Table 4.

RD values obtained for 1AMK and 4DRS and for their respective secondary folds

Triose phosphate isomerase (1AMK) 1AMK – E.C.5.3.1.1			Pyruvate kinase – domain 2 (4DRS) E.C.2.7.1.40 – absent in domain 2
Fragment	Characteristics	RD	Fragment	Characteristics	RD
Protein	250	0.506	Protein	248	0.559
6–12 B	E 11 N, 13 K,	0.401	47–52 B		0.330
17–30 H		0.402	53–57 H		0.278
38–42 B		0.452	58–69 H		0.475
44–47 H		0.747	71–77 B		0.497
48–55 H		0.336	81–98 H		0.432
59–63 B		0.263	105–110 B		0.580
79–86 H		0.330	214–224 H		0.404
89–93 B		0.148	231–235 B		0.378
95–102 H	E 95H	0.634	240–253 H		0.387
105–119 H		0.366	266–271 B		0.477
122–127 B		0.321	273–279 H		0.551
130–136 H		0.541	280–287 H		0.329
138–152 H		0.364	289–294 B		0.390
153–154 H		0.319	296–301 H		0.647
155–160 H		0.340	302–305 H		0.534
161–167 B	E 167E	0.317	306–321 H		0.569
168–172 H		0.571	323–327 B		0.395
179–198 H	E 173G	0.423	331–336 H		0.440
199–206 H		0.654	341–355 H		0.418
207–212 B		0.542	357–361 B		0.306
218–224 H		0.382	362–367 H		0.603
229–233 B		0.524	370–387 H		0.553
234–239 H		0.222
240–241 H		0.600
242–248 H		0.160
Β-sheet			β-sheet		0.429
Helices			Helices		0.482
Eliminated	95–100,198–203	0.479	No ligand		0.546
No ligand		0.498	No residues	74–80 L, 229–236 L, 259–262, 264–272 L, 293–296, 319–321 L	0.486
NoE	11,13,95,167,173	0.500

Values listed in boldface satisfy RD > 0.5. “B” and “H” stand for β- and helical forms respectively; “L” indicates a ligand-binding fragment while “E” denotes that the given fragment contains an enzymatically active residue (listing its number and type). The row labeled “NoE” represents the status of each domain following elimination of catalytic residues — the observed reduction in RD values indicates that catalytic residues diverge from the theoretical model.