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- PDB-2v7q: The structure of F1-ATPase inhibited by I1-60HIS, a monomeric for... -

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Basic information

Entry
Database: PDB / ID: 2v7q
TitleThe structure of F1-ATPase inhibited by I1-60HIS, a monomeric form of the inhibitor protein, IF1.
Components
  • (ATP SYNTHASE ...) x 5
  • ATPASE INHIBITOR
KeywordsHYDROLASE / ION TRANSPORT / MITOCHONDRION / TRANSIT PEPTIDE / INHIBITOR PROTEIN
Function / homology
Function and homology information


angiostatin binding / Formation of ATP by chemiosmotic coupling / Cristae formation / ATPase inhibitor activity / mitochondrial envelope / mitochondrial proton-transporting ATP synthase complex assembly / negative regulation of hydrolase activity / proton-transporting ATP synthase complex / heme biosynthetic process / Mitochondrial protein degradation ...angiostatin binding / Formation of ATP by chemiosmotic coupling / Cristae formation / ATPase inhibitor activity / mitochondrial envelope / mitochondrial proton-transporting ATP synthase complex assembly / negative regulation of hydrolase activity / proton-transporting ATP synthase complex / heme biosynthetic process / Mitochondrial protein degradation / mitochondrial proton-transporting ATP synthase, catalytic core / mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1) / mitochondrial proton-transporting ATP synthase complex / negative regulation of endothelial cell proliferation / proton motive force-driven ATP synthesis / proton transmembrane transporter activity / proton motive force-driven mitochondrial ATP synthesis / proton-transporting ATP synthase complex, catalytic core F(1) / H+-transporting two-sector ATPase / aerobic respiration / proton transmembrane transport / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / erythrocyte differentiation / ADP binding / ATPase binding / protein homotetramerization / mitochondrial inner membrane / calmodulin binding / structural molecule activity / cell surface / protein homodimerization activity / ATP hydrolysis activity / protein-containing complex / mitochondrion / ATP binding / identical protein binding / plasma membrane
Similarity search - Function
Single helix bin / ATP synthase, F1 complex, epsilon subunit superfamily, mitochondrial / ATP synthase delta/epsilon subunit, C-terminal domain / ATP Synthase; domain 1 / F0F1 ATP synthase delta/epsilon subunit, N-terminal / ATP synthase, F1 complex, gamma subunit / Atp Synthase Epsilon Chain; Chain: I; / ATP synthase alpha/beta chain, C-terminal domain / Lysin / Thrombin, subunit H - #170 ...Single helix bin / ATP synthase, F1 complex, epsilon subunit superfamily, mitochondrial / ATP synthase delta/epsilon subunit, C-terminal domain / ATP Synthase; domain 1 / F0F1 ATP synthase delta/epsilon subunit, N-terminal / ATP synthase, F1 complex, gamma subunit / Atp Synthase Epsilon Chain; Chain: I; / ATP synthase alpha/beta chain, C-terminal domain / Lysin / Thrombin, subunit H - #170 / Mitochondrial ATPase inhibitor / Mitochondrial ATPase inhibitor, IATP / Elongation Factor Tu (Ef-tu); domain 3 - #20 / Pyruvate Kinase; Chain: A, domain 1 / Bovine Mitochondrial F1-ATPase, ATP Synthase Beta Chain; Chain D, domain3 / Bovine Mitochondrial F1-atpase; Atp Synthase Beta Chain; Chain D, domain 3 / : / Metazoan delta subunit of F1F0-ATP synthase, C-terminal domain / 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 / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / 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 / ADENOSINE-5'-TRIPHOSPHATE / PHOSPHATE ION / ATP synthase subunit beta, mitochondrial / ATPase inhibitor, mitochondrial / ATP synthase subunit delta, mitochondrial / ATP synthase subunit gamma, mitochondrial / ATP synthase subunit epsilon, mitochondrial / ATP synthase subunit alpha, mitochondrial / ATP synthase subunit alpha, mitochondrial
Similarity search - Component
Biological speciesBOS TAURUS (cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å
AuthorsGledhill, J.R. / Montgomery, M.G. / Leslie, A.G.W. / Walker, J.E.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2007
Title: How the Regulatory Protein, If1, Inhibits F1- ATPase from Bovine Mitochondria.
Authors: Gledhill, J.R. / Montgomery, M.G. / Leslie, A.G.W. / Walker, J.E.
History
DepositionJul 31, 2007Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 18, 2007Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Refinement description / Version format compliance
Revision 1.2Dec 13, 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
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.pdbx_dist_value / _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_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
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 13-STRANDED BARREL THIS IS REPRESENTED BY A 14-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 11-STRANDED BARREL THIS IS REPRESENTED BY A 12-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "CA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 11-STRANDED BARREL THIS IS REPRESENTED BY A 12-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM
B: ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM
C: ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM
D: ATP SYNTHASE SUBUNIT BETA
E: ATP SYNTHASE SUBUNIT BETA
F: ATP SYNTHASE SUBUNIT BETA
G: ATP SYNTHASE GAMMA CHAIN
H: ATP SYNTHASE DELTA CHAIN
I: ATP SYNTHASE EPSILON CHAIN
J: ATPASE INHIBITOR
hetero molecules


Theoretical massNumber of molelcules
Total (without water)382,24821
Polymers379,65510
Non-polymers2,59211
Water34,9491940
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area47950 Å2
ΔGint-230.6 kcal/mol
Surface area144720 Å2
MethodPISA
Unit cell
Length a, b, c (Å)262.534, 103.271, 135.559
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 ... , 5 types, 9 molecules ABCDEFGHI

#1: Protein ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM / / ATP SYNTHASE ALPHA CHAIN HEART ISOFORM


Mass: 55332.219 Da / Num. of mol.: 3 / Fragment: RESIDUES 44-553 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle
References: UniProt: Q1JQC4, UniProt: P19483*PLUS, EC: 3.6.1.14
#2: Protein ATP SYNTHASE SUBUNIT BETA / / ATP SYNTHASE BETA CHAIN


Mass: 51757.836 Da / Num. of mol.: 3 / Fragment: RESIDUES 47-528 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P00829, EC: 3.6.1.14
#3: Protein ATP SYNTHASE GAMMA CHAIN / ATP SYNTHASE GAMMA SUBUNIT


Mass: 30185.674 Da / Num. of mol.: 1 / Fragment: RESIDUES 26-297 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P05631, EC: 3.6.1.34
#4: Protein ATP SYNTHASE DELTA CHAIN / ATP SYNTHASE DELTA SUBUNIT


Mass: 15074.813 Da / Num. of mol.: 1 / Fragment: RESIDUES 23-168 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P05630, EC: 3.6.1.14
#5: Protein/peptide ATP SYNTHASE EPSILON CHAIN / ATP SYNTHASE EPSILON SUBUNIT


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, EC: 3.6.1.14

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Protein , 1 types, 1 molecules J

#6: Protein ATPASE INHIBITOR / BOVINE MITOCHONDRIAL F1-ATPASE INHIBITOR PROTEIN


Mass: 7462.098 Da / Num. of mol.: 1 / Fragment: RESIDUES 26-85
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) BOS TAURUS (cattle) / Tissue: MUSCLESkeletal muscle / Organ: HEART / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 (DE3) / References: UniProt: P01096

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Non-polymers , 5 types, 1951 molecules

#7: Chemical ChemComp-ATP / ADENOSINE-5'-TRIPHOSPHATE / Adenosine triphosphate


Mass: 507.181 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C10H16N5O13P3 / Comment: ATP, energy-carrying molecule*YM
#8: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Mg
#9: Chemical ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE / Adenosine diphosphate


Mass: 427.201 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#10: Chemical ChemComp-PO4 / PHOSPHATE ION / Phosphate


Mass: 94.971 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: PO4
#11: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 1940 / Source method: isolated from a natural source / Formula: H2O

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Details

Sequence detailsI1-60HIS IS A TRUNCATED FRAGMENT OF THE BOVINE ATPASE INHIBITOR PROTEIN. RESIDUES 1-60 PLUS 6 C- ...I1-60HIS IS A TRUNCATED FRAGMENT OF THE BOVINE ATPASE INHIBITOR PROTEIN. RESIDUES 1-60 PLUS 6 C-TERMINAL HISTIDINES

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.39 Å3/Da / Density % sol: 48.21 % / Description: NONE
Crystal growpH: 8.2 / Details: pH 8.2

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.979
DetectorType: ADSC CCD / Detector: CCD
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979 Å / Relative weight: 1
ReflectionResolution: 2.1→69.7 Å / Num. obs: 212416 / % possible obs: 99.2 % / Redundancy: 3.5 % / Rmerge(I) obs: 0.11 / Net I/σ(I): 9.1
Reflection shellResolution: 2.1→2.21 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.42 / Mean I/σ(I) obs: 2 / % possible all: 97.7

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Processing

Software
NameVersionClassification
REFMAC5.2.0019refinement
MOSFLMdata reduction
SCALAdata scaling
AMoREphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1OHH

1ohh


Resolution: 2.1→37.19 Å / Cor.coef. Fo:Fc: 0.949 / Cor.coef. Fo:Fc free: 0.916 / SU B: 10.233 / SU ML: 0.144 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.223 / ESU R Free: 0.193 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.245 10665 5 %RANDOM
Rwork0.19 ---
obs0.193 201634 99 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 41.41 Å2
Baniso -1Baniso -2Baniso -3
1--2.17 Å20 Å20 Å2
2---1.19 Å20 Å2
3---3.36 Å2
Refinement stepCycle: LAST / Resolution: 2.1→37.19 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms25321 0 157 1940 27418
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.02225875
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.221.98734986
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.34453308
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.16524.2051075
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.62154581
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.15615187
X-RAY DIFFRACTIONr_chiral_restr0.0810.24074
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0219107
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.1940.212301
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.2980.217841
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.140.22050
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2470.259
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1720.216
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.329316952
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it2.117526419
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it3.5879939
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it5.114108562
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: 2.1→2.15 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.301 728
Rwork0.227 14277
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)
12.2828-0.49970.75172.06560.21413.6564-0.07430.04340.26350.06470.0611-0.1434-0.2070.18510.0131-0.0566-0.0133-0.0515-0.0486-0.0003-0.0919138.64639.444510.7341
20.8711-0.1331-0.23330.5633-0.40131.3481-0.0441-0.12850.11820.0990.04310.0612-0.037-0.04790.0009-0.00270.00680.0042-0.0948-0.0364-0.0921110.704146.341521.3246
35.39320.8695-0.24514.38810.35451.81020.0451-0.45750.54550.4082-0.01830.8193-0.0687-0.6037-0.0269-0.16960.05670.16650.0857-0.06060.005981.16252.770528.701
42.02720.0469-0.42653.18791.1291.860.0163-0.1203-0.08680.17560.0395-0.11570.09290.0992-0.0558-0.03870.0495-0.0128-0.0520.0391-0.1071135.0199-2.057112.8418
50.72260.1413-0.07031.40440.05730.66730.0113-0.0905-0.08190.1594-0.02920.16170.0821-0.05510.0179-0.00870.02080.0489-0.07310.0516-0.068105.6848-10.588412.8718
64.19560.8294-1.50655.5583-0.95633.2522-0.04040.3095-0.3529-0.0359-0.02121.34850.1779-0.64430.0617-0.2805-0.06630.1924-0.0808-0.12770.37475.8119-16.734513.8062
72.3066-0.23480.14062.4988-0.8072.58820.00950.188-0.2334-0.00790.02770.02820.0420.0383-0.0372-0.10950.00070.02790.0549-0.053-0.1395135.423616.736-24.4997
80.8911-0.3001-0.11741.50020.19580.4528-0.00840.19030.035-0.2644-0.04630.2433-0.0320.01210.0547-0.0574-0.0172-0.06350.00130.0178-0.0772106.577725.5145-30.5418
94.02140.3550.04442.94930.87593.3894-0.08720.17890.2087-0.14980.09370.8517-0.0832-0.6419-0.0065-0.18840.0339-0.2720.03160.01460.300176.200529.6639-34.3755
100.8787-0.2556-0.1412.14930.15531.97130.00060.09520.0768-0.00460.0521-0.171-0.1360.1853-0.0528-0.0875-0.0396-0.00520.00870.0005-0.075136.833838.7-15.4815
110.8155-0.1436-0.06450.42660.0330.4905-0.030.1380.1551-0.00690.01960.0483-0.06380.01630.0104-0.0254-0.0227-0.0165-0.06670.0698-0.0393110.519451.5018-11.8904
122.17850.3614-0.04871.1751-0.14940.7404-0.0660.22110.145-0.08610.0270.435-0.1825-0.20480.039-0.09760.0655-0.0767-0.08170.05520.079279.64851.6288-7.7982
131.67060.5244-0.48742.1075-0.03521.7439-0.0837-0.1705-0.12550.2335-0.0199-0.13470.06020.12210.1036-0.01260.0584-0.0525-0.01690.0029-0.1224136.06421.038525.2549
140.8549-0.09570.02931.24170.31080.8518-0.0774-0.2485-0.06220.28460.0180.22390.0469-0.13120.05940.00640.04110.08080.01220.0376-0.0938108.382715.564635.025
1513.40240.4487-0.60141.3070.51632.3778-0.0762-0.48050.1856-0.06550.14120.6206-0.3514-0.6689-0.065-0.05860.05810.3019-0.07770.10420.005278.145114.278640.7009
161.63490.89090.37911.512-0.68832.5030.00330.1066-0.1686-0.00780.031-0.0780.10370.2134-0.0343-0.06450.0610.0459-0.0102-0.0159-0.0828133.7519-5.5075-10.7222
170.6887-0.0575-0.03131.57480.18370.32030.00750.1081-0.0446-0.0126-0.04870.23330.1227-0.03760.0412-0.0603-0.0120.0205-0.0443-0.0137-0.0495105.3235-5.7924-18.641
180.961-1.0128-0.40363.01060.84381.7434-0.1650.1472-0.48320.2486-0.2271.10750.1124-0.44680.392-0.2973-0.07380.0772-0.0983-0.18520.506775.76211.9843-14.6179
1911.7138-2.1464-1.53950.55410.40030.7181-0.0027-0.14280.15540.13130.01330.1078-0.0055-0.0456-0.0106-0.0970.0140.073-0.1250.05350.053187.137322.69436.2944
205.5342-0.1733-1.31082.14750.70352.4676-0.0080.9042-0.3098-0.26940.03440.1369-0.0685-0.7809-0.0265-0.22890.02730.14490.2885-0.10450.002244.104326.6609-0.1327
219.02970.498-3.32573.68490.63116.00640.12230.0055-0.1386-0.0631-0.0338-0.00490.1361-0.3914-0.0885-0.24050.1130.11140.1064-0.0211-0.106728.95231.944719.2857
225.6765-0.48814.40337.26832.05915.9251-0.40390.07320.9281-0.59780.28340.5239-1.56490.36680.12050.03560.03550.19240.0392-0.09580.057435.889554.168714.6789
233.250.73210.37183.0277.429618.8960.15140.79030.498-0.95560.21660.2467-2.4371-0.2453-0.36810.09230.15280.20940.05270.12170.057535.899146.21697.7481
2411.7888-4.7329-34.25226.54422.9968121.07790.1090.17370.9971-0.7538-1.93650.1214-4.79350.24761.8275-0.0018-0.00120.00130.00120.0009-0.000251.639642.212810.0609
257.21011.4528-3.77088.44822.681111.43510.2179-0.02540.22240.41280.007-0.2589-0.35970.6694-0.22490.07530.01780.00850.08730.10110.262787.215433.22843.4972
2611.1979-11.62376.696415.1358-7.89425.3075-0.06960.20230.0497-0.1270.00040.29770.1419-0.22470.06920.05370.007-0.07020.2301-0.02130.42669.101142.6475-11.6685
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A24 - 95
2X-RAY DIFFRACTION2A96 - 379
3X-RAY DIFFRACTION2A1511 - 1512
4X-RAY DIFFRACTION3A380 - 510
5X-RAY DIFFRACTION4B24 - 95
6X-RAY DIFFRACTION5B96 - 379
7X-RAY DIFFRACTION5B1511 - 1512
8X-RAY DIFFRACTION6B380 - 510
9X-RAY DIFFRACTION7C23 - 95
10X-RAY DIFFRACTION8C96 - 379
11X-RAY DIFFRACTION8C1511 - 1512
12X-RAY DIFFRACTION9C380 - 510
13X-RAY DIFFRACTION10D9 - 82
14X-RAY DIFFRACTION11D83 - 363
15X-RAY DIFFRACTION11D1478 - 1479
16X-RAY DIFFRACTION12D364 - 477
17X-RAY DIFFRACTION13E10 - 82
18X-RAY DIFFRACTION14E83 - 363
19X-RAY DIFFRACTION15E364 - 474
20X-RAY DIFFRACTION16F9 - 82
21X-RAY DIFFRACTION17F83 - 363
22X-RAY DIFFRACTION17F1475 - 1476
23X-RAY DIFFRACTION18F364 - 474
24X-RAY DIFFRACTION19G1 - 30
25X-RAY DIFFRACTION19G220 - 272
26X-RAY DIFFRACTION20G31 - 219
27X-RAY DIFFRACTION21H15 - 97
28X-RAY DIFFRACTION22H98 - 145
29X-RAY DIFFRACTION23I1 - 27
30X-RAY DIFFRACTION24I28 - 47
31X-RAY DIFFRACTION25J8 - 20
32X-RAY DIFFRACTION26J21 - 50

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