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- PDB-4n5j: Crystal structure of hemagglutinin from an H7N9 influenza virus -

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Basic information

Entry
Database: PDB / ID: 4n5j
TitleCrystal structure of hemagglutinin from an H7N9 influenza virus
Components
  • Hemagglutinin HA1
  • Hemagglutinin HA2
KeywordsVIRAL PROTEIN / viral envelope protein / hemagglutinin / viral fusion protein
Function / homology
Function and homology information


viral budding from plasma membrane / clathrin-dependent endocytosis of virus by host cell / host cell surface receptor binding / apical plasma membrane / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / host cell plasma membrane / virion membrane / metal ion binding
Similarity search - Function
Hemagglutinin; Chain A, domain 2 / Hemagglutinin Chain A, Domain 2 / Hemagglutinin Ectodomain; Chain B - #10 / Hemagglutinin Ectodomain; Chain B / Hemagglutinin (Ha1 Chain); Chain: A; domain 1 / Haemagglutinin, alpha/beta domain, HA1 chain / Haemagglutinin, influenzavirus A / Haemagglutinin, HA1 chain, alpha/beta domain superfamily / Haemagglutinin / Haemagglutinin, influenzavirus A/B ...Hemagglutinin; Chain A, domain 2 / Hemagglutinin Chain A, Domain 2 / Hemagglutinin Ectodomain; Chain B - #10 / Hemagglutinin Ectodomain; Chain B / Hemagglutinin (Ha1 Chain); Chain: A; domain 1 / Haemagglutinin, alpha/beta domain, HA1 chain / Haemagglutinin, influenzavirus A / Haemagglutinin, HA1 chain, alpha/beta domain superfamily / Haemagglutinin / Haemagglutinin, influenzavirus A/B / Viral capsid/haemagglutinin protein / Ribbon / Alpha-Beta Complex / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Biological speciesInfluenza A virus
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.702 Å
AuthorsXu, R. / Wilson, I.A.
CitationJournal: Science / Year: 2013
Title: Preferential recognition of avian-like receptors in human influenza A H7N9 viruses.
Authors: Xu, R. / de Vries, R.P. / Zhu, X. / Nycholat, C.M. / McBride, R. / Yu, W. / Paulson, J.C. / Wilson, I.A.
History
DepositionOct 10, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 18, 2013Provider: repository / Type: Initial release
Revision 1.1Nov 15, 2017Group: Refinement description / Category: software
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_struct_special_symmetry / pdbx_validate_close_contact / struct_asym / struct_conn / struct_ref_seq_dif / struct_site / struct_site_gen
Item: _atom_site.auth_asym_id / _atom_site.auth_seq_id ..._atom_site.auth_asym_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_entity_id / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_special_symmetry.label_asym_id / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_seq_id_2 / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _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_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Hemagglutinin HA1
B: Hemagglutinin HA2
C: Hemagglutinin HA1
D: Hemagglutinin HA2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)113,1787
Polymers112,1504
Non-polymers1,0293
Water1,06359
1
A: Hemagglutinin HA1
B: Hemagglutinin HA2
hetero molecules

A: Hemagglutinin HA1
B: Hemagglutinin HA2
hetero molecules

A: Hemagglutinin HA1
B: Hemagglutinin HA2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)171,31115
Polymers168,2246
Non-polymers3,0879
Water1086
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation8_544-z,x-1/2,-y-1/21
crystal symmetry operation11_545y+1/2,-z-1/2,-x1
Buried area31050 Å2
ΔGint-139 kcal/mol
Surface area57160 Å2
MethodPISA
2
C: Hemagglutinin HA1
D: Hemagglutinin HA2

C: Hemagglutinin HA1
D: Hemagglutinin HA2

C: Hemagglutinin HA1
D: Hemagglutinin HA2


Theoretical massNumber of molelcules
Total (without water)168,2246
Polymers168,2246
Non-polymers00
Water1086
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation5_555z,x,y1
crystal symmetry operation9_555y,z,x1
Buried area29300 Å2
ΔGint-129 kcal/mol
Surface area57700 Å2
MethodPISA
Unit cell
Length a, b, c (Å)154.513, 154.513, 154.513
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number198
Space group name H-MP213
Components on special symmetry positions
IDModelComponents
11B-306-

HOH

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Components

#1: Protein Hemagglutinin HA1


Mass: 34993.559 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Influenza A virus / Strain: A/Shanghai/2/2013 / Gene: HA, hemagglutinin / Plasmid: pFastbac-HT / Production host: Trichoplusia ni (cabbage looper) / Strain (production host): Hi5 / References: UniProt: R4NN21
#2: Protein Hemagglutinin HA2


Mass: 21081.207 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Influenza A virus / Strain: A/Shanghai/2/2013 / Gene: HA, hemagglutinin / Plasmid: pFastbac-HT / Production host: Trichoplusia ni (cabbage looper) / Strain (production host): Hi5 / References: UniProt: R4NN21
#3: Polysaccharide beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 586.542 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}}LINUCSPDB-CARE
#4: Sugar ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 2
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
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 59 / Source method: isolated from a natural source / Formula: H2O

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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: 2.74 Å3/Da / Density % sol: 55.13 %
Crystal growTemperature: 295.5 K / Method: vapor diffusion, sitting drop / pH: 8
Details: 17-20% PEG3350, 0.2 M ammonium acetate, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 295.5K

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Data collection

DiffractionMean temperature: 110 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL12-2 / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jun 2, 2013 / Details: K-B focusing mirrors
RadiationMonochromator: Liquid nitrogen-cooled double crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionRedundancy: 6.6 % / Number: 223195 / Rmerge(I) obs: 0.089 / Χ2: 1.07 / D res high: 2.7 Å / D res low: 50 Å / Num. obs: 33899 / % possible obs: 99.8
Diffraction reflection shell
Highest resolution (Å)Lowest resolution (Å)% possible obs (%)IDRmerge(I) obsChi squaredRedundancy
5.815099.310.0481.056.4
4.625.8110010.0621.0946.8
4.034.6299.810.0791.036.5
3.664.0310010.0991.066.8
3.43.6699.710.1261.0976.4
3.23.499.910.1691.0956.6
3.043.210010.2531.0796.8
2.913.0410010.3671.0356.9
2.82.9199.910.5191.066.2
2.72.810010.7571.0996.5
ReflectionResolution: 2.7→50 Å / Num. obs: 33899 / % possible obs: 99.8 % / Rmerge(I) obs: 0.089

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Phasing

PhasingMethod: molecular replacement
Phasing MRRfactor: 37.46 / Model details: Phaser MODE: MR_AUTO
Highest resolutionLowest resolution
Rotation2.7 Å46.59 Å
Translation2.7 Å46.59 Å

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
PHASER2.1.4phasing
PHENIX1.8.2_1309refinement
PDB_EXTRACT3.11data extraction
Blu-Icedata collection
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.702→46.587 Å / Occupancy max: 1 / Occupancy min: 1 / SU ML: 0.4 / σ(F): 1.35 / Phase error: 30.75 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2766 1718 5.07 %
Rwork0.2249 --
obs0.2276 33870 99.85 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 100.1201 Å2
Refinement stepCycle: LAST / Resolution: 2.702→46.587 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7538 0 67 59 7664
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0037762
X-RAY DIFFRACTIONf_angle_d0.66910472
X-RAY DIFFRACTIONf_dihedral_angle_d15.5652875
X-RAY DIFFRACTIONf_chiral_restr0.0261139
X-RAY DIFFRACTIONf_plane_restr0.0031382
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.702-2.78150.41441190.33422685X-RAY DIFFRACTION100
2.7815-2.87130.32381460.29922640X-RAY DIFFRACTION100
2.8713-2.97390.35291310.27542667X-RAY DIFFRACTION100
2.9739-3.0930.31941360.27212673X-RAY DIFFRACTION100
3.093-3.23370.33371370.27662653X-RAY DIFFRACTION100
3.2337-3.40410.29631370.25072656X-RAY DIFFRACTION100
3.4041-3.61730.28181710.24532654X-RAY DIFFRACTION100
3.6173-3.89650.2821390.22182666X-RAY DIFFRACTION100
3.8965-4.28840.26411530.19672680X-RAY DIFFRACTION100
4.2884-4.90830.24151500.18332657X-RAY DIFFRACTION100
4.9083-6.18170.26981510.20672745X-RAY DIFFRACTION100
6.1817-46.59430.24751480.21032776X-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)
12.64013.314-3.42135.2276-5.43996.98740.09570.24610.53820.27660.43850.8521-0.1702-0.7829-0.4890.43770.04350.11120.38240.02540.512-2.2083-57.23430.7829
24.02882.961-1.91861.7398-1.39511.20520.6196-0.53390.47840.4907-0.20230.4355-0.22660.3977-0.3440.5899-0.11040.07280.466-0.09860.592237.0875-28.3083-15.8125
33.31292.7336-0.23997.2238-4.68455.73240.27970.01220.82971.1656-0.26230.5875-1.06971.1377-0.12240.5672-0.2230.0520.6431-0.09870.480152.9692-14.6694-26.2554
44.25921.4745-0.77515.1474-3.86086.48130.2850.6252-0.0861-0.1294-0.3484-0.1690.04621.6550.08070.3563-0.0249-0.06181.1235-0.15610.433160.1439-23.3908-30.9072
52.5991-0.94220.83614.9897-4.06444.09710.29941.2062-0.5302-1.40190.3770.52330.90690.9263-0.70730.6294-0.017-0.22770.9882-0.15510.594250.6242-23.1415-38.849
64.757-2.01942.93945.4301-3.59156.6407-0.04690.75730.32580.14090.146-0.222-0.39710.6874-0.09840.3672-0.0866-0.09070.5524-0.0160.476142.8333-22.0873-32.0942
72.6188-0.02530.36171.6725-0.70242.75760.52320.0549-0.46410.2816-0.3544-0.15280.34971.0298-0.13810.51510.0155-0.17290.6525-0.17210.515451.7606-30.8572-23.9018
85.12676.9945-1.28062.0201-0.25031.08911.0458-1.33980.43831.6655-0.9088-0.5334-1.02170.068-0.1730.9186-0.22060.19570.6353-0.18360.725726.0715-32.6119-6.0812
98.09636.5106-1.15595.329-0.95552.19660.2944-0.23220.013-0.145-0.3547-0.4005-0.21090.3931-0.01040.4921-0.01180.08630.2395-0.03840.517220.8983-43.2743-11.2132
108.34325.233-5.50647.1832-6.76012.2072-0.17780.23210.87910.14050.58940.6918-0.2713-1.5254-0.19210.4694-0.01670.15980.5018-0.14140.59531.0407-52.9231-3.5093
112.0034-2.15480.39952.006-0.44970.97010.15620.7960.54910.0981-0.0241.2601-0.2455-2.1315-0.27550.7012-0.22920.10781.09420.10790.6709-12.6292-66.30058.6212
125.22662.5543-4.87342.4719-2.6474.54810.3293-0.63140.54830.52560.01540.1257-0.7802-0.2724-0.42540.49390.00010.1750.6111-0.08970.601-6.3973-62.520916.3846
132.03545.5642-7.23097.556-5.27019.5218-0.2439-0.8178-0.89840.1072-0.7718-0.9698-0.04390.99750.90430.4756-0.0337-0.02950.95040.05280.578812.5245-60.49685.7349
148.95071.0751-1.42659.8362-0.36298.8640.2341-1.1953-0.15640.3058-0.2316-0.1998-0.39610.3373-0.04220.4157-0.097-0.00690.548-0.00390.544929.1802-40.1796-18.5438
157.4166.8114-8.29696.8743-7.75438.9519-0.25380.1839-0.1527-0.05570.174-0.06020.1925-0.39680.0960.3673-0.02930.07370.3521-0.03010.354510.6885-59.1654-9.5055
162.4844-0.83512.77955.5287-1.56613.2499-0.0471-0.4021-0.34760.19160.18360.88110.2398-0.8102-0.09450.5102-0.18660.16330.6772-0.03310.4775-11.419-77.738216.8333
176.8797-0.73022.47978.94731.70785.5512-0.0726-0.9997-0.28040.8341-0.2354-0.05521.0845-0.64630.37610.6376-0.01550.15520.65260.07310.3184-7.8295-80.610523.4937
181.45562.19712.54215.51183.02764.85770.44720.2415-0.71280.45250.2434-0.06830.913-0.8916-0.26711.9207-1.1059-0.19861.9954-1.08652.0749-33.7242-40.4177-15.8333
190.61080.44180.88870.2860.59821.1984-0.29090.5765-0.43790.186-0.01810.7590.9354-0.36550.432.2157-0.9786-0.71170.9275-0.41282.4991-1.467-31.62333.9527
203.6825-0.99930.14032.28791.07774.7480.7799-0.44910.159-0.7077-0.3032-0.07890.4054-0.0724-0.48571.1187-0.0669-0.02550.7722-0.3591.000817.5368-8.482511.7328
210.9393-0.12752.28530.0239-0.34415.5430.21040.6041-1.04760.2283-1.00480.78181.1638-0.49580.71551.9439-0.5632-0.66631.7388-0.69492.0487-2.5265-32.72053.1657
222.1464-0.6265-0.79711.96840.03120.32120.08250.3628-0.3659-0.1332-0.57080.21560.1359-0.20030.12941.8045-0.9662-1.46331.066-1.25121.7714-10.9527-27.0447-4.903
234.47836.80111.83121.99632.8370.756-0.44780.22660.26620.03190.26130.366-0.7502-0.40720.33071.0621-1.5974-0.49831.926-1.17061.9723-30.8252-37.1268-11.9874
241.1697-2.00712.0515.0794-1.34366.4492-0.47470.69480.4076-0.33960.151-0.05430.0279-0.08920.2741.8039-1.1622-0.37782.4322-0.92822.3661-36.0944-49.705-21.1669
257.49698.26251.64339.35351.41391.0041-0.0042-0.26080.7580.32560.39-0.30020.96620.3532-0.56352.0986-0.6797-0.54291.6437-0.49512.2715-39.0737-60.3903-27.2155
263.70924.23852.51594.82742.92072.6624-0.12670.0120.53820.08150.709-0.57820.62970.4292-0.61791.3766-0.0193-0.33071.7567-1.05522.8457-19.8466-42.3849-23.3231
270.75991.05490.92251.5180.74615.0367-0.31140.5058-0.7029-0.8239-0.1828-0.25690.4265-0.21540.33081.6637-0.1832-0.21610.9-0.65891.7623-3.1772-23.7695-9.615
284.6962-1.8312.379.2396-2.30252.00140.2009-0.4753-0.54220.9618-0.54170.27510.5017-0.7080.47331.4112-0.237-0.43081.2182-0.44891.5876-3.9117-12.7077.6671
291.10291.37050.64892.16341.67671.3934-0.59570.4508-0.6674-0.72360.52140.62271.059-1.05320.13052.6097-2.0751-0.89911.6359-0.81681.7314-23.9308-28.2557-18.5927
300.446-0.47610.01915.39734.63444.4306-0.1330.55240.1651-0.39260.01490.3483-0.3254-0.56990.02922.8914-0.6671-1.21933.1421-0.91042.4334-44.082-52.0783-42.7234
314.7841-3.18120.58582.3007-0.78080.8781-0.12540.1073-0.0289-0.14670.3911-0.22480.23230.0493-0.20942.1973-0.8201-1.13292.7458-1.11872.6969-45.0733-56.7244-35.32
324.94960.7617-1.27325.4353-0.4265.3295-0.30720.11270.2899-0.68750.2846-0.4328-0.12670.13220.03331.6957-0.2744-0.52661.8958-1.12873.1127-34.0675-61.3431-37.1897
330.03070.4089-0.17635.4948-1.80243.5326-0.29390.04840.5614-0.98070.47110.2344-0.0659-0.3929-0.04362.0856-0.8034-0.28881.7892-1.43943.3445-44.3654-60.7244-47.352
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 11 through 41 )
2X-RAY DIFFRACTION2chain 'A' and (resid 42 through 122 )
3X-RAY DIFFRACTION3chain 'A' and (resid 123 through 153 )
4X-RAY DIFFRACTION4chain 'A' and (resid 154 through 175 )
5X-RAY DIFFRACTION5chain 'A' and (resid 176 through 220 )
6X-RAY DIFFRACTION6chain 'A' and (resid 221 through 237 )
7X-RAY DIFFRACTION7chain 'A' and (resid 238 through 269 )
8X-RAY DIFFRACTION8chain 'A' and (resid 270 through 288 )
9X-RAY DIFFRACTION9chain 'A' and (resid 289 through 308 )
10X-RAY DIFFRACTION10chain 'A' and (resid 309 through 327 )
11X-RAY DIFFRACTION11chain 'B' and (resid 4 through 11 )
12X-RAY DIFFRACTION12chain 'B' and (resid 12 through 37 )
13X-RAY DIFFRACTION13chain 'B' and (resid 38 through 56 )
14X-RAY DIFFRACTION14chain 'B' and (resid 57 through 74 )
15X-RAY DIFFRACTION15chain 'B' and (resid 75 through 126 )
16X-RAY DIFFRACTION16chain 'B' and (resid 127 through 145 )
17X-RAY DIFFRACTION17chain 'B' and (resid 146 through 172 )
18X-RAY DIFFRACTION18chain 'C' and (resid 12 through 41 )
19X-RAY DIFFRACTION19chain 'C' and (resid 42 through 65 )
20X-RAY DIFFRACTION20chain 'C' and (resid 66 through 269 )
21X-RAY DIFFRACTION21chain 'C' and (resid 270 through 288 )
22X-RAY DIFFRACTION22chain 'C' and (resid 289 through 308 )
23X-RAY DIFFRACTION23chain 'C' and (resid 309 through 327 )
24X-RAY DIFFRACTION24chain 'D' and (resid 9 through 22 )
25X-RAY DIFFRACTION25chain 'D' and (resid 23 through 37 )
26X-RAY DIFFRACTION26chain 'D' and (resid 38 through 56 )
27X-RAY DIFFRACTION27chain 'D' and (resid 57 through 66 )
28X-RAY DIFFRACTION28chain 'D' and (resid 67 through 74 )
29X-RAY DIFFRACTION29chain 'D' and (resid 75 through 126 )
30X-RAY DIFFRACTION30chain 'D' and (resid 127 through 132 )
31X-RAY DIFFRACTION31chain 'D' and (resid 133 through 145 )
32X-RAY DIFFRACTION32chain 'D' and (resid 146 through 158 )
33X-RAY DIFFRACTION33chain 'D' and (resid 159 through 169 )

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