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- PDB-3coj: Crystal Structure of the BRCT Domains of Human BRCA1 in Complex w... -

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Basic information

Entry
Database: PDB / ID: 3coj
TitleCrystal Structure of the BRCT Domains of Human BRCA1 in Complex with a Phosphorylated Peptide from Human Acetyl-CoA Carboxylase 1
Components
  • Acetyl-CoA carboxylase 1
  • Breast cancer type 1 susceptibility protein
KeywordsANTITUMOR PROTEIN/LIGASE / Breast Cancer / Ovarian Cancer / Fatty Acid Biosynthesis / lipid synthesis / Obesity / Protein-peptide complex / Protein Protein interaction / Anti-oncogene / Cell cycle / Disease mutation / DNA damage / DNA repair / DNA-binding / Metal-binding / Nucleus / Phosphoprotein / Zinc-finger / Alternative promoter usage / ATP-binding / Biotin / Ligase / Manganese / Multifunctional enzyme / Nucleotide-binding / ANTITUMOR PROTEIN-LIGASE COMPLEX
Function / homology
Function and homology information


fatty-acyl-CoA biosynthetic process / Defective DNA double strand break response due to BRCA1 loss of function / Defective DNA double strand break response due to BARD1 loss of function / BRCA1-BARD1 complex / Defective HLCS causes multiple carboxylase deficiency / acetyl-CoA carboxylase / BRCA1-C complex / BRCA1-B complex / Biotin transport and metabolism / BRCA1-A complex ...fatty-acyl-CoA biosynthetic process / Defective DNA double strand break response due to BRCA1 loss of function / Defective DNA double strand break response due to BARD1 loss of function / BRCA1-BARD1 complex / Defective HLCS causes multiple carboxylase deficiency / acetyl-CoA carboxylase / BRCA1-C complex / BRCA1-B complex / Biotin transport and metabolism / BRCA1-A complex / random inactivation of X chromosome / negative regulation of centriole replication / sex-chromosome dosage compensation / Fatty acyl-CoA biosynthesis / acetyl-CoA metabolic process / negative regulation of intracellular estrogen receptor signaling pathway / gamma-tubulin ring complex / malonyl-CoA biosynthetic process / nuclear ubiquitin ligase complex / ChREBP activates metabolic gene expression / acetyl-CoA carboxylase activity / chordate embryonic development / cellular response to indole-3-methanol / negative regulation of fatty acid biosynthetic process / lateral element / homologous recombination / DNA strand resection involved in replication fork processing / tissue homeostasis / protein K6-linked ubiquitination / regulation of DNA damage checkpoint / Carnitine metabolism / Impaired BRCA2 binding to PALB2 / protein metabolic process / XY body / mitotic G2/M transition checkpoint / postreplication repair / DNA repair complex / RNA polymerase binding / centrosome cycle / Defective homologous recombination repair (HRR) due to BRCA1 loss of function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function / Homologous DNA Pairing and Strand Exchange / Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA) / Resolution of D-loop Structures through Holliday Junction Intermediates / intracellular non-membrane-bounded organelle / HDR through Single Strand Annealing (SSA) / negative regulation of gene expression via chromosomal CpG island methylation / Impaired BRCA2 binding to RAD51 / DNA-binding transcription activator activity / response to ionizing radiation / Transcriptional Regulation by E2F6 / lipid homeostasis / mitotic G2 DNA damage checkpoint signaling / Presynaptic phase of homologous DNA pairing and strand exchange / negative regulation of cell cycle / positive regulation of vascular endothelial growth factor production / negative regulation of reactive oxygen species metabolic process / protein autoubiquitination / SUMOylation of DNA damage response and repair proteins / regulation of DNA repair / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / ubiquitin ligase complex / Meiotic synapsis / positive regulation of DNA repair / tubulin binding / Activation of gene expression by SREBF (SREBP) / male germ cell nucleus / chromosome segregation / cellular response to ionizing radiation / TP53 Regulates Transcription of DNA Repair Genes / Nonhomologous End-Joining (NHEJ) / double-strand break repair via homologous recombination / RING-type E3 ubiquitin transferase / G2/M DNA damage checkpoint / HDR through Homologous Recombination (HRR) / negative regulation of cell growth / Metalloprotease DUBs / Meiotic recombination / fibrillar center / fatty acid biosynthetic process / cellular response to prostaglandin E stimulus / positive regulation of angiogenesis / ubiquitin-protein transferase activity / intrinsic apoptotic signaling pathway in response to DNA damage / KEAP1-NFE2L2 pathway / double-strand break repair / p53 binding / actin cytoskeleton / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / cellular response to tumor necrosis factor / chromosome / Neddylation / Processing of DNA double-strand break ends / protein homotetramerization / Regulation of TP53 Activity through Phosphorylation / damaged DNA binding / transcription coactivator activity / nuclear body / regulation of cell cycle
Similarity search - Function
Breast cancer type 1 susceptibility protein (BRCA1) / BRCA1, serine-rich domain / BRCA1-associated / Serine-rich domain associated with BRCT / Acetyl-CoA carboxylase, central domain / : / : / Acetyl-CoA carboxylase, central region / Acetyl-CoA carboxylase, BT domain / BRCT domain ...Breast cancer type 1 susceptibility protein (BRCA1) / BRCA1, serine-rich domain / BRCA1-associated / Serine-rich domain associated with BRCT / Acetyl-CoA carboxylase, central domain / : / : / Acetyl-CoA carboxylase, central region / Acetyl-CoA carboxylase, BT domain / BRCT domain / Acetyl-coenzyme A carboxyltransferase, C-terminal / Acetyl-coenzyme A (CoA) carboxyltransferase C-terminal domain profile. / Acetyl-coenzyme A carboxyltransferase, N-terminal / Acetyl-coenzyme A (CoA) carboxyltransferase N-terminal domain profile. / Acetyl-CoA carboxylase / Carboxyl transferase domain / Biotin-binding site / Biotin-requiring enzymes attachment site. / Biotin carboxylase-like, N-terminal domain / Biotin carboxylase, C-terminal / Biotin carboxylation domain / Biotin carboxylase, N-terminal domain / Biotin carboxylase C-terminal domain / Biotin carboxylation domain profile. / Biotin carboxylase C-terminal domain / Carbamoyl-phosphate synthase subdomain signature 1. / Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain / Carbamoyl-phosphate synthase L chain, ATP binding domain / Biotin-requiring enzyme / Rudiment single hybrid motif / Biotinyl/lipoyl domain profile. / Biotin/lipoyl attachment / Single hybrid motif / Zinc finger, C3HC4 RING-type / Zinc finger, C3HC4 type (RING finger) / ATP-grasp fold, subdomain 1 / BRCA1 C Terminus (BRCT) domain / Pre-ATP-grasp domain superfamily / ATP-grasp fold / ATP-grasp fold profile. / breast cancer carboxy-terminal domain / ClpP/crotonase-like domain superfamily / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. / BRCT domain profile. / BRCT domain / BRCT domain superfamily / Ring finger / Zinc finger RING-type profile. / Zinc finger, RING-type / Carbamoyl-phosphate synthase subdomain signature 2. / Zinc finger, RING/FYVE/PHD-type / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Breast cancer type 1 susceptibility protein / Acetyl-CoA carboxylase 1
Similarity search - Component
Biological speciesHomo sapiens (human)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.21 Å
AuthorsShen, Y. / Tong, L.
CitationJournal: Biochemistry / Year: 2008
Title: Structural evidence for direct interactions between the BRCT domains of human BRCA1 and a phospho-peptide from human ACC1
Authors: Shen, Y. / Tong, L.
History
DepositionMar 28, 2008Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 27, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Oct 25, 2017Group: Refinement description / Source and taxonomy / Category: pdbx_entity_src_syn / software
Item: _pdbx_entity_src_syn.ncbi_taxonomy_id / _pdbx_entity_src_syn.organism_scientific ..._pdbx_entity_src_syn.ncbi_taxonomy_id / _pdbx_entity_src_syn.organism_scientific / _software.classification / _software.name
Revision 1.3Aug 30, 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 / struct_conn / struct_ncs_dom_lim / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
X: Breast cancer type 1 susceptibility protein
A: Breast cancer type 1 susceptibility protein
B: Breast cancer type 1 susceptibility protein
C: Breast cancer type 1 susceptibility protein
D: Breast cancer type 1 susceptibility protein
E: Breast cancer type 1 susceptibility protein
F: Breast cancer type 1 susceptibility protein
G: Breast cancer type 1 susceptibility protein
H: Acetyl-CoA carboxylase 1
I: Acetyl-CoA carboxylase 1
J: Acetyl-CoA carboxylase 1
K: Acetyl-CoA carboxylase 1
L: Acetyl-CoA carboxylase 1
M: Acetyl-CoA carboxylase 1
N: Acetyl-CoA carboxylase 1
O: Acetyl-CoA carboxylase 1


Theoretical massNumber of molelcules
Total (without water)225,94516
Polymers225,94516
Non-polymers00
Water00
1
X: Breast cancer type 1 susceptibility protein
H: Acetyl-CoA carboxylase 1


Theoretical massNumber of molelcules
Total (without water)28,2432
Polymers28,2432
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1130 Å2
ΔGint-8.2 kcal/mol
Surface area11600 Å2
MethodPISA
2
A: Breast cancer type 1 susceptibility protein
I: Acetyl-CoA carboxylase 1


Theoretical massNumber of molelcules
Total (without water)28,2432
Polymers28,2432
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1080 Å2
ΔGint-8.6 kcal/mol
Surface area11360 Å2
MethodPISA
3
B: Breast cancer type 1 susceptibility protein
J: Acetyl-CoA carboxylase 1


Theoretical massNumber of molelcules
Total (without water)28,2432
Polymers28,2432
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1050 Å2
ΔGint-9.9 kcal/mol
Surface area11670 Å2
MethodPISA
4
C: Breast cancer type 1 susceptibility protein
K: Acetyl-CoA carboxylase 1


Theoretical massNumber of molelcules
Total (without water)28,2432
Polymers28,2432
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
D: Breast cancer type 1 susceptibility protein
L: Acetyl-CoA carboxylase 1


Theoretical massNumber of molelcules
Total (without water)28,2432
Polymers28,2432
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1050 Å2
ΔGint-8.9 kcal/mol
Surface area11470 Å2
MethodPISA
6
E: Breast cancer type 1 susceptibility protein
M: Acetyl-CoA carboxylase 1


Theoretical massNumber of molelcules
Total (without water)28,2432
Polymers28,2432
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area680 Å2
ΔGint-8.1 kcal/mol
Surface area11660 Å2
MethodPISA
7
F: Breast cancer type 1 susceptibility protein
N: Acetyl-CoA carboxylase 1


Theoretical massNumber of molelcules
Total (without water)28,2432
Polymers28,2432
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
8
G: Breast cancer type 1 susceptibility protein
O: Acetyl-CoA carboxylase 1


Theoretical massNumber of molelcules
Total (without water)28,2432
Polymers28,2432
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area770 Å2
ΔGint-9 kcal/mol
Surface area11500 Å2
MethodPISA
Unit cell
Length a, b, c (Å)83.330, 181.513, 194.643
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11X
21A
31B
41C
51D
61E
71F
81G
12H
22I
32J
42K
52L
62M
72N
82O

NCS domain segments:

Component-ID: 1 / Refine code: 4

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11LYSLYSPROPROXA1648 - 185924 - 235
21LYSLYSPROPROAB1648 - 185924 - 235
31LYSLYSPROPROBC1648 - 185924 - 235
41LYSLYSPROPROCD1648 - 185924 - 235
51ARGARGPROPRODE1649 - 185925 - 235
61ARGARGPROPROEF1649 - 185925 - 235
71ARGARGPROPROFG1649 - 185925 - 235
81LYSLYSPROPROGH1648 - 185924 - 235
12PROPROGLYGLYHI1261 - 12704 - 13
22PROPROGLYGLYIJ1261 - 12704 - 13
32PROPROGLYGLYJK1261 - 12704 - 13
42PROPROGLYGLYKL1261 - 12704 - 13
52PROPROGLYGLYLM1261 - 12704 - 13
62PROPROPROPROMN1261 - 12674 - 10
72GLNGLNPHEPHENO1262 - 12665 - 9
82PROPROPROPROOP1261 - 12674 - 10

NCS ensembles :
ID
1
2

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Components

#1: Protein
Breast cancer type 1 susceptibility protein / RING finger protein 53


Mass: 26833.805 Da / Num. of mol.: 8 / Fragment: BRCT1 and BRCT2 domains
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: BRCA1, RNF53 / Plasmid: pET28a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21/Star (DE3) / References: UniProt: P38398
#2: Protein/peptide
Acetyl-CoA carboxylase 1 / ACC-alpha


Mass: 1409.347 Da / Num. of mol.: 8 / Fragment: residues 1258-1270 / Source method: obtained synthetically
Details: Synthesized human ACC1 peptide with Ser1263 phosphorylated.
Source: (synth.) synthetic construct (others) / References: UniProt: Q13085, acetyl-CoA carboxylase

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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: 3.58 Å3/Da / Density % sol: 65.6 %
Crystal growTemperature: 294 K / Method: vapor diffusion, sitting drop / pH: 4.5
Details: 100 mM sodium acetate (pH 4.5), 25-27% (v/v) PEG400, and 200 mM calcium acetate, VAPOR DIFFUSION, SITTING DROP, temperature 294K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X4A / Wavelength: 0.97905 / Wavelength: 0.97905 Å
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: Oct 21, 2006 / Details: MIRRORS
RadiationMonochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97905 Å / Relative weight: 1
ReflectionResolution: 3.2→30 Å / Num. all: 44707 / Num. obs: 42426 / % possible obs: 92.5 % / Observed criterion σ(I): 0 / Redundancy: 3.2 % / Rmerge(I) obs: 0.118 / Net I/σ(I): 7.7876
Reflection shellResolution: 3.2→3.31 Å / Redundancy: 2.2 % / Rmerge(I) obs: 0.391 / Mean I/σ(I) obs: 2.843 / Num. unique all: 3981 / % possible all: 83.5

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Processing

Software
NameVersionClassification
SnBTHEN SOLVE/RESOLVEphasing
REFMAC5.2.0003refinement
DENZOdata reduction
SCALEPACKdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 1JNX

1jnx


Resolution: 3.21→29.89 Å / Cor.coef. Fo:Fc: 0.888 / Cor.coef. Fo:Fc free: 0.84 / SU B: 77.017 / SU ML: 0.575 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R Free: 0.592 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.3075 2249 5 %RANDOM
Rwork0.25713 ---
obs0.2597 42426 91.56 %-
all-44707 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 87.613 Å2
Baniso -1Baniso -2Baniso -3
1--0.91 Å20 Å20 Å2
2--0.58 Å20 Å2
3---0.33 Å2
Refinement stepCycle: LAST / Resolution: 3.21→29.89 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13867 0 0 0 13867
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.02214199
X-RAY DIFFRACTIONr_angle_refined_deg1.1621.9319246
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.20751699
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.54723.696644
X-RAY DIFFRACTIONr_dihedral_angle_3_deg21.39215.0492429
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.3751588
X-RAY DIFFRACTIONr_chiral_restr0.080.22140
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0210587
X-RAY DIFFRACTIONr_nbd_refined0.2130.26509
X-RAY DIFFRACTIONr_nbtor_refined0.310.29399
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1540.2438
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2120.260
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.070.23
X-RAY DIFFRACTIONr_mcbond_it0.1381.58796
X-RAY DIFFRACTIONr_mcangle_it0.244214001
X-RAY DIFFRACTIONr_scbond_it0.30536118
X-RAY DIFFRACTIONr_scangle_it0.5254.55245
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
12X1633medium positional0.590.5
13A1633medium positional0.650.5
14B1633medium positional0.640.5
15C1633medium positional0.590.5
16D1633medium positional0.680.5
17E1633medium positional0.610.5
18F1633medium positional0.60.5
11G1633medium positional0.60.5
22H44medium positional0.360.5
23I44medium positional0.470.5
24J44medium positional0.370.5
25K44medium positional0.350.5
26L44medium positional0.570.5
27M44medium positional0.620.5
28N44medium positional0.720.5
22O44medium positional0.820.5
12X1633medium thermal0.212
13A1633medium thermal0.192
14B1633medium thermal0.222
15C1633medium thermal0.212
16D1633medium thermal0.152
17E1633medium thermal0.152
18F1633medium thermal0.172
11G1633medium thermal0.172
22H44medium thermal0.22
23I44medium thermal0.242
24J44medium thermal0.432
25K44medium thermal0.132
26L44medium thermal0.152
27M44medium thermal0.122
28N44medium thermal0.172
22O44medium thermal0.262
LS refinement shellResolution: 3.21→3.297 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.387 137 -
Rwork0.368 2370 -
obs-2370 71.73 %
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)
13.1641-0.38443.11293.2091-1.229211.34350.03540.2076-0.1394-0.00250.1498-0.02620.3333-0.0472-0.1852-0.2807-0.1346-0.1056-0.57860.0685-0.232414.25-20.134-22.312
22.40111.5303-0.09419.2122-2.78655.0932-0.1756-0.06570.06550.43010.06810.0063-0.3927-0.45570.1076-0.04690.2262-0.2316-0.32790.0073-0.410817.9082.2552.922
33.663-2.60450.19738.39430.63952.6954-0.2283-0.10830.40260.24170.0431-0.4627-0.08050.14970.1852-0.07320.1268-0.1012-0.35590.0449-0.53135.835-22.70525.142
42.1639-0.10831.11544.86041.88939.8292-0.24230.04340.08650.22910.21880.35880.10410.18440.0235-0.39040.10370.2109-0.4770.1206-0.277336.18-49.8146.457
57.34790.8483-0.10581.68460.19952.3647-0.20580.2156-0.5312-0.2996-0.1403-1.11050.56740.56120.34610.2865-0.00240.20750.10830.36740.438840.527-19.174-45.633
68.9444-0.85982.7560.3504-0.99242.8881-0.17040.53830.1848-0.36960.2442-0.337-0.14140.9553-0.07380.2751-0.0322-0.23640.1667-0.36180.471563.214-0.84128.002
77.41561.99351.69294.9333-0.2975.4473-0.3491-0.05670.01391.00360.69740.7942-0.5993-1.1226-0.34840.92950.70810.0334-0.14530.0424-0.1306-0.74829.867-3.705
84.7521-2.0263-1.25255.8583-0.39884.1594-0.4402-0.19140.27840.51740.1875-1.3789-0.11230.97760.25270.52770.1402-0.5262-0.0925-0.12210.210526.66446.718-23.483
913.7702-2.1544-1.821615.7838-0.18970.2555-2.0493-2.30211.15531.39860.76910.6077-1.2759-1.73391.28010.37320.0319-0.06390.096-0.0553-0.09115.686-14.851-16.96
105.2131-3.90491.910117.14766.41735.03051.9208-0.84660.4429-1.1457-0.38852.20411.0834-2.0592-1.53230.28750.1366-0.10980.00470.08190.141412.8948.76611.166
1114.411513.7649-22.350745.4439-14.809335.9875-1.20222.90063.78961.8501-4.3158-4.24890.2982.98255.5180.0572-0.0889-0.29330.0336-0.03850.015227.706-27.70732.122
126.32623.43241.50816.67544.304821.5481.3294-1.0905-1.31870.9807-1.11190.88740.0428-1.4704-0.2174-0.04-0.20150.15730.20490.08050.062730.69-58.6351.914
1359.846425.052-50.992163.6514-15.177346.95391.2495-0.05680.7351-3.262-1.03182.2169-0.2646-0.8267-0.21780.5215-0.3371-0.35670.30930.02220.060836.284-7.601-42.867
1430.92813.085-24.138339.449332.780650.47343.4587-3.2812-3.30244.31571.0651-0.37031.52470.0456-4.52380.73190.0265-0.44230.12130.25150.429958.701-5.01439.414
1596.90211.678321.406879.8136-4.788947.02122.4167-2.7479-1.43830.9159-4.4141-0.6739-0.74560.48091.99740.50310.23870.0287-0.0799-0.2147-0.0745-3.55242.455-1.518
16153.83252.4709-73.618242.6651-33.855542.40083.8472.97382.15612.22640.35011.8069-1.7043-0.3133-4.1970.56880.2091-0.35520.0832-0.01910.411230.22850.188-11.473
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
1X-RAY DIFFRACTION1XA1649 - 185925 - 235
2X-RAY DIFFRACTION2AB1649 - 185925 - 235
3X-RAY DIFFRACTION3BC1649 - 185925 - 235
4X-RAY DIFFRACTION4CD1649 - 185925 - 235
5X-RAY DIFFRACTION5DE1649 - 185925 - 235
6X-RAY DIFFRACTION6EF1649 - 185925 - 235
7X-RAY DIFFRACTION7FG1649 - 185925 - 235
8X-RAY DIFFRACTION8GH1649 - 185925 - 235
9X-RAY DIFFRACTION9HI1261 - 12704 - 13
10X-RAY DIFFRACTION10IJ1261 - 12704 - 13
11X-RAY DIFFRACTION11JK1261 - 12704 - 13
12X-RAY DIFFRACTION12KL1258 - 12701 - 13
13X-RAY DIFFRACTION13LM1261 - 12704 - 13
14X-RAY DIFFRACTION14MN1261 - 12674 - 10
15X-RAY DIFFRACTION15NO1262 - 12665 - 9
16X-RAY DIFFRACTION16OP1261 - 12674 - 10

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