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- PDB-5vk0: Crystal structure of human MDM2 in complex with a 12-mer lysine-c... -

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Basic information

Entry
Database: PDB / ID: 5vk0
TitleCrystal structure of human MDM2 in complex with a 12-mer lysine-cysteine side chain dithiocarbamate stapled peptide inhibitor PMI
Components
  • E3 ubiquitin-protein ligase Mdm2
  • Lysine-cysteine side chain dithiocarbamate stapled peptide inhibitor PMI
KeywordsLIGASE/LIGASE INHIBITOR / MDM2-PEPTIDE INHIBITOR COMPLEX / ONCOPROTEIN / HOST-VIRUS INTERACTION / LIGASE / METAL-BINDING / NUCLEUS / PHOSPHOPROTEIN / PROTO-ONCOGENE / UBL CONJUGATION PATHWAY / ZINC-FINGER / stapled peptide / LIGASE-LIGASE INHIBITOR complex
Function / homology
Function and homology information


cellular response to vitamin B1 / response to formaldehyde / response to water-immersion restraint stress / response to ether / traversing start control point of mitotic cell cycle / negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator / negative regulation of signal transduction by p53 class mediator / fibroblast activation / atrial septum development / receptor serine/threonine kinase binding ...cellular response to vitamin B1 / response to formaldehyde / response to water-immersion restraint stress / response to ether / traversing start control point of mitotic cell cycle / negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator / negative regulation of signal transduction by p53 class mediator / fibroblast activation / atrial septum development / receptor serine/threonine kinase binding / Trafficking of AMPA receptors / positive regulation of vascular associated smooth muscle cell migration / peroxisome proliferator activated receptor binding / response to iron ion / negative regulation of protein processing / SUMO transferase activity / response to steroid hormone / NEDD8 ligase activity / AKT phosphorylates targets in the cytosol / cellular response to peptide hormone stimulus / atrioventricular valve morphogenesis / ventricular septum development / endocardial cushion morphogenesis / cellular response to alkaloid / positive regulation of muscle cell differentiation / SUMOylation of ubiquitinylation proteins / blood vessel development / regulation of protein catabolic process / cardiac septum morphogenesis / Constitutive Signaling by AKT1 E17K in Cancer / negative regulation of DNA damage response, signal transduction by p53 class mediator / response to magnesium ion / protein sumoylation / ligase activity / SUMOylation of transcription factors / protein localization to nucleus / cellular response to actinomycin D / cellular response to UV-C / blood vessel remodeling / cellular response to estrogen stimulus / protein autoubiquitination / ribonucleoprotein complex binding / DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest / positive regulation of vascular associated smooth muscle cell proliferation / transcription repressor complex / NPAS4 regulates expression of target genes / regulation of heart rate / proteolysis involved in protein catabolic process / positive regulation of mitotic cell cycle / positive regulation of protein export from nucleus / response to cocaine / ubiquitin binding / Stabilization of p53 / Regulation of RUNX3 expression and activity / protein destabilization / RING-type E3 ubiquitin transferase / cellular response to gamma radiation / establishment of protein localization / Oncogene Induced Senescence / Regulation of TP53 Activity through Methylation / response to toxic substance / cellular response to hydrogen peroxide / cellular response to growth factor stimulus / protein polyubiquitination / ubiquitin-protein transferase activity / endocytic vesicle membrane / ubiquitin protein ligase activity / disordered domain specific binding / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Regulation of TP53 Degradation / negative regulation of neuron projection development / p53 binding / 5S rRNA binding / ubiquitin-dependent protein catabolic process / cellular response to hypoxia / proteasome-mediated ubiquitin-dependent protein catabolic process / regulation of gene expression / protein-containing complex assembly / Oxidative Stress Induced Senescence / Regulation of TP53 Activity through Phosphorylation / amyloid fibril formation / protein ubiquitination / regulation of cell cycle / Ub-specific processing proteases / response to xenobiotic stimulus / protein domain specific binding / response to antibiotic / negative regulation of DNA-templated transcription / apoptotic process / ubiquitin protein ligase binding / positive regulation of cell population proliferation / positive regulation of gene expression / nucleolus / negative regulation of apoptotic process / negative regulation of transcription by RNA polymerase II / enzyme binding / protein-containing complex / zinc ion binding / nucleoplasm / identical protein binding
Similarity search - Function
MDM2 / SWIB/MDM2 domain / E3 ubiquitin-protein ligase Mdm2 / MDM2, modified RING finger, HC subclass / p53 negative regulator Mdm2/Mdm4 / SWIB/MDM2 domain / SWIB/MDM2 domain / SWIB/MDM2 domain profile. / SWIB/MDM2 domain superfamily / Zn-finger in Ran binding protein and others ...MDM2 / SWIB/MDM2 domain / E3 ubiquitin-protein ligase Mdm2 / MDM2, modified RING finger, HC subclass / p53 negative regulator Mdm2/Mdm4 / SWIB/MDM2 domain / SWIB/MDM2 domain / SWIB/MDM2 domain profile. / SWIB/MDM2 domain superfamily / Zn-finger in Ran binding protein and others / Zinc finger, C3HC4 type (RING finger) / Zinc finger RanBP2 type profile. / Zinc finger RanBP2-type signature. / Zinc finger, RanBP2-type superfamily / Zinc finger, RanBP2-type / Zinc finger RING-type profile. / Zinc finger, RING-type / Zinc finger, RING/FYVE/PHD-type / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
E3 ubiquitin-protein ligase Mdm2
Similarity search - Component
Biological speciesHomo sapiens (human)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å
AuthorsTolbert, W.D. / Gohain, N. / Pazgier, M.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)R01AI116274 United States
CitationJournal: Chem Sci / Year: 2019
Title: Dithiocarbamate-inspired side chain stapling chemistry for peptide drug design.
Authors: Li, X. / Tolbert, W.D. / Hu, H.G. / Gohain, N. / Zou, Y. / Niu, F. / He, W.X. / Yuan, W. / Su, J.C. / Pazgier, M. / Lu, W.
History
DepositionApr 20, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 25, 2018Provider: repository / Type: Initial release
Revision 1.1Jan 30, 2019Group: Data collection / Database references / Source and taxonomy
Category: citation / citation_author / pdbx_entity_src_syn
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.title / _citation.year / _pdbx_entity_src_syn.ncbi_taxonomy_id / _pdbx_entity_src_syn.organism_scientific
Revision 1.2Mar 13, 2019Group: Data collection / Database references / Category: citation / citation_author / pdbx_database_proc
Item: _citation.journal_id_ISSN / _citation.journal_volume ..._citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.name
Revision 1.3Dec 11, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.4Oct 4, 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
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: E3 ubiquitin-protein ligase Mdm2
B: Lysine-cysteine side chain dithiocarbamate stapled peptide inhibitor PMI
C: E3 ubiquitin-protein ligase Mdm2
D: Lysine-cysteine side chain dithiocarbamate stapled peptide inhibitor PMI
E: E3 ubiquitin-protein ligase Mdm2
F: Lysine-cysteine side chain dithiocarbamate stapled peptide inhibitor PMI
G: E3 ubiquitin-protein ligase Mdm2
H: Lysine-cysteine side chain dithiocarbamate stapled peptide inhibitor PMI
I: E3 ubiquitin-protein ligase Mdm2
J: Lysine-cysteine side chain dithiocarbamate stapled peptide inhibitor PMI
K: E3 ubiquitin-protein ligase Mdm2
L: Lysine-cysteine side chain dithiocarbamate stapled peptide inhibitor PMI
M: E3 ubiquitin-protein ligase Mdm2
N: Lysine-cysteine side chain dithiocarbamate stapled peptide inhibitor PMI
O: E3 ubiquitin-protein ligase Mdm2
P: Lysine-cysteine side chain dithiocarbamate stapled peptide inhibitor PMI
Q: E3 ubiquitin-protein ligase Mdm2
R: Lysine-cysteine side chain dithiocarbamate stapled peptide inhibitor PMI
S: E3 ubiquitin-protein ligase Mdm2
T: Lysine-cysteine side chain dithiocarbamate stapled peptide inhibitor PMI
U: E3 ubiquitin-protein ligase Mdm2
V: Lysine-cysteine side chain dithiocarbamate stapled peptide inhibitor PMI
W: E3 ubiquitin-protein ligase Mdm2
X: Lysine-cysteine side chain dithiocarbamate stapled peptide inhibitor PMI
hetero molecules


Theoretical massNumber of molelcules
Total (without water)138,82326
Polymers138,75224
Non-polymers712
Water7,530418
1
A: E3 ubiquitin-protein ligase Mdm2
B: Lysine-cysteine side chain dithiocarbamate stapled peptide inhibitor PMI


Theoretical massNumber of molelcules
Total (without water)11,5632
Polymers11,5632
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1300 Å2
ΔGint-10 kcal/mol
Surface area6120 Å2
MethodPISA
2
C: E3 ubiquitin-protein ligase Mdm2
D: Lysine-cysteine side chain dithiocarbamate stapled peptide inhibitor PMI
hetero molecules


Theoretical massNumber of molelcules
Total (without water)11,5983
Polymers11,5632
Non-polymers351
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1390 Å2
ΔGint-19 kcal/mol
Surface area6090 Å2
MethodPISA
3
E: E3 ubiquitin-protein ligase Mdm2
F: Lysine-cysteine side chain dithiocarbamate stapled peptide inhibitor PMI


Theoretical massNumber of molelcules
Total (without water)11,5632
Polymers11,5632
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1320 Å2
ΔGint-8 kcal/mol
Surface area6200 Å2
MethodPISA
4
G: E3 ubiquitin-protein ligase Mdm2
H: Lysine-cysteine side chain dithiocarbamate stapled peptide inhibitor PMI


Theoretical massNumber of molelcules
Total (without water)11,5632
Polymers11,5632
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1320 Å2
ΔGint-10 kcal/mol
Surface area5880 Å2
MethodPISA
5
I: E3 ubiquitin-protein ligase Mdm2
J: Lysine-cysteine side chain dithiocarbamate stapled peptide inhibitor PMI


Theoretical massNumber of molelcules
Total (without water)11,5632
Polymers11,5632
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1320 Å2
ΔGint-11 kcal/mol
Surface area6050 Å2
MethodPISA
6
K: E3 ubiquitin-protein ligase Mdm2
L: Lysine-cysteine side chain dithiocarbamate stapled peptide inhibitor PMI


Theoretical massNumber of molelcules
Total (without water)11,5632
Polymers11,5632
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1430 Å2
ΔGint-10 kcal/mol
Surface area6150 Å2
MethodPISA
7
M: E3 ubiquitin-protein ligase Mdm2
N: Lysine-cysteine side chain dithiocarbamate stapled peptide inhibitor PMI


Theoretical massNumber of molelcules
Total (without water)11,5632
Polymers11,5632
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1380 Å2
ΔGint-10 kcal/mol
Surface area5810 Å2
MethodPISA
8
O: E3 ubiquitin-protein ligase Mdm2
P: Lysine-cysteine side chain dithiocarbamate stapled peptide inhibitor PMI


Theoretical massNumber of molelcules
Total (without water)11,5632
Polymers11,5632
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1260 Å2
ΔGint-10 kcal/mol
Surface area6180 Å2
MethodPISA
9
Q: E3 ubiquitin-protein ligase Mdm2
R: Lysine-cysteine side chain dithiocarbamate stapled peptide inhibitor PMI


Theoretical massNumber of molelcules
Total (without water)11,5632
Polymers11,5632
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1330 Å2
ΔGint-10 kcal/mol
Surface area5690 Å2
MethodPISA
10
S: E3 ubiquitin-protein ligase Mdm2
T: Lysine-cysteine side chain dithiocarbamate stapled peptide inhibitor PMI


Theoretical massNumber of molelcules
Total (without water)11,5632
Polymers11,5632
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1320 Å2
ΔGint-9 kcal/mol
Surface area6020 Å2
MethodPISA
11
U: E3 ubiquitin-protein ligase Mdm2
V: Lysine-cysteine side chain dithiocarbamate stapled peptide inhibitor PMI


Theoretical massNumber of molelcules
Total (without water)11,5632
Polymers11,5632
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1400 Å2
ΔGint-12 kcal/mol
Surface area5830 Å2
MethodPISA
12
W: E3 ubiquitin-protein ligase Mdm2
X: Lysine-cysteine side chain dithiocarbamate stapled peptide inhibitor PMI
hetero molecules


Theoretical massNumber of molelcules
Total (without water)11,5983
Polymers11,5632
Non-polymers351
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1380 Å2
ΔGint-18 kcal/mol
Surface area5950 Å2
MethodPISA
Unit cell
Length a, b, c (Å)90.838, 157.470, 196.650
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221

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Components

#1: Protein
E3 ubiquitin-protein ligase Mdm2 / Double minute 2 protein / Hdm2 / Oncoprotein Mdm2 / RING-type E3 ubiquitin transferase Mdm2 / p53- ...Double minute 2 protein / Hdm2 / Oncoprotein Mdm2 / RING-type E3 ubiquitin transferase Mdm2 / p53-binding protein Mdm2


Mass: 10044.889 Da / Num. of mol.: 12 / Fragment: residues 25-109 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human)
References: UniProt: Q00987, RING-type E3 ubiquitin transferase
#2: Protein/peptide
Lysine-cysteine side chain dithiocarbamate stapled peptide inhibitor PMI


Mass: 1517.791 Da / Num. of mol.: 12 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)
#3: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 418 / 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: 2.53 Å3/Da / Density % sol: 51.46 %
Crystal growTemperature: 294 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 1340 mM ammonium sulfate, 6.7% glycerol, 50 mM magnesium sulfate, 100 mM imidazole pH 6.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL12-2 / Wavelength: 0.97946 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Jan 15, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97946 Å / Relative weight: 1
Reflection twin
Crystal-IDIDOperatorDomain-IDFraction
11H, K, L10.338
111/2H+1/2K, 3/2H-1/2K, -L20.32
11-1/2H+1/2K, 3/2H+1/2K, -L30.343
ReflectionResolution: 1.8→50 Å / Num. obs: 123372 / % possible obs: 95.5 % / Redundancy: 3.4 % / Rmerge(I) obs: 0.076 / Net I/σ(I): 23.2
Reflection shellResolution: 1.8→1.83 Å / Redundancy: 3.4 % / Rmerge(I) obs: 0.299 / Mean I/σ(I) obs: 3 / Num. unique all: 4192 / % possible all: 97.9

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Processing

Software
NameVersionClassification
REFMAC5.8.0158refinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3EQS

3eqs


Resolution: 1.8→41.7 Å / Cor.coef. Fo:Fc: 0.94 / Cor.coef. Fo:Fc free: 0.924 / SU B: 3.755 / SU ML: 0.079 / Cross valid method: THROUGHOUT / ESU R: 0.028 / ESU R Free: 0.029 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.24656 6374 5.2 %RANDOM
Rwork0.19793 ---
obs0.20046 116968 95.21 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 26.736 Å2
Baniso -1Baniso -2Baniso -3
1-10.8 Å20 Å20 Å2
2--5.31 Å20 Å2
3----16.11 Å2
Refinement stepCycle: 1 / Resolution: 1.8→41.7 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9689 0 2 418 10109
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.020.029948
X-RAY DIFFRACTIONr_bond_other_d0.0030.029777
X-RAY DIFFRACTIONr_angle_refined_deg2.4951.99913252
X-RAY DIFFRACTIONr_angle_other_deg1.3723.00122567
X-RAY DIFFRACTIONr_dihedral_angle_1_deg9.27451118
X-RAY DIFFRACTIONr_dihedral_angle_2_deg43.17123.202406
X-RAY DIFFRACTIONr_dihedral_angle_3_deg20.576151872
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.4361548
X-RAY DIFFRACTIONr_chiral_restr0.1330.21504
X-RAY DIFFRACTIONr_gen_planes_refined0.0110.0210282
X-RAY DIFFRACTIONr_gen_planes_other0.0040.022042
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
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_it0.9761.9314661
X-RAY DIFFRACTIONr_mcbond_other0.9761.9314659
X-RAY DIFFRACTIONr_mcangle_it1.3482.8735676
X-RAY DIFFRACTIONr_mcangle_other1.3482.8735677
X-RAY DIFFRACTIONr_scbond_it0.8481.9865286
X-RAY DIFFRACTIONr_scbond_other0.8481.9865287
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other1.1842.9557575
X-RAY DIFFRACTIONr_long_range_B_refined3.09136.51441030
X-RAY DIFFRACTIONr_long_range_B_other3.09136.51441028
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.803→1.849 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.281 517 -
Rwork0.185 8459 -
obs--93.77 %
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)
10.6328-0.85750.05743.3814-0.3781.10280.03710.0415-0.05380.23540.01020.2453-0.02850.0554-0.04730.04440.00190.02340.0243-0.00710.0219-3.6307-20.1555-27.7916
20.8466-0.4677-0.07713.4754-0.21251.11890.03990.05940.00010.2031-0.01840.09430.02670.078-0.02140.02310.00410.00720.0147-0.00260.004718.7919.1983-27.8852
30.4218-0.1985-0.07542.66170.13381.0204-0.00220.0203-0.010.2022-0.02280.049-0.0762-0.03230.0250.05020.0121-0.00620.10010.00750.058539.7361-22.9086-27.1111
42.32210.2788-0.49310.69290.09362.03740.03660.14490.0425-0.2061-0.0956-0.1135-0.12950.07560.0590.07060.03310.03490.03730.02950.02726.693-33.2233-60.6782
51.9429-0.089-0.15181.9129-0.07561.8922-0.0239-0.1120.09460.2402-0.09810.1942-0.1487-0.06530.1220.0407-0.00570.01340.0153-0.0220.0354-4.24396.7174-37.9134
60.94620.1488-0.25431.42430.07131.573-0.0672-0.19380.03390.08610.046-0.007-0.0257-0.00330.02120.0906-0.01050.00230.09030.00650.122537.7255-13.2251-4.8078
70.6712-0.2696-0.32891.00950.02731.60430.0205-0.14180.06160.0591-0.0204-0.0141-0.04430.115-00.0773-0.028-0.00320.07280.00270.0957-7.847-12.4535-5.1783
81.01410.1670.46491.05440.34771.1291-0.00450.1047-0.0502-0.08680.02910.0368-0.0752-0.0455-0.02460.10630.0167-0.00190.09340.00390.087812.0286-26.55275.8769
92.3716-0.3921-0.66711.0573-0.13131.8551-0.0368-0.1819-0.10090.2110.02730.10840.0220.10410.00940.04520.00420.02060.01570.00760.012816.9104-35.4843-38.8081
101.0772-0.2099-0.0623.0328-0.03031.3374-0.02870.0484-0.02660.13650.03870.0935-0.0451-0.0623-0.010.02250.01520.00490.05960.00990.061417.417-62.887-26.642
111.3724-0.7227-0.10471.2111-0.11571.0098-0.0088-0.16540.00110.16330.01920.11560.0171-0.0472-0.01040.1135-0.02560.00590.0999-0.0050.119811.0818-52.3736-5.9983
122.61030.0618-0.10451.3953-0.35192.24470.0123-0.2350.07730.2639-0.0380.1035-0.0591-0.11340.02580.0502-0.00790.02130.03-0.01390.021139.62712.7405-38.68
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A25 - 109
2X-RAY DIFFRACTION2C25 - 109
3X-RAY DIFFRACTION3E26 - 108
4X-RAY DIFFRACTION4G25 - 109
5X-RAY DIFFRACTION5I26 - 109
6X-RAY DIFFRACTION6K27 - 109
7X-RAY DIFFRACTION7M25 - 109
8X-RAY DIFFRACTION8O26 - 108
9X-RAY DIFFRACTION9Q26 - 108
10X-RAY DIFFRACTION10S25 - 109
11X-RAY DIFFRACTION11U25 - 108
12X-RAY DIFFRACTION12W25 - 108

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