FMO DATABASE

FMODB ID: KV293

Calculation Name: 2ACF-A-Xray547

Preferred Name: Replicase polyprotein 1ab

Target Type: SINGLE PROTEIN

Ligand Name: glycerol

Ligand 3-letter code: GOL

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2ACF

Chain ID: A

ChEMBL ID: CHEMBL5118

UniProt ID: P0C6X7

Base Structure: X-ray

Registration Date: 2025-10-05

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	172
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1681811.162735
FMO2-HF: Nuclear repulsion	1616516.978841
FMO2-HF: Total energy	-65294.183894
FMO2-MP2: Total energy	-65482.286831

3D Structure Molmil

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:180:HIS)

Summations of interaction energy for fragment #1(A:180:HIS)

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
-0.242	2.851	-0.017	-1.388	-1.686	-0.006

Interaction energy analysis for fragmet #1(A:180:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.808 / q_NPA : 0.892

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

Sort

Graph Options

X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	182	HIS	0	0.006	0.020	3.480	6.099	9.027	-0.016	-1.360	-1.551	-0.006
4	A	183	MET	0	0.040	0.014	4.693	-7.041	-6.876	-0.001	-0.028	-0.135	0.000
5	A	184	PRO	0	-0.002	0.004	7.486	2.484	2.484	0.000	0.000	0.000	0.000
6	A	185	VAL	0	0.043	0.033	11.142	-0.318	-0.318	0.000	0.000	0.000	0.000
7	A	186	ASN	0	-0.003	-0.001	13.580	0.631	0.631	0.000	0.000	0.000	0.000
8	A	187	GLN	0	-0.025	-0.012	12.688	0.625	0.625	0.000	0.000	0.000	0.000
9	A	188	PHE	0	-0.015	-0.004	16.016	0.093	0.093	0.000	0.000	0.000	0.000
10	A	189	THR	0	0.025	0.007	18.441	0.702	0.702	0.000	0.000	0.000	0.000
11	A	190	GLY	0	0.001	0.000	21.010	-0.053	-0.053	0.000	0.000	0.000	0.000
12	A	191	TYR	0	-0.078	-0.069	21.181	0.306	0.306	0.000	0.000	0.000	0.000
13	A	192	LEU	0	0.014	0.025	26.220	-0.018	-0.018	0.000	0.000	0.000	0.000
14	A	193	LYS	1	0.868	0.917	29.672	10.053	10.053	0.000	0.000	0.000	0.000
15	A	194	LEU	0	0.002	0.005	30.782	0.279	0.279	0.000	0.000	0.000	0.000
16	A	195	THR	0	0.035	0.009	32.894	0.201	0.201	0.000	0.000	0.000	0.000
17	A	196	ASP	-1	-0.857	-0.932	31.998	-9.888	-9.888	0.000	0.000	0.000	0.000
18	A	197	ASN	0	-0.077	-0.031	30.647	-0.105	-0.105	0.000	0.000	0.000	0.000
19	A	198	VAL	0	0.018	0.017	29.886	-0.291	-0.291	0.000	0.000	0.000	0.000
20	A	199	ALA	0	0.035	0.027	26.908	0.213	0.213	0.000	0.000	0.000	0.000
21	A	200	ILE	0	0.005	0.004	28.097	-0.225	-0.225	0.000	0.000	0.000	0.000
22	A	201	LYS	1	0.822	0.891	19.939	14.276	14.276	0.000	0.000	0.000	0.000
23	A	202	CYS	0	0.003	0.014	26.577	0.154	0.154	0.000	0.000	0.000	0.000
24	A	203	VAL	0	-0.073	-0.034	20.648	-0.230	-0.230	0.000	0.000	0.000	0.000
25	A	204	ASP	-1	-0.865	-0.934	21.100	-12.786	-12.786	0.000	0.000	0.000	0.000
26	A	205	ILE	0	0.071	0.019	20.540	-0.608	-0.608	0.000	0.000	0.000	0.000
27	A	206	VAL	0	0.002	0.007	17.283	-0.651	-0.651	0.000	0.000	0.000	0.000
28	A	207	LYS	1	0.912	0.955	16.099	12.395	12.395	0.000	0.000	0.000	0.000
29	A	208	GLU	-1	-0.747	-0.835	15.824	-15.912	-15.912	0.000	0.000	0.000	0.000
30	A	209	ALA	0	-0.035	-0.016	16.603	-0.762	-0.762	0.000	0.000	0.000	0.000
31	A	210	GLN	0	-0.030	-0.034	12.275	-0.845	-0.845	0.000	0.000	0.000	0.000
32	A	211	SER	0	-0.056	-0.002	11.431	-1.960	-1.960	0.000	0.000	0.000	0.000
33	A	212	ALA	0	0.032	0.014	13.056	-1.140	-1.140	0.000	0.000	0.000	0.000
34	A	213	ASN	0	-0.045	-0.016	9.910	0.211	0.211	0.000	0.000	0.000	0.000
35	A	214	PRO	0	0.020	0.024	12.877	-0.142	-0.142	0.000	0.000	0.000	0.000
36	A	215	MET	0	0.003	-0.021	16.056	-1.044	-1.044	0.000	0.000	0.000	0.000
37	A	216	VAL	0	0.006	-0.004	17.634	0.171	0.171	0.000	0.000	0.000	0.000
38	A	217	ILE	0	-0.014	0.007	19.458	0.045	0.045	0.000	0.000	0.000	0.000
39	A	218	VAL	0	0.013	0.009	21.367	0.248	0.248	0.000	0.000	0.000	0.000
40	A	219	ASN	0	-0.034	-0.043	24.979	-0.009	-0.009	0.000	0.000	0.000	0.000
41	A	220	ALA	0	-0.010	0.005	26.573	0.251	0.251	0.000	0.000	0.000	0.000
42	A	221	ALA	0	-0.003	0.006	29.820	0.084	0.084	0.000	0.000	0.000	0.000
43	A	222	ASN	0	0.017	-0.017	31.442	0.343	0.343	0.000	0.000	0.000	0.000
44	A	223	ILE	0	0.061	0.019	34.053	-0.248	-0.248	0.000	0.000	0.000	0.000
45	A	224	HIS	0	0.009	0.013	35.828	-0.103	-0.103	0.000	0.000	0.000	0.000
46	A	225	LEU	0	-0.013	0.001	29.579	-0.164	-0.164	0.000	0.000	0.000	0.000
47	A	226	LYS	1	0.852	0.933	30.624	9.221	9.221	0.000	0.000	0.000	0.000
48	A	227	HIS	0	0.002	-0.012	27.136	0.333	0.333	0.000	0.000	0.000	0.000
49	A	228	GLY	0	-0.010	-0.007	28.768	-0.211	-0.211	0.000	0.000	0.000	0.000
50	A	229	GLY	0	0.015	0.002	30.129	0.210	0.210	0.000	0.000	0.000	0.000
51	A	230	GLY	0	0.022	0.009	29.908	-0.152	-0.152	0.000	0.000	0.000	0.000
52	A	231	VAL	0	0.027	0.007	25.274	-0.205	-0.205	0.000	0.000	0.000	0.000
53	A	232	ALA	0	0.064	0.048	25.513	-0.443	-0.443	0.000	0.000	0.000	0.000
54	A	233	GLY	0	0.006	0.002	25.692	-0.352	-0.352	0.000	0.000	0.000	0.000
55	A	234	ALA	0	-0.045	-0.020	23.422	-0.267	-0.267	0.000	0.000	0.000	0.000
56	A	235	LEU	0	0.037	0.010	20.754	-0.547	-0.547	0.000	0.000	0.000	0.000
57	A	236	ASN	0	0.089	0.031	20.834	-0.857	-0.857	0.000	0.000	0.000	0.000
58	A	237	LYS	1	0.942	0.981	21.503	11.373	11.373	0.000	0.000	0.000	0.000
59	A	238	ALA	0	-0.009	0.002	17.416	-0.304	-0.304	0.000	0.000	0.000	0.000
60	A	239	THR	0	-0.038	-0.004	16.933	-0.688	-0.688	0.000	0.000	0.000	0.000
61	A	240	ASN	0	-0.045	-0.028	18.602	0.337	0.337	0.000	0.000	0.000	0.000
62	A	241	GLY	0	0.015	0.014	20.306	0.259	0.259	0.000	0.000	0.000	0.000
63	A	242	ALA	0	-0.011	-0.005	19.669	0.393	0.393	0.000	0.000	0.000	0.000
64	A	243	MET	0	0.032	0.025	21.169	0.388	0.388	0.000	0.000	0.000	0.000
65	A	244	GLN	0	-0.032	-0.025	23.129	0.448	0.448	0.000	0.000	0.000	0.000
66	A	245	LYS	1	0.913	0.961	24.231	12.519	12.519	0.000	0.000	0.000	0.000
67	A	246	GLU	-1	-0.770	-0.880	22.755	-13.830	-13.830	0.000	0.000	0.000	0.000
68	A	247	SER	0	0.009	-0.004	25.725	0.306	0.306	0.000	0.000	0.000	0.000
69	A	248	ASP	-1	-0.815	-0.876	28.383	-9.573	-9.573	0.000	0.000	0.000	0.000
70	A	249	ASP	-1	-0.909	-0.958	27.358	-10.936	-10.936	0.000	0.000	0.000	0.000
71	A	250	TYR	0	-0.011	-0.010	28.895	0.091	0.091	0.000	0.000	0.000	0.000
72	A	251	ILE	0	-0.020	-0.009	30.786	0.299	0.299	0.000	0.000	0.000	0.000
73	A	252	LYS	1	0.913	0.956	33.052	9.714	9.714	0.000	0.000	0.000	0.000
74	A	253	LEU	0	-0.059	-0.014	31.087	0.181	0.181	0.000	0.000	0.000	0.000
75	A	254	ASN	0	-0.036	-0.034	34.197	0.117	0.117	0.000	0.000	0.000	0.000
76	A	255	GLY	0	0.032	0.036	36.073	0.272	0.272	0.000	0.000	0.000	0.000
77	A	256	PRO	0	-0.032	-0.025	36.204	-0.277	-0.277	0.000	0.000	0.000	0.000
78	A	257	LEU	0	-0.005	-0.003	32.706	0.036	0.036	0.000	0.000	0.000	0.000
79	A	258	THR	0	0.018	-0.001	36.652	0.161	0.161	0.000	0.000	0.000	0.000
80	A	259	VAL	0	0.024	0.003	37.493	-0.238	-0.238	0.000	0.000	0.000	0.000
81	A	260	GLY	0	-0.008	0.002	37.561	0.189	0.189	0.000	0.000	0.000	0.000
82	A	261	GLY	0	0.001	0.019	35.961	-0.102	-0.102	0.000	0.000	0.000	0.000
83	A	262	SER	0	-0.043	-0.053	30.411	-0.262	-0.262	0.000	0.000	0.000	0.000
84	A	263	CYS	0	-0.020	0.008	29.794	0.098	0.098	0.000	0.000	0.000	0.000
85	A	264	LEU	0	-0.005	0.005	23.754	-0.262	-0.262	0.000	0.000	0.000	0.000
86	A	265	LEU	0	-0.007	0.005	24.165	-0.102	-0.102	0.000	0.000	0.000	0.000
87	A	266	SER	0	-0.016	-0.025	18.460	-0.900	-0.900	0.000	0.000	0.000	0.000
88	A	267	GLY	0	-0.008	0.005	17.752	0.708	0.708	0.000	0.000	0.000	0.000
89	A	268	HIS	0	-0.064	-0.054	16.304	-0.673	-0.673	0.000	0.000	0.000	0.000
90	A	269	ASN	0	-0.024	-0.025	12.404	-0.710	-0.710	0.000	0.000	0.000	0.000
91	A	270	LEU	0	-0.052	-0.015	13.185	-0.332	-0.332	0.000	0.000	0.000	0.000
92	A	271	ALA	0	0.028	0.015	15.245	-0.026	-0.026	0.000	0.000	0.000	0.000
93	A	272	LYS	1	0.939	0.983	15.219	19.593	19.593	0.000	0.000	0.000	0.000
94	A	273	LYS	1	0.906	0.942	16.166	15.499	15.499	0.000	0.000	0.000	0.000
95	A	274	CYS	0	0.012	0.008	19.892	-0.077	-0.077	0.000	0.000	0.000	0.000
96	A	275	LEU	0	-0.003	0.013	22.309	0.325	0.325	0.000	0.000	0.000	0.000
97	A	276	HIS	0	0.045	0.009	24.492	0.489	0.489	0.000	0.000	0.000	0.000
98	A	277	VAL	0	0.009	-0.002	28.098	0.260	0.260	0.000	0.000	0.000	0.000
99	A	278	VAL	0	-0.033	0.003	31.117	0.009	0.009	0.000	0.000	0.000	0.000
100	A	279	GLY	0	0.025	0.014	34.347	0.168	0.168	0.000	0.000	0.000	0.000
101	A	280	PRO	0	0.003	0.006	35.998	0.011	0.011	0.000	0.000	0.000	0.000
102	A	281	ASN	0	0.006	-0.001	38.531	0.013	0.013	0.000	0.000	0.000	0.000
103	A	282	LEU	0	0.026	0.016	39.915	0.179	0.179	0.000	0.000	0.000	0.000
104	A	283	ASN	0	-0.067	-0.038	39.640	0.320	0.320	0.000	0.000	0.000	0.000
105	A	284	ALA	0	-0.051	-0.019	41.906	0.087	0.087	0.000	0.000	0.000	0.000
106	A	285	GLY	0	-0.013	0.003	43.765	0.110	0.110	0.000	0.000	0.000	0.000
107	A	286	GLU	-1	-0.902	-0.944	40.600	-7.711	-7.711	0.000	0.000	0.000	0.000
108	A	287	ASP	-1	-0.831	-0.929	44.444	-6.867	-6.867	0.000	0.000	0.000	0.000
109	A	288	ILE	0	0.023	0.000	41.297	-0.194	-0.194	0.000	0.000	0.000	0.000
110	A	289	GLN	0	0.001	-0.004	42.367	-0.250	-0.250	0.000	0.000	0.000	0.000
111	A	290	LEU	0	-0.011	-0.006	40.908	-0.131	-0.131	0.000	0.000	0.000	0.000
112	A	291	LEU	0	-0.020	-0.012	36.203	-0.262	-0.262	0.000	0.000	0.000	0.000
113	A	292	LYS	1	0.940	0.983	37.488	7.895	7.895	0.000	0.000	0.000	0.000
114	A	293	ALA	0	-0.006	-0.003	37.840	-0.184	-0.184	0.000	0.000	0.000	0.000
115	A	294	ALA	0	0.033	0.011	34.908	-0.240	-0.240	0.000	0.000	0.000	0.000
116	A	295	TYR	0	0.025	-0.020	31.692	-0.454	-0.454	0.000	0.000	0.000	0.000
117	A	296	GLU	-1	-0.821	-0.889	33.214	-9.061	-9.061	0.000	0.000	0.000	0.000
118	A	297	ASN	0	-0.037	-0.011	31.419	-0.250	-0.250	0.000	0.000	0.000	0.000
119	A	298	PHE	0	0.031	0.008	29.006	-0.407	-0.407	0.000	0.000	0.000	0.000
120	A	299	ASN	0	-0.044	-0.035	29.055	-0.609	-0.609	0.000	0.000	0.000	0.000
121	A	300	SER	0	-0.041	-0.011	29.293	-0.056	-0.056	0.000	0.000	0.000	0.000
122	A	301	GLN	0	-0.030	-0.026	24.594	-0.902	-0.902	0.000	0.000	0.000	0.000
123	A	302	ASP	-1	-0.865	-0.902	23.753	-12.705	-12.705	0.000	0.000	0.000	0.000
124	A	303	ILE	0	-0.044	-0.033	21.220	0.035	0.035	0.000	0.000	0.000	0.000
125	A	304	LEU	0	-0.063	-0.009	22.377	-0.498	-0.498	0.000	0.000	0.000	0.000
126	A	305	LEU	0	0.000	0.019	19.110	0.162	0.162	0.000	0.000	0.000	0.000
127	A	306	ALA	0	0.018	-0.008	22.363	0.036	0.036	0.000	0.000	0.000	0.000
128	A	307	PRO	0	-0.004	0.014	25.520	0.029	0.029	0.000	0.000	0.000	0.000
129	A	308	LEU	0	0.010	0.007	27.805	0.106	0.106	0.000	0.000	0.000	0.000
130	A	309	LEU	0	0.005	0.011	30.515	0.061	0.061	0.000	0.000	0.000	0.000
131	A	310	SER	0	0.020	-0.021	33.127	0.152	0.152	0.000	0.000	0.000	0.000
132	A	311	ALA	0	0.006	0.024	33.335	0.259	0.259	0.000	0.000	0.000	0.000
133	A	312	GLY	0	0.004	-0.005	34.052	-0.132	-0.132	0.000	0.000	0.000	0.000
134	A	313	ILE	0	-0.009	-0.013	33.656	0.206	0.206	0.000	0.000	0.000	0.000
135	A	314	PHE	0	-0.020	0.014	33.497	0.158	0.158	0.000	0.000	0.000	0.000
136	A	315	GLY	0	0.036	0.027	37.534	0.168	0.168	0.000	0.000	0.000	0.000
137	A	316	ALA	0	-0.004	-0.003	38.484	0.200	0.200	0.000	0.000	0.000	0.000
138	A	317	LYS	1	0.944	0.967	38.713	7.135	7.135	0.000	0.000	0.000	0.000
139	A	318	PRO	0	0.039	0.017	35.354	-0.036	-0.036	0.000	0.000	0.000	0.000
140	A	319	LEU	0	0.074	0.036	36.639	-0.174	-0.174	0.000	0.000	0.000	0.000
141	A	320	GLN	0	0.007	0.009	38.806	-0.009	-0.009	0.000	0.000	0.000	0.000
142	A	321	SER	0	-0.013	-0.026	35.328	-0.097	-0.097	0.000	0.000	0.000	0.000
143	A	322	LEU	0	0.026	0.011	32.970	-0.164	-0.164	0.000	0.000	0.000	0.000
144	A	323	GLN	0	0.011	0.013	35.848	-0.001	-0.001	0.000	0.000	0.000	0.000
145	A	324	VAL	0	0.026	0.012	38.009	-0.023	-0.023	0.000	0.000	0.000	0.000
146	A	325	CYS	0	-0.034	0.002	31.814	-0.153	-0.153	0.000	0.000	0.000	0.000
147	A	326	VAL	0	0.021	0.006	35.119	-0.112	-0.112	0.000	0.000	0.000	0.000
148	A	327	GLN	0	-0.049	-0.017	36.409	0.026	0.026	0.000	0.000	0.000	0.000
149	A	328	THR	0	-0.089	-0.049	35.805	0.229	0.229	0.000	0.000	0.000	0.000
150	A	329	VAL	0	-0.060	-0.020	30.412	-0.087	-0.087	0.000	0.000	0.000	0.000
151	A	330	ARG	1	0.883	0.923	33.617	9.187	9.187	0.000	0.000	0.000	0.000
152	A	331	THR	0	-0.030	-0.027	27.915	-0.082	-0.082	0.000	0.000	0.000	0.000
153	A	332	GLN	0	-0.015	-0.005	25.335	0.294	0.294	0.000	0.000	0.000	0.000
154	A	333	VAL	0	-0.041	-0.031	25.943	-0.350	-0.350	0.000	0.000	0.000	0.000
155	A	334	TYR	0	0.028	0.019	22.937	0.204	0.204	0.000	0.000	0.000	0.000
156	A	335	ILE	0	0.007	-0.011	24.738	-0.228	-0.228	0.000	0.000	0.000	0.000
157	A	336	ALA	0	0.014	0.002	23.499	-0.021	-0.021	0.000	0.000	0.000	0.000
158	A	337	VAL	0	-0.017	-0.018	25.625	0.335	0.335	0.000	0.000	0.000	0.000
159	A	338	ASN	0	-0.003	-0.018	26.856	-0.001	-0.001	0.000	0.000	0.000	0.000
160	A	339	ASP	-1	-0.861	-0.909	28.070	-8.594	-8.594	0.000	0.000	0.000	0.000
161	A	340	LYS	1	0.909	0.923	29.854	9.578	9.578	0.000	0.000	0.000	0.000
162	A	341	ALA	0	0.021	0.015	32.051	0.072	0.072	0.000	0.000	0.000	0.000
163	A	342	LEU	0	-0.021	-0.016	32.860	0.134	0.134	0.000	0.000	0.000	0.000
164	A	343	TYR	0	-0.047	-0.026	29.308	0.036	0.036	0.000	0.000	0.000	0.000
165	A	344	GLU	-1	-0.787	-0.907	33.053	-9.049	-9.049	0.000	0.000	0.000	0.000
166	A	345	GLN	0	-0.085	-0.035	35.696	0.200	0.200	0.000	0.000	0.000	0.000
167	A	346	VAL	0	-0.007	-0.018	34.108	0.072	0.072	0.000	0.000	0.000	0.000
168	A	347	VAL	0	-0.041	-0.017	33.841	-0.036	-0.036	0.000	0.000	0.000	0.000
169	A	348	MET	0	-0.026	-0.022	36.369	0.091	0.091	0.000	0.000	0.000	0.000
170	A	349	ASP	-1	-0.885	-0.937	39.408	-7.477	-7.477	0.000	0.000	0.000	0.000
171	A	350	TYR	0	-0.114	-0.057	35.310	-0.028	-0.028	0.000	0.000	0.000	0.000
172	A	351	LEU	-1	-0.973	-0.960	38.394	-7.378	-7.378	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

Interactive mode: IFIE and PIEDA for fragment #1(A:180:HIS)