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- PDB-3sjq: Crystal structure of a small conductance potassium channel splice... -

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Basic information

Entry
Database: PDB / ID: 3sjq
TitleCrystal structure of a small conductance potassium channel splice variant complexed with calcium-calmodulin
Components
  • Calmodulin
  • Small conductance calcium-activated potassium channel protein 2
KeywordsMETAL BINDING PROTEIN / protein-protein complex / EF hand / calmodulin / calcium binding
Function / homology
Function and homology information


Ca2+ activated K+ channels / regulation of store-operated calcium channel activity / : / : / small conductance calcium-activated potassium channel activity / membrane repolarization during atrial cardiac muscle cell action potential / regulation of response to tumor cell / positive regulation of autophagic cell death / DAPK1-calmodulin complex / calcium-activated potassium channel activity ...Ca2+ activated K+ channels / regulation of store-operated calcium channel activity / : / : / small conductance calcium-activated potassium channel activity / membrane repolarization during atrial cardiac muscle cell action potential / regulation of response to tumor cell / positive regulation of autophagic cell death / DAPK1-calmodulin complex / calcium-activated potassium channel activity / : / : / : / : / : / positive regulation of potassium ion transport / inward rectifier potassium channel activity / establishment of protein localization to mitochondrial membrane / type 3 metabotropic glutamate receptor binding / establishment of protein localization to membrane / regulation of potassium ion transmembrane transport / positive regulation of DNA binding / negative regulation of high voltage-gated calcium channel activity / negative regulation of ryanodine-sensitive calcium-release channel activity / organelle localization by membrane tethering / mitochondrion-endoplasmic reticulum membrane tethering / autophagosome membrane docking / negative regulation of calcium ion export across plasma membrane / regulation of cardiac muscle cell action potential / presynaptic endocytosis / nitric-oxide synthase binding / regulation of synaptic vesicle exocytosis / calcineurin-mediated signaling / alpha-actinin binding / smooth endoplasmic reticulum / adenylate cyclase binding / regulation of ryanodine-sensitive calcium-release channel activity / protein phosphatase activator activity / regulation of neuronal synaptic plasticity / catalytic complex / detection of calcium ion / regulation of synaptic vesicle endocytosis / regulation of cardiac muscle contraction / postsynaptic cytosol / activation of adenylate cyclase activity / cellular response to interferon-beta / phosphatidylinositol 3-kinase binding / calcium channel inhibitor activity / presynaptic cytosol / positive regulation of nitric-oxide synthase activity / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / enzyme regulator activity / titin binding / sperm midpiece / regulation of calcium-mediated signaling / voltage-gated potassium channel complex / potassium ion transmembrane transport / calcium channel complex / T-tubule / regulation of heart rate / calyx of Held / response to amphetamine / adenylate cyclase activator activity / sarcomere / protein serine/threonine kinase activator activity / nitric-oxide synthase regulator activity / regulation of cytokinesis / spindle microtubule / calcium channel regulator activity / positive regulation of receptor signaling pathway via JAK-STAT / calcium-mediated signaling / sarcolemma / response to calcium ion / modulation of chemical synaptic transmission / potassium ion transport / cellular response to type II interferon / G2/M transition of mitotic cell cycle / Schaffer collateral - CA1 synapse / Z disc / spindle pole / disordered domain specific binding / calcium-dependent protein binding / myelin sheath / protein autophosphorylation / growth cone / vesicle / dendritic spine / transmembrane transporter binding / postsynaptic membrane / calmodulin binding / neuron projection / positive regulation of apoptotic process / protein domain specific binding / neuronal cell body / calcium ion binding / centrosome / protein kinase binding / glutamatergic synapse / cell surface / protein homodimerization activity
Similarity search - Function
Calmodulin-binding domain / Potassium channel, calcium-activated, SK / SK, calmodulin-binding domain superfamily / Calmodulin binding domain / Calcium-activated SK potassium channel / Calmodulin binding domain / Helix Hairpins - #70 / Potassium channel domain / Ion channel / : ...Calmodulin-binding domain / Potassium channel, calcium-activated, SK / SK, calmodulin-binding domain superfamily / Calmodulin binding domain / Calcium-activated SK potassium channel / Calmodulin binding domain / Helix Hairpins - #70 / Potassium channel domain / Ion channel / : / EF-hand domain pair / EF-hand, calcium binding motif / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. / EF-hand calcium-binding domain profile. / EF-hand domain / EF-hand domain pair / Helix Hairpins / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
1-phenylurea / Calmodulin-1 / Calmodulin-1 / Small conductance calcium-activated potassium channel protein 2
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å
AuthorsZhang, M. / Pascal, J.M. / Zhang, J.-F.
CitationJournal: Structure / Year: 2012
Title: Structural basis for calmodulin as a dynamic calcium sensor.
Authors: Zhang, M. / Abrams, C. / Wang, L. / Gizzi, A. / He, L. / Lin, R. / Chen, Y. / Loll, P.J. / Pascal, J.M. / Zhang, J.F.
History
DepositionJun 21, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 30, 2012Provider: repository / Type: Initial release
Revision 1.1Sep 13, 2023Group: 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 / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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_asym_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_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 / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Calmodulin
B: Calmodulin
C: Small conductance calcium-activated potassium channel protein 2
D: Small conductance calcium-activated potassium channel protein 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)56,77830
Polymers54,5924
Non-polymers2,18626
Water6,125340
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11200 Å2
ΔGint-264 kcal/mol
Surface area25570 Å2
MethodPISA
Unit cell
Length a, b, c (Å)47.740, 65.630, 66.080
Angle α, β, γ (deg.)90.68, 110.45, 111.02
Int Tables number1
Space group name H-MP1

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Components

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Protein , 2 types, 4 molecules ABCD

#1: Protein Calmodulin / CaM


Mass: 16852.545 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat)
Gene: Calm1, Calm, Cam, Cam1, Calm2, Cam2, Camb, Calm3, Cam3, Camc
Plasmid: pET-28b / Production host: Escherichia coli (E. coli) / References: UniProt: P62161, UniProt: P0DP29*PLUS
#2: Protein Small conductance calcium-activated potassium channel protein 2 / SK2 / SKCa 2 / SKCa2 / KCa2.2


Mass: 10443.243 Da / Num. of mol.: 2 / Fragment: Calmodulin binding domain, UNP residues 412-487
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Kcnn2 / Plasmid: pET-28b / Production host: Escherichia coli (E. coli) / References: UniProt: P70604

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Non-polymers , 5 types, 366 molecules

#3: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Ca
#4: Chemical
ChemComp-PHU / 1-phenylurea / Phenylurea


Mass: 136.151 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C7H8N2O
#5: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C3H8O3
#6: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: SO4
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 340 / 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: 3.28 Å3/Da / Density % sol: 62.45 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 4.65
Details: 0.75 M Li2SO4, 0.5 M (NH4)2SO4, 0.1 M Sodium citrate pH 4.65 and Silver Bullets 22 reagent 70, VAPOR DIFFUSION, HANGING DROP, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X29A / Wavelength: 1.075 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Oct 5, 2010
RadiationMonochromator: Si 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.075 Å / Relative weight: 1
ReflectionResolution: 1.9→30 Å / Num. all: 53499 / Num. obs: 53499 / % possible obs: 97.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3
Reflection shellResolution: 1.9→2 Å / % possible all: 96.1

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Processing

Software
NameVersionClassification
CBASSdata collection
PHASERphasing
PHENIX(phenix.refine: 1.6.4_486)refinement
XDSdata reduction
XDSdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1G4Y

1g4y


Resolution: 1.9→19.994 Å / SU ML: 0.23 / σ(F): 2.04 / Phase error: 20.4 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2005 2675 5 %Random
Rwork0.1695 ---
obs0.1711 53459 97.96 %-
Solvent computationShrinkage radii: 0.83 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 61.671 Å2 / ksol: 0.386 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-3.497 Å2-0.1519 Å24.2567 Å2
2---2.5944 Å2-3.5547 Å2
3----0.9026 Å2
Refinement stepCycle: LAST / Resolution: 1.9→19.994 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3619 0 124 340 4083
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0143915
X-RAY DIFFRACTIONf_angle_d0.95177
X-RAY DIFFRACTIONf_dihedral_angle_d13.2661502
X-RAY DIFFRACTIONf_chiral_restr0.065563
X-RAY DIFFRACTIONf_plane_restr0.003679
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.9-1.96790.29292740.24354945X-RAY DIFFRACTION95
1.9679-2.04660.2382910.20035029X-RAY DIFFRACTION97
2.0466-2.13960.20662650.17475072X-RAY DIFFRACTION98
2.1396-2.25230.22042370.16245098X-RAY DIFFRACTION98
2.2523-2.39320.2022570.16625102X-RAY DIFFRACTION98
2.3932-2.57760.2312450.17765111X-RAY DIFFRACTION98
2.5776-2.83640.22312900.17855104X-RAY DIFFRACTION99
2.8364-3.24530.21982610.17095128X-RAY DIFFRACTION99
3.2453-4.0830.18312820.15535153X-RAY DIFFRACTION99
4.083-19.99460.17052730.16325042X-RAY DIFFRACTION98
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)
13.25231.67191.09875.88152.14821.45860.31291.3104-0.4957-1.1702-0.2143-0.2377-0.10180.026-0.13950.23940.0187-0.02370.43080.00540.2953.837553.5008-20.3789
22.61910.4241-0.54831.12790.83985.78460.0703-0.53720.55130.018-0.0369-0.0491-0.8038-0.0954-0.08350.05330.0185-0.0350.10020.00460.26371.976462.6074-5.9661
30.89490.7466-0.11540.82560.18920.43890.1286-0.73870.4170.2624-0.26570.39470.0461-0.58680.11180.1626-0.01590.02120.3464-0.06070.2865-6.237457.66231.9767
40.48391.09360.42494.7311.21424.7934-0.1575-0.6713-0.24130.2769-0.33110.38260.348-0.66870.26940.2524-0.0378-0.02210.33840.01760.2846-2.202149.90375.3027
51.41620.2207-0.72020.3117-0.19710.4157-0.0618-0.1555-0.15110.1726-0.0283-0.15490.4134-0.00430.11810.15240.0061-0.03550.2471-0.01460.28087.37152.3261-4.4922
60.6722-1.4424-1.98573.17313.85159.64730.05750.0172-1.0106-0.0806-0.59450.89630.8331-0.66290.00330.06550.03-0.06990.21720.00250.304-0.036345.5621-14.2115
71.17591.47710.52942.06990.2720.9658-0.40250.92380.6984-0.6990.1374-0.0398-0.39350.58040.18540.2413-0.0273-0.01480.407-0.02440.3675-8.00540.3604-19.5133
82.61090.79841.33151.83710.66430.8422-0.02030.5170.3769-0.221-0.12580.48830.2115-0.14970.14710.2782-0.0259-0.01810.2919-0.01740.2431-19.476434.6303-22.6995
92.0249-3.112-1.80136.03130.18670.69860.34211.8333-0.025-1.2401-0.74720.8575-0.0648-1.65060.2790.5605-0.0247-0.04440.5372-0.16910.2119-18.489125.6927-31.8173
104.95490.00021.07450.22910.91097.7808-0.04950.5586-1.28470.12260.1702-0.04972.62370.0817-0.10760.92960.0440.07750.1705-0.04150.4386-16.25617.4993-24.8128
111.49610.5040.363.95974.69555.61660.18250.2359-0.06241.72360.02690.02472.0301-0.2017-0.0210.8699-0.08130.02660.16810.03980.2626-19.458722.8142-14.7295
126.8104-5.0398-0.73817.41453.45162.8615-0.07480.158-0.15891.54510.5152-1.37181.28610.4954-0.51430.40390.1049-0.13040.2564-0.06930.3635-11.076129.6232-16.4131
133.1829-0.7255-0.90463.08191.660.97640.183-1.3340.88550.4192-0.0333-0.1672-0.31920.1639-0.18220.20080.0060.03380.4446-0.0330.28193.5378-11.25363.512
140.9179-0.9021-1.66562.29552.85644.5492-0.06020.5088-0.41920.2085-0.13980.15140.72-0.47990.10530.1532-0.00590.01170.2246-0.00890.28771.6042-19.9178-10.8312
150.19090.31230.12851.0065-0.03261.52270.02290.7287-0.309-0.1728-0.123-0.0239-0.1124-0.08170.11040.16620.0076-0.03160.327-0.03270.2476-6.3351-14.8697-18.8631
162.3644-0.71681.39340.7906-0.02831.08150.01140.88150.6571-0.3535-0.30290.0802-0.5994-0.13410.19160.26220.0588-0.02210.50640.0480.3288-2.4682-7.1709-22.1076
170.96050.0840.81790.08260.08120.67960.05850.1360.3511-0.1977-0.0153-0.0409-0.29420.14180.01680.15580.0060.02880.24820.02390.28266.4985-9.3308-11.4932
182.7493-1.2353-2.54021.86441.65792.62760.17970.04280.55130.3115-0.25450.7485-0.7918-0.4360.24180.2015-0.0280.04230.3447-0.07030.4454-1.3921-1.4954-1.4624
197.7311-5.45596.9849.6354-1.85327.95320.0251-0.4814-1.240.661-0.06740.89420.1626-0.98460.4623-0.0096-0.0205-0.00630.0865-0.07810.1793-9.52812.91483.5478
204.1256-3.2615-2.83924.67760.38974.69050.1671-0.0166-0.74980.3558-0.27291.3071-0.2423-0.42940.11780.2297-0.00420.08610.17930.01010.2935-20.68048.4886.208
213.3381-2.00620.8463.4529-0.47510.2449-0.2429-0.9999-0.01980.89550.01510.4211-0.3594-0.58370.08970.50760.01410.1340.2271-0.00760.2517-19.612817.180213.4456
220.83731.16670.69012.66483.56399.4917-0.2878-0.46890.235-0.0587-0.22310.6915-1.90380.39330.25620.7935-0.02240.2140.21270.01330.4143-16.861925.38388.17
231.66391.77050.12442.80921.58012.36730.2182-0.07780.4442-1.35560.14220.1289-1.35820.0324-0.32420.68140.04250.06870.21530.03070.3428-19.012717.519-2.21
248.4232-3.6321-5.70168.05754.52258.58-0.2203-0.42230.8816-1.78970.3698-2.6385-0.60540.8538-0.30820.3565-0.10230.20850.2704-0.090.5471-10.76913.715-0.4791
252.2995-0.6936-0.08563.2863-3.81035.2017-0.71670.42760.619-1.40250.8529-0.490.3741-0.35270.05920.6179-0.15480.09450.25720.01920.4037-4.941324.3513.1532
262.0801-0.45750.7852.4245-0.32840.44870.009-0.4526-0.34561.54930.0612-0.47420.27690.1029-0.1570.80040.0281-0.05420.30850.03270.2209-7.00968.485518.8064
271.96090.574-1.27550.2468-0.38591.7507-0.136-0.26140.82191.45630.2994-0.2752-0.04890.2738-0.1360.6905-0.0091-0.00250.20720.05760.4624-5.49526.945112.4689
283.9691-1.90941.41244.0481-1.51783.4180.7292-0.5984-0.42020.4505-0.00721.3986-0.0158-0.2153-0.66770.3308-0.0709-0.07590.39010.11690.6267-9.126438.89872.5059
290.8105-0.41650.4820.66690.19610.7837-0.03840.18-0.19520.13590.00880.30560.2207-0.0510.19020.1150.0051-0.01450.3092-0.01970.3072-6.825752.0019-10.4427
302.2059-0.6872-1.93850.65752.11337.93660.3138-0.3815-1.82531.79670.0289-0.3644-1.99220.4731-0.36381.05260.0949-0.25340.38270.28791.359-1.868214.3733-16.9918
312.3640.9827-3.53991.97210.36048.1678-0.640.0484-0.571-0.04380.4714-0.59040.3465-0.49330.18880.52830.09770.09820.29010.00470.3122-7.450127.0976-26.6952
321.39830.0302-0.170.9654-0.33180.7745-0.10170.47960.0885-0.17890.2303-0.6363-0.91280.1174-0.10410.94760.09160.24270.30370.06520.2709-5.776636.0746-38.0761
33-0.06740.6508-0.30826.5942-3.35581.63630.2179-0.02550.017-0.9754-0.11690.20380.06020.1605-0.08850.49650.02290.09050.23670.02010.4124-6.86339.2139-24.0579
340.38260.35030.03021.55960.50311.5969-0.1878-0.3156-0.06510.5705-0.2350.2086-0.2407-0.01670.31220.1757-0.0008-0.0110.33670.01720.3003-6.5261-12.607-3.7079
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(chain A and resid 1:12)
2X-RAY DIFFRACTION2(chain A and resid 13:26)
3X-RAY DIFFRACTION3(chain A and resid 27:42)
4X-RAY DIFFRACTION4(chain A and resid 43:53)
5X-RAY DIFFRACTION5(chain A and resid 54:71)
6X-RAY DIFFRACTION6(chain A and resid 72:79)
7X-RAY DIFFRACTION7(chain A and resid 80:86)
8X-RAY DIFFRACTION8(chain A and resid 87:99)
9X-RAY DIFFRACTION9(chain A and resid 100:116)
10X-RAY DIFFRACTION10(chain A and resid 117:128)
11X-RAY DIFFRACTION11(chain A and resid 129:136)
12X-RAY DIFFRACTION12(chain A and resid 137:147)
13X-RAY DIFFRACTION13(chain B and resid 2:12)
14X-RAY DIFFRACTION14(chain B and resid 13:26)
15X-RAY DIFFRACTION15(chain B and resid 27:42)
16X-RAY DIFFRACTION16(chain B and resid 43:53)
17X-RAY DIFFRACTION17(chain B and resid 54:73)
18X-RAY DIFFRACTION18(chain B and resid 74:80)
19X-RAY DIFFRACTION19(chain B and resid 81:87)
20X-RAY DIFFRACTION20(chain B and resid 88:98)
21X-RAY DIFFRACTION21(chain B and resid 99:116)
22X-RAY DIFFRACTION22(chain B and resid 117:128)
23X-RAY DIFFRACTION23(chain B and resid 129:138)
24X-RAY DIFFRACTION24(chain B and resid 139:146)
25X-RAY DIFFRACTION25(chain C and resid 414:428)
26X-RAY DIFFRACTION26(chain C and resid 429:454)
27X-RAY DIFFRACTION27(chain C and resid 455:469)
28X-RAY DIFFRACTION28(chain C and resid 470:475)
29X-RAY DIFFRACTION29(chain C and resid 476:493)
30X-RAY DIFFRACTION30(chain D and resid 415:419)
31X-RAY DIFFRACTION31(chain D and resid 420:435)
32X-RAY DIFFRACTION32(chain D and resid 436:453)
33X-RAY DIFFRACTION33(chain D and resid 454:481)
34X-RAY DIFFRACTION34(chain D and resid 482:492)

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