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- PDB-4asu: F1-ATPase in which all three catalytic sites contain bound nucleo... -

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Basic information

Entry
Database: PDB / ID: 4asu
TitleF1-ATPase in which all three catalytic sites contain bound nucleotide, with magnesium ion released in the Empty site
Components(ATP SYNTHASE SUBUNIT ...) x 5
KeywordsHYDROLASE
Function / homology
Function and homology information


Formation of ATP by chemiosmotic coupling / Cristae formation / mitochondrial proton-transporting ATP synthase complex assembly / mitochondrial envelope / mitochondrial proton-transporting ATP synthase, catalytic core / proton-transporting ATP synthase complex / mitochondrial proton-transporting ATP synthase complex / mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1) / proton motive force-driven mitochondrial ATP synthesis / proton motive force-driven ATP synthesis ...Formation of ATP by chemiosmotic coupling / Cristae formation / mitochondrial proton-transporting ATP synthase complex assembly / mitochondrial envelope / mitochondrial proton-transporting ATP synthase, catalytic core / proton-transporting ATP synthase complex / mitochondrial proton-transporting ATP synthase complex / mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1) / proton motive force-driven mitochondrial ATP synthesis / proton motive force-driven ATP synthesis / proton transmembrane transporter activity / proton-transporting ATP synthase complex, catalytic core F(1) / aerobic respiration / H+-transporting two-sector ATPase / proton-transporting ATPase activity, rotational mechanism / proton transmembrane transport / proton-transporting ATP synthase activity, rotational mechanism / ADP binding / mitochondrial inner membrane / ATP hydrolysis activity / ATP binding / plasma membrane
Similarity search - Function
ATP Synthase; domain 1 / F0F1 ATP synthase delta/epsilon subunit, N-terminal / ATP synthase, F1 complex, gamma subunit / ATP synthase alpha/beta chain, C-terminal domain / Lysin / Thrombin, subunit H - #170 / Elongation Factor Tu (Ef-tu); domain 3 - #20 / Pyruvate Kinase; Chain: A, domain 1 / : / Metazoan delta subunit of F1F0-ATP synthase, C-terminal domain ...ATP Synthase; domain 1 / F0F1 ATP synthase delta/epsilon subunit, N-terminal / ATP synthase, F1 complex, gamma subunit / ATP synthase alpha/beta chain, C-terminal domain / Lysin / Thrombin, subunit H - #170 / Elongation Factor Tu (Ef-tu); domain 3 - #20 / Pyruvate Kinase; Chain: A, domain 1 / : / Metazoan delta subunit of F1F0-ATP synthase, C-terminal domain / Bovine Mitochondrial F1-ATPase, ATP Synthase Beta Chain; Chain D, domain3 / Bovine Mitochondrial F1-atpase; Atp Synthase Beta Chain; Chain D, domain 3 / ATP synthase, gamma subunit, helix hairpin domain / ATP synthase delta/epsilon subunit, C-terminal domain superfamily / ATP synthase, F1 complex, epsilon subunit, mitochondrial / ATP synthase, F1 complex, epsilon subunit superfamily, mitochondrial / Mitochondrial ATP synthase epsilon chain / ATP synthase, F1 complex, delta/epsilon subunit / ATP synthase, F1 complex, delta/epsilon subunit, N-terminal / F0F1 ATP synthase delta/epsilon subunit, N-terminal / ATP synthase, Delta/Epsilon chain, beta-sandwich domain / ATP synthase, F1 complex, gamma subunit conserved site / ATP synthase gamma subunit signature. / ATP synthase, F1 complex, beta subunit / ATP synthase, alpha subunit, C-terminal domain superfamily / ATP synthase, F1 complex, gamma subunit / ATP synthase, F1 complex, gamma subunit superfamily / ATP synthase / ATP synthase, alpha subunit, C-terminal / ATP synthase, F1 complex, alpha subunit / ATP synthase, F1 complex, alpha subunit nucleotide-binding domain / ATP synthase alpha/beta chain, C terminal domain / ATPase, F1/V1 complex, beta/alpha subunit, C-terminal / ATP synthase subunit alpha, N-terminal domain-like superfamily / ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain superfamily / ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain / ATP synthase alpha/beta family, beta-barrel domain / ATPase, alpha/beta subunit, nucleotide-binding domain, active site / ATP synthase alpha and beta subunits signature. / ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain / ATP synthase alpha/beta family, nucleotide-binding domain / Elongation Factor Tu (Ef-tu); domain 3 / Helix Hairpins / Thrombin, subunit H / P-loop containing nucleotide triphosphate hydrolases / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / Up-down Bundle / Beta Barrel / Sandwich / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
ADENOSINE-5'-DIPHOSPHATE / ATP synthase subunit beta, mitochondrial / ATP synthase subunit delta, mitochondrial / ATP synthase subunit gamma, mitochondrial / ATP synthase subunit epsilon, mitochondrial / ATP synthase subunit alpha, mitochondrial
Similarity search - Component
Biological speciesBOS TAURUS (cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.6 Å
AuthorsRees, D.M. / Montgomery, M.G. / Leslie, A.G.W. / Walker, J.E.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2012
Title: Structural Evidence of a New Catalytic Intermediate in the Pathway of ATP Hydrolysis by F1-ATPase from Bovine Heart Mitochondria.
Authors: Rees, D.M. / Montgomery, M.G. / Leslie, A.G. / Walker, J.E.
History
DepositionMay 3, 2012Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 27, 2012Provider: repository / Type: Initial release
Revision 1.1Jul 4, 2012Group: Other
Revision 1.2Jul 25, 2012Group: Database references
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 / pdbx_struct_conn_angle / struct_conn / struct_sheet / 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_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_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.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_conn.ptnr2_label_seq_id / _struct_sheet.number_strands / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Remark 700 SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 19-STRANDED BARREL THIS IS REPRESENTED BY A 20-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "FA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL
B: ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL
C: ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL
D: ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL
E: ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL
F: ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL
G: ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL
H: ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL
I: ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL
hetero molecules


Theoretical massNumber of molelcules
Total (without water)374,47420
Polymers371,7899
Non-polymers2,68511
Water5,549308
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area39750 Å2
ΔGint-237.3 kcal/mol
Surface area110810 Å2
MethodPISA
Unit cell
Length a, b, c (Å)105.268, 135.113, 266.355
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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ATP SYNTHASE SUBUNIT ... , 5 types, 9 molecules ABCDEFGHI

#1: Protein ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL /


Mass: 55301.207 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P19483
#2: Protein ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL /


Mass: 51615.684 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle
References: UniProt: P00829, H+-transporting two-sector ATPase
#3: Protein ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL / / F-ATPASE GAMMA SUBUNIT


Mass: 30300.760 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P05631
#4: Protein ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL / / F-ATPASE DELTA SUBUNIT


Mass: 15074.813 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P05630
#5: Protein/peptide ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL / / ATPASE SUBUNIT EPSILON


Mass: 5662.693 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P05632

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Non-polymers , 3 types, 319 molecules

#6: Chemical
ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE / Adenosine diphosphate


Mass: 427.201 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#7: Chemical
ChemComp-MG / MAGNESIUM ION


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


Mass: 18.015 Da / Num. of mol.: 308 / Source method: isolated from a natural source / Formula: H2O

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Details

Sequence detailsDIFFERENT RESIDUE: GLY A 481, GLY B 481, GLY C 481 THIS RESIDUE WAS IDENTIFIED AS A GLY FROM THE ...DIFFERENT RESIDUE: GLY A 481, GLY B 481, GLY C 481 THIS RESIDUE WAS IDENTIFIED AS A GLY FROM THE PROTEIN SEQUENCE. IN THE CDNA SEQUENCE THE CODON FOR THIS RESIDUE WAS AGC (SER) IN THREE CLONES, WHILE IN TWO OTHERS IT WAS GGC (GLY). THE DIFFERENCE WAS THOUGHT TO BE DUE TO A MUTATION OCCURRING DURING EITHER PROPAGATION OF THE CLONES IN THE LIBRARY OR SUBCLONING INTO M13 VECTORS. THE ELECTRON DENSITY IN HIGHER RESOLUTION STRUCTURES SUGGESTS A GLY IN THIS POSITION.

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.8 Å3/Da / Density % sol: 56 % / Description: NONE

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.9393
DetectorType: ADSC CCD / Detector: CCD / Date: Sep 2, 2006 / Details: TORODIAL FOCUSING MIRROR
RadiationMonochromator: CHANNEL CUT / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9393 Å / Relative weight: 1
ReflectionResolution: 2.59→133.18 Å / Num. obs: 92081 / % possible obs: 78.4 % / Observed criterion σ(I): 3 / Redundancy: 3.7 % / Rmerge(I) obs: 0.12 / Net I/σ(I): 4.4
Reflection shellResolution: 2.59→2.73 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.84 / Mean I/σ(I) obs: 1.7 / % possible all: 66

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Processing

Software
NameVersionClassification
REFMAC5.6.0119refinement
MOSFLMdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2JDI

2jdi


Resolution: 2.6→63.5 Å / Cor.coef. Fo:Fc: 0.905 / Cor.coef. Fo:Fc free: 0.864 / SU B: 31.727 / SU ML: 0.326 / Cross valid method: THROUGHOUT / ESU R Free: 0.437 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.28933 4568 5 %RANDOM
Rwork0.24487 ---
obs0.24711 87491 77.98 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 50.97 Å2
Baniso -1Baniso -2Baniso -3
1-1.02 Å20 Å20 Å2
2--0.88 Å20 Å2
3----1.9 Å2
Refinement stepCycle: LAST / Resolution: 2.6→63.5 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms23808 0 167 308 24283
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0040.01924341
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg0.8921.9932947
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.12853112
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.2924.154999
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.391154288
X-RAY DIFFRACTIONr_dihedral_angle_4_deg12.57415177
X-RAY DIFFRACTIONr_chiral_restr0.0560.23854
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.02117936
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it
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: 2.595→2.662 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.37 256 -
Rwork0.32 4849 -
obs--60.82 %
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)
19.82671.13750.47742.7572-1.28472.15370.05150.23180.6841-0.0069-0.05780.0149-0.4168-0.16330.00620.31730.03080.04810.14840.08860.0987-26.059225.76330.9305
21.1143-0.10920.0361.16110.27221.6131-0.0462-0.09220.32740.03850.0557-0.0433-0.1720.0911-0.00950.20210.01560.00660.1169-0.04030.1099-23.947230.607231.7552
31.33230.1662-0.08312.99110.44481.96050.0095-0.21110.08170.0952-0.14750.0430.14420.08340.1380.25490.0240.03180.3029-0.13540.1191-25.737931.627662.9126
45.34560.89991.05085.3868-0.61361.9355-0.11220.2140.13990.02620.0225-0.0307-0.27790.06120.08970.17890.02820.0630.21670.02510.0465-2.5557-8.0785-0.1407
51.473-0.01890.30370.8549-0.24171.1340.0303-0.048-0.210.08610.0009-0.14260.03790.1733-0.03120.15320.05330.01570.1189-0.00460.0692-1.4017-22.199327.433
63.53430.30680.36932.3939-0.57292.8870.0372-0.2066-0.41080.22140.0116-0.0660.3232-0.1688-0.04880.28410.0633-0.03360.23460.16120.16820.9054-34.4155.961
75.1208-1.85030.80264.93710.33275.14050.08230.3357-0.2943-0.3723-0.04490.19050.2122-0.2475-0.03740.2330.03910.00060.1298-0.01240.0194-42.922-11.3595-6.4436
81.2878-0.172-0.38120.99920.09951.1805-0.00440.0366-0.0576-0.00850.04140.1377-0.0296-0.0736-0.0370.14480.03850.02120.05940.0140.0262-56.7534-13.342921.5747
93.34030.44950.24961.37480.20992.62350.1152-0.5371-0.06860.17860.06250.0034-0.2183-0.061-0.17770.27950.0680.05640.21390.110.0944-65.8485-15.674251.2976
101.81090.7073-0.67944.6548-0.29510.45990.11980.46960.3366-0.4-0.05910.1695-0.2594-0.0812-0.06070.32850.0031-0.05110.22760.11510.0838-47.164311.9045-2.9874
111.13480.42760.24920.94290.35881.4353-0.0591-0.11370.3210.02530.00940.3459-0.1551-0.17110.04970.19070.06880.01310.1109-0.00550.163-54.545318.211824.4728
122.7389-0.40910.62982.7432-1.02942.13870.0683-0.4502-0.15570.4570.10950.373-0.0861-0.3658-0.17780.38920.05940.11880.3547-0.10070.1665-54.898514.581755.0862
133.0263-0.6132-0.31233.861-0.20181.55410.11640.16040.2323-0.2923-0.0956-0.2939-0.14340.1601-0.02070.2024-0.00460.06910.1880.07430.0898-4.192417.15014.7481
140.97710.240.40031.07490.03251.03750.014-0.15870.17520.19210.0344-0.2428-0.020.2391-0.04840.22310.01410.00710.2306-0.07530.15523.436911.810133.0816
151.93160.4043-1.10512.9844-0.62333.53380.1684-0.5045-0.01470.38210.07810.21210.08830.1736-0.24640.4530.0418-0.13560.4816-0.040.31957.39715.072461.43
164.3227-0.05351.244.3047-0.30242.41230.27850.66350.1808-0.2148-0.12860.09060.16350.0571-0.14990.20920.0570.04840.2057-0.0070.0674-20.2836-23.2939-4.516
171.5362-0.4124-0.22210.63160.04331.2482-0.0049-0.0326-0.37880.02650.01150.08850.2393-0.0282-0.00660.1910.04860.0130.06560.00530.1055-30.0054-33.993120.9982
182.461-0.00890.32531.65550.25261.2670.0427-0.4382-0.33650.416-0.0108-0.10670.17220.088-0.03190.34440.0286-0.00640.28690.19840.1483-35.4815-32.460551.3618
190.45130.16371.01840.3784-0.671820.0995-0.0927-0.24940.12760.1488-0.263-0.0502-0.4692-0.33670.35570.4086-0.01750.00330.35370.00920.1532-28.4018-0.475867.1792
2019.26994.9952-11.55563.76290.433711.7446-0.6576-0.5465-1.02650.2329-0.35980.13890.76790.37561.01740.8894-0.15920.06510.7219-0.15670.2175-34.3658-13.884277.7504
213.89471.4733-2.01553.2239-1.24751.508-0.0563-0.4042-0.4405-0.1444-0.0270.00330.1153-0.00750.08330.8038-0.0891-0.0520.57530.06240.2828-36.0607-10.787883.1301
220.5850.3905-2.27510.4356-0.965913.23490.0359-0.1949-0.08990.1928-0.1303-0.03530.29070.19040.09430.37490.03670.01080.31260.02250.1089-27.0387-4.777657.7285
236.7132.35411.12113.8621-0.63344.0793-0.0985-0.413-0.01540.15870.14760.19640.113-0.1275-0.04910.5249-0.01570.0470.4938-0.03070.128-28.9611.9508109.1659
240000000000000000.2145000.214500.2145000
259.135811.0194-6.405213.3099-7.80984.88320.572-0.63860.69820.4815-0.49040.7925-0.1072-0.2782-0.08150.9394-0.08560.1451.6176-0.41030.5859-44.77981.6728100.2176
260000000000000000.2145000.214500.2145000
279.05369.465717.37699.918118.197533.39360.3485-0.4835-0.08860.1641-0.3308-0.04890.3593-0.8034-0.01770.8299-0.19320.02350.60620.1080.4643-47.2497-6.223883.1878
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A24 - 93
2X-RAY DIFFRACTION2A94 - 379
3X-RAY DIFFRACTION2A600 - 601
4X-RAY DIFFRACTION2A2020 - 2023
5X-RAY DIFFRACTION3A380 - 510
6X-RAY DIFFRACTION4B23 - 93
7X-RAY DIFFRACTION5B94 - 379
8X-RAY DIFFRACTION5B600 - 601
9X-RAY DIFFRACTION5B2028 - 2032
10X-RAY DIFFRACTION6B380 - 510
11X-RAY DIFFRACTION7C24 - 93
12X-RAY DIFFRACTION8C94 - 379
13X-RAY DIFFRACTION8C600 - 601
14X-RAY DIFFRACTION8C2018 - 2021
15X-RAY DIFFRACTION9C380 - 510
16X-RAY DIFFRACTION10D9 - 81
17X-RAY DIFFRACTION11D82 - 357
18X-RAY DIFFRACTION11D600 - 620
19X-RAY DIFFRACTION11D2012 - 2016
20X-RAY DIFFRACTION12D358 - 475
21X-RAY DIFFRACTION13E9 - 81
22X-RAY DIFFRACTION14E82 - 357
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29X-RAY DIFFRACTION18F358 - 475
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31X-RAY DIFFRACTION20G60 - 99
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33X-RAY DIFFRACTION22G197 - 272
34X-RAY DIFFRACTION23H16 - 103
35X-RAY DIFFRACTION24H104 - 144
36X-RAY DIFFRACTION25I1 - 25
37X-RAY DIFFRACTION26I26 - 31
38X-RAY DIFFRACTION27I32 - 45

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