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- PDB-7cjb: VHL recognizes hydroxyproline in RIPK1 -

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Basic information

Entry
Database: PDB / ID: 7cjb
TitleVHL recognizes hydroxyproline in RIPK1
Components
  • Elongin-B
  • Elongin-C
  • THR-LEU-TYR-TYR-MET-ALA-PRO-GLU-HIS-LEU-ASN-ASP-VAL-ASN-ALA
  • von Hippel-Lindau disease tumor suppressor
KeywordsAPOPTOSIS / hydroxyproline / VHL / RIPK1 / inflammation
Function / homology
Function and homology information


: / ripoptosome assembly / positive regulation of miRNA processing / positive regulation of interleukin-6-mediated signaling pathway / ripoptosome assembly involved in necroptotic process / death domain binding / ripoptosome / Defective RIPK1-mediated regulated necrosis / TRIF-mediated programmed cell death / Microbial modulation of RIPK1-mediated regulated necrosis ...: / ripoptosome assembly / positive regulation of miRNA processing / positive regulation of interleukin-6-mediated signaling pathway / ripoptosome assembly involved in necroptotic process / death domain binding / ripoptosome / Defective RIPK1-mediated regulated necrosis / TRIF-mediated programmed cell death / Microbial modulation of RIPK1-mediated regulated necrosis / Regulation by c-FLIP / CASP8 activity is inhibited / Dimerization of procaspase-8 / TLR3-mediated TICAM1-dependent programmed cell death / TNF signaling / regulation of cellular response to hypoxia / Caspase activation via Death Receptors in the presence of ligand / programmed necrotic cell death / positive regulation of macrophage differentiation / SARS-CoV-1-mediated effects on programmed cell death / T cell apoptotic process / necroptotic signaling pathway / peptidyl-serine autophosphorylation / RHOBTB3 ATPase cycle / negative regulation of receptor signaling pathway via JAK-STAT / NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10 / death-inducing signaling complex / positive regulation of necroptotic process / RIP-mediated NFkB activation via ZBP1 / negative regulation of necroptotic process / JUN kinase kinase kinase activity / target-directed miRNA degradation / transcription elongation factor activity / VCB complex / elongin complex / positive regulation of tumor necrosis factor-mediated signaling pathway / death receptor binding / positive regulation of programmed cell death / positive regulation of extrinsic apoptotic signaling pathway / Replication of the SARS-CoV-1 genome / positive regulation of programmed necrotic cell death / TNFR1-induced proapoptotic signaling / Cul5-RING ubiquitin ligase complex / RIPK1-mediated regulated necrosis / TRP channels / intracellular membraneless organelle / Cul2-RING ubiquitin ligase complex / SUMOylation of ubiquitinylation proteins / necroptotic process / negative regulation of transcription elongation by RNA polymerase II / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / positive regulation of execution phase of apoptosis / response to tumor necrosis factor / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / negative regulation of extrinsic apoptotic signaling pathway in absence of ligand / Tat-mediated elongation of the HIV-1 transcript / ubiquitin-like ligase-substrate adaptor activity / Formation of HIV-1 elongation complex containing HIV-1 Tat / negative regulation of signal transduction / Formation of HIV elongation complex in the absence of HIV Tat / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / tumor necrosis factor-mediated signaling pathway / extrinsic apoptotic signaling pathway / negative regulation of canonical NF-kappaB signal transduction / negative regulation of TORC1 signaling / signaling adaptor activity / protein serine/threonine kinase binding / RNA Polymerase II Pre-transcription Events / negative regulation of autophagy / TICAM1, RIP1-mediated IKK complex recruitment / IKK complex recruitment mediated by RIP1 / transcription corepressor binding / TNFR1-induced NF-kappa-B signaling pathway / positive regulation of interleukin-8 production / negative regulation of extrinsic apoptotic signaling pathway / positive regulation of cell differentiation / TP53 Regulates Transcription of DNA Repair Genes / transcription initiation at RNA polymerase II promoter / positive regulation of JNK cascade / transcription elongation by RNA polymerase II / Regulation of TNFR1 signaling / protein catabolic process / Vif-mediated degradation of APOBEC3G / positive regulation of non-canonical NF-kappaB signal transduction / Inactivation of CSF3 (G-CSF) signaling / cell morphogenesis / cellular response to growth factor stimulus / Evasion by RSV of host interferon responses / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / Regulation of necroptotic cell death / cellular response to hydrogen peroxide / Regulation of expression of SLITs and ROBOs / positive regulation of inflammatory response / positive regulation of reactive oxygen species metabolic process / positive regulation of NF-kappaB transcription factor activity / ubiquitin-protein transferase activity / transcription corepressor activity
Similarity search - Function
RIP1, Death domain / von Hippel-Lindau disease tumour suppressor, beta/alpha domain / von Hippel-Lindau disease tumour suppressor, alpha domain / von Hippel-Lindau disease tumour suppressor, beta domain / VHL superfamily / von Hippel-Lindau disease tumour suppressor, alpha domain superfamily / von Hippel-Lindau disease tumour suppressor, beta domain superfamily / VHL beta domain / VHL box domain / Elongin B ...RIP1, Death domain / von Hippel-Lindau disease tumour suppressor, beta/alpha domain / von Hippel-Lindau disease tumour suppressor, alpha domain / von Hippel-Lindau disease tumour suppressor, beta domain / VHL superfamily / von Hippel-Lindau disease tumour suppressor, alpha domain superfamily / von Hippel-Lindau disease tumour suppressor, beta domain superfamily / VHL beta domain / VHL box domain / Elongin B / Death domain profile. / DEATH domain, found in proteins involved in cell death (apoptosis). / Death domain / Death domain / : / Death-like domain superfamily / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / Ubiquitin-like (UB roll) / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Serine-threonine/tyrosine-protein kinase, catalytic domain / Protein tyrosine and serine/threonine kinase / Ubiquitin-like domain superfamily / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Serine/Threonine protein kinases, catalytic domain / Roll / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / Alpha Beta
Similarity search - Domain/homology
von Hippel-Lindau disease tumor suppressor / Receptor-interacting serine/threonine-protein kinase 1 / Elongin-B
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.8 Å
AuthorsLiu, J. / Wang, Y. / Pan, L.
Funding support China, 2items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)31500597 China
National Natural Science Foundation of China (NSFC)21621002 China
CitationJournal: To Be Published
Title: VHL recognizes hydroxyproline in RIPK1
Authors: Liu, J. / Wang, Y. / Pan, L.
History
DepositionJul 9, 2020Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jul 14, 2021Provider: repository / Type: Initial release
Revision 1.1Nov 29, 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: von Hippel-Lindau disease tumor suppressor
B: Elongin-B
C: Elongin-C
D: THR-LEU-TYR-TYR-MET-ALA-PRO-GLU-HIS-LEU-ASN-ASP-VAL-ASN-ALA
E: von Hippel-Lindau disease tumor suppressor
F: Elongin-B
G: Elongin-C
H: THR-LEU-TYR-TYR-MET-ALA-PRO-GLU-HIS-LEU-ASN-ASP-VAL-ASN-ALA
I: von Hippel-Lindau disease tumor suppressor
J: Elongin-B
K: Elongin-C
L: THR-LEU-TYR-TYR-MET-ALA-PRO-GLU-HIS-LEU-ASN-ASP-VAL-ASN-ALA
M: von Hippel-Lindau disease tumor suppressor
N: Elongin-B
O: Elongin-C
P: THR-LEU-TYR-TYR-MET-ALA-PRO-GLU-HIS-LEU-ASN-ASP-VAL-ASN-ALA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)180,31618
Polymers180,13116
Non-polymers1842
Water00
1
A: von Hippel-Lindau disease tumor suppressor
B: Elongin-B
C: Elongin-C
D: THR-LEU-TYR-TYR-MET-ALA-PRO-GLU-HIS-LEU-ASN-ASP-VAL-ASN-ALA


Theoretical massNumber of molelcules
Total (without water)45,0334
Polymers45,0334
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5880 Å2
ΔGint-44 kcal/mol
Surface area17460 Å2
MethodPISA
2
E: von Hippel-Lindau disease tumor suppressor
F: Elongin-B
G: Elongin-C
H: THR-LEU-TYR-TYR-MET-ALA-PRO-GLU-HIS-LEU-ASN-ASP-VAL-ASN-ALA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,1255
Polymers45,0334
Non-polymers921
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5920 Å2
ΔGint-45 kcal/mol
Surface area17540 Å2
MethodPISA
3
I: von Hippel-Lindau disease tumor suppressor
J: Elongin-B
K: Elongin-C
L: THR-LEU-TYR-TYR-MET-ALA-PRO-GLU-HIS-LEU-ASN-ASP-VAL-ASN-ALA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,1255
Polymers45,0334
Non-polymers921
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6160 Å2
ΔGint-46 kcal/mol
Surface area17340 Å2
MethodPISA
4
M: von Hippel-Lindau disease tumor suppressor
N: Elongin-B
O: Elongin-C
P: THR-LEU-TYR-TYR-MET-ALA-PRO-GLU-HIS-LEU-ASN-ASP-VAL-ASN-ALA


Theoretical massNumber of molelcules
Total (without water)45,0334
Polymers45,0334
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5700 Å2
ΔGint-43 kcal/mol
Surface area17150 Å2
MethodPISA
Unit cell
Length a, b, c (Å)94.831, 94.831, 361.605
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number91
Space group name H-MP4122
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21E
12A
22I
13A
23M
14B
24F
15B
25J
16B
26N
17C
27G
18C
28K
19C
29O
110E
210I
111E
211M
112F
212J
113F
213N
114G
214K
115G
215O
116I
216M
117J
217N
118K
218O

NCS domain segments:

Refine code: _

Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111ARGARGARGARGAA60 - 20510 - 155
221ARGARGARGARGEE60 - 20510 - 155
132PROPROARGARGAA61 - 20511 - 155
242PROPROARGARGII61 - 20511 - 155
153PROPROARGARGAA61 - 20511 - 155
263PROPROARGARGMM61 - 20511 - 155
174SERSERPROPROBB0 - 1054 - 109
284SERSERPROPROFF0 - 1054 - 109
195METMETLYSLYSBB1 - 1045 - 108
2105METMETLYSLYSJJ1 - 1045 - 108
1116ASPASPLYSLYSBB2 - 1046 - 108
2126ASPASPLYSLYSNN2 - 1046 - 108
1137SERSERCYSCYSCC16 - 1124 - 100
2147SERSERCYSCYSGG16 - 1124 - 100
1158GLYGLYCYSCYSCC15 - 1123 - 100
2168GLYGLYCYSCYSKK15 - 1123 - 100
1179SERSERCYSCYSCC16 - 1124 - 100
2189SERSERCYSCYSOO16 - 1124 - 100
11910PROPROILEILEEE61 - 20611 - 156
22010PROPROILEILEII61 - 20611 - 156
12111PROPROILEILEEE61 - 20611 - 156
22211PROPROILEILEMM61 - 20611 - 156
12312METMETPROPROFF1 - 1055 - 109
22412METMETPROPROJJ1 - 1055 - 109
12513ASPASPPROPROFF2 - 1056 - 109
22613ASPASPPROPRONN2 - 1056 - 109
12714SERSERASPASPGG16 - 1114 - 99
22814SERSERASPASPKK16 - 1114 - 99
12915SERSERCYSCYSGG16 - 1124 - 100
23015SERSERCYSCYSOO16 - 1124 - 100
13116PROPROALAALAII61 - 20711 - 157
23216PROPROALAALAMM61 - 20711 - 157
13317ASPASPLYSLYSJJ2 - 1046 - 108
23417ASPASPLYSLYSNN2 - 1046 - 108
13518SERSERASPASPKK16 - 1114 - 99
23618SERSERASPASPOO16 - 1114 - 99

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15
16
17
18

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Components

#1: Protein
von Hippel-Lindau disease tumor suppressor / Protein G7 / pVHL


Mass: 18725.262 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: VHL / Production host: Escherichia coli (E. coli) / References: UniProt: P40337
#2: Protein
Elongin-B / EloB / Elongin 18 kDa subunit / RNA polymerase II transcription factor SIII subunit B / SIII p18 / ...EloB / Elongin 18 kDa subunit / RNA polymerase II transcription factor SIII subunit B / SIII p18 / Transcription elongation factor B polypeptide 2


Mass: 13397.948 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ELOB, TCEB2 / Production host: Escherichia coli (E. coli) / References: UniProt: Q15370
#3: Protein
Elongin-C


Mass: 11141.717 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli)
#4: Protein/peptide
THR-LEU-TYR-TYR-MET-ALA-PRO-GLU-HIS-LEU-ASN-ASP-VAL-ASN-ALA / 15-mer peptide from Receptor-interacting serine/threonine-protein kinase 1


Mass: 1767.933 Da / Num. of mol.: 4 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human)
References: UniProt: Q13546, non-specific serine/threonine protein kinase
#5: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
Has ligand of interestY

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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: 2.26 Å3/Da / Density % sol: 45.51 %
Description: The entry contains friedel pairs in F_plus/minus columns and I_plus/minus columns
Crystal growTemperature: 289 K / Method: evaporation / pH: 6.5
Details: sodium cacodylate pH 6.5, 100 mM magnesium acetate, 15%(w/v) PEG 6000

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL17U1 / Wavelength: 0.97949 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jan 19, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97949 Å / Relative weight: 1
ReflectionResolution: 2.8→50 Å / Num. obs: 34589 / % possible obs: 95.3 % / Redundancy: 8.2 % / Rmerge(I) obs: 0.137 / Rpim(I) all: 0.048 / Rrim(I) all: 0.146 / Χ2: 0.977 / Net I/σ(I): 6.7 / Num. measured all: 609253
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allΧ2% possible all
2.8-2.858.41.76637640.5440.6251.8810.89597.8
2.85-2.98.41.38737570.6620.4931.4780.91996.3
2.9-2.968.31.06437110.7340.3791.1340.995.2
2.96-3.028.20.97437150.7360.3491.0390.90896.9
3.02-3.088.20.7837270.8120.280.8320.93494.5
3.08-3.158.10.71736880.840.260.7660.9294.3
3.15-3.238.10.58636410.9080.2120.6260.91394.6
3.23-3.328.10.40935980.9380.1470.4370.93592.1
3.32-3.427.80.36836220.9510.1340.3940.94392.6
3.42-3.537.40.31636600.9530.1190.3390.97592.7
3.53-3.656.70.25435010.9530.1010.2750.95990.5
3.65-3.87.60.18136850.9840.0670.1941.02494.8
3.8-3.978.10.14837440.9920.0520.1571.06496
3.97-4.188.10.1237080.9980.0420.1281.07895.5
4.18-4.448.10.09537150.9990.0330.1011.11295.3
4.44-4.7980.08637370.9970.030.0911.09995.3
4.79-5.2780.08337150.9970.0290.0881.00395.1
5.27-6.0380.08437650.9970.0290.090.96596.8
6.03-7.598.10.07138600.9980.0250.0760.97698.7
7.59-50120.05339720.9990.0160.0561.00399.9

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
REFMAC5.8.0257refinement
DENZOdata reduction
SCALEPACKdata scaling
PHASERphasing
PDB_EXTRACT3.25data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4AJY

4ajy


Resolution: 2.8→47.06 Å / Cor.coef. Fo:Fc: 0.931 / Cor.coef. Fo:Fc free: 0.901 / SU B: 39.806 / SU ML: 0.335 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.44 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: U VALUES : WITH TLS ADDED HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT. The entry contains friedel pairs in F_plus/minus columns and I_plus/minus columns
RfactorNum. reflection% reflectionSelection details
Rfree0.2594 1783 4.9 %RANDOM
Rwork0.2199 ---
obs0.2219 34589 86.92 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 145.12 Å2 / Biso mean: 51.478 Å2 / Biso min: 15.49 Å2
Baniso -1Baniso -2Baniso -3
1--0.38 Å20 Å20 Å2
2---0.38 Å20 Å2
3---0.76 Å2
Refinement stepCycle: final / Resolution: 2.8→47.06 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11185 0 12 0 11197
Biso mean--58.71 --
Num. residues----1392
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.01211462
X-RAY DIFFRACTIONr_angle_refined_deg1.6791.65315560
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.80951373
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.1121.085627
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.256151958
X-RAY DIFFRACTIONr_dihedral_angle_4_deg22.79615100
X-RAY DIFFRACTIONr_chiral_restr0.1260.21495
X-RAY DIFFRACTIONr_gen_planes_refined0.0090.028877
Refine LS restraints NCS

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

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A46070.1
12E46070.1
21A45870.08
22I45870.08
31A46240.08
32M46240.08
41B28530.08
42F28530.08
51B30900.08
52J30900.08
61B30560.08
62N30560.08
71C26770.09
72G26770.09
81C26950.08
82K26950.08
91C26370.09
92O26370.09
101E45860.11
102I45860.11
111E45060.11
112M45060.11
121F28040.1
122J28040.1
131F27510.1
132N27510.1
141G26430.08
142K26430.08
151G26180.09
152O26180.09
161I46300.09
162M46300.09
171J30420.08
172N30420.08
181K26610.07
182O26610.07
LS refinement shellResolution: 2.801→2.874 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.363 65 -
Rwork0.332 1165 -
all-1230 -
obs--40.61 %
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)
12.68740.9091.42156.6743.64744.8708-0.0361-0.3256-0.31940.4129-0.0089-0.02620.3125-0.10330.04490.19120.01630.13420.04130.04440.137-39.6758-29.8856-8.1711
26.35571.6312-3.23683.0589-0.65645.9378-0.08040.4765-0.2327-0.5269-0.03590.2249-0.0429-0.11320.11630.128-0.0044-0.02550.0748-0.05910.0621-30.1704-45.758-43.032
33.643-0.4363-1.44647.15650.28794.830.0005-0.0897-0.37260.3412-0.0658-0.13740.4850.27080.06530.2195-0.01730.06530.0271-0.01580.0906-32.854-50.2556-26.1006
44.96220.7976-3.6686.4561-2.99843.6489-0.00920.0661-0.11670.2355-0.02140.1432-0.162-0.09810.03060.42120.0984-0.02320.34440.01950.3007-40.2101-11.98531.5738
53.19091.42891.31325.5782.74344.32520.096-0.3617-0.39120.4756-0.06820.0390.3884-0.1917-0.02780.1970.02570.12190.0550.0690.14947.8233-34.3214-7.9421
65.94311.3383-2.47344.777-1.67116.4524-0.02110.7261-0.2881-0.7964-0.0824-0.06560.54180.38990.10340.43120.09270.02280.3205-0.1630.208616.4703-48.99-42.2753
73.3013-1.0263-0.78187.5048-1.44544.21570.0791-0.0003-0.4762-0.2059-0.156-0.22160.60440.31960.07690.35010.02760.03710.1054-0.06940.208714.245-54.1665-26.0689
87.0448-2.51380.32956.37420.61820.27730.0807-0.76790.02170.265-0.02240.21350.0371-0.2712-0.05820.3091-0.0306-0.0210.36850.03160.29347.4587-17.20662.6673
96.3971.0817-1.91243.5731-0.8533.567-0.10060.27890.0973-0.1421-0.0426-0.15770.103-0.1740.14320.0170.0447-0.01890.2495-0.12470.088918.161-40.2429-82.324
103.71431.6451.44244.05992.72497.1866-0.1224-0.6170.11460.4493-0.0427-0.081-0.0922-0.40560.16510.1484-0.00270.00380.2782-0.11410.05530.6395-34.2122-47.6652
117.9119-1.5190.06293.2951-0.08824.97930.0410.33360.50820.01390.01370.2157-0.202-0.3848-0.05470.0386-0.06520.04160.2756-0.06220.1057-2.7132-35.5494-64.8649
125.9566-0.87162.65932.72420.80759.2849-0.08860.1147-0.099-0.1343-0.1362-0.16110.6270.86080.22480.2655-0.00720.10590.3017-0.03570.394136.2218-39.4644-91.7967
136.32450.8644-1.32543.5978-0.68312.3574-0.01790.31030.0756-0.2734-0.0646-0.04290.2063-0.35610.08250.1221-0.02590.00640.4166-0.08910.140413.87037.4859-82.4232
144.75981.68260.18224.8141.48446.20610.0259-0.87730.17110.6755-0.088-0.1019-0.2048-0.11290.06210.34090.0106-0.01720.65870.03180.1134-3.751112.1039-47.2923
157.1754-1.2121.04753.6344-0.0432.6852-0.26460.08820.2401-0.0260.26550.0963-0.1942-0.2616-0.00090.1258-0.09730.02960.5178-0.01860.0432-6.926811.3625-64.6834
166.28693.1208-5.11393.6205-3.84669.4268-0.01270.16020.4301-0.68060.286-0.30291.3631-0.0424-0.27330.4209-0.02710.07370.33110.02420.420631.61437.994-91.9658
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A60 - 206
2X-RAY DIFFRACTION2B0 - 105
3X-RAY DIFFRACTION3C15 - 112
4X-RAY DIFFRACTION4D190 - 199
5X-RAY DIFFRACTION5E59 - 207
6X-RAY DIFFRACTION6F0 - 105
7X-RAY DIFFRACTION7G16 - 112
8X-RAY DIFFRACTION8H191 - 197
9X-RAY DIFFRACTION9I61 - 207
10X-RAY DIFFRACTION10J1 - 105
11X-RAY DIFFRACTION11K14 - 112
12X-RAY DIFFRACTION12L190 - 198
13X-RAY DIFFRACTION13M61 - 207
14X-RAY DIFFRACTION14N2 - 105
15X-RAY DIFFRACTION15O16 - 112
16X-RAY DIFFRACTION16P191 - 197

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