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- PDB-2zp9: The Nature of the TRAP:Anti-TRAP complex -

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Basic information

Entry
Database: PDB / ID: 2zp9
TitleThe Nature of the TRAP:Anti-TRAP complex
Components
  • Transcription attenuation protein mtrB
  • Tryptophan RNA-binding attenuator protein-inhibitory protein
KeywordsRNA BINDING PROTEIN/TRANSCRIPTION / PROTEIN-PROTEIN COMPLEX / TRANSCRIPTION / RNA-binding / Transcription regulation / RNA BINDING PROTEIN-TRANSCRIPTION COMPLEX
Function / homology
Function and homology information


DNA-templated transcription termination / regulation of DNA-templated transcription / RNA binding / identical protein binding / cytoplasm
Similarity search - Function
Alpha-Beta Plaits - #30 / Chaperone, DNAj Protein; Chain A / Chaperone, DNAj Protein; Chain A - #10 / Tryptophan RNA-binding attenuator protein inhibitory protein / Tryptophan RNA-binding attenuator protein inhibitory protein / Alpha-Beta Plaits / TRAP-like / Heat shock protein DnaJ, cysteine-rich domain superfamily / Transcription attenuation protein MtrB / Tryptophan RNA-binding attenuator protein domain ...Alpha-Beta Plaits - #30 / Chaperone, DNAj Protein; Chain A / Chaperone, DNAj Protein; Chain A - #10 / Tryptophan RNA-binding attenuator protein inhibitory protein / Tryptophan RNA-binding attenuator protein inhibitory protein / Alpha-Beta Plaits / TRAP-like / Heat shock protein DnaJ, cysteine-rich domain superfamily / Transcription attenuation protein MtrB / Tryptophan RNA-binding attenuator protein domain / Tryptophan RNA-binding attenuator protein / Tryptophan RNA-binding attenuator protein-like domain superfamily / Other non-globular / Special / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
TRYPTOPHAN / Tryptophan RNA-binding attenuator protein inhibitory protein / Transcription attenuation protein MtrB
Similarity search - Component
Biological speciesBacillus stearothermophilus (bacteria)
Bacillus subtilis (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / PHASER / Resolution: 3.2 Å
AuthorsWatanabe, M. / Heddle, J.G. / Unzai, S. / Akashi, S. / Park, S.Y. / Tame, J.R.H.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2009
Title: The nature of the TRAP-Anti-TRAP complex.
Authors: Watanabe, M. / Heddle, J.G. / Kikuchi, K. / Unzai, S. / Akashi, S. / Park, S.Y. / Tame, J.R.
History
DepositionJul 8, 2008Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Feb 3, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Refinement description / Version format compliance
Revision 1.2Mar 5, 2014Group: Database references
Revision 1.3Nov 1, 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_ncs_dom_lim / struct_ref_seq_dif / struct_site
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.end_auth_comp_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Transcription attenuation protein mtrB
B: Transcription attenuation protein mtrB
C: Tryptophan RNA-binding attenuator protein-inhibitory protein
D: Tryptophan RNA-binding attenuator protein-inhibitory protein
E: Tryptophan RNA-binding attenuator protein-inhibitory protein
F: Transcription attenuation protein mtrB
G: Transcription attenuation protein mtrB
H: Tryptophan RNA-binding attenuator protein-inhibitory protein
I: Tryptophan RNA-binding attenuator protein-inhibitory protein
J: Tryptophan RNA-binding attenuator protein-inhibitory protein
K: Transcription attenuation protein mtrB
L: Transcription attenuation protein mtrB
M: Tryptophan RNA-binding attenuator protein-inhibitory protein
N: Tryptophan RNA-binding attenuator protein-inhibitory protein
O: Tryptophan RNA-binding attenuator protein-inhibitory protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)104,98226
Polymers103,43015
Non-polymers1,55211
Water00
1
F: Transcription attenuation protein mtrB
G: Transcription attenuation protein mtrB
H: Tryptophan RNA-binding attenuator protein-inhibitory protein
I: Tryptophan RNA-binding attenuator protein-inhibitory protein
J: Tryptophan RNA-binding attenuator protein-inhibitory protein
K: Transcription attenuation protein mtrB
L: Transcription attenuation protein mtrB
M: Tryptophan RNA-binding attenuator protein-inhibitory protein
N: Tryptophan RNA-binding attenuator protein-inhibitory protein
O: Tryptophan RNA-binding attenuator protein-inhibitory protein
hetero molecules

F: Transcription attenuation protein mtrB
G: Transcription attenuation protein mtrB
H: Tryptophan RNA-binding attenuator protein-inhibitory protein
I: Tryptophan RNA-binding attenuator protein-inhibitory protein
J: Tryptophan RNA-binding attenuator protein-inhibitory protein
K: Transcription attenuation protein mtrB
L: Transcription attenuation protein mtrB
M: Tryptophan RNA-binding attenuator protein-inhibitory protein
N: Tryptophan RNA-binding attenuator protein-inhibitory protein
O: Tryptophan RNA-binding attenuator protein-inhibitory protein
hetero molecules

F: Transcription attenuation protein mtrB
G: Transcription attenuation protein mtrB
H: Tryptophan RNA-binding attenuator protein-inhibitory protein
I: Tryptophan RNA-binding attenuator protein-inhibitory protein
J: Tryptophan RNA-binding attenuator protein-inhibitory protein
K: Transcription attenuation protein mtrB
L: Transcription attenuation protein mtrB
M: Tryptophan RNA-binding attenuator protein-inhibitory protein
N: Tryptophan RNA-binding attenuator protein-inhibitory protein
O: Tryptophan RNA-binding attenuator protein-inhibitory protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)209,70248
Polymers206,85930
Non-polymers2,84318
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_565-y,x-y+1,z1
crystal symmetry operation3_455-x+y-1,-x,z1
Buried area53730 Å2
ΔGint-288 kcal/mol
Surface area61690 Å2
MethodPISA
2
A: Transcription attenuation protein mtrB
B: Transcription attenuation protein mtrB
C: Tryptophan RNA-binding attenuator protein-inhibitory protein
D: Tryptophan RNA-binding attenuator protein-inhibitory protein
E: Tryptophan RNA-binding attenuator protein-inhibitory protein
hetero molecules
x 6


Theoretical massNumber of molelcules
Total (without water)210,48760
Polymers206,85930
Non-polymers3,62830
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-y,x-y,z1
crystal symmetry operation3_555-x+y,-x,z1
crystal symmetry operation4_555-x,-y,z1
crystal symmetry operation5_555y,-x+y,z1
crystal symmetry operation6_555x-y,x,z1
Buried area60010 Å2
ΔGint-318 kcal/mol
Surface area66700 Å2
MethodPISA
Unit cell
Length a, b, c (Å)197.134, 197.135, 56.658
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number168
Space group name H-MP6
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31F
41G
51K
61L
12C
22D
32E
42H
52I
62J
72M
82O
13C
23D
33E
43H
53I
63J
73M
83O
14C
24D
34E
44H
54I
64J
74M
84N
94O

NCS domain segments:

Component-ID: 1 / Refine code: 3

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11ASPASPTHRTHRAA8 - 656 - 63
21ASPASPTHRTHRBB8 - 656 - 63
31ASPASPTHRTHRFF8 - 656 - 63
41ASPASPTHRTHRGG8 - 656 - 63
51ASPASPTHRTHRKK8 - 656 - 63
61ASPASPTHRTHRLL8 - 656 - 63
12VALVALCYSCYSCC2 - 122 - 12
22VALVALCYSCYSDD2 - 122 - 12
32VALVALCYSCYSEE2 - 122 - 12
42VALVALCYSCYSHH2 - 122 - 12
52THRTHRCYSCYSII5 - 125 - 12
62VALVALCYSCYSJJ2 - 122 - 12
72VALVALCYSCYSMM2 - 122 - 12
82VALVALCYSCYSOO2 - 122 - 12
13PROPROLYSLYSCC13 - 3213 - 32
23PROPROLYSLYSDD13 - 3213 - 32
33PROPROLYSLYSEE13 - 3213 - 32
43PROPROLYSLYSHH13 - 3213 - 32
53PROPROLYSLYSII13 - 3213 - 32
63PROPROLYSLYSJJ13 - 3213 - 32
73PROPROLYSLYSMM13 - 3213 - 32
83PROPROLYSLYSOO13 - 3213 - 32
14GLYGLYASNASNCC33 - 5233 - 52
24GLYGLYASNASNDD33 - 5233 - 52
34GLYGLYASNASNEE33 - 5233 - 52
44GLYGLYLEULEUHH33 - 5133 - 51
54GLYGLYASNASNII33 - 5233 - 52
64GLYGLYLEULEUJJ33 - 5133 - 51
74GLYGLYLEULEUMM33 - 5133 - 51
84LEULEUASNASNNN36 - 5236 - 52
94GLYGLYLEULEUOO33 - 5133 - 51

NCS ensembles :
ID
1
2
3
4
DetailsTHIS PDB FILE SHOWS THE COMPLEX BETWEEN MUTANT BACILLUS STEAROTHERMOPHILUS TRAP AND BACILLUS SUBTILIS ANTI-TRAP. THE TRAP CARRIES THREE SUBUNITS ON A SINGLE POLYPEPTIDE. THESE TRIMER CHAINS ASSOCIATE TO FORM A 12-MER RING IN SOLUTION INSTEAD OF THE USUAL 11-MER FORM. THE WILD-TYPE PROTEIN CAN ALSO FORM A 12-MER RING. MUTATIONAL ANALYSIS INDICATES THE TRAP:ANTI-TRAP INTERFACE TO BE THE SAME AS THAT MADE BY WILD-TYPE TRAP IN BOTH THE 11-MER AND 12-MER FORMS. THERE IS NO ELECTRON DENSITY INDICATING THE POSITION OF THE PEPTIDE LINKERS BETWEEN TRAP SUBUNITS IN THIS STRUCTURE. IT HAS PREVIOUSLY BEEN SHOWN THAT THESE LINKERS PASS THROUGH THE CENTRAL HOLE AND DO NOT INTERFERE WITH ANTI-TRAP BINDING. SEE PDB 2ZCZ. ONE COPY OF ANTI-TRAP (CHAIN N) IS VERY INCOMPLETE IN THIS MODEL. A BETTER MODEL FOR THE TRAP:ANTI-TRAP COMPLEX WAS OBTAINED WITH WILD-TYPE TRAP. SEE PDB 2ZP8. THE OVERALL GEOMETRY FOR THIS MODEL AND 2ZP8 IS THE SAME, WITH ANTI-TRAP TRIMERS BINDING AROUND THE TRAP RING. IN SOLUTION, THE TRAP 12-MER RING BINDS UP TO SIX ANTI-TRAP TRIMERS. THE CRYSTAL STRUCTURES REPRESENT THE SATURATED FORM WITH 12 TRAP SUBUNITS AND 18 ANTI-TRAP SUBUNITS.

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Components

#1: Protein
Transcription attenuation protein mtrB / Tryptophan RNA-binding attenuator protein / Trp RNA-binding attenuation protein / TRAP


Mass: 8754.920 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bacillus stearothermophilus (bacteria) / Gene: mtrB / Plasmid: pET21b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q9X6J6
#2: Protein
Tryptophan RNA-binding attenuator protein-inhibitory protein / Anti-TRAP protein / AT


Mass: 5655.565 Da / Num. of mol.: 9
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bacillus subtilis (bacteria) / Gene: rtpA, yczA, BSU02530 / Plasmid: pET21b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: O31466
#3: Chemical
ChemComp-TRP / TRYPTOPHAN


Type: L-peptide linking / Mass: 204.225 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C11H12N2O2
#4: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Zn
Sequence detailsTHE SEQUENCE OF THE TRAP IS :MET TYR THR ASN SER ASP PHE VAL VAL ILE LYS ALA LEU GLU ASP GLY VAL ...THE SEQUENCE OF THE TRAP IS :MET TYR THR ASN SER ASP PHE VAL VAL ILE LYS ALA LEU GLU ASP GLY VAL ASN VAL ILE GLY LEU THR ARG GLY ALA ASP THR ARG PHE HIS HIS SER GLU LYS LEU ASP LYS GLY GLU VAL LEU ILE ALA GLN PHE THR GLU HIS THR SER ALA ILE LYS VAL ARG GLY LYS ALA TYR ILE GLN THR ARG HIS GLY VAL ILE GLU SER GLU GLY LYS LYS ALA ALA ALA ALA ALA ALA ALA MET TYR THR ASN SER ASP PHE VAL VAL ILE LYS ALA LEU GLU ASP GLY VAL ASN VAL ILE GLY LEU THR ARG GLY ALA ASP THR ARG PHE HIS HIS SER GLU LYS LEU ASP LYS GLY GLU VAL LEU ILE ALA GLN PHE THR GLU HIS THR SER ALA ILE LYS VAL ARG GLY LYS ALA TYR ILE GLN THR ARG HIS GLY VAL ILE GLU SER GLU GLY LYS LYS ALA ALA ALA ALA ALA ALA ALA MET TYR THR ASN SER ASP PHE VAL VAL ILE LYS ALA LEU GLU ASP GLY VAL ASN VAL ILE GLY LEU THR ARG GLY ALA ASP THR ARG PHE HIS HIS SER GLU LYS LEU ASP LYS GLY GLU VAL LEU ILE ALA GLN PHE THR GLU HIS THR SER ALA ILE LYS VAL ARG GLY LYS ALA TYR ILE GLN THR ARG HIS GLY VAL ILE GLU SER GLU GLY LYS LYS: BUT THE TRAP SUBUNITS IN THE MODEL ARE INDISTINGUISHABLE, AND HAVE THEREFORE BEEN INTERPRETED AS SEPARATE CHAINS.

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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: 3.07 Å3/Da / Density % sol: 59.97 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7
Details: 0.1M succinate pH 7.0, 13-15% PEG 10000, 2% dioxane, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Photon Factory / Beamline: AR-NW12A / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 210 / Detector: CCD / Date: Feb 16, 2007
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.2→50 Å / Num. obs: 19198 / % possible obs: 90.7 % / Redundancy: 3.1 % / Biso Wilson estimate: 76.85 Å2 / Rmerge(I) obs: 0.056 / Rsym value: 0.053
Reflection shellResolution: 3.2→3.31 Å / Redundancy: 2.1 % / Rmerge(I) obs: 0.195 / Mean I/σ(I) obs: 2.2 / Num. unique all: 19198 / Rsym value: 0.235 / % possible all: 75.9

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Processing

Software
NameVersionClassification
REFMAC5.2.0019refinement
HKL-2000data collection
DENZOdata reduction
SCALEPACKdata scaling
PHASERphasing
RefinementMethod to determine structure: PHASER
Starting model: 2BX9, 1QAW

2bx9

1qaw


Resolution: 3.2→20 Å / Cor.coef. Fo:Fc: 0.823 / Cor.coef. Fo:Fc free: 0.81 / SU B: 58.798 / SU ML: 0.56 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R Free: 0.608 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: ELECTRON DENSITY FOR CERTAIN REGIONS INCLUDING THE ZINC BINDING SITES IS POOR. THE GEOMETRY AROUND THE METAL ATOMS IS NOT DEFINITIVE, IN COMMON WITH OTHER CRYSTAL STRUCTURES OF ANTI-TRAP. ...Details: ELECTRON DENSITY FOR CERTAIN REGIONS INCLUDING THE ZINC BINDING SITES IS POOR. THE GEOMETRY AROUND THE METAL ATOMS IS NOT DEFINITIVE, IN COMMON WITH OTHER CRYSTAL STRUCTURES OF ANTI-TRAP. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.3248 984 5.1 %RANDOM
Rwork0.30349 ---
obs0.30461 18174 90.97 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 84.761 Å2
Baniso -1Baniso -2Baniso -3
1--4.1 Å2-2.05 Å20 Å2
2---4.1 Å20 Å2
3---6.15 Å2
Refinement stepCycle: LAST / Resolution: 3.2→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5633 0 95 0 5728
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.0225699
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.1241.9547661
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.2345698
X-RAY DIFFRACTIONr_dihedral_angle_2_deg38.8124.231234
X-RAY DIFFRACTIONr_dihedral_angle_3_deg19.593151005
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.3561527
X-RAY DIFFRACTIONr_chiral_restr0.0780.2912
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.024090
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2180.22559
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3040.23627
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1570.2235
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2210.295
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2270.211
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.1981.53699
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it0.35525752
X-RAY DIFFRACTIONr_scbond_it0.58132225
X-RAY DIFFRACTIONr_scangle_it1.0074.51909
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
11A232tight positional0.030.05
11B232tight positional0.040.05
11F232tight positional0.020.05
11G232tight positional0.030.05
11K232tight positional0.030.05
11L232tight positional0.020.05
22C16tight positional0.040.05
22D16tight positional0.050.05
22E16tight positional0.030.05
22H16tight positional0.030.05
22I16tight positional0.050.05
22J16tight positional0.030.05
22M16tight positional0.040.05
22O16tight positional0.030.05
33C36tight positional0.020.05
33D36tight positional0.030.05
33E36tight positional0.020.05
33H36tight positional0.020.05
33I36tight positional0.030.05
33J36tight positional0.020.05
33M36tight positional0.030.05
33O36tight positional0.040.05
44C64tight positional0.030.05
44D64tight positional0.030.05
44E64tight positional0.030.05
44H64tight positional0.030.05
44I64tight positional0.030.05
44J64tight positional0.030.05
44M64tight positional0.020.05
44N64tight positional0.020.05
44O64tight positional0.020.05
11A221loose positional0.485
11B221loose positional0.515
11F221loose positional0.65
11G221loose positional0.575
11K221loose positional0.65
11L221loose positional0.635
22C13loose positional0.655
22D13loose positional0.765
22E13loose positional0.615
22H13loose positional1.595
22I13loose positional1.085
22J13loose positional0.655
22M13loose positional0.685
22O13loose positional0.945
33C20loose positional0.615
33D20loose positional0.235
33E20loose positional0.45
33H20loose positional0.475
33I20loose positional0.425
33J20loose positional0.725
33M20loose positional0.455
33O20loose positional0.655
44C67loose positional0.725
44D67loose positional0.775
44E67loose positional0.845
44H67loose positional0.745
44I67loose positional0.715
44J67loose positional0.855
44M67loose positional0.745
44N67loose positional0.725
44O67loose positional0.775
11A232tight thermal0.060.5
11B232tight thermal0.060.5
11F232tight thermal0.030.5
11G232tight thermal0.040.5
11K232tight thermal0.040.5
11L232tight thermal0.040.5
22C16tight thermal0.040.5
22D16tight thermal0.070.5
22E16tight thermal0.060.5
22H16tight thermal0.040.5
22I16tight thermal0.020.5
22J16tight thermal0.020.5
22M16tight thermal0.030.5
22O16tight thermal0.040.5
33C36tight thermal0.030.5
33D36tight thermal0.020.5
33E36tight thermal0.070.5
33H36tight thermal0.020.5
33I36tight thermal0.020.5
33J36tight thermal0.020.5
33M36tight thermal0.020.5
33O36tight thermal0.030.5
44C64tight thermal0.040.5
44D64tight thermal0.040.5
44E64tight thermal0.060.5
44H64tight thermal0.030.5
44I64tight thermal0.030.5
44J64tight thermal0.030.5
44M64tight thermal0.020.5
44N64tight thermal0.030.5
44O64tight thermal0.040.5
11A221loose thermal1.4710
11B221loose thermal1.2810
11F221loose thermal1.0210
11G221loose thermal0.8210
11K221loose thermal0.7710
11L221loose thermal0.8610
22C13loose thermal0.9610
22D13loose thermal0.4710
22E13loose thermal0.3510
22H13loose thermal0.5310
22I13loose thermal0.410
22J13loose thermal0.3110
22M13loose thermal0.310
22O13loose thermal0.2210
33C20loose thermal0.2310
33D20loose thermal0.3710
33E20loose thermal0.3910
33H20loose thermal0.210
33I20loose thermal0.1410
33J20loose thermal0.1910
33M20loose thermal0.1910
33O20loose thermal0.1310
44C67loose thermal0.9710
44D67loose thermal0.5710
44E67loose thermal0.7610
44H67loose thermal0.4610
44I67loose thermal0.3510
44J67loose thermal0.610
44M67loose thermal0.5910
44N67loose thermal0.7310
44O67loose thermal0.8710
LS refinement shellResolution: 3.201→3.282 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.372 59 -
Rwork0.315 1072 -
obs-984 75.5 %
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)
13.0624-2.3052-0.21881.73520.16470.01560.03350.20950.09660.0207-0.10530.3876-0.1066-0.13630.0718-0.06940.07340.00180.05030.0014-0.095-60.231.26894.9431
215.0277-6.8423-3.453716.45945.15398.92140.83722.35770.5754-1.6176-0.8008-0.58830.7431-0.6749-0.03630.0006-0.00350.0004-0.0004-0.0039-0.0004-44.3616-7.1345-7.9415
320.8884-10.2351-0.818119.8432.57243.72130.36280.25590.0381-1.5171-0.52121.7168-0.0177-0.83410.15840.00040.0027-0.00320.0007-0.001-0.0002-58.42743.0355-0.5888
46.17394.06081.023718.50110.50780.17150.58470.03640.662-1.33580.33130.8978-0.50420.0884-0.916-0.0007-0.00130.01390.00340.03510.0053-41.212710.8128-0.124
526.4869-5.08076.331428.4223-8.494433.7442-0.169-2.0583-0.32411.5390.10280.08480.2573-1.5350.066200.00010.0001-0.0005-0.00080.0006-82.009814.190819.2001
622.7484-3.7117-3.844969.937310.14186.5785-0.0919-0.4733-0.51771.87640.44560.30420.25491.0297-0.3536-0.0006-0.00090.0002-0.0001-0.00050.0004-65.59698.160412.8346
716.9258-5.4296-2.449314.17670.67811.91430.1715-0.20170.623-0.1379-0.3430.42-0.2340.6730.17160.00010.0002-0.00020-0.00010.0006-70.171625.928212.3194
836.619316.426617.291752.3545-6.299343.71730.7264-2.29641.38870.0742-0.80881.39651.9857-0.15340.0824-0.00060.0015-0.0006-0.00040.00060.0008-53.76750.023919.9954
972.1215-4.1108-18.451799.243463.089199.74292.9564-2.26993.96672.1071-1.6322-4.59462.24182.1718-1.32420.00170.0014-0.0042-0.0003-0.00210.0038-47.589964.753514.0604
1015.0425-9.15568.329534.3955-5.70247.86330.8224-0.0574-0.04690.2251-0.0044-0.23970.45660.219-0.8180.001-0.00050.00050.0003-0.00130.0003-57.721366.061112.4809
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A10 - 65
2X-RAY DIFFRACTION1B10 - 65
3X-RAY DIFFRACTION1F10 - 65
4X-RAY DIFFRACTION1G10 - 65
5X-RAY DIFFRACTION1K10 - 65
6X-RAY DIFFRACTION1L10 - 65
7X-RAY DIFFRACTION2C1 - 9
8X-RAY DIFFRACTION2C36 - 52
9X-RAY DIFFRACTION2C10 - 35
10X-RAY DIFFRACTION2C54
11X-RAY DIFFRACTION3D1 - 9
12X-RAY DIFFRACTION3D36 - 52
13X-RAY DIFFRACTION3D10 - 35
14X-RAY DIFFRACTION3D54
15X-RAY DIFFRACTION4E1 - 9
16X-RAY DIFFRACTION4E36 - 52
17X-RAY DIFFRACTION4E10 - 35
18X-RAY DIFFRACTION4E54
19X-RAY DIFFRACTION5H1 - 9
20X-RAY DIFFRACTION5H36 - 51
21X-RAY DIFFRACTION5H10 - 35
22X-RAY DIFFRACTION6I5 - 9
23X-RAY DIFFRACTION6I36 - 52
24X-RAY DIFFRACTION6I10 - 35
25X-RAY DIFFRACTION6I54
26X-RAY DIFFRACTION7J1 - 9
27X-RAY DIFFRACTION7J36 - 51
28X-RAY DIFFRACTION7J10 - 35
29X-RAY DIFFRACTION7J54
30X-RAY DIFFRACTION8M1 - 9
31X-RAY DIFFRACTION8M36 - 51
32X-RAY DIFFRACTION8M10 - 35
33X-RAY DIFFRACTION9N36 - 52
34X-RAY DIFFRACTION10O1 - 9
35X-RAY DIFFRACTION10O36 - 51
36X-RAY DIFFRACTION10O10 - 35

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