Table 2. DSSP (Kabsch & Sander, 1983 ▸) assignment of secondary-structure elements in human muscle FBPase in the three states described in this work.

Gaps in the sequence (…) indicate fragments that were not modelled.

	Residue range
Secondary-structure element	R state	T state (−AMP)	T state (+AMP)
Allosteric domain
N-terminal	8–10	11–12	8–12
α1	—	13–19	13–23
βα1	11–15	—	—
L1	16–19…28	20…29	24–28
α2	29–49	30–49	29–48
L2 (catalytic loop)	50–51…73	50…72	49–63…70
αL2	—	—	53–56
α3	74–87	73–86	71–86
L3	88–90	87–90
β1	91–96
L4	97–109	97–112	97–109
βL4	103–104	99–104	103–104
αL4 (310-helix)	107–109
β2	110–121	113–118	110–121
L5	122…129–131	119–122…130–131	122–131
αL5 (310-helix)	—	—	123–128
β3	132–140	132–139	132–140
L6	141…147–160	140–158	141–142…147–160
αL6a (310-helix)	150–152	149–151	149–152
αL6b (310-helix)	156–158
β4	161–167	159–167	161–167
L7	168–170
β5	171–176
L8	177–181
β6	182–187
L9	188–191
β7	192–197
Catalytic domain
L10	198–207
β8	208–210	208–209	208–210
L11	211–220	210–220	211–220
αL11 (310-helix)	213–218	213–215	213–218
α4	221–231
L12	232–240
β9	241–242
L13	243–247
α5	248–258
L14	259–260
β10	261–264
L15	265–280
α6	281–290
L16	291–293
β11	294–296
L17	297–315
αL17 (310-helix)	302–304
β12	316–319
T1	320
α7	321–332	321–335
C-terminal	333–334	336–337	336–337