3hfh

Crystal structure of tandem FF domains

Method: X-RAY DIFFRACTION D_max: 176.7 Å Quality: REASONABLE

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

Transcription elongation regulator 1

Homo sapiens

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 661–845	Fragment：FF domains: UNP residues 661-845 Non-standard monomer：Yes (specific site not provided by mmCIF)	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；50mM Bis-Tris pH 6.5, 50 mM Ammonium sulfate, 30% Pentaerythritol ethoxylate, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.70 Å R-free 0.283
2	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain B； UniProt 661–845	Fragment：FF domains: UNP residues 661-845 Non-standard monomer：Yes (specific site not provided by mmCIF)	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；50mM Bis-Tris pH 6.5, 50 mM Ammonium sulfate, 30% Pentaerythritol ethoxylate, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.70 Å R-free 0.283

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 3HFH	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2DK7 Solution structure of WW domain in transcription elongation regulator 1 Deposited 2006-04-06	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 520–579（60 aa） Fragment：WW domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 120mM；Pressure ambient NMR sample composition 0.8mM U-15N, 13C; 20mM phosphate buffer NA; 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90%H2O,10%D2O \| 90% H2O/10% D2O	Resolution not provided
2DOD Solution structure of the first FF domain of human transcription factor CA150 Deposited 2006-04-28	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 651–719（69 aa） Fragment：FF domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 120mM；Pressure ambient NMR sample composition 1.2mM 13C/15N-PROTEIN; 20mM d-Tris-HCl(pH7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided
2DOE Solution structure of the third FF domain of human transcription factor CA150 Deposited 2006-04-28	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 784–853（70 aa） Fragment：FF domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 120mM；Pressure ambient NMR sample composition 1.1mM 13C/15N-PROTEIN; 20mM d-Tris-HCl(pH7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3;90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided
2DOF Solution structure of the fourth FF domain of human transcription factor CA150 Deposited 2006-04-28	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 888–959（72 aa） Fragment：FF domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 120mM；Pressure ambient NMR sample composition 1.1mM 13C/15N-PROTEIN, 20mM d-Tris-HCl(pH7.0), 100mM NaCl, 1mM d-DTT, 0.02% NaN3, 10% D2O \| 90% H2O/10% D2O	Resolution not provided
2E71 Solution structure of the second FF domain of human transcription factor CA150 Deposited 2007-01-05	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 717–786（70 aa） Fragment：FF domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 120mM；Pressure ambient NMR sample composition 20mM d-Tris-HCl(pH7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided
2KIQ Solution structure of the FF Domain 2 of human transcription elongation factor CA150 Deposited 2009-05-07	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 724–782（59 aa） Fragment：UNP residues 724-782	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；303 K；Ionic strength (raw mmCIF value) 25；Pressure ambient NMR sample composition 1 mM [U-100% 15N] CA150 FF2-1, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1 mM [U-100% 13C; U-100% 15N] CA150 FF2-2, 100% D2O \| 100% D2O	Resolution not provided
2KIS Solution structure of CA150 FF1 domain and FF1-FF2 interdomain linker Deposited 2009-05-08	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 659–724（66 aa） Fragment：FF1 domain: UNP residues 659-724	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；285 K；Ionic strength (raw mmCIF value) 0.137；Pressure ambient NMR sample composition 1-1.7 mM [U-99% 13C; U-99% 15N] protein, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
2MW9 NMR structure of FBP28 WW2 Y438R mutant Deposited 2014-11-03	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 428–464（37 aa） Fragment：WW 2 domain residues 428-464	Mutation：Y438R	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；285 K；Pressure ambient NMR sample composition 0.7 mM protein, 100 mM sodium chloride, 20 mM sodium phosphate, 1 mM sodium azide, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2MWA NMR structure of FBP28 WW2 mutant Y446L Deposited 2014-11-03	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 428–464（37 aa） Fragment：WW 2 domain residues 430-466	Mutation：Y446L	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；285 K；Pressure ambient NMR sample composition 0.7 mM protein, 100 mM sodium chloride, 20 mM sodium phosphate, 1 mM sodium azide, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2MWB FBP28 WW2 mutant W457F Deposited 2014-11-03	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 428–464（37 aa） Fragment：WW 2 domain residues 430-466	Mutation：W457F	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；285 K；Pressure ambient NMR sample composition 0.7 mM protein, 100 mM sodium chloride, 20 mM sodium phosphate, 1 mM sodium azide, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2MWD NMR structure of FBP28 WW2 mutant Y438R DNDC Deposited 2014-11-04	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 433–460（28 aa） Fragment：WW 2 domain residues 433-460	Mutation：Y438R	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；285 K；Pressure ambient NMR sample composition 0.7 mM protein, 100 mM sodium chloride, 20 mM sodium phosphate, 1 mM sodium azide, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2MWE NMR structure of FBP28 WW2 mutant Y438R, L453A DNDC Deposited 2014-11-04	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 433–460（28 aa） Fragment：WW 2 domain residues 433-460	Mutation：Y238R, L453A	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；285 K；Pressure ambient NMR sample composition 0.7 mM protein, 100 mM sodium chloride, 20 mM sodium phosphate, 1 mM sodium azide, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2MWF NMR structure of FBP28 WW2 mutant Y438R DN Deposited 2014-11-04	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 433–464（32 aa） Fragment：WW 2 domain residues 433-464	Mutation：Y438R	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；285 K；Pressure ambient NMR sample composition 0.7 mM protein, 100 mM sodium chloride, 20 mM sodium phosphate, 1 mM sodium azide, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2N4R NMR structure of Fbp28 WW domain L453D mutant Deposited 2015-07-01	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 428–464（37 aa）	Mutation：L453D	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.8；285 K；Pressure ambient NMR sample composition 500-1000 uM protein, 25 mM sodium phosphate, 100 mM sodium chloride, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2N4S NMR structure of Fbp28 WW domain L453E mutant Deposited 2015-07-01	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 428–464（37 aa）	Mutation：L453E	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.8；285 K；Pressure ambient NMR sample composition 500-1000 uM protein, 25 mM sodium phosphate, 100 mM sodium chloride, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2N4T NMR structure of Fbp28 WW domain L453W mutant Deposited 2015-07-01	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 428–464（37 aa）	Mutation：L453W	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.8；285 K；Pressure ambient NMR sample composition 500-1000 uM protein, 25 mM sodium phosphate, 100 mM sodium chloride, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2N4U NMR structure of Fbp28 WW domain E454Y mutant Deposited 2015-07-01	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 428–464（37 aa）	Mutation：E454Y	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.8；285 K；Pressure ambient NMR sample composition 500-1000 uM protein, 25 mM sodium phosphate, 100 mM sodium chloride, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2N4V NMR structure of Fbp28 WW domain T456D mutant Deposited 2015-07-01	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 428–464（37 aa）	Mutation：T456D	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.8；285 K；Pressure ambient NMR sample composition 500-1000 uM protein, 25 mM sodium phosphate, 100 mM sodium chloride, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2N4W NMR structure of Fbp28 WW domain T456Y mutant Deposited 2015-07-01	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 428–464（37 aa）	Mutation：T456Y	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.8；285 K；Pressure ambient NMR sample composition 500-1000 uM protein, 25 mM sodium phosphate, 100 mM sodium chloride, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2NNT General structural motifs of amyloid protofilaments Deposited 2006-10-24	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 428–464（37 aa） Fragment：second WW domain Chain B 428–464（37 aa） Fragment：second WW domain Chain C 428–464（37 aa） Fragment：second WW domain Chain D 428–464（37 aa） Fragment：second WW domain	Mutation：Y446F Mutation：Y446F Mutation：Y446F Mutation：Y446F	No recorded non-water small molecule	SOLID-STATE NMR NMR measurement conditions pH 7；285 K；Pressure 1 NMR sample composition uniform 13C,15N labeling, 15 mg fibre in phosphate buffer \| phosphate buffer NMR sample composition uniform 2H,13C,15N labeling, 15 mg fibre in phosphate buffer \| phosphate buffer NMR sample composition uniform 15N labeling, 13C labeling is based on 1,3[13C]-glycerol as carbon source for the bacteria, 15 mg fibre in phosphate buffer \| phosphate buffer NMR sample composition uniform 15N labeling, 13C labeling is based on 2[13C]-glycerol as carbon source for the bacteria, 15 mg fibre in phosphate buffer \| phosphate buffer	Resolution not provided
3Q1I Polo-like kinase I Polo-box domain in complex with FMPPPMSpSM phosphopeptide from TCERG1 Deposited 2010-12-17	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 99–107（9 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	1PE PENTAETHYLENE GLYCOL × 1 PEG DI(HYDROXYETHYL)ETHER × 1 PG0 2-(2-METHOXYETHOXY)ETHANOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；30% PEG400, 0.1M MES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 1.40 Å R-free 0.222
4FQG Crystal structure of the TCERG1 FF4-6 tandem repeat domain Deposited 2012-06-25	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 895–1081（187 aa） Fragment：TCERG1 FF4-6 tandem repeat domain (unp residues 895:1081)	Not recorded	NI NICKEL (II) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；277 K；0.016 M NiCl2, 0.1 M Tris-HCl, 16% polyethylene glycol monomethyl ether 2000, and 0.13 M glycine, pH 9, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.00 Å R-free 0.241
4FQG Crystal structure of the TCERG1 FF4-6 tandem repeat domain Deposited 2012-06-25	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 895–1081（187 aa） Fragment：TCERG1 FF4-6 tandem repeat domain (unp residues 895:1081)	Not recorded	NI NICKEL (II) ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；277 K；0.016 M NiCl2, 0.1 M Tris-HCl, 16% polyethylene glycol monomethyl ether 2000, and 0.13 M glycine, pH 9, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.00 Å R-free 0.241
7ABF Human pre-Bact-1 spliceosome core structure Deposited 2020-09-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 12 PDB declaration: pentadecameric	Chain A4 1–1077（1077 aa）	Not recorded	IHP INOSITOL HEXAKISPHOSPHATE × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.9 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å
7ABG Human pre-Bact-1 spliceosome Deposited 2020-09-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 54 PDB declaration: 58-meric	Chain A4 1–1098（1098 aa）	Not recorded	IHP INOSITOL HEXAKISPHOSPHATE × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 GTG 7-METHYL-GUANOSINE-5'-TRIPHOSPHATE-5'-GUANOSINE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.9 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 7.80 Å
8Q7N cryo-EM structure of the human spliceosomal B complex protomer (tri-snRNP core region) Deposited 2023-08-16	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 17 PDB declaration: 21-meric	Chain T 1–1098（1098 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.9 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
8QO9 Cryo-EM structure of a human spliceosomal B complex protomer Deposited 2023-09-28	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 66 PDB declaration: 71-meric	Chain T 1–1098（1098 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.9 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 5.29 Å
9R3D Cryo-EM structure of the human pre-Bact-OTS complex (whole map) Deposited 2025-05-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 14 PDB declaration: 17-meric	Chain T 1–1098（1098 aa）	Not recorded	IHP INOSITOL HEXAKISPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.9 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.12 Å
9R8V Cryo-EM structure of the human pre-Bact-OTS complex (whole map) Deposited 2025-05-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 59 PDB declaration: 63-meric	Chain T 1–1098（1098 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.9 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 8.50 Å

28 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TCRG1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 6–190； UniProt 661–845 Author chain B； PDBConstruct 6–190； UniProt 661–845

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.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	3hfh
Deposition date deposition_date	2009-05-11
Structure title title	Crystal structure of tandem FF domains
Keywords keywords	;helix bundle, Activator, Alternative splicing, Coiled coil, Nucleus, Phosphoprotein, Repressor, Transcription, Transcription regulation, TRANSCRIPTION REGULATOR ;; TRANSCRIPTION REGULATOR
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	56.12 Å
Radius of gyration Rg (electron density) rg_electron	57.54 Å
Forward intensity I(0) i0	29334500.00
Molecular weight molecular_weight	45054.0 kDa
Excluded volume excluded_volume	56825 Å³
Envelope volume envelope_volume	120420 Å³
Hydration-shell volume shell_volume	21206 Å³
Envelope diameter envelope_diameter	185.4 Å
Shell Rg shell_rg	44.70 Å
Envelope Rg envelope_rg	56.36 Å
Shape Rg shape_rg	57.65 Å
Total Rg total_rg	56.45 Å
Total atoms total_atoms	3123
Residues n_residues	287
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	176.7 Å
Rg (real space) rg_real	57.21 Å
Rg uncertainty (real space) rg_real_error	2.44 Å
I(0) (real space) i0_real	2.9330e+07
I(0) uncertainty (real space) i0_real_error	6.0270e+05
Rg (reciprocal space) rg_reciprocal	55.17 Å
I(0) (reciprocal space) i0_reciprocal	29240000.0000
Solution quality estimate total_estimate	0.5671
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	18.9 Å
Skewness Skewness skewness	0.458
Kurtosis Kurtosis kurtosis	-0.777
Angular range angular_range	— – 0.1400 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	1200000.0000
Real-space data points n_real_points	29
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.084; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.116; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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8. Citations (1)

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Unit-cell length a length_a	141.300 Å
Unit-cell length b length_b	141.300 Å
Unit-cell length c length_c	155.420 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	24

Space group space_group	P 6 2 2
Space-group number int_tables_number	177
Crystal system crystal_system	—

Resolution resolution	2.703 Å
Low-resolution limit resolution_low	20.016 Å
R factor r_factor	0.2353
R_work r_work	0.2300
R_free r_free	0.2833

Description description	Transcription elongation regulator 1
Molecular weight formula_weight	23830.7 kDa
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	3178

Crystal structure of tandem FF domains

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

Transcription elongation regulator 1

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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	55

fit	/app/data/saxs_computation/hf/3hfh/3hfh.fit
pddf	/app/data/pr_computation/hf/3hfh/3hfh.pr.out
profile	/app/data/saxs_computation/hf/3hfh/3hfh.dat