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- PDB-3mhs: Structure of the SAGA Ubp8/Sgf11/Sus1/Sgf73 DUB module bound to u... -

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Basic information

Entry
Database: PDB / ID: 3mhs
TitleStructure of the SAGA Ubp8/Sgf11/Sus1/Sgf73 DUB module bound to ubiquitin aldehyde
Components
  • (SAGA-associated factor ...) x 2
  • Protein SUS1
  • Ubiquitin
  • Ubiquitin carboxyl-terminal hydrolase 8
KeywordsHydrolase/transcription regulator/protein binding / Multi-protein complex / Hydrolase-transcription regulator-protein binding complex / Acetylation / Cytoplasm / Isopeptide bond / Nucleus / Phosphoprotein / Ubl conjugation
Function / homology
Function and homology information


RITS complex assembly / DUBm complex / : / : / protein modification process => GO:0036211 / regulation of nucleocytoplasmic transport / transcription export complex 2 / nuclear mRNA surveillance / SLIK (SAGA-like) complex / post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery ...RITS complex assembly / DUBm complex / : / : / protein modification process => GO:0036211 / regulation of nucleocytoplasmic transport / transcription export complex 2 / nuclear mRNA surveillance / SLIK (SAGA-like) complex / post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery / regulation of protein localization to chromatin / SAGA complex / poly(A)+ mRNA export from nucleus / Peptide chain elongation / Selenocysteine synthesis / Formation of a pool of free 40S subunits / Eukaryotic Translation Termination / Response of EIF2AK4 (GCN2) to amino acid deficiency / SRP-dependent cotranslational protein targeting to membrane / positive regulation of RNA polymerase II transcription preinitiation complex assembly / Viral mRNA Translation / protein deubiquitination / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / GTP hydrolysis and joining of the 60S ribosomal subunit / L13a-mediated translational silencing of Ceruloplasmin expression / Major pathway of rRNA processing in the nucleolus and cytosol / Ub-specific processing proteases / nuclear pore / mRNA export from nucleus / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / Maturation of protein E / Maturation of protein E / ER Quality Control Compartment (ERQC) / Myoclonic epilepsy of Lafora / FLT3 signaling by CBL mutants / Prevention of phagosomal-lysosomal fusion / IRAK2 mediated activation of TAK1 complex / Alpha-protein kinase 1 signaling pathway / Glycogen synthesis / IRAK1 recruits IKK complex / IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation / Endosomal Sorting Complex Required For Transport (ESCRT) / Membrane binding and targetting of GAG proteins / Negative regulation of FLT3 / Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Regulation of TBK1, IKKε-mediated activation of IRF3, IRF7 upon TLR3 ligation / Constitutive Signaling by NOTCH1 HD Domain Mutants / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / cytosolic ribosome / NOTCH2 Activation and Transmission of Signal to the Nucleus / TICAM1,TRAF6-dependent induction of TAK1 complex / TICAM1-dependent activation of IRF3/IRF7 / APC/C:Cdc20 mediated degradation of Cyclin B / Downregulation of ERBB4 signaling / Regulation of FZD by ubiquitination / APC-Cdc20 mediated degradation of Nek2A / p75NTR recruits signalling complexes / InlA-mediated entry of Listeria monocytogenes into host cells / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / TRAF6-mediated induction of TAK1 complex within TLR4 complex / Regulation of pyruvate metabolism / NF-kB is activated and signals survival / Regulation of innate immune responses to cytosolic DNA / Downregulation of ERBB2:ERBB3 signaling / Pexophagy / RNA splicing / NRIF signals cell death from the nucleus / VLDLR internalisation and degradation / Regulation of PTEN localization / Activated NOTCH1 Transmits Signal to the Nucleus / Regulation of BACH1 activity / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / MAP3K8 (TPL2)-dependent MAPK1/3 activation / TICAM1, RIP1-mediated IKK complex recruitment / Translesion synthesis by REV1 / InlB-mediated entry of Listeria monocytogenes into host cell / Translesion synthesis by POLK / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / Downregulation of TGF-beta receptor signaling / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / Josephin domain DUBs / Translesion synthesis by POLI / Regulation of activated PAK-2p34 by proteasome mediated degradation / IKK complex recruitment mediated by RIP1 / Gap-filling DNA repair synthesis and ligation in GG-NER / PINK1-PRKN Mediated Mitophagy / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / TNFR1-induced NF-kappa-B signaling pathway / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / TCF dependent signaling in response to WNT / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Regulation of NF-kappa B signaling / Asymmetric localization of PCP proteins / Ubiquitin-dependent degradation of Cyclin D / activated TAK1 mediates p38 MAPK activation / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / TNFR2 non-canonical NF-kB pathway
Similarity search - Function
Yeast SAGA-associated factor 11, N-terminal domain / SAGA-associated factor 11 N-terminal domain / ENY2/SUS1 / SAGA-associated factor 73, zinc finger domain / Zinc finger domain / SAGA complex, Sgf11 subunit / Sgf11 (transcriptional regulation protein) / Transcription factor, enhancer of yellow 2 / SAGA-associated factor 73 / Transcription factor EnY2 superfamily ...Yeast SAGA-associated factor 11, N-terminal domain / SAGA-associated factor 11 N-terminal domain / ENY2/SUS1 / SAGA-associated factor 73, zinc finger domain / Zinc finger domain / SAGA complex, Sgf11 subunit / Sgf11 (transcriptional regulation protein) / Transcription factor, enhancer of yellow 2 / SAGA-associated factor 73 / Transcription factor EnY2 superfamily / Transcription factor e(y)2 / SCA7 domain / SCA7, zinc-binding domain / SCA7 domain profile. / Helix Hairpins - #210 / : / Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger / Zinc finger, UBP-type / Zn-finger in ubiquitin-hydrolases and other protein / Zinc finger UBP-type profile. / Classic Zinc Finger / Ubiquitin specific protease (USP) domain signature 2. / Ubiquitin specific protease (USP) domain signature 1. / Ubiquitin specific protease, conserved site / Serum Albumin; Chain A, Domain 1 / Peptidase C19, ubiquitin carboxyl-terminal hydrolase / Ubiquitin carboxyl-terminal hydrolase / Ubiquitin specific protease domain / Ubiquitin specific protease (USP) domain profile. / Cysteine proteinases / Zinc/RING finger domain, C3HC4 (zinc finger) / Cathepsin B; Chain A / Herpes Virus-1 / Double Stranded RNA Binding Domain / Ribosomal L40e family / Ribosomal_L40e / Ribosomal protein L40e / Ribosomal protein L40e superfamily / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / Papain-like cysteine peptidase superfamily / : / Ubiquitin domain signature. / Ubiquitin conserved site / Ubiquitin domain / Ubiquitin-like (UB roll) / Ubiquitin family / Helix Hairpins / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Zinc finger, RING/FYVE/PHD-type / Ubiquitin-like domain superfamily / Roll / Alpha-Beta Complex / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Polyubiquitin-C / Ubiquitin carboxyl-terminal hydrolase 8 / SAGA complex subunit SGF73 / Ubiquitin-60S ribosomal protein L40 / SAGA complex subunit SGF11 / SAGA complex subunit SUS1
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 1.89 Å
AuthorsSamara, N.L. / Datta, A.B. / Berndsen, C.E. / Zhang, X. / Yao, T. / Cohen, R.E. / Wolberger, C.
CitationJournal: Science / Year: 2010
Title: Structural insights into the assembly and function of the SAGA deubiquitinating module.
Authors: Samara, N.L. / Datta, A.B. / Berndsen, C.E. / Zhang, X. / Yao, T. / Cohen, R.E. / Wolberger, C.
History
DepositionApr 8, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 21, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Mar 26, 2025Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / pdbx_struct_conn_angle / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_PDB_ins_code / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_PDB_ins_code / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_ptnr1_PDB_ins_code / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Ubiquitin carboxyl-terminal hydrolase 8
B: Protein SUS1
C: SAGA-associated factor 11
D: Ubiquitin
E: SAGA-associated factor 73
hetero molecules


Theoretical massNumber of molelcules
Total (without water)96,48815
Polymers95,8115
Non-polymers67710
Water15,223845
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area21400 Å2
ΔGint-96 kcal/mol
Surface area34050 Å2
MethodPISA
Unit cell
Length a, b, c (Å)78.600, 102.084, 120.903
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

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Protein , 3 types, 3 molecules ABD

#1: Protein Ubiquitin carboxyl-terminal hydrolase 8 / Ubiquitin thioesterase 8 / Ubiquitin-specific-processing protease 8 / Deubiquitinating enzyme 8


Mass: 54033.633 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: UBP8, YMR223W, YM9959.05 / Plasmid details: T7 based / Plasmid: pET32a, pCDF, pRSF / Production host: Escherichia coli (E. coli) / Strain (production host): Rosettta2 pLysS / References: UniProt: P50102, EC: 3.1.2.15
#2: Protein Protein SUS1


Mass: 11094.497 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: SUS1, YBR111W-A / Plasmid details: T7 based / Plasmid: pET32a, pCDF, pRSF / Production host: Escherichia coli (E. coli) / Strain (production host): Rosettta2 pLysS / References: UniProt: Q6WNK7
#4: Protein Ubiquitin


Mass: 8560.831 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RPS27A, UBA52, UBB, UBC / Plasmid details: T7 based / Plasmid: pET32a, pCDF, pRSF / Production host: Escherichia coli (E. coli) / Strain (production host): Rosettta2 pLysS / References: UniProt: P62988, UniProt: P0CG48*PLUS

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SAGA-associated factor ... , 2 types, 2 molecules CE

#3: Protein SAGA-associated factor 11 / 11 kDa SAGA-associated factor


Mass: 11297.625 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: SGF11, YPL047W / Plasmid details: T7 based / Plasmid: pET32a, pCDF, pRSF / Production host: Escherichia coli (E. coli) / Strain (production host): Rosettta2 pLysS / References: UniProt: Q03067
#5: Protein SAGA-associated factor 73 / 73 kDa SAGA-associated factor / SAGA histone acetyltransferase complex 73 kDa subunit


Mass: 10824.273 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: SGF73, YGL066W / Plasmid details: T7 based / Plasmid: pET32a, pCDF, pRSF / Production host: Escherichia coli (E. coli) / Strain (production host): Rosettta2 pLysS / References: UniProt: P53165

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Non-polymers , 4 types, 855 molecules

#6: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6O2
#7: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#8: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Zn
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 845 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.53 Å3/Da / Density % sol: 51.41 %
Description: THE INITIAL STRUCTURE WAS DETERMINED WITH 3 WAVELENGTH SE-MAD USING THE FOLLOWING WAVELENGTHS (EV): PEAK: 12658.7 HIGH REMOTE: 13058.7 INFLECTION: 12656.9 THE STRUCTURE WAS THEN REFINED ...Description: THE INITIAL STRUCTURE WAS DETERMINED WITH 3 WAVELENGTH SE-MAD USING THE FOLLOWING WAVELENGTHS (EV): PEAK: 12658.7 HIGH REMOTE: 13058.7 INFLECTION: 12656.9 THE STRUCTURE WAS THEN REFINED AGAINST A NATIVE DATA SET COLLECTED AT A WAVELENGTH OF 13058.7 (EV). THE FINAL COORDINATES REPRESENT THE NATIVE DATA SET.
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 0.1 M Hepes pH 6.5, 10% (w/v) PEG 8000, 20% (v/v) Glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-B / Wavelength: 0.94944 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Mar 12, 2010
Details: K-B pair of biomorph mirrors with two additional horizontally deflecting mirrors
RadiationMonochromator: double crystal monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.94944 Å / Relative weight: 1
ReflectionResolution: 1.89→35.1 Å / Num. all: 78011 / Num. obs: 73928 / % possible obs: 99.8 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 13.7 % / Rmerge(I) obs: 0.096 / Rsym value: 0.096 / Net I/σ(I): 29.5
Reflection shellResolution: 1.89→1.93 Å / Redundancy: 8.4 % / Rmerge(I) obs: 0.886 / Mean I/σ(I) obs: 2.25 / Rsym value: 0.886 / % possible all: 98.8

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Processing

Software
NameVersionClassification
Blu-Icedata collection
SHELXDphasing
REFMAC5.5.0102refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MAD / Resolution: 1.89→35.1 Å / Cor.coef. Fo:Fc: 0.966 / Cor.coef. Fo:Fc free: 0.94 / SU B: 5.921 / SU ML: 0.083 / Cross valid method: THROUGHOUT / ESU R: 0.126 / ESU R Free: 0.127 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.20757 3934 5.1 %RANDOM
Rwork0.15904 ---
obs0.16148 73928 99.26 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 30.086 Å2
Baniso -1Baniso -2Baniso -3
1-0.48 Å20 Å20 Å2
2--0.18 Å20 Å2
3----0.65 Å2
Refinement stepCycle: LAST / Resolution: 1.89→35.1 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6391 0 18 845 7254
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0150.0226776
X-RAY DIFFRACTIONr_bond_other_d0.0010.024631
X-RAY DIFFRACTIONr_angle_refined_deg1.3991.969167
X-RAY DIFFRACTIONr_angle_other_deg0.8593.00311385
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.4995858
X-RAY DIFFRACTIONr_dihedral_angle_2_deg38.26325.539334
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.993151276
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.4561529
X-RAY DIFFRACTIONr_chiral_restr0.180.21024
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.027505
X-RAY DIFFRACTIONr_gen_planes_other0.0010.021285
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.3471.54098
X-RAY DIFFRACTIONr_mcbond_other0.4281.51655
X-RAY DIFFRACTIONr_mcangle_it2.29326673
X-RAY DIFFRACTIONr_scbond_it3.79232678
X-RAY DIFFRACTIONr_scangle_it5.2454.52465
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.89→1.939 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.288 240 -
Rwork0.235 4990 -
obs--92.26 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
10.58150.2181-0.00420.9011-0.12030.54120.0104-0.1215-0.00030.1473-0.0343-0.02910.0290.03940.0240.03860.01630.00730.04910.010.043750.944723.120785.7836
21.47630.8384-0.46211.5178-0.09433.5259-0.0643-0.074-0.10490.0333-0.0359-0.3790.30110.81530.10020.06310.0921-0.0490.2820.08880.266176.229825.492891.2926
31.2640.43510.27651.0433-0.01930.5630.0652-0.0124-0.1970.1783-0.0228-0.1220.14010.0572-0.04240.1520.07330.01910.13710.08910.092150.1478.894592.2796
41.3345-0.3020.66661.89650.35210.6849-0.02390.07350.0341-0.187-0.04650.23370.0041-0.07350.07030.0468-0.0307-0.01620.05350.00510.078936.799427.289260.2129
50.330.37220.13391.3448-0.35660.75760.0182-0.12590.0810.3002-0.0676-0.1452-0.10290.07370.04940.14670.0204-0.04430.1856-0.05960.153759.05934.63896.5105
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A-10 - 9999
2X-RAY DIFFRACTION2B-10 - 9999
3X-RAY DIFFRACTION3C-10 - 9999
4X-RAY DIFFRACTION4D-10 - 9999
5X-RAY DIFFRACTION5E-10 - 9999

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