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- PDB-4v5i: Structure of the Phage P2 Baseplate in its Activated Conformation... -

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Basic information

Entry
Database: PDB / ID: 4v5i
TitleStructure of the Phage P2 Baseplate in its Activated Conformation with Ca
Components
  • ORF15
  • ORF16
  • PUTATIVE RECEPTOR BINDING PROTEINReceptor (biochemistry)
KeywordsVIRAL PROTEIN / SIPHOVIRIDAE / LACTOCOCCUS LACTIS
Function / homology
Function and homology information


virus tail, baseplate / entry receptor-mediated virion attachment to host cell / cell adhesion / symbiont entry into host cell / virion attachment to host cell
Similarity search - Function
: / : / Lactophage receptor-binding protein N-terminal shoulder domain / Lactococcus phage p2, Receptor binding protein, neck domain / Receptor-binding protein of phage tail base-plate Siphoviridae, head / Lactophage receptor-binding protein C-terminal head domain / Adenovirus pIV-like, attachment domain
Similarity search - Domain/homology
Receptor binding protein / Receptor binding protein
Similarity search - Component
Biological speciesLACTOCOCCUS PHAGE P2 (virus)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 5.464 Å
AuthorsSciara, G. / Bebeacua, C. / Bron, P. / Tremblay, D. / Ortiz-Lombardia, M. / Lichiere, J. / van Heel, M. / Campanacci, V. / Moineau, S. / Cambillau, C.
CitationJournal: Proc Natl Acad Sci U S A / Year: 2010
Title: Structure of lactococcal phage p2 baseplate and its mechanism of activation.
Authors: Giuliano Sciara / Cecilia Bebeacua / Patrick Bron / Denise Tremblay / Miguel Ortiz-Lombardia / Julie Lichière / Marin van Heel / Valérie Campanacci / Sylvain Moineau / Christian Cambillau /
Abstract: Siphoviridae is the most abundant viral family on earth which infects bacteria as well as archaea. All known siphophages infecting gram+ Lactococcus lactis possess a baseplate at the tip of their ...Siphoviridae is the most abundant viral family on earth which infects bacteria as well as archaea. All known siphophages infecting gram+ Lactococcus lactis possess a baseplate at the tip of their tail involved in host recognition and attachment. Here, we report analysis of the p2 phage baseplate structure by X-ray crystallography and electron microscopy and propose a mechanism for the baseplate activation during attachment to the host cell. This approximately 1 MDa, Escherichia coli-expressed baseplate is composed of three protein species, including six trimers of the receptor-binding protein (RBP). RBPs host-recognition domains point upwards, towards the capsid, in agreement with the electron-microscopy map of the free virion. In the presence of Ca(2+), a cation mandatory for infection, the RBPs rotated 200 degrees downwards, presenting their binding sites to the host, and a channel opens at the bottom of the baseplate for DNA passage. These conformational changes reveal a novel siphophage activation and host-recognition mechanism leading ultimately to DNA ejection.
History
DepositionFeb 5, 2010Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 9, 2014Provider: repository / Type: Initial release
SupersessionDec 10, 2014ID: 2X54, 2X5A
Revision 1.1Dec 10, 2014Group: Other
Revision 1.2Dec 20, 2017Group: Database references / Structure summary / Category: audit_author / citation_author / struct
Item: _audit_author.name / _citation_author.name / _struct.title
Revision 1.3Jun 20, 2018Group: Advisory / Data collection / Derived calculations
Category: pdbx_struct_conn_angle / pdbx_validate_close_contact ...pdbx_struct_conn_angle / pdbx_validate_close_contact / struct_conn / struct_conn_type
Item: _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id ..._pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value
Revision 1.4Jan 10, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_sheet
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_sheet.number_strands
Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A0: ORF16
AA: PUTATIVE RECEPTOR BINDING PROTEIN
AB: PUTATIVE RECEPTOR BINDING PROTEIN
AC: PUTATIVE RECEPTOR BINDING PROTEIN
AD: PUTATIVE RECEPTOR BINDING PROTEIN
AE: PUTATIVE RECEPTOR BINDING PROTEIN
AF: PUTATIVE RECEPTOR BINDING PROTEIN
AG: PUTATIVE RECEPTOR BINDING PROTEIN
AH: PUTATIVE RECEPTOR BINDING PROTEIN
AI: PUTATIVE RECEPTOR BINDING PROTEIN
AJ: PUTATIVE RECEPTOR BINDING PROTEIN
AK: PUTATIVE RECEPTOR BINDING PROTEIN
AL: PUTATIVE RECEPTOR BINDING PROTEIN
AM: PUTATIVE RECEPTOR BINDING PROTEIN
AN: PUTATIVE RECEPTOR BINDING PROTEIN
AO: PUTATIVE RECEPTOR BINDING PROTEIN
AP: PUTATIVE RECEPTOR BINDING PROTEIN
AQ: PUTATIVE RECEPTOR BINDING PROTEIN
AR: PUTATIVE RECEPTOR BINDING PROTEIN
AS: ORF15
AT: ORF15
AU: ORF15
AV: ORF15
AW: ORF15
AX: ORF15
AY: ORF16
AZ: ORF16
B0: ORF16
BA: PUTATIVE RECEPTOR BINDING PROTEIN
BB: PUTATIVE RECEPTOR BINDING PROTEIN
BC: PUTATIVE RECEPTOR BINDING PROTEIN
BD: PUTATIVE RECEPTOR BINDING PROTEIN
BE: PUTATIVE RECEPTOR BINDING PROTEIN
BF: PUTATIVE RECEPTOR BINDING PROTEIN
BG: PUTATIVE RECEPTOR BINDING PROTEIN
BH: PUTATIVE RECEPTOR BINDING PROTEIN
BI: PUTATIVE RECEPTOR BINDING PROTEIN
BJ: PUTATIVE RECEPTOR BINDING PROTEIN
BK: PUTATIVE RECEPTOR BINDING PROTEIN
BL: PUTATIVE RECEPTOR BINDING PROTEIN
BM: PUTATIVE RECEPTOR BINDING PROTEIN
BN: PUTATIVE RECEPTOR BINDING PROTEIN
BO: PUTATIVE RECEPTOR BINDING PROTEIN
BP: PUTATIVE RECEPTOR BINDING PROTEIN
BQ: PUTATIVE RECEPTOR BINDING PROTEIN
BR: PUTATIVE RECEPTOR BINDING PROTEIN
BS: ORF15
BT: ORF15
BU: ORF15
BV: ORF15
BW: ORF15
BX: ORF15
BY: ORF16
BZ: ORF16
hetero molecules


Theoretical massNumber of molelcules
Total (without water)1,697,20966
Polymers1,696,72854
Non-polymers48112
Water0
1
A0: ORF16
AA: PUTATIVE RECEPTOR BINDING PROTEIN
AB: PUTATIVE RECEPTOR BINDING PROTEIN
AC: PUTATIVE RECEPTOR BINDING PROTEIN
AD: PUTATIVE RECEPTOR BINDING PROTEIN
AE: PUTATIVE RECEPTOR BINDING PROTEIN
AF: PUTATIVE RECEPTOR BINDING PROTEIN
AG: PUTATIVE RECEPTOR BINDING PROTEIN
AH: PUTATIVE RECEPTOR BINDING PROTEIN
AI: PUTATIVE RECEPTOR BINDING PROTEIN
AJ: PUTATIVE RECEPTOR BINDING PROTEIN
AK: PUTATIVE RECEPTOR BINDING PROTEIN
AL: PUTATIVE RECEPTOR BINDING PROTEIN
AM: PUTATIVE RECEPTOR BINDING PROTEIN
AN: PUTATIVE RECEPTOR BINDING PROTEIN
AO: PUTATIVE RECEPTOR BINDING PROTEIN
AP: PUTATIVE RECEPTOR BINDING PROTEIN
AQ: PUTATIVE RECEPTOR BINDING PROTEIN
AR: PUTATIVE RECEPTOR BINDING PROTEIN
AS: ORF15
AT: ORF15
AU: ORF15
AV: ORF15
AW: ORF15
AX: ORF15
AY: ORF16
AZ: ORF16
hetero molecules


Theoretical massNumber of molelcules
Total (without water)848,60433
Polymers848,36427
Non-polymers2406
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B0: ORF16
BA: PUTATIVE RECEPTOR BINDING PROTEIN
BB: PUTATIVE RECEPTOR BINDING PROTEIN
BC: PUTATIVE RECEPTOR BINDING PROTEIN
BD: PUTATIVE RECEPTOR BINDING PROTEIN
BE: PUTATIVE RECEPTOR BINDING PROTEIN
BF: PUTATIVE RECEPTOR BINDING PROTEIN
BG: PUTATIVE RECEPTOR BINDING PROTEIN
BH: PUTATIVE RECEPTOR BINDING PROTEIN
BI: PUTATIVE RECEPTOR BINDING PROTEIN
BJ: PUTATIVE RECEPTOR BINDING PROTEIN
BK: PUTATIVE RECEPTOR BINDING PROTEIN
BL: PUTATIVE RECEPTOR BINDING PROTEIN
BM: PUTATIVE RECEPTOR BINDING PROTEIN
BN: PUTATIVE RECEPTOR BINDING PROTEIN
BO: PUTATIVE RECEPTOR BINDING PROTEIN
BP: PUTATIVE RECEPTOR BINDING PROTEIN
BQ: PUTATIVE RECEPTOR BINDING PROTEIN
BR: PUTATIVE RECEPTOR BINDING PROTEIN
BS: ORF15
BT: ORF15
BU: ORF15
BV: ORF15
BW: ORF15
BX: ORF15
BY: ORF16
BZ: ORF16
hetero molecules


Theoretical massNumber of molelcules
Total (without water)848,60433
Polymers848,36427
Non-polymers2406
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)219.521, 219.337, 392.432
Angle α, β, γ (deg.)90.00, 90.02, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein
ORF16


Mass: 42542.848 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) LACTOCOCCUS PHAGE P2 (virus) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21
#2: Protein ...
PUTATIVE RECEPTOR BINDING PROTEIN / Receptor (biochemistry) / ORF18


Mass: 28536.861 Da / Num. of mol.: 36 / Fragment: RESIDUES 2-264
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) LACTOCOCCUS PHAGE P2 (virus) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / References: UniProt: Q1RNF7, UniProt: Q71AW2*PLUS
#3: Protein
ORF15


Mass: 34511.992 Da / Num. of mol.: 12
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) LACTOCOCCUS PHAGE P2 (virus) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21
#4: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: Ca
Nonpolymer detailsCALCIUM (CA): DIVALENT CATION

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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: 5.6 Å3/Da / Density % sol: 77.9 % / Description: NONE
Crystal growpH: 7.5
Details: 20C, PROTEIN 4 MG/ML. 3.3% PEG 8000 IN 33 MM TRIS PH 8.5, 130 MM CA ACETATE, 66 MM LI SULFATE, AND 66 MM IMIDAZOLE.

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SOLEIL / Beamline: PROXIMA 1 / Wavelength: 0.98
DetectorType: ADSC QUANTUM 315r / Detector: CCD
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98 Å / Relative weight: 1
ReflectionResolution: 5.464→44.6 Å / Num. obs: 112351 / % possible obs: 91.4 % / Observed criterion σ(I): 0 / Redundancy: 4.2 % / Biso Wilson estimate: 200 Å2 / Rmerge(I) obs: 0.07 / Net I/σ(I): 12.3
Reflection shellResolution: 5.464→5.8 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.46 / Mean I/σ(I) obs: 2.8 / % possible all: 87.2

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Processing

Software
NameVersionClassification
PHASERmodel building
PHENIX(PHENIX.REFINE)refinement
XDSdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2X53

2x53


Resolution: 5.464→44.563 Å / SU ML: 0.72 / σ(F): 1.35 / Phase error: 32.12 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2974 5615 5 %
Rwork0.2908 --
obs0.2912 112191 91 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 99 Å2 / ksol: 0.289 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-35.9922 Å20 Å20.2241 Å2
2--27.8547 Å20 Å2
3----63.8469 Å2
Refinement stepCycle: LAST / Resolution: 5.464→44.563 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms59736 0 6 0 59742
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01100000
X-RAY DIFFRACTIONf_angle_d1.672100000
X-RAY DIFFRACTIONf_dihedral_angle_d19.0343284
X-RAY DIFFRACTIONf_chiral_restr0.1318912
X-RAY DIFFRACTIONf_plane_restr0.00621360
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
5.4641-5.6590.33255120.34149789X-RAY DIFFRACTION84
5.659-5.88510.32415630.325810824X-RAY DIFFRACTION93
5.8851-6.15230.35085620.331810799X-RAY DIFFRACTION93
6.1523-6.47580.33685730.330510913X-RAY DIFFRACTION93
6.4758-6.88010.31855620.320510741X-RAY DIFFRACTION93
6.8801-7.40910.32265760.313410769X-RAY DIFFRACTION92
7.4091-8.15060.3016190.296610783X-RAY DIFFRACTION92
8.1506-9.32060.29785590.275910680X-RAY DIFFRACTION92
9.3206-11.70770.2495710.256210692X-RAY DIFFRACTION91
11.7077-44.56440.28955180.27610586X-RAY DIFFRACTION88
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)
10.73070.01550.21310.1920.02542.6132-0.17280.8125-0.2911-0.45050.0249-0.73540.23580.5667-03.1340.28810.83414.1052-0.03643.4094115.7349-53.445125.6852
20.8251-0.0666-0.0932-0.6743-0.19763.61850.0116-0.1520.25490.1066-0.5583-0.74930.47920.029402.5067-0.57340.71622.71210.882.5431130.732923.789926.2859
31.2987-0.55220.97530.4160.51150.86350.09511.34511.02820.2257-0.5616-0.6745-0.46280.668-0.16842.9869-0.2928-0.57673.73211.6073.658468.582777.941727.3112
41.3648-0.2778-1.91351.44430.5892.4061-0.20760.51090.4891-0.4703-0.14860.6183-0.6566-0.6836-0.00032.84260.2654-0.94654.08830.10393.2612-5.874848.968525.7516
51.1923-0.52180.9221-0.38330.02441.2026-0.03420.27250.1392-0.5507-0.48660.4-0.488-0.054103.1608-0.73-0.59423.5997-0.71313.3238-21.0229-28.349626.2628
61.248-0.38090.72871.2877-2.02883.2402-0.06381.4146-1.15650.1651-0.80890.76580.7522-0.2702-0.10643.1149-0.03160.52163.9663-1.70033.873141.1129-82.385327.0911
70.5353-0.08010.73082.26481.78531.010.23180.53280.1591-0.3401-0.0306-0.55280.21480.028702.6831-0.23310.44233.0360.5152.825296.4589-16.725868.6152
80.1649-0.1542-0.13270.402-0.12050.5608-0.5240.51790.3786-0.18930.24130.31090.09280.1545-02.7122-0.5284-0.13833.36040.61972.966188.402726.565668.6398
9-0.154-0.60880.57721.78080.1173-0.6880.47760.4804-0.1026-0.3306-0.49780.403-0.04420.681-02.8561-0.3294-0.69292.99340.15042.943246.633341.033168.9224
10-0.28740.1615-0.4125-0.1677-1.40591.4566-0.06510.29240.0089-0.1697-0.05560.1203-0.0129-0.1031-02.8921-0.2709-0.41022.9335-0.52093.029813.060912.309668.7122
110.9254-0.8411-0.21060.19930.4926-0.4243-0.11310.4933-0.3664-0.48310.1405-0.2930.0246-0.1995-02.4626-0.45010.11443.2666-0.28442.6421.3217-31.147968.5446
12-0.26650.32520.51440.05640.68881.019-0.31390.4681-0.5856-0.16710.2838-0.6508-0.32680.076702.3837-0.42320.50052.8908-0.38153.129962.9954-45.636968.7574
132.5658-0.59880.23221.5016-1.15671.0098-1.4678-0.4402-0.0012-1.96340.2409-1.14980.00460.0312-0.0374.9717-0.54390.51615.1897-0.49164.347371.9421-22.054430.4438
14-0.0531-1.10950.19033.3563-2.46580.289-0.22851.17870.16220.2646-0.4643-0.2425-0.9951-0.0122-0.00014.9564-0.2333-0.22835.25650.22444.216363.307123.481130.6885
154.8672.80741.0653.2571.5815-0.1468-0.21-0.9247-0.2962-1.3508-0.79410.40830.3311-0.7911-0.0054.5086-0.1092-0.2645.1155-0.17284.066928.1335-6.546530.6083
161.3992-0.3596-0.54311.128-1.92712.4808-0.1204-0.62360.71440.6224-0.24550.3259-0.5691-0.209-0.00184.09470.4511-0.16932.7512-0.96463.31033.545258.4986170.534
17-1.1352-0.1232-0.07450.6430.60452.8241-0.47240.13740.6274-0.06250.0169-0.34850.217-0.2842-02.6897-0.5207-0.9482.3221-0.55132.554681.036673.3729170.0559
180.5901-0.19030.50442.552-1.72060.9652-0.66520.29680.67151.5605-0.0936-1.521-1.1860.3107-0.32763.5874-0.1598-1.5823.03380.57883.697135.079111.2505168.8804
190.4016-0.30720.03310.87070.76850.1666-0.0685-0.3609-0.42470.3496-0.1386-0.62920.41930.4528-04.23560.1692-0.27193.02770.74773.3717106.0504-63.0334170.5271
200.169-0.6405-0.18231.187-0.89943.9034-0.5652-0.5058-0.50160.3117-0.04110.025-0.25660.659303.4478-0.86420.73573.10060.44863.156228.7136-78.161169.8282
210.5027-1.38620.74583.55661.77871.05-0.96230.3502-1.01052.28260.02382.22960.914-0.393-0.64154.2922-0.22212.24823.0422-0.55654.2955-25.1429-16.1228169.351
222.97960.4769-0.510.196-1.1670.2428-0.11620.35090.35350.4775-0.005-0.0839-0.2901-0.5886-02.843-0.2198-0.33972.6689-0.41212.951540.313339.2873127.6167
23-0.4976-0.13790.7623-1.20990.57980.82010.3863-0.3963-0.02980.4044-0.2577-0.3359-0.0796-0.2425-03.0459-0.4352-0.32412.78720.052.995683.70431.1542127.6253
240.87270.00590.25810.3690.48460.8162-0.1661-0.1942-0.07490.19870.04050.0536-0.1991-0.124702.777-0.4576-0.10092.65750.743.078598.2002-10.5135127.3583
25-0.31920.17660.9476-0.7356-0.02911.0852-0.0271-0.252-0.180.36770.19590.07270.00190.066802.971-0.03640.31892.97070.30023.118269.3828-43.9969127.5118
260.3993-1.68250.30020.15911.08760.56330.1729-0.22520.35110.8212-0.37060.4630.4866-0.3609-03.1777-0.52080.56132.674-0.21832.672825.9485-35.7937127.6333
270.35580.0599-0.6941-1.4378-0.46170.7750.0016-0.05510.47960.2962-0.01330.44560.33460.0464-03.2713-0.48430.31852.7178-0.66913.110411.47085.8251127.438
282.58830.9686-0.73880.4207-1.286-0.71880.0867-0.63510.6417-0.1756-0.72360.52920.18370.030205.5177-0.45110.4084.0083-0.19883.706235.090714.7713165.7374
290.51110.54490.05680.95371.40470.3152-0.2452-0.23570.17730.1274-0.1529-0.6135-0.0518-0.013804.9484-0.2892-0.58424.63990.17353.790580.46766.0275165.5575
300.64561.60580.31753.1163-0.3391-0.5657-0.6403-0.5116-0.253-0.42930.20320.4660.148-0.6338-05.4042-0.55950.12324.84970.27723.588850.3037-28.9608165.656
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN AA OR CHAIN AB OR CHAIN AC
2X-RAY DIFFRACTION2CHAIN AD OR CHAIN AE OR CHAIN AF
3X-RAY DIFFRACTION3CHAIN AG OR CHAIN AH OR CHAIN AI
4X-RAY DIFFRACTION4CHAIN AJ OR CHAIN AK OR CHAIN AL
5X-RAY DIFFRACTION5CHAIN AM OR CHAIN AN OR CHAIN AO
6X-RAY DIFFRACTION6CHAIN AP OR CHAIN AQ OR CHAIN AR
7X-RAY DIFFRACTION7CHAIN AS
8X-RAY DIFFRACTION8CHAIN AT
9X-RAY DIFFRACTION9CHAIN AU
10X-RAY DIFFRACTION10CHAIN AV
11X-RAY DIFFRACTION11CHAIN AW
12X-RAY DIFFRACTION12CHAIN AX
13X-RAY DIFFRACTION13CHAIN AY
14X-RAY DIFFRACTION14CHAIN AZ
15X-RAY DIFFRACTION15CHAIN A0
16X-RAY DIFFRACTION16CHAIN BA OR CHAIN BB OR CHAIN BC
17X-RAY DIFFRACTION17CHAIN BD OR CHAIN BE OR CHAIN BF
18X-RAY DIFFRACTION18CHAIN BG OR CHAIN BH OR CHAIN BI
19X-RAY DIFFRACTION19CHAIN BJ OR CHAIN BK OR CHAIN BL
20X-RAY DIFFRACTION20CHAIN BM OR CHAIN BN OR CHAIN BO
21X-RAY DIFFRACTION21CHAIN BP OR CHAIN BQ OR CHAIN BR
22X-RAY DIFFRACTION22CHAIN BS
23X-RAY DIFFRACTION23CHAIN BT
24X-RAY DIFFRACTION24CHAIN BU
25X-RAY DIFFRACTION25CHAIN BV
26X-RAY DIFFRACTION26CHAIN BW
27X-RAY DIFFRACTION27CHAIN BX
28X-RAY DIFFRACTION28CHAIN BY
29X-RAY DIFFRACTION29CHAIN BZ
30X-RAY DIFFRACTION30CHAIN B0

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