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- PDB-6p5p: Discovery of a Novel, Highly Potent, and Selective Thieno[3,2-d]p... -

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Basic information

Entry
Database: PDB / ID: 6p5p
TitleDiscovery of a Novel, Highly Potent, and Selective Thieno[3,2-d]pyrimidinone-Based Cdc7 inhibitor with a Quinuclidine Moiety (TAK-931) as an Orally Active Investigational Anti-Tumor Agent
ComponentsRho-associated protein kinase 2
KeywordsTRANSFERASE/TRANSFERASE INHIBITOR / Kinase / Inhibitor / Oral / Anti-tumor / TRANSFERASE-TRANSFERASE INHIBITOR / TRANSFERASE-TRANSFERASE INHIBITOR complex
Function / homology
Function and homology information


positive regulation of connective tissue growth factor production / cellular response to acetylcholine / positive regulation of centrosome duplication / regulation of angiotensin-activated signaling pathway / negative regulation of protein localization to lysosome / regulation of keratinocyte differentiation / positive regulation of connective tissue replacement / positive regulation of fibroblast growth factor production / response to transforming growth factor beta / positive regulation of amyloid precursor protein catabolic process ...positive regulation of connective tissue growth factor production / cellular response to acetylcholine / positive regulation of centrosome duplication / regulation of angiotensin-activated signaling pathway / negative regulation of protein localization to lysosome / regulation of keratinocyte differentiation / positive regulation of connective tissue replacement / positive regulation of fibroblast growth factor production / response to transforming growth factor beta / positive regulation of amyloid precursor protein catabolic process / regulation of cell junction assembly / negative regulation of bicellular tight junction assembly / regulation of nervous system process / positive regulation of protein localization to early endosome / regulation of cellular response to hypoxia / modulation by host of viral process / negative regulation of nitric oxide biosynthetic process / embryonic morphogenesis / negative regulation of biomineral tissue development / regulation of cell motility / cellular response to testosterone stimulus / regulation of establishment of endothelial barrier / RHO GTPases Activate ROCKs / regulation of stress fiber assembly / actomyosin structure organization / Sema4D induced cell migration and growth-cone collapse / response to angiotensin / aortic valve morphogenesis / cortical actin cytoskeleton organization / RHOBTB1 GTPase cycle / regulation of establishment of cell polarity / tau-protein kinase activity / regulation of focal adhesion assembly / positive regulation of amyloid-beta formation / RHOB GTPase cycle / EPHA-mediated growth cone collapse / RHOC GTPase cycle / positive regulation of cardiac muscle hypertrophy / mRNA destabilization / mitotic cytokinesis / centrosome duplication / RHOH GTPase cycle / smooth muscle contraction / RHOA GTPase cycle / endopeptidase activator activity / epithelial to mesenchymal transition / Rho protein signal transduction / regulation of cell adhesion / positive regulation of stress fiber assembly / EPHB-mediated forward signaling / positive regulation of endothelial cell migration / negative regulation of angiogenesis / blood vessel diameter maintenance / response to ischemia / protein localization to plasma membrane / regulation of actin cytoskeleton organization / regulation of circadian rhythm / small GTPase binding / tau protein binding / VEGFA-VEGFR2 Pathway / cytoplasmic ribonucleoprotein granule / rhythmic process / G alpha (12/13) signalling events / positive regulation of protein phosphorylation / actin cytoskeleton organization / protease binding / Potential therapeutics for SARS / eukaryotic translation initiation factor 2alpha kinase activity / cytoskeleton / 3-phosphoinositide-dependent protein kinase activity / DNA-dependent protein kinase activity / ribosomal protein S6 kinase activity / histone H3S10 kinase activity / histone H2AXS139 kinase activity / histone H3S28 kinase activity / histone H4S1 kinase activity / histone H2BS14 kinase activity / histone H3T3 kinase activity / histone H2AS121 kinase activity / Rho-dependent protein serine/threonine kinase activity / histone H2BS36 kinase activity / histone H3S57 kinase activity / histone H2AT120 kinase activity / AMP-activated protein kinase activity / histone H2AS1 kinase activity / histone H3T6 kinase activity / histone H3T11 kinase activity / histone H3T45 kinase activity / non-specific serine/threonine protein kinase / positive regulation of MAPK cascade / positive regulation of cell migration / protein phosphorylation / negative regulation of gene expression / protein serine kinase activity / protein serine/threonine kinase activity / centrosome / positive regulation of gene expression / structural molecule activity / RNA binding / zinc ion binding
Similarity search - Function
: / Rho-associated protein kinase 2, HR1 domain / ROCK, Rho binding domain / Rho-associated protein kinase 1/2 / Rho Binding / Rho-binding (RhoBD) domain profile. / : / HR1 rho-binding domain / REM-1 domain profile. / Zinc finger phorbol-ester/DAG-type profile. ...: / Rho-associated protein kinase 2, HR1 domain / ROCK, Rho binding domain / Rho-associated protein kinase 1/2 / Rho Binding / Rho-binding (RhoBD) domain profile. / : / HR1 rho-binding domain / REM-1 domain profile. / Zinc finger phorbol-ester/DAG-type profile. / Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains) / Protein kinase C-like, phorbol ester/diacylglycerol-binding domain / C1-like domain superfamily / Extension to Ser/Thr-type protein kinases / AGC-kinase, C-terminal / AGC-kinase C-terminal domain profile. / PH domain profile. / Pleckstrin homology domain. / Pleckstrin homology domain / PH-like domain superfamily / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Chem-O1V / Rho-associated protein kinase 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.3 Å
AuthorsHoffman, I.D. / Skene, R.J.
CitationJournal: J.Med.Chem. / Year: 2020
Title: Discovery of a Novel, Highly Potent, and Selective Thieno[3,2-d]pyrimidinone-Based Cdc7 Inhibitor with a Quinuclidine Moiety (TAK-931) as an Orally Active Investigational Antitumor Agent.
Authors: Kurasawa, O. / Miyazaki, T. / Homma, M. / Oguro, Y. / Imada, T. / Uchiyama, N. / Iwai, K. / Yamamoto, Y. / Ohori, M. / Hara, H. / Sugimoto, H. / Iwata, K. / Skene, R. / Hoffman, I. / Ohashi, ...Authors: Kurasawa, O. / Miyazaki, T. / Homma, M. / Oguro, Y. / Imada, T. / Uchiyama, N. / Iwai, K. / Yamamoto, Y. / Ohori, M. / Hara, H. / Sugimoto, H. / Iwata, K. / Skene, R. / Hoffman, I. / Ohashi, A. / Nomura, T. / Cho, N.
History
DepositionMay 30, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 15, 2020Provider: repository / Type: Initial release
Revision 1.1Feb 26, 2020Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title / _citation_author.name
Revision 1.2Oct 11, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Rho-associated protein kinase 2
B: Rho-associated protein kinase 2
C: Rho-associated protein kinase 2
D: Rho-associated protein kinase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)186,2368
Polymers184,8704
Non-polymers1,3664
Water00
1
A: Rho-associated protein kinase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)46,5592
Polymers46,2171
Non-polymers3411
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Rho-associated protein kinase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)46,5592
Polymers46,2171
Non-polymers3411
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Rho-associated protein kinase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)46,5592
Polymers46,2171
Non-polymers3411
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: Rho-associated protein kinase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)46,5592
Polymers46,2171
Non-polymers3411
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
A: Rho-associated protein kinase 2
D: Rho-associated protein kinase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)93,1184
Polymers92,4352
Non-polymers6832
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3700 Å2
ΔGint-27 kcal/mol
Surface area34770 Å2
MethodPISA
6
B: Rho-associated protein kinase 2
C: Rho-associated protein kinase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)93,1184
Polymers92,4352
Non-polymers6832
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3310 Å2
ΔGint-28 kcal/mol
Surface area33880 Å2
MethodPISA
Unit cell
Length a, b, c (Å)89.171, 146.438, 111.300
Angle α, β, γ (deg.)90.000, 97.130, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12A
22B
13A
23B
14A
24B
15A
25B
16A
26C
17A
27C
18A
28C
19A
29D
110A
210D
111A
211D
112A
212B
113A
213C
114A
214D
115B
215C
116B
216D
117B
217C
118B
218D
119B
219C
120B
220D
121B
221C
122B
222D
123B
223C
124B
224D
125B
225C
126B
226D
127C
227D
128C
228D
129C
229D
130C
230D
131C
231D

NCS domain segments:

Component-ID: _ / Refine code: _

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11GLNGLNASNASNAA27 - 18315 - 171
21GLNGLNASNASNBB27 - 18315 - 171
12VALVALMETMETAA186 - 244174 - 232
22VALVALMETMETBB186 - 244174 - 232
13VALVALGLYGLYAA251 - 266239 - 254
23VALVALGLYGLYBB251 - 266239 - 254
14TYRTYRPHEPHEAA270 - 315258 - 303
24TYRTYRPHEPHEBB270 - 315258 - 303
15GLUGLUPHEPHEAA320 - 384308 - 372
25GLUGLUPHEPHEBB320 - 384308 - 372
16ARGARGSERSERAA28 - 26416 - 252
26ARGARGSERSERCC28 - 26416 - 252
17TYRTYRPHEPHEAA271 - 315259 - 303
27TYRTYRPHEPHECC271 - 315259 - 303
18ALAALAILEILEAA319 - 387307 - 375
28ALAALAILEILECC319 - 387307 - 375
19GLNGLNVALVALAA27 - 24515 - 233
29GLNGLNVALVALDD27 - 24515 - 233
110ASPASPPHEPHEAA248 - 315236 - 303
210ASPASPPHEPHEDD248 - 315236 - 303
111GLUGLUILEILEAA320 - 387308 - 375
211GLUGLUILEILEDD320 - 387308 - 375
112PHEPHETYRTYRAA397 - 416385 - 404
212PHEPHETYRTYRBB397 - 416385 - 404
113VALVALTYRTYRAA394 - 415382 - 403
213VALVALTYRTYRCC394 - 415382 - 403
114VALVALTYRTYRAA394 - 415382 - 403
214VALVALTYRTYRDD394 - 415382 - 403
115ARGARGASNASNBB28 - 18316 - 171
215ARGARGASNASNCC28 - 18316 - 171
116GLNGLNASNASNBB27 - 18315 - 171
216GLNGLNASNASNDD27 - 18315 - 171
117VALVALMETMETBB186 - 244174 - 232
217VALVALMETMETCC186 - 244174 - 232
118VALVALMETMETBB186 - 244174 - 232
218VALVALMETMETDD186 - 244174 - 232
119VALVALSERSERBB251 - 264239 - 252
219VALVALSERSERCC251 - 264239 - 252
120VALVALGLYGLYBB251 - 266239 - 254
220VALVALGLYGLYDD251 - 266239 - 254
121TYRTYRPROPROBB271 - 316259 - 304
221TYRTYRPROPROCC271 - 316259 - 304
122TYRTYRPHEPHEBB270 - 315258 - 303
222TYRTYRPHEPHEDD270 - 315258 - 303
123GLUGLUPHEPHEBB320 - 384308 - 372
223GLUGLUPHEPHECC320 - 384308 - 372
124GLUGLUPHEPHEBB320 - 384308 - 372
224GLUGLUPHEPHEDD320 - 384308 - 372
125PHEPHETYRTYRBB397 - 415385 - 403
225PHEPHETYRTYRCC397 - 415385 - 403
126PHEPHETYRTYRBB397 - 415385 - 403
226PHEPHETYRTYRDD397 - 415385 - 403
127ARGARGVALVALCC28 - 24516 - 233
227ARGARGVALVALDD28 - 24516 - 233
128ASPASPSERSERCC248 - 264236 - 252
228ASPASPSERSERDD248 - 264236 - 252
129TYRTYRPHEPHECC271 - 315259 - 303
229TYRTYRPHEPHEDD271 - 315259 - 303
130GLUGLUILEILECC320 - 387308 - 375
230GLUGLUILEILEDD320 - 387308 - 375
131VALVALTYRTYRCC394 - 416382 - 404
231VALVALTYRTYRDD394 - 416382 - 404

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15
16
17
18
19
20
21
22
23
24
25
26
27
28
29
30
31

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Components

#1: Protein
Rho-associated protein kinase 2 / Rho kinase 2 / Rho-associated / coiled-coil-containing protein kinase 2 / coiled-coil-containing ...Rho kinase 2 / Rho-associated / coiled-coil-containing protein kinase 2 / coiled-coil-containing protein kinase II / ROCK-II / p164 ROCK-2


Mass: 46217.484 Da / Num. of mol.: 4 / Fragment: UNP residues 18-417 / Mutation: F270Y
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ROCK2, KIAA0619 / Production host: unidentified baculovirus
References: UniProt: O75116, non-specific serine/threonine protein kinase
#2: Chemical
ChemComp-O1V / 2-[(2S)-1-azabicyclo[2.2.2]octan-2-yl]-6-(5-methyl-1H-pyrazol-4-yl)thieno[3,2-d]pyrimidin-4(3H)-one


Mass: 341.431 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C17H19N5OS

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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: 4.09 Å3/Da / Density % sol: 69.93 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 5.2
Details: 0.8 M trisodium citrate, 0.1 M citrate, pH 5.2, Silver Bullets Bio B12 (0.025% thymidine-5'-triphosphate sodium salt, 0.025% alpha-ketoglutaric acid disodium salt, 0.025% 2-nitrophenyl beta- ...Details: 0.8 M trisodium citrate, 0.1 M citrate, pH 5.2, Silver Bullets Bio B12 (0.025% thymidine-5'-triphosphate sodium salt, 0.025% alpha-ketoglutaric acid disodium salt, 0.025% 2-nitrophenyl beta-D-galactopyranoside, 0.025% cis-aconitic acid, 0.002 M HEPES sodium, pH 6.8)

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 5.0.2 / Wavelength: 0.97648 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Nov 23, 2011
RadiationMonochromator: dual crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97648 Å / Relative weight: 1
ReflectionResolution: 3.3→50 Å / Num. obs: 42899 / % possible obs: 99.9 % / Redundancy: 4.2 % / Rmerge(I) obs: 0.147 / Χ2: 1.002 / Net I/σ(I): 5.9 / Num. measured all: 180093
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsΧ2Diffraction-ID% possible all
3.3-3.364.10.8920820.929199.6
3.36-3.424.20.83721480.961199.6
3.42-3.484.20.70521251.0381100
3.48-3.554.20.60821210.9961100
3.55-3.634.20.48721250.9991100
3.63-3.724.20.39521801.1121100
3.72-3.814.20.32321230.9851100
3.81-3.914.20.27521540.9941100
3.91-4.034.30.24721081.0091100
4.03-4.164.20.19221471.0121100
4.16-4.314.20.16621810.9871100
4.31-4.484.20.13521491.0041100
4.48-4.684.20.12521261.0011100
4.68-4.934.20.12321431.0021100
4.93-5.244.20.12221610.9971100
5.24-5.644.20.12121281.0251100
5.64-6.214.10.11721631.0131100
6.21-7.14.10.08321520.9851100
7.1-8.944.10.04521760.994199.7
8.94-504.20.03322070.9961100

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Processing

Software
NameVersionClassification
HKL-2000data scaling
REFMAC5.8.0238refinement
PDB_EXTRACT3.25data extraction
HKL-2000data reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 2F2U

2f2u


Resolution: 3.3→25 Å / Cor.coef. Fo:Fc: 0.929 / Cor.coef. Fo:Fc free: 0.916 / SU B: 53.731 / SU ML: 0.371 / SU R Cruickshank DPI: 0.4369 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.437
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED
RfactorNum. reflection% reflectionSelection details
Rfree0.2357 2150 5 %RANDOM
Rwork0.2058 ---
obs0.2073 40630 98.62 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso max: 217.72 Å2 / Biso mean: 87.372 Å2 / Biso min: 55.8 Å2
Baniso -1Baniso -2Baniso -3
1-4.35 Å20 Å25.36 Å2
2---7.03 Å20 Å2
3---1.3 Å2
Refinement stepCycle: final / Resolution: 3.3→25 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12282 0 96 0 12378
Biso mean--114.47 --
Num. residues----1512
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.01312695
X-RAY DIFFRACTIONr_bond_other_d0.0010.01711627
X-RAY DIFFRACTIONr_angle_refined_deg1.3271.65117166
X-RAY DIFFRACTIONr_angle_other_deg1.1421.58526959
X-RAY DIFFRACTIONr_dihedral_angle_1_deg8.0751495
X-RAY DIFFRACTIONr_dihedral_angle_2_deg32.25622.511697
X-RAY DIFFRACTIONr_dihedral_angle_3_deg20.25152195
X-RAY DIFFRACTIONr_dihedral_angle_4_deg23.2531575
X-RAY DIFFRACTIONr_chiral_restr0.0890.21557
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.0214089
X-RAY DIFFRACTIONr_gen_planes_other0.0020.022764
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A47780.09
12B47780.09
21A16690.1
22B16690.1
31A3340.23
32B3340.23
41A13960.09
42B13960.09
51A18550.08
52B18550.08
61A73340.07
62C73340.07
71A12900.07
72C12900.07
81A19290.1
82C19290.1
91A67390.09
92D67390.09
101A19380.14
102D19380.14
111A19240.08
112D19240.08
121A4960.09
122B4960.09
131A5240.04
132C5240.04
141A5060.1
142D5060.1
151B48050.08
152C48050.08
161B48590.09
162D48590.09
171B16700.09
172C16700.09
181B16900.08
182D16900.08
191B2900.24
192C2900.24
201B3370.2
202D3370.2
211B13030.08
212C13030.08
221B14180.06
222D14180.06
231B18650.09
232C18650.09
241B18500.08
242D18500.08
251B4610.08
252C4610.08
261B4500.08
262D4500.08
271C67410.09
272D67410.09
281C3530.2
282D3530.2
291C12800.07
292D12800.07
301C19110.1
302D19110.1
311C5400.11
312D5400.11
LS refinement shellResolution: 3.283→3.367 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.34 147 -
Rwork0.342 2518 -
all-2665 -
obs--85.28 %
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)
13.83651.63312.00092.27272.09342.94970.0285-0.0834-0.080.02720.0187-0.3599-0.43570.0924-0.04730.2805-0.0228-0.10440.02790.02880.145257.9447-16.369214.7198
23.2835-0.06580.19841.94980.34831.53030.00020.1645-0.0111-0.0284-0.10240.3563-0.2398-0.41480.10230.16250.022-0.08630.22920.02480.119830.4715-15.963411.1104
31.7171-1.55011.26952.5749-1.96165.1621-0.0505-0.0348-0.39460.37550.2135-0.24170.30490.1065-0.1630.47860.0278-0.14690.0567-0.11140.426754.0798-51.109415.6611
40.74150.2917-1.31321.78880.63973.82290.00010.11-0.0903-0.29730.0008-0.2903-0.0071-0.0248-0.00090.3576-0.05160.00130.2133-0.03520.094457.1378-49.2727-12.5873
51.84031.51941.39831.73822.04884.32310.01080.1287-0.3301-0.22660.0736-0.00440.20550.0919-0.08440.48840.1136-0.15170.06160.01980.375773.3484-52.397337.0658
60.70830.2128-0.90332.5037-0.70324.01150.1561-0.0379-0.08030.3205-0.10360.52320.0777-0.048-0.05250.2827-0.00270.01230.18630.05090.208167.2005-52.089563.9583
74.1714-1.56682.1131.937-2.35163.6352-0.10890.14240.173-0.04730.09610.1965-0.4991-0.03450.01280.4284-0.0647-0.12240.02730.03530.234171.1658-17.570739.8396
83.3670.65590.38822.4718-0.43751.49160.1193-0.1744-0.0819-0.123-0.2476-0.6879-0.20610.42850.12830.2205-0.0823-0.03980.3750.06820.235498.3732-18.854546.8356
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A27 - 173
2X-RAY DIFFRACTION2A174 - 417
3X-RAY DIFFRACTION3B27 - 173
4X-RAY DIFFRACTION4B174 - 417
5X-RAY DIFFRACTION5C28 - 173
6X-RAY DIFFRACTION6C174 - 416
7X-RAY DIFFRACTION7D26 - 173
8X-RAY DIFFRACTION8D174 - 416

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