FMO DATABASE

FMODB ID: MVGJZ

Calculation Name: 2B9U-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2B9U

Chain ID: A

ChEMBL ID:

UniProt ID: Q96Z62

Base Structure: X-ray

Registration Date: 2023-09-20

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptHSide
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	175
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1975447.572562
FMO2-HF: Nuclear repulsion	1903837.169778
FMO2-HF: Total energy	-71610.402783
FMO2-MP2: Total energy	-71819.68103

3D Structure

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:1:MET)

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

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.
-3.066	2.43	3.958	-3.729	-5.724	-0.012

Interaction energy analysis for fragmet #1(A:1:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.016 / q_NPA : -0.001

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	3	PHE	0	-0.039	-0.022	2.692	-0.320	1.681	0.314	-0.978	-1.336	0.001
4	A	4	GLU	-1	-0.890	-0.934	2.629	-8.085	-5.165	0.907	-1.921	-1.907	-0.019
5	A	5	PHE	0	0.000	-0.011	5.119	0.316	0.342	-0.001	-0.004	-0.021	0.000
6	A	6	GLU	-1	-0.809	-0.896	8.301	-0.764	-0.764	0.000	0.000	0.000	0.000
7	A	7	ASN	0	-0.032	-0.021	11.596	-0.017	-0.017	0.000	0.000	0.000	0.000
8	A	8	LEU	0	0.032	0.013	14.847	0.033	0.033	0.000	0.000	0.000	0.000
9	A	9	GLY	0	0.012	0.018	17.707	0.044	0.044	0.000	0.000	0.000	0.000
10	A	10	MET	0	-0.037	-0.025	20.357	-0.007	-0.007	0.000	0.000	0.000	0.000
11	A	11	GLY	0	0.030	0.009	18.830	0.016	0.016	0.000	0.000	0.000	0.000
12	A	12	ILE	0	-0.008	0.017	17.772	-0.031	-0.031	0.000	0.000	0.000	0.000
13	A	13	ILE	0	-0.047	-0.022	11.708	-0.009	-0.009	0.000	0.000	0.000	0.000
14	A	14	LEU	0	0.011	0.019	12.450	0.020	0.020	0.000	0.000	0.000	0.000
15	A	15	ILE	0	-0.035	-0.029	8.080	-0.103	-0.103	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.860	0.933	7.576	1.220	1.220	0.000	0.000	0.000	0.000
17	A	17	PRO	0	0.017	0.015	6.469	-0.715	-0.715	0.000	0.000	0.000	0.000
18	A	18	LYS	1	0.845	0.921	2.154	6.030	6.579	2.738	-0.826	-2.460	0.006
19	A	19	VAL	0	0.008	0.005	7.734	0.260	0.260	0.000	0.000	0.000	0.000
20	A	20	PHE	0	-0.033	-0.021	6.531	0.035	0.035	0.000	0.000	0.000	0.000
21	A	21	PRO	0	0.024	0.013	11.635	0.074	0.074	0.000	0.000	0.000	0.000
22	A	22	ASP	-1	-0.801	-0.884	14.724	-0.178	-0.178	0.000	0.000	0.000	0.000
23	A	23	LYS	1	0.974	0.977	17.440	0.077	0.077	0.000	0.000	0.000	0.000
24	A	24	ARG	1	0.790	0.863	17.242	0.202	0.202	0.000	0.000	0.000	0.000
25	A	25	GLY	0	0.022	0.028	19.974	0.006	0.006	0.000	0.000	0.000	0.000
26	A	26	PHE	0	-0.040	-0.021	15.207	-0.003	-0.003	0.000	0.000	0.000	0.000
27	A	27	PHE	0	-0.006	0.003	12.145	0.032	0.032	0.000	0.000	0.000	0.000
28	A	28	LEU	0	0.040	0.014	11.262	-0.098	-0.098	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.824	-0.883	8.723	-0.655	-0.655	0.000	0.000	0.000	0.000
30	A	30	VAL	0	0.017	0.012	10.053	-0.231	-0.231	0.000	0.000	0.000	0.000
31	A	31	PHE	0	0.043	0.002	11.077	-0.102	-0.102	0.000	0.000	0.000	0.000
32	A	32	LYS	1	0.798	0.893	7.090	0.730	0.730	0.000	0.000	0.000	0.000
33	A	33	SER	0	0.026	0.017	9.978	-0.046	-0.046	0.000	0.000	0.000	0.000
34	A	34	GLU	-1	-0.827	-0.890	8.987	0.182	0.182	0.000	0.000	0.000	0.000
35	A	35	ASP	-1	-0.819	-0.931	5.369	-0.756	-0.756	0.000	0.000	0.000	0.000
36	A	36	PHE	0	0.040	0.003	7.250	-0.059	-0.059	0.000	0.000	0.000	0.000
37	A	37	THR	0	0.021	0.007	10.165	0.072	0.072	0.000	0.000	0.000	0.000
38	A	38	LYS	1	0.778	0.885	6.382	0.064	0.064	0.000	0.000	0.000	0.000
39	A	39	MET	0	-0.054	-0.028	7.229	0.140	0.140	0.000	0.000	0.000	0.000
40	A	40	ARG	1	0.859	0.932	11.186	0.449	0.449	0.000	0.000	0.000	0.000
41	A	41	ILE	0	-0.017	0.008	12.067	0.034	0.034	0.000	0.000	0.000	0.000
42	A	42	PRO	0	-0.016	-0.002	14.668	0.005	0.005	0.000	0.000	0.000	0.000
43	A	43	ASN	0	0.007	-0.011	16.787	-0.057	-0.057	0.000	0.000	0.000	0.000
44	A	44	VAL	0	-0.014	-0.008	16.956	0.007	0.007	0.000	0.000	0.000	0.000
45	A	45	ILE	0	-0.058	-0.031	19.626	0.021	0.021	0.000	0.000	0.000	0.000
46	A	46	GLN	0	0.040	0.023	23.099	0.025	0.025	0.000	0.000	0.000	0.000
47	A	47	THR	0	-0.018	-0.007	21.815	-0.037	-0.037	0.000	0.000	0.000	0.000
48	A	48	ASN	0	-0.004	0.020	23.804	0.030	0.030	0.000	0.000	0.000	0.000
49	A	49	MET	0	0.030	0.011	24.319	-0.030	-0.030	0.000	0.000	0.000	0.000
50	A	50	SER	0	-0.053	0.001	26.360	0.023	0.023	0.000	0.000	0.000	0.000
51	A	51	PHE	0	0.029	0.011	27.245	-0.014	-0.014	0.000	0.000	0.000	0.000
52	A	52	SER	0	-0.025	-0.007	28.887	0.019	0.019	0.000	0.000	0.000	0.000
53	A	53	ARG	1	1.003	1.011	30.507	0.137	0.137	0.000	0.000	0.000	0.000
54	A	54	LYS	1	0.965	0.972	31.750	0.185	0.185	0.000	0.000	0.000	0.000
55	A	55	GLY	0	0.018	0.010	32.134	0.011	0.011	0.000	0.000	0.000	0.000
56	A	56	VAL	0	-0.048	-0.016	31.896	0.005	0.005	0.000	0.000	0.000	0.000
57	A	57	VAL	0	-0.013	-0.003	31.557	-0.014	-0.014	0.000	0.000	0.000	0.000
58	A	58	ARG	1	0.860	0.937	29.376	0.211	0.211	0.000	0.000	0.000	0.000
59	A	59	GLY	0	0.007	0.011	29.859	-0.018	-0.018	0.000	0.000	0.000	0.000
60	A	60	LEU	0	-0.047	-0.007	29.313	0.009	0.009	0.000	0.000	0.000	0.000
61	A	61	HIS	0	-0.032	-0.050	29.586	0.000	0.000	0.000	0.000	0.000	0.000
62	A	62	TYR	0	-0.036	-0.048	28.712	-0.020	-0.020	0.000	0.000	0.000	0.000
63	A	63	GLN	0	-0.036	-0.021	29.571	0.012	0.012	0.000	0.000	0.000	0.000
64	A	64	ARG	1	0.905	0.953	30.654	0.105	0.105	0.000	0.000	0.000	0.000
65	A	65	THR	0	0.063	0.011	30.945	-0.001	-0.001	0.000	0.000	0.000	0.000
66	A	66	PRO	0	-0.117	-0.059	32.210	0.007	0.007	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.893	0.935	30.711	0.129	0.129	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.791	-0.874	27.047	-0.158	-0.158	0.000	0.000	0.000	0.000
69	A	69	GLN	0	-0.051	-0.047	25.225	-0.006	-0.006	0.000	0.000	0.000	0.000
70	A	70	GLY	0	0.008	0.018	21.225	0.000	0.000	0.000	0.000	0.000	0.000
71	A	71	LYS	1	0.895	0.947	20.702	0.267	0.267	0.000	0.000	0.000	0.000
72	A	72	ILE	0	0.007	0.008	14.460	-0.030	-0.030	0.000	0.000	0.000	0.000
73	A	73	ILE	0	-0.023	0.009	17.627	0.028	0.028	0.000	0.000	0.000	0.000
74	A	74	PHE	0	0.047	0.009	15.055	-0.054	-0.054	0.000	0.000	0.000	0.000
75	A	75	VAL	0	0.014	0.008	17.862	0.060	0.060	0.000	0.000	0.000	0.000
76	A	76	PRO	0	-0.016	0.007	19.189	-0.015	-0.015	0.000	0.000	0.000	0.000
77	A	77	LYS	1	0.848	0.899	20.126	0.292	0.292	0.000	0.000	0.000	0.000
78	A	78	GLY	0	0.042	0.026	23.378	0.009	0.009	0.000	0.000	0.000	0.000
79	A	79	ARG	1	0.831	0.875	22.781	0.263	0.263	0.000	0.000	0.000	0.000
80	A	80	ILE	0	-0.039	-0.004	21.980	0.034	0.034	0.000	0.000	0.000	0.000
81	A	81	LEU	0	-0.012	0.000	23.090	-0.023	-0.023	0.000	0.000	0.000	0.000
82	A	82	ASP	-1	-0.754	-0.898	21.262	-0.345	-0.345	0.000	0.000	0.000	0.000
83	A	83	VAL	0	-0.006	-0.018	23.163	-0.005	-0.005	0.000	0.000	0.000	0.000
84	A	84	ALA	0	0.011	0.011	22.618	0.002	0.002	0.000	0.000	0.000	0.000
85	A	85	VAL	0	0.014	-0.005	24.604	0.002	0.002	0.000	0.000	0.000	0.000
86	A	86	ASP	-1	-0.710	-0.798	26.952	-0.187	-0.187	0.000	0.000	0.000	0.000
87	A	87	VAL	0	0.013	0.007	28.145	0.013	0.013	0.000	0.000	0.000	0.000
88	A	88	ARG	1	0.851	0.904	24.314	0.216	0.216	0.000	0.000	0.000	0.000
89	A	89	LYS	1	0.995	0.979	31.502	0.104	0.104	0.000	0.000	0.000	0.000
90	A	90	SER	0	-0.036	-0.017	33.223	0.001	0.001	0.000	0.000	0.000	0.000
91	A	91	SER	0	-0.032	-0.026	28.393	0.004	0.004	0.000	0.000	0.000	0.000
92	A	92	PRO	0	-0.022	-0.010	28.647	0.004	0.004	0.000	0.000	0.000	0.000
93	A	93	THR	0	-0.086	-0.074	26.693	0.001	0.001	0.000	0.000	0.000	0.000
94	A	94	PHE	0	0.026	0.028	29.494	-0.011	-0.011	0.000	0.000	0.000	0.000
95	A	95	GLY	0	0.036	0.021	31.312	0.007	0.007	0.000	0.000	0.000	0.000
96	A	96	LYS	1	0.908	0.968	27.939	0.150	0.150	0.000	0.000	0.000	0.000
97	A	97	TYR	0	0.016	-0.006	26.233	-0.008	-0.008	0.000	0.000	0.000	0.000
98	A	98	VAL	0	-0.006	0.010	19.790	0.002	0.002	0.000	0.000	0.000	0.000
99	A	99	LYS	1	0.896	0.952	22.983	0.228	0.228	0.000	0.000	0.000	0.000
100	A	100	ALA	0	0.018	0.002	18.382	-0.017	-0.017	0.000	0.000	0.000	0.000
101	A	101	GLU	-1	-0.793	-0.850	20.407	-0.330	-0.330	0.000	0.000	0.000	0.000
102	A	102	LEU	0	-0.041	-0.001	16.359	-0.050	-0.050	0.000	0.000	0.000	0.000
103	A	103	ASN	0	-0.002	-0.028	18.226	0.017	0.017	0.000	0.000	0.000	0.000
104	A	104	GLU	-1	-0.756	-0.847	18.073	-0.378	-0.378	0.000	0.000	0.000	0.000
105	A	105	GLU	-1	-0.964	-0.970	17.888	-0.457	-0.457	0.000	0.000	0.000	0.000
106	A	106	ASN	0	0.006	-0.008	14.863	-0.071	-0.071	0.000	0.000	0.000	0.000
107	A	107	HIS	0	-0.015	0.000	13.456	-0.164	-0.164	0.000	0.000	0.000	0.000
108	A	108	TYR	0	-0.005	-0.019	11.427	-0.158	-0.158	0.000	0.000	0.000	0.000
109	A	109	MET	0	-0.055	-0.021	10.598	0.141	0.141	0.000	0.000	0.000	0.000
110	A	110	LEU	0	0.017	0.025	13.770	-0.059	-0.059	0.000	0.000	0.000	0.000
111	A	111	TRP	0	-0.001	-0.008	14.688	0.041	0.041	0.000	0.000	0.000	0.000
112	A	112	ILE	0	-0.022	-0.021	16.321	0.019	0.019	0.000	0.000	0.000	0.000
113	A	113	PRO	0	-0.002	0.013	19.093	0.019	0.019	0.000	0.000	0.000	0.000
114	A	114	PRO	0	0.041	0.002	21.242	0.012	0.012	0.000	0.000	0.000	0.000
115	A	115	GLY	0	-0.022	-0.010	24.929	0.001	0.001	0.000	0.000	0.000	0.000
116	A	116	PHE	0	0.003	-0.013	23.349	0.004	0.004	0.000	0.000	0.000	0.000
117	A	117	ALA	0	-0.047	-0.011	26.629	0.001	0.001	0.000	0.000	0.000	0.000
118	A	118	HIS	0	-0.093	-0.071	23.407	0.010	0.010	0.000	0.000	0.000	0.000
119	A	119	GLY	0	0.070	0.012	26.283	0.020	0.020	0.000	0.000	0.000	0.000
120	A	120	PHE	0	-0.045	-0.010	25.155	-0.019	-0.019	0.000	0.000	0.000	0.000
121	A	121	GLN	0	0.009	0.011	27.162	0.013	0.013	0.000	0.000	0.000	0.000
122	A	122	ALA	0	-0.024	-0.005	27.532	-0.021	-0.021	0.000	0.000	0.000	0.000
123	A	123	LEU	0	0.017	-0.008	25.304	0.021	0.021	0.000	0.000	0.000	0.000
124	A	124	GLU	-1	-0.921	-0.975	27.060	-0.247	-0.247	0.000	0.000	0.000	0.000
125	A	125	ASP	-1	-0.835	-0.921	28.940	-0.190	-0.190	0.000	0.000	0.000	0.000
126	A	126	SER	0	-0.029	-0.033	25.287	-0.018	-0.018	0.000	0.000	0.000	0.000
127	A	127	ILE	0	-0.062	-0.026	24.060	0.022	0.022	0.000	0.000	0.000	0.000
128	A	128	VAL	0	0.022	0.022	22.237	-0.028	-0.028	0.000	0.000	0.000	0.000
129	A	129	ILE	0	-0.011	-0.016	19.973	0.036	0.036	0.000	0.000	0.000	0.000
130	A	130	TYR	0	-0.012	-0.030	20.667	-0.027	-0.027	0.000	0.000	0.000	0.000
131	A	131	PHE	0	0.018	-0.003	16.598	0.027	0.027	0.000	0.000	0.000	0.000
132	A	132	ILE	0	-0.009	-0.001	20.124	-0.017	-0.017	0.000	0.000	0.000	0.000
133	A	133	THR	0	0.071	0.009	18.260	0.000	0.000	0.000	0.000	0.000	0.000
134	A	134	HIS	0	-0.003	0.012	20.745	-0.001	-0.001	0.000	0.000	0.000	0.000
135	A	135	ASN	0	-0.012	-0.006	24.252	0.030	0.030	0.000	0.000	0.000	0.000
136	A	136	GLU	-1	-0.875	-0.928	27.173	-0.159	-0.159	0.000	0.000	0.000	0.000
137	A	137	TYR	0	-0.071	-0.041	28.901	0.005	0.005	0.000	0.000	0.000	0.000
138	A	138	SER	0	-0.001	-0.008	31.324	0.012	0.012	0.000	0.000	0.000	0.000
139	A	139	PRO	0	0.066	0.024	34.253	0.000	0.000	0.000	0.000	0.000	0.000
140	A	140	PRO	0	-0.020	0.001	37.041	0.001	0.001	0.000	0.000	0.000	0.000
141	A	141	HIS	0	-0.011	-0.005	34.359	0.003	0.003	0.000	0.000	0.000	0.000
142	A	142	GLU	-1	-0.805	-0.867	33.665	-0.151	-0.151	0.000	0.000	0.000	0.000
143	A	143	ARG	1	0.859	0.934	34.014	0.126	0.126	0.000	0.000	0.000	0.000
144	A	144	CYS	0	-0.054	0.003	33.638	-0.007	-0.007	0.000	0.000	0.000	0.000
145	A	145	ILE	0	0.039	0.026	32.107	0.009	0.009	0.000	0.000	0.000	0.000
146	A	146	SER	0	-0.012	-0.003	34.545	-0.009	-0.009	0.000	0.000	0.000	0.000
147	A	147	TYR	0	0.110	0.036	33.512	-0.005	-0.005	0.000	0.000	0.000	0.000
148	A	148	SER	0	-0.038	-0.011	34.277	-0.005	-0.005	0.000	0.000	0.000	0.000
149	A	149	TYR	0	-0.072	-0.047	31.801	0.006	0.006	0.000	0.000	0.000	0.000
150	A	150	ILE	0	-0.049	-0.022	29.680	-0.005	-0.005	0.000	0.000	0.000	0.000
151	A	151	ASP	-1	-0.927	-0.944	32.601	-0.153	-0.153	0.000	0.000	0.000	0.000
152	A	152	TRP	0	-0.057	-0.053	28.001	-0.020	-0.020	0.000	0.000	0.000	0.000
153	A	153	PRO	0	0.023	0.014	29.393	0.008	0.008	0.000	0.000	0.000	0.000
154	A	154	ILE	0	-0.070	-0.027	31.554	0.009	0.009	0.000	0.000	0.000	0.000
155	A	155	LYS	1	0.930	0.957	34.576	0.128	0.128	0.000	0.000	0.000	0.000
156	A	156	GLU	-1	-0.879	-0.938	38.101	-0.130	-0.130	0.000	0.000	0.000	0.000
157	A	157	VAL	0	-0.002	0.002	35.778	-0.007	-0.007	0.000	0.000	0.000	0.000
158	A	158	ILE	0	-0.049	-0.019	36.180	0.008	0.008	0.000	0.000	0.000	0.000
159	A	159	ILE	0	0.029	0.007	35.834	-0.010	-0.010	0.000	0.000	0.000	0.000
160	A	160	SER	0	0.000	0.010	36.806	0.009	0.009	0.000	0.000	0.000	0.000
161	A	161	ASP	-1	-0.827	-0.929	38.923	-0.109	-0.109	0.000	0.000	0.000	0.000
162	A	162	LYS	1	0.872	0.913	36.085	0.142	0.142	0.000	0.000	0.000	0.000
163	A	163	ASP	-1	-0.803	-0.909	34.249	-0.166	-0.166	0.000	0.000	0.000	0.000
164	A	164	LEU	0	-0.052	-0.024	37.613	0.000	0.000	0.000	0.000	0.000	0.000
165	A	165	GLN	0	-0.019	-0.005	40.655	0.005	0.005	0.000	0.000	0.000	0.000
166	A	167	PRO	0	0.014	0.021	38.856	0.002	0.002	0.000	0.000	0.000	0.000
167	A	168	SER	0	0.033	0.001	38.476	-0.007	-0.007	0.000	0.000	0.000	0.000
168	A	169	LEU	0	0.051	0.018	34.044	0.001	0.001	0.000	0.000	0.000	0.000
169	A	170	GLU	-1	-0.928	-0.973	37.334	-0.116	-0.116	0.000	0.000	0.000	0.000
170	A	171	LYS	1	0.856	0.933	40.366	0.093	0.093	0.000	0.000	0.000	0.000
171	A	172	ALA	0	-0.009	0.013	37.385	0.003	0.003	0.000	0.000	0.000	0.000
172	A	173	GLU	-1	-0.923	-0.942	38.953	-0.094	-0.094	0.000	0.000	0.000	0.000
173	A	174	VAL	0	-0.079	-0.032	34.499	-0.008	-0.008	0.000	0.000	0.000	0.000
174	A	175	PHE	0	0.033	0.018	29.428	0.003	0.003	0.000	0.000	0.000	0.000
175	A	176	ASP	-1	-0.935	-0.945	32.131	-0.112	-0.112	0.000	0.000	0.000	0.000

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