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- PDB-7ta6: Trimer-to-Monomer Disruption of Tumor Necrosis Factor-alpha (TNF-... -

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Basic information

Entry
Database: PDB / ID: 7ta6
TitleTrimer-to-Monomer Disruption of Tumor Necrosis Factor-alpha (TNF-alpha) by unnatural alpha/beta-peptide-1
Components
  • Alpha/Beta-peptide-1
  • Tumor necrosis factor
KeywordsSIGNALING PROTEIN / tumor necrosis factor-alpha / signaling
Function / homology
Function and homology information


negative regulation of L-glutamate import across plasma membrane / negative regulation of branching involved in lung morphogenesis / negative regulation of bile acid secretion / response to Gram-negative bacterium / positive regulation of interleukin-33 production / positive regulation of neutrophil activation / positive regulation of blood microparticle formation / positive regulation of chronic inflammatory response to antigenic stimulus / positive regulation of fractalkine production / positive regulation of vitamin D biosynthetic process ...negative regulation of L-glutamate import across plasma membrane / negative regulation of branching involved in lung morphogenesis / negative regulation of bile acid secretion / response to Gram-negative bacterium / positive regulation of interleukin-33 production / positive regulation of neutrophil activation / positive regulation of blood microparticle formation / positive regulation of chronic inflammatory response to antigenic stimulus / positive regulation of fractalkine production / positive regulation of vitamin D biosynthetic process / response to macrophage colony-stimulating factor / positive regulation of leukocyte adhesion to arterial endothelial cell / positive regulation of translational initiation by iron / response to 3,3',5-triiodo-L-thyronine / regulation of membrane lipid metabolic process / regulation of endothelial cell apoptotic process / regulation of branching involved in salivary gland morphogenesis / chronic inflammatory response to antigenic stimulus / negative regulation of protein-containing complex disassembly / response to gold nanoparticle / positive regulation of humoral immune response mediated by circulating immunoglobulin / positive regulation of hair follicle development / : / death receptor agonist activity / negative regulation of myelination / negative regulation of vascular wound healing / negative regulation of bicellular tight junction assembly / negative regulation of amyloid-beta clearance / negative regulation of cytokine production involved in immune response / response to isolation stress / positive regulation of calcidiol 1-monooxygenase activity / inflammatory response to wounding / sequestering of triglyceride / positive regulation of action potential / positive regulation of I-kappaB phosphorylation / positive regulation of interleukin-18 production / positive regulation of protein transport / TNF signaling / epithelial cell proliferation involved in salivary gland morphogenesis / toll-like receptor 3 signaling pathway / embryonic digestive tract development / leukocyte migration involved in inflammatory response / necroptotic signaling pathway / vascular endothelial growth factor production / response to fructose / cellular response to toxic substance / positive regulation of neuroinflammatory response / positive regulation of calcineurin-NFAT signaling cascade / positive regulation of mononuclear cell migration / positive regulation of synoviocyte proliferation / leukocyte tethering or rolling / positive regulation of fever generation / negative regulation of myoblast differentiation / negative regulation of D-glucose import / regulation of establishment of endothelial barrier / endothelial cell apoptotic process / macrophage activation involved in immune response / positive regulation of protein localization to cell surface / negative regulation of oxidative phosphorylation / TNFR1-mediated ceramide production / positive regulation of cytokine production involved in inflammatory response / negative regulation of systemic arterial blood pressure / tumor necrosis factor receptor binding / positive regulation of osteoclast differentiation / regulation of immunoglobulin production / regulation of metabolic process / positive regulation of heterotypic cell-cell adhesion / positive regulation of chemokine (C-X-C motif) ligand 2 production / positive regulation of extrinsic apoptotic signaling pathway / positive regulation of protein-containing complex disassembly / positive regulation of programmed cell death / positive regulation of podosome assembly / positive regulation of hepatocyte proliferation / positive regulation of membrane protein ectodomain proteolysis / regulation of canonical NF-kappaB signal transduction / regulation of fat cell differentiation / positive regulation of leukocyte adhesion to vascular endothelial cell / regulation of reactive oxygen species metabolic process / TNFR1-induced proapoptotic signaling / response to L-glutamate / cortical actin cytoskeleton organization / negative regulation of heart rate / positive regulation of amyloid-beta formation / negative regulation of viral genome replication / positive regulation of DNA biosynthetic process / regulation of synapse organization / negative regulation of fat cell differentiation / : / negative regulation of endothelial cell proliferation / Interleukin-10 signaling / negative regulation of interleukin-6 production / negative regulation of blood vessel endothelial cell migration / skeletal muscle contraction / negative regulation of apoptotic signaling pathway / phagocytic cup / humoral immune response / negative regulation of lipid storage / negative regulation of mitotic cell cycle / negative regulation of extrinsic apoptotic signaling pathway in absence of ligand / extrinsic apoptotic signaling pathway via death domain receptors
Similarity search - Function
Tumour necrosis factor alpha / Tumour necrosis factor / Tumour necrosis factor, conserved site / Tumor necrosis factor (TNF) homology domain (THD) signature. / Tumour necrosis factor family. / TNF(Tumour Necrosis Factor) family / Tumour necrosis factor domain / Tumor necrosis factor (TNF) homology domain (THD) profile. / Tumour necrosis factor-like domain superfamily
Similarity search - Domain/homology
: / AMINO GROUP / Tumor necrosis factor
Similarity search - Component
Biological speciesHomo sapiens (human)
Synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.67 Å
AuthorsNiu, J. / Bingman, C.A. / Gellman, S.H.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01-GM056414 United States
CitationJournal: J.Am.Chem.Soc. / Year: 2022
Title: Trimer-to-Monomer Disruption Mechanism for a Potent, Protease-Resistant Antagonist of Tumor Necrosis Factor-alpha Signaling.
Authors: Niu, J. / Cederstrand, A.J. / Eddinger, G.A. / Yin, B. / Checco, J.W. / Bingman, C.A. / Outlaw, V.K. / Gellman, S.H.
History
DepositionDec 20, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 29, 2022Provider: repository / Type: Initial release
Revision 2.0Feb 15, 2023Group: Atomic model / Author supporting evidence ...Atomic model / Author supporting evidence / Data collection / Database references / Derived calculations / Polymer sequence / Refinement description / Source and taxonomy / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / entity / entity_poly / entity_poly_seq / pdbx_entity_instance_feature / pdbx_entity_nonpoly / pdbx_entity_src_syn / pdbx_nonpoly_scheme / pdbx_poly_seq_scheme / pdbx_refine_tls_group / pdbx_struct_assembly_gen / pdbx_validate_peptide_omega / pdbx_validate_rmsd_angle / struct_asym / struct_conf / struct_conn / struct_ref_seq
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.group_PDB / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.label_seq_id / _atom_site.type_symbol / _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _atom_site_anisotrop.id / _atom_site_anisotrop.pdbx_auth_asym_id / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_auth_comp_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_asym_id / _atom_site_anisotrop.pdbx_label_atom_id / _atom_site_anisotrop.pdbx_label_comp_id / _atom_site_anisotrop.pdbx_label_seq_id / _atom_site_anisotrop.type_symbol / _entity_poly.pdbx_seq_one_letter_code / _entity_poly.pdbx_seq_one_letter_code_can / _pdbx_entity_src_syn.pdbx_end_seq_num / _pdbx_refine_tls_group.beg_auth_seq_id / _pdbx_refine_tls_group.end_auth_seq_id / _pdbx_refine_tls_group.selection_details / _pdbx_struct_assembly_gen.asym_id_list / _struct_conf.end_auth_comp_id / _struct_conf.end_auth_seq_id / _struct_conf.end_label_comp_id / _struct_conf.end_label_seq_id / _struct_conf.pdbx_PDB_helix_length / _struct_conn.pdbx_dist_value / _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_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ref_seq.db_align_end / _struct_ref_seq.pdbx_auth_seq_align_end / _struct_ref_seq.seq_align_end
Revision 3.0Nov 15, 2023Group: Atomic model / Data collection / Category: atom_site / chem_comp_atom / chem_comp_bond
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_atom_id / _atom_site.label_atom_id
Revision 3.1Apr 3, 2024Group: Refinement description / Category: pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Tumor necrosis factor
B: Tumor necrosis factor
C: Tumor necrosis factor
D: Tumor necrosis factor
E: Tumor necrosis factor
F: Tumor necrosis factor
G: Tumor necrosis factor
H: Tumor necrosis factor
I: Alpha/Beta-peptide-1
J: Alpha/Beta-peptide-1
K: Alpha/Beta-peptide-1
L: Alpha/Beta-peptide-1
M: Alpha/Beta-peptide-1
N: Alpha/Beta-peptide-1
O: Alpha/Beta-peptide-1
P: Alpha/Beta-peptide-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)166,67633
Polymers166,01316
Non-polymers66417
Water81145
1
A: Tumor necrosis factor
N: Alpha/Beta-peptide-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)20,9546
Polymers20,7522
Non-polymers2024
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Tumor necrosis factor
I: Alpha/Beta-peptide-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)20,8304
Polymers20,7522
Non-polymers782
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Tumor necrosis factor
J: Alpha/Beta-peptide-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)20,8925
Polymers20,7522
Non-polymers1403
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: Tumor necrosis factor
K: Alpha/Beta-peptide-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)20,8304
Polymers20,7522
Non-polymers782
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
E: Tumor necrosis factor
M: Alpha/Beta-peptide-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)20,8304
Polymers20,7522
Non-polymers782
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
6
F: Tumor necrosis factor
L: Alpha/Beta-peptide-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)20,7683
Polymers20,7522
Non-polymers161
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
7
G: Tumor necrosis factor
O: Alpha/Beta-peptide-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)20,7683
Polymers20,7522
Non-polymers161
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
8
H: Tumor necrosis factor
P: Alpha/Beta-peptide-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)20,8074
Polymers20,7522
Non-polymers552
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)143.774, 143.552, 76.888
Angle α, β, γ (deg.)90.000, 97.850, 90.000
Int Tables number5
Space group name H-MC121

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Components

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Protein / Protein/peptide , 2 types, 16 molecules ABCDEFGHIJKLMNOP

#1: Protein
Tumor necrosis factor / Cachectin / TNF-alpha / Tumor necrosis factor ligand superfamily member 2 / TNF-a


Mass: 17457.736 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TNF, TNFA, TNFSF2 / Production host: Escherichia coli (E. coli) / References: UniProt: P01375
#2: Protein/peptide
Alpha/Beta-peptide-1


Mass: 3293.842 Da / Num. of mol.: 8 / Source method: obtained synthetically / Source: (synth.) Synthetic construct (others)

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Non-polymers , 4 types, 62 molecules

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


Mass: 62.068 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C2H6O2
#4: Chemical ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: K
#5: Chemical
ChemComp-NH2 / AMINO GROUP


Mass: 16.023 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: NH2
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 45 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY

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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: 2.38 Å3/Da / Density % sol: 48.32 %
Crystal growTemperature: 292 K / Method: vapor diffusion / pH: 8.5
Details: 0.8 M potassium sodium tartrate, 0.1 M Tris HCl pH 8.5, 4% ethylene glycol

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 1.03323 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Dec 12, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.03323 Å / Relative weight: 1
ReflectionResolution: 2.67→101.11 Å / Num. obs: 43735 / % possible obs: 100 % / Redundancy: 6.8 % / Biso Wilson estimate: 75.67 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.117 / Rpim(I) all: 0.048 / Rrim(I) all: 0.127 / Net I/σ(I): 9.5 / Num. measured all: 298842
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. measured allNum. unique obsCC1/2Rpim(I) allRrim(I) allNet I/σ(I) obs% possible all
2.67-2.8271.7894447963480.4280.7241.9311.1100
8.45-101.116.30.052894314110.9980.0220.05725.899.7

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Processing

Software
NameVersionClassification
XDSJan 31, 2020data reduction
Aimless0.7.4data scaling
PHENIX1.19.2refinement
PDB_EXTRACT3.27data extraction
PHASERphasing
autoPROC20190923data processing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1TNF_A

Resolution: 2.67→39.74 Å / SU ML: 0.42 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 31.6 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2727 1997 4.57 %
Rwork0.2449 41695 -
obs0.2463 43692 99.9 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 228.26 Å2 / Biso mean: 101.43 Å2 / Biso min: 54.12 Å2
Refinement stepCycle: final / Resolution: 2.67→39.74 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10204 0 217 45 10466
Biso mean--92.87 73.89 -
Num. residues----1320
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 14

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.67-2.740.38941000.34329993099100
2.74-2.810.35592000.336928973097100
2.81-2.90.3784990.337330223121100
2.9-2.990.33472000.329529073107100
2.99-3.10.32931000.320630243124100
3.1-3.220.35951850.300328943079100
3.22-3.370.28671150.282230263141100
3.37-3.540.37551000.287530093109100
3.54-3.770.30922000.256529313131100
3.77-4.060.32621000.243530403140100
4.06-4.460.26132000.203229143114100
4.46-5.110.2269990.196330333132100
5.11-6.430.26221990.231529393138100
6.43-39.740.18181000.22083060316099
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)
14.5494-1.538-1.08072.8330.48034.08870.18220.0527-0.2818-0.45810.19390.25720.8911-0.15820.00021.0438-0.1094-0.25160.4820.05110.6778-38.91612.3869.163
24.3669-2.2788-1.09783.52351.4133.13630.00690.0638-0.50320.0619-0.2751.03760.0836-0.544300.5813-0.0233-0.01880.91440.05490.8805-59.37931.495-24.849
34.26952.1275-0.37812.9726-1.012.2215-0.0275-0.0494-0.79320.0111-0.1395-0.27530.30440.213600.8246-0.0086-0.03510.615-0.05290.7699-29.37312.944-25.266
44.24491.7934-1.36064.5327-1.74034.10330.02620.4037-0.3865-0.06210.2815-0.52530.09960.779500.5220.0044-0.0131.0089-0.29420.6991-11.32633.7739.177
53.0217-1.58910.90843.8123-0.64313.8341-0.1169-0.10250.5681-0.22140.1098-0.8165-0.1010.281600.5895-0.02990.01320.9255-0.04380.8078-11.81242.56-24.82
63.51321.81551.86133.16871.71933.8571-0.01750.34790.2617-0.06530.30030.246-0.1857-0.619500.50180.02630.06191.04210.24690.6745-60.31339.9228.632
73.4043-1.47990.97543.3912-1.33713.41170.44370.11740.6028-0.4580.001-0.3986-0.85290.11820.00111.1347-0.06560.35680.4761-0.03960.81-32.73761.3559.134
83.62860.83590.53552.9534-0.18773.3505-0.05280.4540.91240.1004-0.06930.4192-0.45540.033400.87890.09010.03450.56190.06310.8504-41.72260.716-25.065
90.7174-0.4557-0.3670.686-0.17110.29720.11221.06940.2136-1.0882-0.2227-0.64150.1419-0.2891-00.83720.0361-0.03760.9330.03580.7181-46.8333.993-34.212
100.5253-0.34510.50850.5215-0.49510.48520.68630.65460.406-0.1108-0.24710.58520.0108-0.418500.8129-0.02020.0510.7553-0.07070.8246-32.58126.078-33.98
110.51520.2452-0.46960.6456-0.1170.42740.2006-0.62850.44230.7020.29130.9862-0.390.3468-00.8013-0.06810.05840.81850.02030.8581-24.36935.3318.266
120.24870.2959-0.07950.5722-0.28390.20560.1388-0.1285-0.11520.30870.6313-0.901-0.46620.0233-0.00020.7922-0.04410.02540.84350.02690.7112-47.38338.45818.175
130.58910.02790.25690.61110.42630.32650.28161.0822-1.0288-0.5913-0.10051.2483-0.4640.23020.00770.85540.037-0.03231.0320.19440.8176-24.61139.926-34.344
141.205-0.22270.95260.55220.17490.73160.2022-0.45540.81170.14330.0696-0.6827-0.12180.14580.00010.7074-0.00620.00020.63970.02180.7325-37.72325.8717.611
150.8576-0.2282-0.7760.4392-0.29650.69670.7831-0.406-0.80310.274-0.32030.5487-0.2748-0.3316-00.8252-0.04540.11560.80030.0330.8913-34.03248.03417.835
160.6313-0.0407-0.06670.27960.22490.0881-0.09040.98220.1319-0.4262-0.1014-0.5694-0.2908-0.12340.00010.90560.0145-0.15191.0237-0.0250.922-38.8647.823-34.13
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND RESID 7:157 )A7 - 157
2X-RAY DIFFRACTION2( CHAIN B AND RESID 7:157 )B7 - 157
3X-RAY DIFFRACTION3( CHAIN C AND RESID 7:157 )C7 - 157
4X-RAY DIFFRACTION4( CHAIN D AND RESID 6:157 )D6 - 157
5X-RAY DIFFRACTION5( CHAIN E AND RESID 7:157 )E7 - 157
6X-RAY DIFFRACTION6( CHAIN F AND RESID 5:157 )F5 - 157
7X-RAY DIFFRACTION7( CHAIN G AND RESID 6:157 )G6 - 157
8X-RAY DIFFRACTION8( CHAIN H AND RESID 7:157 )H7 - 157
9X-RAY DIFFRACTION9( CHAIN I AND ( RESID 1:28 OR RESID 29:29 ) )I1 - 28
10X-RAY DIFFRACTION9( CHAIN I AND ( RESID 1:28 OR RESID 29:29 ) )I29
11X-RAY DIFFRACTION10( CHAIN J AND ( RESID 1:28 OR RESID 29:29 ) )J1 - 28
12X-RAY DIFFRACTION10( CHAIN J AND ( RESID 1:28 OR RESID 29:29 ) )J29
13X-RAY DIFFRACTION11( CHAIN K AND ( RESID 1:28 OR RESID 29:29 ) )K1 - 28
14X-RAY DIFFRACTION11( CHAIN K AND ( RESID 1:28 OR RESID 29:29 ) )K29
15X-RAY DIFFRACTION12( CHAIN L AND ( RESID 1:28 OR RESID 29:29 ) )L1 - 28
16X-RAY DIFFRACTION12( CHAIN L AND ( RESID 1:28 OR RESID 29:29 ) )L29
17X-RAY DIFFRACTION13( CHAIN M AND ( RESID 1:28 OR RESID 29:29 ) )M1 - 28
18X-RAY DIFFRACTION13( CHAIN M AND ( RESID 1:28 OR RESID 29:29 ) )M29
19X-RAY DIFFRACTION14( CHAIN N AND ( RESID 1:28 OR RESID 29:29 ) )N1 - 28
20X-RAY DIFFRACTION14( CHAIN N AND ( RESID 1:28 OR RESID 29:29 ) )N29
21X-RAY DIFFRACTION15( CHAIN O AND ( RESID 1:28 OR RESID 29:29 ) )O1 - 28
22X-RAY DIFFRACTION15( CHAIN O AND ( RESID 1:28 OR RESID 29:29 ) )O29
23X-RAY DIFFRACTION16( CHAIN P AND ( RESID 1:28 OR RESID 29:29 ) )P1 - 28
24X-RAY DIFFRACTION16( CHAIN P AND ( RESID 1:28 OR RESID 29:29 ) )P29

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