SAXSdb — 6zca

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

;Probable DNA-directed RNA polymerase subunit delta,Probable DNA-directed RNA polymerase subunit delta,Probable DNA-directed RNA polymerase subunit delta ;

OrganismNot specified

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 heterocomplex Heteromer Protein × 7 PDB declaration: heptameric（7） Consistent with protein copy count	Chain D； UniProt 1–92	Not recorded	RNA polymerase subunit omega × 1 （A0A410WI33） DNA-directed RNA polymerase subunit alpha × 2 （A0A063XB83） DNA-directed RNA polymerase subunit beta × 1 （A0A2J0WBQ0） ;DNA-directed RNA polymerase subunit beta' ; × 1 （A0A063XB23） DNA helicase × 1 （A0A164TSE8） ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.6 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 4.20 Å

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	A0A0D1KIU7_BACIU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain D； PDBConstruct 1–92； UniProt 1–92

RNA polymerase subunit omega

OrganismNot specified

UniProt A0A410WI33

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 heterocomplex Heteromer Protein × 7 PDB declaration: heptameric（7） Consistent with protein copy count	Chain E； UniProt 1–69	Not recorded	;Probable DNA-directed RNA polymerase subunit delta,Probable DNA-directed RNA polymerase subunit delta,Probable DNA-directed RNA polymerase subunit delta ; × 1 （A0A0D1KIU7） DNA-directed RNA polymerase subunit alpha × 2 （A0A063XB83） DNA-directed RNA polymerase subunit beta × 1 （A0A2J0WBQ0） ;DNA-directed RNA polymerase subunit beta' ; × 1 （A0A063XB23） DNA helicase × 1 （A0A164TSE8） ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.6 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 4.20 Å

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 6ZCA	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6ZFB Structure of the B. subtilis RNA POLYMERASE in complex with HelD (dimer) Deposited 2020-06-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: tetradecameric	Chain E 1–69（69 aa） Chain e 1–69（69 aa）	Not recorded	ZN ZINC ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	A0A410WI33_BACVA
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain E； PDBConstruct 1–69； UniProt 1–69

DNA-directed RNA polymerase subunit alpha

OrganismNot specified

UniProt A0A063XB83

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 heterocomplex Heteromer Protein × 7 PDB declaration: heptameric（7） Consistent with protein copy count	Chain U； UniProt 1–314 Chain V； UniProt 1–314	Not recorded	;Probable DNA-directed RNA polymerase subunit delta,Probable DNA-directed RNA polymerase subunit delta,Probable DNA-directed RNA polymerase subunit delta ; × 1 （A0A0D1KIU7） RNA polymerase subunit omega × 1 （A0A410WI33） DNA-directed RNA polymerase subunit beta × 1 （A0A2J0WBQ0） ;DNA-directed RNA polymerase subunit beta' ; × 1 （A0A063XB23） DNA helicase × 1 （A0A164TSE8） ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.6 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 4.20 Å

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 6ZCA	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6ZFB Structure of the B. subtilis RNA POLYMERASE in complex with HelD (dimer) Deposited 2020-06-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: tetradecameric	Chain U 1–314（314 aa） Chain V 1–314（314 aa） Chain u 1–314（314 aa） Chain v 1–314（314 aa）	Not recorded	ZN ZINC ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	A0A063XB83_BACIU
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain U； PDBConstruct 1–314； UniProt 1–314 Author chain V； PDBConstruct 1–314； UniProt 1–314

DNA-directed RNA polymerase subunit beta

OrganismNot specified

UniProt A0A2J0WBQ0

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 heterocomplex Heteromer Protein × 7 PDB declaration: heptameric（7） Consistent with protein copy count	Chain X； UniProt 1–1193	Not recorded	;Probable DNA-directed RNA polymerase subunit delta,Probable DNA-directed RNA polymerase subunit delta,Probable DNA-directed RNA polymerase subunit delta ; × 1 （A0A0D1KIU7） RNA polymerase subunit omega × 1 （A0A410WI33） DNA-directed RNA polymerase subunit alpha × 2 （A0A063XB83） ;DNA-directed RNA polymerase subunit beta' ; × 1 （A0A063XB23） DNA helicase × 1 （A0A164TSE8） ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.6 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 4.20 Å

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 6ZCA	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6WVJ Cryo-EM structure of Bacillus subtilis RNA Polymerase elongation complex Deposited 2020-05-06	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: octameric	Chain C 1–1193（1193 aa）	Not recorded	ZN ZINC ION × 2 MG MAGNESIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.8 cryo-EM vitrification conditions Cryogen ETHANE；Sample loading volume ranged between 2 and 3 microlitres. Samples were blotted for 5 seconds prior to vitrification.	Resolution 3.36 Å
6ZFB Structure of the B. subtilis RNA POLYMERASE in complex with HelD (dimer) Deposited 2020-06-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: tetradecameric	Chain X 1–1193（1193 aa） Chain x 1–1193（1193 aa）	Not recorded	ZN ZINC ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	A0A2J0WBQ0_BACIU
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain X； PDBConstruct 1–1193； UniProt 1–1193

;DNA-directed RNA polymerase subunit beta' ;

OrganismNot specified

UniProt A0A063XB23

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 heterocomplex Heteromer Protein × 7 PDB declaration: heptameric（7） Consistent with protein copy count	Chain Y； UniProt 1–1199	Not recorded	;Probable DNA-directed RNA polymerase subunit delta,Probable DNA-directed RNA polymerase subunit delta,Probable DNA-directed RNA polymerase subunit delta ; × 1 （A0A0D1KIU7） RNA polymerase subunit omega × 1 （A0A410WI33） DNA-directed RNA polymerase subunit alpha × 2 （A0A063XB83） DNA-directed RNA polymerase subunit beta × 1 （A0A2J0WBQ0） DNA helicase × 1 （A0A164TSE8） ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.6 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 4.20 Å

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 6ZCA	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6WVJ Cryo-EM structure of Bacillus subtilis RNA Polymerase elongation complex Deposited 2020-05-06	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: octameric	Chain D 1–1199（1199 aa）	Not recorded	ZN ZINC ION × 2 MG MAGNESIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.8 cryo-EM vitrification conditions Cryogen ETHANE；Sample loading volume ranged between 2 and 3 microlitres. Samples were blotted for 5 seconds prior to vitrification.	Resolution 3.36 Å
6ZFB Structure of the B. subtilis RNA POLYMERASE in complex with HelD (dimer) Deposited 2020-06-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: tetradecameric	Chain Y 1–1199（1199 aa） Chain y 1–1199（1199 aa）	Not recorded	ZN ZINC ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	A0A063XB23_BACIU
Isoform	—
PDB entities	5
Chains and sequence ranges	Author chain Y； PDBConstruct 1–1199； UniProt 1–1199

DNA helicase

OrganismNot specified

UniProt A0A164TSE8

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 heterocomplex Heteromer Protein × 7 PDB declaration: heptameric（7） Consistent with protein copy count	Chain H； UniProt 1–774	Not recorded	;Probable DNA-directed RNA polymerase subunit delta,Probable DNA-directed RNA polymerase subunit delta,Probable DNA-directed RNA polymerase subunit delta ; × 1 （A0A0D1KIU7） RNA polymerase subunit omega × 1 （A0A410WI33） DNA-directed RNA polymerase subunit alpha × 2 （A0A063XB83） DNA-directed RNA polymerase subunit beta × 1 （A0A2J0WBQ0） ;DNA-directed RNA polymerase subunit beta' ; × 1 （A0A063XB23） ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.6 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 4.20 Å

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 6ZCA	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6VSX X-ray crystal structure of the C-terminal domain of Bacillus subtilis RNA polymerase binding helicase HelD Deposited 2020-02-12	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 608–774（167 aa）	Not recorded	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.2；300 K；0.1M Na/K phosphate, pH 6.2, 0.2 M NaCl, 50 % PEG200	Resolution 2.00 Å R-free 0.202
6ZFB Structure of the B. subtilis RNA POLYMERASE in complex with HelD (dimer) Deposited 2020-06-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: tetradecameric	Chain H 1–774（774 aa） Chain h 1–774（774 aa）	Not recorded	ZN ZINC ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	A0A164TSE8_BACIU
Isoform	—
PDB entities	6
Chains and sequence ranges	Author chain H； PDBConstruct 1–774； UniProt 1–774

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	6zca
Deposition date deposition_date	2020-06-10
Structure title title	Structure of the B. subtilis RNA POLYMERASE in complex with HelD (monomer)
Keywords keywords	TRANSCRIPTION/DNA/RNA, DNA-DEPENDENT RNA POLYMERASE, BACTERIAL, TRANSCRIPTION, Helicase; TRANSCRIPTION
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	52.98 Å
Radius of gyration Rg (electron density) rg_electron	52.57 Å
Forward intensity I(0) i0	2377160000.00
Molecular weight molecular_weight	408070.0 kDa
Excluded volume excluded_volume	511210 Å³
Envelope volume envelope_volume	770100 Å³
Hydration-shell volume shell_volume	118610 Å³
Envelope diameter envelope_diameter	170.1 Å
Shell Rg shell_rg	59.06 Å
Envelope Rg envelope_rg	51.17 Å
Shape Rg shape_rg	52.58 Å
Total Rg total_rg	52.72 Å
Total atoms total_atoms	28721
Residues n_residues	3640
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	173.4 Å
Rg (real space) rg_real	52.79 Å
Rg uncertainty (real space) rg_real_error	1.16 Å
I(0) (real space) i0_real	2.3770e+09
I(0) uncertainty (real space) i0_real_error	4.4500e+07
Rg (reciprocal space) rg_reciprocal	53.13 Å
I(0) (reciprocal space) i0_reciprocal	2378000000.0000
Solution quality estimate total_estimate	0.8771
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	69.4 Å
Skewness Skewness skewness	0.185
Kurtosis Kurtosis kurtosis	-0.424
Angular range angular_range	— – 0.1500 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	320000000.0000
Real-space data points n_real_points	31
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.865; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.963; Smooth: 0.840

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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	;Probable DNA-directed RNA polymerase subunit delta,Probable DNA-directed RNA polymerase subunit delta,Probable DNA-directed RNA polymerase subunit delta ;
Molecular weight formula_weight	14914.2 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D
Atom count atom_count	28721

MGIKQYSQEELKEMALVEIAHELFEEHKKPVPFQELLNEIASLLGVKKEELGDRIAQFYTDLNIDGRFLALSDQTWGLRSWYPYDQLDEETQXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX

Entity 2 Entity 2 polymer

Description description	RNA polymerase subunit omega
Molecular weight formula_weight	8228.4 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E

MIYKVFYQEKADEVPVREKTDSLYIEGVSERDVRTKLKEKKLNIEFITPVNGAFLEYEQQSENFKVLEL

Entity 3 Entity 3 polymer

Description description	DNA-directed RNA polymerase subunit alpha
Molecular weight formula_weight	34842.4 kDa
EC 编号 ec_number	2.7.7.6
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	U,V

MIEIEKPKIETVEISDDAKFGKFVVEPLERGYGTTLGNSLRRILLSSLPGAAVTSIQIDGVLHEFSTIEGVVEDVTTIILHIKKLALKIYSDEEKTLEIDVQGEGTVTAADITHDSDVEILNPDLHIATLGENASFRVRLTAQRGRGYTPADANKRDDQPIGVIPIDSIYTPVSRVSYQVENTRVGQVANYDKLTLDVWTDGSTGPKEAIALGSKILTEHLNIFVGLTDEAQHAEIMVEKEEDQKEKVLEMTIEELDLSVRSYNCLKRAGINTVQELANKTEEDMMKVRNLGRKSLEEVKAKLEELGLGLRKDD

Entity 4 Entity 4 polymer

Description description	DNA-directed RNA polymerase subunit beta
Molecular weight formula_weight	133847.9 kDa
EC 编号 ec_number	2.7.7.6
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	X

MTGQLVQYGRHRQRRSYARISEVLELPNLIEIQTSSYQWFLDEGLREMFQDISPIEDFTGNLSLEFIDYSLGEPKYPVEESKERDVTYSAPLRVKVRLINKETGEVKDQDVFMGDFPIMTDTGTFIINGAERVIVSQLVRSPSVYFSGKVDKNGKKGFTATVIPNRGAWLEYETDAKDVVYVRIDRTRKLPVTVLLRALGFGSDQEILDLIGENEYLRNTLDKDNTENSDKALLEIYERLRPGEPPTVENAKSLLDSRFFDPKRYDLANVGRYKINKKLHIKNRLFNQRLAETLVDPETGEILAEKGQILDRRTLDKVLPYLENGIGFRKLYPNGGVVEDEVTLQSIKIFAPTDQEGEQVINVIGNAYIEEEIKNITPADIISSISYFFNLLHGVGDTDDIDHLGNRRLRSVGELLQNQFRIGLSRMERVVRERMSIQDTNTITPQQLINIRPVIASIKEFFGSSQLSQFMDQTNPLAELTHKRRLSALGPGGLTRERAGMEVRDVHYSHYGRMCPIETPEGPNIGLINSLSSYAKVNRFGFIETPYRRVDPETGKVTGRIDYLTADEEDNYVVAQANARLDDEGAFIDDSIVARFRGENTVVSRNRVDYMDVSPKQVVSAATACIPFLENDDSNRALMGANMQRQAVPLMQPEAPFVGTGMEYVSGKDSGAAVICKHPGIVERVEAKNVWVRRYEEVDGQKVKGNLDKYSLLKFVRSNQGTCYNQRPIVSVGDEVVKGEILADGPSMELGELALGRNVMVGFMTWDGYNYEDAIIMSERLVKDDVYTSIHIEEYESEARDTKLGPEEITRDIPNVGEDALRNLDDRGIIRIGAEVKDGDLLVGKVTPKGVTELTAEERLLHAIFGEKAREVRDTSLRVPHGGGGIIHDVKVFNREDGDELPPGVNQLVRVYIVQKRKISEGDKMAGRHGNKGVISKILPEEDMPYLPDGTPIDIMLNPLGVPSRMNIGQVLELHMGMAARYLGIHIASPVFDGAREEDVWETLEEAGMSRDAKTVLYDGRTGEPFDNRVSVGIMYMIKLAHMVDDKLHARSTGPYSLVTQQPLGGKAQFGGQRFGEMEVWALEAYGAAYTLQEILTVKSDDVVGRVKTYEAIVKGDNVPEPGVPESFKVLIKELQSLGMDVKILSGDEEEIEMRDLEDEEDAKQADGLALSGDEEPEETASADVERDVVTKE

Entity 5 Entity 5 polymer

Description description	;DNA-directed RNA polymerase subunit beta' ;
Molecular weight formula_weight	134445.0 kDa
EC 编号 ec_number	2.7.7.6
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	Y

MLDVNNFEYMNIGLASPDKIRSWSFGEVKKPETINYRTLKPEKDGLFCERIFGPTKDWECHCGKYKRVRYKGVVCDRCGVEVTRAKVRRERMGHIELAAPVSHIWYFKGIPSRMGLVLDMSPRALEEVIYFASYVVTDPANTPLEKKQLLSEKEYRAYLDKYGNKFQASMGAEAIHKLLQDIDLVKEVDMLKEELKTSQGQRRTRAIKRLEVLEAFRNSGNKPSWMILDVLPVIPPELRPMVQLDGGRFATSDLNDLYRRVINRNNRLKRLLDLGAPSIIVQNEKRMLQEAVDALIDNGRRGRPVTGPGNRPLKSLSHMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPHLKMYQCGLPKEMALELFKPFVMKELVEKGLAHNIKSAKRKIERVQPEVWDVLESVIKEHPVLLNRAPTLHRLGIQAFEPTLVEGRAIRLHPLVCTAYNADFDGDQMAVHVPLSAEAQAEARILMLAAQNILNPKDGKPVVTPSQDMVLGNYYLTLERAGAVGEGMVFKNTDEALLAYQNGYVHLHTRVAVAANSLKNVTFTEEQRSKLLITTVGKLVFNEILPESFPYMNEPTKSNIEEKTPDRFFLEKGADVKAVIAQQPINAPFKKGILGKIIAEIFKRFHITETSKMLDRMKNLGFKYSTKAGITVGVSDIVVLDDKQEILEEAQSKVDNVMKQFRRGLITEEERYERVISIWSAAKDVIQGKLMKSLDELNPIYMMSDSGARGNASNFTQLAGMRGLMANPAGRIIELPIKSSFREGLTVLEYFISTHGARKGLADTALKTADSGYLTRRLVDVAQDVIIRETDCGTDRGILAKPLKEGTETIERLEERLIGRFARKQVKHPETGEVLVNENELIDEDKALEIVEAGIEEVWIRSAFTCNTPHGVCKRCYGRNLATGSDVEVGEAVGIIAAQSIGEPGTQLTMRTFHTGGVAGDDITQGLPRIQELFEARNPKGQATITEIDGTVVEINEVRDKQQEIVVQGAVETRSYTAPYNSRLKVAEGDKITRGQVLTEGSIDPKELLKVTDLTTVQEYLLHEVQKVYRMQGVEIGDKHVEVMVRQMLRKVRVIDAGDTDVLPGTLLDIHQFTEANKKVLLEGNRPATGRPVLLGITKASLETDSFLSAASFQETTRVLTDAAIKGKRDELLGLKENVIIGKLVPAGTGMMKYRKVKPVSNVQPTDDMVPVE

Entity 6 Entity 6 polymer

Description description	DNA helicase
Molecular weight formula_weight	90052.5 kDa
EC 编号 ec_number	3.6.4.12
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H

MNQQDKEWKEEQSRIDEVLKELEKKERFLETSAGGLKHDIIGLRKSFWEDVKVNFDDAHEAIETMASIKQQAELLSDREHNHRRMDQQLKRIHQLKKSPYFGRIDFIENGEEQAERIYIGLASCLDEKEEHFLIYDWRAPISSLYYNYSPGKAEYEVPGETIEGEMVLKRQFMIKNGTLKAMFNTDMTIGDEMLQEVLSHHSDTQMKNIVSTIQKEQNQIIRNEKSKILIVQGAAGSGKTSAALQRVAYLLYRHRGVIDAGQIVLFSPNFLFNSYVSSVLPELGEENMEQATFQEYIEHRLGRKFKCESPFDQLEYCLTETKGGDFPTRLAGITWKAGLSFQQFINEYVTRLSSEGMIFKNIIFRGQKLITKEQIQSYFYSLDQNHSIPNRMEQTAKWLLSELNKLEKKERRKDWVVHEAELLDKEDYLDVYKKLQERKRFSESTFNDYQREQQLLAAIIVKKAFKPLKQAVRLLAFLDVTQLYLQLFSGWGGKFQHEKMDAIGELTRSAFTDNKLLYEDAAPFLYMQDLIEGRKKNTKIKHLFIDEAQDYSPFQMAYMRSIFPAASMTVLGDINQSIYAHTINGDQRMDACFEDEPAEYVRLKRTYRSTRQIVEFTKAMLQDGADIEPFNRSGEMPLVVKTEGHESLCQKLAQEIGRLKKKGHETIAVICKTAHQCIQAHAHMSEYTDVRLIHKENQPFQKGVCVIPVYLAKGIEFDAVLVYDASEEHYHTEHDRRLLYTACTRAMHMLAVFYTGEASPFVTAVPPHLYQIAE

Entity 7 Entity 7 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	1

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	—

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

Resolution resolution	4.200 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Resolution resolution	4.20 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	81279

fit	/app/data/saxs_computation/zc/6zca/6zca.fit
pddf	/app/data/pr_computation/zc/6zca/6zca.pr.out
profile	/app/data/saxs_computation/zc/6zca/6zca.dat

Structure of the B. subtilis RNA POLYMERASE in complex with HelD (monomer)

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

;Probable DNA-directed RNA polymerase subunit delta,Probable DNA-directed RNA polymerase subunit delta,Probable DNA-directed RNA polymerase subunit delta ;

State in the Current Structure

Other States of the Same Protein in the Database

RNA polymerase subunit omega

State in the Current Structure

Other States of the Same Protein in the Database

DNA-directed RNA polymerase subunit alpha

State in the Current Structure

Other States of the Same Protein in the Database

DNA-directed RNA polymerase subunit beta

State in the Current Structure

Other States of the Same Protein in the Database

;DNA-directed RNA polymerase subunit beta' ;

State in the Current Structure

Other States of the Same Protein in the Database

DNA helicase

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (7)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 polymer

Polymer Polymer

Entity 5 Entity 5 polymer

Polymer Polymer

Entity 6 Entity 6 polymer

Polymer Polymer

Entity 7 Entity 7 non-polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)