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- PDB-6y32: Structure of the GTPase heterodimer of human SRP54 and SRalpha -

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Basic information

Entry
Database: PDB / ID: 6y32
TitleStructure of the GTPase heterodimer of human SRP54 and SRalpha
Components(Signal recognition particle ...) x 2
KeywordsRNA BINDING PROTEIN / SRP54 NG domain / SR alpha NG domain / Targeting complex Protein translocation
Function / homology
Function and homology information


signal recognition particle receptor complex / SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition / endoplasmic reticulum signal peptide binding / signal recognition particle, endoplasmic reticulum targeting / signal recognition particle binding / cotranslational protein targeting to membrane / protein targeting to ER / granulocyte differentiation / signal-recognition-particle GTPase / SRP-dependent cotranslational protein targeting to membrane, translocation ...signal recognition particle receptor complex / SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition / endoplasmic reticulum signal peptide binding / signal recognition particle, endoplasmic reticulum targeting / signal recognition particle binding / cotranslational protein targeting to membrane / protein targeting to ER / granulocyte differentiation / signal-recognition-particle GTPase / SRP-dependent cotranslational protein targeting to membrane, translocation / XBP1(S) activates chaperone genes / 7S RNA binding / SRP-dependent cotranslational protein targeting to membrane / exocrine pancreas development / SRP-dependent cotranslational protein targeting to membrane / ribonucleoprotein complex binding / neutrophil chemotaxis / intracellular protein transport / GDP binding / nuclear speck / GTPase activity / endoplasmic reticulum membrane / GTP binding / endoplasmic reticulum / ATP hydrolysis activity / RNA binding / extracellular exosome / nucleus / membrane / cytoplasm / cytosol
Similarity search - Function
Signal recognition particle receptor, alpha subunit, N-terminal / Signal recognition particle, alpha subunit, N-terminal / Signal recognition particle, SRP54 subunit, eukaryotic / SRP/SRP receptor, N-terminal / Signal recognition particle, SRP54 subunit / Signal recognition particle, SRP54 subunit, M-domain / Signal recognition particle, SRP54 subunit, M-domain superfamily / Signal peptide binding domain / SRP54-type proteins GTP-binding domain signature. / Signal recognition particle SRP54, helical bundle ...Signal recognition particle receptor, alpha subunit, N-terminal / Signal recognition particle, alpha subunit, N-terminal / Signal recognition particle, SRP54 subunit, eukaryotic / SRP/SRP receptor, N-terminal / Signal recognition particle, SRP54 subunit / Signal recognition particle, SRP54 subunit, M-domain / Signal recognition particle, SRP54 subunit, M-domain superfamily / Signal peptide binding domain / SRP54-type proteins GTP-binding domain signature. / Signal recognition particle SRP54, helical bundle / Signal recognition particle SRP54, N-terminal domain superfamily / SRP54-type protein, helical bundle domain / SRP54-type protein, helical bundle domain / Signal recognition particle, SRP54 subunit, GTPase domain / SRP54-type protein, GTPase domain / SRP54-type protein, GTPase domain / Longin-like domain superfamily / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER / Signal recognition particle receptor subunit alpha / Signal recognition particle subunit SRP54
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.6 Å
AuthorsJuaire, K.D. / Becker, M.M.M. / Wild, K. / Sinning, I.
Funding support Germany, 1items
OrganizationGrant numberCountry
German Research Foundation (DFG)SI 586/6-1 Germany
CitationJournal: Structure / Year: 2021
Title: Structural and Functional Impact of SRP54 Mutations Causing Severe Congenital Neutropenia.
Authors: Juaire, K.D. / Lapouge, K. / Becker, M.M.M. / Kotova, I. / Michelhans, M. / Carapito, R. / Wild, K. / Bahram, S. / Sinning, I.
History
DepositionFeb 17, 2020Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 23, 2020Provider: repository / Type: Initial release
Revision 1.1Dec 16, 2020Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2Jan 20, 2021Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.year
Revision 1.3Jan 24, 2024Group: 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 1.4Oct 16, 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: Signal recognition particle 54 kDa protein
B: Signal recognition particle receptor subunit alpha
C: Signal recognition particle 54 kDa protein
D: Signal recognition particle receptor subunit alpha
E: Signal recognition particle 54 kDa protein
F: Signal recognition particle receptor subunit alpha
G: Signal recognition particle 54 kDa protein
H: Signal recognition particle receptor subunit alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)277,70338
Polymers271,9868
Non-polymers5,71730
Water8,395466
1
A: Signal recognition particle 54 kDa protein
B: Signal recognition particle receptor subunit alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,3789
Polymers67,9972
Non-polymers1,3817
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5470 Å2
ΔGint-54 kcal/mol
Surface area24320 Å2
MethodPISA
2
C: Signal recognition particle 54 kDa protein
D: Signal recognition particle receptor subunit alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,2828
Polymers67,9972
Non-polymers1,2856
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5760 Å2
ΔGint-62 kcal/mol
Surface area23920 Å2
MethodPISA
3
E: Signal recognition particle 54 kDa protein
F: Signal recognition particle receptor subunit alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,3789
Polymers67,9972
Non-polymers1,3817
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5600 Å2
ΔGint-61 kcal/mol
Surface area24300 Å2
MethodPISA
4
G: Signal recognition particle 54 kDa protein
H: Signal recognition particle receptor subunit alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,66612
Polymers67,9972
Non-polymers1,66910
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6110 Å2
ΔGint-89 kcal/mol
Surface area24040 Å2
MethodPISA
Unit cell
Length a, b, c (Å)155.825, 70.634, 172.573
Angle α, β, γ (deg.)90.000, 116.810, 90.000
Int Tables number3
Space group name H-MP121

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Components

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Signal recognition particle ... , 2 types, 8 molecules ACEGBDFH

#1: Protein
Signal recognition particle 54 kDa protein / SRP54


Mass: 33511.711 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SRP54 / Production host: Escherichia coli (E. coli) / References: UniProt: P61011
#2: Protein
Signal recognition particle receptor subunit alpha / SR-alpha / Docking protein alpha / DP-alpha


Mass: 34484.855 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SRPRA, SRPR / Production host: Escherichia coli (E. coli) / References: UniProt: P08240

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Non-polymers , 4 types, 496 molecules

#3: Chemical
ChemComp-GNP / PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER


Mass: 522.196 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C10H17N6O13P3 / Feature type: SUBJECT OF INVESTIGATION
Comment: GppNHp, GMPPNP, energy-carrying molecule analogue*YM
#4: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Mg
#5: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 14 / Source method: obtained synthetically / Formula: SO4
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 466 / Source method: isolated from a natural source / Formula: H2O

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Details

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: 3.12 Å3/Da / Density % sol: 60.53 %
Crystal growTemperature: 291.15 K / Method: vapor diffusion, sitting drop
Details: 0.4 M lithium sulfate, 13% (w/v) PEG 3350, 0.1 M Tris (pH 8.0)

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 1.072 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: May 9, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.072 Å / Relative weight: 1
Reflection twinOperator: h,-k,-h-l / Fraction: 0.26
ReflectionResolution: 2.4→49.553 Å / Num. obs: 130686 / % possible obs: 99.6 % / Redundancy: 3.8 % / Rpim(I) all: 0.06233 / Net I/σ(I): 11.34
Reflection shellResolution: 2.4→2.49 Å / Num. unique obs: 12547 / Rpim(I) all: 0.6239

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Processing

Software
NameVersionClassification
PHENIX1.15.2_3472refinement
PDB_EXTRACT3.25data extraction
XDSdata reduction
Aimlessdata scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5L3Q

5l3q


Resolution: 2.6→49.553 Å / Cross valid method: THROUGHOUT / σ(F): 97.23 / Phase error: 28.98
RfactorNum. reflection% reflection
Rfree0.1844 5184 5.02 %
Rwork0.149 --
obs0.1543 103314 99.55 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 178.99 Å2 / Biso mean: 59.3332 Å2 / Biso min: 13.07 Å2
Refinement stepCycle: final / Resolution: 2.6→49.553 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17559 0 334 466 18359
Biso mean--52.81 47.48 -
Num. residues----2288
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 20

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.6-2.64480.2672520.24184849510195
2.6448-2.69290.27062820.23634872515494
2.6929-2.74470.28542580.23194877513595
2.7447-2.80070.27812530.21414862511595
2.8007-2.86160.25492650.21574865513094
2.8616-2.92820.2682610.21014913517495
2.9282-3.00140.24232560.20124857511395
3.0014-3.08250.23852220.19374900512295
3.0825-3.17320.23432680.1924870513894
3.1732-3.27560.22932600.18314864512495
3.2756-3.39260.22172660.17324930519695
3.3926-3.52840.19342420.15854911515395
3.5284-3.68890.17922650.15274869513494
3.6889-3.88330.17812590.13974902516195
3.8833-4.12640.1662460.12534921516794
4.1264-4.44470.14792560.11714905516194
4.4447-4.89150.12672640.11114943520795
4.8915-5.59820.14962490.12194955520495
5.5982-7.04860.17832700.14094973524394
7.0486-44.49780.1462670.12115112537994
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)
10.58360.50440.51560.51570.68071.1539-0.08840.18390.0029-0.18340.01070.2122-0.0318-0.13060.04791.0417-0.0762-0.11320.26870.0450.3855130.338113.296441.3066
20.64760.0779-0.06081.2430.00060.5981-0.0070.03660.2404-0.17490.03330.4494-0.1126-0.2035-0.01991.1190.0508-0.04460.00250.00940.4445130.644740.926653.1762
30.5853-0.58040.18254.0754-0.75850.1528-0.076-0.1463-0.31080.35140.0606-0.44160.18520.10420.04851.01730.0297-0.05460.09970.02970.4648152.0615.05658.4299
41.14120.35080.46190.57670.10640.8393-0.0442-0.0748-0.04980.07360.0476-0.0484-0.10190.1009-0.04681.01240.00760.0804-0.0284-0.07290.2169159.125645.581762.4525
50.25840.2362-0.11510.9251-0.00610.71640.04120.0603-0.0509-0.0129-0.0081-0.08160.06070.0606-0.01271.04510.01540.0764-0.1276-0.05760.1773156.68534.041255.6306
60.1139-0.6370.61693.5762-3.44133.3276-0.0706-0.4432-0.5538-0.126-0.1203-0.15020.23730.23020.17691.04880.05890.05620.69630.18650.9323170.26355.0717106.1115
72.05940.24650.71610.99160.40851.9111-0.077-0.0958-0.46150.19830.0764-0.38430.31080.3425-0.02580.84910.0738-0.02940.4320.06670.4696181.227417.9395101.7337
80.7103-0.18680.03671.348-0.27480.7359-0.02490.02330.2660.117-0.0504-0.2824-0.17160.2390.04991.0448-0.099-0.0220.12770.04230.3801176.629244.499389.1005
91.4069-0.91280.11252.4829-0.46880.3598-0.0665-0.1825-0.09820.3007-0.023-0.127-0.03720.11930.08760.8903-0.0478-0.08470.15220.06360.2338176.227931.27101.368
101.94940.4282-0.64230.1536-0.05430.3339-0.30920.1782-0.5452-0.45320.2053-0.6160.3067-0.11980.11520.9701-0.024-0.01790.1669-0.03850.663159.03683.796793.6152
111.3457-1.2503-1.54551.16181.43561.77520.08220.0968-0.13140.7556-0.24581.12380.6562-0.57150.15760.9529-0.1266-0.01530.29720.11880.8328151.9316.047996.5163
122.7064-2.63841.7222.5722-1.67941.09640.2820.3229-0.5716-0.7176-0.2641.07810.2478-0.2868-0.00511.0846-0.1702-0.01290.5125-0.08710.9784150.64386.482286.6813
130.629-1.10310.35183.8171-0.41051.0632-0.0198-0.0497-0.77630.11770.12110.80730.4332-0.4425-0.09470.8045-0.04850.02230.80270.04850.8428135.412933.913288.7957
140.28580.0474-0.00820.908-0.15220.47480.0438-0.02720.07920.11060.0440.117-0.0859-0.1446-0.07491.10920.0010.1592-0.10040.12160.2151149.215544.473994.812
151.2196-0.21790.00312.4648-0.70641.61940.0151-0.0373-0.20490.05610.01170.21750.2892-0.1014-0.02250.8873-0.04830.05610.0552-0.02550.1394151.818327.62390.0091
161.2414-0.8198-0.45977.22222.6731.9431-0.0985-0.34880.70030.576-0.1623-0.0837-0.9573-0.0890.26571.0376-0.0145-0.02630.3886-0.1210.6703179.686151.071933.9543
171.77270.37560.15552.0741-0.35281.6241-0.331-0.10040.1970.18810.17530.4172-0.2843-0.37070.12270.80930.12740.12620.49530.0490.2992168.535438.989429.3547
181.37660.4978-0.10411.4814-0.21870.42020.02380.0063-0.38350.299-0.05970.13770.2017-0.18270.0740.8606-0.11610.15640.0971-0.05850.2811175.41737.871620.7089
193.14670.3779-2.1551.9724-1.77844.6538-0.08180.4876-0.44770.10160.06150.79870.7254-0.84740.02780.6904-0.16250.08380.557-0.1930.5966168.1573.143310.8425
201.114-0.5206-0.35910.5990.24381.4738-0.07820.2538-0.1139-0.0652-0.02380.2430.2268-0.32430.05240.786-0.04660.10610.20920.01270.1535173.541719.735913.1359
211.283-0.7492-0.49082.8706-0.37160.4464-0.0285-0.0690.00860.3750.12410.2291-0.1353-0.1037-0.05950.8761-0.0090.17780.16730.00490.2312174.273525.539328.9318
222.97162.23522.04471.89841.65161.4679-0.3278-0.06710.5903-0.03620.1090.2494-0.2906-0.07250.20011.17380.00190.06890.23740.02880.6779191.64155.457321.6625
232.95612.5422-0.45894.45470.13930.19610.04770.28790.6055-0.40650.106-0.5289-0.59080.161-0.18291.0694-0.08410.16680.22130.00990.6159198.511749.321119.0419
241.35-0.9135-0.04191.10950.7941.9046-0.0743-0.01320.2929-0.08760.2702-0.4326-0.12030.4177-0.22790.8225-0.02690.09520.0452-0.08460.2541206.173716.00717.9559
250.0579-0.1797-0.52560.70511.48884.7002-0.02860.0606-0.2312-0.05170.2522-0.25230.48280.5653-0.22640.79160.05130.00350.2068-0.1590.3697201.66343.174111.4182
260.32960.10680.04561.03840.47390.9684-0.0214-0.05640.010.14960.0868-0.18390.00460.1155-0.1091.09260.01090.0513-0.0368-0.0980.2128199.83321.933923.6783
271.76062.17391.5842.98422.7053.2998-0.2907-0.54010.83150.5221-0.3552-0.0062-1.0367-0.32370.63070.96980.0332-0.03660.5251-0.12420.6165100.347151.198231.725
284.2066-0.9633-1.04534.78921.10144.974-0.0449-0.15150.4654-0.04080.05020.2124-0.6019-0.30370.02760.74030.03360.07850.36650.00340.420793.558545.967724.2578
291.89180.60120.32874.31321.29841.8526-0.1021-0.36470.12340.0803-0.07580.4662-0.1915-0.4470.14460.84960.07920.23270.64490.07320.366486.042534.914331.9383
301.26680.07880.19011.5501-0.47540.18450.0278-0.1731-0.44940.3244-0.01330.40560.1454-0.1666-0.03960.8947-0.1420.11840.08270.01480.324493.26137.779519.7391
313.3545-0.0456-1.18672.373-0.90763.62920.04460.1576-0.69530.1420.05690.84280.4295-0.8772-0.10260.7147-0.1943-0.03810.7197-0.07350.934183.83473.148611.6531
321.7021-0.4573-0.05391.9486-0.14291.67960.03190.0255-0.2387-0.03870.0130.44360.1535-0.4429-0.03420.8002-0.05430.0980.18110.04260.23889.702919.680512.7596
331.7402-0.9539-1.73816.3656-0.63344.50430.0103-0.48830.16980.1398-0.10080.11040.2296-0.27130.07780.56840.02040.20670.2093-0.0080.313995.226924.506124.7485
341.3889-0.6144-0.30513.03290.36520.6187-0.0029-0.22010.02140.6501-0.06280.3124-0.0493-0.19010.03071.0304-0.01510.18690.30030.01210.305893.429925.750629.264
351.00931.81550.12914.9530.29420.0195-0.11980.17320.1065-0.48390.1254-0.4181-0.27650.1256-0.00541.0212-0.0610.11780.10530.01850.4395112.8751.804914.1403
361.134-0.3638-0.37970.63860.02390.8769-0.03380.05010.04050.0485-0.0083-0.08490.07610.0833-0.04191.0516-0.00240.0455-0.0042-0.02270.2062120.175611.5110.2218
370.3189-0.17970.13410.8327-0.05220.80640.0487-0.06040.06990.1505-0.01-0.0678-0.04720.0703-0.00391.122-0.01840.0346-0.09330.04130.2188117.740222.853816.8829
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 22 through 101 )A22 - 101
2X-RAY DIFFRACTION2chain 'A' and (resid 102 through 296 )A102 - 296
3X-RAY DIFFRACTION3chain 'B' and (resid 330 through 397 )B330 - 397
4X-RAY DIFFRACTION4chain 'B' and (resid 398 through 497 )B398 - 497
5X-RAY DIFFRACTION5chain 'B' and (resid 498 through 638 )B498 - 638
6X-RAY DIFFRACTION6chain 'C' and (resid 22 through 41 )C22 - 41
7X-RAY DIFFRACTION7chain 'C' and (resid 42 through 101 )C42 - 101
8X-RAY DIFFRACTION8chain 'C' and (resid 102 through 239 )C102 - 239
9X-RAY DIFFRACTION9chain 'C' and (resid 240 through 296 )C240 - 296
10X-RAY DIFFRACTION10chain 'D' and (resid 330 through 355 )D330 - 355
11X-RAY DIFFRACTION11chain 'D' and (resid 356 through 377 )D356 - 377
12X-RAY DIFFRACTION12chain 'D' and (resid 378 through 397 )D378 - 397
13X-RAY DIFFRACTION13chain 'D' and (resid 398 through 414 )D398 - 414
14X-RAY DIFFRACTION14chain 'D' and (resid 415 through 572 )D415 - 572
15X-RAY DIFFRACTION15chain 'D' and (resid 573 through 638 )D573 - 638
16X-RAY DIFFRACTION16chain 'E' and (resid 22 through 42 )E22 - 42
17X-RAY DIFFRACTION17chain 'E' and (resid 43 through 101 )E43 - 101
18X-RAY DIFFRACTION18chain 'E' and (resid 102 through 167 )E102 - 167
19X-RAY DIFFRACTION19chain 'E' and (resid 168 through 181 )E168 - 181
20X-RAY DIFFRACTION20chain 'E' and (resid 182 through 239 )E182 - 239
21X-RAY DIFFRACTION21chain 'E' and (resid 240 through 296 )E240 - 296
22X-RAY DIFFRACTION22chain 'F' and (resid 330 through 351 )F330 - 351
23X-RAY DIFFRACTION23chain 'F' and (resid 352 through 397 )F352 - 397
24X-RAY DIFFRACTION24chain 'F' and (resid 398 through 460 )F398 - 460
25X-RAY DIFFRACTION25chain 'F' and (resid 461 through 490 )F461 - 490
26X-RAY DIFFRACTION26chain 'F' and (resid 491 through 638 )F491 - 638
27X-RAY DIFFRACTION27chain 'G' and (resid 22 through 42 )G22 - 42
28X-RAY DIFFRACTION28chain 'G' and (resid 43 through 59 )G43 - 59
29X-RAY DIFFRACTION29chain 'G' and (resid 60 through 101 )G60 - 101
30X-RAY DIFFRACTION30chain 'G' and (resid 102 through 167 )G102 - 167
31X-RAY DIFFRACTION31chain 'G' and (resid 168 through 181 )G168 - 181
32X-RAY DIFFRACTION32chain 'G' and (resid 182 through 239 )G182 - 239
33X-RAY DIFFRACTION33chain 'G' and (resid 240 through 256 )G240 - 256
34X-RAY DIFFRACTION34chain 'G' and (resid 257 through 296 )G257 - 296
35X-RAY DIFFRACTION35chain 'H' and (resid 330 through 397 )H330 - 397
36X-RAY DIFFRACTION36chain 'H' and (resid 398 through 497 )H398 - 497
37X-RAY DIFFRACTION37chain 'H' and (resid 498 through 638 )H498 - 638

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