9yx5

Structure of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis with MSMEG_0435-MSMEG_0436 bound

Method: ELECTRON MICROSCOPY

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

Biotin-dependent acyl-coenzyme A carboxylase alpha3 subunit

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 26	Acetyl-/propionyl-coenzyme A carboxylase AccE5 × 2 （A0QTE6） Propionyl-CoA carboxylase beta chain × 2 （A0R616） Propionyl-CoA carboxylase beta chain × 4 （A0QTE7） Allophanate hydrolase subunit 2 × 2 （A0QPL0） Allophanate hydrolase subunit 1 × 2 （A0QPL1） ;S-{(3S,5S,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5,10,14-tetraoxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} (11E,14E,16E)-icosa-11,14,16-trienethioate (non-preferred name) ; × 2 propionyl Coenzyme A × 4 BIOTIN × 5 BICARBONATE ION × 2 ADENOSINE-5'-TRIPHOSPHATE × 2 MAGNESIUM ION × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0QTE1_MYCS2
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–598； UniProt 1–598 Author chain B； PDBConstruct 1–598； UniProt 1–598 Author chain C； PDBConstruct 1–598； UniProt 1–598 Author chain D； PDBConstruct 1–598； UniProt 1–598 Author chain I； PDBConstruct 1–598； UniProt 1–598 Author chain J； PDBConstruct 1–598； UniProt 1–598 Author chain K； PDBConstruct 1–598； UniProt 1–598 Author chain L； PDBConstruct 1–598； UniProt 1–598 Author chain Q； PDBConstruct 1–598； UniProt 1–598 Author chain R； PDBConstruct 1–598； UniProt 1–598 Author chain S； PDBConstruct 1–598； UniProt 1–598 Author chain T； PDBConstruct 1–598； UniProt 1–598 Author chain U； PDBConstruct 1–598； UniProt 1–598 Author chain X； PDBConstruct 1–598； UniProt 1–598

Acetyl-/propionyl-coenzyme A carboxylase AccE5

OrganismNot specified

UniProt A0QTE6

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 26	Biotin-dependent acyl-coenzyme A carboxylase alpha3 subunit × 14 （A0QTE1） Propionyl-CoA carboxylase beta chain × 2 （A0R616） Propionyl-CoA carboxylase beta chain × 4 （A0QTE7） Allophanate hydrolase subunit 2 × 2 （A0QPL0） Allophanate hydrolase subunit 1 × 2 （A0QPL1） ;S-{(3S,5S,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5,10,14-tetraoxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} (11E,14E,16E)-icosa-11,14,16-trienethioate (non-preferred name) ; × 2 propionyl Coenzyme A × 4 BIOTIN × 5 BICARBONATE ION × 2 ADENOSINE-5'-TRIPHOSPHATE × 2 MAGNESIUM ION × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0QTE6_MYCS2
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain E； PDBConstruct 1–94； UniProt 1–94 Author chain P； PDBConstruct 1–94； UniProt 1–94

Propionyl-CoA carboxylase beta chain

OrganismNot specified

UniProt A0R616

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 26	Biotin-dependent acyl-coenzyme A carboxylase alpha3 subunit × 14 （A0QTE1） Acetyl-/propionyl-coenzyme A carboxylase AccE5 × 2 （A0QTE6） Propionyl-CoA carboxylase beta chain × 4 （A0QTE7） Allophanate hydrolase subunit 2 × 2 （A0QPL0） Allophanate hydrolase subunit 1 × 2 （A0QPL1） ;S-{(3S,5S,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5,10,14-tetraoxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} (11E,14E,16E)-icosa-11,14,16-trienethioate (non-preferred name) ; × 2 propionyl Coenzyme A × 4 BIOTIN × 5 BICARBONATE ION × 2 ADENOSINE-5'-TRIPHOSPHATE × 2 MAGNESIUM ION × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0R616_MYCS2
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain F； PDBConstruct 1–517； UniProt 1–517 Author chain O； PDBConstruct 1–517； UniProt 1–517

Propionyl-CoA carboxylase beta chain

OrganismNot specified

UniProt A0QTE7

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 26	Biotin-dependent acyl-coenzyme A carboxylase alpha3 subunit × 14 （A0QTE1） Acetyl-/propionyl-coenzyme A carboxylase AccE5 × 2 （A0QTE6） Propionyl-CoA carboxylase beta chain × 2 （A0R616） Allophanate hydrolase subunit 2 × 2 （A0QPL0） Allophanate hydrolase subunit 1 × 2 （A0QPL1） ;S-{(3S,5S,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5,10,14-tetraoxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} (11E,14E,16E)-icosa-11,14,16-trienethioate (non-preferred name) ; × 2 propionyl Coenzyme A × 4 BIOTIN × 5 BICARBONATE ION × 2 ADENOSINE-5'-TRIPHOSPHATE × 2 MAGNESIUM ION × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0QTE7_MYCS2
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain G； PDBConstruct 1–542； UniProt 1–542 Author chain H； PDBConstruct 1–542； UniProt 1–542 Author chain M； PDBConstruct 1–542； UniProt 1–542 Author chain N； PDBConstruct 1–542； UniProt 1–542

Allophanate hydrolase subunit 2

OrganismNot specified

UniProt A0QPL0

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 26	Biotin-dependent acyl-coenzyme A carboxylase alpha3 subunit × 14 （A0QTE1） Acetyl-/propionyl-coenzyme A carboxylase AccE5 × 2 （A0QTE6） Propionyl-CoA carboxylase beta chain × 2 （A0R616） Propionyl-CoA carboxylase beta chain × 4 （A0QTE7） Allophanate hydrolase subunit 1 × 2 （A0QPL1） ;S-{(3S,5S,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5,10,14-tetraoxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} (11E,14E,16E)-icosa-11,14,16-trienethioate (non-preferred name) ; × 2 propionyl Coenzyme A × 4 BIOTIN × 5 BICARBONATE ION × 2 ADENOSINE-5'-TRIPHOSPHATE × 2 MAGNESIUM ION × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0QPL0_MYCS2
Isoform	—
PDB entities	5
Chains and sequence ranges	Author chain V； PDBConstruct 1–294； UniProt 1–294 Author chain Y； PDBConstruct 1–294； UniProt 1–294

Allophanate hydrolase subunit 1

OrganismNot specified

UniProt A0QPL1

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 26	Biotin-dependent acyl-coenzyme A carboxylase alpha3 subunit × 14 （A0QTE1） Acetyl-/propionyl-coenzyme A carboxylase AccE5 × 2 （A0QTE6） Propionyl-CoA carboxylase beta chain × 2 （A0R616） Propionyl-CoA carboxylase beta chain × 4 （A0QTE7） Allophanate hydrolase subunit 2 × 2 （A0QPL0） ;S-{(3S,5S,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5,10,14-tetraoxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} (11E,14E,16E)-icosa-11,14,16-trienethioate (non-preferred name) ; × 2 propionyl Coenzyme A × 4 BIOTIN × 5 BICARBONATE ION × 2 ADENOSINE-5'-TRIPHOSPHATE × 2 MAGNESIUM ION × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0QPL1_MYCS2
Isoform	—
PDB entities	6
Chains and sequence ranges	Author chain W； PDBConstruct 1–210； UniProt 1–210 Author chain Z； PDBConstruct 1–210； UniProt 1–210

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	9yx5
Deposition date deposition_date	2025-10-26
Structure title title	Structure of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis with MSMEG_0435-MSMEG_0436 bound
Keywords keywords	Carboxylase, transferase, lipid synthesis, mycolic acid synthesis, LIGASE; LIGASE
Experimental Method method	ELECTRON MICROSCOPY

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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.

9yx5__assembly_1__model_1

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

Download this curve (.dat)

9yx5__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

9yx5__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	71.74 Å
Rg (electron density)	69.98 Å
Total Rg	69.32 Å
Atom count	56321
Residues	8786
Excluded volume	972980 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`9yx5__assembly_1__model_1`	26-meric （26）	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 (12)

Entity 1 Entity 1 polymer

Description description	Biotin-dependent acyl-coenzyme A carboxylase alpha3 subunit
Molecular weight formula_weight	63215.2 kDa
EC 编号 ec_number	6.3.4.14
Source method src_method	nat
Copy count entity_count	14

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,I,J,K,L,Q,X,U,B,C,D,R,S,T
Atom count atom_count	56321

MANHASSKISKVLVANRGEIAVRVIRAAKDAGLASVAVYAEPDADAPHVRLADEAFALGGQTSAESYLVFEKILDAAEKSGANAIHPGYGFLSENADFAQAVIDAGLIWIGPSPQSIRDLGDKVTARHIAARAKAPLVPGTPDPVKDADEVVAFAKEHGVPVAIKAAFGGGGRGMKVARTLEEIPELFESATREAIAAFGRGECFVERYLDKPRHVEAQVIADQHGNVVVAGTRDCSLQRRFQKLVEEAPAPFLTDAQRKEIHESAKRICKEAGYYGAGTVEYLVGQDGLISFLEVNTRLQVEHPVTEETSGIDLVRQQFKIANGEPLDITEDPTPRGHSFEFRINGEDAGRGFLPAPGPVTKFVAPTGPGVRMDSGVETGSVIGGQFDSMLAKLIVTGATREEALERSRRALAEFTVEGLATVIPFHRAVVSDPAFIGDGEKFDVHTRWIETEWNNTVEPFTGGDPIEEEDTVPRQTVVVEVGGRRLEVSLPGDLAIGGGGGAAAPGVVRKKPKPRKRGGGGAKAASGDAVTAPMQGTVVKVAVEEGQEVSAGDLVVVLEAMKMENPVTAHKDGTITGLAVEAGAAITQGTVIAEIK

Entity 2 Entity 2 polymer

Description description	Acetyl-/propionyl-coenzyme A carboxylase AccE5
Molecular weight formula_weight	10357.7 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

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

MSGANDSTTVSGEVQADVTDEAKADHEAHIKVLRGEPTPEEMAALMAVLASAGGGPAEPVKKERNMWGHPVDKLRYSVFSWQRVTLLERTHMRR

Entity 3 Entity 3 polymer

Description description	Propionyl-CoA carboxylase beta chain
Molecular weight formula_weight	56234.1 kDa
EC 编号 ec_number	6.4.1.3
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

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

MTNKTTAELLAELREKLELAKEPGGEKAVAKREKKGIPSARARINALLDPGSFIEIGALAKTPGDPNALYGDGVVTGRGTIDGRPVGVFSHDQTVFQGSVGEMFGRKVARLMEWVAMVGCPIIGINDSAGARIQDAVTSLAWYAELGRRHEMLRGLVPEISLIFGKCAGGAVYSPIQTDLLVAVRDQGYMFITGPDVIKDVTGEDVTFDELGGADEQAKRGNIHKVVNSEAEAYQYVRDYLSFLPSNHFDNPPIVNPGMEPEITPHDLELDSIVPDADNMAYDMHEILLRIFDDGDVFEIAEQRGPAMITAFARVDGHPVGVIANQPMVLSGAIDNEASDKAASFIRFCDSYNLPLVFVVDTPGAMPGVAEEKGGIIKRGGRFFNAIVEADVPKVTVIIRKAYGGGYAVMGSKQLSADLNFAWPTARIAVIGAEGAAQLLVKRFPDPNAPEVQKIRDDFIEGYNLNMATPWIAAERGYIDAVIQPHETRLLLRKSLRLLRDKQNGPKVQRKHGLLPL

Entity 4 Entity 4 polymer

Description description	Propionyl-CoA carboxylase beta chain
Molecular weight formula_weight	58488.1 kDa
EC 编号 ec_number	6.4.1.3
Source method src_method	nat
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G,H,M,N

MTSVTEPSAEHQVDIHTTAGKLADLKRRTEETLHPVGEAAVDKVHAKGKLTARERILALLDEGSFVELDALAKHRSTNFGLEKNRPLGDGVITGYGTIDGRDVCIFSQDATVFGGSLGEVYGEKIVKVQELAIKTGRPLIGINDGAGARIQEGVVSLGLYSRIFHNNIKASGVIPQISLIMGAAAGGHVYSPALTDFVVMVDQTSQMFITGPDVIKTVTGEDVTMEELGGAHTHMAKSGTAHYVASGEQDAFDYVRDLLSYLPPNNYADPPLYPVAIPEGSIEETLTDEDLELDTLIPDSPNQPYDMHEVITRILDDDEFLEVQAGYAGNIVVGFGRVEGRPVGIVANQPTQFAGCLDINASEKAARFIRTCDCFNIPIVLLVDVPGFLPGTDQEYNGIIRRGAKLLYAYGEATVAKVTVITRKSYGGAYCVMGSKDMGADVVVAWPTAQIAVMGASGAVGFVYRQQLKEAAKNGEDVDALRLELQQTYEDTLVNPYIAAERGYVDAVIPPSHTRGYVANALRLLERKIVQMPPKKHGNIPL

Entity 5 Entity 5 polymer

Description description	Allophanate hydrolase subunit 2
Molecular weight formula_weight	31280.2 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

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

MGTTLEVLRTGPLALVEDLGRPGLAHMGVTRSGAADRRSHTLANRLVANPGESATIEVTFGGFSARVCGGDVAIAVTGADTDPAVNGIPFGTNSIHHVHDGQVISLGAPHSGLRSYLAVRGGIDVTPVLGSRSYDVMSAIGPSPLRPGDVLPVGEHTDEFPELDQAPVAAIAEDVVELQVVPGPRDDWFVDPDILVRTNWLVTNRSDRVGMRLVGMPLEYRNPDRQLPSEGATRGAIQVPPNGFPVILGPDHPVTGGYPVIGVVTEEDIDKLGQVRPGQTVRLHWAYPRRPFET

Entity 6 Entity 6 polymer

Description description	Allophanate hydrolase subunit 1
Molecular weight formula_weight	22659.8 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	W,Z

MTLGTVHNYGDQALLLEFDSTAEVLAWTETLREAELLGVVDIVPAARTVLVKLAGPRYQAPTRQRLGKLRVRPEAITHQPPGDRVDVTIDVVYDGADLHEVASLTGMTPAQVIAAHTGTPWRVGFCGFAPGFAYLVDGDARLQVPRRAEPRTSVPAGAVALAGEFSGVYPRQSPGGWQLIGHTDAVMFDVNRDKPALLTPGMWVQFRAVG

Entity 7 Entity 7 non-polymer

Description description	;S-{(3S,5S,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5,10,14-tetraoxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} (11E,14E,16E)-icosa-11,14,16-trienethioate (non-preferred name) ;
Molecular weight formula_weight	1056.0 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 8 Entity 8 non-polymer

Description description	propionyl Coenzyme A
Molecular weight formula_weight	823.6 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 9 Entity 9 non-polymer

Description description	BIOTIN
Molecular weight formula_weight	244.3 kDa
Source method src_method	syn
Copy count entity_count	5

Entity 10 Entity 10 non-polymer

Description description	BICARBONATE ION
Molecular weight formula_weight	61.0 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 11 Entity 11 non-polymer

Description description	ADENOSINE-5'-TRIPHOSPHATE
Molecular weight formula_weight	507.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 12 Entity 12 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	2

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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	—

Resolution resolution	2.900 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Resolution resolution	2.90 Å
Resolution测定Method resolution_method	—
颗粒数 num_particles	10016

Structure of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis with MSMEG_0435-MSMEG_0436 bound

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

Biotin-dependent acyl-coenzyme A carboxylase alpha3 subunit

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Acetyl-/propionyl-coenzyme A carboxylase AccE5

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Propionyl-CoA carboxylase beta chain

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Propionyl-CoA carboxylase beta chain

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Allophanate hydrolase subunit 2

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Allophanate hydrolase subunit 1

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

9yx5__assembly_1__model_1

9yx5__assembly_1__model_1 | I(q)

9yx5__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (12)

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

Entity 8 Entity 8 non-polymer

Entity 9 Entity 9 non-polymer

Entity 10 Entity 10 non-polymer

Entity 11 Entity 11 non-polymer

Entity 12 Entity 12 non-polymer

7. Citations (1)