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- PDB-4o6c: West Nile Virus Non-structural protein 1 (NS1) Form 2 crystal -

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Open data


ID or keywords:

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Basic information

Entry
Database: PDB / ID: 4o6c
TitleWest Nile Virus Non-structural protein 1 (NS1) Form 2 crystal
ComponentsNS1
KeywordsVIRAL PROTEIN / flavivirus / non-structural protein 1 / NS1
Function / homology
Function and homology information


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 / ribonucleoside triphosphate phosphatase activity / double-stranded RNA binding / viral capsid / nucleoside-triphosphate phosphatase / mRNA (guanine-N7)-methyltransferase / methyltransferase cap1 / mRNA (nucleoside-2'-O-)-methyltransferase 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 / ribonucleoside triphosphate phosphatase activity / double-stranded RNA binding / viral capsid / nucleoside-triphosphate phosphatase / mRNA (guanine-N7)-methyltransferase / methyltransferase cap1 / mRNA (nucleoside-2'-O-)-methyltransferase activity / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / RNA helicase activity / host cell perinuclear region of cytoplasm / host cell endoplasmic reticulum membrane / protein dimerization activity / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / RNA helicase / symbiont entry into host cell / induction by virus of host autophagy / RNA-directed RNA polymerase / viral RNA genome replication / serine-type endopeptidase activity / RNA-dependent RNA polymerase activity / virus-mediated perturbation of host defense response / fusion of virus membrane with host endosome membrane / host cell nucleus / virion attachment to host cell / structural molecule activity / virion membrane / ATP hydrolysis activity / proteolysis / extracellular region / ATP binding / membrane / metal ion binding
Similarity search - Function
: / Flavivirus capsid protein C superfamily / RNA-directed RNA polymerase, thumb domain, Flavivirus / Flavivirus RNA-directed RNA polymerase, thumb domain / Flavivirus non-structural protein NS2B / Flavivirus envelope glycoprotein E, stem/anchor domain / : / Flavivirus NS3 helicase, C-terminal helical domain / Genome polyprotein, Flavivirus / Flavivirus non-structural protein NS4A ...: / Flavivirus capsid protein C superfamily / RNA-directed RNA polymerase, thumb domain, Flavivirus / Flavivirus RNA-directed RNA polymerase, thumb domain / Flavivirus non-structural protein NS2B / Flavivirus envelope glycoprotein E, stem/anchor domain / : / 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. / 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, flavivirus / Flavivirus envelope glycoprotein M / 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
Genome polyprotein / Genome polyprotein
Similarity search - Component
Biological speciesWest Nile virus
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.7508 Å
AuthorsAkey, D.L. / Smith, J.L.
CitationJournal: Science / Year: 2014
Title: Flavivirus NS1 structures reveal surfaces for associations with membranes and the immune system.
Authors: Akey, D.L. / Brown, W.C. / Dutta, S. / Konwerski, J. / Jose, J. / Jurkiw, T.J. / DelProposto, J. / Ogata, C.M. / Skiniotis, G. / Kuhn, R.J. / Smith, J.L.
History
DepositionDec 20, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 19, 2014Provider: repository / Type: Initial release
Revision 1.1Mar 12, 2014Group: Database references
Revision 1.2Nov 22, 2017Group: Refinement description / Category: software
Item: _software.classification / _software.contact_author ..._software.classification / _software.contact_author / _software.contact_author_email / _software.date / _software.language / _software.location / _software.name / _software.type / _software.version
Revision 1.3Jul 29, 2020Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / struct_conn / struct_ref_seq_dif / struct_site / struct_site_gen
Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _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_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.4Sep 20, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: NS1
B: NS1
C: NS1
D: NS1
E: NS1
F: NS1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)257,29115
Polymers255,6766
Non-polymers1,6159
Water00
1
A: NS1
B: NS1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)85,7645
Polymers85,2252
Non-polymers5383
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5350 Å2
ΔGint-17 kcal/mol
Surface area30650 Å2
MethodPISA
2
C: NS1
D: NS1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)85,7645
Polymers85,2252
Non-polymers5383
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5350 Å2
ΔGint-21 kcal/mol
Surface area30470 Å2
MethodPISA
3
E: NS1
F: NS1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)85,7645
Polymers85,2252
Non-polymers5383
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5400 Å2
ΔGint-22 kcal/mol
Surface area30500 Å2
MethodPISA
Unit cell
Length a, b, c (Å)186.885, 186.885, 81.765
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number143
Space group name H-MP3

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Components

#1: Protein
NS1


Mass: 42612.648 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) West Nile virus / Strain: NY99 / Gene: NS1 / Plasmid: pH-Ac64-7 / Production host: Trichoplusia ni (cabbage looper) / Strain (production host): High Five / References: UniProt: U3N977, UniProt: Q9Q6P4*PLUS
#2: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0
#3: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: SO4

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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: 3.22 Å3/Da / Density % sol: 61.85 %
Crystal growTemperature: 278 K / Method: vapor diffusion, sitting drop / pH: 5.5
Details: 25% PEG 3000, 5% Glycerol, 20 mM Sodium Citrate pH 5.5, vapor diffusion, sitting drop, temperature 278K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 1.0332 Å
DetectorType: MARMOSAIC 300 / Detector: CCD / Date: Oct 12, 2012 / Details: K-B pair of biomorph mirrors
RadiationMonochromator: double crystal monochromator / Protocol: SINGLE WAVELENGTH / Scattering type: x-ray
Radiation wavelengthWavelength: 1.0332 Å / Relative weight: 1
Reflection twinOperator: -h,-k,l / Fraction: 0.52
ReflectionResolution: 2.75→50 Å / Num. all: 82996 / Num. obs: 82996 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5.9 % / Biso Wilson estimate: 67.8 Å2 / Rmerge(I) obs: 0.244 / Net I/σ(I): 7.4
Reflection shellResolution: 2.75→2.8 Å / Redundancy: 5.6 % / Rmerge(I) obs: 2.41 / Mean I/σ(I) obs: 1 / % possible all: 100

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing
PHENIX1.8.2_1309refinement
PDB_EXTRACT3.14data extraction
Blu-Icedata collection
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 4O6D

4o6d


Resolution: 2.7508→48.981 Å / Occupancy max: 1 / Occupancy min: 1 / σ(F): 1.98 / Phase error: 25.9 / Stereochemistry target values: TWIN_LSQ_F
RfactorNum. reflection% reflection
Rfree0.2321 2004 2.41 %
Rwork0.2153 --
obs0.2167 82983 99.96 %
all-82996 -
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 82.9051 Å2
Refinement stepCycle: LAST / Resolution: 2.7508→48.981 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms16014 0 99 0 16113
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00416494
X-RAY DIFFRACTIONf_angle_d0.82422344
X-RAY DIFFRACTIONf_dihedral_angle_d14.9796096
X-RAY DIFFRACTIONf_chiral_restr0.0312466
X-RAY DIFFRACTIONf_plane_restr0.0042892
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.7508-2.81960.30851500.36445793X-RAY DIFFRACTION97
2.8196-2.89580.30431340.32545744X-RAY DIFFRACTION98
2.8958-2.9810.30151440.30555760X-RAY DIFFRACTION98
2.981-3.07710.35421360.29395801X-RAY DIFFRACTION98
3.0771-3.1870.30381420.27535813X-RAY DIFFRACTION98
3.187-3.31450.22981480.25725746X-RAY DIFFRACTION97
3.3145-3.46520.28511400.23965789X-RAY DIFFRACTION98
3.4652-3.64770.19021420.22355786X-RAY DIFFRACTION98
3.6477-3.8760.23131420.21045781X-RAY DIFFRACTION98
3.876-4.17470.19891440.19565773X-RAY DIFFRACTION98
4.1747-4.59390.17451480.17045767X-RAY DIFFRACTION97
4.5939-5.25660.15011500.1535772X-RAY DIFFRACTION97
5.2566-6.61470.22181290.18575792X-RAY DIFFRACTION98
6.6147-33.9930.25981550.19245782X-RAY DIFFRACTION97
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)
10.4086-0.2307-0.27520.13770.10450.43540.0530.0685-0.0283-0.0512-0.03420.0527-0.0049-0.07920.11860.50220.31870.03370.2605-0.0460.7784-4.0096-89.5054-2.8452
23.13380.7120.35660.16210.08110.0401-0.0012-0.3788-0.31890.2107-0.1064-0.26060.18360.07210.07940.7053-0.10140.07721.00470.04680.6944-31.4923-88.9333-22.1156
30.53240.3190.25580.31030.18250.2546-0.0284-0.012-0.0414-0.00810.0347-0.11680.01420.0924-0.06470.1646-0.2220.05060.39450.04440.4652-26.0606-86.8557-27.5595
40.49120.85290.23941.49490.41240.11530.00220.0541-0.1204-0.09340.05860.06650.14010.0247-0.00060.2051-0.0897-0.01830.62680.10190.4865-28.7181-82.5642-27.532
50.40960.31340.2680.24570.1670.68910.0769-0.0509-0.13820.0674-0.01190.0370.1462-0.07480.00670.1325-0.09950.03850.2512-0.02570.6154-25.5733-83.0221-21.1891
6-0.00080.01160.01310.16920.01070.03330.0077-0.0084-0.04840.00760.0348-0.0996-0.04380.070.1205-0.2169-0.07930.0283-0.1668-0.0030.6224-6.1236-70.6765-11.617
70.081-0.02130.06960.02470.0130.12720.0070.1505-0.019-0.0529-0.0176-0.0569-0.05450.0791-0.01620.00010.0318-0.05250.24330.04650.68873.2491-62.507-26.6835
80.0831-0.0265-0.16260.00890.04650.32010.1192-0.1258-0.0859-0.0232-0.0673-0.0497-0.08120.41850.04080.66080.0898-0.02360.39030.07510.65260.6241-83.516611.2192
91.4563-0.55570.44940.234-0.12120.27590.0339-0.0816-0.10110.01280.0680.00740.04210.01470.00990.071-0.12080.1110.5648-0.06630.71237.2418-72.056928.2528
100.1457-0.05630.04710.12790.04030.06540.123-0.0687-0.00430.0212-0.0247-0.0747-0.0220.08730.1489-0.0852-0.06590.0273-0.20050.02620.6861-7.5775-73.162514.857
110.1907-0.0439-0.26610.02340.06260.39010.0687-0.0606-0.07130.06010.07580.1288-0.1059-0.35170.00610.2246-0.00090.01180.49660.01460.4973-28.5499-75.561526.3602
120.10560.18620.36690.32630.64761.3011-0.0684-0.0973-0.00440.00070.01450.02740.0383-0.12350.07271.0321-0.02320.0920.8061-0.10371.1508-0.0539-19.431-12.1486
133.16330.2646-0.13020.0231-0.01030.00480.030.39210.369-0.1552-0.0434-0.1356-0.18870.04060.0170.895-0.1046-0.01831.07650.07020.8044-26.5097-27.79826.9165
142.0253-0.7442-0.94250.29350.29590.62610.0879-0.02330.1712-0.02440.011-0.1775-0.11820.0989-0.07310.75360.12480.04910.9046-0.01230.6741-20.7129-28.330212.3406
151.0056-1.0297-0.29771.05710.30670.0934-0.0631-0.08910.075-0.03110.0026-0.0073-0.01520.10210.00350.6740.1045-0.03530.97660.01650.7255-22.1098-33.189712.2783
160.4766-0.2282-0.39140.21540.31130.71280.0667-0.14250.1739-0.09880.15010.094-0.2477-0.23340.01230.62140.03320.01130.4607-0.02370.4307-7.3594-35.5848-1.0002
170.1276-0.09110.21350.1054-0.20490.42810.0553-0.0536-0.02980.03280.0529-0.2728-0.00920.15580.00950.653-0.03910.08310.7276-0.0070.504512.7022-42.149710.5054
180.0412-0.11290.23060.3641-0.69751.3659-0.07710.07370.0005-0.0246-0.00630.03670.07050.15070.03891.21250.11520.15140.86190.0731.2073-3.6933-19.0297-18.7659
193.4249-0.8869-0.36570.2360.09910.0425-0.0007-0.36250.34520.15830.15590.0464-0.13420.0095-0.10690.8479-0.206-0.02171.06120.05010.791521.022-31.4945-37.8208
201.57870.7015-0.7110.3295-0.31670.3330.00240.13520.07050.0202-0.032-0.0272-0.0536-0.0304-0.00510.6562-0.14770.04470.9463-0.08780.670315.482-33.5569-43.2521
210.63570.2353-0.44090.1254-0.22970.75790.01870.1330.0597-0.04260.0806-0.1044-0.21650.0954-0.01650.7177-0.06720.06480.47860.01150.38870.8795-36.1457-29.9485
220.15740.08170.2460.06720.14930.40240.00140.00040.0719-0.11890.02690.10860.0408-0.19190.01750.68320.06610.03640.7050.0030.5478-20.0064-39.3976-41.3706
230.0653-0.1613-0.30430.41210.78061.48060.0563-0.0663-0.00890.0296-0.11650.02990.2005-0.03860.04481.0880.2620.15681.0530.00751.1386-79.9668-66.9128.7314
241.21411.8404-0.39242.8342-0.61670.1363-0.0780.33740.2976-0.25920.05980.2428-0.0552-0.139-0.03020.9857-0.11240.01371.24680.02840.9874-89.4042-92.923547.8596
252.14350.2964-0.2810.0494-0.050.0525-0.0224-0.09390.0495-0.0165-0.07150.09580.01060.0730.01760.8145-0.4173-0.02281.2680.1280.7483-84.0696-90.573153.2871
260.49330.177-0.44110.1145-0.05380.62580.0146-0.0008-0.07510.2006-0.03460.23840.3147-0.30860.02470.3819-0.15770.04760.98570.09990.4719-71.6108-82.436839.9833
270.20780.04030.2740.01540.05380.386-0.0252-0.0760.15570.01790.0364-0.0975-0.19230.18570.00890.5352-0.1129-0.01760.75050.0960.3729-54.2078-70.460351.5581
280.3976-0.13650.76070.0562-0.27181.4622-0.14780.00130.0141-0.06090.0756-0.0331-0.06640.15750.08660.90330.2320.0320.91780.08461.1047-82.311-69.167522.2244
292.33691.8006-0.26321.3951-0.20580.02970.1598-0.25810.16960.3001-0.03440.2821-0.155-0.1313-0.12080.8868-0.0715-0.04321.08540.02430.8114-57.17-57.44083.2433
300.1308-0.0311-0.1390.8299-0.12730.1807-0.04610.01430.0151-0.11050.00230.0491-0.0526-0.04590.01090.6211-0.1253-0.03610.65860.11080.6101-58.9802-63.0334-2.2083
310.13790.1443-0.07980.5714-0.42620.7277-0.0291-0.05010.00840.01920.0569-0.06480.0579-0.1367-0.01580.5631-0.0713-0.06520.67330.03430.4255-66.087-76.134411.0548
320.00790.02050.02510.18780.2660.38680.01630.0376-0.10890.00550.00180.07350.1846-0.03820.02790.8075-0.2002-0.04060.88480.01890.6113-76.5926-94.4404-0.4322
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 0 through 31 )
2X-RAY DIFFRACTION2chain 'A' and (resid 32 through 51 )
3X-RAY DIFFRACTION3chain 'A' and (resid 52 through 80 )
4X-RAY DIFFRACTION4chain 'A' and (resid 81 through 125 )
5X-RAY DIFFRACTION5chain 'A' and (resid 126 through 184 )
6X-RAY DIFFRACTION6chain 'A' and (resid 185 through 283 )
7X-RAY DIFFRACTION7chain 'A' and (resid 284 through 352 )
8X-RAY DIFFRACTION8chain 'B' and (resid 0 through 51 )
9X-RAY DIFFRACTION9chain 'B' and (resid 52 through 125 )
10X-RAY DIFFRACTION10chain 'B' and (resid 126 through 262 )
11X-RAY DIFFRACTION11chain 'B' and (resid 263 through 352 )
12X-RAY DIFFRACTION12chain 'C' and (resid 0 through 31 )
13X-RAY DIFFRACTION13chain 'C' and (resid 32 through 51 )
14X-RAY DIFFRACTION14chain 'C' and (resid 52 through 80 )
15X-RAY DIFFRACTION15chain 'C' and (resid 81 through 125 )
16X-RAY DIFFRACTION16chain 'C' and (resid 126 through 262 )
17X-RAY DIFFRACTION17chain 'C' and (resid 263 through 352 )
18X-RAY DIFFRACTION18chain 'D' and (resid 0 through 31 )
19X-RAY DIFFRACTION19chain 'D' and (resid 32 through 51 )
20X-RAY DIFFRACTION20chain 'D' and (resid 52 through 125 )
21X-RAY DIFFRACTION21chain 'D' and (resid 126 through 262 )
22X-RAY DIFFRACTION22chain 'D' and (resid 263 through 352 )
23X-RAY DIFFRACTION23chain 'E' and (resid 0 through 31 )
24X-RAY DIFFRACTION24chain 'E' and (resid 32 through 51 )
25X-RAY DIFFRACTION25chain 'E' and (resid 52 through 125 )
26X-RAY DIFFRACTION26chain 'E' and (resid 126 through 262 )
27X-RAY DIFFRACTION27chain 'E' and (resid 263 through 352 )
28X-RAY DIFFRACTION28chain 'F' and (resid 0 through 31 )
29X-RAY DIFFRACTION29chain 'F' and (resid 32 through 51 )
30X-RAY DIFFRACTION30chain 'F' and (resid 52 through 125 )
31X-RAY DIFFRACTION31chain 'F' and (resid 126 through 262 )
32X-RAY DIFFRACTION32chain 'F' and (resid 263 through 352 )

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