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- PDB-4imy: The AFF4 scaffold binds human P-TEFb adjacent to HIV Tat -

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Basic information

Entry
Database: PDB / ID: 4imy
TitleThe AFF4 scaffold binds human P-TEFb adjacent to HIV Tat
Components
  • AF4/FMR2 family member 4
  • Cyclin-T1
  • Cyclin-dependent kinase 9
KeywordsTRANSFERASE / Transcriptional CDK9-CycT1 complex / phosphorylated / intrinsically disordered AFF4 / regulation of transcription elongation / Ser/Thr kinase / phosphorylation of PolII-CTD / DSIF / and NELF / HIV-1 Tat / Host-virus interaction / phosphoprotein / nucleus
Function / homology
Function and homology information


super elongation complex / P-TEFb complex / Interactions of Tat with host cellular proteins / nucleus localization / 7SK snRNA binding / cyclin/CDK positive transcription elongation factor complex / regulation of mRNA 3'-end processing / regulation of muscle cell differentiation / positive regulation of protein localization to chromatin / transcription elongation factor activity ...super elongation complex / P-TEFb complex / Interactions of Tat with host cellular proteins / nucleus localization / 7SK snRNA binding / cyclin/CDK positive transcription elongation factor complex / regulation of mRNA 3'-end processing / regulation of muscle cell differentiation / positive regulation of protein localization to chromatin / transcription elongation factor activity / regulation of cyclin-dependent protein serine/threonine kinase activity / cyclin-dependent protein serine/threonine kinase activator activity / host-mediated activation of viral transcription / [RNA-polymerase]-subunit kinase / RNA polymerase binding / positive regulation of DNA-templated transcription, elongation / negative regulation of protein localization to chromatin / transcription elongation-coupled chromatin remodeling / cellular response to cytokine stimulus / spermatid development / replication fork processing / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / RNA polymerase II transcribes snRNA genes / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / cyclin-dependent kinase / Tat-mediated elongation of the HIV-1 transcript / cyclin-dependent protein serine/threonine kinase activity / Formation of HIV-1 elongation complex containing HIV-1 Tat / Formation of HIV elongation complex in the absence of HIV Tat / regulation of DNA repair / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / RNA Polymerase II Pre-transcription Events / RNA polymerase II CTD heptapeptide repeat kinase activity / response to endoplasmic reticulum stress / transcription elongation factor complex / transcription initiation at RNA polymerase II promoter / TP53 Regulates Transcription of DNA Repair Genes / transcription elongation by RNA polymerase II / positive regulation of transcription elongation by RNA polymerase II / SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription / molecular condensate scaffold activity / euchromatin / transcription coactivator binding / PML body / cytoplasmic ribonucleoprotein granule / fibrillar center / kinase activity / regulation of gene expression / DNA-binding transcription factor binding / Estrogen-dependent gene expression / transcription by RNA polymerase II / cell population proliferation / transcription cis-regulatory region binding / regulation of cell cycle / protein kinase activity / nuclear body / protein phosphorylation / response to xenobiotic stimulus / RNA polymerase II cis-regulatory region sequence-specific DNA binding / cell division / protein serine kinase activity / DNA repair / protein serine/threonine kinase activity / chromatin binding / protein kinase binding / positive regulation of transcription by RNA polymerase II / DNA binding / nucleoplasm / ATP binding / nucleus / membrane / cytosol
Similarity search - Function
Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #2670 / AF4/FMR2 family / AF4 interaction motif / AF4/FMR2, C-terminal homology domain / AF-4 proto-oncoprotein N-terminal region / AF4 interaction motif / AFF4, C-terminal homology domain / : / Cyclin-T2-like, C-terminal domain / Cyclin/Cyclin-like subunit Ssn8 ...Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #2670 / AF4/FMR2 family / AF4 interaction motif / AF4/FMR2, C-terminal homology domain / AF-4 proto-oncoprotein N-terminal region / AF4 interaction motif / AFF4, C-terminal homology domain / : / Cyclin-T2-like, C-terminal domain / Cyclin/Cyclin-like subunit Ssn8 / Cyclin-like / Cyclin A; domain 1 / Cyclin, N-terminal / Cyclin, N-terminal domain / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Cyclin-like / domain present in cyclins, TFIIB and Retinoblastoma / Cyclin-like superfamily / : / Helix non-globular / Special / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
ADENOSINE MONOPHOSPHATE / Cyclin-T1 / Cyclin-dependent kinase 9 / AF4/FMR2 family member 4
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.94 Å
AuthorsAlber, T. / Schulze-Gahmen, U.
CitationJournal: Elife / Year: 2013
Title: The AFF4 scaffold binds human P-TEFb adjacent to HIV Tat.
Authors: Schulze-Gahmen, U. / Upton, H. / Birnberg, A. / Bao, K. / Chou, S. / Krogan, N.J. / Zhou, Q. / Alber, T.
History
DepositionJan 3, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 13, 2013Provider: repository / Type: Initial release
Revision 1.1Apr 3, 2013Group: Database references
Revision 1.2Sep 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.3Nov 20, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Cyclin-dependent kinase 9
B: Cyclin-T1
C: Cyclin-dependent kinase 9
D: Cyclin-T1
E: Cyclin-dependent kinase 9
F: Cyclin-T1
G: AF4/FMR2 family member 4
H: AF4/FMR2 family member 4
I: AF4/FMR2 family member 4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)233,94712
Polymers232,9059
Non-polymers1,0423
Water34219
1
A: Cyclin-dependent kinase 9
B: Cyclin-T1
G: AF4/FMR2 family member 4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)77,9824
Polymers77,6353
Non-polymers3471
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5390 Å2
ΔGint-39 kcal/mol
Surface area28060 Å2
MethodPISA
2
C: Cyclin-dependent kinase 9
D: Cyclin-T1
H: AF4/FMR2 family member 4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)77,9824
Polymers77,6353
Non-polymers3471
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6530 Å2
ΔGint-30 kcal/mol
Surface area28870 Å2
MethodPISA
3
E: Cyclin-dependent kinase 9
F: Cyclin-T1
I: AF4/FMR2 family member 4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)77,9824
Polymers77,6353
Non-polymers3471
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5380 Å2
ΔGint-33 kcal/mol
Surface area27530 Å2
MethodPISA
Unit cell
Length a, b, c (Å)100.691, 126.298, 195.626
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
31
12
22
32
13
23
33

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111chain 'A' and (resseq 8:23 or resseq 33: 87 or...
211chain 'C' and (resseq 8:23 or resseq 33: 87 or...
311chain 'E' and (resseq 8:23 or resseq 33: 49 or...
112chain 'B' and (resseq 8:215 or resseq 218:252 ) and (not element H)
212chain 'D' and (resseq 7:255 ) and (not element H)
312chain 'F' and (resseq 8:215 or resseq 218:255 ) and (not element H)
113chain 'G' and (resseq 35:65 ) and (not element H)
213chain 'H' and (resseq 39:65 ) and (not element H)
313chain 'I' and (resseq 35:65 ) and (not element H)

NCS ensembles :
ID
1
2
3

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Components

#1: Protein Cyclin-dependent kinase 9 / C-2K / Cell division cycle 2-like protein kinase 4 / Cell division protein kinase 9 / ...C-2K / Cell division cycle 2-like protein kinase 4 / Cell division protein kinase 9 / Serine/threonine-protein kinase PITALRE / Tat-associated kinase complex catalytic subunit


Mass: 38226.309 Da / Num. of mol.: 3 / Fragment: 1-330
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CDK9, CDC2L4, TAK / Production host: Spodoptera frugiperda (fall armyworm)
References: UniProt: P50750, cyclin-dependent kinase, [RNA-polymerase]-subunit kinase
#2: Protein Cyclin-T1 / CycT1 / Cyclin-T


Mass: 30618.959 Da / Num. of mol.: 3 / Fragment: 1-264
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CCNT1 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: O60563
#3: Protein AF4/FMR2 family member 4 / ALL1-fused gene from chromosome 5q31 protein / Protein AF-5q31 / Major CDK9 elongation factor- ...ALL1-fused gene from chromosome 5q31 protein / Protein AF-5q31 / Major CDK9 elongation factor-associated protein


Mass: 8789.776 Da / Num. of mol.: 3 / Fragment: 2-73
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: AFF4, AF5Q31, MCEF, HSPC092 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9UHB7
#4: Chemical ChemComp-AMP / ADENOSINE MONOPHOSPHATE


Mass: 347.221 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C10H14N5O7P / Comment: AMP*YM
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 19 / Source method: isolated from a natural source / Formula: H2O
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: 2.67 Å3/Da / Density % sol: 53.94 %
Crystal growTemperature: 291 K / pH: 7
Details: 0.1 M HEPES, pH 7.0, 16% PEG 3350, 0.1% Gly-Phe, 0.1% Gly-Tyr, 0.1% Leu-Gly-Gly. Microseeding, VAPOR DIFFUSION, SITTING DROP, temperature 291K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 8.3.1 / Wavelength: 1.11
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Jul 9, 2012
RadiationMonochromator: DOUBLE FLAT CRYSTAL SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.11 Å / Relative weight: 1
ReflectionResolution: 2.94→50 Å / Num. obs: 54164 / % possible obs: 100 % / Observed criterion σ(I): -3 / Redundancy: 8.1 % / Rsym value: 0.093 / Net I/σ(I): 23.2
Reflection shellResolution: 2.94→2.99 Å / Redundancy: 7.5 % / Rmerge(I) obs: 0 / Mean I/σ(I) obs: 1.3 / Rsym value: 0 / % possible all: 100

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Processing

Software
NameVersionClassification
HKL-2000data collection
PHASERphasing
PHENIX(phenix.refine: 1.8_1069)refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3MI9

3mi9


Resolution: 2.94→48.76 Å / SU ML: 0.34 / σ(F): 1.35 / Phase error: 27.38 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.245 2000 3.7 %
Rwork0.207 --
obs0.209 54118 99.7 %
all-54118 -
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.94→48.76 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms14496 0 69 19 14584
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00414907
X-RAY DIFFRACTIONf_angle_d0.66620225
X-RAY DIFFRACTIONf_dihedral_angle_d14.175540
X-RAY DIFFRACTIONf_chiral_restr0.0422288
X-RAY DIFFRACTIONf_plane_restr0.0022562
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A2373X-RAY DIFFRACTIONPOSITIONAL
12C373X-RAY DIFFRACTIONPOSITIONAL0.015
13E2291X-RAY DIFFRACTIONPOSITIONAL0.019
21B956X-RAY DIFFRACTIONPOSITIONAL
22D1956X-RAY DIFFRACTIONPOSITIONAL0.065
23F1956X-RAY DIFFRACTIONPOSITIONAL0.012
31G189X-RAY DIFFRACTIONPOSITIONAL
32H189X-RAY DIFFRACTIONPOSITIONAL0.012
33I219X-RAY DIFFRACTIONPOSITIONAL0.012
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.9309-3.00420.35971360.29943522X-RAY DIFFRACTION96
3.0042-3.08540.3731400.29113690X-RAY DIFFRACTION100
3.0854-3.17610.34571420.28343680X-RAY DIFFRACTION100
3.1761-3.27860.3111410.27373695X-RAY DIFFRACTION100
3.2786-3.39580.28351420.25873693X-RAY DIFFRACTION100
3.3958-3.53170.28481430.23793697X-RAY DIFFRACTION100
3.5317-3.69240.29021420.2253703X-RAY DIFFRACTION100
3.6924-3.8870.27021420.21783723X-RAY DIFFRACTION100
3.887-4.13040.24351430.19523703X-RAY DIFFRACTION100
4.1304-4.44910.20651420.1743736X-RAY DIFFRACTION100
4.4491-4.89650.22211450.16593755X-RAY DIFFRACTION100
4.8965-5.60410.22841440.18293773X-RAY DIFFRACTION100
5.6041-7.05720.25031470.21733807X-RAY DIFFRACTION100
7.0572-48.76350.20531510.19623941X-RAY DIFFRACTION99
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)
14.56260.2149-2.46130.226-0.96114.54720.2632-0.46610.18520.3786-0.3696-0.2861-0.6160.51470.0590.9809-0.16910.16540.5757-0.01191.015322.91148.062744.118
24.1389-2.36312.78652.0433-1.04492.89060.13040.20510.2084-0.1618-0.3341-0.24160.54520.15030.14580.7414-0.04960.27920.4525-0.03790.86636.00276.38441.904
33.6179-1.01711.51555.3068-0.50375.6475-0.0174-0.47140.62270.56210.09370.29840.1302-0.2576-0.03350.6795-0.13010.27950.6159-0.17840.9425-9.450214.570349.6188
46.62810.6545-2.38534.9951-0.89667.75640.565-1.0654-0.30430.8074-0.7369-0.5096-0.54851.14950.1470.8608-0.4102-0.02171.00240.2070.892929.3816-7.082864.0977
51.55641.9028-0.92556.4605-0.49743.1750.3701-0.6496-0.38180.3799-0.5304-0.2288-0.2140.69020.14250.5906-0.12050.00670.84180.20810.991220.2588-16.463366.5084
66.1764-3.12772.7095.9989-6.84399.07290.4118-0.0309-0.554-0.50120.39230.78380.35830.028-0.61970.76630.04180.07460.4428-0.04330.685410.864542.536963.9887
74.13310.7329-1.43173.3038-1.61135.03360.11860.31970.4219-0.14580.08220.0365-0.5640.2788-0.1970.7414-0.03970.1670.7204-0.04120.650227.200946.609859.1512
84.12440.0766-1.93474.1734-1.27538.1141-0.09250.0362-0.2251-0.0650.3101-0.53550.1790.9009-0.19590.6125-0.08930.15020.9286-0.21210.815842.509937.062853.3899
93.70071.4037-1.71464.20262.95424.3520.32160.19480.9331.52440.6980.5062-1.436-0.7552-1.28061.22640.2550.17071.05570.29011.15726.109548.893890.627
104.59310.82110.83346.3467-1.83956.15590.1785-0.1924-0.96830.42720.46090.45091.0941-0.498-0.47470.8915-0.01010.01720.49010.20430.863510.556528.511385.33
115.13661.32460.04825.2072-1.30417.36210.1749-0.8130.43140.9852-0.2846-0.5462-1.61981.15580.03421.0897-0.19220.02870.7915-0.02460.637726.250144.418198.9456
125.44564.8134-3.6524.8149-4.95017.6325-0.9367-0.5990.6629-0.73720.36520.08730.0913-0.99650.48070.94270.22650.08151.2734-0.09591.1009-2.55420.1696105.0887
137.2762-2.0079-0.33612.64041.09840.5007-0.06430.20550.39630.11140.00940.73570.0277-1.13920.21281.1640.19810.02671.23010.13630.80910.60870.4653103.5292
145.11523.12343.59824.84291.38855.2553-0.3131-0.13210.0513-0.16410.1423-0.0023-0.2979-0.67550.19620.56360.04320.11980.5857-0.01760.489716.2015-0.172111.4071
154.6074-0.21280.07644.34641.31315.0979-0.06970.6998-0.2588-0.65850.1795-1.5297-0.35060.5737-0.11570.9227-0.15360.3750.7435-0.09141.29534.83461.0426105.8201
163.8756-0.7408-1.89864.3301-1.03273.7955-0.003-0.0672-0.3281-0.19370.12010.12030.3553-1.0947-0.11660.7374-0.3467-0.11081.21790.06090.5405-3.7026-25.8892101.2172
173.7452-2.08251.92465.1281-2.27173.10470.4272-0.4973-0.406-0.1223-0.0415-0.29040.8524-0.4698-0.34820.8745-0.3639-0.22591.18330.13450.63288.057-36.8617119.3716
184.08062.8975-0.99314.12222.85578.7156-1.0757-0.6136-1.83330.77021.02461.2505-1.18251.37130.51160.8337-0.06730.3540.61650.32121.29627.144-34.835573.5282
194.3746-4.3046-0.54649.6002-3.5373.1625-0.1244-1.1344-3.4703-0.11930.05723.86812.56560.47990.12541.7457-0.0567-0.311.33530.76572.454423.96-33.263375.2731
202.72432.6906-0.92233.0249-1.70852.23720.1625-1.9182.15971.1696-1.0175-0.70110.69671.54511.12061.3468-0.4532-0.24451.56970.21591.19617.764-24.579383.3039
211.33060.78240.05791.6350.93610.6844-2.6991-0.76621.3031-0.31990.76390.1661.0460.6621.3331.75070.0126-0.52191.70890.56321.403438.290545.7008110.7471
223.5983-2.9271-0.00785.7096-3.82984.4988-1.512-4.11952.58813.32382.5017-2.81390.63041.24-1.18761.62210.3077-0.27031.3377-0.38571.552222.568641.1258113.4154
232.92821.99815.00782.67452.64312.0004-0.9618-0.16080.51722.41290.6698-0.62493.51663.8980.40041.20770.23160.2091.57860.18080.852629.238730.3778109.5443
242.80862.9368-1.3634.1581-0.78129.4457-1.0487-2.5074-2.14-2.0855-0.1177-0.75330.05710.67621.09421.1747-0.09480.03451.16390.21681.254217.0117-49.1775126.1919
253.51390.62462.20173.08081.06012.67440.55240.3113-1.67521.18560.0392-0.09081.64730.10250.04871.506-0.5731-0.69670.6006-0.1250.95456.4625-51.1819115.1379
264.69571.19431.54715.2496-2.73926.1190.2532-1.33841.75031.4180.5387-0.3179-0.08020.4382-0.92041.3233-0.41560.2031.3509-0.63511.583944.31259.957264.5045
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resseq 8:72)
2X-RAY DIFFRACTION2chain 'A' and (resseq 73:180)
3X-RAY DIFFRACTION3chain 'A' and (resseq 181:330)
4X-RAY DIFFRACTION4chain 'B' and (resseq 8:112)
5X-RAY DIFFRACTION5chain 'B' and (resseq 113:257)
6X-RAY DIFFRACTION6chain 'C' and (resseq 8:72)
7X-RAY DIFFRACTION7chain 'C' and (resseq 73:180)
8X-RAY DIFFRACTION8chain 'C' and (resseq 181:330)
9X-RAY DIFFRACTION9chain 'D' and (resseq 7:30)
10X-RAY DIFFRACTION10chain 'D' and (resseq 31:143)
11X-RAY DIFFRACTION11chain 'D' and (resseq 144:257)
12X-RAY DIFFRACTION12chain 'E' and (resseq 8:32)
13X-RAY DIFFRACTION13chain 'E' and (resseq 33:60)
14X-RAY DIFFRACTION14chain 'E' and (resseq 61:180)
15X-RAY DIFFRACTION15chain 'E' and (resseq 181:330)
16X-RAY DIFFRACTION16chain 'F' and (resseq 8:143)
17X-RAY DIFFRACTION17chain 'F' and (resseq 144:256)
18X-RAY DIFFRACTION18chain 'G' and (resseq 34:46)
19X-RAY DIFFRACTION19chain 'G' and (resseq 47:55)
20X-RAY DIFFRACTION20chain 'G' and (resseq 56:66)
21X-RAY DIFFRACTION21chain 'H' and (resseq 34:46)
22X-RAY DIFFRACTION22chain 'H' and (resseq 47:56)
23X-RAY DIFFRACTION23chain 'H' and (resseq 57:67)
24X-RAY DIFFRACTION24chain 'I' and (resseq 34:46)
25X-RAY DIFFRACTION25chain 'I' and (resseq 47:66)
26X-RAY DIFFRACTION26chain 'H' and (resseq 3:21)

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