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- PDB-2yaw: HG INHIBITED SULFUR OXYGENASE REDUCTASE -

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Basic information

Entry
Database: PDB / ID: 2yaw
TitleHG INHIBITED SULFUR OXYGENASE REDUCTASE
ComponentsSULFUR OXYGENASE/REDUCTASE
KeywordsOXIDOREDUCTASE / MONONUCLEAR NON-HEME IRON / BIOGEOCHEMICAL SULFUR CYCLE / THERMOPHILIC / CYSTEINE PERSULPHIDE / ICOSATETRAMER
Function / homology
Function and homology information


sulfur oxygenase/reductase / sulfur oxygenase/reductase activity / metal ion binding / cytoplasm
Similarity search - Function
Sulphur oxygenase reductase / Sulphur oxygenase reductase / Dimeric alpha-beta barrel
Similarity search - Domain/homology
ACETATE ION / : / : / Sulfur oxygenase/reductase
Similarity search - Component
Biological speciesACIDIANUS AMBIVALENS (archaea)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.499 Å
AuthorsVeith, A. / Urich, T. / Seyfarth, K. / Protze, J. / Frazao, C. / Kletzin, A.
Citation
Journal: Front.Microbiol. / Year: 2011
Title: Substrate Pathways and Mechanisms of Inhibition in the Sulfur Oxygenase Reductase of Acidianus Ambivalens.
Authors: Veith, A. / Urich, T. / Seyfarth, K. / Protze, J. / Frazao, C. / Kletzin, A.
#1: Journal: Science / Year: 2006
Title: X-Ray Structure of a Self-Compartmentalizing Sulfur Cycle Metalloenzyme.
Authors: Urich, T. / Gomes, C.M. / Kletzin, A. / Frazao, C.
History
DepositionFeb 25, 2011Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 21, 2011Provider: repository / Type: Initial release
Revision 1.1May 8, 2019Group: Data collection / Derived calculations ...Data collection / Derived calculations / Experimental preparation / Other
Category: exptl_crystal_grow / pdbx_database_proc ...exptl_crystal_grow / pdbx_database_proc / pdbx_database_status / struct_conn
Item: _exptl_crystal_grow.method / _pdbx_database_status.recvd_author_approval / _struct_conn.pdbx_leaving_atom_flag
Revision 1.2Dec 20, 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_sheet / 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_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_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_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.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _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_conn.ptnr2_label_seq_id / _struct_sheet.number_strands / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.3Nov 20, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature
Remark 700 SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "CA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "DA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "EA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "FA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: SULFUR OXYGENASE/REDUCTASE
B: SULFUR OXYGENASE/REDUCTASE
C: SULFUR OXYGENASE/REDUCTASE
D: SULFUR OXYGENASE/REDUCTASE
E: SULFUR OXYGENASE/REDUCTASE
F: SULFUR OXYGENASE/REDUCTASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)221,57430
Polymers218,4786
Non-polymers3,09624
Water9,296516
1
A: SULFUR OXYGENASE/REDUCTASE
B: SULFUR OXYGENASE/REDUCTASE
C: SULFUR OXYGENASE/REDUCTASE
D: SULFUR OXYGENASE/REDUCTASE
E: SULFUR OXYGENASE/REDUCTASE
F: SULFUR OXYGENASE/REDUCTASE
hetero molecules

A: SULFUR OXYGENASE/REDUCTASE
B: SULFUR OXYGENASE/REDUCTASE
C: SULFUR OXYGENASE/REDUCTASE
D: SULFUR OXYGENASE/REDUCTASE
E: SULFUR OXYGENASE/REDUCTASE
F: SULFUR OXYGENASE/REDUCTASE
hetero molecules

A: SULFUR OXYGENASE/REDUCTASE
B: SULFUR OXYGENASE/REDUCTASE
C: SULFUR OXYGENASE/REDUCTASE
D: SULFUR OXYGENASE/REDUCTASE
E: SULFUR OXYGENASE/REDUCTASE
F: SULFUR OXYGENASE/REDUCTASE
hetero molecules

A: SULFUR OXYGENASE/REDUCTASE
B: SULFUR OXYGENASE/REDUCTASE
C: SULFUR OXYGENASE/REDUCTASE
D: SULFUR OXYGENASE/REDUCTASE
E: SULFUR OXYGENASE/REDUCTASE
F: SULFUR OXYGENASE/REDUCTASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)886,298120
Polymers873,91224
Non-polymers12,38696
Water43224
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation3_655-y+1,x,z1
crystal symmetry operation2_665-x+1,-y+1,z1
crystal symmetry operation4_565y,-x+1,z1
Buried area153110 Å2
ΔGint-2503.3 kcal/mol
Surface area207540 Å2
MethodPISA
Unit cell
Length a, b, c (Å)161.876, 161.876, 154.373
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number79
Space group name H-MI4
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
31
41
51
61

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111CHAIN A AND (RESSEQ 1:29 OR RESSEQ 31:307)
211CHAIN B AND (RESSEQ 1:29 OR RESSEQ 31:307)
311CHAIN C AND (RESSEQ 1:29 OR RESSEQ 31:307)
411CHAIN D AND (RESSEQ 1:29 OR RESSEQ 31:307)
511CHAIN E AND (RESSEQ 1:29 OR RESSEQ 31:307)
611CHAIN F AND (RESSEQ 1:29 OR RESSEQ 31:307)

NCS oper:
IDCodeMatrixVector
1given(-0.04062, -0.18103, 0.98264), (-0.18286, -0.96549, -0.18543), (0.9823, -0.18721, 0.00612)22.40683, 188.13092, 12.93282
2given(0.96656, -0.17884, 0.18377), (-0.18113, 0.03107, 0.98297), (-0.1815, -0.98339, -0.00236)2.7383, 17.0184, 172.17535
3given(0.03176, 0.18129, -0.98292), (0.1859, 0.96518, 0.18402), (0.98206, -0.18857, -0.00304)139.78061, -26.38772, 13.63341
4given(-0.18738, -0.96411, -0.18809), (0.03285, 0.18523, -0.98215), (0.98174, -0.19021, -0.00304)188.46288, 139.16936, 13.81386
5given(0.93034, -0.36663, 0.00651), (-0.36664, -0.93036, 0.00108), (0.00566, -0.00339, -0.99998)34.48994, 185.68706, 155.11234

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Components

#1: Protein
SULFUR OXYGENASE/REDUCTASE / SULFUR OXYGENASE REDUCTASE / SOR


Mass: 36413.004 Da / Num. of mol.: 6 / Fragment: RESIDUES 1-308
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) ACIDIANUS AMBIVALENS (archaea) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P29082, sulfur oxygenase/reductase
#2: Chemical
ChemComp-FE / FE (III) ION


Mass: 55.845 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Fe
#3: Chemical
ChemComp-HG / MERCURY (II) ION


Mass: 200.590 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: Hg
#4: Chemical
ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C2H3O2
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 516 / Source method: isolated from a natural source / Formula: H2O
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: 2.52 Å3/Da / Density % sol: 51.2 % / Description: NONE
Crystal growMethod: vapor diffusion, sitting drop / pH: 7.5
Details: VAPOR DIFFUSION OF SITTING DROPS OF 1 MICRO LITER OF 13 MG/ML SOR IN 50 MM TRIS/HCL MIXED WITH 1 MICRO LITER OF WELL SOLUTION 0.1 M SODIUM ACETATE WITH 8% MPD AND 50 MM SODIUM CHLORIDE, ...Details: VAPOR DIFFUSION OF SITTING DROPS OF 1 MICRO LITER OF 13 MG/ML SOR IN 50 MM TRIS/HCL MIXED WITH 1 MICRO LITER OF WELL SOLUTION 0.1 M SODIUM ACETATE WITH 8% MPD AND 50 MM SODIUM CHLORIDE, AGAINST 500 ML OF WELL SOLUTION., pH 7.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-3 / Wavelength: 0.934
DetectorType: ADSC QUANTUM 4r / Detector: CCD / Details: E.G. MIRRORS
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.934 Å / Relative weight: 1
ReflectionResolution: 2.5→49.04 Å / Num. obs: 68600 / % possible obs: 99.9 % / Observed criterion σ(I): 0 / Redundancy: 15 % / Biso Wilson estimate: 29.69 Å2 / Rmerge(I) obs: 0.08 / Net I/σ(I): 33.3
Reflection shellResolution: 2.5→2.53 Å / Rmerge(I) obs: 0.49 / Mean I/σ(I) obs: 5 / % possible all: 98.9

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
HKLdata reduction
SCALEPACKdata scaling
REFMACphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2CB2

2cb2


Resolution: 2.499→49.04 Å / SU ML: 0.3 / σ(F): 0 / Phase error: 15.63 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.1825 3245 4.9 %
Rwork0.1621 --
obs0.1669 68589 99.89 %
Solvent computationShrinkage radii: 0.83 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 24.503 Å2 / ksol: 0.373 e/Å3
Displacement parametersBiso mean: 29 Å2
Baniso -1Baniso -2Baniso -3
1-1.7814 Å20 Å20 Å2
2--1.7814 Å20 Å2
3----3.5628 Å2
Refinement stepCycle: LAST / Resolution: 2.499→49.04 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms14802 0 42 516 15360
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01715503
X-RAY DIFFRACTIONf_angle_d0.97420934
X-RAY DIFFRACTIONf_dihedral_angle_d14.5635794
X-RAY DIFFRACTIONf_chiral_restr0.1032197
X-RAY DIFFRACTIONf_plane_restr0.0032688
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A2472X-RAY DIFFRACTIONPOSITIONAL
12B2472X-RAY DIFFRACTIONPOSITIONAL0.036
13C2478X-RAY DIFFRACTIONPOSITIONAL0.047
14D2456X-RAY DIFFRACTIONPOSITIONAL0.039
15E2460X-RAY DIFFRACTIONPOSITIONAL0.037
16F2478X-RAY DIFFRACTIONPOSITIONAL0.04
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.4995-2.536800.19722677X-RAY DIFFRACTION90
2.5368-2.57640.25321740.2042573X-RAY DIFFRACTION93
2.5764-2.61870.23463550.18992422X-RAY DIFFRACTION93
2.6187-2.663800.18482810X-RAY DIFFRACTION94
2.6638-2.712300.18762780X-RAY DIFFRACTION95
2.7123-2.76440.2319660.18382809X-RAY DIFFRACTION95
2.7644-2.82080.22634400.16742432X-RAY DIFFRACTION96
2.8208-2.882200.16512845X-RAY DIFFRACTION97
2.8822-2.949200.1682910X-RAY DIFFRACTION97
2.9492-3.02290.20274700.1612409X-RAY DIFFRACTION97
3.0229-3.104700.17022939X-RAY DIFFRACTION98
3.1047-3.19600.16372934X-RAY DIFFRACTION98
3.196-3.299100.15832899X-RAY DIFFRACTION98
3.2991-3.4170.18584900.16032468X-RAY DIFFRACTION99
3.417-3.553800.16352939X-RAY DIFFRACTION99
3.5538-3.715500.16732945X-RAY DIFFRACTION98
3.7155-3.91130.17214100.1462509X-RAY DIFFRACTION99
3.9113-4.156200.13432997X-RAY DIFFRACTION99
4.1562-4.47690.1383830.12682587X-RAY DIFFRACTION100
4.4769-4.927100.11773015X-RAY DIFFRACTION100
4.9271-5.639200.15252972X-RAY DIFFRACTION100
5.6392-7.10130.20072970.19382720X-RAY DIFFRACTION100
7.1013-49.0490.15291600.20752881X-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)
10.0727-0.0022-0.11850.0292-0.01480.0642-0.02930.0360.01230.01210.147-0.07530.00380.002-00.15880.0241-0.03020.120.0070.138955.061178.01537.1529
2-0.0020.02410.02750.00820.00420.03050.0231-0.08930.04830.01-0.15450.15380.03150.0599-0.01310.092-0.04050.01430.16690.01790.174445.13768.516331.5475
30.1151-0.0809-0.10980.05790.10670.2752-0.0234-0.00840.002-0.02410.02240.03240.001-0.0136-00.04620.0064-0.02250.05160.01270.045252.247282.485126.6661
40.0420.0188-0.02620.0310.01650.017-0.04320.06560.0037-0.01950.0965-0.0749-0.0009-0.02470.0010.0867-0.0010.01320.06470.02760.058255.737589.048725.1429
50.0702-0.0219-0.13460.0096-0.00620.0423-0.1327-0.003-0.03660.21580.13750.05530.0142-0.0272-00.17940.0233-0.0350.14080.00140.143942.597895.877552.6534
60.00520.00520.01810.0056-0.0091-0.01470.0591-0.09370.013-0.0786-0.093-0.1355-0.0082-0.094100.15360.00490.02520.11850.02720.132439.2754107.960644.6203
70.0742-0.0559-0.12780.12580.10390.077-0.0078-0.00070.0025-0.00560.01110.0250.0084-0.018300.10390.0158-0.01230.11630.02030.098631.558494.016348.9959
8-0.00840.0373-0.00630.00790.01150.0362-0.05160.0457-0.01030.03570.04470.0106-0.02550.002900.10050.0078-0.00550.14010.03290.141828.562387.188451.0226
90.06050.14240.03660.04680.02070.0056-0.0338-0.0315-0.003-0.0316-0.0552-0.0103-0.01610.221300.1660.03770.03790.14090.01450.125164.033125.317569.8889
100.0031-0.0141-0.00340.00480.01620.04340.11290.06990.1385-0.06280.1113-0.137-0.0368-0.17260.00280.1348-0.0150.00050.17270.02140.127257.1778132.304958.7474
110.08110.10460.00180.0022-0.15960.0794-0.0120.01520.0169-0.02580.0223-0.0189-0.04680.005300.13930.02370.01970.10920.00650.12662.4442136.309973.8422
120.0317-0.01580.02870.0407-0.02250.0010.0279-0.04150.0351-0.03690.00950.0057-0.09110.036600.1074-0.00220.02090.12170.00840.135164.7253137.543481.0783
130.0354-0.00880.07490.03660.01710.0487-0.11270.00560.0356-0.08980.13530.0638-0.01970.0086-00.1666-0.02260.00560.1404-0.00450.151939.771380.9499102.4207
140.01010.0092-0.0127-0.0039-0.0018-0.00890.10150.141-0.04120.1327-0.11110.0314-0.0008-0.03500.1666-0.0221-0.00830.13060.03570.157332.151471.0469110.4138
150.14250.02160.13580.08790.01180.27250.0171-0.00770.00260.01930.03970.0502-0.0038-0.05180.43250.0854-0.00610.0140.10910.01540.113930.303486.6683106.0157
160.0179-0.01460.04220.0107-0.03370.0392-0.07370.0287-0.0390.05050.12640.0439-0.0234-0.0182-00.12570.00620.00220.130.02160.150429.96994.2284103.9902
170.09310.1150.04210.02890.04970.0209-0.0770.0168-0.0129-0.0170.0158-0.0050.1656-0.066600.17330.0350.01680.12280.03080.11545.933112.836485.0791
180.0065-0.0120.01760.0512-0.00480.22490.1462-0.0539-0.1289-0.01120.08440.0481-0.20780.08480.01770.1802-0.00370.00060.1044-0.01340.130241.9774121.723796.3738
190.12210.1742-0.12960.00010.05980.09460.01230.0062-0.0198-0.0130.00740.0047-0.0121-0.0409-0.0490.05920.03620.00020.03450.02590.060436.3351118.311881.3326
200.00810.0323-0.02270.01280.03980.0265-0.03570.01990.0534-0.05160.03340.06950.0578-0.0886-00.14820.0052-0.01950.17220.02850.147134.2162116.726573.9669
21-0.0211-0.01110.1050.0489-0.08420.1110.00330.0533-0.04640.07240.1204-0.11740.00860.0288-00.1635-0.03770.00420.1596-0.00310.19457.946993.0346117.9783
22-0.0175-0.023-0.01350.0114-0.0006-0.00320.06240.01840.1239-0.1482-0.09250.13340.04780.10380.00010.13460.0414-0.00680.11720.00150.17352.1708105.6039123.4742
230.18050.06320.07440.0603-0.03690.1281-0.03880.00340.01090.04140.02460.021-0.01330.00100.06230.00620.01320.0306-0.00480.042253.650889.913128.4435
240.0293-0.01150.0430.0088-0.00790.01120.00870.0531-0.06510.07280.0539-0.0092-0.00230.0156-00.15160.0095-0.01160.12150.00730.113754.253482.4041130.1647
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(CHAIN A AND RESID 1:71)
2X-RAY DIFFRACTION2(CHAIN A AND RESID 72:104)
3X-RAY DIFFRACTION3(CHAIN A AND RESID 105:268)
4X-RAY DIFFRACTION4(CHAIN A AND RESID 269:307)
5X-RAY DIFFRACTION5(CHAIN B AND RESID 1:71)
6X-RAY DIFFRACTION6(CHAIN B AND RESID 72:104)
7X-RAY DIFFRACTION7(CHAIN B AND RESID 105:268)
8X-RAY DIFFRACTION8(CHAIN B AND RESID 269:307)
9X-RAY DIFFRACTION9(CHAIN C AND RESID 1:71)
10X-RAY DIFFRACTION10(CHAIN C AND RESID 72:104)
11X-RAY DIFFRACTION11(CHAIN C AND RESID 105:268)
12X-RAY DIFFRACTION12(CHAIN C AND RESID 269:307)
13X-RAY DIFFRACTION13(CHAIN D AND RESID 1:71)
14X-RAY DIFFRACTION14(CHAIN D AND RESID 72:104)
15X-RAY DIFFRACTION15(CHAIN D AND RESID 105:268)
16X-RAY DIFFRACTION16(CHAIN D AND RESID 269:307)
17X-RAY DIFFRACTION17(CHAIN E AND RESID 1:71)
18X-RAY DIFFRACTION18(CHAIN E AND RESID 72:104)
19X-RAY DIFFRACTION19(CHAIN E AND RESID 105:268)
20X-RAY DIFFRACTION20(CHAIN E AND RESID 269:307)
21X-RAY DIFFRACTION21(CHAIN F AND RESID 1:71)
22X-RAY DIFFRACTION22(CHAIN F AND RESID 72:104)
23X-RAY DIFFRACTION23(CHAIN F AND RESID 105:268)
24X-RAY DIFFRACTION24(CHAIN F AND RESID 269:307)

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