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- PDB-2vfx: Structure of the Symmetric Mad2 Dimer -

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Basic information

Entry
Database: PDB / ID: 2vfx
TitleStructure of the Symmetric Mad2 Dimer
ComponentsMITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A
KeywordsCELL CYCLE / MAD2 / MAD1 / CDC2 / NUCLEUS / MITOSIS / ANAPHASE / CELL DIVISION / SPINDLE CHECKPOINT / ANAPHASE-PROMOTING COMPLEX
Function / homology
Function and homology information


mitotic spindle assembly checkpoint MAD1-MAD2 complex / Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components / mitotic checkpoint complex / positive regulation of mitotic cell cycle spindle assembly checkpoint / establishment of centrosome localization / Inactivation of APC/C via direct inhibition of the APC/C complex / APC/C:Cdc20 mediated degradation of mitotic proteins / nuclear pore nuclear basket / negative regulation of ubiquitin protein ligase activity / mitotic spindle assembly checkpoint signaling ...mitotic spindle assembly checkpoint MAD1-MAD2 complex / Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components / mitotic checkpoint complex / positive regulation of mitotic cell cycle spindle assembly checkpoint / establishment of centrosome localization / Inactivation of APC/C via direct inhibition of the APC/C complex / APC/C:Cdc20 mediated degradation of mitotic proteins / nuclear pore nuclear basket / negative regulation of ubiquitin protein ligase activity / mitotic spindle assembly checkpoint signaling / establishment of mitotic spindle orientation / mitotic sister chromatid segregation / negative regulation of mitotic cell cycle / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Resolution of Sister Chromatid Cohesion / APC-Cdc20 mediated degradation of Nek2A / RHO GTPases Activate Formins / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / negative regulation of protein catabolic process / mitotic spindle / kinetochore / spindle pole / Separation of Sister Chromatids / cell division / negative regulation of apoptotic process / perinuclear region of cytoplasm / protein homodimerization activity / nucleoplasm / identical protein binding / nucleus / cytosol / cytoplasm
Similarity search - Function
Cell Cycle, Spindle Assembly Checkpoint Protein; Chain A / HORMA domain / Mad2-like / HORMA domain / HORMA domain / HORMA domain profile. / HORMA domain superfamily / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Chem-PE3 / DI(HYDROXYETHYL)ETHER / Mitotic spindle assembly checkpoint protein MAD2A
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.95 Å
AuthorsYang, M. / Li, B. / Liu, C.-J. / Tomchick, D.R. / Machius, M. / Rizo, J. / Yu, H. / Luo, X.
CitationJournal: Plos Biol. / Year: 2008
Title: Insights Into MAD2 Regulation in the Spindle Checkpoint Revealed by the Crystal Structure of the Symmetric MAD2 Dimer.
Authors: Yang, M. / Li, B. / Liu, C.-J. / Tomchick, D.R. / Machius, M. / Rizo, J. / Yu, H. / Luo, X.
History
DepositionNov 5, 2007Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 18, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Jan 30, 2019Group: Data collection / Derived calculations ...Data collection / Derived calculations / Experimental preparation / Other
Category: exptl_crystal_grow / pdbx_database_proc ...exptl_crystal_grow / pdbx_database_proc / pdbx_database_status / pdbx_struct_special_symmetry
Item: _exptl_crystal_grow.method / _pdbx_database_status.recvd_author_approval
Revision 1.3May 8, 2019Group: Data collection / Experimental preparation / Category: exptl_crystal_grow / Item: _exptl_crystal_grow.temp
Revision 1.4Dec 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _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.ptnr1_symmetry / _pdbx_struct_conn_angle.ptnr3_auth_asym_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.ptnr3_symmetry / _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.ptnr1_symmetry / _struct_conn.ptnr2_auth_asym_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_conn.ptnr2_symmetry
Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A
B: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A
C: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A
D: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A
E: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A
F: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A
G: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A
H: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A
I: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A
J: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A
K: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A
L: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)288,68567
Polymers282,20112
Non-polymers6,48455
Water28,6621591
1
A: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,0026
Polymers23,5171
Non-polymers4855
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
2
B: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,3187
Polymers23,5171
Non-polymers8016
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
3
C: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,2826
Polymers23,5171
Non-polymers7655
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
4
D: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)23,6946
Polymers23,5171
Non-polymers1775
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
5
E: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,0738
Polymers23,5171
Non-polymers5567
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
6
F: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,2475
Polymers23,5171
Non-polymers7304
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
7
G: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,2114
Polymers23,5171
Non-polymers6953
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
8
H: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,1512
Polymers23,5171
Non-polymers6351
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
9
I: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)23,7656
Polymers23,5171
Non-polymers2485
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
10
J: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)23,6946
Polymers23,5171
Non-polymers1775
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
11
K: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,2475
Polymers23,5171
Non-polymers7304
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
12
L: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,0026
Polymers23,5171
Non-polymers4855
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
Unit cell
Length a, b, c (Å)109.337, 191.407, 154.307
Angle α, β, γ (deg.)90.00, 90.02, 90.00
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11A-1209-

CL

21G-1206-

MG

31K-1206-

MG

41G-2053-

HOH

51L-2051-

HOH

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Components

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Protein , 1 types, 12 molecules ABCDEFGHIJKL

#1: Protein
MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A / MITOTIC ARREST DEFICIENT 2 / MAD2-LIKE 1 / HSMAD2


Mass: 23516.725 Da / Num. of mol.: 12 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: MAD2-L13A / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): M15-PREP4 / References: UniProt: Q13257

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Non-polymers , 6 types, 1646 molecules

#2: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Mg
#3: Chemical...
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 37 / Source method: obtained synthetically / Formula: Cl
#4: Chemical ChemComp-PE4 / 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL / POLYETHYLENE GLYCOL PEG4000


Mass: 354.436 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C16H34O8 / Comment: precipitant*YM
#5: Chemical
ChemComp-PE3 / 3,6,9,12,15,18,21,24,27,30,33,36,39-TRIDECAOXAHENTETRACONTANE-1,41-DIOL / POLYETHYLENE GLYCOL


Mass: 634.751 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C28H58O15
#6: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H10O3
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1591 / Source method: isolated from a natural source / Formula: H2O

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Details

Compound detailsENGINEERED RESIDUE IN CHAIN A, LEU 13 TO ALA ENGINEERED RESIDUE IN CHAIN A, CYS 79 TO SER ...ENGINEERED RESIDUE IN CHAIN A, LEU 13 TO ALA ENGINEERED RESIDUE IN CHAIN A, CYS 79 TO SER ENGINEERED RESIDUE IN CHAIN A, CYS 106 TO SER ENGINEERED RESIDUE IN CHAIN B, LEU 13 TO ALA ENGINEERED RESIDUE IN CHAIN B, CYS 79 TO SER ENGINEERED RESIDUE IN CHAIN B, CYS 106 TO SER ENGINEERED RESIDUE IN CHAIN C, LEU 13 TO ALA ENGINEERED RESIDUE IN CHAIN C, CYS 79 TO SER ENGINEERED RESIDUE IN CHAIN C, CYS 106 TO SER ENGINEERED RESIDUE IN CHAIN D, LEU 13 TO ALA ENGINEERED RESIDUE IN CHAIN D, CYS 79 TO SER ENGINEERED RESIDUE IN CHAIN D, CYS 106 TO SER ENGINEERED RESIDUE IN CHAIN E, LEU 13 TO ALA ENGINEERED RESIDUE IN CHAIN E, CYS 79 TO SER ENGINEERED RESIDUE IN CHAIN E, CYS 106 TO SER ENGINEERED RESIDUE IN CHAIN F, LEU 13 TO ALA ENGINEERED RESIDUE IN CHAIN F, CYS 79 TO SER ENGINEERED RESIDUE IN CHAIN F, CYS 106 TO SER ENGINEERED RESIDUE IN CHAIN G, LEU 13 TO ALA ENGINEERED RESIDUE IN CHAIN G, CYS 79 TO SER ENGINEERED RESIDUE IN CHAIN G, CYS 106 TO SER ENGINEERED RESIDUE IN CHAIN H, LEU 13 TO ALA ENGINEERED RESIDUE IN CHAIN H, CYS 79 TO SER ENGINEERED RESIDUE IN CHAIN H, CYS 106 TO SER ENGINEERED RESIDUE IN CHAIN I, LEU 13 TO ALA ENGINEERED RESIDUE IN CHAIN I, CYS 79 TO SER ENGINEERED RESIDUE IN CHAIN I, CYS 106 TO SER ENGINEERED RESIDUE IN CHAIN J, LEU 13 TO ALA ENGINEERED RESIDUE IN CHAIN J, CYS 79 TO SER ENGINEERED RESIDUE IN CHAIN J, CYS 106 TO SER ENGINEERED RESIDUE IN CHAIN K, LEU 13 TO ALA ENGINEERED RESIDUE IN CHAIN K, CYS 79 TO SER ENGINEERED RESIDUE IN CHAIN K, CYS 106 TO SER ENGINEERED RESIDUE IN CHAIN L, LEU 13 TO ALA ENGINEERED RESIDUE IN CHAIN L, CYS 79 TO SER ENGINEERED RESIDUE IN CHAIN L, CYS 106 TO SER
Sequence detailsTHE FIRST GLYCINE IS PART OF THE CLONING LINKER. L13 HAS BEEN MUTATED TO A

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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: 2.9 Å3/Da / Density % sol: 57.1 % / Description: NONE
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8
Details: VAPOR DIFFUSION, HANGING DROP, 20 DEGREES C. 1 MICROLITER PROTEIN: 3 MG/ML IN 20 MM TRIS, PH 8.0, 50 MM NACL, 2 MM TCEP PLUS 1 MICROLITER RESERVOIR: 19% PEG2000, 16% GLYCEROL, 100 MM TRIS, PH 8.0, 0.3 M MGCL2

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.97929
DetectorType: ADSC CCD / Detector: CCD / Date: Aug 16, 2006
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97929 Å / Relative weight: 1
ReflectionResolution: 1.95→45.37 Å / Num. obs: 223558 / % possible obs: 97.7 % / Observed criterion σ(I): -3 / Redundancy: 2.9 % / Biso Wilson estimate: 23.5 Å2 / Rmerge(I) obs: 0.07 / Net I/σ(I): 14.9
Reflection shellResolution: 1.95→1.98 Å / Redundancy: 2.6 % / Rmerge(I) obs: 0.55 / Mean I/σ(I) obs: 1.6 / % possible all: 95.7

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Processing

Software
NameVersionClassification
REFMAC5.2.0005refinement
HKL-3000data reduction
HKL-3000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1KLQ

1klq


Resolution: 1.95→45 Å / Cor.coef. Fo:Fc: 0.957 / Cor.coef. Fo:Fc free: 0.937 / SU B: 7.407 / SU ML: 0.115 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.165 / ESU R Free: 0.153 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.247 2700 1.2 %RANDOM
Rwork0.208 ---
obs0.209 220725 97.3 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 25.39 Å2
Baniso -1Baniso -2Baniso -3
1-0.81 Å20 Å20.2 Å2
2---0.83 Å20 Å2
3---0.02 Å2
Refinement stepCycle: LAST / Resolution: 1.95→45 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms19613 0 151 1591 21355
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.02220370
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.5011.97127614
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg2.00852493
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.02224.677913
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.773153744
X-RAY DIFFRACTIONr_dihedral_angle_4_deg18.85715122
X-RAY DIFFRACTIONr_chiral_restr0.0960.23241
X-RAY DIFFRACTIONr_gen_planes_refined0.0090.0217410
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.1990.28407
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3060.214075
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1390.21462
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1710.2554
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2110.2166
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.7061.512843
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.156220329
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it1.78838629
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it2.8774.57285
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
LS refinement shellResolution: 1.95→2 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.307 189
Rwork0.284 15243
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)
12.03120.1478-0.1971.2883-0.22391.184-0.0382-0.0986-0.19580.1575-0.01280.00340.178-0.01720.0510.05830.0165-0.0042-0.05210.016-0.0617111.45860.300194.3765
21.50970.5672-0.32381.62030.1181.2899-0.06910.099-0.116-0.09960.0368-0.1747-0.02020.1210.0322-0.0911-0.00880.023-0.0931-0.0213-0.09670.2582-23.950659.7361
32.32930.2889-0.2261.4034-0.28811.19280.0202-0.1502-0.23660.1721-0.0515-0.0230.1536-0.01540.0313-0.01680.0017-0.0074-0.09280.0224-0.1121111.47-3.701317.1909
41.14540.3433-0.36232.43870.02491.5067-0.0096-0.04510.09420.15910.03670.2031-0.0897-0.0891-0.027-0.10520.00620.0207-0.08850.0044-0.104790.705227.738593.8832
51.07530.31010.28672.1035-0.09321.4607-0.0059-0.0387-0.10660.19750.0312-0.18440.05040.0812-0.0254-0.07350-0.026-0.09640.004-0.094972.9525-20.099294.2212
62.05390.0820.16861.25820.17841.3147-0.0215-0.08630.17680.1496-0.0066-0.0189-0.19950.0170.0281-0.02480.01770.0035-0.1143-0.0166-0.112452.52213.63817.2114
71.70320.49510.28381.5982-0.17851.4231-0.04880.11570.1168-0.11260.02980.18270.0159-0.1320.019-0.0924-0.0132-0.0275-0.09650.0209-0.099393.720831.86359.7178
82.18450.25060.11381.44250.25881.19110.03-0.14420.22230.1645-0.05770.008-0.12790.00520.02770.0022-0.00270.0056-0.1027-0.023-0.116552.49927.644494.3547
91.14030.265-0.30282.28210.07661.4249-0.0002-0.02340.09310.17870.020.1715-0.041-0.1052-0.0198-0.1182-0.00160.0274-0.0952-0.0055-0.102390.746523.729316.737
101.15250.40620.27322.3781-0.03091.493-0.0105-0.0397-0.1210.16610.0387-0.1850.07270.094-0.0283-0.11960.0073-0.0268-0.0926-0.0054-0.095473.3241-23.831216.6369
111.5050.4897-0.21751.48690.05431.5812-0.05810.1251-0.0922-0.13110.0405-0.1953-0.03190.12670.0176-0.0595-0.01730.0354-0.04-0.0256-0.033370.3707-27.6241-17.6712
121.67790.51660.36411.7632-0.11461.3736-0.0670.10590.1167-0.09940.03090.1544-0.0016-0.11620.0361-0.0683-0.0099-0.0233-0.04240.021-0.043893.750727.8788-17.4612
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A10 - 205
2X-RAY DIFFRACTION2B10 - 205
3X-RAY DIFFRACTION3C10 - 205
4X-RAY DIFFRACTION4D10 - 205
5X-RAY DIFFRACTION5E10 - 205
6X-RAY DIFFRACTION6F10 - 205
7X-RAY DIFFRACTION7G10 - 205
8X-RAY DIFFRACTION8H10 - 205
9X-RAY DIFFRACTION9I10 - 205
10X-RAY DIFFRACTION10J10 - 205
11X-RAY DIFFRACTION11K10 - 205
12X-RAY DIFFRACTION12L10 - 205

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