SAXSdb — 5lm7

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

Transcription termination/antitermination protein NusA

Escherichia coli O157:H7

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein–RNA	Heteromer	Protein 4 RNA 1	N utilization substance protein B homolog × 1 （B7MD74） 30S ribosomal protein S10 × 1 （B7MCT6） Antitermination protein N × 1 （P03045） RNA (29-MER) × 1	Consistent with all polymers
2	Protein–RNA	Heteromer	Protein 4 RNA 1	N utilization substance protein B homolog × 1 （B7MD74） 30S ribosomal protein S10 × 1 （B7MCT6） Antitermination protein N × 1 （P03045） RNA (29-MER) × 1	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	NUSA_ECO57
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–428； UniProt 1–426 Author chain C； PDBConstruct 3–428； UniProt 1–426

N utilization substance protein B homolog

Escherichia coli O45:K1 (strain S88 / ExPEC)

UniProt B7MD74

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein–RNA	Heteromer	Protein 4 RNA 1	Transcription termination/antitermination protein NusA × 1 （P0AFF8） 30S ribosomal protein S10 × 1 （B7MCT6） Antitermination protein N × 1 （P03045） RNA (29-MER) × 1	Consistent with all polymers
2	Protein–RNA	Heteromer	Protein 4 RNA 1	Transcription termination/antitermination protein NusA × 1 （P0AFF8） 30S ribosomal protein S10 × 1 （B7MCT6） Antitermination protein N × 1 （P03045） RNA (29-MER) × 1	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	NUSB_ECO45
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 3–141； UniProt 1–139 Author chain D； PDBConstruct 3–141； UniProt 1–139

30S ribosomal protein S10

Escherichia coli O45:K1 (strain S88 / ExPEC)

UniProt B7MCT6

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein–RNA	Heteromer	Protein 4 RNA 1	Transcription termination/antitermination protein NusA × 1 （P0AFF8） N utilization substance protein B homolog × 1 （B7MD74） Antitermination protein N × 1 （P03045） RNA (29-MER) × 1	Consistent with all polymers
2	Protein–RNA	Heteromer	Protein 4 RNA 1	Transcription termination/antitermination protein NusA × 1 （P0AFF8） N utilization substance protein B homolog × 1 （B7MD74） Antitermination protein N × 1 （P03045） RNA (29-MER) × 1	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	RS10_ECO45
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain E； PDBConstruct 6–108； UniProt 1–103 Author chain J； PDBConstruct 6–108； UniProt 1–103

Antitermination protein N

Enterobacteria phage lambda

UniProt P03045

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein–RNA	Heteromer	Protein 4 RNA 1	Transcription termination/antitermination protein NusA × 1 （P0AFF8） N utilization substance protein B homolog × 1 （B7MD74） 30S ribosomal protein S10 × 1 （B7MCT6） RNA (29-MER) × 1	Consistent with all polymers
2	Protein–RNA	Heteromer	Protein 4 RNA 1	Transcription termination/antitermination protein NusA × 1 （P0AFF8） N utilization substance protein B homolog × 1 （B7MD74） 30S ribosomal protein S10 × 1 （B7MCT6） RNA (29-MER) × 1	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	REGN_LAMBD
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain F； PDBConstruct 6–89； UniProt 1–84 Author chain N； PDBConstruct 6–89； UniProt 1–84

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	5lm7
Deposition date deposition_date	2016-07-29
Structure title title	Crystal structure of the lambda N-Nus factor complex
Keywords keywords	Transcription regulation antitermination Nus proteins Phage lambda N protein, transcription; TRANSCRIPTION
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

5lm7__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

5lm7__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

5lm7__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	37.67 Å
Rg (electron density)	37.47 Å
Total Rg	37.68 Å
Atom count	6488
Residues	772
Excluded volume	113040 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`5lm7__assembly_1__model_1`	pentameric （5）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`5lm7__assembly_2__model_1`	pentameric （5）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	Transcription termination/antitermination protein NusA
Molecular weight formula_weight	47666.6 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C
Atom count atom_count	12834

GAMNKEILAVVEAVSNEKALPREKIFEALESALATATKKKYEQEIDVRVQIDRKSGDFDTFRRWLVVDEVTQPTKEITLEAARYEDESLNLGDYVEDQIESVTFDRITTQTAKQVIVQKVREAERAMVVDQFREHEGEIITGVVKKVNRDNISLDLGNNAEAVILREDMLPRENFRPGDRVRGVLYSVRPEARGAQLFVTRSKPEMLIELFRIEVPEIGEEVIEIKAAARDPGSRAKIAVKTNDKRIDPVGACVGMRGARVQAVSTELGGERIDIVLWDDNPAQFVINAMAPADVASIVVDEDKHTMDIAVEAGNLAQAIGRNGQNVRLASQLSGWELNVMTVDDLQAKHQAEAHAAIDTFTKYLDIDEDFATVLVEEGFSTLEELAYVPMKELLEIEGLDEPTVEALRERAKNALATIAQAQEESLG

Source Source

Source organism organism	Escherichia coli O157:H7
NCBI taxonomy ID ncbi_taxonomy_id	83334
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	N utilization substance protein B homolog
Molecular weight formula_weight	15838.2 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D

GAMKPAARRRARECAVQALYSWQLSQNDIADVEYQFLAEQDVKDVDVLYFRELLAGVATNTAYLDGLMKPYLSRLLEELGQVEKAVLRIALYELSKRSDVPYKVAINEAIELAKSFGAEDSHKFVNGVLDKAAPVIRPNKK

Source Source

Source organism organism	Escherichia coli O45:K1 (strain S88 / ExPEC)
NCBI taxonomy ID ncbi_taxonomy_id	585035
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 polymer

Description description	30S ribosomal protein S10
Molecular weight formula_weight	12167.1 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	J,E

GPLGSMQNQRIRIRLKAFDHRLIDQATAEIVETAKRTGAQVRGPIPLPTRKERFTVLISPHVNKDARDQYEIRTHLRLVDIVEPTEKTVDALMRLDLAAGVDVQISLG

Source Source

Source organism organism	Escherichia coli O45:K1 (strain S88 / ExPEC)
NCBI taxonomy ID ncbi_taxonomy_id	585035
Host organism host_organism	Escherichia coli

Entity 4 Entity 4 polymer

Description description	Antitermination protein N
Molecular weight formula_weight	10279.8 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	N,F

GPLGSMDAQTRRRERRAEKQAQWKAANPLLVGVSAKPVNRPILSLNRKPKSRVESALNPIDLTVLAEYHKQIESNLQRIERKNQRTWYS

Source Source

Source organism organism	Enterobacteria phage lambda
NCBI taxonomy ID ncbi_taxonomy_id	10710
Host organism host_organism	Escherichia coli

Entity 5 Entity 5 polymer

Description description	RNA (29-MER)
Molecular weight formula_weight	9573.7 kDa
Source method src_method	syn
Copy count entity_count	2

Polymer Polymer

Polymer type type	polyribonucleotide
Chain IDs strand_id	R,G

CUCUUUAACAUUAAGCCCUGAAGAAGGGCC

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6. Fold Classification (SCOP + CATH) 10 domains

CATH v4.4 (10 domains)

Domain ID domain_id	5lm7A01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1480 — N Utilization Substance Protein A; Chain:P; domain 4
Homologous superfamily homologous superfamily	10 — NusA, N-terminal domain

Domain ID domain_id	5lm7A02
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	5lm7A03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily	20 — 5' to 3' exonuclease, C-terminal subdomain

Domain ID domain_id	5lm7B00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	940 — N-utilizing Substance Protein B Homolog; Chain A
Homologous superfamily homologous superfamily	10 — NusB-like

Domain ID domain_id	5lm7C01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1480 — N Utilization Substance Protein A; Chain:P; domain 4
Homologous superfamily homologous superfamily	10 — NusA, N-terminal domain

Domain ID domain_id	5lm7C02
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	5lm7C03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily	20 — 5' to 3' exonuclease, C-terminal subdomain

Domain ID domain_id	5lm7D00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	940 — N-utilizing Substance Protein B Homolog; Chain A
Homologous superfamily homologous superfamily	10 — NusB-like

Domain ID domain_id	5lm7E00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	600 — Ribosomal protein S10

Domain ID domain_id	5lm7J00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	600 — Ribosomal protein S10

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Unit-cell length a length_a	95.776 Å
Unit-cell length b length_b	101.803 Å
Unit-cell length c length_c	279.918 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	3.350 Å
Low-resolution limit resolution_low	39.520 Å
R factor r_factor	0.2986
R_work r_work	0.2966
R_free r_free	0.3354

Crystal structure of the lambda N-Nus factor complex

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

Transcription termination/antitermination protein NusA

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

N utilization substance protein B homolog

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

30S ribosomal protein S10

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Antitermination protein N

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

5lm7__assembly_1__model_1

5lm7__assembly_1__model_1 | I(q)

5lm7__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 polymer

Polymer Polymer

Source Source

Entity 5 Entity 5 polymer

Polymer Polymer

6. Fold Classification (SCOP + CATH) 10 domains

CATH v4.4 (10 domains)

7. Citations (1)