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- PDB-4bgu: 1.50 A resolution structure of the malate dehydrogenase from Halo... -

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Basic information

Entry
Database: PDB / ID: 4bgu
Title1.50 A resolution structure of the malate dehydrogenase from Haloferax volcanii
ComponentsMALATE DEHYDROGENASE
KeywordsOXIDOREDUCTASE / TRICARBOXYLIC ACID CYCLE
Function / homology
Function and homology information


malate dehydrogenase / L-malate dehydrogenase (NAD+) activity / carboxylic acid metabolic process / tricarboxylic acid cycle / carbohydrate metabolic process
Similarity search - Function
L-2-Hydroxyisocaproate Dehydrogenase; Chain A, domain 2 / Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal / L-lactate/malate dehydrogenase / Lactate/malate dehydrogenase, N-terminal / Lactate/malate dehydrogenase, C-terminal / lactate/malate dehydrogenase, NAD binding domain / lactate/malate dehydrogenase, alpha/beta C-terminal domain / Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal / NAD(P)-binding Rossmann-like Domain / NAD(P)-binding domain superfamily ...L-2-Hydroxyisocaproate Dehydrogenase; Chain A, domain 2 / Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal / L-lactate/malate dehydrogenase / Lactate/malate dehydrogenase, N-terminal / Lactate/malate dehydrogenase, C-terminal / lactate/malate dehydrogenase, NAD binding domain / lactate/malate dehydrogenase, alpha/beta C-terminal domain / Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal / NAD(P)-binding Rossmann-like Domain / NAD(P)-binding domain superfamily / Alpha-Beta Complex / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
: / TRIETHYLENE GLYCOL / Malate dehydrogenase
Similarity search - Component
Biological speciesHALOFERAX VOLCANII (archaea)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SIRAS / Resolution: 1.487 Å
AuthorsTalon, R. / Madern, D. / Girard, E.
Citation
Journal: To be Published
Title: Insight Into Structural Evolution of Extremophilic Proteins
Authors: Talon, R. / Girard, E. / Franzetti, B. / Zaccai, G. / Madern, D.
#1: Journal: Mol.Biol.Evol. / Year: 2012
Title: Sampling the Conformational Energy Landscape of a Hyperthermophilic Protein by Engineering Key Substitutions.
Authors: Colletier, J. / Aleksandrov, A. / Coquelle, N. / Mraihi, S. / Mendoza-Barbera, E. / Field, M. / Madern, D.
#2: Journal: J.Mol.Biol. / Year: 2010
Title: Gradual Adaptive Changes of a Protein Facing High Salt Concentrations.
Authors: Coquelle, N. / Talon, R. / Juers, D.H. / Girard, E. / Kahn, R. / Madern, D.
#3: Journal: J.Synchrotron Radia. / Year: 2007
Title: Specific Radiation Damage to Acidic Residues and its Relation to Their Chemical and Structural Environment.
Authors: Fioravanti, E. / Vellieux, F.M.D. / Amara, P. / Madern, D. / Weik, M.
#4: Journal: J.Mol.Biol. / Year: 2003
Title: The Oligomeric States of Haloarcula Marismortui Malate Dehydrogenase are Modulated by Solvent Components as Shown by Crystallographic and Biochemical Studies.
Authors: Irimia, A. / Ebel, C. / Madern, D. / Richard, S.B. / Cosenza, L.W. / Zaccai, G. / Vellieux, F.M.D.
#5: Journal: Acta Crystallogr.,Sect.D / Year: 2002
Title: Gd-Hpdo3A, a Complex to Obtain High-Phasing-Power Heavy-Atom Derivatives for Sad and MAD Experiments: Results with Tetragonal Hen Egg-White Lysozyme.
Authors: Girard, E. / Chantalat, L. / Vicat, J. / Kahn, R.
#6: Journal: J.Synchrotron.Radiat. / Year: 2011
Title: Using Lanthanoid Complexes to Phase Large Macromolecular Assemblies.
Authors: Talon, R. / Kahn, R. / Dura, M.A. / Maury, O. / Vellieux, F.M.D. / Franzetti, B. / Girard, E.
History
DepositionMar 28, 2013Deposition site: PDBE / Processing site: PDBE
Revision 1.0Apr 16, 2014Provider: repository / Type: Initial release
Revision 1.1Mar 6, 2019Group: Data collection / Experimental preparation / Other
Category: exptl_crystal_grow / pdbx_database_proc / pdbx_database_status
Item: _exptl_crystal_grow.temp / _pdbx_database_status.recvd_author_approval
Revision 1.2May 8, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_struct_conn_angle / struct_conn / struct_site
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _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.ptnr1_symmetry / _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.ptnr3_symmetry / _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.ptnr1_symmetry / _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_conn.ptnr2_symmetry / _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: MALATE DEHYDROGENASE
B: MALATE DEHYDROGENASE
C: MALATE DEHYDROGENASE
D: MALATE DEHYDROGENASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)135,509108
Polymers130,2074
Non-polymers5,303104
Water32,6791814
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area14430 Å2
ΔGint-54 kcal/mol
Surface area52110 Å2
MethodPISA
Unit cell
Length a, b, c (Å)143.760, 82.319, 112.750
Angle α, β, γ (deg.)90.00, 101.72, 90.00
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11D-1330-

CL

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Components

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Protein , 1 types, 4 molecules ABCD

#1: Protein
MALATE DEHYDROGENASE


Mass: 32551.703 Da / Num. of mol.: 4 / Source method: obtained synthetically
Details: COMPLETE GENE WAS SYNTHESIZED BY GENECUST EUROPE COMPANY
Source: (synth.) HALOFERAX VOLCANII (archaea) / References: UniProt: Q9P9L2, malate dehydrogenase

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Non-polymers , 8 types, 1918 molecules

#2: Chemical...
ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 23 / Source method: obtained synthetically / Formula: K
#3: Chemical...
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 71 / Source method: obtained synthetically / Formula: Cl
#4: Chemical ChemComp-TRS / 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / TRIS BUFFER


Mass: 122.143 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C4H12NO3 / Comment: pH buffer*YM
#5: Chemical ChemComp-PGE / TRIETHYLENE GLYCOL


Mass: 150.173 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C6H14O4
#6: Chemical ChemComp-1PE / PENTAETHYLENE GLYCOL / PEG400


Mass: 238.278 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H22O6 / Comment: precipitant*YM
#7: Chemical ChemComp-P33 / 3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL / HEPTAETHYLENE GLYCOL / PEG330


Mass: 326.383 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C14H30O8 / Comment: precipitant*YM
#8: Chemical ChemComp-PG4 / TETRAETHYLENE GLYCOL


Mass: 194.226 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C8H18O5 / Comment: precipitant*YM
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1814 / Source method: isolated from a natural source / Formula: H2O

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Details

Sequence detailsDUE TO THE PROTEIN PRODUCTION PROTOCOL, EACH MONOMER WERE FOUND DELETED OF THEIR N-TERMINAL METHIONINE.

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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: 2.12 Å3/Da / Density % sol: 40 % / Description: NONE
Crystal growTemperature: 293 K / pH: 8
Details: 31-36% PEG 400, 0.1 M TRIS HCL PH 8.0, 0.1 M MGCL2, 293 K, 2-4 DAYS

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: BM30A / Wavelength: 0.979
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Feb 23, 2011 / Details: TWO MIRRORS
RadiationMonochromator: DOUBLE CRYSTALS MONOCHROMATOR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979 Å / Relative weight: 1
ReflectionResolution: 1.49→48.34 Å / Num. obs: 205562 / % possible obs: 100 % / Observed criterion σ(I): -3 / Redundancy: 7.4 % / Biso Wilson estimate: 12.34 Å2 / Rmerge(I) obs: 0.06 / Net I/σ(I): 21.6
Reflection shellResolution: 1.49→1.58 Å / Redundancy: 7.3 % / Rmerge(I) obs: 0.4 / Mean I/σ(I) obs: 4.9 / % possible all: 99.9

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
XDS10-05-2010data reduction
SCALA3.3.16data scaling
SHARPphasing
RefinementMethod to determine structure: SIRAS
Starting model: NONE

Resolution: 1.487→48.479 Å / SU ML: 0.12 / σ(F): 1.34 / Phase error: 17.47 / Stereochemistry target values: ML
Details: THE PROTEIN WERE FOUND IN ITS NATIVE HOMOTETRAMERIC STATE INSIDE THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT.
RfactorNum. reflection% reflection
Rfree0.1788 10263 5 %
Rwork0.1558 --
obs0.1569 205541 97.39 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 14.24 Å2
Refinement stepCycle: LAST / Resolution: 1.487→48.479 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9152 0 211 1814 11177
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.019705
X-RAY DIFFRACTIONf_angle_d1.30313201
X-RAY DIFFRACTIONf_dihedral_angle_d12.5823652
X-RAY DIFFRACTIONf_chiral_restr0.0871477
X-RAY DIFFRACTIONf_plane_restr0.0061784
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.4866-1.50350.2498930.22141991X-RAY DIFFRACTION30
1.5035-1.52120.21173180.20386102X-RAY DIFFRACTION92
1.5212-1.53970.23043510.19546664X-RAY DIFFRACTION100
1.5397-1.55920.20963530.18526695X-RAY DIFFRACTION100
1.5592-1.57970.21713480.19046619X-RAY DIFFRACTION100
1.5797-1.60140.22063490.18736657X-RAY DIFFRACTION100
1.6014-1.62420.2053520.17816689X-RAY DIFFRACTION100
1.6242-1.64850.18523490.17836625X-RAY DIFFRACTION100
1.6485-1.67420.21673500.17586663X-RAY DIFFRACTION100
1.6742-1.70170.20263530.17156682X-RAY DIFFRACTION100
1.7017-1.7310.19163490.16946653X-RAY DIFFRACTION100
1.731-1.76250.18963530.16956706X-RAY DIFFRACTION100
1.7625-1.79640.19523500.17266646X-RAY DIFFRACTION100
1.7964-1.83310.19743490.16886631X-RAY DIFFRACTION100
1.8331-1.87290.18553510.16356671X-RAY DIFFRACTION100
1.8729-1.91650.1923520.16336693X-RAY DIFFRACTION100
1.9165-1.96440.18963530.16036692X-RAY DIFFRACTION100
1.9644-2.01760.16663510.1586675X-RAY DIFFRACTION100
2.0176-2.07690.1893500.1576642X-RAY DIFFRACTION100
2.0769-2.1440.17833490.15076647X-RAY DIFFRACTION100
2.144-2.22060.18133520.14656686X-RAY DIFFRACTION100
2.2206-2.30950.18173520.15136692X-RAY DIFFRACTION100
2.3095-2.41460.17733540.15176697X-RAY DIFFRACTION100
2.4146-2.54190.17783520.15076697X-RAY DIFFRACTION100
2.5419-2.70120.16723530.15066706X-RAY DIFFRACTION100
2.7012-2.90970.173520.1546702X-RAY DIFFRACTION100
2.9097-3.20250.18573530.14916709X-RAY DIFFRACTION100
3.2025-3.66570.15293550.13596738X-RAY DIFFRACTION100
3.6657-4.61780.13153550.12516760X-RAY DIFFRACTION100
4.6178-48.50460.19333620.16646848X-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)
11.49430.0645-0.18031.0635-0.09572.1011-0.0177-0.0828-0.07220.1013-0.0154-0.12590.04440.20790.01830.05860.0021-0.00380.08910.00580.079929.108516.097842.4723
22.83910.64180.20720.6474-0.62842.60920.0141-0.2453-0.1870.0520.0009-0.15120.0710.1626-0.01060.0770.0217-0.01770.12930.01580.078223.21359.151158.1047
31.32810.27380.50280.38160.22861.6926-0.0093-0.046-0.17270.01380.04250.00570.1204-0.0156-0.04030.08210.00760.01760.04050.01460.07874.4822-0.453340.4918
41.83291.252-0.21882.1687-0.6472.01170.0302-0.1197-0.85910.0197-0.032-0.06220.36960.04960.02440.20920.0233-0.00930.09080.01920.203410.8638-10.358940.1269
51.11110.03-0.2260.70160.01870.6561-0.0177-0.1283-0.0360.07750.00440.01890.0060.03720.01040.05860.0094-0.00560.06890.01350.045310.693510.569750.1447
65.24070.4172.26852.5073-0.81813.52720.1126-0.4501-0.44080.08950.02030.16850.4023-0.3413-0.13330.1654-0.00970.03970.11820.04640.15343.0284-4.011157.0535
72.1428-2.62881.3584.33720.28824.2991-0.1488-0.4765-0.39350.4997-0.0181-0.28090.39450.35020.01440.19790.0727-0.01210.29550.10150.150718.7018-1.444266.3226
81.03040.0712-0.56011.12970.06761.6403-0.09060.1281-0.2283-0.03560.0066-0.12660.19360.07320.05810.08280.01020.02370.0981-0.02440.107921.51850.416824.338
96.72422.29340.24523.98821.14252.55770.12520.2189-0.6830.1239-0.005-0.59250.34480.2728-0.13570.19780.05730.05130.2079-0.03980.238338.1278-1.131813.089
101.461-0.6835-0.9563.2249-1.13491.5496-0.15470.2088-0.0859-0.35730.01980.06510.2823-0.13960.11640.1688-0.00310.06590.1771-0.0640.103124.89113.090810.9559
110.6080.2098-0.05821.15020.38890.6829-0.0160.1189-0.0126-0.05660.0178-0.08170.01020.1177-0.00440.05730.00040.01920.14130.00090.08733.271321.140117.5902
121.04321.5686-1.09633.3976-2.69643.0297-0.0485-0.189-0.10270.1444-0.2435-0.6653-0.09740.3650.28410.0973-0.00470.01060.19680.00950.193643.93823.774327.9695
130.46250.04280.26760.8214-0.10850.1777-0.04820.1775-0.0428-0.1190.0055-0.0549-0.01080.120.05340.07760.00060.02760.165-0.00950.086727.900515.858113.902
141.2762-0.5919-0.37191.17580.45851.2529-0.03720.31060.0815-0.21750.1176-0.2907-0.08590.2269-0.09710.1388-0.02250.0560.268-0.00850.168438.393219.77256.7377
151.44130.58450.07361.92840.28881.1895-0.0085-0.01240.21090.1014-0.03030.1224-0.1352-0.04850.02560.0725-0.00550.00010.05720.00150.0711-2.781337.127336.0476
162.0160.2857-0.81862.3208-0.02681.93120.00010.02830.2872-0.0602-0.02560.1852-0.2347-0.11920.0230.1371-0.0126-0.02950.0621-0.01670.16386.025252.863634.9049
171.25120.0669-0.39270.81550.53481.3234-0.0310.140.1162-0.08570.0118-0.1399-0.10720.08530.01340.0913-0.02950.00290.1090.04650.101416.585739.143613.6575
181.60941.5196-1.20861.5046-0.87872.0086-0.0160.54860.4527-0.19360.09260.0171-0.15-0.0485-0.08450.1679-0.02360.00070.18190.06960.14738.516444.46926.6122
191.20620.0403-0.09210.8825-0.15480.9018-0.0013-0.03060.14660.0557-0.0057-0.1388-0.14680.17260.00520.0957-0.02840.00310.08120.00860.103915.85843.121229.0384
201.329-0.0865-0.14951.20370.24250.83180.12030.27650.3678-0.441-0.0192-0.4218-0.38420.1893-0.06750.3019-0.08040.05540.1840.07450.283122.141254.49316.8752
210.8101-1.09530.0474.3472-0.92097.01420.18860.14350.5991-0.25960.18420.0388-0.5744-0.3162-0.36830.2929-0.0535-0.00010.11790.03950.290910.823263.968327.4361
220.94240.74430.18281.62370.31711.2398-0.06770.20880.1291-0.09470.04580.1639-0.0458-0.07680.00540.0717-0.00810.00080.10880.02310.0636-3.645327.770712.6814
231.94571.3611-0.5632.4018-0.42472.41990.06230.43190.4155-0.20260.07110.5136-0.3262-0.434-0.12020.1383-0.0238-0.0510.22660.04960.2029-22.554621.992311.4442
241.7139-0.05880.53312.1951-2.48883.7856-0.15780.1809-0.0772-0.27980.06690.06980.31540.15440.090.0796-0.0614-0.0140.1307-0.010.0769-10.694716.647510.8867
250.67870.2030.33390.50020.04241.7374-0.00720.0014-0.0146-0.00390.01080.05540.0549-0.0636-0.00590.0422-0.0080.00960.04830.00420.0613-13.060714.435831.2938
260.99611.6881-1.11073.6789-2.11382.28710.1176-0.06210.17710.31160.13040.4838-0.2578-0.2372-0.23470.08290.00880.02120.1301-0.00350.1182-19.447523.716241.0433
270.68680.0277-0.16871.2241-0.10480.7029-0.04780.0903-0.0503-0.01590.04480.03450.1093-0.02140.00310.0642-0.0148-0.00330.07590.00440.0334-9.953812.678323.4066
281.6005-0.06-0.18811.3896-0.49881.8157-0.04030.0156-0.0525-0.00870.06510.20160.1075-0.2424-0.02270.0936-0.04820.00250.096-0.02690.1115-21.99516.769526.5717
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(CHAIN A AND RESID 2:84)
2X-RAY DIFFRACTION2(CHAIN A AND RESID 85:143)
3X-RAY DIFFRACTION3(CHAIN A AND RESID 144:196)
4X-RAY DIFFRACTION4(CHAIN A AND RESID 197:218)
5X-RAY DIFFRACTION5(CHAIN A AND RESID 219:279)
6X-RAY DIFFRACTION6(CHAIN A AND RESID 280:296)
7X-RAY DIFFRACTION7(CHAIN A AND RESID 297:304)
8X-RAY DIFFRACTION8(CHAIN B AND RESID 2:84)
9X-RAY DIFFRACTION9(CHAIN B AND RESID 85:109)
10X-RAY DIFFRACTION10(CHAIN B AND RESID 110:121)
11X-RAY DIFFRACTION11(CHAIN B AND RESID 122:196)
12X-RAY DIFFRACTION12(CHAIN B AND RESID 197:218)
13X-RAY DIFFRACTION13(CHAIN B AND RESID 219:270)
14X-RAY DIFFRACTION14(CHAIN B AND RESID 271:304)
15X-RAY DIFFRACTION15(CHAIN C AND RESID 2:84)
16X-RAY DIFFRACTION16(CHAIN C AND RESID 85:143)
17X-RAY DIFFRACTION17(CHAIN C AND RESID 144:196)
18X-RAY DIFFRACTION18(CHAIN C AND RESID 197:218)
19X-RAY DIFFRACTION19(CHAIN C AND RESID 219:279)
20X-RAY DIFFRACTION20(CHAIN C AND RESID 280:296)
21X-RAY DIFFRACTION21(CHAIN C AND RESID 297:304)
22X-RAY DIFFRACTION22(CHAIN D AND RESID 2:84)
23X-RAY DIFFRACTION23(CHAIN D AND RESID 85:109)
24X-RAY DIFFRACTION24(CHAIN D AND RESID 110:121)
25X-RAY DIFFRACTION25(CHAIN D AND RESID 122:196)
26X-RAY DIFFRACTION26(CHAIN D AND RESID 197:218)
27X-RAY DIFFRACTION27(CHAIN D AND RESID 219:270)
28X-RAY DIFFRACTION28(CHAIN D AND RESID 271:304)

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