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- PDB-3aoi: RNA polymerase-Gfh1 complex (Crystal type 2) -

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Basic information

Entry
Database: PDB / ID: 3aoi
TitleRNA polymerase-Gfh1 complex (Crystal type 2)
Components
  • (DNA-directed RNA polymerase subunit ...Polymerase) x 4
  • Anti-cleavage anti-GreA transcription factor Gfh1
  • DNA (5'-D(*GP*GP*TP*CP*TP*GP*TP*AP*TP*CP*AP*CP*GP*AP*GP*CP*CP*A*CP*CP*GP*CP*CP*GP*CP*AP*T)-3')
  • RNA (5'-R(*CP*CP*CP*GP*GP*AP*AP*GP*AP*UP*CP*AP*UP*CP*UP*UP*CP*CP*GP*GP*GP*GP*GP*AP*U*GP*CP*GP*GP*CP*GP*G)-3')
KeywordsTranscription / TRANSFERASE/DNA/RNA / Structural Genomics / RIKEN Structural Genomics/Proteomics Initiative / RSGI / TRANSFERASE-DNA-RNA complex
Function / homology
Function and homology information


RNA polymerase binding / DNA-directed RNA polymerase complex / regulation of DNA-templated transcription elongation / ribonucleoside binding / DNA-directed 5'-3' RNA polymerase activity / DNA-directed RNA polymerase / protein dimerization activity / DNA-templated transcription / magnesium ion binding / DNA binding ...RNA polymerase binding / DNA-directed RNA polymerase complex / regulation of DNA-templated transcription elongation / ribonucleoside binding / DNA-directed 5'-3' RNA polymerase activity / DNA-directed RNA polymerase / protein dimerization activity / DNA-templated transcription / magnesium ion binding / DNA binding / zinc ion binding / metal ion binding / cytoplasm
Similarity search - Function
Transcription elongation factor, GreA/GreB, conserved site / Transcription elongation factor, GreA/GreB, N-terminal / Transcription elongation factor, GreA/GreB, N-terminal domain superfamily / Transcription elongation factor, N-terminal / Prokaryotic transcription elongation factors signature 2. / Transcription elongation factor, GreA/GreB, C-terminal / Transcription elongation factor GreA/GreB family / Transcription elongation factor, GreA/GreB, C-term / Transcription elongation factor GreA/GreB, C-terminal domain superfamily / : ...Transcription elongation factor, GreA/GreB, conserved site / Transcription elongation factor, GreA/GreB, N-terminal / Transcription elongation factor, GreA/GreB, N-terminal domain superfamily / Transcription elongation factor, N-terminal / Prokaryotic transcription elongation factors signature 2. / Transcription elongation factor, GreA/GreB, C-terminal / Transcription elongation factor GreA/GreB family / Transcription elongation factor, GreA/GreB, C-term / Transcription elongation factor GreA/GreB, C-terminal domain superfamily / : / DNA-directed RNA polymerase subunit beta', hybrid domain / DNA-directed RNA polymerase, omega subunit / DNA-directed RNA polymerase, subunit beta-prime, bacterial type / DNA-directed RNA polymerase, beta subunit, external 1 domain superfamily / DNA-directed RNA polymerase, beta subunit, external 1 domain / RNA polymerase beta subunit external 1 domain / RNA polymerase, alpha subunit, C-terminal / Bacterial RNA polymerase, alpha chain C terminal domain / DNA-directed RNA polymerase, alpha subunit / DNA-directed RNA polymerase beta subunit, bacterial-type / RNA polymerase Rpb6 / RNA polymerase, subunit omega/Rpo6/RPB6 / RNA polymerase Rpb6 / RNA polymerase Rpb1, domain 3 superfamily / RNA polymerase Rpb1, clamp domain superfamily / RPB6/omega subunit-like superfamily / DNA-directed RNA polymerase, subunit beta-prime / RNA polymerase Rpb1, domain 3 / RNA polymerase Rpb1, domain 3 / RNA polymerase Rpb2, domain 2 superfamily / RNA polymerase Rpb1, domain 1 / RNA polymerase Rpb1, domain 1 / RNA polymerase, alpha subunit / RNA polymerase Rpb1, domain 4 / RNA polymerase Rpb1, domain 2 / RNA polymerase Rpb1, domain 4 / RNA polymerase, N-terminal / RNA polymerase Rpb1, funnel domain superfamily / RNA polymerase I subunit A N-terminus / RNA polymerase Rpb1, domain 5 / RNA polymerase Rpb1, domain 5 / RNA polymerase, beta subunit, protrusion / RNA polymerase beta subunit / DNA-directed RNA polymerase, insert domain / DNA-directed RNA polymerase, RpoA/D/Rpb3-type / RNA polymerase Rpb3/RpoA insert domain / RNA polymerase Rpb3/Rpb11 dimerisation domain / RNA polymerases D / DNA-directed RNA polymerase, insert domain superfamily / RNA polymerase, RBP11-like subunit / RNA polymerase Rpb2, domain 2 / RNA polymerase Rpb2, domain 2 / RNA polymerase, beta subunit, conserved site / RNA polymerase Rpb2, domain 7 / RNA polymerase Rpb2, domain 3 / RNA polymerase Rpb2, OB-fold / RNA polymerase Rpb2, domain 7 / RNA polymerase Rpb2, domain 3 / RNA polymerases beta chain signature. / DNA-directed RNA polymerase, subunit 2, hybrid-binding domain / DNA-directed RNA polymerase, subunit 2 / DNA-directed RNA polymerase, subunit 2, hybrid-binding domain superfamily / RNA polymerase Rpb2, domain 6
Similarity search - Domain/homology
DNA / DNA (> 10) / RNA / RNA (> 10) / DNA-directed RNA polymerase subunit alpha / Transcription inhibitor protein Gfh1 / DNA-directed RNA polymerase subunit omega / DNA-directed RNA polymerase subunit beta' / DNA-directed RNA polymerase subunit beta
Similarity search - Component
Biological speciesThermus thermophilus (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4.3 Å
AuthorsTagami, S. / Sekine, S. / Kumarevel, T. / Yamamoto, M. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI)
CitationJournal: Nature / Year: 2010
Title: Crystal structure of bacterial RNA polymerase bound with a transcription inhibitor protein
Authors: Tagami, S. / Sekine, S.I. / Kumarevel, T. / Hino, N. / Murayama, Y. / Kamegamori, S. / Yamamoto, M. / Sakamoto, K. / Yokoyama, S.
History
DepositionSep 30, 2010Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Dec 8, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Nov 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 / pdbx_struct_conn_angle / struct_conn / struct_ref_seq / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _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.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _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.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_ref_seq.db_align_beg / _struct_ref_seq.db_align_end / _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: DNA-directed RNA polymerase subunit alpha
B: DNA-directed RNA polymerase subunit alpha
C: DNA-directed RNA polymerase subunit beta
D: DNA-directed RNA polymerase subunit beta'
E: DNA-directed RNA polymerase subunit omega
F: DNA-directed RNA polymerase subunit alpha
G: DNA-directed RNA polymerase subunit alpha
H: DNA-directed RNA polymerase subunit beta
I: DNA-directed RNA polymerase subunit beta'
J: DNA-directed RNA polymerase subunit omega
K: DNA-directed RNA polymerase subunit alpha
L: DNA-directed RNA polymerase subunit alpha
M: DNA-directed RNA polymerase subunit beta
N: DNA-directed RNA polymerase subunit beta'
O: DNA-directed RNA polymerase subunit omega
P: DNA (5'-D(*GP*GP*TP*CP*TP*GP*TP*AP*TP*CP*AP*CP*GP*AP*GP*CP*CP*A*CP*CP*GP*CP*CP*GP*CP*AP*T)-3')
Q: RNA (5'-R(*CP*CP*CP*GP*GP*AP*AP*GP*AP*UP*CP*AP*UP*CP*UP*UP*CP*CP*GP*GP*GP*GP*GP*AP*U*GP*CP*GP*GP*CP*GP*G)-3')
R: DNA (5'-D(*GP*GP*TP*CP*TP*GP*TP*AP*TP*CP*AP*CP*GP*AP*GP*CP*CP*A*CP*CP*GP*CP*CP*GP*CP*AP*T)-3')
S: RNA (5'-R(*CP*CP*CP*GP*GP*AP*AP*GP*AP*UP*CP*AP*UP*CP*UP*UP*CP*CP*GP*GP*GP*GP*GP*AP*U*GP*CP*GP*GP*CP*GP*G)-3')
T: DNA (5'-D(*GP*GP*TP*CP*TP*GP*TP*AP*TP*CP*AP*CP*GP*AP*GP*CP*CP*A*CP*CP*GP*CP*CP*GP*CP*AP*T)-3')
U: RNA (5'-R(*CP*CP*CP*GP*GP*AP*AP*GP*AP*UP*CP*AP*UP*CP*UP*UP*CP*CP*GP*GP*GP*GP*GP*AP*U*GP*CP*GP*GP*CP*GP*G)-3')
X: Anti-cleavage anti-GreA transcription factor Gfh1
Y: Anti-cleavage anti-GreA transcription factor Gfh1
Z: Anti-cleavage anti-GreA transcription factor Gfh1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)1,241,94130
Polymers1,241,67224
Non-polymers2696
Water0
1
A: DNA-directed RNA polymerase subunit alpha
B: DNA-directed RNA polymerase subunit alpha
C: DNA-directed RNA polymerase subunit beta
D: DNA-directed RNA polymerase subunit beta'
E: DNA-directed RNA polymerase subunit omega
P: DNA (5'-D(*GP*GP*TP*CP*TP*GP*TP*AP*TP*CP*AP*CP*GP*AP*GP*CP*CP*A*CP*CP*GP*CP*CP*GP*CP*AP*T)-3')
Q: RNA (5'-R(*CP*CP*CP*GP*GP*AP*AP*GP*AP*UP*CP*AP*UP*CP*UP*UP*CP*CP*GP*GP*GP*GP*GP*AP*U*GP*CP*GP*GP*CP*GP*G)-3')
X: Anti-cleavage anti-GreA transcription factor Gfh1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)413,98010
Polymers413,8918
Non-polymers902
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
F: DNA-directed RNA polymerase subunit alpha
G: DNA-directed RNA polymerase subunit alpha
H: DNA-directed RNA polymerase subunit beta
I: DNA-directed RNA polymerase subunit beta'
J: DNA-directed RNA polymerase subunit omega
R: DNA (5'-D(*GP*GP*TP*CP*TP*GP*TP*AP*TP*CP*AP*CP*GP*AP*GP*CP*CP*A*CP*CP*GP*CP*CP*GP*CP*AP*T)-3')
S: RNA (5'-R(*CP*CP*CP*GP*GP*AP*AP*GP*AP*UP*CP*AP*UP*CP*UP*UP*CP*CP*GP*GP*GP*GP*GP*AP*U*GP*CP*GP*GP*CP*GP*G)-3')
Y: Anti-cleavage anti-GreA transcription factor Gfh1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)413,98010
Polymers413,8918
Non-polymers902
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
K: DNA-directed RNA polymerase subunit alpha
L: DNA-directed RNA polymerase subunit alpha
M: DNA-directed RNA polymerase subunit beta
N: DNA-directed RNA polymerase subunit beta'
O: DNA-directed RNA polymerase subunit omega
T: DNA (5'-D(*GP*GP*TP*CP*TP*GP*TP*AP*TP*CP*AP*CP*GP*AP*GP*CP*CP*A*CP*CP*GP*CP*CP*GP*CP*AP*T)-3')
U: RNA (5'-R(*CP*CP*CP*GP*GP*AP*AP*GP*AP*UP*CP*AP*UP*CP*UP*UP*CP*CP*GP*GP*GP*GP*GP*AP*U*GP*CP*GP*GP*CP*GP*G)-3')
Z: Anti-cleavage anti-GreA transcription factor Gfh1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)413,98010
Polymers413,8918
Non-polymers902
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)189.230, 264.510, 193.930
Angle α, β, γ (deg.)90.00, 116.68, 90.00
Int Tables number4
Space group name H-MP1211

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Components

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DNA-directed RNA polymerase subunit ... , 4 types, 15 molecules ABFGKLCHMDINEJO

#1: Protein
DNA-directed RNA polymerase subunit alpha / Polymerase / RNAP subunit alpha / Transcriptase subunit alpha / RNA polymerase subunit alpha


Mass: 35056.164 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: Q5SHR6, DNA-directed RNA polymerase
#2: Protein DNA-directed RNA polymerase subunit beta / Polymerase / RNAP subunit beta / Transcriptase subunit beta / RNA polymerase subunit beta


Mass: 125436.539 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: Q8RQE9, DNA-directed RNA polymerase
#3: Protein DNA-directed RNA polymerase subunit beta' / Polymerase / RNAP subunit beta' / Transcriptase subunit beta' / RNA polymerase subunit beta'


Mass: 170997.391 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: Q8RQE8, DNA-directed RNA polymerase
#4: Protein DNA-directed RNA polymerase subunit omega / Polymerase / RNAP omega subunit / Transcriptase subunit omega / RNA polymerase omega subunit


Mass: 11533.316 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: Q8RQE7, DNA-directed RNA polymerase

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DNA chain / RNA chain / Protein , 3 types, 9 molecules PRTQSUXYZ

#5: DNA chain DNA (5'-D(*GP*GP*TP*CP*TP*GP*TP*AP*TP*CP*AP*CP*GP*AP*GP*CP*CP*A*CP*CP*GP*CP*CP*GP*CP*AP*T)-3')


Mass: 8238.298 Da / Num. of mol.: 3 / Source method: obtained synthetically / Details: DNA oligomer
#6: RNA chain RNA (5'-R(*CP*CP*CP*GP*GP*AP*AP*GP*AP*UP*CP*AP*UP*CP*UP*UP*CP*CP*GP*GP*GP*GP*GP*AP*U*GP*CP*GP*GP*CP*GP*G)-3')


Mass: 10366.212 Da / Num. of mol.: 3 / Source method: obtained synthetically / Details: RNA oligomer
#7: Protein Anti-cleavage anti-GreA transcription factor Gfh1


Mass: 17206.482 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Thermus thermophilus (bacteria) / Strain: HB8 / Gene: TTHA1042 / Production host: Escherichia coli (E. coli) / References: UniProt: Q5SJG6

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Non-polymers , 2 types, 6 molecules

#8: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Zn
#9: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Mg

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Details

Sequence detailsONE MORE DNA OLIGOMER (NONTEMPLATE DNA) WAS USED IN CRYSTALLIZATION, HOWEVER ITS ELECTRON DENSITY ...ONE MORE DNA OLIGOMER (NONTEMPLATE DNA) WAS USED IN CRYSTALLIZATION, HOWEVER ITS ELECTRON DENSITY WAS NOT OBSERVED. THE SEQUENCE IS (DC)(DG)(DT)(DG)(DA)(DT)(DA)(DC)(DA)(DG)(DA)(DC)(DC).

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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: 3.49 Å3/Da / Density % sol: 64.78 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.4
Details: 50mM Hepes-NaOH buffer (pH 6.4), 5.5% PEG 8000, 300mM LiCl, 10mM MgCl2, 1% dimethyl sulfoxide, 5mM taurine, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 0.9801 Å
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: Sep 29, 2008
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9801 Å / Relative weight: 1
ReflectionResolution: 4.3→50 Å / Num. obs: 112834 / % possible obs: 97.9 %

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Processing

Software
NameVersionClassification
PHASERphasing
CNS1.2refinement
XDSdata reduction
XDSdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRIES 2O5I, 3DXJ, 2F23, and 3AOH
Resolution: 4.3→47.57 Å / Rfactor Rfree error: 0.006 / Data cutoff high absF: 8706429.03 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Details: BULK SOLVENT MODEL USED
RfactorNum. reflection% reflectionSelection details
Rfree0.338 3392 3 %RANDOM
Rwork0.317 ---
obs0.317 112830 97.6 %-
Solvent computationSolvent model: FLAT MODEL / Bsol: 102.644 Å2 / ksol: 0.3 e/Å3
Displacement parametersBiso mean: 160.4 Å2
Baniso -1Baniso -2Baniso -3
1-20.46 Å20 Å232.91 Å2
2---32.81 Å20 Å2
3---12.35 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.88 Å0.81 Å
Luzzati d res low-5 Å
Luzzati sigma a1.46 Å1.31 Å
Refinement stepCycle: LAST / Resolution: 4.3→47.57 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms72811 829 6 0 73646
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONc_bond_d0.01
X-RAY DIFFRACTIONc_bond_d_na
X-RAY DIFFRACTIONc_bond_d_prot
X-RAY DIFFRACTIONc_angle_d
X-RAY DIFFRACTIONc_angle_d_na
X-RAY DIFFRACTIONc_angle_d_prot
X-RAY DIFFRACTIONc_angle_deg1.7
X-RAY DIFFRACTIONc_angle_deg_na
X-RAY DIFFRACTIONc_angle_deg_prot
X-RAY DIFFRACTIONc_dihedral_angle_d24.6
X-RAY DIFFRACTIONc_dihedral_angle_d_na
X-RAY DIFFRACTIONc_dihedral_angle_d_prot
X-RAY DIFFRACTIONc_improper_angle_d1.43
X-RAY DIFFRACTIONc_improper_angle_d_na
X-RAY DIFFRACTIONc_improper_angle_d_prot
X-RAY DIFFRACTIONc_mcbond_it25.071.5
X-RAY DIFFRACTIONc_mcangle_it38.872
X-RAY DIFFRACTIONc_scbond_it28.962
X-RAY DIFFRACTIONc_scangle_it41.472.5
LS refinement shellResolution: 4.3→4.57 Å / Rfactor Rfree error: 0.018 / Total num. of bins used: 6
RfactorNum. reflection% reflection
Rfree0.412 528 2.9 %
Rwork0.404 17502 -
obs--94.1 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1protein_rep.paramprotein.top
X-RAY DIFFRACTION2ion.paramion.top
X-RAY DIFFRACTION3dna-rna_rep.paramdna-rna_rep.top

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