FMO DATABASE

FMODB ID: R8228

Calculation Name: 4AY0-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4AY0

Chain ID: A

ChEMBL ID:

UniProt ID: P26926

Base Structure: X-ray

Registration Date: 2023-09-23

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

DOI:

Apendix: None

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	190
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1985695.292564
FMO2-HF: Nuclear repulsion	1912056.55304
FMO2-HF: Total energy	-73638.739524
FMO2-MP2: Total energy	-73856.423698

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:13:GLY)

Summations of interaction energy for fragment #1(A:13:GLY)

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.
0.733	1.949	-0.011	-0.532	-0.673	0

Interaction energy analysis for fragmet #1(A:13:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.006 / q_NPA : -0.012

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].
3	A	15	THR	0	-0.016	0.003	3.747	1.572	2.788	-0.011	-0.532	-0.673
4	A	16	ILE	0	0.006	-0.003	5.561	-0.352	-0.352	0.000	0.000	0.000
5	A	17	GLY	0	0.006	0.012	9.232	0.081	0.081	0.000	0.000	0.000
6	A	18	GLU	-1	-0.796	-0.867	10.306	-0.301	-0.301	0.000	0.000	0.000
7	A	19	SER	0	0.010	0.007	11.830	0.015	0.015	0.000	0.000	0.000
8	A	20	ARG	1	0.794	0.874	13.841	0.033	0.033	0.000	0.000	0.000
9	A	21	ILE	0	0.001	0.002	16.911	0.030	0.030	0.000	0.000	0.000
10	A	22	ILE	0	0.008	0.011	19.608	-0.016	-0.016	0.000	0.000	0.000
11	A	23	TYR	0	-0.034	-0.039	23.192	0.011	0.011	0.000	0.000	0.000
12	A	24	PRO	0	0.032	0.013	25.725	-0.007	-0.007	0.000	0.000	0.000
13	A	25	LEU	0	0.013	0.011	29.283	0.001	0.001	0.000	0.000	0.000
14	A	26	ASP	-1	-0.784	-0.862	31.683	0.000	0.000	0.000	0.000	0.000
15	A	27	ALA	0	-0.020	0.011	29.406	0.004	0.004	0.000	0.000	0.000
16	A	28	ALA	0	0.041	0.030	31.092	-0.003	-0.003	0.000	0.000	0.000
17	A	29	GLY	0	-0.016	-0.026	27.746	-0.003	-0.003	0.000	0.000	0.000
18	A	30	VAL	0	-0.034	0.004	22.579	0.004	0.004	0.000	0.000	0.000
19	A	31	MET	0	-0.002	0.002	22.337	-0.009	-0.009	0.000	0.000	0.000
20	A	32	VAL	0	0.004	0.011	15.824	0.006	0.006	0.000	0.000	0.000
21	A	33	SER	0	0.013	0.010	14.705	-0.003	-0.003	0.000	0.000	0.000
22	A	34	VAL	0	-0.014	-0.011	13.113	0.002	0.002	0.000	0.000	0.000
23	A	35	LYS	1	0.893	0.919	10.242	-0.590	-0.590	0.000	0.000	0.000
24	A	36	ASN	0	-0.008	0.002	9.921	0.022	0.022	0.000	0.000	0.000
25	A	37	THR	0	-0.008	-0.011	4.806	-0.164	-0.164	0.000	0.000	0.000
26	A	38	GLN	0	0.021	0.039	5.665	0.061	0.061	0.000	0.000	0.000
27	A	39	ASP	-1	-0.828	-0.921	9.130	0.584	0.584	0.000	0.000	0.000
28	A	40	TYR	0	0.002	-0.016	9.518	-0.052	-0.052	0.000	0.000	0.000
29	A	41	PRO	0	-0.020	-0.006	13.415	0.019	0.019	0.000	0.000	0.000
30	A	42	VAL	0	-0.025	-0.014	12.207	-0.029	-0.029	0.000	0.000	0.000
31	A	43	LEU	0	-0.029	-0.022	15.380	0.021	0.021	0.000	0.000	0.000
32	A	44	ILE	0	-0.014	-0.004	13.554	-0.026	-0.026	0.000	0.000	0.000
33	A	45	GLN	0	0.034	0.018	16.813	0.011	0.011	0.000	0.000	0.000
34	A	46	SER	0	0.004	-0.001	17.287	-0.023	-0.023	0.000	0.000	0.000
35	A	47	ARG	1	0.853	0.928	18.921	0.054	0.054	0.000	0.000	0.000
36	A	48	ILE	0	0.025	0.009	19.828	-0.009	-0.009	0.000	0.000	0.000
37	A	49	TYR	0	-0.019	0.001	19.513	-0.001	-0.001	0.000	0.000	0.000
38	A	50	ASP	-1	-0.696	-0.865	22.932	-0.102	-0.102	0.000	0.000	0.000
39	A	51	GLU	-1	-0.835	-0.892	22.847	-0.114	-0.114	0.000	0.000	0.000
40	A	52	ASN	0	-0.054	-0.038	22.408	-0.023	-0.023	0.000	0.000	0.000
41	A	53	LYS	1	0.810	0.912	15.629	0.234	0.234	0.000	0.000	0.000
42	A	54	GLU	-1	-0.892	-0.931	21.161	-0.125	-0.125	0.000	0.000	0.000
43	A	55	LYS	1	0.776	0.868	24.349	0.065	0.065	0.000	0.000	0.000
44	A	56	GLU	-1	-0.746	-0.860	26.049	-0.060	-0.060	0.000	0.000	0.000
45	A	57	SER	0	-0.009	-0.009	29.048	0.002	0.002	0.000	0.000	0.000
46	A	58	GLU	-1	-0.923	-0.956	32.360	-0.025	-0.025	0.000	0.000	0.000
47	A	59	ASP	-1	-0.892	-0.932	27.246	-0.053	-0.053	0.000	0.000	0.000
48	A	60	PRO	0	0.019	0.017	27.580	0.006	0.006	0.000	0.000	0.000
49	A	61	PHE	0	-0.018	-0.017	25.540	0.006	0.006	0.000	0.000	0.000
50	A	62	VAL	0	0.047	0.026	26.710	-0.004	-0.004	0.000	0.000	0.000
51	A	63	VAL	0	-0.027	-0.019	20.445	0.006	0.006	0.000	0.000	0.000
52	A	64	THR	0	-0.052	0.009	23.911	-0.003	-0.003	0.000	0.000	0.000
53	A	65	PRO	0	0.033	-0.006	21.954	0.007	0.007	0.000	0.000	0.000
54	A	66	PRO	0	0.045	0.011	21.928	0.001	0.001	0.000	0.000	0.000
55	A	67	LEU	0	0.009	-0.012	20.507	-0.012	-0.012	0.000	0.000	0.000
56	A	68	PHE	0	-0.006	-0.005	17.266	0.009	0.009	0.000	0.000	0.000
57	A	69	ARG	1	0.877	0.919	19.017	-0.111	-0.111	0.000	0.000	0.000
58	A	70	LEU	0	-0.050	0.004	13.440	0.010	0.010	0.000	0.000	0.000
59	A	71	ASP	-1	-0.775	-0.884	15.616	0.144	0.144	0.000	0.000	0.000
60	A	72	DAL	0	0.040	0.024	13.150	0.033	0.033	0.000	0.000	0.000
61	A	73	LYS	1	0.810	0.909	8.985	-0.770	-0.770	0.000	0.000	0.000
62	A	74	GLN	0	0.027	0.037	12.624	0.012	0.012	0.000	0.000	0.000
63	A	75	GLN	0	0.023	-0.006	13.801	0.083	0.083	0.000	0.000	0.000
64	A	76	ASN	0	0.028	0.013	15.620	-0.032	-0.032	0.000	0.000	0.000
65	A	77	SER	0	-0.047	-0.030	17.487	0.018	0.018	0.000	0.000	0.000
66	A	78	LEU	0	-0.005	0.017	17.064	-0.014	-0.014	0.000	0.000	0.000
67	A	79	ARG	1	0.975	0.982	20.563	-0.033	-0.033	0.000	0.000	0.000
68	A	80	ILE	0	-0.011	-0.004	19.703	-0.009	-0.009	0.000	0.000	0.000
69	A	81	ALA	0	0.017	-0.002	24.052	0.005	0.005	0.000	0.000	0.000
70	A	82	GLN	0	-0.044	-0.037	27.791	-0.009	-0.009	0.000	0.000	0.000
71	A	83	ALA	0	-0.034	-0.036	29.793	0.004	0.004	0.000	0.000	0.000
72	A	84	GLY	0	0.042	0.024	31.936	-0.001	-0.001	0.000	0.000	0.000
73	A	85	GLY	0	-0.028	-0.001	32.101	-0.002	-0.002	0.000	0.000	0.000
74	A	86	VAL	0	-0.008	0.004	33.133	0.003	0.003	0.000	0.000	0.000
75	A	87	PHE	0	-0.010	-0.011	29.647	-0.005	-0.005	0.000	0.000	0.000
76	A	88	PRO	0	0.003	0.013	32.590	0.003	0.003	0.000	0.000	0.000
77	A	89	ARG	1	0.861	0.872	34.091	0.007	0.007	0.000	0.000	0.000
78	A	90	ASP	-1	-0.853	-0.908	36.281	-0.031	-0.031	0.000	0.000	0.000
79	A	91	LYS	1	0.931	0.950	32.154	0.049	0.049	0.000	0.000	0.000
80	A	92	GLU	-1	-0.740	-0.854	26.377	-0.038	-0.038	0.000	0.000	0.000
81	A	93	SER	0	-0.043	-0.016	28.160	-0.004	-0.004	0.000	0.000	0.000
82	A	94	LEU	0	-0.034	0.000	20.629	0.004	0.004	0.000	0.000	0.000
83	A	95	LYS	1	0.821	0.907	23.106	0.061	0.061	0.000	0.000	0.000
84	A	96	TRP	0	-0.007	-0.022	14.983	-0.030	-0.030	0.000	0.000	0.000
85	A	97	LEU	0	0.023	0.029	16.381	0.011	0.011	0.000	0.000	0.000
86	A	98	CYS	0	-0.104	-0.052	10.721	0.056	0.056	0.000	0.000	0.000
87	A	99	VAL	0	0.022	-0.003	13.042	0.032	0.032	0.000	0.000	0.000
88	A	100	LYS	1	0.973	0.986	12.976	0.103	0.103	0.000	0.000	0.000
89	A	101	GLY	0	0.024	0.018	12.503	0.044	0.044	0.000	0.000	0.000
90	A	102	ILE	0	-0.057	-0.038	13.471	-0.043	-0.043	0.000	0.000	0.000
91	A	103	PRO	0	0.082	0.042	14.793	0.029	0.029	0.000	0.000	0.000
92	A	104	PRO	0	0.009	0.021	17.061	-0.011	-0.011	0.000	0.000	0.000
93	A	119	ASN	0	0.007	0.007	8.880	-0.115	-0.115	0.000	0.000	0.000
94	A	121	ILE	0	0.006	0.012	12.647	-0.034	-0.034	0.000	0.000	0.000
95	A	122	LYS	1	0.848	0.919	14.676	0.214	0.214	0.000	0.000	0.000
96	A	123	LEU	0	0.004	0.008	18.027	0.022	0.022	0.000	0.000	0.000
97	A	124	LEU	0	0.019	-0.001	20.991	-0.010	-0.010	0.000	0.000	0.000
98	A	125	VAL	0	0.002	0.012	23.646	0.012	0.012	0.000	0.000	0.000
99	A	126	ARG	1	0.751	0.818	24.706	0.009	0.009	0.000	0.000	0.000
100	A	127	PRO	0	0.029	0.024	29.127	0.006	0.006	0.000	0.000	0.000
101	A	128	ASN	0	-0.019	-0.015	32.793	0.003	0.003	0.000	0.000	0.000
102	A	129	GLU	-1	-0.775	-0.885	34.375	-0.006	-0.006	0.000	0.000	0.000
103	A	130	LEU	0	-0.041	0.005	30.863	-0.001	-0.001	0.000	0.000	0.000
104	A	131	LYS	1	0.814	0.893	34.299	0.006	0.006	0.000	0.000	0.000
105	A	132	GLY	0	0.015	0.009	32.735	-0.004	-0.004	0.000	0.000	0.000
106	A	133	THR	0	-0.002	-0.001	27.173	0.001	0.001	0.000	0.000	0.000
107	A	134	PRO	0	0.055	0.017	24.632	-0.002	-0.002	0.000	0.000	0.000
108	A	135	ILE	0	0.053	0.009	25.056	-0.005	-0.005	0.000	0.000	0.000
109	A	136	GLN	0	-0.029	-0.001	27.496	0.001	0.001	0.000	0.000	0.000
110	A	137	PHE	0	-0.023	-0.021	30.025	0.000	0.000	0.000	0.000	0.000
111	A	138	ALA	0	0.036	0.028	27.256	-0.005	-0.005	0.000	0.000	0.000
112	A	139	GLU	-1	-0.782	-0.880	28.960	-0.043	-0.043	0.000	0.000	0.000
113	A	140	ASN	0	-0.037	-0.030	31.878	-0.001	-0.001	0.000	0.000	0.000
114	A	141	LEU	0	-0.012	0.025	27.385	-0.001	-0.001	0.000	0.000	0.000
115	A	142	SER	0	-0.067	-0.024	32.108	0.002	0.002	0.000	0.000	0.000
116	A	143	TRP	0	0.071	0.014	26.931	-0.007	-0.007	0.000	0.000	0.000
117	A	144	LYS	1	0.993	1.000	34.259	0.062	0.062	0.000	0.000	0.000
118	A	145	VAL	0	-0.007	-0.005	33.991	-0.007	-0.007	0.000	0.000	0.000
119	A	146	ASP	-1	-0.861	-0.922	35.868	-0.062	-0.062	0.000	0.000	0.000
120	A	147	GLY	0	-0.005	-0.007	36.010	-0.005	-0.005	0.000	0.000	0.000
121	A	148	GLY	0	-0.032	-0.011	34.896	-0.004	-0.004	0.000	0.000	0.000
122	A	149	LYS	1	0.839	0.910	29.340	0.119	0.119	0.000	0.000	0.000
123	A	150	LEU	0	-0.004	0.008	28.404	0.008	0.008	0.000	0.000	0.000
124	A	151	ILE	0	-0.014	-0.014	30.174	-0.008	-0.008	0.000	0.000	0.000
125	A	152	ALA	0	0.000	0.006	29.112	0.006	0.006	0.000	0.000	0.000
126	A	153	GLU	-1	-0.883	-0.948	31.133	-0.055	-0.055	0.000	0.000	0.000
127	A	154	ASN	0	0.008	0.001	28.938	0.007	0.007	0.000	0.000	0.000
128	A	155	PRO	0	0.054	0.036	32.179	0.001	0.001	0.000	0.000	0.000
129	A	156	SER	0	-0.061	-0.036	30.890	0.006	0.006	0.000	0.000	0.000
130	A	157	PRO	0	0.018	-0.005	32.576	-0.004	-0.004	0.000	0.000	0.000
131	A	158	PHE	0	0.026	0.003	27.423	0.001	0.001	0.000	0.000	0.000
132	A	159	TYR	0	-0.025	-0.032	24.106	-0.004	-0.004	0.000	0.000	0.000
133	A	160	MET	0	-0.031	0.021	25.140	0.004	0.004	0.000	0.000	0.000
134	A	161	ASN	0	0.000	-0.021	19.583	-0.029	-0.029	0.000	0.000	0.000
135	A	162	ILE	0	0.002	0.010	20.760	0.003	0.003	0.000	0.000	0.000
136	A	163	GLY	0	0.009	-0.008	17.675	-0.024	-0.024	0.000	0.000	0.000
137	A	164	GLU	-1	-0.891	-0.933	17.839	-0.173	-0.173	0.000	0.000	0.000
138	A	165	LEU	0	0.016	0.009	20.483	0.023	0.023	0.000	0.000	0.000
139	A	166	THR	0	-0.028	-0.010	23.335	-0.012	-0.012	0.000	0.000	0.000
140	A	167	PHE	0	0.053	0.008	25.854	0.012	0.012	0.000	0.000	0.000
141	A	168	GLY	0	0.014	0.012	29.219	-0.005	-0.005	0.000	0.000	0.000
142	A	169	GLY	0	-0.048	-0.021	28.460	0.000	0.000	0.000	0.000	0.000
143	A	170	LYS	1	0.921	0.973	25.901	0.119	0.119	0.000	0.000	0.000
144	A	171	SER	0	0.034	0.010	20.908	0.006	0.006	0.000	0.000	0.000
145	A	172	ILE	0	-0.045	-0.017	23.009	-0.003	-0.003	0.000	0.000	0.000
146	A	173	PRO	0	0.006	0.000	19.070	-0.007	-0.007	0.000	0.000	0.000
147	A	174	SER	0	0.020	0.018	17.074	0.016	0.016	0.000	0.000	0.000
148	A	175	HIS	1	0.890	0.939	19.475	0.149	0.149	0.000	0.000	0.000
149	A	176	TYR	0	-0.075	-0.062	20.741	0.004	0.004	0.000	0.000	0.000
150	A	177	ILE	0	0.010	0.011	22.767	-0.001	-0.001	0.000	0.000	0.000
151	A	178	PRO	0	0.018	0.012	26.493	0.006	0.006	0.000	0.000	0.000
152	A	179	PRO	0	-0.003	0.009	27.942	0.002	0.002	0.000	0.000	0.000
153	A	180	LYS	1	0.783	0.877	30.673	0.033	0.033	0.000	0.000	0.000
154	A	181	SER	0	-0.006	0.009	31.537	0.000	0.000	0.000	0.000	0.000
155	A	182	THR	0	-0.005	-0.002	31.742	0.000	0.000	0.000	0.000	0.000
156	A	183	TRP	0	0.030	-0.002	25.551	-0.002	-0.002	0.000	0.000	0.000
157	A	184	ALA	0	0.008	0.020	29.160	0.002	0.002	0.000	0.000	0.000
158	A	185	PHE	0	-0.037	-0.024	23.004	-0.008	-0.008	0.000	0.000	0.000
159	A	186	ASP	-1	-0.819	-0.911	26.621	-0.135	-0.135	0.000	0.000	0.000
160	A	187	LEU	0	0.006	0.007	27.075	-0.010	-0.010	0.000	0.000	0.000
161	A	188	PRO	0	0.000	-0.001	26.010	0.003	0.003	0.000	0.000	0.000
162	A	189	LYS	1	0.998	0.985	28.806	0.122	0.122	0.000	0.000	0.000
163	A	190	GLY	0	0.013	-0.004	31.815	-0.004	-0.004	0.000	0.000	0.000
164	A	191	LEU	0	-0.020	-0.003	29.149	0.005	0.005	0.000	0.000	0.000
165	A	192	ALA	0	0.018	0.015	33.825	0.002	0.002	0.000	0.000	0.000
166	A	193	GLY	0	0.014	0.011	37.324	0.003	0.003	0.000	0.000	0.000
167	A	194	ALA	0	-0.044	-0.009	33.627	0.003	0.003	0.000	0.000	0.000
168	A	195	ARG	1	0.958	0.951	35.731	0.058	0.058	0.000	0.000	0.000
169	A	196	ASN	0	0.027	0.027	32.372	0.001	0.001	0.000	0.000	0.000
170	A	197	VAL	0	0.021	0.010	28.898	-0.008	-0.008	0.000	0.000	0.000
171	A	198	SER	0	0.012	0.008	27.506	0.013	0.013	0.000	0.000	0.000
172	A	199	TRP	0	-0.017	-0.011	24.780	-0.015	-0.015	0.000	0.000	0.000
173	A	200	ARG	1	0.915	0.965	20.800	0.109	0.109	0.000	0.000	0.000
174	A	201	ILE	0	-0.010	-0.007	21.983	-0.019	-0.019	0.000	0.000	0.000
175	A	202	ILE	0	-0.028	-0.004	15.782	0.004	0.004	0.000	0.000	0.000
176	A	203	ASN	0	0.037	0.020	19.693	0.011	0.011	0.000	0.000	0.000
177	A	204	ASP	-1	-0.726	-0.865	19.769	-0.014	-0.014	0.000	0.000	0.000
178	A	205	GLN	0	-0.035	-0.022	19.231	-0.003	-0.003	0.000	0.000	0.000
179	A	206	GLY	0	0.009	0.016	15.585	0.028	0.028	0.000	0.000	0.000
180	A	207	GLY	0	-0.002	-0.005	15.195	-0.015	-0.015	0.000	0.000	0.000
181	A	208	LEU	0	-0.033	-0.019	16.721	-0.015	-0.015	0.000	0.000	0.000
182	A	209	ASP	-1	-0.801	-0.893	19.185	-0.017	-0.017	0.000	0.000	0.000
183	A	210	ARG	1	0.781	0.868	22.962	0.027	0.027	0.000	0.000	0.000
184	A	211	LEU	0	-0.042	-0.017	24.933	-0.007	-0.007	0.000	0.000	0.000
185	A	212	TYR	0	-0.070	-0.028	26.707	0.012	0.012	0.000	0.000	0.000
186	A	213	SER	0	0.022	-0.015	29.046	-0.008	-0.008	0.000	0.000	0.000
187	A	214	LYS	1	0.818	0.910	31.749	0.059	0.059	0.000	0.000	0.000
188	A	215	ASN	0	-0.018	-0.010	33.938	-0.008	-0.008	0.000	0.000	0.000
189	A	216	VAL	0	-0.009	0.003	34.351	0.002	0.002	0.000	0.000	0.000
190	A	217	THR	0	-0.021	-0.003	36.803	0.005	0.005	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:13:GLY)