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- PDB-2xok: Refined structure of yeast F1c10 ATPase complex to 3 A resolution -

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Basic information

Entry
Database: PDB / ID: 2xok
TitleRefined structure of yeast F1c10 ATPase complex to 3 A resolution
Components
  • (ATP SYNTHASE SUBUNIT ...) x 4
  • ATP SYNTHASE
  • ATP SYNTHASE CATALYTIC SECTOR F1 EPSILON SUBUNIT
KeywordsHYDROLASE / ATP-BINDING / F(O) / F(1) / ATP SYNTHASE / MITOCHONDRIA / INNER MEMBRANE / TRANSMEMBRANE
Function / homology
Function and homology information


Mitochondrial protein degradation / proton transmembrane transporter activity / proton motive force-driven ATP synthesis / proton-transporting two-sector ATPase complex, proton-transporting domain / mitochondrial nucleoid / proton motive force-driven mitochondrial ATP synthesis / proton-transporting ATPase activity, rotational mechanism / H+-transporting two-sector ATPase / proton-transporting ATP synthase complex / proton-transporting ATP synthase activity, rotational mechanism ...Mitochondrial protein degradation / proton transmembrane transporter activity / proton motive force-driven ATP synthesis / proton-transporting two-sector ATPase complex, proton-transporting domain / mitochondrial nucleoid / proton motive force-driven mitochondrial ATP synthesis / proton-transporting ATPase activity, rotational mechanism / H+-transporting two-sector ATPase / proton-transporting ATP synthase complex / proton-transporting ATP synthase activity, rotational mechanism / ADP binding / mitochondrial intermembrane space / mitochondrial inner membrane / lipid binding / ATP hydrolysis activity / mitochondrion / ATP binding / identical protein binding / cytosol
Similarity search - Function
ATP synthase, F1 complex, epsilon subunit superfamily, mitochondrial / ATP Synthase; domain 1 / F0F1 ATP synthase delta/epsilon subunit, N-terminal / ATP synthase, F1 complex, gamma subunit / Atp Synthase Epsilon Chain; Chain: I; / : / Fungal epsilon subunit of F1F0-ATP synthase C-terminal domain / ATP synthase alpha/beta chain, C-terminal domain / Lysin / Thrombin, subunit H - #170 ...ATP synthase, F1 complex, epsilon subunit superfamily, mitochondrial / ATP Synthase; domain 1 / F0F1 ATP synthase delta/epsilon subunit, N-terminal / ATP synthase, F1 complex, gamma subunit / Atp Synthase Epsilon Chain; Chain: I; / : / Fungal epsilon subunit of F1F0-ATP synthase C-terminal domain / ATP synthase alpha/beta chain, C-terminal domain / Lysin / Thrombin, subunit H - #170 / F1F0 ATP synthase subunit C / F1FO ATP Synthase / Elongation Factor Tu (Ef-tu); domain 3 - #20 / 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 / Pyruvate Kinase; Chain: A, domain 1 / 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, F0 complex, subunit C / F1F0 ATP synthase subunit C superfamily / ATP synthase, F0 complex, subunit C, DCCD-binding site / ATP synthase c subunit signature. / 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, alpha subunit nucleotide-binding domain / 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 alpha/beta chain, C terminal domain / V-ATPase proteolipid subunit C-like domain / F/V-ATP synthase subunit C superfamily / ATP synthase subunit C / : / ATPase, F1/V1 complex, beta/alpha subunit, C-terminal / C-terminal domain of V and A type ATP synthase / 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. / Elongation Factor Tu (Ef-tu); domain 3 / ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain / ATP synthase alpha/beta family, nucleotide-binding domain / 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 / Rossmann fold / P-loop containing nucleoside triphosphate hydrolase / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / ATP synthase catalytic sector F1 epsilon subunit / ATP synthase subunit beta, mitochondrial / ATP synthase subunit alpha, mitochondrial / ATP synthase subunit gamma, mitochondrial / ATP synthase subunit 9, mitochondrial / ATP synthase subunit delta, mitochondrial / :
Similarity search - Component
Biological speciesSACCHAROMYCES CEREVISIAE (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.01 Å
AuthorsStock, D. / W Leslie, A.G. / Walker, J.E.
CitationJournal: Science / Year: 1999
Title: Molecular architecture of the rotary motor in ATP synthase.
Authors: Stock, D. / Leslie, A.G. / Walker, J.E.
History
DepositionAug 18, 2010Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 22, 2010Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3May 8, 2019Group: Data collection / Experimental preparation / Other
Category: exptl_crystal_grow / pdbx_database_proc ...exptl_crystal_grow / pdbx_database_proc / pdbx_database_status / struct_biol
Item: _exptl_crystal_grow.method / _pdbx_database_status.recvd_author_approval
Revision 1.4Oct 9, 2019Group: Data collection / Database references / Other / Category: citation / pdbx_database_status
Item: _citation.page_last / _citation.pdbx_database_id_DOI ..._citation.page_last / _citation.pdbx_database_id_DOI / _citation.title / _pdbx_database_status.status_code_sf
Revision 1.5Dec 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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 / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Remark 700 SHEET DETERMINATION METHOD: DSSP

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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
I: ATP SYNTHASE CATALYTIC SECTOR F1 EPSILON SUBUNIT
K: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL
L: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL
M: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL
N: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL
O: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL
P: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL
Q: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL
R: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL
S: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL
T: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL
hetero molecules


Theoretical massNumber of molelcules
Total (without water)478,94929
Polymers476,29719
Non-polymers2,65310
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area30730 Å2
ΔGint-379.6 kcal/mol
Surface area25100 Å2
MethodPISA
Unit cell
Length a, b, c (Å)135.352, 173.711, 137.889
Angle α, β, γ (deg.)90.00, 91.77, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11K
21L
31M
41N
51O
61P
71Q
81R
91S
101T
12O
22P
32Q
42R

NCS domain segments:

Beg auth comp-ID: LEU / Beg label comp-ID: LEU

Dom-IDComponent-IDEns-IDEnd auth comp-IDEnd label comp-IDRefine codeAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111SERSER2KJ3 - 383 - 38
211SERSER2LK3 - 383 - 38
311SERSER2ML3 - 383 - 38
411SERSER2NM3 - 383 - 38
511SERSER2ON3 - 383 - 38
611SERSER2PO3 - 383 - 38
711SERSER2QP3 - 383 - 38
811SERSER2RQ3 - 383 - 38
911SERSER2SR3 - 383 - 38
1011SERSER2TS3 - 383 - 38
121LEULEU2KJ53 - 7253 - 72
221LEULEU2LK53 - 7253 - 72
321LEULEU2ML53 - 7253 - 72
421LEULEU2NM53 - 7253 - 72
521LEULEU2ON53 - 7253 - 72
621LEULEU2PO53 - 7253 - 72
721LEULEU2QP53 - 7253 - 72
821LEULEU2RQ53 - 7253 - 72
921LEULEU2SR53 - 7253 - 72
1021LEULEU2TS53 - 7253 - 72
112SERSER6ON3 - 383 - 38
212SERSER6PO3 - 383 - 38
312SERSER6QP3 - 383 - 38
412SERSER6RQ3 - 383 - 38
122LEULEU6ON53 - 7253 - 72
222LEULEU6PO53 - 7253 - 72
322LEULEU6QP53 - 7253 - 72
422LEULEU6RQ53 - 7253 - 72

NCS ensembles :
ID
1
2

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Components

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ATP SYNTHASE SUBUNIT ... , 4 types, 17 molecules ABCDEFGKLMNOPQRST

#1: Protein ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL


Mass: 58677.777 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) SACCHAROMYCES CEREVISIAE (brewer's yeast) / Organelle: MITOCHONDRION / References: UniProt: P07251
#2: Protein ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL


Mass: 54854.488 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) SACCHAROMYCES CEREVISIAE (brewer's yeast) / Organelle: MITOCHONDRION / References: UniProt: P00830, EC: 3.6.1.34
#3: Protein ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL / F-ATPASE GAMMA SUBUNIT


Mass: 34396.539 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) SACCHAROMYCES CEREVISIAE (brewer's yeast) / Organelle: MITOCHONDRION / References: UniProt: P38077
#6: Protein
ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL / LIPID-BINDING PROTEIN / OLIGOMYCIN RESISTANCE PROTEIN 1


Mass: 7762.375 Da / Num. of mol.: 10 / Source method: isolated from a natural source / Source: (natural) SACCHAROMYCES CEREVISIAE (brewer's yeast) / Organelle: MITOCHONDRION / References: UniProt: P61829

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Protein , 2 types, 2 molecules HI

#4: Protein ATP SYNTHASE


Mass: 17037.344 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: MITOCHONDRION / Source: (natural) SACCHAROMYCES CEREVISIAE (brewer's yeast) / References: UniProt: Q12165
#5: Protein ATP SYNTHASE CATALYTIC SECTOR F1 EPSILON SUBUNIT


Mass: 6642.381 Da / Num. of mol.: 1 / Fragment: RESIDUES 2-62 / Source method: isolated from a natural source / Source: (natural) SACCHAROMYCES CEREVISIAE (brewer's yeast) / Organelle: MITOCHONDRION / References: UniProt: Q2XN67, UniProt: E9P9X4*PLUS

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Non-polymers , 2 types, 10 molecules

#7: Chemical
ChemComp-ANP / PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER


Mass: 506.196 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C10H17N6O12P3 / Comment: AMP-PNP, energy-carrying molecule analogue*YM
#8: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Mg

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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: 3.84 Å3/Da / Density % sol: 67.75 % / Description: NONE
Crystal growMethod: microbatch / pH: 8
Details: 0.1 M TRIS/CL PH8.0, 12% PEG 6000, 150 MM NACL, 1 MM AMP-PNP, 40 MICROM ADP, 1 MM DTT, 0.02% NAN3. MIXED 1:1 WITH PROTEIN SOLUTION UNDER PARAFFIN OIL IN MICROBATCH PLATE.

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-2 / Wavelength: 0.933
DetectorType: ADSC CCD / Detector: CCD / Date: Dec 1, 1999
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.933 Å / Relative weight: 1
ReflectionResolution: 3.01→20 Å / Num. obs: 93955 / % possible obs: 74.8 % / Observed criterion σ(I): 2 / Redundancy: 1.8 % / Biso Wilson estimate: 80.8 Å2 / Rmerge(I) obs: 0.09 / Net I/σ(I): 4.1
Reflection shellResolution: 3→3.16 Å / Redundancy: 1.3 % / Rmerge(I) obs: 0.18 / Mean I/σ(I) obs: 3.9 / % possible all: 41.5

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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 2HLD

2hld


Resolution: 3.01→20 Å / Cor.coef. Fo:Fc: 0.946 / Cor.coef. Fo:Fc free: 0.922 / SU B: 44.376 / SU ML: 0.357 / Cross valid method: THROUGHOUT / ESU R Free: 0.486 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS.
RfactorNum. reflection% reflectionSelection details
Rfree0.25335 2352 2.5 %RANDOM
Rwork0.20954 ---
obs0.21066 91603 74.83 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1 Å / Solvent model: MASK
Displacement parametersBiso mean: 116.881 Å2
Baniso -1Baniso -2Baniso -3
1-4.54 Å20 Å26.94 Å2
2---6.25 Å20 Å2
3---2.14 Å2
Refinement stepCycle: LAST / Resolution: 3.01→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms29953 0 160 0 30113
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.02230557
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.3681.99141439
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.0153986
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.57624.3681147
X-RAY DIFFRACTIONr_dihedral_angle_3_deg20.207155190
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.07115173
X-RAY DIFFRACTIONr_chiral_restr0.0830.24952
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.0222461
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2270.215595
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.310.221201
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.150.21049
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined0.1970.27
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2230.219
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_it1.197320196
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it2.265531745
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it3.642711270
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it6.072109694
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
11K224tight positional0.050.1
12L224tight positional0.050.1
13M224tight positional0.050.1
14N224tight positional0.050.1
15O224tight positional0.040.1
16P224tight positional0.040.1
17Q224tight positional0.040.1
18R224tight positional0.030.1
19S224tight positional0.050.1
110T224tight positional0.040.1
11K163medium positional0.210.3
12L163medium positional0.190.3
13M163medium positional0.210.3
14N163medium positional0.220.3
15O163medium positional0.120.3
16P163medium positional0.120.3
17Q163medium positional0.110.3
18R163medium positional0.120.3
19S163medium positional0.190.3
110T163medium positional0.190.3
21O387loose positional0.040.1
22P387loose positional0.040.1
23Q387loose positional0.040.1
24R387loose positional0.040.1
11K224tight thermal4.7820
12L224tight thermal5.4720
13M224tight thermal3.8220
14N224tight thermal2.5720
15O224tight thermal4.0720
16P224tight thermal5.0920
17Q224tight thermal6.220
18R224tight thermal3.5920
19S224tight thermal3.2720
110T224tight thermal3.3120
11K163medium thermal4.1420
12L163medium thermal5.4420
13M163medium thermal3.7320
14N163medium thermal3.5820
15O163medium thermal3.620
16P163medium thermal4.5320
17Q163medium thermal5.1620
18R163medium thermal3.320
19S163medium thermal3.2920
110T163medium thermal3.3720
21O387loose thermal2.1110
22P387loose thermal1.7210
23Q387loose thermal2.1910
24R387loose thermal2.0810
LS refinement shellResolution: 3.01→3.086 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.334 136 -
Rwork0.269 4867 -
obs--55.43 %
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)
11.70010.2209-0.4881.36280.05111.2660.0223-0.0091-0.0899-0.0273-0.01590.20080.1298-0.3157-0.0063-0.09840.00990.0858-0.4168-0.0579-0.05948.3033-32.1375-11.9225
21.72350.2106-0.03663.09750.10880.8949-0.05340.27520.2496-0.126-0.06540.8398-0.1127-0.52810.11880.09670.2868-0.30290.20060.2257-0.033827.560916.1027-37.9438
31.3058-0.0589-0.22221.28680.34952.49530.0519-0.00710.04060.1272-0.0589-0.0143-0.1275-0.18280.007-0.1455-0.00390.2353-0.61960.0334-0.195564.647619.03514.4256
41.63040.4789-0.80311.36470.04631.71050.0015-0.2207-0.17380.3239-0.0456-0.18750.06740.06920.0441-0.09060.0740.0692-0.52240.0691-0.13467.2176-11.48585.6502
52.15870.6686-0.01161.5501-0.1760.9882-0.04780.4004-0.2043-0.3013-0.00730.55690.112-0.61260.0551-0.02430.0301-0.17820.146-0.0457-0.0428.1511-19.0131-35.9305
61.21680.1782-0.46172.08540.31851.73890.12260.17090.5466-0.34780.01640.3617-0.6494-0.2322-0.139-0.07440.2539-0.0377-0.32720.1888-0.191446.063831.0578-20.0049
74.2143-0.2761-3.33140.30550.19123.54740.1446-0.49470.26870.16420.00350.1913-0.19590.0095-0.1480.02790.10090.23770.2948-0.07430.106311.7334.528516.5663
810.93970.4769-3.98371.3496-1.20036.3424-0.7942-0.2058-1.07660.1175-0.01870.02710.6031-0.21160.8129-0.07290.19860.34750.0124-0.0552-0.027-5.6199-9.163732.5235
94.6944-0.2205-2.56421.48110.10422.63690.0126-0.7031-0.09330.4164-0.1620.0367-0.06960.75920.1494-0.456-0.12850.5196-0.3145-0.0555-0.5651-35.5244-0.272767.358
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A26 - 700
2X-RAY DIFFRACTION2B25 - 700
3X-RAY DIFFRACTION3C26 - 700
4X-RAY DIFFRACTION4D6 - 700
5X-RAY DIFFRACTION5E8 - 475
6X-RAY DIFFRACTION6F7 - 601
7X-RAY DIFFRACTION7G1 - 276
8X-RAY DIFFRACTION8H13 - 90
9X-RAY DIFFRACTION8I8 - 61
10X-RAY DIFFRACTION9K3 - 74
11X-RAY DIFFRACTION9L2 - 72
12X-RAY DIFFRACTION9M1 - 72
13X-RAY DIFFRACTION9N1 - 72
14X-RAY DIFFRACTION9O1 - 73
15X-RAY DIFFRACTION9P1 - 74
16X-RAY DIFFRACTION9Q1 - 74
17X-RAY DIFFRACTION9R1 - 73
18X-RAY DIFFRACTION9S1 - 73
19X-RAY DIFFRACTION9T2 - 73

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