SAXSdb — 2y7c

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

TYPE-1 RESTRICTION ENZYME ECOKI SPECIFICITY PROTEIN

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 × 5 PDB declaration: pentameric（5） Consistent with protein copy count	Chain A； UniProt 1–464	Not recorded	TYPE I RESTRICTION ENZYME ECOKI M PROTEIN × 2 （P08957） GENE 0.3 PROTEIN × 2 （P03775）	ELECTRON MICROSCOPY cryo-EM buffer：20MM TRIS-CL, 100 MM NACL；pH 4.7；20MM TRIS-CL, 100 MM NACL	Resolution 18.00 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 2Y7C	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2Y7H Atomic model of the DNA-bound methylase complex from the Type I restriction-modification enzyme EcoKI (M2S1). Based on fitting into EM map 1534. Deposited 2011-01-31	Different oligomeric state Different ligand/ion	Assembly 1 Protein–DNA Heteromer；Protein × 3 PDB declaration: pentameric	Chain A 1–464（464 aa）	Not recorded	SAM S-ADENOSYLMETHIONINE × 2	ELECTRON MICROSCOPY cryo-EM buffer 20MM TRIS-CL, 100 MM NACL；pH 4.7；20MM TRIS-CL, 100 MM NACL	Resolution 18.00 Å

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

View Construct and Data Evidence

UniProt name	T1SK_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–464； UniProt 1–464

TYPE I RESTRICTION ENZYME ECOKI M PROTEIN

OrganismNot specified

UniProt P08957

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 × 5 PDB declaration: pentameric（5） Consistent with protein copy count	Chain B； UniProt 1–529 Chain C； UniProt 1–529	Not recorded	TYPE-1 RESTRICTION ENZYME ECOKI SPECIFICITY PROTEIN × 1 （P05719） GENE 0.3 PROTEIN × 2 （P03775）	ELECTRON MICROSCOPY cryo-EM buffer：20MM TRIS-CL, 100 MM NACL；pH 4.7；20MM TRIS-CL, 100 MM NACL	Resolution 18.00 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 2Y7C	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2AR0 Crystal structure of Type I restriction enzyme EcoKI M protein (EC 2.1.1.72) (M.EcoKI) Deposited 2005-08-18	Different construct Different mutation/modification 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 2–527（526 aa）	Mutation：MSE/MET Non-standard monomer：Yes (specific site not provided by mmCIF)	UNX UNKNOWN LIGAND × 10	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.25；291 K；2.15M (NH2)2SO4, 0.1M Na Citrate, pH 8.25, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 2.80 Å R-free 0.261
2AR0 Crystal structure of Type I restriction enzyme EcoKI M protein (EC 2.1.1.72) (M.EcoKI) Deposited 2005-08-18	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–527（526 aa）	Mutation：MSE/MET 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 8.25；291 K；2.15M (NH2)2SO4, 0.1M Na Citrate, pH 8.25, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 2.80 Å R-free 0.261
2Y7H Atomic model of the DNA-bound methylase complex from the Type I restriction-modification enzyme EcoKI (M2S1). Based on fitting into EM map 1534. Deposited 2011-01-31	Different oligomeric state Different ligand/ion	Assembly 1 Protein–DNA Heteromer；Protein × 3 PDB declaration: pentameric	Chain B 1–529（529 aa） Chain C 1–529（529 aa）	Not recorded	SAM S-ADENOSYLMETHIONINE × 2	ELECTRON MICROSCOPY cryo-EM buffer 20MM TRIS-CL, 100 MM NACL；pH 4.7；20MM TRIS-CL, 100 MM NACL	Resolution 18.00 Å

2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	T1MK_ECOLI
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–529； UniProt 1–529 Author chain C； PDBConstruct 1–529； UniProt 1–529

GENE 0.3 PROTEIN

ENTEROBACTERIA PHAGE T7

UniProt P03775

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 × 5 PDB declaration: pentameric（5） Consistent with protein copy count	Chain D； UniProt 1–116 Chain E； UniProt 1–116	Not recorded	TYPE-1 RESTRICTION ENZYME ECOKI SPECIFICITY PROTEIN × 1 （P05719） TYPE I RESTRICTION ENZYME ECOKI M PROTEIN × 2 （P08957）	ELECTRON MICROSCOPY cryo-EM buffer：20MM TRIS-CL, 100 MM NACL；pH 4.7；20MM TRIS-CL, 100 MM NACL	Resolution 18.00 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 2Y7C	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1S7Z Structure of Ocr from Bacteriophage T7 Deposited 2004-01-30	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 × 2 PDB declaration: dimeric	Chain A 1–117（117 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	CS CESIUM ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.2；291 K；32%PEG-8000, 0.1M Tris-HCl, 0.2M caesium chloride, pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 1.83 Å R-free 0.239
1S7Z Structure of Ocr from Bacteriophage T7 Deposited 2004-01-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–117（117 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	CS CESIUM ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.2；291 K；32%PEG-8000, 0.1M Tris-HCl, 0.2M caesium chloride, pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 1.83 Å R-free 0.239
1S7Z Structure of Ocr from Bacteriophage T7 Deposited 2004-01-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–117（117 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	CS CESIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.2；291 K；32%PEG-8000, 0.1M Tris-HCl, 0.2M caesium chloride, pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 1.83 Å R-free 0.239
6R9B Cryo-EM structure of bacterial RNAP with a DNA mimic protein Ocr from T7 phage Deposited 2019-04-03	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain F 1–117（117 aa） Chain G 1–117（117 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
6R9G Structural basis of transcription inhibition by the DNA mimic Ocr protein of bacteriophage T7 Deposited 2019-04-03	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain F 1–117（117 aa） Chain G 1–117（117 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å
7BST EcoR124I-Ocr in the Intermediate State Deposited 2020-03-31	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain F 1–117（117 aa） Chain G 1–117（117 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.37 Å
7BTP EcoR124I-Ocr in Restriction-Alleviation State Deposited 2020-04-02	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain D 1–117（117 aa） Chain F 1–117（117 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.01 Å
7EEW Crystal structure of the intact MTase from Vibrio vulnificus YJ016 in complex with the DNA-mimicking Ocr protein and the S-adenosyl-L-homocysteine (SAH) Deposited 2021-03-19	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 × 4 PDB declaration: tetrameric	Chain B 1–117（117 aa）	Not recorded	SAH S-ADENOSYL-L-HOMOCYSTEINE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；20% (w/v) polyethylene glycol 6000, 0.1 M sodium chloride, 0.1 M HEPES pH 8.5	Resolution 2.90 Å R-free 0.293
8Q56 PglX methyltransferase of Salmonella BREX phage defence system (aka BrxX) bound to inhibitor Ocr Deposited 2023-08-08	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 × 4 PDB declaration: tetrameric	Chain B 1–117（117 aa）	Not recorded	SAM S-ADENOSYLMETHIONINE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.2；293 K；0.1 M NaCl, 0.1 M KCl, 14% PEG 4000, 6% MPD	Resolution 3.50 Å R-free 0.292
8V45 CryoEM structure of AriA-Ocr complex Deposited 2023-11-28	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain O 1–117（117 aa） Chain P 1–117（117 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.63 Å
8ZEK Cryo-EM structure of the E. coli BrxX methyltransferase complexed with Ocr Deposited 2024-05-06	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–117（117 aa） Chain C 1–117（117 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.15 Å
9EX7 Cryo-EM structure of the E. coli BrxX methyltransferase in complex with Ocr Deposited 2024-04-05	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1–117（117 aa） Chain D 1–117（117 aa）	Not recorded	MG MAGNESIUM ION × 2 SAM S-ADENOSYLMETHIONINE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.91 Å

10 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	V03_BPT7
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain D； PDBConstruct 1–116； UniProt 1–116 Author chain E； PDBConstruct 1–116； UniProt 1–116

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	2y7c
Deposition date deposition_date	2011-01-31
Structure title title	Atomic model of the Ocr-bound methylase complex from the Type I restriction-modification enzyme EcoKI (M2S1). Based on fitting into EM map 1534.
Keywords keywords	TRANSFERASE; TRANSFERASE
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	40.48 Å
Radius of gyration Rg (electron density) rg_electron	39.76 Å
Forward intensity I(0) i0	590653000.00
Molecular weight molecular_weight	194870.0 kDa
Excluded volume excluded_volume	242540 Å³
Envelope volume envelope_volume	356150 Å³
Hydration-shell volume shell_volume	72504 Å³
Envelope diameter envelope_diameter	135.4 Å
Shell Rg shell_rg	47.13 Å
Envelope Rg envelope_rg	39.05 Å
Shape Rg shape_rg	39.75 Å
Total Rg total_rg	40.20 Å
Total atoms total_atoms	13725
Residues n_residues	1735
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	127.5 Å
Rg (real space) rg_real	40.29 Å
Rg uncertainty (real space) rg_real_error	0.94 Å
I(0) (real space) i0_real	5.9070e+08
I(0) uncertainty (real space) i0_real_error	1.1010e+07
Rg (reciprocal space) rg_reciprocal	40.47 Å
I(0) (reciprocal space) i0_reciprocal	590800000.0000
Solution quality estimate total_estimate	0.8850
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	52.3 Å
Skewness Skewness skewness	0.144
Kurtosis Kurtosis kurtosis	-0.370
Angular range angular_range	— – 0.1950 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	71330000.0000
Real-space data points n_real_points	40
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.889; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.853

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	TYPE-1 RESTRICTION ENZYME ECOKI SPECIFICITY PROTEIN
Molecular weight formula_weight	51468.2 kDa
EC 编号 ec_number	3.1.21.3
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	13725

MSAGKLPEGWVIAPVSTVTTLIRGVTYKKEQAINYLKDDYLPLIRANNIQNGKFDTTDLVFVPKNLVKESQKISPEDIVIAMSSGSKSVVGKSAHQHLPFECSFGAFCGVLRPEKLIFSGFIAHFTKSSLYRNKISSLSAGANINNIKPASFDLINIPIPPLAEQKIIAEKLDTLLAQVDSTKARFEQIPQILKRFRQAVLGGAVNGKLTEKWRNFEPQHSVFKKLNFESILTELRNGLSSKPNESGVGHPILRISSVRAGHVDQNDIRFLECSESELNRHKLQDGDLLFTRYNGSLEFVGVCGLLKKLQHQNLLYPDKLIRARLTKDALPEYIEIFFSSPSARNAMMNCVKTTSGQKGISGKDIKSQVVLLPPVKEQAEIVRRVEQLFAYADTIEKQVNNALARVNNLTQSILAKAFRGELTAQWRAENPDLISGENSAAALLEKIKAERAASGGKKASRKKS

Entity 2 Entity 2 polymer

Description description	TYPE I RESTRICTION ENZYME ECOKI M PROTEIN
Molecular weight formula_weight	59378.3 kDa
EC 编号 ec_number	3.1.21.3, 2.1.1.72
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

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

MNNNDLVAKLWKLCDNLRDGGVSYQNYVNELASLLFLKMCKETGQEAEYLPEGYRWDDLKSRIGQEQLQFYRKMLVHLGEDDKKLVQAVFHNVSTTITEPKQITALVSNMDSLDWYNGAHGKSRDDFGDMYEGLLQKNANETKSGAGQYFTPRPLIKTIIHLLKPQPREVVQDPAAGTAGFLIEADRYVKSQTNDLDDLDGDTQDFQIHRAFIGLELVPGTRRLALMNCLLHDIEGNLDHGGAIRLGNTLGSDGENLPKAHIVATNPPFGSAAGTNITRTFVHPTSNKQLCFMQHIIETLHPGGRAAVVVPDNVLFEGGKGTDIRRDLMDKCHLHTILRLPTGIFYAQGVKTNVLFFTKGTVANPNQDKNCTDDVWVYDLRTNMPSFGKRTPFTDEHLQPFERVYGEDPHGLSPRTEGEWSFNAEETEVADSEENKNTDQHLATSRWRKFSREWIRTAKSDSLDISWLKDKDSIDADSLPEPDVLAAEAMGELVQALSELDALMRELGASDEADLQRQLLEEAFGGVKE

Entity 3 Entity 3 polymer

Description description	GENE 0.3 PROTEIN
Molecular weight formula_weight	13689.9 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

MAMSNMTYNNVFDHAYEMLKENIRYDDIRDTDDLHDAIHMAADNAVPHYYADIFSVMASEGIDLEFEDSGLMPDTKDVIRILQARIYEQLTIDLWEDAEDLLNEYLEEVEEYEEDE

来源 Source

来源生物 organism	ENTEROBACTERIA PHAGE T7
NCBI Class编号 ncbi_taxonomy_id	10760
宿主生物 host_organism	ESCHERICHIA COLI

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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	1

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

Resolution resolution	18.000 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Resolution resolution	18.00 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	17807

fit	/app/data/saxs_computation/y7/2y7c/2y7c.fit
pddf	/app/data/pr_computation/y7/2y7c/2y7c.pr.out
profile	/app/data/saxs_computation/y7/2y7c/2y7c.dat

Atomic model of the Ocr-bound methylase complex from the Type I restriction-modification enzyme EcoKI (M2S1). Based on fitting into EM map 1534.

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

TYPE-1 RESTRICTION ENZYME ECOKI SPECIFICITY PROTEIN

State in the Current Structure

Other States of the Same Protein in the Database

TYPE I RESTRICTION ENZYME ECOKI M PROTEIN

State in the Current Structure

Other States of the Same Protein in the Database

GENE 0.3 PROTEIN

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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)