SAXSdb — 3ice

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Transcription termination factor rho

Escherichia coli K-12

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein–RNA Homooligomer Protein × 6 RNA 1 PDB declaration: heptameric（7） Consistent with all polymer counts	Chain A； UniProt 1–419 Chain B； UniProt 1–419 Chain C； UniProt 1–419 Chain D； UniProt 1–419 Chain E； UniProt 1–419 Chain F； UniProt 1–419	Non-standard monomer：Yes (specific site not provided by mmCIF)	5'-R(PUPUPUPUPUPUPUPUPUPUPUPU)-3' × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6 BEF BERYLLIUM TRIFLUORIDE ION × 6 SPD SPERMIDINE × 2	X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.9；291 K；2.5% MPD, 50mM HEPES, 5mM Tris-HCL, 160mM sodium chloride, 1.25mM magnesium chloride, 5mM spermidine-HCL, 0.5mM TCEP, 1.25mM ADP-BeF3,, pH 7.9, MICROBATCH, temperature 291K	Resolution 2.80 Å R-free 0.295

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 3ICE	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1PV4 X-ray crystal structure of the Rho transcription termination factor in complex with single stranded DNA Deposited 2003-06-26	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 6 PDB declaration: undecameric	Chain A 1–419（419 aa） Fragment：bacterial transcription termination Chain B 1–419（419 aa） Fragment：bacterial transcription termination Chain C 1–419（419 aa） Fragment：bacterial transcription termination Chain D 1–419（419 aa） Fragment：bacterial transcription termination Chain E 1–419（419 aa） Fragment：bacterial transcription termination Chain F 1–419（419 aa） Fragment：bacterial transcription termination	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；291 K；0.05M Nacacodylate (pH 6.5), 0.05M NaCl, 2.5% PEG 8K, 20% glycerol, 0.3mM n-Nonyl-beta-D-thiomaltoside, 1mM TCEP, VAPOR DIFFUSION, HANGING DROP, temperature 18K	Resolution 3.00 Å R-free 0.296
1PVO X-ray crystal structure of Rho transcription termination factor in complex with ssRNA substrate and ANPPNP Deposited 2003-06-27	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Homooligomer；Protein × 6 PDB declaration: undecameric	Chain A 1–419（419 aa） Chain B 1–419（419 aa） Chain C 1–419（419 aa） Chain D 1–419（419 aa） Chain E 1–419（419 aa） Chain F 1–419（419 aa）	Not recorded	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；291 K；0.05 M Cacodylate (pH 6.5), 0.05 M NaCl, 2.5% PEG 8K, 20% glycerol, 0.3 mM n-Nonyl-beta-D-thiomaltoside, 1mM TCEP, VAPOR DIFFUSION, HANGING DROP, temperature 18K	Resolution 3.00 Å R-free 0.304
2HT1 The closed ring structure of the Rho transcription termination factor in complex with nucleic acid in the motor domains Deposited 2006-07-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Homooligomer；Protein × 6 PDB declaration: pentadecameric	Chain A 1–411（411 aa） Chain B 1–411（411 aa）	Not recorded	SO4 SULFATE ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions Microbatch under paraffine oil；pH 6.5；291 K；50 mM Na cacodylate, 10 mM MgOAc, 1.8 M LiSO4, 2% benzamidine, 10 mM spermine-HCl, pH 6.5, Microbatch under paraffine oil, temperature 291K	Resolution 3.51 Å R-free 0.328
6WA8 Crystal structure of the E. coli transcription termination factor Rho Deposited 2020-03-24	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–419（419 aa） Chain B 1–419（419 aa） Chain C 1–419（419 aa） Chain D 1–419（419 aa） Chain E 1–419（419 aa） Chain F 1–419（419 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.3；293 K；100 mM NaCl, 100 mM Tris pH 8.3, 28% PEG2000MME, 20 mM ATP, pH 7.5	Resolution 3.30 Å R-free 0.296
6XAS CryoEM Structure of E. coli Rho-dependent Transcription Pre-termination Complex Deposited 2020-06-04	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 12 PDB declaration: pentadecameric	Chain A 1–419（419 aa） Chain B 1–419（419 aa） Chain C 1–419（419 aa） Chain D 1–419（419 aa） Chain E 1–419（419 aa） Chain F 1–419（419 aa）	Not recorded	MG MAGNESIUM ION × 1 ZN ZINC ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
6XAV CryoEM Structure of E. coli Rho-dependent Transcription Pre-termination Complex bound with NusG Deposited 2020-06-04	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 13 PDB declaration: hexadecameric	Chain A 1–419（419 aa） Chain B 1–419（419 aa） Chain C 1–419（419 aa） Chain D 1–419（419 aa） Chain E 1–419（419 aa） Chain F 1–419（419 aa）	Not recorded	MG MAGNESIUM ION × 1 ZN ZINC ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 7.70 Å
6Z9P Transcription termination intermediate complex 1 Deposited 2020-06-04	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 13 PDB declaration: hexadecameric	Chain a 1–419（419 aa） Chain b 1–419（419 aa） Chain c 1–419（419 aa） Chain d 1–419（419 aa） Chain e 1–419（419 aa） Chain f 1–419（419 aa）	Not recorded	BEF BERYLLIUM TRIFLUORIDE ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 6 ZN ZINC ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å
6Z9R Transcription termination intermediate complex 3 Deposited 2020-06-04	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 13 PDB declaration: hexadecameric	Chain a 1–419（419 aa） Chain b 1–419（419 aa） Chain c 1–419（419 aa） Chain d 1–419（419 aa） Chain e 1–419（419 aa） Chain f 1–419（419 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 6 BEF BERYLLIUM TRIFLUORIDE ION × 5 ZN ZINC ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.10 Å
6Z9T Transcription termination intermediate complex 5 Deposited 2020-06-04	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 12 PDB declaration: pentadecameric	Chain a 1–419（419 aa） Chain b 1–419（419 aa） Chain c 1–419（419 aa） Chain d 1–419（419 aa） Chain e 1–419（419 aa） Chain f 1–419（419 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 6 BEF BERYLLIUM TRIFLUORIDE ION × 5 ZN ZINC ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.10 Å
8PEX Rho P167L-ATPgS-Psu complex II Deposited 2023-06-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 22 PDB declaration: 22-meric	Chain A 1–419（419 aa） Chain B 1–419（419 aa） Chain C 1–419（419 aa） Chain D 1–419（419 aa） Chain E 1–419（419 aa） Chain F 1–419（419 aa） Chain I 1–419（419 aa） Chain J 1–419（419 aa） Chain K 1–419（419 aa） Chain L 1–419（419 aa） Chain M 1–419（419 aa） Chain N 1–419（419 aa）	Not recorded	AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 12 MG MAGNESIUM ION × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 3.10 Å
8PEY Rho P167L-ATPgS-Psu complex II locked Deposited 2023-06-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 23 PDB declaration: 23-meric	Chain A 1–419（419 aa） Chain B 1–419（419 aa） Chain C 1–419（419 aa） Chain D 1–419（419 aa） Chain E 1–419（419 aa） Chain F 1–419（419 aa） Chain G 1–419（419 aa） Chain I 1–419（419 aa） Chain J 1–419（419 aa） Chain K 1–419（419 aa） Chain L 1–419（419 aa） Chain M 1–419（419 aa） Chain N 1–419（419 aa）	Not recorded	AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 12 MG MAGNESIUM ION × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 3.00 Å
8PTG Structure of the transcription termination factor Rho bound to RNA at the PBS and SBS Deposited 2023-07-14	Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Homooligomer；Protein × 6 PDB declaration: heptameric	Chain A 1–419（419 aa） Chain B 1–419（419 aa） Chain C 1–419（419 aa） Chain D 1–419（419 aa） Chain E 1–419（419 aa） Chain F 1–419（419 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6 BEF BERYLLIUM TRIFLUORIDE ION × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 2.90 Å
8PTM Structure of the transcription termination factor Rho in complex with Rof and ADP Deposited 2023-07-14	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 11 PDB declaration: 11-meric	Chain A 1–419（419 aa） Chain B 1–419（419 aa） Chain C 1–419（419 aa） Chain D 1–419（419 aa） Chain E 1–419（419 aa） Chain F 1–419（419 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 3 MG MAGNESIUM ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 2.90 Å
8PTN Structure of the transcription termination factor Rho in complex with Rof Deposited 2023-07-14	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 11 PDB declaration: undecameric	Chain A 1–419（419 aa） Chain B 1–419（419 aa） Chain C 1–419（419 aa） Chain D 1–419（419 aa） Chain E 1–419（419 aa） Chain F 1–419（419 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 3.30 Å
8PTO Structure of Rho pentamer in complex with Rof and ADP Deposited 2023-07-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain A 1–419（419 aa） Chain B 1–419（419 aa） Chain C 1–419（419 aa） Chain D 1–419（419 aa） Chain E 1–419（419 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 2.70 Å
8PTP Structure of Rho pentamer in complex with Rof Deposited 2023-07-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain A 1–419（419 aa） Chain B 1–419（419 aa） Chain C 1–419（419 aa） Chain D 1–419（419 aa） Chain E 1–419（419 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 3.00 Å
8Q3P Bacterial transcription termination factor Rho G150D mutant bound to ADP; C-terminal 8xHis-tag Deposited 2023-08-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 18 PDB declaration: 18-meric	Chain a 1–419（419 aa） Chain b 1–419（419 aa） Chain c 1–419（419 aa） Chain d 1–419（419 aa） Chain e 1–419（419 aa） Chain f 1–419（419 aa） Chain g 1–419（419 aa） Chain h 1–419（419 aa） Chain i 1–419（419 aa） Chain j 1–419（419 aa） Chain k 1–419（419 aa） Chain l 1–419（419 aa） Chain m 1–419（419 aa） Chain n 1–419（419 aa） Chain o 1–419（419 aa） Chain p 1–419（419 aa） Chain q 1–419（419 aa） Chain r 1–419（419 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 18 MG MAGNESIUM ION × 18	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
8Q3Q Bacterial transcription termination factor Rho G152D mutant bound to ADP; C-terminal 8xHis-tag Deposited 2023-08-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 18 PDB declaration: 18-meric	Chain a 1–419（419 aa） Chain b 1–419（419 aa） Chain c 1–419（419 aa） Chain d 1–419（419 aa） Chain e 1–419（419 aa） Chain f 1–419（419 aa） Chain g 1–419（419 aa） Chain h 1–419（419 aa） Chain i 1–419（419 aa） Chain j 1–419（419 aa） Chain k 1–419（419 aa） Chain l 1–419（419 aa） Chain m 1–419（419 aa） Chain n 1–419（419 aa） Chain o 1–419（419 aa） Chain p 1–419（419 aa） Chain q 1–419（419 aa） Chain r 1–419（419 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 18 MG MAGNESIUM ION × 18	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
8W8D Structural mechanism of inhibition of the Rho transcription termination factor by Rof Deposited 2023-09-01	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: 12-meric	Chain A 1–419（419 aa） Chain B 1–419（419 aa） Chain C 1–419（419 aa） Chain D 1–419（419 aa） Chain E 1–419（419 aa） Chain F 1–419（419 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.80 Å
9GCS Rho-ATP-Psu complex II Deposited 2024-08-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 22 PDB declaration: 22-meric	Chain B 1–419（419 aa） Chain C 1–419（419 aa） Chain D 1–419（419 aa） Chain E 1–419（419 aa） Chain F 1–419（419 aa） Chain G 1–419（419 aa） Chain J 1–419（419 aa） Chain K 1–419（419 aa） Chain L 1–419（419 aa） Chain M 1–419（419 aa） Chain N 1–419（419 aa） Chain O 1–419（419 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 12 MG MAGNESIUM ION × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å
9GCT Rho-ATP-Psu complex II expanded Deposited 2024-08-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 30 PDB declaration: 30-meric	Chain A 1–419（419 aa） Chain B 1–419（419 aa） Chain C 1–419（419 aa） Chain D 1–419（419 aa） Chain E 1–419（419 aa） Chain F 1–419（419 aa） Chain G 1–419（419 aa） Chain H 1–419（419 aa） Chain J 1–419（419 aa） Chain K 1–419（419 aa） Chain L 1–419（419 aa） Chain M 1–419（419 aa） Chain N 1–419（419 aa） Chain O 1–419（419 aa） Chain P 1–419（419 aa） Chain Y 1–419（419 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 15 MG MAGNESIUM ION × 15	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å
9GCU Rho-P167L-ATP gamma S Deposited 2024-08-02	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–419（419 aa） Chain B 1–419（419 aa） Chain C 1–419（419 aa） Chain D 1–419（419 aa） Chain E 1–419（419 aa） Chain F 1–419（419 aa）	Not recorded	MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.80 Å

22 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	RHO_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–422； UniProt 1–419 Author chain B； PDBConstruct 4–422； UniProt 1–419 Author chain C； PDBConstruct 4–422； UniProt 1–419 Author chain D； PDBConstruct 4–422； UniProt 1–419 Author chain E； PDBConstruct 4–422； UniProt 1–419 Author chain F； PDBConstruct 4–422； UniProt 1–419

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	3ice
Deposition date deposition_date	2009-07-17
Structure title title	Rho transcription termination factor bound to RNA and ADP-BeF3
Keywords keywords	;transcription, ATPase, hexamer, helicase, RNA, RecA, OB fold, motor, ATP-binding, Hydrolase, Nucleotide-binding, RNA-binding, Transcription regulation, Transcription termination, TRANSCRIPTION REGULATOR-RNA COMPLEX ;; TRANSCRIPTION REGULATOR/RNA
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	44.34 Å
Radius of gyration Rg (electron density) rg_electron	43.92 Å
Forward intensity I(0) i0	1226190000.00
Molecular weight molecular_weight	281470.0 kDa
Excluded volume excluded_volume	347760 Å³
Envelope volume envelope_volume	477570 Å³
Hydration-shell volume shell_volume	85360 Å³
Envelope diameter envelope_diameter	143.5 Å
Shell Rg shell_rg	53.07 Å
Envelope Rg envelope_rg	43.73 Å
Shape Rg shape_rg	43.93 Å
Total Rg total_rg	44.22 Å
Total atoms total_atoms	19453
Residues n_residues	2355
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	140.9 Å
Rg (real space) rg_real	44.13 Å
Rg uncertainty (real space) rg_real_error	0.93 Å
I(0) (real space) i0_real	1.2260e+09
I(0) uncertainty (real space) i0_real_error	2.3060e+07
Rg (reciprocal space) rg_reciprocal	44.34 Å
I(0) (reciprocal space) i0_reciprocal	1226000000.0000
Solution quality estimate total_estimate	0.9005
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	54.8 Å
Skewness Skewness skewness	0.149
Kurtosis Kurtosis kurtosis	-0.560
Angular range angular_range	— – 0.1800 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	107000000.0000
Real-space data points n_real_points	37
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.921; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.952

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (7)

Entity 1 Entity 1 polymer

Description description	Transcription termination factor rho
Molecular weight formula_weight	48193.8 kDa
EC 编号 ec_number	3.6.1.-
Source method src_method	man
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F
Atom count atom_count	19558

MGHMNLTELKNTPVSELITLGENMGLENLARMRKQDIIFAILKQHAKSGEDIFGDGVLEILQDGFGFLRSADSSYLAGPDDIYVSPSQIRRFNLRTGDTISGKIRPPKEGERYFALLKVNEVNFDKPENARNKILFENLTPLHANSRLRMERGNGSTEDLTARVLDLASPIGRGQRGLIVAPPKAGKTMLLQNIAQSIAYNHPDCVLMVLLIDERPEEVTEMQRLVKGEVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVIILLDSITRLARAYNTVVPASGKVLTGGVDANALHRPKRFFGAARNVEEGGSLTIIATALIDTGSKMDEVIYEEFKGTGNMELHLSRKIAEKRVFPAIDYNRSGTRKEELLTTQEELQKMWILRKIIHPMGEIDAMEFLINKLAMTKTNDDFFEMMKRS

来源 Source

来源生物 organism	Escherichia coli K-12
NCBI Class编号 ncbi_taxonomy_id	83333
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	5'-R(PUPUPUPUPUPUPUPUPUPUPUPU)-3'
Molecular weight formula_weight	3629.0 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polyribonucleotide
Chain IDs strand_id	G

UUUUUUUUUUUU

Entity 3 Entity 3 non-polymer

Description description	ADENOSINE-5'-DIPHOSPHATE
Molecular weight formula_weight	427.2 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 4 Entity 4 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 5 Entity 5 non-polymer

Description description	BERYLLIUM TRIFLUORIDE ION
Molecular weight formula_weight	66.0 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 6 Entity 6 non-polymer

Description description	SPERMIDINE
Molecular weight formula_weight	145.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 7 Entity 7 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	84

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7. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

Domain ID domain_id	3iceA01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	140 — Nucleic acid-binding proteins

Domain ID domain_id	3iceA02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	3iceB01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	140 — Nucleic acid-binding proteins

Domain ID domain_id	3iceB02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	3iceC01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	140 — Nucleic acid-binding proteins

Domain ID domain_id	3iceC02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	3iceD01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	140 — Nucleic acid-binding proteins

Domain ID domain_id	3iceD02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	3iceE01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	140 — Nucleic acid-binding proteins

Domain ID domain_id	3iceE02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	3iceF01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	140 — Nucleic acid-binding proteins

Domain ID domain_id	3iceF02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

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8. Citations (1)

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Unit-cell length a length_a	69.230 Å
Unit-cell length b length_b	127.030 Å
Unit-cell length c length_c	127.170 Å
Unit-cell angle α angle_alpha	60.48 °
Unit-cell angle β angle_beta	90.26 °
Unit-cell angle γ angle_gamma	89.77 °
Molecules per unit cell Z z_pdb	6

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	2.800 Å
Low-resolution limit resolution_low	41.880 Å
R factor r_factor	0.2710
R_work r_work	0.2700
R_free r_free	0.2950

fit	/app/data/saxs_computation/ic/3ice/3ice.fit
pddf	/app/data/pr_computation/ic/3ice/3ice.pr.out
profile	/app/data/saxs_computation/ic/3ice/3ice.dat

Rho transcription termination factor bound to RNA and ADP-BeF3

1. Protein Identity and Related Structures Protein Identity & Related Structures

Transcription termination factor rho

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (7)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 water

7. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)