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- PDB-4kvm: The NatA (Naa10p/Naa15p) amino-terminal acetyltransferase complex... -

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Basic information

Entry
Database: PDB / ID: 4kvm
TitleThe NatA (Naa10p/Naa15p) amino-terminal acetyltransferase complex bound to a bisubstrate analog
Components
  • (N-terminal acetyltransferase A complex ...) x 2
  • bisubstrate analog inhibitor
Keywordstransferase/transferase inhibitor / Acetyltransferase / TPR repeats / amino-terminal acetylation / transferase-transferase inhibitor complex
Function / homology
Function and homology information


protein-N-terminal-glutamate acetyltransferase activity / N-terminal amino-acid Nalpha-acetyltransferase NatA / NatA complex / protein N-terminal-serine acetyltransferase activity / protein-N-terminal-alanine acetyltransferase activity / acetyltransferase activator activity / protein maturation / nucleus / cytosol / cytoplasm
Similarity search - Function
Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat - #1010 / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat - #1040 / N-terminal acetyltransferase A, auxiliary subunit / N-terminal acetyltransferase A, auxiliary subunit / N-acetyltransferase Ard1-like / Acetyltransferase (GNAT) family / Gcn5-related N-acetyltransferase (GNAT) / Gcn5-related N-acetyltransferase (GNAT) domain profile. / GNAT domain / TPR repeat region circular profile. ...Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat - #1010 / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat - #1040 / N-terminal acetyltransferase A, auxiliary subunit / N-terminal acetyltransferase A, auxiliary subunit / N-acetyltransferase Ard1-like / Acetyltransferase (GNAT) family / Gcn5-related N-acetyltransferase (GNAT) / Gcn5-related N-acetyltransferase (GNAT) domain profile. / GNAT domain / TPR repeat region circular profile. / Acyl-CoA N-acyltransferase / Tetratricopeptide repeats / Aminopeptidase / Tetratricopeptide repeat / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat / Alpha Horseshoe / Tetratricopeptide-like helical domain superfamily / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Chem-1XE / N-terminal acetyltransferase A complex subunit nat1 / N-terminal acetyltransferase A complex catalytic subunit ard1
Similarity search - Component
Biological speciesSchizosaccharomyces pombe (fission yeast)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.597 Å
AuthorsLiszczak, G.P. / Marmorstein, R.Q.
CitationJournal: Nat.Struct.Mol.Biol. / Year: 2013
Title: Molecular basis for N-terminal acetylation by the heterodimeric NatA complex.
Authors: Liszczak, G. / Goldberg, J.M. / Foyn, H. / Petersson, E.J. / Arnesen, T. / Marmorstein, R.
History
DepositionMay 22, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 31, 2013Provider: repository / Type: Initial release
Revision 1.1Aug 28, 2013Group: Database references
Revision 1.2Oct 23, 2013Group: Database references
Revision 2.0Sep 22, 2021Group: Advisory / Database references ...Advisory / Database references / Derived calculations / Non-polymer description / Polymer sequence / Source and taxonomy / Structure summary
Category: chem_comp / database_2 ...chem_comp / database_2 / entity / entity_poly / entity_poly_seq / entity_src_gen / pdbx_entity_src_syn / pdbx_poly_seq_scheme / pdbx_unobs_or_zero_occ_residues / struct_conn / struct_ref / struct_ref_seq / struct_ref_seq_dif / struct_site
Item: _chem_comp.formula / _chem_comp.formula_weight ..._chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _entity.formula_weight / _entity.pdbx_ec / _entity_poly.nstd_monomer / _entity_poly.pdbx_seq_one_letter_code / _entity_poly.pdbx_seq_one_letter_code_can / _entity_src_gen.pdbx_beg_seq_num / _entity_src_gen.pdbx_end_seq_num / _entity_src_gen.pdbx_gene_src_scientific_name / _entity_src_gen.pdbx_seq_type / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_label_asym_id / _struct_ref.pdbx_align_begin / _struct_ref_seq.db_align_end / _struct_ref_seq.pdbx_auth_seq_align_end / _struct_ref_seq.seq_align_end / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 2.1Sep 20, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model
Revision 2.2Oct 30, 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: N-terminal acetyltransferase A complex subunit nat1
B: N-terminal acetyltransferase A complex subunit nat1
C: N-terminal acetyltransferase A complex subunit nat1
D: N-terminal acetyltransferase A complex subunit nat1
E: N-terminal acetyltransferase A complex catalytic subunit ard1
F: N-terminal acetyltransferase A complex catalytic subunit ard1
G: N-terminal acetyltransferase A complex catalytic subunit ard1
H: N-terminal acetyltransferase A complex catalytic subunit ard1
I: bisubstrate analog inhibitor
J: bisubstrate analog inhibitor
K: bisubstrate analog inhibitor
L: bisubstrate analog inhibitor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)416,05982
Polymers410,31212
Non-polymers5,74770
Water5,855325
1
A: N-terminal acetyltransferase A complex subunit nat1
E: N-terminal acetyltransferase A complex catalytic subunit ard1
I: bisubstrate analog inhibitor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)104,09822
Polymers102,5783
Non-polymers1,52019
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: N-terminal acetyltransferase A complex subunit nat1
F: N-terminal acetyltransferase A complex catalytic subunit ard1
J: bisubstrate analog inhibitor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)104,00221
Polymers102,5783
Non-polymers1,42418
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: N-terminal acetyltransferase A complex subunit nat1
G: N-terminal acetyltransferase A complex catalytic subunit ard1
K: bisubstrate analog inhibitor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)103,89618
Polymers102,5783
Non-polymers1,31815
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: N-terminal acetyltransferase A complex subunit nat1
H: N-terminal acetyltransferase A complex catalytic subunit ard1
L: bisubstrate analog inhibitor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)104,06321
Polymers102,5783
Non-polymers1,48518
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)81.439, 119.381, 134.063
Angle α, β, γ (deg.)80.20, 76.60, 70.42
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
31
41
12
22
32
42

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111chain 'A' and (resseq 100:632 or resseq 642:731 )
211chain 'B' and (resseq 100:632 or resseq 642:731 )
311chain 'C' and (resseq 100:632 or resseq 642:731 )
411chain 'D' and (resseq 100:632 or resseq 642:731 )
112chain 'E' and (resseq 1:153 )
212chain 'F' and (resseq 1:153 )
312chain 'G' and (resseq 1:153 )
412chain 'H' and (resseq 1:153 )

NCS ensembles :
ID
1
2

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Components

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N-terminal acetyltransferase A complex ... , 2 types, 8 molecules ABCDEFGH

#1: Protein
N-terminal acetyltransferase A complex subunit nat1 / NatA complex subunit nat1


Mass: 84154.812 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (yeast)
Strain: 972 / ATCC 24843 / Gene: nat1, SPCC338.07c / Production host: Escherichia coli (E. coli) / References: UniProt: O74985
#2: Protein
N-terminal acetyltransferase A complex catalytic subunit ard1 / NatA complex subunit ARD1


Mass: 18030.750 Da / Num. of mol.: 4 / Fragment: unp residues 1-156
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (yeast)
Strain: 972 / ATCC 24843 / Gene: ard1, SPAC15E1.08 / Production host: Escherichia coli (E. coli)
References: UniProt: Q9UTI3, N-terminal amino-acid Nalpha-acetyltransferase NatA

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Protein/peptide , 1 types, 4 molecules IJKL

#3: Protein/peptide
bisubstrate analog inhibitor


Mass: 392.362 Da / Num. of mol.: 4 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)

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Non-polymers , 4 types, 395 molecules

#4: Chemical...
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 64 / Source method: obtained synthetically / Formula: Cl
#5: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: SO4
#6: Chemical
ChemComp-1XE / [5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)furan-2-yl]methyl (3R)-4-{[3-({(E)-2-[(2,2-dihydroxyethyl)sulfanyl]ethenyl}amino)-3-oxopropyl]amino}-3-hydroxy-2,2-dimethyl-4-oxobutyl dihydrogen diphosphate


Mass: 821.538 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C23H34N7O18P3S
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 325 / 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: 2.89 Å3/Da / Density % sol: 57.45 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop
Details: Protein Buffer: 25 mM Hepes, pH 7.0, 200 mM NaCl, 1 mM TCEP Crystallization buffer: 100 mM Hepes, pH 7.0, 10% Peg 4000, 10% isopropanol, VAPOR DIFFUSION, HANGING DROP, temperature 298K
PH range: pH 7.0

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X25 / Wavelength: 0.9795 Å
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: Oct 3, 2012 / Details: Si-111 double crystal monochromator
RadiationMonochromator: Si (111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.6→50 Å / Num. all: 137695 / Num. obs: 137534

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Processing

Software
NameVersionClassification
HKL-2000data collection
PHASERphasing
PHENIX(phenix.refine: 1.7.3_928)refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: pdb entry 4KVX

4kvx


Resolution: 2.597→49.59 Å / SU ML: 0.44 / σ(F): 1.96 / Phase error: 31.65 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2596 6906 5.02 %
Rwork0.2216 --
obs0.2235 137534 96.85 %
Solvent computationShrinkage radii: 0.86 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 64.832 Å2 / ksol: 0.295 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-29.535 Å2-2.238 Å24.8581 Å2
2---25.4792 Å2-1.1654 Å2
3----4.0558 Å2
Refinement stepCycle: LAST / Resolution: 2.597→49.59 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms28076 0 278 325 28679
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00828960
X-RAY DIFFRACTIONf_angle_d1.16639102
X-RAY DIFFRACTIONf_dihedral_angle_d16.94910928
X-RAY DIFFRACTIONf_chiral_restr0.0864227
X-RAY DIFFRACTIONf_plane_restr0.0054991
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A4984X-RAY DIFFRACTIONPOSITIONAL
12B4984X-RAY DIFFRACTIONPOSITIONAL0.044
13C4941X-RAY DIFFRACTIONPOSITIONAL0.053
14D4963X-RAY DIFFRACTIONPOSITIONAL0.036
21E1231X-RAY DIFFRACTIONPOSITIONAL
22F1231X-RAY DIFFRACTIONPOSITIONAL0.043
23G1231X-RAY DIFFRACTIONPOSITIONAL0.045
24H1231X-RAY DIFFRACTIONPOSITIONAL0.037
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.5974-2.62690.36191900.34223311X-RAY DIFFRACTION74
2.6269-2.65780.41191900.3323914X-RAY DIFFRACTION87
2.6578-2.69020.34652100.34654029X-RAY DIFFRACTION90
2.6902-2.72430.36592330.32284195X-RAY DIFFRACTION93
2.7243-2.76010.34342290.30924219X-RAY DIFFRACTION96
2.7601-2.79790.3152230.30794455X-RAY DIFFRACTION97
2.7979-2.83790.35432340.30764400X-RAY DIFFRACTION98
2.8379-2.88030.34432110.30584378X-RAY DIFFRACTION98
2.8803-2.92530.35162650.29544449X-RAY DIFFRACTION98
2.9253-2.97320.28552350.27894397X-RAY DIFFRACTION98
2.9732-3.02450.33822350.27934402X-RAY DIFFRACTION98
3.0245-3.07950.30822060.28344444X-RAY DIFFRACTION98
3.0795-3.13870.33852420.27724420X-RAY DIFFRACTION98
3.1387-3.20270.31822480.27564375X-RAY DIFFRACTION98
3.2027-3.27240.30632170.27094464X-RAY DIFFRACTION98
3.2724-3.34850.30842300.26584415X-RAY DIFFRACTION98
3.3485-3.43220.31592640.26984442X-RAY DIFFRACTION99
3.4322-3.5250.32822330.26044446X-RAY DIFFRACTION99
3.525-3.62870.29772190.25294443X-RAY DIFFRACTION99
3.6287-3.74570.29382430.24144432X-RAY DIFFRACTION99
3.7457-3.87960.27022340.24354476X-RAY DIFFRACTION99
3.8796-4.03480.26672290.22734409X-RAY DIFFRACTION99
4.0348-4.21840.2332430.2014439X-RAY DIFFRACTION99
4.2184-4.44060.19762320.18194458X-RAY DIFFRACTION99
4.4406-4.71870.22682250.17684474X-RAY DIFFRACTION99
4.7187-5.08270.21032340.17844472X-RAY DIFFRACTION99
5.0827-5.59350.21292480.19194462X-RAY DIFFRACTION99
5.5935-6.40150.28242310.22764497X-RAY DIFFRACTION100
6.4015-8.05960.22072410.17984472X-RAY DIFFRACTION100
8.0596-49.59920.20842320.1724439X-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)
14.1028-0.4968-1.06821.1851-0.32890.88550.3476-0.09150.34120.1192-0.1917-0.3651-0.2050.3277-0.13940.5812-0.18650.00010.5505-0.09790.5248-22.47329.3058-75.222
22.1085-1.5747-0.80827.1473-1.55491.63730.2495-0.2976-0.3985-0.09750.12461.07670.0121-0.1526-0.37820.6419-0.1011-0.01740.68080.08030.6861-67.4317-4.0499-54.9502
31.44030.676-0.20463.1777-1.45321.4147-0.1048-0.0084-0.2262-0.24920.20810.03140.17860.0046-0.10030.5917-0.127-0.01210.5624-0.04060.449-37.0185-14.694-63.7184
42.8327-0.6532-0.164.68690.60862.2923-0.3493-0.3997-0.37481.19410.3444-0.5057-0.18360.28340.03410.96990.0111-0.13680.63190.00550.5515-23.4672-20.5999-46.3397
53.1643-0.59890.1822.78560.45921.7029-0.73220.201-0.0291-0.00720.3406-0.6852-0.8032-0.00410.11410.3477-0.34220.1020.41080.0690.6335-11.327768.8885-79.0369
62.78061.20680.31740.62530.19310.87240.20480.538-0.6176-0.48880.6484-1.3179-0.04950.93580.62440.6633-0.08290.80051.4866-0.55351.945516.021329.6563-99.2112
70.90720.45490.66743.72910.37220.70980.0110.1789-0.2285-0.1615-0.0321-0.34620.02650.10030.04960.4539-0.15180.19050.619-0.02940.5322-14.51140.5659-90.5344
84.23530.7412-0.47174.4308-0.283.5075-0.28480.89420.1554-1.4690.11610.5967-0.6365-0.41280.15911.002-0.1315-0.06570.7963-0.05320.5568-28.719344.5593-107.9859
93.83180.1055-0.04062.86310.59821.7043-0.43350.04130.00240.11770.3364-0.6630.4574-0.0333-0.0060.5330.2969-0.17270.5264-0.0350.7467-41.8666-48.5124-140.9496
102.405-0.5976-0.50050.17310.06110.88310.4735-0.27380.80430.69060.2736-1.67330.01820.7066-0.5050.8557-0.0965-0.43071.2267-0.48122.0553-15.6934-8.5084-121.3334
111.6201-0.8832-1.17933.76621.5931.54760.3660.20630.3726-0.1546-0.1931-0.5602-0.04090.1099-0.1570.47610.2103-0.10270.58040.04060.5667-45.7456-20.4603-130.1901
123.7671-1.32190.53014.4866-0.17222.6275-0.2337-0.35290.10331.1460.05840.51450.9181-0.13830.09720.95490.16240.10570.5710.00260.6206-60.0245-24.3624-112.7679
133.93470.31610.71512.1158-0.88521.00840.31860.0616-0.2422-0.8129-0.3546-0.64610.40630.37610.02280.95480.35180.34250.62510.07410.6913-23.090424.3349-14.9421
141.97310.34641.30216.6339-1.11061.32640.32030.1017-0.02180.32620.04220.53060.3299-0.2225-0.34640.95930.0594-0.03420.75980.0530.5538-68.502937.5562-35.2609
151.6761-0.7974-0.04992.3017-1.55991.589-0.1931-0.0025-0.0161-0.1436-0.00750.05820.12060.14910.20920.82860.17740.01070.5704-0.0580.5043-37.86648.0189-26.3412
163.17851.01850.02494.2180.17892.3579-0.55350.54420.075-1.26610.359-0.34490.60590.29330.14081.18790.07870.17370.68080.04070.5963-24.506854.2464-43.9804
174.4868-0.1783-0.38446.3592-0.97931.44750.3314-0.03030.09690.1186-0.1910.30980.16830.0047-0.16910.4287-0.1422-0.01040.4889-0.10310.3358-45.7445-1.4947-74.8082
181.77641.75730.36192.26420.44411.25780.14230.3252-0.1598-0.8999-0.05781.22240.5113-0.3849-0.12740.8492-0.1299-0.11930.7285-0.12580.7913-52.2893-6.3442-87.3115
194.8163-0.25510.75033.6458-0.41380.743-0.1077-0.1381-1.0189-0.16910.0449-1.63990.12660.2626-0.01860.4667-0.12940.08540.71740.06611.29880.601745.4662-79.0614
202.53193.13930.0255.41140.09342.07240.2247-0.4868-1.27781.292-0.2676-1.56940.60130.3644-0.03080.892-0.0815-0.36520.95710.4181.76392.307437.1027-66.6203
215.2113-0.5457-1.00734.3169-0.44711.3430.13550.18311.39130.06350.0767-1.6854-0.34170.1145-0.16820.5220.189-0.00720.6752-0.01321.3415-30.5757-25.0876-141.6012
222.5235-2.6121.45166.3016-0.12623.17460.03280.84941.3043-1.038-0.1493-0.7861-0.90250.135-0.0530.96720.23630.45820.95980.45031.7871-29.041-16.9295-154.2056
234.99630.3922-0.86286.5336-0.87952.06470.1628-0.05110.0193-0.7257-0.15260.54280.0244-0.0317-0.02470.57060.1959-0.04680.5145-0.07890.3979-46.435134.8761-15.2502
242.3256-1.9498-0.57872.1882-0.09131.74250.2146-0.34840.29620.27460.00041.3439-0.5058-0.3664-0.26720.70580.17250.02480.7764-0.1050.9578-53.091439.8761-2.8024
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(chain A and resid 5:269)
2X-RAY DIFFRACTION2(chain A and resid 270:428)
3X-RAY DIFFRACTION3(chain A and resid 429:572)
4X-RAY DIFFRACTION4(chain A and resid 573:731)
5X-RAY DIFFRACTION5(chain B and resid 5:266)
6X-RAY DIFFRACTION6(chain B and resid 267:428)
7X-RAY DIFFRACTION7(chain B and resid 429:572)
8X-RAY DIFFRACTION8(chain B and resid 573:731)
9X-RAY DIFFRACTION9(chain C and resid 5:269)
10X-RAY DIFFRACTION10(chain C and resid 270:428)
11X-RAY DIFFRACTION11(chain C and resid 429:572)
12X-RAY DIFFRACTION12(chain C and resid 573:731)
13X-RAY DIFFRACTION13(chain D and resid 5:269)
14X-RAY DIFFRACTION14(chain D and resid 270:428)
15X-RAY DIFFRACTION15(chain D and resid 429:572)
16X-RAY DIFFRACTION16(chain D and resid 573:731)
17X-RAY DIFFRACTION17(chain E and resid 1:97)
18X-RAY DIFFRACTION18(chain E and resid 98:153)
19X-RAY DIFFRACTION19(chain F and resid 1:99)
20X-RAY DIFFRACTION20(chain F and resid 100:153)
21X-RAY DIFFRACTION21(chain G and resid 1:99)
22X-RAY DIFFRACTION22(chain G and resid 100:153)
23X-RAY DIFFRACTION23(chain H and resid 1:98)
24X-RAY DIFFRACTION24(chain H and resid 99:153)

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