CODON PLUS (RIPL) / References: UniProt: P18064, EC: 3.6.5.1

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Non-polymers , 5 types, 264 molecules

#2: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Mg
#3: Chemical ChemComp-GSP / 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE


Mass: 539.246 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C10H16N5O13P3S
#4: Chemical
ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Cl
#5: Chemical
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: SO4
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 249 / Source method: isolated from a natural source / Formula: H2O

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Details

Sequence detailsTHE 36 N-TERMINAL RESIDUES OF THE FULL-LENGTH PROTEIN WERE REMOVED FOR CRYSTALLIZATION PURPOSES. ...THE 36 N-TERMINAL RESIDUES OF THE FULL-LENGTH PROTEIN WERE REMOVED FOR CRYSTALLIZATION PURPOSES. THE N-TERMINAL SEQUENCE 'GAMGSGI' OF THE FINAL PROTEIN STEMS FROM THE EXPRESSION LINKER.

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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: 2.6 Å3/Da / Density % sol: 53.3 % / Description: NONE
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6
Details: CRYSTALS OF ATGPA1 WERE GROWN AT 4 DEGREES CELSIUS USING THE HANGING-DROP VAPOR-DIFFUSION METHOD. DROPS CONTAINED 1.5 UL OF PROTEIN SOLUTION (20 MG/ML ATGPA1 IN 25 MM TRIS-HCL, PH 7.4, 5% ...Details: CRYSTALS OF ATGPA1 WERE GROWN AT 4 DEGREES CELSIUS USING THE HANGING-DROP VAPOR-DIFFUSION METHOD. DROPS CONTAINED 1.5 UL OF PROTEIN SOLUTION (20 MG/ML ATGPA1 IN 25 MM TRIS-HCL, PH 7.4, 5% (V/V) GLYCEROL, 150 MM SODIUM CHLORIDE, 1 MM DTT, 500 UL GTP-GAMMA-S) AND WERE EQUILIBRATED AGAINST 1.5 UL OF 0.3 M MAGNESIUM SULFATE, 0.1 M SODIUM CACODYLATE, PH 6.0, 21% (W/V) PEG 8000. INITIALLY OBTAINED CRYSTALS WERE USED FOR MACROSEEDING. CRYSTALS REACHED THEIR FINAL ROD-SHAPE FORM WITHIN 14 DAYS AFTER MACROSEEDING AND WERE CRYOPROTECTED IN THE MOTHER LIQUOR WITH 8% (V/V) GLYCEROL.

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1
DetectorType: MARRESEARCH MX300 / Detector: CCD / Date: Nov 16, 2009 / Details: CUSTOM
RadiationMonochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.34→44.6 Å / Num. obs: 55808 / % possible obs: 100 % / Observed criterion σ(I): -3 / Redundancy: 6 % / Biso Wilson estimate: 52.9 Å2 / Rmerge(I) obs: 0.11 / Net I/σ(I): 17.5
Reflection shellResolution: 2.34→2.36 Å / Redundancy: 5.8 % / Rmerge(I) obs: 0.84 / Mean I/σ(I) obs: 1.9 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.5.0109refinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1FQJ

1fqj


Resolution: 2.34→96.03 Å / Cor.coef. Fo:Fc: 0.931 / Cor.coef. Fo:Fc free: 0.904 / SU B: 14.851 / SU ML: 0.164 / Cross valid method: THROUGHOUT / ESU R: 0.295 / ESU R Free: 0.229 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS
RfactorNum. reflection% reflectionSelection details
Rfree0.25378 1520 2.7 %RANDOM
Rwork0.2113 ---
obs0.21247 54216 99.89 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 44.512 Å2
Baniso -1Baniso -2Baniso -3
1-0.03 Å20 Å20 Å2
2--1.37 Å20 Å2
3----1.4 Å2
Refinement stepCycle: LAST / Resolution: 2.34→96.03 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7505 0 128 249 7882
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.0227813
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.2491.98410547
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.2565900
X-RAY DIFFRACTIONr_dihedral_angle_2_deg38.60924.016381
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.294151459
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.8571553
X-RAY DIFFRACTIONr_chiral_restr0.0790.21153
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0215743
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.1950.23254
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3040.25281
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1470.2378
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined0.0430.23
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1880.261
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1570.219
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.4071.54520
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it0.80227340
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it1.47333293
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it2.3684.53207
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.338→2.399 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.321 129 -
Rwork0.261 3918 -
obs--98.92 %
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)
12.3786-0.86162.84861.8837-0.32324.2930.0125-0.0102-0.2321-0.09230.0750.10720.1089-0.2476-0.08760.0377-0.06830.04070.1298-0.08270.0797-25.1582-28.32510.5359
220.58997.2709-6.3582.7529-2.35462.0328-0.32220.7298-0.5566-0.31450.2620.05770.2558-0.24390.06020.4933-0.112-0.11090.4865-0.16720.4514-17.9729-41.49342.7805
37.73951.19067.14571.42651.817810.8649-0.32370.16230.53010.0884-0.1585-0.3789-0.1830.8610.48220.09670.02-0.03580.32250.10930.26374.8471-31.441816.1836
40.1450.68230.20874.4106-0.00249.9746-0.0720.13790.0435-0.15180.116-0.3144-0.19881.7469-0.0440.23360.0892-0.0740.77450.05710.467415.6693-33.343719.4822
51.73910.73130.99392.01470.91533.5297-0.02340.0764-0.26480.1513-0.0936-0.14950.83160.55980.1170.26050.16730.06230.26060.03260.2282.3427-39.424415.0722
65.7881-2.1051-0.07153.6772-1.13052.99040.16150.5161-0.23320.0967-0.19170.28830.2059-0.0590.03010.0973-0.02330.04780.0826-0.04940.0501-17.8151-31.32218.5662
76.30853.31153.10524.4591.75973.4343-0.27620.36330.354-0.56640.12230.1312-0.287-0.16250.15390.08750.016-0.00440.08650.02230.023-21.5513-19.347210.3325
81.84030.31580.21371.9106-0.85192.65310.0162-0.1901-0.00990.1868-0.1053-0.0614-0.00260.0020.08910.0244-0.01780.0020.0476-0.01350.0147-17.3075-25.343929.4339
93.592-1.0546-0.70973.33960.88171.9279-0.0497-0.0108-0.16660.0558-0.06780.29960.3187-0.24650.11750.0593-0.05240.0130.0598-0.0150.0302-29.5288-28.006323.7806
1033.6417-16.27820.531816.70254.53712.1049-0.2641-0.22590.7825-1.08740.33870.9717-0.2194-1.4948-0.07460.2671-0.1373-0.17020.40530.08880.3706-43.4818-26.858617.6012
112.50782.44395.37432.38765.241711.52080.45780.3266-0.25870.5140.2098-0.26471.17710.6967-0.66750.29580.10450.0130.0585-0.03430.0745-12.5299-31.501216.8848
122.6484-0.3055-0.26263.93330.34335.0032-0.03550.3361-0.2814-0.5938-0.0456-0.21140.21210.26770.08110.1088-0.00540.03910.153-0.00020.0564-23.7615-68.628332.1529
136.9845-1.1293-3.87490.5670.45832.4006-0.070.8936-1.5933-0.6499-0.53070.31090.1871-0.1930.60071.16970.2839-0.10590.7378-0.24840.6053-30.709-71.309518.8855
1412.5482-6.05-7.8389.62012.3838.32250.0104-0.058-0.42860.10260.23851.4712-0.466-0.8659-0.24890.35890.067-0.13120.43680.0950.4944-48.8139-62.748228.9494
156.6477-1.5785-2.588110.01512.35559.11260.24940.17440.1181-0.4770.04470.2016-0.4292-0.3891-0.29410.40420.097-0.10080.56460.06880.6419-52.8999-56.724925.5209
1611.315-1.41-0.95712.29794.3428.72490.20850.74460.3154-0.2255-0.19110.1301-0.1772-0.3632-0.01750.6132-0.0165-0.20360.41380.15190.4852-41.5838-60.123219.2915
175.8564-1.5190.52829.0399-4.69569.5575-0.1050.3833-0.0704-0.76080.23870.47520.2189-0.433-0.13370.1916-0.0756-0.06940.17810.01710.0329-32.7622-68.701928.2347
188.0355-0.1085-4.27321.7309-0.23256.1187-0.25690.4627-0.4822-0.42420.046-0.27820.41980.23980.21080.14450.00030.06560.14320.00010.1375-22.9623-75.524936.7112
191.60190.4325-0.25454.032-0.77621.51460.0256-0.0750.11660.1246-0.00280.097-0.17450.1332-0.02280.0225-0.0291-0.00120.12280.02650.0185-27.0691-57.268145.4745
202.1323-0.02972.41162.5279-0.51026.10.03180.17950.0312-0.215-0.0149-0.345-0.03550.5912-0.01690.0422-0.01350.05220.18520.05060.1019-15.1847-60.744140.3394
2133.9929-5.47226.444417.318110.761528.1225-0.22690.5257-0.39780.70650.4486-2.08490.50552.5472-0.22170.30120.09580.07970.5150.150.5403-4.0264-66.159635.8075
220.17540.9546-1.67315.2308-9.158916.0390.0977-0.0654-0.02240.3579-0.2782-0.0829-0.63490.54490.18050.1558-0.0733-0.02760.10390.06860.0517-32.2264-63.222333.11
233.2246-0.06921.17432.87520.52144.4284-0.0555-0.1796-0.878-0.1204-0.08880.4681.09960.02350.14430.39670.07370.10370.07470.03680.3471-34.7925-71.8196-17.6907
2422.40144.7921-0.12992.7495-0.44324.91240.40010.5035-0.2270.3036-0.3055-0.25630.38360.4598-0.09450.66810.22110.0450.35110.14250.6621-20.0006-80.2206-12.5577
257.18910.42474.23721.12770.3122.5240.2496-0.78210.14790.7813-0.2220.10430.2216-0.611-0.02770.94280.12060.02021.22270.14480.9412-6.1498-80.1726-2.1699
261.4392-1.31310.00329.1163-2.48892.136-0.0252-0.4449-0.41870.7704-0.306-0.26630.37920.48380.33120.75880.15070.02180.70340.0950.7345-17.0338-81.0119-5.2871
273.30961.3305-1.01184.2863-0.67335.5205-0.1277-0.1008-0.72680.10270.02510.07990.491-0.07840.10260.5610.1130.15790.18820.06770.5231-30.2127-77.9586-16.1432
285.16651.7448-0.77762.77060.64293.2594-0.33460.2559-0.635-0.10.22090.14090.71430.07910.11360.23910.05020.05570.0660.02740.2155-32.7875-65.7932-21.8643
296.275-0.34040.21233.31140.08454.963-0.20750.0399-0.0484-0.11950.08740.04910.32320.44590.12010.08340.04850.03990.05560.02170.0388-31.0149-57.78-18.2664
303.73340.2541.46254.85090.99037.361-0.0795-0.788-0.11431.27460.0849-0.42-0.21610.8217-0.00530.4270.0652-0.05710.50.08570.1124-27.2656-55.34590.6685
314.4022-1.74871.13173.8513-1.38733.878-0.1319-0.3638-0.1250.27710.12070.27860.1447-0.14820.01110.0690.03520.06570.08630.02640.0813-40.0616-55.8019-10.3611
3214.8542-4.17437.03545.3645-1.87069.92-0.0326-0.9284-0.6354-0.43780.36410.83551.0335-1.1416-0.33140.4863-0.15710.10140.22050.13910.5254-48.3449-70.4161-11.045
3325.3479-1.0984-20.9050.09161.833236.80090.5808-0.5566-0.6493-0.01430.0246-0.0235-0.3097-0.0854-0.60530.37370.17840.10230.1330.12190.2726-26.1138-70.8601-11.9296
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A32 - 60
2X-RAY DIFFRACTION2A61 - 73
3X-RAY DIFFRACTION3A74 - 100
4X-RAY DIFFRACTION4A101 - 124
5X-RAY DIFFRACTION5A125 - 184
6X-RAY DIFFRACTION6A185 - 204
7X-RAY DIFFRACTION7A211 - 234
8X-RAY DIFFRACTION8A235 - 331
9X-RAY DIFFRACTION9A332 - 372
10X-RAY DIFFRACTION10A373 - 380
11X-RAY DIFFRACTION11A1382
12X-RAY DIFFRACTION12B38 - 61
13X-RAY DIFFRACTION13B62 - 77
14X-RAY DIFFRACTION14B78 - 92
15X-RAY DIFFRACTION15B93 - 152
16X-RAY DIFFRACTION16B161 - 182
17X-RAY DIFFRACTION17B183 - 198
18X-RAY DIFFRACTION18B199 - 234
19X-RAY DIFFRACTION19B235 - 331
20X-RAY DIFFRACTION20B332 - 370
21X-RAY DIFFRACTION21B371 - 377
22X-RAY DIFFRACTION22B1379
23X-RAY DIFFRACTION23C38 - 59
24X-RAY DIFFRACTION24C60 - 89
25X-RAY DIFFRACTION25C90 - 144
26X-RAY DIFFRACTION26C158 - 181
27X-RAY DIFFRACTION27C182 - 203
28X-RAY DIFFRACTION28C213 - 249
29X-RAY DIFFRACTION29C250 - 287
30X-RAY DIFFRACTION30C288 - 320
31X-RAY DIFFRACTION31C321 - 356
32X-RAY DIFFRACTION32C357 - 380
33X-RAY DIFFRACTION33C1382

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