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- PDB-6lzg: Structure of novel coronavirus spike receptor-binding domain comp... -

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Basic information

Entry
Database: PDB / ID: 6lzg
TitleStructure of novel coronavirus spike receptor-binding domain complexed with its receptor ACE2
Components
  • Angiotensin-converting enzyme 2
  • Spike protein S1
KeywordsVIRAL PROTEIN / Novel Coronavirus / Spike protein / receptor
Function / homology
Function and homology information


positive regulation of amino acid transport / angiotensin-converting enzyme 2 / positive regulation of L-proline import across plasma membrane / Hydrolases; Acting on peptide bonds (peptidases); Metallocarboxypeptidases / angiotensin-mediated drinking behavior / positive regulation of gap junction assembly / regulation of systemic arterial blood pressure by renin-angiotensin / tryptophan transport / regulation of cardiac conduction / maternal process involved in female pregnancy ...positive regulation of amino acid transport / angiotensin-converting enzyme 2 / positive regulation of L-proline import across plasma membrane / Hydrolases; Acting on peptide bonds (peptidases); Metallocarboxypeptidases / angiotensin-mediated drinking behavior / positive regulation of gap junction assembly / regulation of systemic arterial blood pressure by renin-angiotensin / tryptophan transport / regulation of cardiac conduction / maternal process involved in female pregnancy / peptidyl-dipeptidase activity / regulation of vasoconstriction / transporter activator activity / Metabolism of Angiotensinogen to Angiotensins / carboxypeptidase activity / angiotensin maturation / Attachment and Entry / receptor-mediated endocytosis of virus by host cell / metallocarboxypeptidase activity / viral life cycle / positive regulation of cardiac muscle contraction / regulation of cytokine production / blood vessel diameter maintenance / negative regulation of smooth muscle cell proliferation / brush border membrane / negative regulation of ERK1 and ERK2 cascade / positive regulation of reactive oxygen species metabolic process / metallopeptidase activity / endocytic vesicle membrane / regulation of cell population proliferation / virus receptor activity / regulation of inflammatory response / endopeptidase activity / symbiont-mediated disruption of host tissue / Maturation of spike protein / Translation of Structural Proteins / Virion Assembly and Release / host cell surface / host extracellular space / viral translation / symbiont-mediated-mediated suppression of host tetherin activity / Potential therapeutics for SARS / Induction of Cell-Cell Fusion / structural constituent of virion / entry receptor-mediated virion attachment to host cell / membrane fusion / Attachment and Entry / host cell endoplasmic reticulum-Golgi intermediate compartment membrane / positive regulation of viral entry into host cell / receptor-mediated virion attachment to host cell / host cell surface receptor binding / cilium / symbiont-mediated suppression of host innate immune response / apical plasma membrane / receptor ligand activity / membrane raft / endocytosis involved in viral entry into host cell / endoplasmic reticulum lumen / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / symbiont entry into host cell / virion attachment to host cell / SARS-CoV-2 activates/modulates innate and adaptive immune responses / host cell plasma membrane / virion membrane / cell surface / negative regulation of transcription by RNA polymerase II / extracellular space / extracellular exosome / extracellular region / zinc ion binding / identical protein binding / membrane / plasma membrane
Similarity search - Function
Collectrin domain / Renal amino acid transporter / Collectrin-like domain profile. / Peptidase M2, peptidyl-dipeptidase A / Angiotensin-converting enzyme / Peptidase family M2 domain profile. / Neutral zinc metallopeptidases, zinc-binding region signature. / Spike (S) protein S1 subunit, receptor-binding domain, SARS-CoV-2 / Spike (S) protein S1 subunit, N-terminal domain, SARS-CoV-like / Coronavirus spike glycoprotein S1, C-terminal ...Collectrin domain / Renal amino acid transporter / Collectrin-like domain profile. / Peptidase M2, peptidyl-dipeptidase A / Angiotensin-converting enzyme / Peptidase family M2 domain profile. / Neutral zinc metallopeptidases, zinc-binding region signature. / Spike (S) protein S1 subunit, receptor-binding domain, SARS-CoV-2 / Spike (S) protein S1 subunit, N-terminal domain, SARS-CoV-like / Coronavirus spike glycoprotein S1, C-terminal / Coronavirus spike glycoprotein S1, C-terminal / Spike glycoprotein, N-terminal domain superfamily / Spike S1 subunit, receptor binding domain superfamily, betacoronavirus / Spike glycoprotein, betacoronavirus / Betacoronavirus spike (S) glycoprotein S1 subunit N-terminal (NTD) domain profile. / Betacoronavirus spike (S) glycoprotein S1 subunit C-terminal (CTD) domain profile. / Spike (S) protein S1 subunit, receptor-binding domain, betacoronavirus / Betacoronavirus spike glycoprotein S1, receptor binding / Spike glycoprotein S1, N-terminal domain, betacoronavirus-like / Betacoronavirus-like spike glycoprotein S1, N-terminal / Spike glycoprotein S2 superfamily, coronavirus / Spike glycoprotein S2, coronavirus, heptad repeat 1 / Spike glycoprotein S2, coronavirus, heptad repeat 2 / Coronavirus spike (S) glycoprotein S2 subunit heptad repeat 1 (HR1) region profile. / Coronavirus spike (S) glycoprotein S2 subunit heptad repeat 2 (HR2) region profile. / Spike glycoprotein S2, coronavirus / Coronavirus spike glycoprotein S2
Similarity search - Domain/homology
Spike glycoprotein / Angiotensin-converting enzyme 2
Similarity search - Component
Biological speciesHomo sapiens (human)
Severe acute respiratory syndrome coronavirus 2
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å
AuthorsWang, Q.H. / Song, H. / Qi, J.X.
CitationJournal: Cell / Year: 2020
Title: Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2.
Authors: Wang, Q. / Zhang, Y. / Wu, L. / Niu, S. / Song, C. / Zhang, Z. / Lu, G. / Qiao, C. / Hu, Y. / Yuen, K.Y. / Wang, Q. / Zhou, H. / Yan, J. / Qi, J.
History
DepositionFeb 19, 2020Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Mar 18, 2020Provider: repository / Type: Initial release
Revision 1.1Apr 8, 2020Group: Structure summary / Category: entity / Item: _entity.pdbx_description
Revision 2.0Apr 22, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Author supporting evidence / Database references / Polymer sequence / Refinement description / Source and taxonomy / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / citation / citation_author / entity / entity_poly / entity_poly_seq / entity_src_gen / pdbx_entity_instance_feature / pdbx_poly_seq_scheme / pdbx_refine_tls / pdbx_refine_tls_group / pdbx_unobs_or_zero_occ_residues / refine / refine_ls_restr / refine_ls_shell / software / struct_ref / struct_ref_seq
Item: _citation.journal_abbrev / _citation.journal_id_CSD ..._citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _entity.formula_weight / _entity_poly.pdbx_seq_one_letter_code / _entity_poly.pdbx_seq_one_letter_code_can / _entity_src_gen.pdbx_end_seq_num / _refine.B_iso_mean / _refine.ls_R_factor_R_free / _refine.ls_R_factor_R_work / _refine.ls_R_factor_obs / _refine.overall_SU_ML / _refine.pdbx_overall_phase_error / _refine_ls_restr.dev_ideal / _refine_ls_restr.number / _refine_ls_shell.R_factor_R_free / _refine_ls_shell.R_factor_R_work / _software.version / _struct_ref.pdbx_seq_one_letter_code / _struct_ref_seq.db_align_end / _struct_ref_seq.pdbx_auth_seq_align_end / _struct_ref_seq.seq_align_end
Description: Model orientation/position / Provider: author / Type: Coordinate replacement
Revision 2.1May 6, 2020Group: Database references / Source and taxonomy / Structure summary
Category: entity / entity_name_com ...entity / entity_name_com / entity_src_gen / struct_ref / struct_ref_seq
Item: _entity.pdbx_description / _entity.pdbx_ec ..._entity.pdbx_description / _entity.pdbx_ec / _entity_src_gen.gene_src_common_name / _entity_src_gen.pdbx_gene_src_gene / _struct_ref.db_code / _struct_ref.db_name / _struct_ref.pdbx_align_begin / _struct_ref.pdbx_db_accession / _struct_ref.pdbx_seq_one_letter_code / _struct_ref_seq.pdbx_db_accession
Revision 2.2May 27, 2020Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 2.3Jul 29, 2020Group: Data collection / Derived calculations / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / struct_conn / struct_site / struct_site_gen
Item: _chem_comp.name / _entity.pdbx_description ..._chem_comp.name / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _struct_conn.conn_type_id / _struct_conn.id / _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_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
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.4Mar 10, 2021Group: Structure summary / Category: chem_comp / entity / entity_name_com
Item: _chem_comp.pdbx_synonyms / _entity.pdbx_description / _entity_name_com.name
Revision 2.5Nov 29, 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
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 2.6Nov 6, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Angiotensin-converting enzyme 2
B: Spike protein S1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)93,5027
Polymers92,5522
Non-polymers9505
Water5,801322
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2770 Å2
ΔGint-23 kcal/mol
Surface area34880 Å2
Unit cell
Length a, b, c (Å)104.448, 104.448, 229.786
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number92
Space group name H-MP41212
Space group name HallP4abw2nw
Symmetry operation#1: x,y,z
#2: -y+1/2,x+1/2,z+1/4
#3: y+1/2,-x+1/2,z+3/4
#4: x+1/2,-y+1/2,-z+3/4
#5: -x+1/2,y+1/2,-z+1/4
#6: -x,-y,z+1/2
#7: y,x,-z
#8: -y,-x,-z+1/2

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Components

#1: Protein Angiotensin-converting enzyme 2 / ACE-related carboxypeptidase / Angiotensin-converting enzyme homolog / ACEH / Metalloprotease MPROT15


Mass: 69038.578 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ACE2, UNQ868/PRO1885
Production host: Insect cell expression vector pTIE1 (others)
References: UniProt: Q9BYF1, angiotensin-converting enzyme 2, Hydrolases; Acting on peptide bonds (peptidases); Metallocarboxypeptidases
#2: Protein Spike protein S1 / S glycoprotein / E2 / Peplomer protein / Spike glycoprotein


Mass: 23513.389 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Severe acute respiratory syndrome coronavirus 2
Gene: S, 2
Production host: Insect cell expression vector pTIE1 (others)
References: UniProt: P0DTC2
#3: 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.: 4
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6 / Feature type: SUBJECT OF INVESTIGATION
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
#4: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn / Feature type: SUBJECT OF INVESTIGATION
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 322 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY
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: 3.29 Å3/Da / Density % sol: 62.67 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 0.1M MES pH 6.5,10%w/v PEG 5000 MME,12% v/v 1-propanol

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL17U1 / Wavelength: 0.97919 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Feb 11, 2020
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97919 Å / Relative weight: 1
ReflectionResolution: 2.5→50 Å / Num. obs: 44981 / % possible obs: 100 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 21.6 % / Biso Wilson estimate: 35.62 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.129 / Net I/σ(I): 26.7
Reflection shellResolution: 2.5→2.59 Å / Redundancy: 22.3 % / Mean I/σ(I) obs: 3.3 / Num. unique obs: 4384 / CC1/2: 0.867 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX1.16_3549refinement
Blu-Icedata collection
HKL-2000data reduction
HKL-2000data processing
PHASERphasing
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2ajf

2ajf


Resolution: 2.5→34.5 Å / SU ML: 0.2505 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 20.6451
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2156 2304 5.14 %
Rwork0.1884 42557 -
obs0.1898 44861 99.88 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 44.01 Å2
Refinement stepCycle: LAST / Resolution: 2.5→34.5 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6405 0 57 322 6784
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00546649
X-RAY DIFFRACTIONf_angle_d0.82989040
X-RAY DIFFRACTIONf_chiral_restr0.2842957
X-RAY DIFFRACTIONf_plane_restr0.00511173
X-RAY DIFFRACTIONf_dihedral_angle_d23.90622428
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.5-2.550.23691030.25112617X-RAY DIFFRACTION98.69
2.55-2.610.2991420.23432598X-RAY DIFFRACTION100
2.61-2.680.241510.21812618X-RAY DIFFRACTION100
2.68-2.750.24861520.21642608X-RAY DIFFRACTION100
2.75-2.830.271310.21172612X-RAY DIFFRACTION100
2.83-2.920.2441500.21962619X-RAY DIFFRACTION100
2.92-3.030.24341450.20912623X-RAY DIFFRACTION100
3.03-3.150.26291230.20782669X-RAY DIFFRACTION100
3.15-3.290.23661400.20812642X-RAY DIFFRACTION100
3.29-3.460.23071350.19342642X-RAY DIFFRACTION100
3.46-3.680.21051540.18462647X-RAY DIFFRACTION100
3.68-3.960.23891260.16832690X-RAY DIFFRACTION100
3.96-4.360.17521490.1592691X-RAY DIFFRACTION100
4.36-4.990.17411670.14992678X-RAY DIFFRACTION100
4.99-6.280.21981630.17852725X-RAY DIFFRACTION100
6.28-34.50.17621730.18712878X-RAY DIFFRACTION99.41
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)
10.715851578218-0.154721369542-0.2801042550682.925480296150.2666386140451.370729247150.07229950140370.1439275179590.06997567979760.04442626267840.02981603343780.615512083351-0.237659428587-0.260228196461-0.002186580815880.3148805147140.06085670667570.0710310626380.4283819372160.01360456389870.435901516712-40.264207696225.9052284911-7.12159673486
20.0685148145115-0.027836569305-0.03793071457530.0532562033081-0.1625015363710.874236892887-0.00793154805256-0.09102101561750.109415687688-0.0813949686983-0.02803809637770.170806647181-0.361886627404-0.124728634574-0.02653486849840.2806773639730.01291595689710.0597699087160.360620706815-0.04125951779020.383049449778-37.636820387633.4168026782-20.6939129259
31.0556755778-0.844342794357-0.3553713465950.782052655034-0.103549085651.52973415717-0.0007445414784940.120083458698-0.18604329735-0.125896027886-0.04967869896590.5838773106610.134520181638-0.3125745124950.04666680441020.169900557741-0.0579965651246-0.0343075523140.277551250022-0.02979214909590.339629412766-39.177778093311.6544040819-40.1053030872
40.83424517063-0.283246505933-0.407441225721.132512228070.4966228537761.395640300610.00797890211550.0143942547490.0357993513693-0.1021946354860.0154525924774-0.0194054335224-0.03962720097210.112896454013-0.06311430806530.193984335413-0.03913635688350.01292367575840.251237779872-0.01157017585970.2167998996-18.737244074215.7175186278-35.9795825191
50.641731780615-0.0387068452731-0.2231660189862.330791230030.1164407578081.44140944788-0.0605121026563-0.12694812162-0.09093022932650.06370917353670.08938657770360.1189382216130.2671600920590.09924967938720.001229411395020.2106505721810.03700965769790.01346256967040.26541117691-0.006223008720690.202635448836-22.34563868895.4821477869-11.3024484569
60.680056622261-0.2127735076690.142535517510.844874525720.123237418481.55368290954-0.0181722644122-0.01697583493940.0615798502772-0.03205129067140.0521257348951-0.0880418974382-0.02351099269580.19400975714-0.04615892598420.1884659565-0.02433697051490.03058148655490.269160383344-0.00879626158210.244060953926-17.337554009316.8565602627-32.113966184
70.9376970962830.319657814436-0.1456737274210.5218617697440.5714206656221.41526375981-0.238020696114-0.620641224194-0.25805315970.4953128349760.161164862264-0.0846149458670.414559298040.154871625035-0.03985170262270.5052857902710.1261701910680.01797709947560.5743006637660.05286011577180.291761022289-36.550072225720.862741860630.7792845293
81.143177005990.0851754041685-0.9406589582670.0361316510435-0.3308685856063.89028894534-0.0600774589822-0.601197057017-0.5747086046970.603205415345-0.11132539691-0.3654563993020.6081376909960.3822878212310.03844643731160.5774337653750.1496690593-0.02754728194740.7552765526740.1243109349920.623052475769-23.663285512114.4235747626.9633193757
90.00160714773989-0.05920530963710.0345255178422.19014694179-1.251642277780.722905442778-0.406473626551-0.385481884352-0.3664989132410.1483289344430.0833055741723-0.4365453830180.4181384085050.694364359750.03639856031430.8474392222870.260051635621-0.2031998330221.39234733817-0.08966266819740.827711489467-20.243289947519.602883719637.6787450642
101.33729826853-0.308171288114-0.2925171512921.38073281921-0.1369269396441.1187360840.00119727589103-0.185698348893-0.06272680156690.09460423293640.0719065802416-0.201811365186-0.08589308685260.269462209534-0.06043194563190.3051974975420.008172711439410.04216382819110.440370881693-0.01998899768570.323712076851-31.380354995326.315109301716.8885215757
111.12493444192-0.223718857207-0.1927719032220.814442812762-0.2404583168161.797436550190.167695685606-0.04686991688570.4650173062320.1725632496430.01669540842290.181215587349-0.500173106423-0.0785996042557-0.1057680230070.4865226488150.02433409752480.09912354842130.4504344747450.004934318421930.4532281313-39.527903907140.799308568110.0840123775
120.590022126031-0.0731587571597-0.8012557669642.223849993971.139270219521.57620974938-0.0273780436430.1158257827320.0958884143619-0.008014285293140.1144937275230.120200583976-0.0263076393792-0.005094587989610.03478700357340.2924308927990.04155269897580.08605157659410.364925291320.02008326125340.277248219471-34.950392391617.30971156425.94610477428
132.02103163130.100660217532-0.1328153091961.81938369623-0.04822253714062.01773936063-0.128034343685-0.7878349703980.1018315742850.6730905119390.132086723752-0.320009649157-0.09737447658390.453996199514-0.06341102988320.4798878872640.0667060258956-0.1094986907020.736835026519-0.066434362830.402252476284-28.273820267124.266566296633.8684400335
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 19 through 82 )
2X-RAY DIFFRACTION2chain 'A' and (resid 83 through 129 )
3X-RAY DIFFRACTION3chain 'A' and (resid 130 through 193 )
4X-RAY DIFFRACTION4chain 'A' and (resid 194 through 293 )
5X-RAY DIFFRACTION5chain 'A' and (resid 294 through 431 )
6X-RAY DIFFRACTION6chain 'A' and (resid 432 through 614 )
7X-RAY DIFFRACTION7chain 'B' and (resid 333 through 364 )
8X-RAY DIFFRACTION8chain 'B' and (resid 365 through 380 )
9X-RAY DIFFRACTION9chain 'B' and (resid 381 through 393 )
10X-RAY DIFFRACTION10chain 'B' and (resid 394 through 459 )
11X-RAY DIFFRACTION11chain 'B' and (resid 460 through 494 )
12X-RAY DIFFRACTION12chain 'B' and (resid 495 through 506 )
13X-RAY DIFFRACTION13chain 'B' and (resid 507 through 527 )

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