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- PDB-5k8f: Crystal structure of Acetyl-CoA Synthetase in complex with ATP an... -

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Basic information

Entry
Database: PDB / ID: 5k8f
TitleCrystal structure of Acetyl-CoA Synthetase in complex with ATP and Acetyl-AMP from Cryptococcus neoformans H99
ComponentsAcetyl-coenzyme A synthetase
KeywordsLIGASE / SSGCID / NIH / NIAID / Synthetase / ACS1 / Acetyl-AMP / ATP / Adenosine TriPhosphate / Acetyl Adenylate / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease
Function / homology
Function and homology information


acetate-CoA ligase / acetate-CoA ligase activity / acetyl-CoA biosynthetic process from acetate / AMP binding / ATP binding / metal ion binding
Similarity search - Function
Acetate-CoA ligase / Acetyl-coenzyme A synthetase, N-terminal domain / Acetyl-coenzyme A synthetase N-terminus / ANL, C-terminal domain / ANL, N-terminal domain / ANL, N-terminal domain / AMP-binding enzyme, C-terminal domain / AMP-binding enzyme C-terminal domain / AMP-binding, conserved site / Putative AMP-binding domain signature. ...Acetate-CoA ligase / Acetyl-coenzyme A synthetase, N-terminal domain / Acetyl-coenzyme A synthetase N-terminus / ANL, C-terminal domain / ANL, N-terminal domain / ANL, N-terminal domain / AMP-binding enzyme, C-terminal domain / AMP-binding enzyme C-terminal domain / AMP-binding, conserved site / Putative AMP-binding domain signature. / GMP Synthetase; Chain A, domain 3 / AMP-dependent synthetase/ligase / AMP-binding enzyme / AMP-binding enzyme, C-terminal domain superfamily / Rossmann fold / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Chem-6R9 / ADENOSINE-5'-TRIPHOSPHATE / PHOSPHATE ION / Acetyl-coenzyme A synthetase
Similarity search - Component
Biological speciesCryptococcus neoformans var. grubii serotype A (fungus)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.45 Å
AuthorsSeattle Structural Genomics Center for Infectious Disease (SSGCID) / Fox III, D. / Delker, S.L. / Potts, K.T. / Lorimer, D.D. / Edwards, T.E. / Mutz, M.W.
CitationJournal: To Be Published
Title: Crystal structure of Acetyl-CoA Synthetase in complex with ATP and Acetyl-AMP from Cryptococcus neoformans H99
Authors: Seattle Structural Genomics Center for Infectious Disease (SSGCID) / Fox III, D. / Delker, S.L. / Potts, K.T. / Numa, M.M. / Edwards, T.E. / Lorimer, D.D. / Mutz, M.W. / Krysan, D.J.
History
DepositionMay 30, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 13, 2016Provider: repository / Type: Initial release
Revision 2.0Apr 28, 2021Group: Advisory / Atomic model ...Advisory / Atomic model / Author supporting evidence / Data collection / Database references / Derived calculations / Refinement description / Source and taxonomy / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / audit_author / citation_author / diffrn / entity / entity_src_gen / pdbx_entity_instance_feature / pdbx_entity_nonpoly / pdbx_entry_details / pdbx_nonpoly_scheme / pdbx_prerelease_seq / pdbx_refine_tls / pdbx_refine_tls_group / pdbx_struct_assembly / pdbx_struct_assembly_gen / pdbx_struct_conn_angle / pdbx_struct_oper_list / pdbx_struct_sheet_hbond / pdbx_unobs_or_zero_occ_atoms / pdbx_validate_close_contact / pdbx_validate_peptide_omega / pdbx_validate_torsion / refine / refine_hist / refine_ls_restr / refine_ls_shell / reflns / reflns_shell / software / struct_asym / struct_conf / struct_conn / struct_mon_prot_cis / struct_ref_seq_dif / struct_sheet_range / struct_site / struct_site_gen
Item: _diffrn.pdbx_serial_crystal_experiment / _entity.formula_weight ..._diffrn.pdbx_serial_crystal_experiment / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity_src_gen.gene_src_common_name / _entity_src_gen.pdbx_host_org_scientific_name / _entity_src_gen.pdbx_host_org_strain / _pdbx_entity_nonpoly.comp_id / _pdbx_entity_nonpoly.name / _pdbx_refine_tls.L[1][1] / _pdbx_refine_tls.L[1][2] / _pdbx_refine_tls.L[1][3] / _pdbx_refine_tls.L[2][2] / _pdbx_refine_tls.L[2][3] / _pdbx_refine_tls.L[3][3] / _pdbx_refine_tls.S[1][1] / _pdbx_refine_tls.S[1][2] / _pdbx_refine_tls.S[1][3] / _pdbx_refine_tls.S[2][1] / _pdbx_refine_tls.S[2][2] / _pdbx_refine_tls.S[2][3] / _pdbx_refine_tls.S[3][1] / _pdbx_refine_tls.S[3][2] / _pdbx_refine_tls.S[3][3] / _pdbx_refine_tls.T[1][1] / _pdbx_refine_tls.T[1][2] / _pdbx_refine_tls.T[1][3] / _pdbx_refine_tls.T[2][2] / _pdbx_refine_tls.T[2][3] / _pdbx_refine_tls.T[3][3] / _pdbx_refine_tls.origin_x / _pdbx_refine_tls.origin_y / _pdbx_refine_tls.origin_z / _pdbx_struct_assembly.details / _pdbx_struct_assembly.method_details / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_oper_list.symmetry_operation / _pdbx_struct_sheet_hbond.range_1_auth_comp_id / _pdbx_struct_sheet_hbond.range_1_auth_seq_id / _pdbx_struct_sheet_hbond.range_1_label_comp_id / _pdbx_struct_sheet_hbond.range_1_label_seq_id / _pdbx_struct_sheet_hbond.range_2_auth_comp_id / _pdbx_struct_sheet_hbond.range_2_auth_seq_id / _pdbx_struct_sheet_hbond.range_2_label_comp_id / _pdbx_struct_sheet_hbond.range_2_label_seq_id / _refine.B_iso_max / _refine.B_iso_mean / _refine.B_iso_min / _refine.ls_R_factor_R_free / _refine.ls_R_factor_R_work / _refine.ls_R_factor_obs / _refine.ls_number_reflns_R_work / _refine.ls_number_reflns_obs / _refine.ls_percent_reflns_obs / _refine.pdbx_ls_sigma_F / _refine.pdbx_overall_phase_error / _refine.pdbx_stereochemistry_target_values / _refine.solvent_model_details / _refine_hist.cycle_id / _refine_hist.number_atoms_solvent / _refine_hist.number_atoms_total / _refine_hist.pdbx_B_iso_mean_ligand / _refine_hist.pdbx_B_iso_mean_solvent / _refine_hist.pdbx_number_atoms_ligand / _refine_hist.pdbx_number_atoms_protein / _refine_hist.pdbx_number_residues_total / _refine_ls_restr.dev_ideal / _refine_ls_restr.number / _reflns.B_iso_Wilson_estimate / _reflns.pdbx_CC_half / _reflns.pdbx_Rrim_I_all / _reflns.pdbx_chi_squared / _reflns.pdbx_redundancy / _struct_conf.beg_auth_asym_id / _struct_conf.beg_auth_comp_id / _struct_conf.beg_auth_seq_id / _struct_conf.beg_label_asym_id / _struct_conf.beg_label_comp_id / _struct_conf.beg_label_seq_id / _struct_conf.end_auth_asym_id / _struct_conf.end_auth_comp_id / _struct_conf.end_auth_seq_id / _struct_conf.end_label_asym_id / _struct_conf.end_label_comp_id / _struct_conf.end_label_seq_id / _struct_conf.pdbx_PDB_helix_class / _struct_conf.pdbx_PDB_helix_length / _struct_mon_prot_cis.pdbx_omega_angle / _struct_ref_seq_dif.details / _struct_sheet_range.beg_auth_comp_id / _struct_sheet_range.beg_auth_seq_id / _struct_sheet_range.beg_label_comp_id / _struct_sheet_range.beg_label_seq_id / _struct_sheet_range.end_auth_comp_id / _struct_sheet_range.end_auth_seq_id / _struct_sheet_range.end_label_comp_id / _struct_sheet_range.end_label_seq_id
Description: Ligand identity
Details: Removed low occupancy Mg atom and alt loop conformation near ATP.
Provider: author / Type: Coordinate replacement
Revision 2.1Sep 27, 2023Group: 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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Acetyl-coenzyme A synthetase
B: Acetyl-coenzyme A synthetase
C: Acetyl-coenzyme A synthetase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)235,86723
Polymers232,4273
Non-polymers3,44020
Water6,684371
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A: Acetyl-coenzyme A synthetase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)78,6458
Polymers77,4761
Non-polymers1,1697
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
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B: Acetyl-coenzyme A synthetase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)78,5837
Polymers77,4761
Non-polymers1,1076
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: Acetyl-coenzyme A synthetase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)78,6408
Polymers77,4761
Non-polymers1,1647
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)71.370, 83.920, 101.570
Angle α, β, γ (deg.)110.060, 105.240, 87.650
Int Tables number1
Space group name H-MP1

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Components

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Protein , 1 types, 3 molecules ABC

#1: Protein Acetyl-coenzyme A synthetase


Mass: 77475.750 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (fungus)
Strain: H99 / ATCC 208821 / CBS 10515 / FGSC 9487 / Gene: CNAG_00797 / Plasmid: PEMB7013 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: J9VFT1, acetate-CoA ligase

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Non-polymers , 6 types, 391 molecules

#2: Chemical ChemComp-ATP / ADENOSINE-5'-TRIPHOSPHATE


Mass: 507.181 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C10H16N5O13P3 / Feature type: SUBJECT OF INVESTIGATION / Comment: ATP, energy-carrying molecule*YM
#3: Chemical ChemComp-6R9 / [[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] ethanoate


Mass: 389.258 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C12H16N5O8P / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg
#5: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: C2H6O2
#6: Chemical ChemComp-PO4 / PHOSPHATE ION


Mass: 94.971 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: PO4
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 371 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY

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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: 2.37 Å3/Da / Density % sol: 48.07 %
Crystal growTemperature: 289 K / Method: vapor diffusion, sitting drop / pH: 6.2
Details: ACETYL COA SYNTHETASE FROM CRYPTOCOCCUS NEOFORMANS (CRNEC.00629.A.FS11.PD00402) AT 10MG/ ML (IN 10 MM TRIS, PH = 7.5, 20 MM NACL) WAS SET UP IN SPARSE CRYSTALLIZATION TRIALS AT 16C. 1MM ATP ...Details: ACETYL COA SYNTHETASE FROM CRYPTOCOCCUS NEOFORMANS (CRNEC.00629.A.FS11.PD00402) AT 10MG/ ML (IN 10 MM TRIS, PH = 7.5, 20 MM NACL) WAS SET UP IN SPARSE CRYSTALLIZATION TRIALS AT 16C. 1MM ATP AND 1MM MGCL2 WERE ADDED TO THE PROTEIN SOLUTION AND INCUBATED FOR 5 MINUTES BEFORE SETTING UP TRIALS. CRYSTALS WERE PRODUCED BY SITTING DROP VAPOR DIFFUSION WITH AN EQUAL VOLUME COMBINATION OF THE PROTEIN/LIGAND IN WIZARD 1 AND 2 SCREEN CONDITION E8 (10% W/V PEG8,000, 0.1M NA/K PHOSPHATE PH6.2) AND CRYO-PROTECTED IN 20% ETHYLENE GLYCOL. CRYSTAL ID 271854A7 GJX4-8 APS21-ID-G), PH 6.20, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
PH range: 6.2

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-G / Wavelength: 0.97856 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Apr 22, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97856 Å / Relative weight: 1
ReflectionResolution: 2.45→50 Å / Num. obs: 77299 / % possible obs: 98.5 % / Observed criterion σ(I): -3 / Redundancy: 4 % / Biso Wilson estimate: 37.68 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.076 / Rrim(I) all: 0.088 / Χ2: 0.975 / Net I/σ(I): 14.19
Reflection shell

Diffraction-ID: 1

Resolution (Å)Rmerge(I) obsMean I/σ(I) obsNum. unique obsCC1/2Rrim(I) all% possible all
2.45-2.510.5172.5656460.8610.59797.8
2.51-2.580.4512.9755240.8820.52197.7
2.58-2.660.3783.554010.9170.43798.2
2.66-2.740.3174.2552760.940.36698.1
2.74-2.830.265.1150860.9560.398.3
2.83-2.930.2036.4748880.9710.23598.2
2.93-3.040.1717.7347840.9770.19798.3
3.04-3.160.12510.1145970.9870.14498.6
3.16-3.30.09413.2143850.9920.10998.5
3.3-3.460.07516.3742420.9950.08798.8
3.46-3.650.06219.239690.9960.07298.6
3.65-3.870.05521.4738230.9970.06498.9
3.87-4.140.04624.9135740.9970.05399
4.14-4.470.0428.4433380.9980.04798.9
4.47-4.90.03730.5530530.9980.04299.2
4.9-5.480.03730.8327620.9980.04399
5.48-6.330.03830.0924540.9980.04499.4
6.33-7.750.03432.8120650.9980.0499
7.75-10.960.02739.1215770.9990.03198.9
10.96-500.02637.368550.9990.03196.5

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Processing

Software
NameVersionClassification
PHENIX1.19rc4_4035refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5IFI

5ifi


Resolution: 2.45→26.62 Å / SU ML: 0.27 / Cross valid method: FREE R-VALUE / σ(F): 1.98 / Phase error: 24.84 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2242 1997 2.59 %
Rwork0.1879 75209 -
obs0.1889 77206 98.59 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 130.47 Å2 / Biso mean: 52.7124 Å2 / Biso min: 20.5 Å2
Refinement stepCycle: final / Resolution: 2.45→26.62 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms14907 0 216 377 15500
Biso mean--49.38 39.02 -
Num. residues----1962
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00215682
X-RAY DIFFRACTIONf_angle_d0.46721462
X-RAY DIFFRACTIONf_dihedral_angle_d12.7025484
X-RAY DIFFRACTIONf_chiral_restr0.0422329
X-RAY DIFFRACTIONf_plane_restr0.0042766
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 14

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.45-2.510.27811400.26025301544198
2.51-2.580.26461420.24795315545798
2.58-2.650.30861420.23995355549798
2.65-2.740.29091430.24455374551798
2.74-2.840.27841420.23595355549798
2.84-2.950.26481420.22615342548498
2.95-3.090.25921440.22215418556299
3.09-3.250.24321430.21785372551599
3.25-3.450.2271420.20175371551399
3.45-3.720.22361440.18245408555299
3.72-4.090.20481430.16735377552099
4.09-4.680.19871450.14595439558499
4.68-5.880.18491430.15215403554699
5.89-26.620.18371420.16115379552199
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)
12.0538-0.4756-0.88011.0730.18591.7920.08370.06980.139-0.1861-0.08260.011-0.1952-0.1454-0.00580.2097-0.0037-0.04710.1728-0.02030.2236-9.424112.3094-2.3171
22.6637-0.6995-1.38110.7992-0.29132.93360.1147-0.07930.1177-0.1123-0.1536-0.1195-0.25850.14520.03610.2076-0.0141-0.02530.1472-0.01380.2572-0.559212.1362-4.8149
32.1924-0.5648-0.76951.19640.45861.83730.11160.21340.2086-0.1634-0.08660.1569-0.3071-0.4792-0.02960.21680.0604-0.03950.30370.00420.3283-19.748420.88611.9543
43.1221-0.4888-0.22517.0624-1.63482.66810.24660.10280.8893-0.0938-0.266-0.8349-0.8308-0.12970.03330.60120.1901-0.0050.462-0.05310.7257-19.715141.89418.6471
50.9516-0.16070.361.2036-0.33021.5146-0.2418-0.6045-0.53140.34860.20090.18210.5324-0.1401-0.1120.54160.11430.15680.60690.28440.53527.6847-20.615629.356
61.52770.2020.22611.4021-0.061.2183-0.2219-0.47920.05820.22080.2266-0.12230.02980.2752-0.00050.22850.0815-0.04120.4698-0.01440.257317.96855.034522.198
70.02750.36090.09496.0786-0.69244.8247-0.1243-0.6391-0.45330.24330.2785-0.46490.41590.3542-0.26430.36270.16060.04710.50320.13830.373917.4983-14.695522.3884
80.94150.23220.16981.3622-0.59631.2426-0.2296-0.7271-0.34360.6030.2346-0.06580.2672-0.1229-0.01190.65190.24960.0640.84290.2710.448816.504-17.27440.0888
91.0626-0.46790.59182.264-0.73922.24580.1271-0.4807-0.39110.1423-0.0033-0.09240.64320.4251-0.15170.61180.21780.06750.5720.22260.598327.8289-27.148725.9459
102.89611.49870.98581.28662.00416.4632-0.6886-0.3808-0.03570.45670.5518-0.3407-0.56880.12320.07720.92510.3039-0.11720.98490.13540.57840.447-18.720646.0254
110.6742-0.1046-0.78321.00320.24510.9287-0.44190.4061-0.6536-0.2308-0.17250.01560.8353-0.38650.20961.1092-0.36370.32220.6214-0.35530.93860.4643-35.4285-30.7547
121.3302-0.2387-0.08650.72-0.0641.8551-0.1503-0.0183-0.2935-0.0722-0.04-0.15130.48540.30.14820.41960.07640.11360.22290.04110.407220.5449-15.964-8.6875
130.97790.06420.09990.89610.1181.1316-0.34010.3716-0.6463-0.1311-0.01410.02620.91990.10580.140.85060.0260.2660.2743-0.09620.615615.8214-29.3228-23.9256
141.8007-0.462-0.42484.670.50252.2848-0.0120.5516-0.2099-0.5175-0.31760.52930.2999-0.58780.2520.4191-0.02410.0220.414-0.11990.31011.6291-11.7892-31.2927
155.1275-0.23453.04363.24830.73292.84990.05650.64480.0333-0.8419-0.5153-0.00450.3414-0.2250.48420.8557-0.03860.18870.5108-0.17830.496312.379-21.8216-44.8553
166.33360.13010.80213.53570.75816.7650.03440.6167-0.4478-0.07670.1576-0.2341-0.3020.7386-0.17380.7889-0.0170.20410.6329-0.10190.471725.8537-20.7034-48.4122
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 11 through 245 )A11 - 245
2X-RAY DIFFRACTION2chain 'A' and (resid 246 through 317 )A246 - 317
3X-RAY DIFFRACTION3chain 'A' and (resid 318 through 526 )A318 - 526
4X-RAY DIFFRACTION4chain 'A' and (resid 527 through 681 )A527 - 681
5X-RAY DIFFRACTION5chain 'B' and (resid 11 through 132 )B11 - 132
6X-RAY DIFFRACTION6chain 'B' and (resid 133 through 278 )B133 - 278
7X-RAY DIFFRACTION7chain 'B' and (resid 279 through 317 )B279 - 317
8X-RAY DIFFRACTION8chain 'B' and (resid 318 through 493 )B318 - 493
9X-RAY DIFFRACTION9chain 'B' and (resid 494 through 555 )B494 - 555
10X-RAY DIFFRACTION10chain 'B' and (resid 556 through 681 )B556 - 681
11X-RAY DIFFRACTION11chain 'C' and (resid 11 through 63 )C11 - 63
12X-RAY DIFFRACTION12chain 'C' and (resid 64 through 278 )C64 - 278
13X-RAY DIFFRACTION13chain 'C' and (resid 279 through 463 )C279 - 463
14X-RAY DIFFRACTION14chain 'C' and (resid 464 through 526 )C464 - 526
15X-RAY DIFFRACTION15chain 'C' and (resid 527 through 579 )C527 - 579
16X-RAY DIFFRACTION16chain 'C' and (resid 580 through 681 )C580 - 681

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