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- PDB-6gfz: pVHL:EloB:EloC in complex with modified VH032 containing (3S,4S)-... -

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Basic information

Entry
Database: PDB / ID: 6gfz
TitlepVHL:EloB:EloC in complex with modified VH032 containing (3S,4S)-3-fluoro-4-hydroxyproline (ligand 14b)
Components
  • Elongin-B
  • Elongin-C
  • von Hippel-Lindau disease tumor suppressor
KeywordsLIGASE / protein complex / ubiquitin ligase / hypoxia inducible factor / fluorinated hydroxyproline
Function / homology
Function and homology information


regulation of cellular response to hypoxia / RHOBTB3 ATPase cycle / negative regulation of receptor signaling pathway via JAK-STAT / transcription elongation factor activity / target-directed miRNA degradation / elongin complex / VCB complex / Replication of the SARS-CoV-1 genome / Cul5-RING ubiquitin ligase complex / Cul2-RING ubiquitin ligase complex ...regulation of cellular response to hypoxia / RHOBTB3 ATPase cycle / negative regulation of receptor signaling pathway via JAK-STAT / transcription elongation factor activity / target-directed miRNA degradation / elongin complex / VCB complex / Replication of the SARS-CoV-1 genome / Cul5-RING ubiquitin ligase complex / Cul2-RING ubiquitin ligase complex / intracellular non-membrane-bounded organelle / SUMOylation of ubiquitinylation proteins / negative regulation of transcription elongation by RNA polymerase II / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / ubiquitin-like ligase-substrate adaptor activity / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / Formation of HIV elongation complex in the absence of HIV Tat / negative regulation of signal transduction / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / negative regulation of TORC1 signaling / RNA Polymerase II Pre-transcription Events / negative regulation of autophagy / transcription corepressor binding / transcription elongation by RNA polymerase II / transcription initiation at RNA polymerase II promoter / positive regulation of cell differentiation / TP53 Regulates Transcription of DNA Repair Genes / Vif-mediated degradation of APOBEC3G / cell morphogenesis / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / Inactivation of CSF3 (G-CSF) signaling / Regulation of expression of SLITs and ROBOs / ubiquitin-protein transferase activity / transcription corepressor activity / protein-macromolecule adaptor activity / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Antigen processing: Ubiquitination & Proteasome degradation / Neddylation / Replication of the SARS-CoV-2 genome / ubiquitin-dependent protein catabolic process / cellular response to hypoxia / proteasome-mediated ubiquitin-dependent protein catabolic process / regulation of gene expression / protein-containing complex assembly / DNA-binding transcription factor binding / amyloid fibril formation / protein stabilization / molecular adaptor activity / protein ubiquitination / negative regulation of cell population proliferation / negative regulation of gene expression / ubiquitin protein ligase binding / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / negative regulation of apoptotic process / positive regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / enzyme binding / endoplasmic reticulum / mitochondrion / proteolysis / nucleoplasm / nucleus / plasma membrane / cytosol
Similarity search - Function
von Hippel-Lindau disease tumour suppressor, alpha domain / von Hippel-Lindau disease tumour suppressor, beta domain / Elongin C; Chain C, domain 1 / von Hippel-Lindau disease tumour suppressor, beta/alpha domain / von Hippel-Lindau disease tumour suppressor, alpha domain / von Hippel-Lindau disease tumour suppressor, beta domain / VHL superfamily / von Hippel-Lindau disease tumour suppressor, alpha domain superfamily / von Hippel-Lindau disease tumour suppressor, beta domain superfamily / VHL beta domain ...von Hippel-Lindau disease tumour suppressor, alpha domain / von Hippel-Lindau disease tumour suppressor, beta domain / Elongin C; Chain C, domain 1 / von Hippel-Lindau disease tumour suppressor, beta/alpha domain / von Hippel-Lindau disease tumour suppressor, alpha domain / von Hippel-Lindau disease tumour suppressor, beta domain / VHL superfamily / von Hippel-Lindau disease tumour suppressor, alpha domain superfamily / von Hippel-Lindau disease tumour suppressor, beta domain superfamily / VHL beta domain / VHL box domain / Elongin B / Elongin-C / Potassium Channel Kv1.1; Chain A / Potassium Channel Kv1.1; Chain A / S-phase kinase-associated protein 1-like / SKP1 component, POZ domain / Skp1 family, tetramerisation domain / Found in Skp1 protein family / SKP1/BTB/POZ domain superfamily / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / Ubiquitin-like (UB roll) / Ubiquitin family / Ubiquitin homologues / Ubiquitin-like domain / Ubiquitin domain profile. / Ubiquitin-like domain superfamily / Roll / Immunoglobulin-like / Sandwich / 2-Layer Sandwich / Orthogonal Bundle / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Chem-EXE / von Hippel-Lindau disease tumor suppressor / Elongin-C / Elongin-B
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å
Model detailspVHL:EloB:EloC in complex with ........ (ligand 14b)
AuthorsGadd, M.S. / Testa, A. / Ciulli, A.
Funding support1items
OrganizationGrant numberCountry
European Research CouncilERC-2012-StG-311460 DrugE3CRLs
CitationJournal: J. Am. Chem. Soc. / Year: 2018
Title: 3-Fluoro-4-hydroxyprolines: Synthesis, Conformational Analysis, and Stereoselective Recognition by the VHL E3 Ubiquitin Ligase for Targeted Protein Degradation.
Authors: Testa, A. / Lucas, X. / Castro, G.V. / Chan, K.H. / Wright, J.E. / Runcie, A.C. / Gadd, M.S. / Harrison, W.T.A. / Ko, E.J. / Fletcher, D. / Ciulli, A.
History
DepositionMay 2, 2018Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 11, 2018Provider: repository / Type: Initial release
Revision 1.1Aug 1, 2018Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2Jan 17, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Elongin-B
B: Elongin-C
C: von Hippel-Lindau disease tumor suppressor
D: Elongin-B
E: Elongin-C
F: von Hippel-Lindau disease tumor suppressor
G: Elongin-B
H: Elongin-C
I: von Hippel-Lindau disease tumor suppressor
J: Elongin-B
K: Elongin-C
L: von Hippel-Lindau disease tumor suppressor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)168,91116
Polymers166,94912
Non-polymers1,9624
Water12,304683
1
A: Elongin-B
B: Elongin-C
C: von Hippel-Lindau disease tumor suppressor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,2284
Polymers41,7373
Non-polymers4911
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
D: Elongin-B
E: Elongin-C
F: von Hippel-Lindau disease tumor suppressor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,2284
Polymers41,7373
Non-polymers4911
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
G: Elongin-B
H: Elongin-C
I: von Hippel-Lindau disease tumor suppressor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,2284
Polymers41,7373
Non-polymers4911
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
4
J: Elongin-B
K: Elongin-C
L: von Hippel-Lindau disease tumor suppressor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,2284
Polymers41,7373
Non-polymers4911
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)93.609, 93.609, 364.511
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number91
Space group name H-MP4122
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21D
31G
41J
12B
22E
32H
42K
13C
23F
33I
43L
14C
24F
34I
15C
25F
35I
45L

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1114A1 - 999
2114D1 - 999
3114G1 - 999
4114J1 - 999
1124B1 - 999
2124E1 - 999
3124H1 - 999
4124K1 - 999
1134C1 - 169
2134F1 - 169
3134I1 - 169
4134L1 - 169
1144C170 - 186
2144F170 - 186
3144I170 - 186
1154C186 - 999
2154F186 - 999
3154I186 - 999
4154L186 - 999

NCS ensembles :
ID
1
2
3
4
5

NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(0.999829, 0.01673, -0.007915), (-0.016709, 0.999857, 0.002691), (0.007959, -0.002559, 0.999965)-3.77709, 48.00103, -0.27033
3given(0.998271, -0.057435, 0.012485), (0.058231, 0.995313, -0.077213), (-0.007992, 0.077806, 0.996937)41.919071, 55.368698, -0.64527
4given(0.999023, -0.035365, 0.026514), (0.037037, 0.997167, -0.065473), (-0.024123, 0.066392, 0.997502)46.62101, 7.34833, -4.00368
5given(1), (1), (1)
6given(0.999912, 0.011353, -0.006895), (-0.011383, 0.999926, -0.004304), (0.006846, 0.004382, 0.999967)-3.88556, 48.130341, -0.33825
7given(0.998857, -0.039187, 0.027359), (0.041794, 0.993869, -0.102356), (-0.02318, 0.103383, 0.994371)40.900291, 56.625431, -0.63677
8given(0.999183, -0.018294, 0.036035), (0.021558, 0.995492, -0.092362), (-0.034183, 0.093063, 0.995073)45.18663, 8.81966, -5.32789
9given(1), (1), (1)
10given(0.999781, -0.020777, 0.002535), (0.020819, 0.999627, -0.017703), (-0.002167, 0.017752, 0.99984)-4.40006, 47.76609, 0.05201
11given(0.997983, -0.059442, 0.022275), (0.060527, 0.996826, -0.051713), (-0.019131, 0.052957, 0.998414)41.045559, 52.696091, -0.58325
12given(0.998339, -0.047983, 0.031894), (0.04927, 0.997949, -0.040879), (-0.029867, 0.042382, 0.998655)46.810242, 4.92586, -2.97214
13given(1), (1), (1)
14given(0.999972, -0.003392, -0.006745), (0.003169, 0.999459, -0.032738), (0.006853, 0.032715, 0.999441)-3.80987, 49.552349, -0.27511
15given(0.995554, -0.082878, -0.044768), (0.080345, 0.99521, -0.055692), (0.049169, 0.051848, 0.997444)46.246361, 53.604061, -0.72298
16given(1), (1), (1)
17given(0.999999, 0.000931, 0.00118), (-0.000912, 0.999879, -0.0155), (-0.001194, 0.015499, 0.999879)-4.42258, 48.396069, 0.01085
18given(0.996562, -0.074274, 0.036719), (0.076364, 0.995317, -0.059263), (-0.032146, 0.061863, 0.997567)39.814369, 53.398479, -0.51606
19given(0.999216, 0.000389, 0.039582), (0.001358, 0.999027, -0.04409), (-0.039561, 0.044109, 0.998243)43.55587, 4.49308, -3.09222

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Components

#1: Protein
Elongin-B / EloB / Elongin 18 kDa subunit / RNA polymerase II transcription factor SIII subunit B / SIII p18 / ...EloB / Elongin 18 kDa subunit / RNA polymerase II transcription factor SIII subunit B / SIII p18 / Transcription elongation factor B polypeptide 2


Mass: 11956.372 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ELOB, TCEB2 / Plasmid: pCDFDuet-1 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q15370
#2: Protein
Elongin-C / EloC / Elongin 15 kDa subunit / RNA polymerase II transcription factor SIII subunit C / SIII p15 / ...EloC / Elongin 15 kDa subunit / RNA polymerase II transcription factor SIII subunit C / SIII p15 / Transcription elongation factor B polypeptide 1


Mass: 10974.616 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ELOC, TCEB1 / Plasmid: pCDFDuet-1 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q15369
#3: Protein
von Hippel-Lindau disease tumor suppressor / Protein G7 / pVHL


Mass: 18806.273 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: VHL / Plasmid: pHAT4 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P40337
#4: Chemical
ChemComp-EXE / (2~{R},3~{S},4~{S})-1-[(2~{S})-2-acetamido-3,3-dimethyl-butanoyl]-3-fluoranyl-~{N}-[[4-(4-methyl-1,3-thiazol-5-yl)phenyl]methyl]-4-oxidanyl-pyrrolidine-2-carboxamide


Mass: 490.591 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C24H31FN4O4S / Feature type: SUBJECT OF INVESTIGATION
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 683 / Source method: isolated from a natural source / Formula: H2O

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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: 2.39 Å3/Da / Density % sol: 48.57 % / Mosaicity: 0.05 °
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 6.4 / Details: PEG 3350, MgOAc, Sodium cacodylate, DTT

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.9795 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Dec 1, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.3→49.01 Å / Num. obs: 73389 / % possible obs: 100 % / Redundancy: 8.8 % / CC1/2: 0.999 / Rmerge(I) obs: 0.085 / Rpim(I) all: 0.03 / Rrim(I) all: 0.091 / Net I/σ(I): 14.5
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) all% possible all
2.3-2.358.90.89844410.820.3150.954100
11.27-49.016.90.037730.9990.0130.03398.8

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Processing

Software
NameVersionClassification
XDSdata reduction
Aimless0.3.11data scaling
REFMACrefinement
PDB_EXTRACT3.24data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5NVV

5nvv


Resolution: 2.3→49.01 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.942 / SU B: 14.349 / SU ML: 0.185 / SU R Cruickshank DPI: 0.316 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.316 / ESU R Free: 0.233
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED
RfactorNum. reflection% reflectionSelection details
Rfree0.2449 3703 5.1 %RANDOM
Rwork0.1948 ---
obs0.1974 69573 99.88 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso max: 165.69 Å2 / Biso mean: 54.614 Å2 / Biso min: 24.9 Å2
Baniso -1Baniso -2Baniso -3
1-0.25 Å2-0 Å2-0 Å2
2--0.25 Å2-0 Å2
3----0.5 Å2
Refinement stepCycle: final / Resolution: 2.3→49.01 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10620 0 136 683 11439
Biso mean--39.52 49.44 -
Num. residues----1338
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.01911002
X-RAY DIFFRACTIONr_bond_other_d0.0020.0210524
X-RAY DIFFRACTIONr_angle_refined_deg1.3112.00114964
X-RAY DIFFRACTIONr_angle_other_deg0.7613.00424193
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.07651322
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.35323.32485
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.583151810
X-RAY DIFFRACTIONr_dihedral_angle_4_deg18.9951589
X-RAY DIFFRACTIONr_chiral_restr0.0670.21709
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.02112168
X-RAY DIFFRACTIONr_gen_planes_other0.0010.022445
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
11A1584MEDIUM POSITIONAL0.280.5
12D1584MEDIUM POSITIONAL0.330.5
13G1584MEDIUM POSITIONAL0.290.5
14J1584MEDIUM POSITIONAL0.280.5
11A1584MEDIUM THERMAL4.672
12D1584MEDIUM THERMAL3.782
13G1584MEDIUM THERMAL7.422
14J1584MEDIUM THERMAL4.912
21B1358MEDIUM POSITIONAL0.350.5
22E1358MEDIUM POSITIONAL0.350.5
23H1358MEDIUM POSITIONAL0.410.5
24K1358MEDIUM POSITIONAL0.370.5
21B1358MEDIUM THERMAL6.042
22E1358MEDIUM THERMAL5.242
23H1358MEDIUM THERMAL6.212
24K1358MEDIUM THERMAL5.422
31C1690MEDIUM POSITIONAL0.370.5
32F1690MEDIUM POSITIONAL0.380.5
33I1690MEDIUM POSITIONAL0.320.5
34L1690MEDIUM POSITIONAL0.420.5
31C1690MEDIUM THERMAL3.142
32F1690MEDIUM THERMAL5.582
33I1690MEDIUM THERMAL3.422
34L1690MEDIUM THERMAL5.752
41C252MEDIUM POSITIONAL0.30.5
42F252MEDIUM POSITIONAL0.260.5
43I252MEDIUM POSITIONAL0.50.5
41C252MEDIUM THERMAL7.162
42F252MEDIUM THERMAL4.292
43I252MEDIUM THERMAL7.42
51C228MEDIUM POSITIONAL0.540.5
52F228MEDIUM POSITIONAL0.460.5
53I228MEDIUM POSITIONAL0.530.5
54L228MEDIUM POSITIONAL0.530.5
51C228MEDIUM THERMAL5.352
52F228MEDIUM THERMAL8.682
53I228MEDIUM THERMAL6.772
54L228MEDIUM THERMAL8.172
LS refinement shellResolution: 2.3→2.36 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.29 280 -
Rwork0.249 5013 -
all-5293 -
obs--99.77 %
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)
12.3682-1.26771.25643.5846-2.02743.66340.04730.30220.0399-0.5468-0.2606-0.17580.13090.4220.21330.15530.00470.03980.18910.04720.038444.71464.80647.6
22.9719-0.71570.34571.2928-1.10033.3987-0.1087-0.14190.07990.069-0.0164-0.2799-0.08140.0910.12510.07210.00230.00490.25080.04460.099148.32561.13165.186
34.5238-0.9675-2.07531.35870.67671.8564-0.053-0.1452-0.0540.1039-0.0324-0.04260.03510.03140.08550.0536-0.0591-0.03610.30910.09860.05327.31654.33182.344
42.8252-1.04722.94891.7401-1.29575.9952-0.12320.90460.2374-0.3289-0.1306-0.0338-0.71171.64650.25380.342-0.23070.02730.70390.03350.082448.2718.07447.317
53.74370.01752.05540.3144-0.78094.7307-0.15250.71170.02190.05530.0436-0.0951-0.28130.74120.10890.1209-0.0730.02450.4788-0.03040.059852.814.08865.121
65.3261-0.8037-1.05881.55670.50852.2618-0.0755-0.1635-0.15940.07360.0796-0.0437-0.0226-0.0388-0.00410.0337-0.0171-0.01320.25040.04010.017231.7917.7582.037
73.4984-1.04360.40742.1745-1.38053.9690.03120.34940.2024-0.3209-0.09710.006-0.18080.41710.06590.2074-0.09320.03840.470.01950.05033.13412.98347.459
84.78821.2103-0.79761.5172-1.32382.345-0.131-0.84770.11790.0456-0.0087-0.0043-0.15690.55420.13970.15-0.02040.03690.7727-0.03230.05586.76910.83565.243
92.6693-0.6068-1.54541.8285-0.07264.2299-0.0576-0.22740.01730.0333-0.0590.05220.06010.66770.11660.0132-0.0321-0.00710.45-0.00370.0286-14.4736.78982.326
102.8963-1.0802-0.68112.6082-0.74083.5586-0.00350.24090.0725-0.2245-0.11010.0827-0.07330.30710.11360.1315-0.0542-0.01610.20290.05730.027-0.88760.62347.726
113.37140.2829-0.2010.7467-0.96123.2032-0.1364-0.25180.10610.0730.01240.0095-0.1350.36240.1240.079-0.01460.0130.3110.04240.03942.12658.50665.494
122.7311-0.2905-1.61491.44670.05613.1212-0.1495-0.2640.0808-0.01480.0180.06730.08720.30790.13140.0411-0.0098-0.02530.30470.08020.077-19.06653.9682.603
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 104
2X-RAY DIFFRACTION2B16 - 112
3X-RAY DIFFRACTION3C62 - 202
4X-RAY DIFFRACTION4D1 - 103
5X-RAY DIFFRACTION5E16 - 112
6X-RAY DIFFRACTION6F62 - 204
7X-RAY DIFFRACTION7G1 - 103
8X-RAY DIFFRACTION8H16 - 112
9X-RAY DIFFRACTION9I62 - 204
10X-RAY DIFFRACTION10J1 - 103
11X-RAY DIFFRACTION11K16 - 112
12X-RAY DIFFRACTION12L62 - 204

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