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- PDB-2xns: Crystal Structure Of Human G alpha i1 Bound To A Designed Helical... -

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Basic information

Entry
Database: PDB / ID: 2xns
TitleCrystal Structure Of Human G alpha i1 Bound To A Designed Helical Peptide Derived From The Goloco Motif Of RGS14
Components
  • GUANINE NUCLEOTIDE-BINDING PROTEIN G(I) SUBUNIT ALPHA-1
  • REGULATOR OF G-PROTEIN SIGNALING 14
KeywordsHYDROLASE/PEPTIDE / HYDROLASE-PEPTIDE COMPLEX / ADP-RIBOSYLATION / ARGININE FINGER / GTP-BINDING / LIPOPROTEIN / NUCLEOTIDE-BINDING / PALMITATE / SIGNALING PROTEIN / TRANSDUCER / PROTEIN-PROTEIN INTERFACE DESIGN
Function / homology
Function and homology information


zygote asymmetric cell division / negative regulation of synaptic plasticity / regulation of G protein-coupled receptor signaling pathway / GTPase activating protein binding / positive regulation of neurogenesis / nucleocytoplasmic transport / spindle organization / GDP-dissociation inhibitor activity / negative regulation of G protein-coupled receptor signaling pathway / platelet-derived growth factor receptor signaling pathway ...zygote asymmetric cell division / negative regulation of synaptic plasticity / regulation of G protein-coupled receptor signaling pathway / GTPase activating protein binding / positive regulation of neurogenesis / nucleocytoplasmic transport / spindle organization / GDP-dissociation inhibitor activity / negative regulation of G protein-coupled receptor signaling pathway / platelet-derived growth factor receptor signaling pathway / negative regulation of MAP kinase activity / G-protein alpha-subunit binding / long-term memory / adenylate cyclase inhibitor activity / positive regulation of protein localization to cell cortex / T cell migration / Adenylate cyclase inhibitory pathway / D2 dopamine receptor binding / response to prostaglandin E / adenylate cyclase regulator activity / G protein-coupled serotonin receptor binding / adenylate cyclase-inhibiting serotonin receptor signaling pathway / cellular response to forskolin / GTPase activator activity / regulation of mitotic spindle organization / learning / chromosome segregation / Regulation of insulin secretion / positive regulation of cholesterol biosynthetic process / negative regulation of insulin secretion / G protein-coupled receptor binding / response to peptide hormone / adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway / PML body / visual learning / negative regulation of ERK1 and ERK2 cascade / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / G-protein beta/gamma-subunit complex binding / centriolar satellite / spindle / long-term synaptic potentiation / spindle pole / ADP signalling through P2Y purinoceptor 12 / Adrenaline,noradrenaline inhibits insulin secretion / GDP binding / G alpha (z) signalling events / ADORA2B mediated anti-inflammatory cytokines production / GPER1 signaling / heterotrimeric G-protein complex / mitotic cell cycle / signaling receptor complex adaptor activity / G protein activity / response to oxidative stress / midbody / cell cortex / G alpha (i) signalling events / G alpha (s) signalling events / microtubule binding / dendritic spine / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / microtubule / Extra-nuclear estrogen signaling / postsynaptic density / nuclear body / ciliary basal body / G protein-coupled receptor signaling pathway / lysosomal membrane / cell division / GTPase activity / dendrite / centrosome / protein kinase binding / GTP binding / nucleolus / glutamatergic synapse / magnesium ion binding / Golgi apparatus / extracellular exosome / nucleoplasm / nucleus / plasma membrane / cytoplasm / cytosol
Similarity search - Function
RGS14, RGS domain / : / : / : / GoLoco motif / GoLoco motif / GoLoco/GPR motif profile. / LGN motif, putative GEFs specific for G-alpha GTPases / RGS, subdomain 1/3 / GI Alpha 1, domain 2-like ...RGS14, RGS domain / : / : / : / GoLoco motif / GoLoco motif / GoLoco/GPR motif profile. / LGN motif, putative GEFs specific for G-alpha GTPases / RGS, subdomain 1/3 / GI Alpha 1, domain 2-like / GI Alpha 1, domain 2-like / Regulator of G protein signaling domain / RGS domain / RGS domain profile. / Regulator of G protein signalling domain / RGS, subdomain 2 / RGS domain superfamily / Raf-like Ras-binding domain / Raf-like Ras-binding / Ras-binding domain (RBD) profile. / Raf-like Ras-binding domain / G-protein alpha subunit, group I / Guanine nucleotide binding protein (G-protein), alpha subunit / G protein alpha subunit, helical insertion / G-protein alpha subunit / G-alpha domain profile. / G protein alpha subunit / Ubiquitin-like domain superfamily / P-loop containing nucleotide triphosphate hydrolases / Rossmann fold / P-loop containing nucleoside triphosphate hydrolase / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
GUANOSINE-5'-DIPHOSPHATE / S,R MESO-TARTARIC ACID / Regulator of G-protein signaling 14 / Guanine nucleotide-binding protein G(i) subunit alpha-1
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.41 Å
AuthorsBosch, D. / Sammond, D.W. / Butterfoss, G.L. / Machius, M. / Siderovski, D.P. / Kuhlman, B.
Citation
Journal: J.Am.Chem.Soc. / Year: 2011
Title: Computational Design of the Sequence and Structure of a Protein-Binding Peptide.
Authors: Sammond, D.W. / Bosch, D.E. / Butterfoss, G.L. / Purbeck, C. / Machius, M. / Siderovski, D.P. / Kuhlman, B.
#1: Journal: J.Mol.Biol. / Year: 2007
Title: Structure-Based Protocol for Identifying Mutations that Enhance Protein-Protein Binding Affinities.
Authors: Sammond, D.W. / Eletr, Z.M. / Purbeck, C. / Kimple, R.J. / Siderovski, D.P. / Kuhlman, B.
#2: Journal: Nature / Year: 2002
Title: Structural Determinants for Goloco-Induced Inhibition of Nucleotide Release by Galpha Subunits.
Authors: Kimple, R.J. / Kimple, M.E. / Betts, L. / Sondek, J. / Siderovski, D.P.
History
DepositionAug 5, 2010Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 8, 2011Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2May 8, 2019Group: Data collection / Experimental preparation / Other
Category: database_PDB_rev / database_PDB_rev_record ...database_PDB_rev / database_PDB_rev_record / exptl_crystal_grow / pdbx_database_proc / pdbx_database_status
Item: _exptl_crystal_grow.method / _pdbx_database_status.recvd_author_approval
Revision 1.3Dec 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 / 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 / _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
B: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I) SUBUNIT ALPHA-1
C: REGULATOR OF G-PROTEIN SIGNALING 14
D: REGULATOR OF G-PROTEIN SIGNALING 14
hetero molecules


Theoretical massNumber of molelcules
Total (without water)85,51810
Polymers84,1394
Non-polymers1,3796
Water18010
1
B: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I) SUBUNIT ALPHA-1
D: REGULATOR OF G-PROTEIN SIGNALING 14
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,7595
Polymers42,0702
Non-polymers6893
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5130 Å2
ΔGint-39.8 kcal/mol
Surface area16800 Å2
MethodPISA
2
A: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I) SUBUNIT ALPHA-1
C: REGULATOR OF G-PROTEIN SIGNALING 14
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,7595
Polymers42,0702
Non-polymers6893
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5140 Å2
ΔGint-39.9 kcal/mol
Surface area16830 Å2
MethodPISA
Unit cell
Length a, b, c (Å)265.261, 265.261, 265.261
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number197
Space group name H-MI23
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11B
21A
12D
22C

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1112B32 - 355
2112A32 - 355
1122D496 - 534
2122C496 - 534

NCS ensembles :
ID
1
2

NCS oper:
IDCodeMatrixVector
1given(-2.7E-5, -1, -0.000241), (-1, 2.7E-5, -0.000326), (0.000326, 0.000241, -1)0.026, 0.04029, 265.3
2given(-1.3E-5, -1, -0.001151), (-1, 1.3E-5, 4.9E-5), (-4.9E-5, 0.001151, -1)0.1261, 0.0031, 265.3

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Components

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Protein / Protein/peptide , 2 types, 4 molecules ABCD

#1: Protein GUANINE NUCLEOTIDE-BINDING PROTEIN G(I) SUBUNIT ALPHA-1 / ADENYLATE CYCLASE-INHIBITING G ALPHA PROTEIN


Mass: 37374.555 Da / Num. of mol.: 2 / Fragment: RESIDUES 30-354
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PLICGNAI1 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / References: UniProt: P63096, EC: 3.6.5.1
#2: Protein/peptide REGULATOR OF G-PROTEIN SIGNALING 14 / RGS14


Mass: 4695.173 Da / Num. of mol.: 2 / Fragment: RESIDUES 497-517 / Source method: obtained synthetically
Details: DESIGNED HELICAL PEPTIDE DERIVED FROM REGULATOR OF G- PROTEIN SIGNALING 14 GOLOCO MOTIF PEPTIDE
Source: (synth.) HOMO SAPIENS (human) / References: UniProt: O43566

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Non-polymers , 4 types, 16 molecules

#3: Chemical ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE


Type: RNA linking / Mass: 443.201 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H15N5O11P2 / Comment: GDP, energy-carrying molecule*YM
#4: Chemical ChemComp-SRT / S,R MESO-TARTARIC ACID


Mass: 150.087 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C4H6O6
#5: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: SO4
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 10 / Source method: isolated from a natural source / Formula: H2O

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Details

Sequence detailsRESIDUES 28-29 OF CHAINS A, B ARE CLONING LINKERS. PEPTIDE RESIDUES 496-516 FOR CHAINS C AND D, ...RESIDUES 28-29 OF CHAINS A, B ARE CLONING LINKERS. PEPTIDE RESIDUES 496-516 FOR CHAINS C AND D, CORRESPOND TO RESIDUES 497-517 OF HUMAN RGS14.THE 19 C-TERMINAL RESIDUES (517-535) ARE NON-BIOLOGICAL AND WAS DESIGNED TO OPTIMIZE A PROTEIN-PEPTIDE INTERFACE.

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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: 9.3 Å3/Da / Density % sol: 86.78 % / Description: NONE
Crystal growMethod: vapor diffusion, hanging drop / pH: 5.5
Details: HEXAGONAL CRYSTALS WERE GROWN BY HANGING DROP VAPOR DIFFUSION USING 1 MICROLITER PREMIXED GALPHA I1 AND GOLOCO PEPTIDE (1:1.5 MOLAR RATIO) AT 12 MG/ML IN BUFFER (10 MM TRIS PH 7.5, 1 MM ...Details: HEXAGONAL CRYSTALS WERE GROWN BY HANGING DROP VAPOR DIFFUSION USING 1 MICROLITER PREMIXED GALPHA I1 AND GOLOCO PEPTIDE (1:1.5 MOLAR RATIO) AT 12 MG/ML IN BUFFER (10 MM TRIS PH 7.5, 1 MM MAGNESIUM CHLORIDE, 10 MICROMOLAR GDP, 5 MM DTT) AND 1 MICROLITER CRYSTALLIZATION SOLUTION (800 MM AMMONIUM SULFATE, 200 MM K/NA TARTRATE, 100 MM SODIUM CITRATE PH 5.5).

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1
DetectorType: MARRESEARCH / Detector: CCD / Date: Apr 10, 2010 / Details: MIRRORS
RadiationMonochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.41→40 Å / Num. obs: 42418 / % possible obs: 100 % / Observed criterion σ(I): -3 / Redundancy: 11.1 % / Biso Wilson estimate: 99.9 Å2 / Rmerge(I) obs: 0.12 / Net I/σ(I): 22.1
Reflection shellResolution: 3.41→3.42 Å / Redundancy: 11.1 % / Rmerge(I) obs: 1 / Mean I/σ(I) obs: 2.2 / % 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 2OM2

2om2


Resolution: 3.41→39.99 Å / Cor.coef. Fo:Fc: 0.924 / Cor.coef. Fo:Fc free: 0.886 / SU B: 30.905 / SU ML: 0.234 / Cross valid method: THROUGHOUT / ESU R: 0.445 / ESU R Free: 0.319 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES WITH TLS ADDED.
RfactorNum. reflection% reflectionSelection details
Rfree0.24434 1489 3.5 %RANDOM
Rwork0.2226 ---
obs0.22335 40893 99.83 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 108.9 Å2
Refinement stepCycle: LAST / Resolution: 3.41→39.99 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5728 0 86 10 5824
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0060.0225958
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.0911.968044
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.7295714
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.19124.371302
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.585151076
X-RAY DIFFRACTIONr_dihedral_angle_4_deg14.7141540
X-RAY DIFFRACTIONr_chiral_restr0.0650.2882
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.024480
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.1840.22751
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3010.24047
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1240.2166
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1860.261
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1470.22
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.2721.53542
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it0.51425706
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it0.49132416
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it0.894.52338
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
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
12A1268tight positional0.030.05
11B1268tight positional0.030.05
22C160tight positional00.05
21D160tight positional00.05
12A1313medium positional0.060.5
11B1313medium positional0.060.5
22C170medium positional00.5
21D170medium positional00.5
12A1268tight thermal0.030.5
11B1268tight thermal0.030.5
22C160tight thermal00.5
21D160tight thermal00.5
12A1313medium thermal0.042
11B1313medium thermal0.042
22C170medium thermal0.012
21D170medium thermal0.012
LS refinement shellResolution: 3.406→3.494 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.312 107 -
Rwork0.3 3020 -
obs--99.84 %
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)
16.11790.0571-2.4782.71690.59361.52440.12961.12430.7124-0.7756-0.03840.0881-0.2799-0.3672-0.09120.2725-0.039-0.11020.53440.06050.5962-39.600923.772112.1388
29.7352-1.26640.36066.2406-1.09814.135-0.21050.1310.5506-0.2506-0.0228-0.0766-0.3976-0.41330.23330.0888-0.0141-0.06280.303-0.13730.4134-56.638215.6098129.8422
34.02762.2645-1.79831.7861-1.83873.3477-0.2550.8210.348-0.14870.23540.1164-0.3649-0.43180.01960.29990.0179-0.11630.58310.00570.7719-42.88224.9603116.8896
44.6948-2.68681.95323.05961.45987.69570.61431.3069-0.6718-1.017-0.73020.32630.5722-0.37980.1161.1999-0.4060.1370.9068-0.13410.7643-29.553812.1253102.431
52.7635-1.47392.89443.2263-1.27683.15670.38530.4203-0.2515-1.0236-0.38820.46340.50440.32160.00290.6441-0.09910.24620.2161-0.27250.8101-26.50096.6605118.4637
64.119-0.57-1.40886.1039-3.42778.8715-0.05070.3614-0.2157-0.3136-0.1261-0.26990.14170.6420.17680.0284-0.0037-0.04670.1235-0.07830.5659-22.39216.9902124.4159
72.92110.05070.41035.8689-2.5221.904-0.0409-0.75490.07221.15130.11880.6747-0.3511-0.2916-0.07790.5385-0.04780.04970.2567-0.11150.5837-23.77539.6014153.1366
86.1522-1.227-1.18049.60680.22555.0539-0.0088-0.2366-0.10570.114-0.23380.5648-0.4493-0.41820.24250.2963-0.0168-0.14060.0849-0.05990.4092-15.612756.639135.4318
91.88182.5006-1.81824.1667-1.95113.03930.2478-0.14780.12080.803-0.30030.3733-0.3904-0.33230.05240.58450.00460.00390.2774-0.12220.7759-24.963342.8821148.3855
102.6296-2.71750.87844.51942.18518.169-0.8095-0.85140.39991.30040.6747-0.7-0.35250.73070.13480.9066-0.3963-0.13281.1320.1450.7862-12.128729.5572162.8464
113.5312-1.2926-0.9632.59952.73373.0177-0.3817-1.02790.4540.39350.41-0.26580.29150.5081-0.02830.217-0.1064-0.24940.63520.22970.7934-6.662726.5021146.815
125.9852-0.451-3.1344.3928-1.56768.5403-0.126-0.3337-0.260.3506-0.0429-0.18350.65670.1520.16890.1248-0.0008-0.06930.032-0.05140.5646-16.991522.3927140.8618
1389.6311-26.1329-15.11837.863613.95275.5819-1.1671-2.4066-0.6778-0.30431.9962-2.52930.14740.905-0.82911.49840.20890.06731.1575-0.15220.8329-26.2772-1.4936106.7664
1415.92951.6278-3.1772.44480.10830.7258-0.6096-0.4874-0.3931-0.43550.55360.0270.10080.16950.0560.4514-0.2755-0.01430.6911-0.11410.5478-39.10887.2939115.2741
152.01972.2068-0.11322.5761-0.26260.1256-0.71410.96970.1042-0.79560.7283-0.00370.10570.1867-0.01430.2586-0.19720.09151.021-0.08290.9269-58.29559.7384116.6115
1611.05965.9311-11.35819.4993-13.505120.3643-0.58450.5877-0.0270.1762-0.9725-1.3933-0.00240.83051.55710.1732-0.0718-0.24290.6983-0.18050.8483-59.82853.0884128.0146
1738.1365-36.720516.876886.7972-22.25488.18111.9574-0.2186-2.7971-2.4244-1.084-0.75690.97730.1738-0.87331.16330.1347-0.1441.42380.07880.90141.481826.2864158.5341
184.34310.8250.590317.2833-4.26021.20840.6889-0.27790.0229-0.2186-0.726-0.19370.12420.19590.03710.66-0.2821-0.11650.42580.00810.5171-7.302639.1145150.0199
192.09752.82420.3193.84850.47560.09710.754-0.51440.12191.2006-0.6870.15050.2774-0.0515-0.06710.8581-0.1321-0.15730.17570.070.9062-9.742458.3007148.6703
209.78583.866-12.663813.8742-8.07617.1535-0.95350.2448-1.34290.5624-0.54950.150.9462-0.17011.5030.6392-0.0903-0.20040.2075-0.23290.7634-3.091759.8284137.269
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A32 - 82
2X-RAY DIFFRACTION2A83 - 145
3X-RAY DIFFRACTION3A146 - 193
4X-RAY DIFFRACTION4A194 - 218
5X-RAY DIFFRACTION5A219 - 263
6X-RAY DIFFRACTION6A264 - 347
7X-RAY DIFFRACTION7B32 - 82
8X-RAY DIFFRACTION8B83 - 145
9X-RAY DIFFRACTION9B146 - 193
10X-RAY DIFFRACTION10B194 - 218
11X-RAY DIFFRACTION11B219 - 263
12X-RAY DIFFRACTION12B264 - 347
13X-RAY DIFFRACTION13C496 - 502
14X-RAY DIFFRACTION14C503 - 517
15X-RAY DIFFRACTION15C518 - 528
16X-RAY DIFFRACTION16C529 - 534
17X-RAY DIFFRACTION17D496 - 502
18X-RAY DIFFRACTION18D503 - 517
19X-RAY DIFFRACTION19D518 - 528
20X-RAY DIFFRACTION20D529 - 534

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