SAXSdb — 7aqo

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

THO complex subunit 2

Saccharomyces cerevisiae S288C

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 × 12 PDB declaration: dodecameric（12） Consistent with protein copy count	Chain A； UniProt 1–1597 Chain G； UniProt 1–1597	Not recorded	THO complex subunit HPR1 × 2 （P17629） TEX1 isoform 1 × 2 （A0A6A5Q4V2） EM14S01-3B_G0007820.mRNA.1.CDS.1 × 2 （A0A6A5Q316） BJ4_G0025130.mRNA.1.CDS.1 × 2 （A0A6A5PZX4） THO complex subunit MFT1 × 2 （P33441）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE-PROPANE	Resolution 4.50 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	A0A6A5Q535_YEASX
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 5–1601； UniProt 1–1597 Author chain G； PDBConstruct 5–1601； UniProt 1–1597

THO complex subunit HPR1

Saccharomyces cerevisiae S288C

UniProt P17629

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 × 12 PDB declaration: dodecameric（12） Consistent with protein copy count	Chain B； UniProt 1–720 Chain H； UniProt 1–720	Not recorded	THO complex subunit 2 × 2 （A0A6A5Q535） TEX1 isoform 1 × 2 （A0A6A5Q4V2） EM14S01-3B_G0007820.mRNA.1.CDS.1 × 2 （A0A6A5Q316） BJ4_G0025130.mRNA.1.CDS.1 × 2 （A0A6A5PZX4） THO complex subunit MFT1 × 2 （P33441）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE-PROPANE	Resolution 4.50 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 7AQO	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
7APX yeast THO-Sub2 complex Deposited 2020-10-20	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 1–720（720 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.40 Å
7LUV Cryo-EM structure of the yeast THO-Sub2 complex Deposited 2021-02-23	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 1–603（603 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å
7V2W protomer structure from the dimer of yeast THO complex Deposited 2021-08-10	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain F 1–752（752 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
7V2Y cryo-EM structure of yeast THO complex with Sub2 Deposited 2021-08-10	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 1–752（752 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	HPR1_YEAST
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–720； UniProt 1–720 Author chain H； PDBConstruct 1–720； UniProt 1–720

TEX1 isoform 1

Saccharomyces cerevisiae S288C

UniProt A0A6A5Q4V2

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 × 12 PDB declaration: dodecameric（12） Consistent with protein copy count	Chain E； UniProt 1–380 Chain K； UniProt 1–380	Not recorded	THO complex subunit 2 × 2 （A0A6A5Q535） THO complex subunit HPR1 × 2 （P17629） EM14S01-3B_G0007820.mRNA.1.CDS.1 × 2 （A0A6A5Q316） BJ4_G0025130.mRNA.1.CDS.1 × 2 （A0A6A5PZX4） THO complex subunit MFT1 × 2 （P33441）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE-PROPANE	Resolution 4.50 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	A0A6A5Q4V2_YEASX
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain E； PDBConstruct 1–380； UniProt 1–380 Author chain K； PDBConstruct 1–380； UniProt 1–380

EM14S01-3B_G0007820.mRNA.1.CDS.1

Saccharomyces cerevisiae S288C

UniProt A0A6A5Q316

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 × 12 PDB declaration: dodecameric（12） Consistent with protein copy count	Chain F； UniProt 51–446 Chain L； UniProt 51–446	Not recorded	THO complex subunit 2 × 2 （A0A6A5Q535） THO complex subunit HPR1 × 2 （P17629） TEX1 isoform 1 × 2 （A0A6A5Q4V2） BJ4_G0025130.mRNA.1.CDS.1 × 2 （A0A6A5PZX4） THO complex subunit MFT1 × 2 （P33441）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE-PROPANE	Resolution 4.50 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	A0A6A5Q316_YEASX
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain F； PDBConstruct 5–400； UniProt 51–446 Author chain L； PDBConstruct 5–400； UniProt 51–446

BJ4_G0025130.mRNA.1.CDS.1

Saccharomyces cerevisiae S288C

UniProt A0A6A5PZX4

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 × 12 PDB declaration: dodecameric（12） Consistent with protein copy count	Chain C； UniProt 1–261 Chain J； UniProt 1–261	Not recorded	THO complex subunit 2 × 2 （A0A6A5Q535） THO complex subunit HPR1 × 2 （P17629） TEX1 isoform 1 × 2 （A0A6A5Q4V2） EM14S01-3B_G0007820.mRNA.1.CDS.1 × 2 （A0A6A5Q316） THO complex subunit MFT1 × 2 （P33441）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE-PROPANE	Resolution 4.50 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	A0A6A5PZX4_YEASX
Isoform	—
PDB entities	5
Chains and sequence ranges	Author chain C； PDBConstruct 1–261； UniProt 1–261 Author chain J； PDBConstruct 1–261； UniProt 1–261

THO complex subunit MFT1

Saccharomyces cerevisiae S288C

UniProt P33441

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 × 12 PDB declaration: dodecameric（12） Consistent with protein copy count	Chain D； UniProt 1–392 Chain I； UniProt 1–392	Not recorded	THO complex subunit 2 × 2 （A0A6A5Q535） THO complex subunit HPR1 × 2 （P17629） TEX1 isoform 1 × 2 （A0A6A5Q4V2） EM14S01-3B_G0007820.mRNA.1.CDS.1 × 2 （A0A6A5Q316） BJ4_G0025130.mRNA.1.CDS.1 × 2 （A0A6A5PZX4）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE-PROPANE	Resolution 4.50 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 7AQO	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
7APX yeast THO-Sub2 complex Deposited 2020-10-20	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain D 1–392（392 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.40 Å
7LUV Cryo-EM structure of the yeast THO-Sub2 complex Deposited 2021-02-23	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain D 1–256（256 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å
7V2W protomer structure from the dimer of yeast THO complex Deposited 2021-08-10	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain I 1–392（392 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
7V2Y cryo-EM structure of yeast THO complex with Sub2 Deposited 2021-08-10	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain D 1–392（392 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	MFT1_YEAST
Isoform	—
PDB entities	6
Chains and sequence ranges	Author chain D； PDBConstruct 1–392； UniProt 1–392 Author chain I； PDBConstruct 1–392； UniProt 1–392

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	7aqo
Deposition date deposition_date	2020-10-22
Structure title title	yeast THO-Sub2 complex dimer
Keywords keywords	yeast THO complex S. cerevisiae THO-Sub2 the transcription-export (TREX) complex, RNA BINDING PROTEIN; RNA BINDING PROTEIN
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	79.70 Å
Radius of gyration Rg (electron density) rg_electron	79.94 Å
Forward intensity I(0) i0	4294630000.00
Molecular weight molecular_weight	568170.0 kDa
Excluded volume excluded_volume	714600 Å³
Envelope volume envelope_volume	1283200 Å³
Hydration-shell volume shell_volume	141610 Å³
Envelope diameter envelope_diameter	306.0 Å
Shell Rg shell_rg	74.09 Å
Envelope Rg envelope_rg	77.22 Å
Shape Rg shape_rg	80.01 Å
Total Rg total_rg	79.61 Å
Total atoms total_atoms	40251
Residues n_residues	5611
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	225.1 Å
Rg (real space) rg_real	77.50 Å
Rg uncertainty (real space) rg_real_error	0.85 Å
I(0) (real space) i0_real	4.1730e+09
I(0) uncertainty (real space) i0_real_error	7.6080e+07
Rg (reciprocal space) rg_reciprocal	78.38 Å
I(0) (reciprocal space) i0_reciprocal	4279000000.0000
Solution quality estimate total_estimate	0.6481
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	101.3 Å
Skewness Skewness skewness	0.242
Kurtosis Kurtosis kurtosis	-0.605
Angular range angular_range	— – 0.1000 Å⁻¹
Current regularization parameter α current_alpha	1.0080
Highest regularization parameter α highest_alpha	215800000.0000
Real-space data points n_real_points	21
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.001; Oscil: 1.000; Stabil: 0.980; Sysdev: 0.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.003

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	THO complex subunit 2
Molecular weight formula_weight	184450.0 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G,A
Atom count atom_count	40261

GAASMAEQTLLSKLNALSQKVIPPASPSQASILTEEVIRNWPERSKTLCSDFTALESNDEKEDWLRTLFIELFDFINKNDENSPLKLSDVASFTNELVNHERQVSQASIVGKMFIAVSSTVPNINDLTTISLCKLIPSLHEELFKFSWISSKLLNKEQTTLLRHLLKKSKYELKKYNLLVENSVGYGQLVALLILAYYDPDNFSKVSAYLKEIYHIMGKYSLDSIRTLDVILNVSSQFITEGYKFFIALLRKSDSWPSSHVANNSNYSSLNEGGNMIAANIISFNLSQYNEEVDKENYERYMDMCCILLKNGFVNFYSIWDNVKPEMEFLQEYIQNLETELEEESTKGVENPLAMAAALSTENETDEDNALVVNDDVNMKDKISEETNADIESKGKQKTQQDILLFGKIKLLERLLIHGCVIPVIHVLKQYPKVLYVSESLSRYLGRVFEYLLNPLYTSMTSSGESKDMATALMITRIDNGILAHKPRLIHKYKTHEPFESLELNSSYVFYYSEWNSNLTPFASVNDLFENSHIYLSIIGPYLGRIPTLLSKISRIGVADIQKNHGSESLHVTIDKWIDYVRKFIFPATSLLQNNPIATSEVYELMKFFPFEKRYFIYNEMMTKLSQDILPLKVSFNKAEREAKSILKALSIDTIAKESRRFAKLISTNPLASLVPAVKQIENYDKVSELVVYTTKYFNDFAYDVLQFVLLLRLTYNRPAVQFDGVNQAMWVQRLSIFIAGLAKNCPNMDISNIITYILKTLHNGNIIAVSILKELIITVGGIRDLNEVNMKQLLMLNSGSPLKQYARHLIYDFRDDNSVISSRLTSFFTDQSAISEIILLLYTLNLKANTQNSHYKILSTRCDEMNTLLWSFIELIKHCLKGKAFEENVLPFVELNNRFHLSTPWTFHIWRDYLDNQLNSNENFSIDELIEGAEFSDVDLTKISKDLFTTFWRLSLYDIHFDKSLYDERKNALSGENTGHMSNRKKHLIQNQIKDILVTGISHQRAFKKTSEFISEKSNVWNKDCGEDQIKIFLQNCVVPRVLFSPSDALFSSFFIFMAFRTENLMSILNTCITSNILKTLLFCCTSSEAGNLGLFFTDVLKKLEKMRLNGDFNDQASRKLYEWHSVITEQVIDLLSEKNYMSIRNGIEFMKHVTSVFPVVKAHIQLVYTTLEENLINEEREDIKLPSSALIGHLKARLKDALELDEFCTLTEEEAEQKRIREMELEEIKNYETACQNEQKQVALRKQLELNKSQRLQNDPPKSVASGSAGLNSKDRYTYSRNEPVIPTKPSSSQWSYSKVTRHVDDINHYLATNHLQKAISLVENDDETRNLRKLSKQNMPIFDFRNSTLEIFERYFRTLIQNPQNPDFAEKIDSLKRYIKNISREPYPDTTSSYSEAAAPEYTKRSSRYSGNAGGKDGYGSSNYRGPSNDRSAPKNIKPISSYAHKRSELPTRPSKSKTYNDRSRALRPTGPDRGDGFDQRDNRLREEYKKNSSQRSQLRFPEKPFQEGKDSSKANPYQASSYKRDSPSENEEKPNKRFKKDETIRNKFQTQDYRNTRDSGAAHRANENQRYNGNRKSNTQALPQGPKGGNYVSRYQR

来源 Source

来源生物 organism	Saccharomyces cerevisiae S288C
NCBI Class编号 ncbi_taxonomy_id	559292
宿主生物 host_organism	Spodoptera frugiperda

Entity 2 Entity 2 polymer

Description description	THO complex subunit HPR1
Molecular weight formula_weight	84544.0 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

MSNTEELIQNSIGFLQKTFKALPVSFDSIRHEPLPSSMLHASVLNFEWEPLEKNISAIHDRDSLIDIILKRFIIDSMTNAIEDEEENNLEKGLLNSCIGLDFVYNSRFNRSNPASWGNTFFELFSTIIDLLNSPSTFLKFWPYAESRIEWFKMNTSVEPVSLGESNLISYKQPLYEKLRHWNDILAKLENNDILNTVKHYNMKYKLENFLSELLPINEESNFNRSASISALQESDNEWNRSARERESNRSSDVIFAADYNFVFYHLIICPIEFAFSDLEYKNDVDRSLSPLLDAILEIEENFYSKIKMNNRTRYSLEEALNTEYYANYDVMTPKLPVYMKHSNAMKMDRNEFWANLQNIKESDDYTLRPTIMDISLSNTTCLYKQLTQEDDDYYRKQFILQLCFTTNLIRNLISSDETRNFYKSCYLRENPLSDIDFENLDEVNKKRGLNLCSYICDNRVLKFYKIKDPDFYRVIRKLMSSDEKFTTAKIDGFKEFQNFRISKEKIPPPAFDETFKKFTFIKMGNKLINNVWKIPTGLDKIEQEVKKPEGVYEAAQAKWESKISSETSGGEAKDEIIRQWQTLRFLRSRYLFDFDKVNEKTGVDGLFEEPRKVEALDDSFKEKLLYKINQEHRKKLQDAREYKIGKERKKRALEEEASFPEREQKIKSQRINSASQTEGDELKSEQTQPKGEISEENTKIKSSEVSSQDPDSGVAGEFAP

来源 Source

来源生物 organism	Saccharomyces cerevisiae S288C
NCBI Class编号 ncbi_taxonomy_id	559292
宿主生物 host_organism	Spodoptera frugiperda

Entity 3 Entity 3 polymer

Description description	TEX1 isoform 1
Molecular weight formula_weight	42315.2 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

MSTIGAVDILNQKTITSEVAASVTSKYLQSTFSKGNTSHIEDKRFIHVSSRSHSRFTSTPITPNEILSLKFHVSGSSMAYSRMDGSLTVWFIKDASFDKSVEVYIPDCCGSDKLATDLSWNPTSLNQIAVVSNSSEISLLLINEKSLTASKLRTLSLGSKTKVNTCLYDPLGNWLLAATKSEKIYLFDVKKDHSSVCSLNISDISQEDNDVVYSLAWSNGGSHIFIGFKSGYLAILKAKHGILEVCTKIKAHTGPITEIKMDPWGRNFITGSIDGNCYVWNMKSLCCELIINDLNSAVTTLDVCHLGKILGICTEDEMVYFYDLNSGNLLHSKSLANYKTDPVLKFYPDKSWYIMSGKNDTLSNHFVKNEKNLITYWKDM

来源 Source

来源生物 organism	Saccharomyces cerevisiae S288C
NCBI Class编号 ncbi_taxonomy_id	559292
宿主生物 host_organism	Spodoptera frugiperda

Entity 4 Entity 4 polymer

Description description	EM14S01-3B_G0007820.mRNA.1.CDS.1
Molecular weight formula_weight	45521.0 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

GAASDKKGSYVGIHSTGFKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDPVPGEVAVVVICNARELAYQIRNEYLRFSKYMPDVKTAVFYGGTPISKDAELLKNKDTAPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVLEELDMRRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEIFVDDEAKLTLHGLQQYYIKLEEREKNRKLAQLLDDLEFNQVIIFVKSTTRANELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRICVSTDVFGRGIDIERINLAINYDLTNEADQYLHRVGRAGRFGTKGLAISFVSSKEDEEVLAKIQERFDVKIAEFPEEGIDPSTYLNN

来源 Source

来源生物 organism	Saccharomyces cerevisiae S288C
NCBI Class编号 ncbi_taxonomy_id	559292
宿主生物 host_organism	Spodoptera frugiperda

Entity 5 Entity 5 polymer

Description description	BJ4_G0025130.mRNA.1.CDS.1
Molecular weight formula_weight	30340.3 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

MTKEEGRTYFESLCEEEQSLQESQTHLLNILDILSVLADPRSSDDLLTESLKKLPDLHRELINSSIRLRYDKYQTREAQLLEDTKTGRDVAAGVQNPKSISEYYSTFEHLNRDTLRYINLLKRLSVDLAKQVEVSDPSVTVYEMDKWVPSEKLQGILEQYCAPDTDIRGVDAQIKNYLDQIKMARAKFGLENKYSLKERLSTLTKELNHWRKEWDDIEMLMFGDDAHSMKKMIQKIDSLKSEINAPSESYPVDKEGDIVLE

来源 Source

来源生物 organism	Saccharomyces cerevisiae S288C
NCBI Class编号 ncbi_taxonomy_id	559292
宿主生物 host_organism	Spodoptera frugiperda

Entity 6 Entity 6 polymer

Description description	THO complex subunit MFT1
Molecular weight formula_weight	45055.0 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

MPLSQKQIDQVRTKVHYSEVDTPFNKYLDILGKVTKLTGSIINGTLSNDDSKIEKLTEQNISQLKESAHLRFLDLQSSIDTKKVADENWETCQQETLAKLENLKDKLPDIKSIHSKLLLRIGKLQGLYDSVQVINREVEGLSEGRTSLVVTRAEWEKELGTDLVKFLIEKNYLKLVDPGLKKDSSEERYRIYDDFSKGPKELESINASMKSDIENVRQEVSSYKEKWLRDAEIFGKITSIFKEELLKRDGLLNEAEGDNIDEDYESDEDEERKERFKRQRSMVEVNTIENVDEKEESDHEYDDQEDEENEEEDDMEVDVEDIKEDNEVDGESSQQEDNSRQGNNEETDKETGVIEEPDAVNDAEEADSDHSSRKLGGTTSDFSASSSVEEVK

来源 Source

来源生物 organism	Saccharomyces cerevisiae S288C
NCBI Class编号 ncbi_taxonomy_id	559292
宿主生物 host_organism	Spodoptera frugiperda

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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	—

Resolution resolution	4.50 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	113076

fit	/app/data/saxs_computation/aq/7aqo/7aqo.fit
pddf	/app/data/pr_computation/aq/7aqo/7aqo.pr.out
profile	/app/data/saxs_computation/aq/7aqo/7aqo.dat

yeast THO-Sub2 complex dimer

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

THO complex subunit 2

State in the Current Structure

Other States of the Same Protein in the Database

THO complex subunit HPR1

State in the Current Structure

Other States of the Same Protein in the Database

TEX1 isoform 1

State in the Current Structure

Other States of the Same Protein in the Database

EM14S01-3B_G0007820.mRNA.1.CDS.1

State in the Current Structure

Other States of the Same Protein in the Database

BJ4_G0025130.mRNA.1.CDS.1

State in the Current Structure

Other States of the Same Protein in the Database

THO complex subunit MFT1

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

Entity 4 Entity 4 polymer

Polymer Polymer

来源 Source

Entity 5 Entity 5 polymer

Polymer Polymer

来源 Source

Entity 6 Entity 6 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)