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- PDB-4pv1: Cytochrome B6F structure from M. laminosus with the quinone analo... -

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Basic information

Entry
Database: PDB / ID: 4pv1
TitleCytochrome B6F structure from M. laminosus with the quinone analog inhibitor stigmatellin
Components
  • (Cytochrome b6-f complex subunit ...) x 5
  • Apocytochrome f
  • Cytochrome b6
  • Cytochrome b6-f complex iron-sulfur subunit
KeywordsELECTRON TRANSPORT/INHIBITOR / ALPHA HELIX / BETA SHEET / PLASTOQUINOL:PLASTOCYANIN OXIDOREDUCTASE / PLASTOCYANIN / THYLAKOID MEMBRANE / ELECTRON TRANSPORT-INHIBITOR COMPLEX
Function / homology
Function and homology information


plastoquinol--plastocyanin reductase activity / cytochrome b6f complex / plastoquinol-plastocyanin reductase / electron transporter, transferring electrons within cytochrome b6/f complex of photosystem II activity / cytochrome complex assembly / photosynthetic electron transport chain / ubiquinol-cytochrome-c reductase activity / plasma membrane-derived thylakoid membrane / electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity / photosynthesis ...plastoquinol--plastocyanin reductase activity / cytochrome b6f complex / plastoquinol-plastocyanin reductase / electron transporter, transferring electrons within cytochrome b6/f complex of photosystem II activity / cytochrome complex assembly / photosynthetic electron transport chain / ubiquinol-cytochrome-c reductase activity / plasma membrane-derived thylakoid membrane / electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity / photosynthesis / respiratory electron transport chain / 2 iron, 2 sulfur cluster binding / electron transfer activity / iron ion binding / heme binding / metal ion binding
Similarity search - Function
Single helix bin / plastocyanin oxidoreductase / Cytochrome b6-f complex subunit 6 / Cytochrome b6-f complex iron-sulfur subunit / Cytochrome b6/f complex, subunit 5 / Cytochrome b6-f complex, subunit 8 / Cytochrome b6/f complex, subunit IV / PetM of cytochrome b6/f complex subunit 7 / Cytochrome b6, PetB / Cytochrome b6/f complex, subunit 5 superfamily ...Single helix bin / plastocyanin oxidoreductase / Cytochrome b6-f complex subunit 6 / Cytochrome b6-f complex iron-sulfur subunit / Cytochrome b6/f complex, subunit 5 / Cytochrome b6-f complex, subunit 8 / Cytochrome b6/f complex, subunit IV / PetM of cytochrome b6/f complex subunit 7 / Cytochrome b6, PetB / Cytochrome b6/f complex, subunit 5 superfamily / Cytochrome b6-f complex, subunit 8 superfamily / Cytochrome B6-F complex subunit 5 / PetN / PetM family of cytochrome b6f complex subunit 7 / Cytochrome f large domain / Cytochrome f transmembrane anchor / Cytochrome f / Cytochrome f large domain / Cytochrome f large domain superfamily / Apocytochrome F, C-terminal / Apocytochrome F, N-terminal / Cytochrome f family profile. / Single helix bin / Cytochrome Bc1 Complex; Chain C / Cytochrome Bc1 Complex; Chain C / Rieske Iron-sulfur Protein / Rieske [2Fe-2S] iron-sulphur domain / 3-layer Sandwich / : / : / Cytochrome b/b6, C-terminal / Cytochrome b(C-terminal)/b6/petD / Cytochrome b/b6 C-terminal region profile. / Cytochrome b/b6, C-terminal domain superfamily / Cytochrome b/b6/petB / RNA polymerase II/Efflux pump adaptor protein, barrel-sandwich hybrid domain / Rieske iron-sulphur protein, C-terminal / Cytochrome b/b6, N-terminal / Cytochrome b/b6-like domain superfamily / Cytochrome b/b6 N-terminal region profile. / Di-haem cytochrome, transmembrane / Rudiment single hybrid motif / Rieske iron-sulphur protein / Rieske [2Fe-2S] iron-sulphur domain / Rieske [2Fe-2S] domain / Rieske [2Fe-2S] iron-sulfur domain profile. / Rieske [2Fe-2S] iron-sulphur domain superfamily / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Helix Hairpins / Up-down Bundle / Immunoglobulin-like / Beta Barrel / Sandwich / Orthogonal Bundle / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
Chem-7PH / Octadecane / BETA-CAROTENE / : / CHLOROPHYLL A / FE2/S2 (INORGANIC) CLUSTER / HEME C / PENTADECANE / Chem-OPC / STIGMATELLIN A ...Chem-7PH / Octadecane / BETA-CAROTENE / : / CHLOROPHYLL A / FE2/S2 (INORGANIC) CLUSTER / HEME C / PENTADECANE / Chem-OPC / STIGMATELLIN A / Chem-SQD / Cytochrome b6 / Cytochrome b6-f complex subunit 4 / Cytochrome f / Cytochrome b6-f complex iron-sulfur subunit / Cytochrome b6-f complex subunit 6 / Cytochrome b6-f complex subunit 7 / Cytochrome b6-f complex subunit 5 / Cytochrome b6-f complex subunit 8
Similarity search - Component
Biological speciesMastigocladus laminosus (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / RIGID BODY REFINEMENT, RESTRAINED REFINEMENT / Resolution: 3 Å
AuthorsHasan, S.S. / Yamashita, E. / Cramer, W.A.
CitationJournal: Biophys.J. / Year: 2014
Title: Traffic within the cytochrome b6f lipoprotein complex: gating of the quinone portal.
Authors: Hasan, S.S. / Proctor, E.A. / Yamashita, E. / Dokholyan, N.V. / Cramer, W.A.
History
DepositionMar 14, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 20, 2014Provider: repository / Type: Initial release
Revision 1.1Jan 14, 2015Group: Database references
Revision 1.2Jul 17, 2019Group: Advisory / Data collection ...Advisory / Data collection / Derived calculations / Refinement description
Category: pdbx_unobs_or_zero_occ_atoms / software / struct_conn
Item: _software.name / _software.version / _struct_conn.pdbx_leaving_atom_flag
Revision 2.0Mar 10, 2021Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Non-polymer description / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / database_PDB_caveat / entity / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_conn_angle / pdbx_validate_close_contact / struct_conn / struct_conn_type / struct_ref_seq_dif / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.type_symbol / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.name / _chem_comp.pdbx_synonyms / _entity.formula_weight / _entity.pdbx_description / _pdbx_entity_nonpoly.comp_id / _pdbx_entity_nonpoly.name / _pdbx_nonpoly_scheme.mon_id / _pdbx_nonpoly_scheme.pdb_mon_id / _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 / _pdbx_validate_close_contact.auth_comp_id_2 / _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_type.id / _struct_ref_seq_dif.details / _struct_site.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id / _struct_site_gen.auth_comp_id / _struct_site_gen.label_comp_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Cytochrome b6
B: Cytochrome b6-f complex subunit 4
C: Apocytochrome f
D: Cytochrome b6-f complex iron-sulfur subunit
E: Cytochrome b6-f complex subunit 6
F: Cytochrome b6-f complex subunit 7
G: Cytochrome b6-f complex subunit 5
H: Cytochrome b6-f complex subunit 8
hetero molecules


Theoretical massNumber of molelcules
Total (without water)118,19128
Polymers107,6518
Non-polymers10,54020
Water28816
1
A: Cytochrome b6
B: Cytochrome b6-f complex subunit 4
C: Apocytochrome f
D: Cytochrome b6-f complex iron-sulfur subunit
E: Cytochrome b6-f complex subunit 6
F: Cytochrome b6-f complex subunit 7
G: Cytochrome b6-f complex subunit 5
H: Cytochrome b6-f complex subunit 8
hetero molecules

A: Cytochrome b6
B: Cytochrome b6-f complex subunit 4
C: Apocytochrome f
D: Cytochrome b6-f complex iron-sulfur subunit
E: Cytochrome b6-f complex subunit 6
F: Cytochrome b6-f complex subunit 7
G: Cytochrome b6-f complex subunit 5
H: Cytochrome b6-f complex subunit 8
hetero molecules


Theoretical massNumber of molelcules
Total (without water)236,38256
Polymers215,30316
Non-polymers21,07940
Water1448
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation12_565x,x-y+1,-z+1/61
Buried area88260 Å2
ΔGint-936 kcal/mol
Surface area78310 Å2
MethodPISA
Unit cell
Length a, b, c (Å)159.085, 159.085, 361.322
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number178
Space group name H-MP6122

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Components

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Protein , 3 types, 3 molecules ACD

#1: Protein Cytochrome b6


Mass: 24245.529 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Mastigocladus laminosus (bacteria) / References: UniProt: P83791
#3: Protein Apocytochrome f


Mass: 31655.088 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 45-333 / Source method: isolated from a natural source / Source: (natural) Mastigocladus laminosus (bacteria) / References: UniProt: P83793
#4: Protein Cytochrome b6-f complex iron-sulfur subunit / Plastohydroquinone:plastocyanin oxidoreductase iron-sulfur protein / ISP / RISP / Rieske iron-sulfur protein


Mass: 19422.178 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Mastigocladus laminosus (bacteria) / References: UniProt: P83794, EC: 1.10.9.1

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Cytochrome b6-f complex subunit ... , 5 types, 5 molecules BEFGH

#2: Protein Cytochrome b6-f complex subunit 4 / 17 kDa polypeptide


Mass: 17687.049 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Mastigocladus laminosus (bacteria) / References: UniProt: P83792
#5: Protein/peptide Cytochrome b6-f complex subunit 6 / Cytochrome b6-f complex subunit PetL / Cytochrome b6-f complex subunit VI


Mass: 3504.444 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Mastigocladus laminosus (bacteria) / References: UniProt: P83795
#6: Protein/peptide Cytochrome b6-f complex subunit 7 / Cytochrome b6-f complex subunit PetM / Cytochrome b6-f complex subunit VII


Mass: 3843.595 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Mastigocladus laminosus (bacteria) / References: UniProt: P83796
#7: Protein/peptide Cytochrome b6-f complex subunit 5 / Cytochrome b6-f complex subunit PetG / Cytochrome b6-f complex subunit V


Mass: 4016.661 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Mastigocladus laminosus (bacteria) / References: UniProt: P83797
#8: Protein/peptide Cytochrome b6-f complex subunit 8 / Cytochrome b6-f complex subunit PetN / Cytochrome b6-f complex subunit VIII


Mass: 3276.932 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Mastigocladus laminosus (bacteria) / References: UniProt: P83798

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Non-polymers , 13 types, 36 molecules

#9: Chemical ChemComp-MYS / PENTADECANE


Mass: 212.415 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C15H32
#10: Chemical ChemComp-CD / CADMIUM ION


Mass: 112.411 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cd
#11: Chemical
ChemComp-HEC / HEME C


Mass: 618.503 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C34H34FeN4O4
#12: Chemical ChemComp-UMQ / UNDECYL-MALTOSIDE / UNDECYL-BETA-D-MALTOPYRANOSIDE


Mass: 496.589 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C23H44O11 / Comment: detergent*YM
#13: Chemical ChemComp-SMA / STIGMATELLIN A


Mass: 514.650 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C30H42O7
#14: Chemical ChemComp-7PH / (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate / PHOSPHATIDIC ACID


Mass: 564.732 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C29H57O8P
#15: Chemical ChemComp-8K6 / Octadecane / N-Octadecane


Mass: 254.494 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C18H38
#16: Chemical ChemComp-CLA / CHLOROPHYLL A


Mass: 893.489 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C55H72MgN4O5
#17: Chemical ChemComp-OPC / (7R,17E)-4-HYDROXY-N,N,N,7-TETRAMETHYL-7-[(8E)-OCTADEC-8-ENOYLOXY]-10-OXO-3,5,9-TRIOXA-4-PHOSPHAHEPTACOS-17-EN-1-AMINIUM 4-OXIDE / DIOLEOYL-PHOSPHATIDYLCHOLINE


Mass: 801.148 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C45H87NO8P / Comment: phospholipid*YM
#18: Chemical ChemComp-FES / FE2/S2 (INORGANIC) CLUSTER


Mass: 175.820 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Fe2S2
#19: Chemical ChemComp-SQD / 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL / SULFOQUINOVOSYLDIACYLGLYCEROL


Mass: 795.116 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C41H78O12S
#20: Chemical ChemComp-BCR / BETA-CAROTENE


Mass: 536.873 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C40H56
#21: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 16 / 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: 6.13 Å3/Da / Density % sol: 79.9 %
Description: RPIM IS 0.035 (0.647 FOR THE HIGHEST RESOLUTION SHELL)
Crystal growpH: 8.3
Details: PH 8.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.97934
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Jul 7, 2006
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97934 Å / Relative weight: 1
ReflectionResolution: 2.997→137.772 Å / Num. obs: 50303 / % possible obs: 91.4 % / Redundancy: 9.8 % / Net I/σ(I): 17.4
Reflection shellResolution: 3→3.05 Å / Redundancy: 5 % / Mean I/σ(I) obs: 0.6 / % possible all: 38

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE: 1.8.4_1496)refinement
REFMACrefinement
HKL-2000data reduction
HKL-2000data scaling
REFMACphasing
RefinementMethod to determine structure: RIGID BODY REFINEMENT, RESTRAINED REFINEMENT
Resolution: 3→48.34 Å / SU ML: 0.37 / σ(F): 1.34 / Phase error: 26.92 / Stereochemistry target values: ML / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflection
Rfree0.247 2552 5.08 %
Rwork0.216 --
obs0.217 50203 91.2 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 108.81 Å2
Baniso -1Baniso -2Baniso -3
1--0.01 Å2-0.01 Å2-0 Å2
2---0.01 Å2-0 Å2
3---0.02 Å2
Refinement stepCycle: LAST / Resolution: 3→48.34 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7330 0 703 16 8049
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0048278
X-RAY DIFFRACTIONf_angle_d0.64611253
X-RAY DIFFRACTIONf_dihedral_angle_d12.7713240
X-RAY DIFFRACTIONf_chiral_restr0.0221189
X-RAY DIFFRACTIONf_plane_restr0.0031329
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.997-3.05470.4676620.38631029X-RAY DIFFRACTION37
3.0547-3.11710.3754800.35721404X-RAY DIFFRACTION50
3.1171-3.18480.38441140.31731996X-RAY DIFFRACTION70
3.1848-3.25890.35231320.30652517X-RAY DIFFRACTION89
3.2589-3.34040.29671570.2922773X-RAY DIFFRACTION98
3.3404-3.43070.32231510.28052838X-RAY DIFFRACTION99
3.4307-3.53160.30871330.26622879X-RAY DIFFRACTION100
3.5316-3.64560.3031740.24392834X-RAY DIFFRACTION100
3.6456-3.77580.28351440.23462879X-RAY DIFFRACTION100
3.7758-3.92690.26261580.20792863X-RAY DIFFRACTION100
3.9269-4.10560.23721510.20342888X-RAY DIFFRACTION100
4.1056-4.32190.21721440.19262900X-RAY DIFFRACTION100
4.3219-4.59250.21871550.17862910X-RAY DIFFRACTION100
4.5925-4.94670.19151690.16962906X-RAY DIFFRACTION100
4.9467-5.44390.22491600.17432915X-RAY DIFFRACTION100
5.4439-6.23030.25771500.21362974X-RAY DIFFRACTION100
6.2303-7.84410.22411630.21492998X-RAY DIFFRACTION100
7.8441-48.34260.22691550.22153148X-RAY DIFFRACTION98
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)
11.8916-1.49541.77331.1754-1.39571.6569-0.1221.08430.4842-0.5815-0.28810.0403-0.37840.9695-0.07541.4714-0.4817-0.0010.8916-0.05640.7266-27.60596.129837.7548
20.6081-0.55260.87260.534-0.79161.24850.40580.87380.3648-0.0057-0.1531-0.39590.24611.09140.09570.6035-0.40450.14321.3043-0.00590.885-21.530288.389618.6571
31.08420.02350.22330.44160.55681.49860.43080.50430.06320.51-0.20580.5106-0.0947-0.25540.03350.30550.05150.01130.4339-0.05270.5596-50.687570.401919.0278
40.5085-0.4166-0.12561.46530.53580.22590.3180.38380.2786-0.1815-0.09240.095-0.25440.41390.06330.20140.014-0.00430.65840.05180.2834-36.246470.39599.3238
50.63570.10890.11430.33270.14050.67960.08150.7274-0.1184-0.0463-0.08950.3350.05150.79970.4282-0.20790.325-0.02920.7263-0.11380.4394-33.97362.441415.8996
60.12490.1031-0.1590.16-0.00330.530.09080.3082-0.56150.30880.010.0520.0975-0.012-0.00080.45560.024-0.0570.6118-0.17510.6507-50.442150.587815.1363
70.9850.26680.56381.0812-0.49181.73340.16130.2565-0.28810.0221-0.1420.19020.15760.26550.00310.32140.0866-0.00080.4969-0.12810.4785-36.13659.98522.1064
80.124-0.3150.06711.39470.34210.23360.0319-0.3136-0.2449-0.32690.051-1.004-0.06660.65010.0970.37-0.23920.211.2661-0.05470.7943-8.988286.607512.4253
91.2036-0.610.05191.36570.61661.79460.2590.24840.6021-0.0939-0.19960.17050.01490.4686-0.02110.38270.01360.03970.61920.0890.3247-38.43580.396211.2647
100.0556-0.1906-0.09210.71840.34590.1506-0.16920.2138-0.39150.51211.1562-0.17120.8120.6254-0.01130.7474-0.1951-0.04861.3151-0.14490.7328-54.407750.43127.6146
110.8323-0.8404-0.37891.0459-0.38951.55170.2610.7945-0.4002-0.1958-0.16740.03210.16560.55450.00230.5170.17780.01611.0787-0.25180.5021-30.909755.85520.6772
120.8947-0.02650.22670.02450.16971.29520.00910.1036-1.34390.2493-0.50090.15441.4633-0.2291-0.03620.5980.0986-0.22191.0965-0.16281.1219-73.449146.79060.0274
132.22471.64870.93831.36820.37412.4165-0.04241.1067-0.0151-0.16460.06170.27640.21620.01470.04430.47980.1391-0.10371.1098-0.19930.6727-70.14457.7551-10.3187
140.9022-0.4922-0.26041.95390.04640.62250.32511.03380.3036-0.1316-0.05340.3497-0.1314-0.32190.20350.37980.1748-0.31391.3378-0.18180.6983-73.378556.2206-6.523
151.14060.0543-0.10030.5663-0.70530.8994-1.16650.6470.2462-0.96610.21760.1850.0268-0.0562-0.49541.94680.151-0.3821.7556-1.11052.8038-73.781520.8963-22.9371
16-0.4439-0.1582-0.5197-0.01770.27860.2070.16750.69430.0688-0.1961-0.02480.0312-0.3644-0.05260.22080.25230.2334-0.50180.892-0.6330.7688-63.83631.919-13.5915
170.6463-0.78270.05540.89530.21342.14580.51670.56560.79330.0724-0.19680.5375-0.7864-0.07170.07740.5158-0.04820.06120.4340.24720.5808-41.423594.27268.0894
181.5116-0.2401-0.85940.2670.00230.42790.10640.41260.9774-0.45510.24350.60670.330.23490.00210.577-0.02310.07420.50450.07010.718-43.884596.270917.1556
190.1644-0.2604-0.28390.57790.51130.35680.53670.2730.320.0862-0.35910.2415-0.20920.19190.00040.61430.16540.02580.48950.080.8071-81.515365.099240.6729
200.7690.57170.01260.46260.23670.3733-0.1651-0.97530.45011.5683-0.29421.2609-1.0686-0.43880.00391.79590.22260.39091.0824-0.09421.5962-77.452374.261854.6859
210.59250.3201-0.40860.1903-0.11580.38421.1109-0.139-0.7272-0.2344-0.2837-0.39250.5327-2.3107-0.00062.03440.1103-0.11071.91570.22982.771-84.950679.425141.425
222.1221-0.7971-1.27390.8030.08321.07830.80670.70840.701-0.0158-0.05220.4289-0.7866-0.50310.50430.6110.16930.27480.74770.56480.7141-46.119396.3609-3.6154
232.13780.326-0.1192.6843-0.58590.2112-0.2441.42460.226-0.82330.4531-0.1141-0.55261.03870.15680.5447-0.02960.01151.45250.28540.4454-40.344782.2469-6.6145
240.4773-0.68140.36241.1056-0.86080.72260.46830.35580.04740.07-0.23920.09450.13470.38350.08990.57920.08290.10041.0318-0.1610.381-33.944271.8396-3.4129
250.074-0.47640.05492.8552-0.33490.0378-0.1757-0.55950.8948-1.07880.69220.8259-0.22470.79760.0131.0713-0.10810.55661.89890.33431.3344-12.093484.013-1.5314
260.01580.0825-0.09190.3394-0.3950.3407-0.47130.0235-0.076-0.17690.1398-0.0369-0.68150.1483-0.08980.5762-0.04440.08151.05450.31780.9292-44.41685.6628-0.0893
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 3 through 12 )
2X-RAY DIFFRACTION2chain 'A' and (resid 13 through 31 )
3X-RAY DIFFRACTION3chain 'A' and (resid 32 through 78 )
4X-RAY DIFFRACTION4chain 'A' and (resid 79 through 114 )
5X-RAY DIFFRACTION5chain 'A' and (resid 115 through 137 )
6X-RAY DIFFRACTION6chain 'A' and (resid 138 through 156 )
7X-RAY DIFFRACTION7chain 'A' and (resid 157 through 215 )
8X-RAY DIFFRACTION8chain 'B' and (resid 2 through 20 )
9X-RAY DIFFRACTION9chain 'B' and (resid 21 through 67 )
10X-RAY DIFFRACTION10chain 'B' and (resid 68 through 78 )
11X-RAY DIFFRACTION11chain 'B' and (resid 79 through 160 )
12X-RAY DIFFRACTION12chain 'C' and (resid 1 through 20 )
13X-RAY DIFFRACTION13chain 'C' and (resid 21 through 91 )
14X-RAY DIFFRACTION14chain 'C' and (resid 92 through 175 )
15X-RAY DIFFRACTION15chain 'C' and (resid 176 through 195 )
16X-RAY DIFFRACTION16chain 'C' and (resid 196 through 251 )
17X-RAY DIFFRACTION17chain 'C' and (resid 252 through 288 )
18X-RAY DIFFRACTION18chain 'D' and (resid 9 through 42 )
19X-RAY DIFFRACTION19chain 'D' and (resid 43 through 101 )
20X-RAY DIFFRACTION20chain 'D' and (resid 102 through 153 )
21X-RAY DIFFRACTION21chain 'D' and (resid 154 through 179 )
22X-RAY DIFFRACTION22chain 'E' and (resid 2 through 29 )
23X-RAY DIFFRACTION23chain 'F' and (resid 2 through 32 )
24X-RAY DIFFRACTION24chain 'G' and (resid 1 through 30 )
25X-RAY DIFFRACTION25chain 'G' and (resid 31 through 37 )
26X-RAY DIFFRACTION26chain 'H' and (resid 2 through 29 )

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