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- PDB-6nip: Crystal structure of a human anti-ZIKV-DENV neutralizing antibody... -

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Basic information

Entry
Database: PDB / ID: 6nip
TitleCrystal structure of a human anti-ZIKV-DENV neutralizing antibody MZ1 in complex with ZIKV E glycoprotein
Components
  • Envelope protein E
  • MZ1 Heavy chain
  • MZ1 Light Chain
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / ZIKV-DENV / Antibody / human / Vaccination / VIRAL PROTEIN-IMMUNE SYSTEM complex
Function / homology
Function and homology information


symbiont-mediated suppression of host JAK-STAT cascade via inhibition of host TYK2 activity / flavivirin / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity / negative regulation of innate immune response / viral capsid / nucleoside-triphosphate phosphatase / double-stranded RNA binding / 4 iron, 4 sulfur cluster binding / mRNA (guanine-N7)-methyltransferase ...symbiont-mediated suppression of host JAK-STAT cascade via inhibition of host TYK2 activity / flavivirin / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity / negative regulation of innate immune response / viral capsid / nucleoside-triphosphate phosphatase / double-stranded RNA binding / 4 iron, 4 sulfur cluster binding / mRNA (guanine-N7)-methyltransferase / methyltransferase cap1 / clathrin-dependent endocytosis of virus by host cell / mRNA (nucleoside-2'-O-)-methyltransferase activity / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / RNA helicase activity / molecular adaptor activity / host cell endoplasmic reticulum membrane / host cell perinuclear region of cytoplasm / protein dimerization activity / RNA helicase / induction by virus of host autophagy / RNA-directed RNA polymerase / viral RNA genome replication / RNA-dependent RNA polymerase activity / serine-type endopeptidase activity / centrosome / fusion of virus membrane with host endosome membrane / viral envelope / lipid binding / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / host cell nucleus / virion attachment to host cell / GTP binding / virion membrane / structural molecule activity / ATP hydrolysis activity / proteolysis / extracellular region / ATP binding / membrane / metal ion binding
Similarity search - Function
: / Flavivirus envelope glycoprotein E, stem/anchor domain / RNA-directed RNA polymerase, thumb domain, Flavivirus / Flavivirus RNA-directed RNA polymerase, thumb domain / Flavivirus capsid protein C superfamily / : / Flavivirus non-structural protein NS2B / Flavivirus NS3 helicase, C-terminal helical domain / Genome polyprotein, Flavivirus / Flavivirus non-structural protein NS4A ...: / Flavivirus envelope glycoprotein E, stem/anchor domain / RNA-directed RNA polymerase, thumb domain, Flavivirus / Flavivirus RNA-directed RNA polymerase, thumb domain / Flavivirus capsid protein C superfamily / : / Flavivirus non-structural protein NS2B / Flavivirus NS3 helicase, C-terminal helical domain / Genome polyprotein, Flavivirus / Flavivirus non-structural protein NS4A / Flavivirus non-structural protein NS2B / Flavivirus capsid protein C / Flavivirus non-structural protein NS4B / mRNA cap 0/1 methyltransferase / Flavivirus capsid protein C / Flavivirus non-structural protein NS4B / Flavivirus non-structural protein NS4A / Flavivirus NS2B domain profile. / mRNA cap 0 and cap 1 methyltransferase (EC 2.1.1.56 and EC 2.1.1.57) domain profile. / Flavivirus non-structural protein NS2A / Flavivirus non-structural protein NS2A / Flavivirus NS3, petidase S7 / Peptidase S7, Flavivirus NS3 serine protease / Flavivirus NS3 protease (NS3pro) domain profile. / Envelope glycoprotein M, flavivirus / Flavivirus envelope glycoprotein M / RNA-directed RNA polymerase, flavivirus / Flavivirus RNA-directed RNA polymerase, fingers and palm domains / Flavivirus non-structural Protein NS1 / Flavivirus non-structural protein NS1 / Envelope glycoprotein M superfamily, flavivirus / Flavivirus polyprotein propeptide / Flavivirus polyprotein propeptide superfamily / Flavivirus polyprotein propeptide / Flaviviral glycoprotein E, central domain, subdomain 1 / Flaviviral glycoprotein E, central domain, subdomain 2 / Flavivirus envelope glycoprotein E, Stem/Anchor domain / Flavivirus glycoprotein E, immunoglobulin-like domain / Flavivirus envelope glycoprotein E, Stem/Anchor domain superfamily / Flavivirus glycoprotein, immunoglobulin-like domain / Flavivirus glycoprotein central and dimerisation domain / Flavivirus glycoprotein, central and dimerisation domains / Ribosomal RNA methyltransferase, FtsJ domain / FtsJ-like methyltransferase / Flavivirus/Alphavirus glycoprotein, immunoglobulin-like domain superfamily / Flavivirus glycoprotein, central and dimerisation domain superfamily / Flaviviral glycoprotein E, dimerisation domain / DEAD box, Flavivirus / Flavivirus DEAD domain / helicase superfamily c-terminal domain / Immunoglobulin E-set / Superfamilies 1 and 2 helicase C-terminal domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / RNA-directed RNA polymerase, catalytic domain / RdRp of positive ssRNA viruses catalytic domain profile. / S-adenosyl-L-methionine-dependent methyltransferase superfamily / Peptidase S1, PA clan / DNA/RNA polymerase superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
Zika virus
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4.16 Å
AuthorsSankhala, R.S. / Dussupt, V. / Donofrio, G. / Choe, M. / Modjarrad, K. / Michael, N.L. / Krebs, S.J. / Joyce, M.G.
Funding support United States, 1items
OrganizationGrant numberCountry
Other governmentW81XWH-07-2-0067 United States
CitationJournal: Nat Med / Year: 2020
Title: Potent Zika and dengue cross-neutralizing antibodies induced by Zika vaccination in a dengue-experienced donor.
Authors: Dussupt, V. / Sankhala, R.S. / Gromowski, G.D. / Donofrio, G. / De La Barrera, R.A. / Larocca, R.A. / Zaky, W. / Mendez-Rivera, L. / Choe, M. / Davidson, E. / McCracken, M.K. / Brien, J.D. / ...Authors: Dussupt, V. / Sankhala, R.S. / Gromowski, G.D. / Donofrio, G. / De La Barrera, R.A. / Larocca, R.A. / Zaky, W. / Mendez-Rivera, L. / Choe, M. / Davidson, E. / McCracken, M.K. / Brien, J.D. / Abbink, P. / Bai, H. / Bryan, A.L. / Bias, C.H. / Berry, I.M. / Botero, N. / Cook, T. / Doria-Rose, N.A. / Escuer, A.G.I. / Frimpong, J.A. / Geretz, A. / Hernandez, M. / Hollidge, B.S. / Jian, N. / Kabra, K. / Leggat, D.J. / Liu, J. / Pinto, A.K. / Rutvisuttinunt, W. / Setliff, I. / Tran, U. / Townsley, S. / Doranz, B.J. / Rolland, M. / McDermott, A.B. / Georgiev, I.S. / Thomas, R. / Robb, M.L. / Eckels, K.H. / Barranco, E. / Koren, M. / Smith, D.R. / Jarman, R.G. / George, S.L. / Stephenson, K.E. / Barouch, D.H. / Modjarrad, K. / Michael, N.L. / Joyce, M.G. / Krebs, S.J.
History
DepositionDec 31, 2018Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 25, 2019Provider: repository / Type: Initial release
Revision 1.1Jan 6, 2021Group: Database references / Category: citation / citation_author
Item: _citation.journal_abbrev / _citation.journal_id_CSD ..._citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Oct 11, 2023Group: 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 / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: MZ1 Heavy chain
B: MZ1 Light Chain
Z: Envelope protein E
E: Envelope protein E
H: MZ1 Heavy chain
L: MZ1 Light Chain


Theoretical massNumber of molelcules
Total (without water)190,6136
Polymers190,6136
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration, Assembly was tested by gel-filtration and native PAGE
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)417.330, 69.300, 212.580
Angle α, β, γ (deg.)90.000, 112.960, 90.000
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 1 through 139 or resid 141 through 195 or resid 197 through 214))
21(chain H and (resid 1 through 139 or resid 141 through 195 or resid 197 through 214))
12chain B
22chain L
13chain E
23chain Z

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111GLNGLNGLYGLY(chain A and (resid 1 through 139 or resid 141 through 195 or resid 197 through 214))AA1 - 1391 - 146
121LEULEUILEILE(chain A and (resid 1 through 139 or resid 141 through 195 or resid 197 through 214))AA141 - 195148 - 202
131ASNASNLYSLYS(chain A and (resid 1 through 139 or resid 141 through 195 or resid 197 through 214))AA197 - 214204 - 221
211GLNGLNGLYGLY(chain H and (resid 1 through 139 or resid 141 through 195 or resid 197 through 214))HE1 - 1391 - 146
221LEULEUILEILE(chain H and (resid 1 through 139 or resid 141 through 195 or resid 197 through 214))HE141 - 195148 - 202
231ASNASNLYSLYS(chain H and (resid 1 through 139 or resid 141 through 195 or resid 197 through 214))HE197 - 214204 - 221
112GLNGLNTHRTHRchain BBB1 - 2101 - 214
212GLNGLNTHRTHRchain LLF1 - 2101 - 214
113ILEILESERSERchain EED1 - 4031 - 403
213ILEILESERSERchain ZZC1 - 4031 - 403

NCS ensembles :
ID
1
2
3

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Components

#1: Antibody MZ1 Heavy chain


Mass: 23927.770 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: IGHV4-59*08 / Details (production host): pVRC8400 / Cell line (production host): Expi293 / Production host: Homo sapiens (human)
#2: Antibody MZ1 Light Chain


Mass: 22981.408 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: IGLV1-44*01 / Details (production host): pVRC8400 / Cell line (production host): Expi293 / Production host: Homo sapiens (human)
#3: Protein Envelope protein E /


Mass: 48397.520 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Zika virus (isolate ZIKV/Human/French Polynesia/10087PF/2013)
Strain: isolate ZIKV/Human/French Polynesia/10087PF/2013 / Details (production host): pMT-BiP / Cell line (production host): DS2 / Production host: Drosophila melanogaster (fruit fly) / References: UniProt: A0A024B7W1

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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: 7.86 Å3/Da / Density % sol: 84.36 % / Description: Plate
Crystal growTemperature: 291 K / Method: vapor diffusion / pH: 6.5
Details: 0.06 M MgCl2, 0.1M Imidazole MES monohydrate (pH 6.5), 20% Ethylene glycol and 10% PEG 8,000

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-E / Wavelength: 0.97 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Nov 18, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97 Å / Relative weight: 1
ReflectionResolution: 4.1→50 Å / Num. obs: 32942 / % possible obs: 75.6 % / Redundancy: 2.4 % / Rpim(I) all: 0.19 / Rsym value: 0.27 / Net I/σ(I): 3.7
Reflection shellResolution: 4.1→4.25 Å / Redundancy: 2.3 % / Mean I/σ(I) obs: 1.04 / Num. unique obs: 3339 / Rpim(I) all: 0.56 / Rsym value: 0.78 / % possible all: 77.5

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Processing

Software
NameVersionClassification
PHENIX1.11.1_2575refinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6MTX, 5IRE

6mtx

5ire


Resolution: 4.16→14.987 Å / SU ML: 0.5 / Cross valid method: THROUGHOUT / σ(F): 1.38 / Phase error: 21.72
RfactorNum. reflection% reflection
Rfree0.2366 1422 5 %
Rwork0.1876 --
obs0.1901 28430 70.07 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 289.3 Å2 / Biso min: 21.37 Å2
Refinement stepCycle: final / Resolution: 4.16→14.987 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12608 0 0 0 12608
Num. residues----1667
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00412944
X-RAY DIFFRACTIONf_angle_d0.6817624
X-RAY DIFFRACTIONf_chiral_restr0.0461994
X-RAY DIFFRACTIONf_plane_restr0.0052254
X-RAY DIFFRACTIONf_dihedral_angle_d10.667764
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A1960X-RAY DIFFRACTION7.87TORSIONAL
12H1960X-RAY DIFFRACTION7.87TORSIONAL
21B1948X-RAY DIFFRACTION7.87TORSIONAL
22L1948X-RAY DIFFRACTION7.87TORSIONAL
31E3739X-RAY DIFFRACTION7.87TORSIONAL
32Z3739X-RAY DIFFRACTION7.87TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
4.16-4.20850.18751480.1343279870
4.2085-4.35530.27107203853
4.3553-4.52510.2882132251066
4.5251-4.72490.2629139264269
4.7249-4.96540.2212148281073
4.9654-5.26380.23791460.1852277973
5.2638-5.64990.2248149282473
5.6499-6.1820.2385146277772
6.182-6.99570.2914154291875
6.9957-8.5340.20191530.1591291275
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)
14.2679-0.73131.42673.0059-1.00731.5972-0.1576-0.73280.15031.0003-0.1082-0.4512-0.237-0.03170.14190.6862-0.21410.2770.6075-0.07950.709872.549-13.86319.543
28.57131.9792-6.82660.4935-1.61555.44510.2263-0.6329-0.880.4913-1.10280.94840.5303-0.27880.23760.2388-0.23530.14040.9587-0.16281.118165.144-14.369.502
33.3727-0.3824-0.5691.0573-1.51722.8657-0.1632-0.5694-1.414-0.0217-0.24790.69631.0096-0.170.43850.5482-0.30780.22040.7343-0.07491.050767.828-20.36116.12
44.4065-4.5905-0.56914.7780.15851.4503-0.0799-0.4263-1.34740.7793-0.32850.601-0.2225-0.04160.18670.3814-0.3129-0.05480.6061-0.02560.82570.741-7.79418.207
51.9138-0.3442-0.061.07160.96421.5280.1739-0.14210.28630.16620.0710.22370.33990.3848-0.1340.4239-0.07690.08020.3861-0.06820.6671104.072-12.9175.98
61.1959-0.62730.19681.31410.09472.53210.1187-0.1115-0.1832-0.3705-0.10560.210.78410.34670.13650.47340.00580.06290.26130.12670.9414113.83-13.3171.806
73.48161.1485-1.06742.5045-0.64831.920.2706-0.1310.12330.27780.1817-0.0653-0.1762-0.5168-0.42590.5132-0.02420.10320.481-0.12580.51276.4398.15615.999
81.72620.7075-0.21880.29120.2951.40250.49970.17660.3035-0.0164-0.50170.15880.2834-0.27780.02330.4142-0.0383-0.00790.3013-0.0890.867490.455-0.9414.955
91.9138-0.692-0.24492.85130.60051.72840.2355-0.2243-0.088-0.46310.44150.5701-0.2957-0.23881.31010.14370.19990.55390.0717-0.27060.960594.883-4.6080.369
101.8514-0.33-0.62274.36993.60815.12120.824-0.1796-0.0434-0.38850.14760.3847-1.03040.23940.06010.41060.2240.25080.0705-0.48330.667795.3023.11-5.74
113.06141.59180.25453.19520.37742.554-1.03760.23220.4968-0.59010.5367-0.0896-0.1540.330.34970.7237-0.1932-0.12040.6760.01520.5851-30.682-14.965-33.284
122.11950.37650.6785-0.02420.2772-0.0064-0.4010.65990.2807-0.12840.65610.14760.22480.532-0.20551.2211-0.2985-0.47331.3556-0.03911.28562.7763.749-26.86
131.8334-0.17050.25620.72180.0334-0.0343-0.423-0.31190.57710.00330.199-0.1336-0.29290.19750.11560.7301-0.201-0.03331.1939-0.02950.7148-16.675-7.051-30.851
142.10290.86410.5261.4541-0.30553.47290.72360.1911-0.897-0.17620.2338-0.01440.45820.1538-0.50670.7646-0.2513-0.24770.81010.38010.6961-41.96-38.952-42.955
151.73940.69550.59722.8251-0.44231.3729-0.18950.3797-0.4298-0.01890.42750.35660.01850.2703-0.3380.4234-0.0651-0.0141.1392-0.41921.028733.053-5.1885.326
160.99960.9760.1020.913-0.0547-0.0217-0.91750.60390.3885-0.55830.9184-0.2636-0.07970.3471-0.02270.7912-0.1942-0.10181.6403-0.12391.3879-3.377-31.766-33.06
172.2373-0.97991.97620.7852-0.06293.441-0.99771.14760.5288-1.78160.04870.1941-0.44770.63050.68371.1057-0.3056-0.06261.1933-0.27641.278142.234-5.884-1.797
181.41340.46611.09860.1130.44760.88410.48460.2286-0.96490.27190.1349-0.00650.4618-0.4373-0.28690.9066-0.25530.04731.3099-0.04731.414416.402-19.377-11.333
191.01430.82040.26040.8739-0.54091.3316-0.0909-0.09470.5283-0.24690.2230.38970.1011-0.2227-0.15590.84740.12540.1381.2794-0.35641.289221.916-10.71-8.018
203.51210.30370.26932.63870.68662.51-0.6117-0.22220.47570.0619-0.14580.1375-0.246-0.23230.69130.5026-0.0085-0.03390.8892-0.20080.566347.53516.72411.858
211.4982-1.78090.90793.0946-0.47051.62370.2814-0.7257-0.19820.38690.30470.6499-0.735-0.7131.11991.127-0.23770.10090.84940.0098-0.0349-63.188-6.075-60.306
221.265-0.79980.74821.26510.53441.91160.3526-0.9530.55241.0235-0.1804-0.1527-0.62820.45150.31091.1801-0.37210.14081.0174-0.09420.048-55.047-2.046-58.224
232.3537-1.61662.33931.8236-1.16643.6447-0.219-0.7192-0.28060.91370.1635-0.0178-0.4759-0.9193-0.15420.5935-0.1298-0.0610.875-0.06730.3628-60.806-11.536-59.947
240.84311.1176-0.16791.3187-0.15912.6746-0.4846-0.11990.1909-0.444-0.56820.1348-0.481-0.1752-0.63990.7264-0.2073-0.20.51570.02260.0406-65.23-6.913-95.325
255.1926-1.1397-0.02587.06683.78933.42790.50640.33490.5237-0.2689-0.5410.7714-0.6169-0.0983-0.17210.6015-0.1818-0.17230.26730.01590.7457-72.284-2.855-95.157
263.9721-1.36712.66293.2991-0.90736.3904-0.09540.77110.0518-1.0124-0.1639-0.22660.60380.52140.29370.5025-0.17790.23330.5067-0.07490.4597-69.102-8.945-92.081
273.05370.1889-0.7743.5175-0.67921.72040.36360.3730.0162-1.1952-0.08870.0156-0.6465-0.33-0.42840.538-0.0456-0.05650.3453-0.070.3726-69.307-6.152-104.906
281.6649-0.4110.66062.89231.34532.77380.0410.10780.14560.09110.15830.14530.65130.4643-0.26420.6573-0.085-0.15220.56870.02870.4716-60.473-27.201-65.421
292.57980.19790.16631.7222-0.83813.39110.2183-0.08490.06740.12690.14470.57230.2828-0.1641-0.24090.5058-0.0363-0.11980.233-0.04610.3765-61.334-20.426-80.394
302.374-0.32820.68940.9731-0.31532.6668-0.22830.09640.3050.20320.4173-0.1830.79350.90330.37050.9967-0.1517-0.15320.07230.2390.4233-57.016-18.512-90.196
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND RESID 1:51 )A1 - 51
2X-RAY DIFFRACTION2( CHAIN A AND RESID 52:63 )A52 - 63
3X-RAY DIFFRACTION3( CHAIN A AND RESID 64:82 )A64 - 82
4X-RAY DIFFRACTION4( CHAIN A AND RESID 83:106 )A83 - 106
5X-RAY DIFFRACTION5( CHAIN A AND RESID 107:177 )A107 - 177
6X-RAY DIFFRACTION6( CHAIN A AND RESID 178:214 )A178 - 214
7X-RAY DIFFRACTION7( CHAIN B AND RESID 1:83 )B1 - 83
8X-RAY DIFFRACTION8( CHAIN B AND RESID 84:150 )B84 - 150
9X-RAY DIFFRACTION9( CHAIN B AND RESID 151:188 )B151 - 188
10X-RAY DIFFRACTION10( CHAIN B AND RESID 189:210 )B189 - 210
11X-RAY DIFFRACTION11( CHAIN Z AND RESID 1:60 )Z1 - 60
12X-RAY DIFFRACTION12( CHAIN Z AND RESID 61:163 )Z61 - 163
13X-RAY DIFFRACTION13( CHAIN Z AND RESID 164:316 )Z164 - 316
14X-RAY DIFFRACTION14( CHAIN Z AND RESID 317:403 )Z317 - 403
15X-RAY DIFFRACTION15( CHAIN E AND RESID 1:60 )E1 - 60
16X-RAY DIFFRACTION16( CHAIN E AND RESID 61:129 )E61 - 129
17X-RAY DIFFRACTION17( CHAIN E AND RESID 130:170 )E130 - 170
18X-RAY DIFFRACTION18( CHAIN E AND RESID 171:257 )E171 - 257
19X-RAY DIFFRACTION19( CHAIN E AND RESID 258:294 )E258 - 294
20X-RAY DIFFRACTION20( CHAIN E AND RESID 295:403 )E295 - 403
21X-RAY DIFFRACTION21( CHAIN H AND RESID 1:51 )H1 - 51
22X-RAY DIFFRACTION22( CHAIN H AND RESID 52:82 )H52 - 82
23X-RAY DIFFRACTION23( CHAIN H AND RESID 83:106 )H83 - 106
24X-RAY DIFFRACTION24( CHAIN H AND RESID 107:143 )H107 - 143
25X-RAY DIFFRACTION25( CHAIN H AND RESID 144:157 )H144 - 157
26X-RAY DIFFRACTION26( CHAIN H AND RESID 158:177 )H158 - 177
27X-RAY DIFFRACTION27( CHAIN H AND RESID 178:214 )H178 - 214
28X-RAY DIFFRACTION28( CHAIN L AND RESID 1:69 )L1 - 69
29X-RAY DIFFRACTION29( CHAIN L AND RESID 70:140 )L70 - 140
30X-RAY DIFFRACTION30( CHAIN L AND RESID 141:210 )L141 - 210

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