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- PDB-2wlm: POTASSIUM CHANNEL FROM MAGNETOSPIRILLUM MAGNETOTACTICUM -

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Basic information

Entry
Database: PDB / ID: 2wlm
TitlePOTASSIUM CHANNEL FROM MAGNETOSPIRILLUM MAGNETOTACTICUM
ComponentsPOTASSIUM CHANNEL
KeywordsMETAL TRANSPORT / INTEGRAL MEMBRANE PROTEIN / IONIC CHANNEL / ION TRANSPORT / TRANSPORT
Function / homology
Function and homology information


inward rectifier potassium channel activity / monoatomic ion channel complex / identical protein binding
Similarity search - Function
G protein-activated inward rectifier potassium channel 1 / Potassium channel, inwardly rectifying, Kir, cytoplasmic / Potassium channel, inwardly rectifying, Kir / Inward rectifier potassium channel, C-terminal / Inward rectifier potassium channel C-terminal domain / Helix Hairpins - #70 / Potassium channel domain / Ion channel / Helix Hairpins / Immunoglobulin E-set ...G protein-activated inward rectifier potassium channel 1 / Potassium channel, inwardly rectifying, Kir, cytoplasmic / Potassium channel, inwardly rectifying, Kir / Inward rectifier potassium channel, C-terminal / Inward rectifier potassium channel C-terminal domain / Helix Hairpins - #70 / Potassium channel domain / Ion channel / Helix Hairpins / Immunoglobulin E-set / Immunoglobulin-like / Sandwich / Orthogonal Bundle / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
: / Inward rectifier potassium channel Kirbac3.1
Similarity search - Component
Biological speciesMAGNETOSPIRILLUM MAGNETOTACTICUM (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.61 Å
AuthorsClarke, O.B. / Caputo, A.T. / Smith, B.J. / Gulbis, J.M.
CitationJournal: Cell(Cambridge,Mass.) / Year: 2010
Title: Domain Reorientation and Rotation of an Intracellular Assembly Regulate Conduction in Kir Potassium Channels.
Authors: Clarke, O.B. / Caputo, A.T. / Hill, A.P. / Vandenberg, J.I. / Smith, B.J. / Gulbis, J.M.
History
DepositionJun 24, 2009Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 9, 2010Provider: repository / Type: Initial release
Revision 1.1Jun 27, 2012Group: Database references / Refinement description ...Database references / Refinement description / Source and taxonomy / Version format compliance
Revision 1.2May 8, 2019Group: Data collection / Experimental preparation / Other
Category: exptl_crystal_grow / pdbx_database_proc / pdbx_database_status
Item: _exptl_crystal_grow.method / _pdbx_database_status.recvd_author_approval
Revision 1.3Dec 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_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.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_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 / _struct_conn.pdbx_dist_value / _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 / _struct_conn.ptnr2_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
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
A: POTASSIUM CHANNEL
B: POTASSIUM CHANNEL
C: POTASSIUM CHANNEL
D: POTASSIUM CHANNEL
hetero molecules


Theoretical massNumber of molelcules
Total (without water)135,2878
Polymers135,1314
Non-polymers1564
Water00
1


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area16720 Å2
ΔGint-115.4 kcal/mol
Surface area49340 Å2
MethodPISA
Unit cell
Length a, b, c (Å)99.261, 151.193, 294.757
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
31
41
12
22
32
42

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111CHAIN A AND RESID 34:136
211CHAIN B AND RESID 34:136
311CHAIN C AND RESID 34:136
411CHAIN D AND RESID 34:136
112CHAIN A AND (RESID 138:184 OR RESID 208:273 OR RESID...
212CHAIN B AND (RESID 138:184 OR RESID 208:273 OR RESID...
312CHAIN C AND (RESID 138:184 OR RESID 208:273 OR RESID...
412CHAIN D AND (RESID 138:184 OR RESID 208:273 OR RESID...

NCS ensembles :
ID
1
2

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Components

#1: Protein
POTASSIUM CHANNEL / KIRBAC3.1


Mass: 33782.766 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Details: C-TERMINAL HEXAHISTIDINE TAG APPENDED
Source: (gene. exp.) MAGNETOSPIRILLUM MAGNETOTACTICUM (bacteria)
Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3)STAR / References: UniProt: D9N164*PLUS
#2: Chemical
ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: K
Sequence detailsRESIDUES 5-295 CORRESPOND TO GENBANK ACCESSION ZP_00055625

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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: 4.6 Å3/Da / Density % sol: 73 % / Description: NONE
Crystal growMethod: vapor diffusion, sitting drop / pH: 6
Details: PRECIPITANT 40 % PEG 200 0.2 M SODIUM CHLORIDE 0.1 M SODIUM PHOSPHATE PH 6.0 PROTEIN KIRBAC3.1, 8MG/ML 150MM KCL 20MM BACL2 4MM LDAO 0.05% TDM 0.2MM PI(4,5)P2 PROTEIN AND PRECIPITANT WERE ...Details: PRECIPITANT 40 % PEG 200 0.2 M SODIUM CHLORIDE 0.1 M SODIUM PHOSPHATE PH 6.0 PROTEIN KIRBAC3.1, 8MG/ML 150MM KCL 20MM BACL2 4MM LDAO 0.05% TDM 0.2MM PI(4,5)P2 PROTEIN AND PRECIPITANT WERE COMBINED IN A 1:1 RATIO AND EQUILIBRATED AGAINST A RESERVOIR OF PRECIPITANT IN A SITTING DROP VAPOUR DIFFUSION SET UP.

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX1 / Wavelength: 0.956608
DetectorType: ADSC CCD / Detector: CCD / Date: Nov 10, 2008 / Details: MIRRORS
RadiationMonochromator: SILICON CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.956608 Å / Relative weight: 1
ReflectionResolution: 3.6→50 Å / Num. obs: 25733 / % possible obs: 94.7 % / Observed criterion σ(I): -3 / Redundancy: 6.3 % / Biso Wilson estimate: 81.82 Å2 / Rmerge(I) obs: 0.13 / Net I/σ(I): 12
Reflection shellResolution: 3.6→3.73 Å / Redundancy: 6 % / Rmerge(I) obs: 0.46 / Mean I/σ(I) obs: 3.8 / % possible all: 92

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
DENZOdata reduction
SCALEPACKdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1XL4

1xl4


Resolution: 3.61→19.971 Å / SU ML: 0.08 / σ(F): 1.34 / Phase error: 28.88 / Stereochemistry target values: ML
Details: BARIUM IN CRYSTALLISATION CONDITION PRECIPITATED OUT DUE TO PRESENCE OF PHOSPHATE, AND WAS NOT OBSERVED IN THE STRUCTURE.
RfactorNum. reflection% reflection
Rfree0.2881 1233 5.1 %
Rwork0.2632 --
obs0.2645 24190 93.73 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 70.71 Å2 / ksol: 0.292 e/Å3
Displacement parametersBiso mean: 0 Å2
Baniso -1Baniso -2Baniso -3
1--8.6718 Å20 Å20 Å2
2---38.7497 Å20 Å2
3----21.7882 Å2
Refinement stepCycle: LAST / Resolution: 3.61→19.971 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8609 0 4 0 8613
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0068820
X-RAY DIFFRACTIONf_angle_d1.03512004
X-RAY DIFFRACTIONf_dihedral_angle_d17.4033015
X-RAY DIFFRACTIONf_chiral_restr0.0661403
X-RAY DIFFRACTIONf_plane_restr0.0061518
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A778X-RAY DIFFRACTIONPOSITIONAL
12B778X-RAY DIFFRACTIONPOSITIONAL0.011
13C778X-RAY DIFFRACTIONPOSITIONAL0.012
14D774X-RAY DIFFRACTIONPOSITIONAL0.01
21A881X-RAY DIFFRACTIONPOSITIONAL
22B881X-RAY DIFFRACTIONPOSITIONAL0.064
23C881X-RAY DIFFRACTIONPOSITIONAL0.065
24D881X-RAY DIFFRACTIONPOSITIONAL0.066
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.6068-3.7503000.3312334X-RAY DIFFRACTION83
3.7503-3.91980.35411490.30622440X-RAY DIFFRACTION91
3.9198-4.12470.3381450.31192456X-RAY DIFFRACTION91
4.1247-4.38060.31712240.2562365X-RAY DIFFRACTION92
4.3806-4.71470.27871020.24762531X-RAY DIFFRACTION92
4.7147-5.18170.24711910.23712498X-RAY DIFFRACTION95
5.1817-5.91440.30691330.25752723X-RAY DIFFRACTION99
5.9144-7.38820.30461360.26472768X-RAY DIFFRACTION100
7.3882-19.97170.2321530.22892842X-RAY DIFFRACTION100
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)
11.352-1.0854-2.8552-2.1266-5.1222-1.8734-0.8153-1.01420.18510.49380.3298-0.27790.2375-1.10170.12131.49-0.4008-0.08721.5778-0.25511.002315.751718.920759.8064
26.5119-0.2476-0.9106-0.77570.8050.9136-0.21160.27560.9432-0.0737-0.30070.0493-1.56220.21390.49521.4793-0.5806-0.06051.0645-0.06261.053130.082636.634554.4045
35.8268-2.73060.67092.86934.14132.69921.0092-0.66031.35160.72710.0604-0.13530.196-0.1326-1.02011.7463-0.674-0.87081.64290.13431.707946.672250.853153.1674
45.18910.758-1.64186.7258-3.58363.38210.2051-0.57160.4333-0.7323-1.3070.2020.20860.83520.69811.014-0.8946-0.36961.2068-0.00641.522637.229145.640948.9626
51.7341-2.3831-0.91822.3663-0.96890.1613-0.3131-0.97180.50910.4378-0.158-0.50040.533-1.05250.28261.1967-0.591-0.3130.96720.36861.073245.191639.711646.6527
62.46810.0998-0.91860.0784-0.27710.5602-0.84511.9568-0.24340.77870.0315-0.21-0.5609-0.57030.8491.3542-0.4033-0.230.924-0.16850.565921.553727.271143.7979
71.36670.4532-0.06544.5919-3.48265.51020.1745-0.65120.33040.30120.15550.4407-0.2372-1.0306-0.36460.7492-0.25480.14831.4432-0.22341.0077-10.251511.077644.0032
87.1037-2.97541.6666-0.3953.98134.8930.4181-3.3308-0.7716-0.8475-0.57530.9634-0.81821.52550.15120.8936-0.1520.54172.1325-0.26820.9165-6.496-2.136666.5818
94.7055-4.42878.3743-3.50611.0751-4.94791.19981.2017-1.8436-0.4878-0.16680.8425-0.0747-1.2065-0.95680.91260.6715-0.07792.20750.25221.5317-18.649523.74123.8181
100.5712-1.03150.19231.86981.69970.5812-0.6210.27220.39770.03910.8241-0.27870.0798-0.56330.02750.7719-0.24360.02771.12360.01560.743134.13380.9145.4909
110.17360.53673.13481.4581.10742.1234-0.33310.2360.026-0.2283-0.70210.023-0.0320.73930.84060.8808-0.4188-0.19771.21010.16370.697745.602326.047338.2437
120.41071.00780.56965.04730.41881.6440.22650.5173-0.278-1.76012.55180.0524-0.0742-0.7195-2.54571.9075-0.7554-0.44741.71050.51241.567156.459444.139932.4431
130.8873-0.8724-0.41251.7238-0.70951.33620.2793-0.3044-0.37560.2813-0.8295-0.92630.3120.27940.34671.5291-1.0803-0.25091.33570.37941.507847.563738.583737.3413
140.0907-0.5108-0.9336-0.38740.02120.37820.4282-0.4895-0.15630.1099-0.38990.00560.3574-0.69880.2391.3601-0.7273-0.22491.38870.17551.115745.422939.48327.4187
15-0.8248-2.18521.11140.85440.1125-0.0040.07480.1407-0.33080.39830.46040.3316-0.10970.162-0.97720.7065-0.5373-0.08151.10720.20071.15329.768221.669340.0508
162.1153-2.1161-1.04526.0012-0.58670.0299-0.5066-0.5638-0.01810.21280.37350.2494-0.3049-0.0750.17271.1844-0.24720.25591.25370.06250.721113.3538-4.302458.3595
173.5752.99410.91713.7312-0.06612.0214-0.1408-1.1626-0.4888-1.892-0.5624-0.26241.2697-1.26210.88542.28340.05090.061.2626-0.01941.008624.1115-24.298445.1617
18-1.9243-0.4753-8.84752.1624-5.5201-5.4216-1.3117-0.4572-0.13621.1727-0.3371-0.97823.0474-1.82971.67541.03410.01890.15261.8243-0.23910.6964.36112.844574.7512
19-0.0471.35830.93481.36841.65511.5196-0.00220.25450.3336-0.38210.4549-0.3592-0.73420.2651-0.54480.5065-0.05630.04880.74530.09720.743822.56197.788715.2391
205.18350.7715-0.50692.7956-2.27686.4802-0.53860.3874-0.06610.3521-0.05541.4733-1.25640.3830.44410.8081-0.3518-0.33420.79730.1690.899932.179735.169619.5311
211.10840.87291.3563-0.86551.42234.4903-0.5567-0.1121.1197-0.05241.43851.9917-2.56180.7436-0.5853.1255-0.9366-0.19741.12240.43251.572839.254155.844220.7506
220.2879-1.3269-0.43542.10841.48062.83950.1058-0.2286-0.6315-1.5484-1.8265-0.7792-2.16120.40991.79972.3307-0.8784-0.46491.09710.26711.376837.864945.159724.9825
230.6387-1.5446-0.88632.70050.80972.5153-0.29020.16870.4745-1.17090.24150.581.31930.19050.32361.2589-0.4873-0.60870.96770.11421.41729.393150.375227.2026
241.1622-1.73121.70742.25870.38450.5096-0.25731.0580.09041.1638-0.6416-0.2521-0.03931.21240.7460.7805-0.2987-0.2710.74890.05890.867726.537823.82530.1344
253.00962.08081.29986.98673.19963.17410.02730.0245-0.2240.4490.2959-0.01810.33490.1559-0.33050.9194-0.04190.01250.88280.09490.862523.2416-12.00630.5789
263.23343.2242-0.44412.67220.6288-0.3669-0.3784-0.29170.9399-1.5099-0.35670.9082-0.30550.15350.28621.71740.0428-0.35871.3694-0.15111.5237.3134-14.075910.1976
275.6739-3.7691-7.03116.4272-7.42522.00480.5228-0.43-0.08661.73051.49840.42741.27320.0896-2.23532.32680.5841-0.96341.2348-0.28761.176239.6799-14.033449.3808
280.82411.217-0.75373.6051.36043.87960.6315-0.0906-0.17681.50440.0251-0.90990.3572-0.42480.32260.825-0.11590.0150.6871-0.26830.72-2.691324.919828.2161
290.83570.560.0973-1.1934-2.38061.35890.7759-0.21220.39540.271-0.526-0.995-0.73890.2469-0.20841.2344-0.2493-0.10640.985-0.15861.697216.562145.721635.6993
30-0.52060.4140.85860.65-2.95810.12441.03480.50930.3290.2358-0.17382.03560.63630.1342-0.98592.1912-0.2809-0.23061.3946-0.39282.024129.233462.524441.7001
310.1692-1.4834-1.13370.16190.92811.27031.7268-0.0883-0.2409-1.5662-2.3777-0.2781-2.25890.1660.42622.1233-0.6195-0.46581.1658-0.03451.930627.454352.208336.7593
320.26010.6747-0.05781.275-0.78660.2396-0.9321-0.0812-0.6064-1.05941.26911.0795-0.2560.5665-0.11341.3357-0.4599-0.29591.13510.03181.529328.707550.302947.0383
333.47151.1866-0.32494.61421.12371.72580.79150.79370.08490.7081-0.2071-2.7232-0.2190.3677-0.29370.6026-0.16150.03210.6588-0.14941.01718.415629.401333.904
344.63630.7696-0.27660.7793-0.27141.94310.21150.0212-0.03080.2372-0.3010.2520.2057-0.1020.13040.9025-0.07040.02970.8149-0.10180.81620.83652.631617.7254
355.26491.62294.62517.27455.5069-1.0411.2058-1.21860.1242.1671.05540.23911.5277-1.3751-1.85521.9137-0.0151-0.47191.89560.10511.4275-22.09816.30529.8022
361.36884.28964.11282.67330.6225-0.41160.6342-0.6085-1.02951.2723-0.3958-1.54061.343-0.2829-0.12121.26660.0663-0.17040.88440.38691.154220.326-3.98084.4723
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN A AND RESID 12:43
2X-RAY DIFFRACTION2CHAIN A AND RESID 44:71
3X-RAY DIFFRACTION3CHAIN A AND RESID 72:81
4X-RAY DIFFRACTION4CHAIN A AND RESID 82:100
5X-RAY DIFFRACTION5CHAIN A AND RESID 101:120
6X-RAY DIFFRACTION6CHAIN A AND RESID 121:137
7X-RAY DIFFRACTION7CHAIN A AND (RESID 138:182 OR RESID 194:274 OR RESID 286:299)
8X-RAY DIFFRACTION8CHAIN A AND RESID 183:193
9X-RAY DIFFRACTION9CHAIN A AND RESID 275:285
10X-RAY DIFFRACTION10CHAIN B AND RESID 12:43
11X-RAY DIFFRACTION11CHAIN B AND RESID 44:71
12X-RAY DIFFRACTION12CHAIN B AND RESID 72:81
13X-RAY DIFFRACTION13CHAIN B AND RESID 82:100
14X-RAY DIFFRACTION14CHAIN B AND RESID 101:120
15X-RAY DIFFRACTION15CHAIN B AND RESID 121:137
16X-RAY DIFFRACTION16CHAIN B AND (RESID 138:182 OR RESID 194:274 OR RESID 286:299)
17X-RAY DIFFRACTION17CHAIN B AND RESID 183:193
18X-RAY DIFFRACTION18CHAIN B AND RESID 275:285
19X-RAY DIFFRACTION19CHAIN C AND RESID 12:43
20X-RAY DIFFRACTION20CHAIN C AND RESID 44:71
21X-RAY DIFFRACTION21CHAIN C AND RESID 72:81
22X-RAY DIFFRACTION22CHAIN C AND RESID 82:100
23X-RAY DIFFRACTION23CHAIN C AND RESID 101:120
24X-RAY DIFFRACTION24CHAIN C AND RESID 121:137
25X-RAY DIFFRACTION25CHAIN C AND (RESID 138:182 OR RESID 194:274 OR RESID 286:299)
26X-RAY DIFFRACTION26CHAIN C AND RESID 183:193
27X-RAY DIFFRACTION27CHAIN C AND RESID 275:285
28X-RAY DIFFRACTION28CHAIN D AND RESID 12:43
29X-RAY DIFFRACTION29CHAIN D AND RESID 44:71
30X-RAY DIFFRACTION30CHAIN D AND RESID 72:81
31X-RAY DIFFRACTION31CHAIN D AND RESID 82:100
32X-RAY DIFFRACTION32CHAIN D AND RESID 101:120
33X-RAY DIFFRACTION33CHAIN D AND RESID 121:137
34X-RAY DIFFRACTION34CHAIN D AND (RESID 138:182 OR RESID 194:274 OR RESID 286:299)
35X-RAY DIFFRACTION35CHAIN D AND RESID 183:193
36X-RAY DIFFRACTION36CHAIN D AND RESID 275:285

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