SHEET AFTER ROTATION OF THE A AND B SUBUNITS ABOUT THE CRYSTALLOGRAPHIC X AXIS, THE GENERATED C AND ...SHEET AFTER ROTATION OF THE A AND B SUBUNITS ABOUT THE CRYSTALLOGRAPHIC X AXIS, THE GENERATED C AND D SUBUNITS FORM EXTENSIONS TO SHEET 3 IN THE SHEET RECORDS BELOW. THE SYMMETRY-GENERATED SHEET RECORDS ARE PRESENTED AS A REMARK BECAUSE PDB SPECIFICATIONS DO NOT ALLOW THE INCLUSION OF STRANDS WHOSE COORDINATES ARE NOT PRESENTED IN THE ENTRY: EXTENSION TO SHEET 3 OF A SUBUNIT: 3A 4 HIS D 9 LEU D 11 -1 N HIS D 9 O VAL A 302 EXTENSION TO SHEET 3 OF B SUBUNIT 3B 4 HIS C 9 LEU C 11 -1 N HIS C 9 O VAL B 302 STRAND 2 OF SHEETS 2A AND 2B IS BIFURCATED. EACH OF THESE IS REPRESENTED BY TWO SHEETS, 2AA AND 2BA AND 2AB AND 2BB BELOW, WHERE THE FIRST STRAND OF 2AA IS IDENTICAL TO THE FIRST STRAND OF 2BA AND THE FIRST STRAND OF 2AB IS IDENTICAL TO THE FIRST STRAND OF 2BB.
TWO LDH SUBUNITS ARE INCLUDED. EACH SUBUNIT HAS NADH AND OXAMATE IN THE ACTIVE SITE AND A SULPHATE ION AT A REMOTE SITE. THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL YIELD APPROXIMATE COORDINATES FOR CHAIN *B* WHEN APPLIED TO CHAIN *A*. THE *SCALE* TRANSFORMATION BELOW GENERATES FRACTIONAL COORDINATES WITH RESPECT TO SPACE GROUP P 21 21 2.
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Components
#1: Protein
LACTATEDEHYDROGENASE
Mass: 36562.453 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Sus scrofa (pig) / References: UniProt: P00339, L-lactate dehydrogenase
Mass: 18.015 Da / Num. of mol.: 153 / Source method: isolated from a natural source / Formula: H2O
Sequence details
RESIDUES ARE NUMBERED ACCORDING TO THE STANDARD LDH NUMBERING SYSTEM DESCRIBED BY S.S.TAYLOR ET AL. ...RESIDUES ARE NUMBERED ACCORDING TO THE STANDARD LDH NUMBERING SYSTEM DESCRIBED BY S.S.TAYLOR ET AL., IN PROC.NAT.ACAD.SCI.USA V.70 1790 1973.
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION
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Sample preparation
Crystal
Density Matthews: 2.42 Å3/Da / Density % sol: 49.15 %
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Data collection
Radiation
Scattering type: x-ray
Radiation wavelength
Relative weight: 1
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Processing
Software
Name: PROLSQ / Classification: refinement
Refinement
Resolution: 2→20 Å / σ(F): 0 /
Rfactor
Num. reflection
obs
0.233
40664
Refinement step
Cycle: LAST / Resolution: 2→20 Å
Protein
Nucleic acid
Ligand
Solvent
Total
Num. atoms
5136
0
110
153
5399
Refine LS restraints
Refine-ID
Type
Dev ideal
Dev ideal target
X-RAY DIFFRACTION
p_bond_d
0.018
0.02
X-RAY DIFFRACTION
p_angle_d
0.069
0.04
X-RAY DIFFRACTION
p_angle_deg
X-RAY DIFFRACTION
p_planar_d
0.075
0.05
X-RAY DIFFRACTION
p_hb_or_metal_coord
X-RAY DIFFRACTION
p_mcbond_it
0.464
1
X-RAY DIFFRACTION
p_mcangle_it
0.817
1.5
X-RAY DIFFRACTION
p_scbond_it
0.496
1
X-RAY DIFFRACTION
p_scangle_it
0.77
1.5
X-RAY DIFFRACTION
p_plane_restr
0.024
0.02
X-RAY DIFFRACTION
p_chiral_restr
0.151
0.15
X-RAY DIFFRACTION
p_singtor_nbd
0.198
0.5
X-RAY DIFFRACTION
p_multtor_nbd
0.286
0.5
X-RAY DIFFRACTION
p_xhyhbond_nbd
0.214
0.5
X-RAY DIFFRACTION
p_xyhbond_nbd
X-RAY DIFFRACTION
p_planar_tor
3.5
3
X-RAY DIFFRACTION
p_staggered_tor
23.4
15
X-RAY DIFFRACTION
p_orthonormal_tor
33.2
30
X-RAY DIFFRACTION
p_transverse_tor
X-RAY DIFFRACTION
p_special_tor
+
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