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- PDB-5q0c: Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosph... -

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Basic information

Entry
Database: PDB / ID: 5q0c
TitleHuman liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosphate 1-phosphatase, E.C.3.1.3.11) complexed with the allosteric inhibitor 1-(5-bromo-1,3-thiazol-2-yl)-3-[5-(4-methoxyphenyl)thiophen-2-yl]sulfonylurea and with fructose-2,6-diphosphate
ComponentsFructose-1,6-bisphosphatase isozyme 2
KeywordsHYDROLASE/HYDROLASE INHIBITOR / D3R docking / HYDROLASE-HYDROLASE INHIBITOR complex
Function / homology
Function and homology information


sucrose biosynthetic process / fructose-bisphosphatase / fructose 1,6-bisphosphate 1-phosphatase activity / fructose 1,6-bisphosphate metabolic process / fructose 6-phosphate metabolic process / fructose metabolic process / Gluconeogenesis / anchoring junction / gluconeogenesis / Z disc ...sucrose biosynthetic process / fructose-bisphosphatase / fructose 1,6-bisphosphate 1-phosphatase activity / fructose 1,6-bisphosphate metabolic process / fructose 6-phosphate metabolic process / fructose metabolic process / Gluconeogenesis / anchoring junction / gluconeogenesis / Z disc / extracellular exosome / identical protein binding / metal ion binding / nucleus / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Fructose-1,6-bisphosphatase / Fructose-1,6-bisphosphatase, active site / Fructose-1-6-bisphosphatase class 1, C-terminal / Fructose-1-6-bisphosphatase active site. / Fructose-1,6-bisphosphatase class 1 / Fructose-1-6-bisphosphatase class I, N-terminal / Fructose-1-6-bisphosphatase, N-terminal domain / Fructose-1-6-bisphosphatase, C-terminal domain / D-Maltodextrin-Binding Protein; domain 2 - #80 / Fructose-1,6-Bisphosphatase, subunit A, domain 1 ...Fructose-1,6-bisphosphatase / Fructose-1,6-bisphosphatase, active site / Fructose-1-6-bisphosphatase class 1, C-terminal / Fructose-1-6-bisphosphatase active site. / Fructose-1,6-bisphosphatase class 1 / Fructose-1-6-bisphosphatase class I, N-terminal / Fructose-1-6-bisphosphatase, N-terminal domain / Fructose-1-6-bisphosphatase, C-terminal domain / D-Maltodextrin-Binding Protein; domain 2 - #80 / Fructose-1,6-Bisphosphatase, subunit A, domain 1 / Fructose-1,6-Bisphosphatase; Chain A, domain 1 / D-Maltodextrin-Binding Protein; domain 2 / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Chem-96G / 2,6-di-O-phosphono-beta-D-fructofuranose / Fructose-1,6-bisphosphatase isozyme 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.4 Å
Model detailsFor D3R project
AuthorsRuf, A. / Joseph, C. / Alker, A. / Banner, D. / Tetaz, T. / Benz, J. / Kuhn, B. / Rudolph, M.G. / Yang, H. / Shao, C. / Burley, S.K.
CitationJournal: To be published
Title: Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosphate 1-phosphatase, E.C.3.1.3.11) complexed with the allosteric inhibitor 1-(5-bromo-1,3-thiazol-2-yl)-3-[5-(4-methoxyphenyl) ...Title: Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosphate 1-phosphatase, E.C.3.1.3.11) complexed with the allosteric inhibitor 1-(5-bromo-1,3-thiazol-2-yl)-3-[5-(4-methoxyphenyl)thiophen-2-yl]sulfonylurea and with f2,6p
Authors: Ruf, A. / Joseph, C. / Alker, A. / Banner, D. / Tetaz, T. / Benz, J. / Kuhn, B. / Rudolph, M.G.
History
DepositionApr 18, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 9, 2019Provider: repository / Type: Initial release
Revision 1.1Jan 16, 2019Group: Data collection / Category: diffrn_radiation / Item: _diffrn_radiation.pdbx_diffrn_protocol
Revision 1.2Feb 6, 2019Group: Data collection / Database references / Structure summary
Category: audit_author / citation_author / Item: _audit_author.name / _citation_author.name
Revision 1.3Jul 29, 2020Group: Data collection / Derived calculations / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / struct_site / struct_site_gen
Item: _chem_comp.mon_nstd_flag / _chem_comp.name ..._chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.4Feb 10, 2021Group: Structure summary / Category: audit_author / chem_comp
Item: _audit_author.identifier_ORCID / _chem_comp.pdbx_synonyms
Revision 1.5Mar 6, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Fructose-1,6-bisphosphatase isozyme 2
B: Fructose-1,6-bisphosphatase isozyme 2
C: Fructose-1,6-bisphosphatase isozyme 2
D: Fructose-1,6-bisphosphatase isozyme 2
E: Fructose-1,6-bisphosphatase isozyme 2
F: Fructose-1,6-bisphosphatase isozyme 2
G: Fructose-1,6-bisphosphatase isozyme 2
H: Fructose-1,6-bisphosphatase isozyme 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)300,90124
Polymers294,3858
Non-polymers6,51616
Water9,818545
1
A: Fructose-1,6-bisphosphatase isozyme 2
B: Fructose-1,6-bisphosphatase isozyme 2
C: Fructose-1,6-bisphosphatase isozyme 2
D: Fructose-1,6-bisphosphatase isozyme 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)150,45012
Polymers147,1924
Non-polymers3,2588
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area19130 Å2
ΔGint-89 kcal/mol
Surface area43720 Å2
MethodPISA
2
E: Fructose-1,6-bisphosphatase isozyme 2
F: Fructose-1,6-bisphosphatase isozyme 2
G: Fructose-1,6-bisphosphatase isozyme 2
H: Fructose-1,6-bisphosphatase isozyme 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)150,45012
Polymers147,1924
Non-polymers3,2588
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area19080 Å2
ΔGint-90 kcal/mol
Surface area43730 Å2
MethodPISA
Unit cell
Length a, b, c (Å)222.475, 240.518, 138.979
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number20
Space group name H-MC2221
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 9 through 66 or resid 73 through 336))
21(chain B and (resid 9 through 66 or resid 73 through 336))
31(chain C and (resid 9 through 66 or resid 73 through 336))
41chain D
51(chain E and (resid 9 through 66 or resid 73 through 336))
61(chain F and (resid 9 through 66 or resid 73 through 336))
71(chain G and (resid 9 through 66 or resid 73 through 336))
81(chain H and (resid 9 through 66 or resid 73 through 336))

NCS domain segments:

Ens-ID: 1

Dom-IDComponent-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11THRTHRVALVAL(chain A and (resid 9 through 66 or resid 73 through 336))AA9 - 669 - 66
12LYSLYSGLNGLN(chain A and (resid 9 through 66 or resid 73 through 336))AA73 - 33673 - 336
21THRTHRVALVAL(chain B and (resid 9 through 66 or resid 73 through 336))BB9 - 669 - 66
22LYSLYSGLNGLN(chain B and (resid 9 through 66 or resid 73 through 336))BB73 - 33673 - 336
31THRTHRVALVAL(chain C and (resid 9 through 66 or resid 73 through 336))CC9 - 669 - 66
32LYSLYSGLNGLN(chain C and (resid 9 through 66 or resid 73 through 336))CC73 - 33673 - 336
41THRTHRGLNGLNchain DDD9 - 3369 - 336
51THRTHRVALVAL(chain E and (resid 9 through 66 or resid 73 through 336))EE9 - 669 - 66
52LYSLYSGLNGLN(chain E and (resid 9 through 66 or resid 73 through 336))EE73 - 33673 - 336
61THRTHRVALVAL(chain F and (resid 9 through 66 or resid 73 through 336))FF9 - 669 - 66
62LYSLYSGLNGLN(chain F and (resid 9 through 66 or resid 73 through 336))FF73 - 33673 - 336
71THRTHRVALVAL(chain G and (resid 9 through 66 or resid 73 through 336))GG9 - 669 - 66
72LYSLYSGLNGLN(chain G and (resid 9 through 66 or resid 73 through 336))GG73 - 33673 - 336
81THRTHRVALVAL(chain H and (resid 9 through 66 or resid 73 through 336))HH9 - 669 - 66
82LYSLYSGLNGLN(chain H and (resid 9 through 66 or resid 73 through 336))HH73 - 33673 - 336

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Components

#1: Protein
Fructose-1,6-bisphosphatase isozyme 2 / FBPase 2 / D-fructose-1 / 6-bisphosphate 1-phosphohydrolase 2 / Muscle FBPase


Mass: 36798.094 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: FBP2 / Production host: Escherichia coli (E. coli) / References: UniProt: O00757, fructose-bisphosphatase
#2: Chemical
ChemComp-96G / N-[(5-bromo-1,3-thiazol-2-yl)carbamoyl]-5-(4-methoxyphenyl)thiophene-2-sulfonamide


Mass: 474.372 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C15H12BrN3O4S3
#3: Sugar
ChemComp-FDP / 2,6-di-O-phosphono-beta-D-fructofuranose / FRUCTOSE-2,6-DIPHOSPHATE / 2,6-di-O-phosphono-beta-D-fructose / 2,6-di-O-phosphono-D-fructose / 2,6-di-O-phosphono-fructose / Fructose 2,6-bisphosphate


Type: D-saccharide, beta linking / Mass: 340.116 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C6H14O12P2
IdentifierTypeProgram
b-D-Fruf2PO36PO3IUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 545 / 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: 3.26 Å3/Da / Density % sol: 62.3 %
Crystal growMethod: vapor diffusion, sitting drop
Details: entry deposited much later from experimental date, thus exact crystallization details not known

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.987 Å
DetectorType: MAR CCD 165 mm / Detector: CCD / Date: Jun 12, 2006
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.987 Å / Relative weight: 1
ReflectionResolution: 2.4→29.793 Å / Num. obs: 141184 / % possible obs: 97.51 %

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
PHENIX1.11.1_2575refinement
PDB_EXTRACT3.23data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.4→29.793 Å / SU ML: 0.28 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 23.83 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2103 6943 4.92 %
Rwork0.1682 134241 -
obs0.1703 141184 97.51 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 185.73 Å2 / Biso mean: 57.1469 Å2 / Biso min: 17.1 Å2
Refinement stepCycle: final / Resolution: 2.4→29.793 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms19932 0 368 545 20845
Biso mean--66.91 48.99 -
Num. residues----2618
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00820627
X-RAY DIFFRACTIONf_angle_d0.9627954
X-RAY DIFFRACTIONf_chiral_restr0.0573225
X-RAY DIFFRACTIONf_plane_restr0.0063519
X-RAY DIFFRACTIONf_dihedral_angle_d11.22312388
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A12348X-RAY DIFFRACTION5.692TORSIONAL
12B12348X-RAY DIFFRACTION5.692TORSIONAL
13C12348X-RAY DIFFRACTION5.692TORSIONAL
14D12348X-RAY DIFFRACTION5.692TORSIONAL
15E12348X-RAY DIFFRACTION5.692TORSIONAL
16F12348X-RAY DIFFRACTION5.692TORSIONAL
17G12348X-RAY DIFFRACTION5.692TORSIONAL
18H12348X-RAY DIFFRACTION5.692TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.4-2.42730.30071860.25283598378479
2.4273-2.45580.31472010.2383776397783
2.4558-2.48570.27712010.23263918411986
2.4857-2.51720.30142280.22754136436491
2.5172-2.55030.30692060.2294326453295
2.5503-2.58520.2742040.21664558476299
2.5852-2.62210.26142470.20584535478299
2.6221-2.66120.2722430.21184471471499
2.6612-2.70280.25872490.20844522477199
2.7028-2.74710.26962120.203345624774100
2.7471-2.79440.29122400.196145434783100
2.7944-2.84520.23212590.192845184777100
2.8452-2.89990.26762530.202245514804100
2.8999-2.9590.27092300.212845724802100
2.959-3.02330.26012320.218845884820100
3.0233-3.09360.25932270.206845644791100
3.0936-3.17080.30112190.208745854804100
3.1708-3.25650.2352320.204345614793100
3.2565-3.35220.25952200.205245764796100
3.3522-3.46020.23812340.204345724806100
3.4602-3.58370.23752230.187746224845100
3.5837-3.72690.21312300.164145694799100
3.7269-3.89620.19782470.154646004847100
3.8962-4.10110.18112510.143845794830100
4.1011-4.35730.17122330.129346044837100
4.3573-4.69260.14732240.11646414865100
4.6926-5.16260.14942370.11646334870100
5.1626-5.90460.16062550.130346294884100
5.9046-7.42010.19372480.154947014949100
7.4201-29.79490.16432720.14434631490396
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)
10.17630.0571-0.14840.029-0.05750.08070.1527-0.20640.06960.0768-0.168-0.01810.02940.0412-00.3562-0.01760.01140.3753-0.09590.375553.94685.5753-23.6298
20.0153-0.0003-0.01860.0223-0.03580.05960.0483-0.3837-0.0872-0.1044-0.0363-0.23330.09920.0217-00.3736-0.0282-0.04380.5065-0.06620.315147.4792.3112-10.4508
30.5645-0.2037-0.2250.1693-0.01240.42850.0643-0.11690.0964-0.03380.00350.0478-0.0677-0.03310.00180.23190.00620.01190.2675-0.0770.194731.36049.8582-23.7315
40.1994-0.03060.13270.01930.01810.02340.10550.1454-0.0073-0.1336-0.0576-0.0774-0.07320.059900.32030.00950.00430.3364-0.10410.337853.5315-7.7661-45.7173
5-0.00180.00530.020.00880.02130.0407-0.07150.2336-0.0291-0.1609-0.0097-0.2075-0.12010.109400.4160.0380.00480.4177-0.10010.294847.3425-4.149-58.9784
60.1903-0.00470.04920.22630.12220.36850.04280.1131-0.0993-0.0293-0.04060.10590.035-0.1037-00.3342-0.0087-0.05630.3569-0.09260.340830.6861-10.5385-45.7219
70.20920.1416-0.10480.0806-0.04740.03760.0745-0.0310.1622-0.016-0.03620.0566-0.01120.0954-00.3285-0.0051-0.01030.371-0.12630.386965.218410.2867-29.514
80.0044-0.00490.02850.0438-0.02680.04660.08040.17030.5533-0.0937-0.0881-0.0968-0.1538-0.10230.00010.41110.02120.0230.4396-0.03060.62572.113722.7072-34.5162
90.38370.0417-0.03250.1789-0.07220.33550.1006-0.04380.1280.082-0.1188-0.1183-0.0103-0.0025-00.3116-0.0263-0.05240.3031-0.03050.375387.92759.7744-25.8999
100.05090.0093-0.00320.0226-0.00110.00370.09520.1315-0.22010.0038-0.08550.00990.09470.0766-00.33320.0217-0.0340.4065-0.11010.345664.2748-16.6111-49.0986
110.05380.011-0.01440.0676-0.08390.0888-0.0001-0.0262-0.24350.1287-0.1620.08740.0922-0.14180.00010.3734-0.0320.00350.312-0.02050.404568.1892-21.5489-31.3993
120.21290.07540.09570.35430.27450.3384-0.00080.0532-0.12950.0762-0.0136-0.13510.07310.034400.29030.0497-0.01640.3052-0.04180.366787.0389-14.5522-43.2537
130.1633-0.0936-0.1520.4937-0.02050.1132-0.1222-0.18060.24540.02690.10460.8178-0.3018-0.0565-0.05730.3434-0.0414-0.23790.36740.14470.718394.667853.5036-1.9141
140.5262-0.0059-0.43290.55890.3060.6128-0.4902-0.0751-0.0569-0.14910.30930.72870.33050.2053-0.21930.3469-0.2601-0.33240.22940.05960.41499.745833.9017-8.4156
150.0484-0.09570.02130.23090.03050.0301-0.10910.03550.1687-0.12080.0562-0.2369-0.0625-0.045200.4631-0.0255-0.12140.380.00990.3997124.762856.87412.9868
160.0308-0.0298-0.01930.01480.01690.0377-0.10190.0830.038-0.28630.0655-0.4062-0.27820.098300.4712-0.04320.00660.44130.05560.4987136.829250.9761-3.6256
170.2742-0.0941-0.00730.3725-0.00430.1462-0.09120.0124-0.0314-0.02370.0304-0.12040.0768-0.001500.38630.0178-0.04880.32560.03560.3305125.981634.18825.9424
180.118-0.0047-0.06610.37710.25680.2959-0.1017-0.0052-0.0471-0.58050.18350.09450.13720.11160.16970.5117-0.0619-0.2810.36090.1010.4685104.703467.8393-11.0772
190.1086-0.06890.0710.0375-0.04790.0410.05470.1727-0.254-0.7995-0.02350.30280.0288-0.18010.07781.0568-0.0505-0.60680.4660.09390.1953106.858174.3508-24.37
200.2012-0.22630.09260.493-0.29320.41780.0099-0.109-0.008-0.27950.1340.465-0.0292-0.05790.4520.40080.0019-0.22470.37740.11940.4199100.862490.5397-10.3169
210.0334-0.01030.03940.23380.02130.0287-0.0442-0.0809-0.05540.10110.14870.07430.16820.04760.00010.33530.0104-0.11150.34710.02870.3828120.031567.78659.6452
220.0082-0.0078-0.00680.02790.02280.0334-0.0642-0.1781-0.16610.36260.02260.02460.07640.037-00.51290.0187-0.09940.48210.04970.3267117.794273.644123.2512
230.1735-0.0810.13120.41140.07180.4121-0.0505-0.02280.04660.10020.0898-0.0975-0.04970.0192-00.3268-0.0041-0.08040.3715-0.00810.3061123.056690.54639.8381
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 9 through 69 )A9 - 69
2X-RAY DIFFRACTION2chain 'A' and (resid 70 through 119 )A70 - 119
3X-RAY DIFFRACTION3chain 'A' and (resid 120 through 336 )A120 - 336
4X-RAY DIFFRACTION4chain 'B' and (resid 9 through 69 )B9 - 69
5X-RAY DIFFRACTION5chain 'B' and (resid 70 through 119 )B70 - 119
6X-RAY DIFFRACTION6chain 'B' and (resid 120 through 336 )B120 - 336
7X-RAY DIFFRACTION7chain 'C' and (resid 9 through 69 )C9 - 69
8X-RAY DIFFRACTION8chain 'C' and (resid 70 through 119 )C70 - 119
9X-RAY DIFFRACTION9chain 'C' and (resid 120 through 336 )C120 - 336
10X-RAY DIFFRACTION10chain 'D' and (resid 9 through 49 )D9 - 49
11X-RAY DIFFRACTION11chain 'D' and (resid 50 through 119 )D50 - 119
12X-RAY DIFFRACTION12chain 'D' and (resid 120 through 336 )D120 - 336
13X-RAY DIFFRACTION13chain 'E' and (resid 9 through 119 )E9 - 119
14X-RAY DIFFRACTION14chain 'E' and (resid 120 through 336 )E120 - 336
15X-RAY DIFFRACTION15chain 'F' and (resid 9 through 69 )F9 - 69
16X-RAY DIFFRACTION16chain 'F' and (resid 70 through 119 )F70 - 119
17X-RAY DIFFRACTION17chain 'F' and (resid 120 through 336 )F120 - 336
18X-RAY DIFFRACTION18chain 'G' and (resid 9 through 69 )G9 - 69
19X-RAY DIFFRACTION19chain 'G' and (resid 70 through 119 )G70 - 119
20X-RAY DIFFRACTION20chain 'G' and (resid 120 through 336 )G120 - 336
21X-RAY DIFFRACTION21chain 'H' and (resid 9 through 69 )H9 - 69
22X-RAY DIFFRACTION22chain 'H' and (resid 70 through 119 )H70 - 119
23X-RAY DIFFRACTION23chain 'H' and (resid 120 through 336 )H120 - 336

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