FMO DATABASE

FMODB ID: YY972

Calculation Name: 1AYY-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1AYY

Chain ID: A

ChEMBL ID:

UniProt ID: Q47898

Base Structure: X-ray

Registration Date: 2023-03-13

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	138
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1149250.615779
FMO2-HF: Nuclear repulsion	1095245.114
FMO2-HF: Total energy	-54005.501779
FMO2-MP2: Total energy	-54161.279756

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:2:THR)

Summations of interaction energy for fragment #1(A:2:THR)

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.
-10.418	-6.023	1.625	-2.367	-3.653	0.022

Interaction energy analysis for fragmet #1(A:2:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.007 / q_NPA : -0.022

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	4	LYS	1	0.956	1.010	2.443	-10.481	-6.111	1.626	-2.359	-3.638	0.022
4	A	5	PRO	0	0.010	-0.008	5.008	-0.128	-0.103	-0.001	-0.008	-0.015	0.000
5	A	6	ILE	0	0.008	-0.013	6.625	-0.257	-0.257	0.000	0.000	0.000	0.000
6	A	7	VAL	0	-0.010	0.000	8.913	0.091	0.091	0.000	0.000	0.000	0.000
7	A	8	LEU	0	-0.015	-0.009	11.853	-0.046	-0.046	0.000	0.000	0.000	0.000
8	A	9	SER	0	0.007	-0.011	14.312	0.017	0.017	0.000	0.000	0.000	0.000
9	A	10	THR	0	0.000	0.004	18.073	-0.009	-0.009	0.000	0.000	0.000	0.000
10	A	11	TRP	0	0.028	0.008	21.072	-0.001	-0.001	0.000	0.000	0.000	0.000
11	A	12	ASN	0	0.037	0.013	22.682	0.000	0.000	0.000	0.000	0.000	0.000
12	A	13	PHE	0	0.039	0.034	24.255	-0.003	-0.003	0.000	0.000	0.000	0.000
13	A	14	GLY	0	0.039	0.015	21.163	0.005	0.005	0.000	0.000	0.000	0.000
14	A	15	LEU	0	-0.046	-0.023	19.726	0.002	0.002	0.000	0.000	0.000	0.000
15	A	16	HIS	0	0.052	0.004	20.641	0.000	0.000	0.000	0.000	0.000	0.000
16	A	17	ALA	0	0.039	0.029	21.431	0.005	0.005	0.000	0.000	0.000	0.000
17	A	18	ASN	0	0.016	0.013	16.741	0.027	0.027	0.000	0.000	0.000	0.000
18	A	19	VAL	0	-0.019	-0.001	17.479	0.012	0.012	0.000	0.000	0.000	0.000
19	A	20	GLU	-1	-0.776	-0.872	19.686	0.055	0.055	0.000	0.000	0.000	0.000
20	A	21	ALA	0	0.017	0.021	16.190	0.014	0.014	0.000	0.000	0.000	0.000
21	A	22	TRP	0	0.033	0.006	10.790	0.052	0.052	0.000	0.000	0.000	0.000
22	A	23	LYS	1	0.780	0.901	15.941	-0.029	-0.029	0.000	0.000	0.000	0.000
23	A	24	VAL	0	0.014	0.019	16.441	0.002	0.002	0.000	0.000	0.000	0.000
24	A	25	LEU	0	0.021	0.016	11.199	0.031	0.031	0.000	0.000	0.000	0.000
25	A	26	SER	0	-0.077	-0.051	12.829	0.052	0.052	0.000	0.000	0.000	0.000
26	A	27	LYS	1	0.849	0.921	14.077	-0.102	-0.102	0.000	0.000	0.000	0.000
27	A	28	GLY	0	-0.022	-0.006	12.636	-0.003	-0.003	0.000	0.000	0.000	0.000
28	A	29	GLY	0	-0.027	-0.014	13.708	0.017	0.017	0.000	0.000	0.000	0.000
29	A	30	LYS	1	0.877	0.911	13.939	-0.211	-0.211	0.000	0.000	0.000	0.000
30	A	31	ALA	0	0.047	0.006	11.804	-0.039	-0.039	0.000	0.000	0.000	0.000
31	A	32	LEU	0	0.049	0.029	13.851	-0.039	-0.039	0.000	0.000	0.000	0.000
32	A	33	ASP	-1	-0.802	-0.888	17.313	0.141	0.141	0.000	0.000	0.000	0.000
33	A	34	ALA	0	-0.008	-0.009	15.108	-0.027	-0.027	0.000	0.000	0.000	0.000
34	A	35	VAL	0	0.006	-0.012	15.204	-0.027	-0.027	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.775	-0.848	17.823	0.094	0.094	0.000	0.000	0.000	0.000
36	A	37	LYS	1	0.758	0.851	20.853	-0.140	-0.140	0.000	0.000	0.000	0.000
37	A	38	GLY	0	0.004	0.015	20.023	-0.012	-0.012	0.000	0.000	0.000	0.000
38	A	39	VAL	0	0.021	-0.003	20.668	-0.011	-0.011	0.000	0.000	0.000	0.000
39	A	40	ARG	1	0.828	0.896	23.040	-0.065	-0.065	0.000	0.000	0.000	0.000
40	A	41	LEU	0	-0.062	-0.013	24.407	-0.005	-0.005	0.000	0.000	0.000	0.000
41	A	42	VAL	0	0.007	-0.013	24.533	-0.005	-0.005	0.000	0.000	0.000	0.000
42	A	43	GLU	-1	-0.768	-0.869	27.369	0.058	0.058	0.000	0.000	0.000	0.000
43	A	44	ASP	-1	-0.809	-0.908	29.467	0.044	0.044	0.000	0.000	0.000	0.000
44	A	45	ASP	-1	-0.840	-0.892	30.238	0.017	0.017	0.000	0.000	0.000	0.000
45	A	46	PRO	0	-0.028	-0.009	32.105	0.000	0.000	0.000	0.000	0.000	0.000
46	A	47	THR	0	-0.099	-0.085	33.109	-0.002	-0.002	0.000	0.000	0.000	0.000
47	A	48	GLU	-1	-0.862	-0.932	29.088	0.013	0.013	0.000	0.000	0.000	0.000
48	A	49	ARG	1	0.782	0.854	32.225	-0.012	-0.012	0.000	0.000	0.000	0.000
49	A	50	SER	0	-0.115	-0.064	30.094	0.000	0.000	0.000	0.000	0.000	0.000
50	A	51	VAL	0	-0.033	-0.024	27.169	0.003	0.003	0.000	0.000	0.000	0.000
51	A	52	GLY	0	0.062	0.035	30.442	-0.001	-0.001	0.000	0.000	0.000	0.000
52	A	53	TYR	0	-0.055	-0.028	32.288	-0.003	-0.003	0.000	0.000	0.000	0.000
53	A	54	GLY	0	0.041	0.027	34.224	-0.001	-0.001	0.000	0.000	0.000	0.000
54	A	55	GLY	0	-0.030	0.002	35.004	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	56	ARG	1	0.794	0.866	35.614	-0.015	-0.015	0.000	0.000	0.000	0.000
56	A	57	PRO	0	-0.029	-0.009	37.680	0.001	0.001	0.000	0.000	0.000	0.000
57	A	58	ASP	-1	-0.774	-0.888	40.277	0.021	0.021	0.000	0.000	0.000	0.000
58	A	59	ARG	1	0.916	0.939	41.465	-0.017	-0.017	0.000	0.000	0.000	0.000
59	A	60	ASP	-1	-0.908	-0.965	44.669	0.017	0.017	0.000	0.000	0.000	0.000
60	A	61	GLY	0	-0.067	-0.029	44.619	0.000	0.000	0.000	0.000	0.000	0.000
61	A	62	ARG	1	0.801	0.872	42.543	-0.024	-0.024	0.000	0.000	0.000	0.000
62	A	63	VAL	0	0.003	-0.005	36.879	0.000	0.000	0.000	0.000	0.000	0.000
63	A	64	THR	0	-0.046	-0.009	36.730	0.001	0.001	0.000	0.000	0.000	0.000
64	A	65	LEU	0	-0.034	-0.004	32.082	0.000	0.000	0.000	0.000	0.000	0.000
65	A	66	ASP	-1	-0.835	-0.913	30.543	0.039	0.039	0.000	0.000	0.000	0.000
66	A	67	ALA	0	-0.024	-0.013	26.622	0.001	0.001	0.000	0.000	0.000	0.000
67	A	68	CYS	0	-0.024	-0.027	23.218	-0.002	-0.002	0.000	0.000	0.000	0.000
68	A	69	ILE	0	-0.044	-0.015	20.568	0.003	0.003	0.000	0.000	0.000	0.000
69	A	70	MET	0	0.004	-0.004	18.064	-0.011	-0.011	0.000	0.000	0.000	0.000
70	A	71	ASP	-1	-0.842	-0.889	16.969	0.219	0.219	0.000	0.000	0.000	0.000
71	A	72	GLU	-1	-0.854	-0.918	13.102	0.327	0.327	0.000	0.000	0.000	0.000
72	A	73	ASN	0	-0.093	-0.056	14.683	0.021	0.021	0.000	0.000	0.000	0.000
73	A	74	TYR	0	-0.015	-0.017	16.633	-0.028	-0.028	0.000	0.000	0.000	0.000
74	A	75	ASN	0	-0.049	-0.009	19.598	-0.031	-0.031	0.000	0.000	0.000	0.000
75	A	76	ILE	0	0.015	-0.020	21.272	0.008	0.008	0.000	0.000	0.000	0.000
76	A	77	GLY	0	0.044	0.020	23.625	-0.004	-0.004	0.000	0.000	0.000	0.000
77	A	78	SER	0	-0.061	-0.028	25.575	0.001	0.001	0.000	0.000	0.000	0.000
78	A	79	VAL	0	0.007	-0.005	28.179	-0.002	-0.002	0.000	0.000	0.000	0.000
79	A	80	ALA	0	0.015	0.004	30.909	0.000	0.000	0.000	0.000	0.000	0.000
80	A	81	CYS	0	-0.024	-0.021	33.395	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	82	MET	0	0.017	0.034	32.691	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	83	GLU	-1	-0.759	-0.861	36.565	0.026	0.026	0.000	0.000	0.000	0.000
83	A	84	HIS	0	-0.014	-0.025	38.961	0.002	0.002	0.000	0.000	0.000	0.000
84	A	85	ILE	0	0.032	0.027	33.497	0.000	0.000	0.000	0.000	0.000	0.000
85	A	86	LYS	1	0.871	0.945	33.051	-0.033	-0.033	0.000	0.000	0.000	0.000
86	A	87	ASN	0	-0.029	-0.024	29.130	-0.001	-0.001	0.000	0.000	0.000	0.000
87	A	88	PRO	0	0.036	0.014	29.175	0.004	0.004	0.000	0.000	0.000	0.000
88	A	89	ILE	0	0.024	0.012	22.767	0.004	0.004	0.000	0.000	0.000	0.000
89	A	90	SER	0	-0.017	-0.030	25.960	0.006	0.006	0.000	0.000	0.000	0.000
90	A	91	VAL	0	-0.015	0.003	27.753	0.003	0.003	0.000	0.000	0.000	0.000
91	A	92	ALA	0	-0.004	0.009	26.582	0.001	0.001	0.000	0.000	0.000	0.000
92	A	93	ARG	1	0.815	0.877	22.227	-0.133	-0.133	0.000	0.000	0.000	0.000
93	A	94	ALA	0	-0.013	-0.004	26.113	0.004	0.004	0.000	0.000	0.000	0.000
94	A	95	VAL	0	-0.029	-0.012	29.526	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	96	MET	0	0.009	0.008	22.022	0.002	0.002	0.000	0.000	0.000	0.000
96	A	97	GLU	-1	-0.909	-0.932	24.666	0.122	0.122	0.000	0.000	0.000	0.000
97	A	98	LYS	1	0.818	0.897	27.960	-0.091	-0.091	0.000	0.000	0.000	0.000
98	A	99	THR	0	-0.035	-0.015	31.065	-0.009	-0.009	0.000	0.000	0.000	0.000
99	A	100	PRO	0	-0.024	0.008	31.202	0.004	0.004	0.000	0.000	0.000	0.000
100	A	101	HIS	0	-0.006	0.000	32.457	0.000	0.000	0.000	0.000	0.000	0.000
101	A	102	VAL	0	0.066	0.023	27.557	0.004	0.004	0.000	0.000	0.000	0.000
102	A	103	MET	0	-0.044	-0.028	29.059	0.002	0.002	0.000	0.000	0.000	0.000
103	A	104	LEU	0	-0.018	0.015	31.535	-0.003	-0.003	0.000	0.000	0.000	0.000
104	A	105	VAL	0	0.011	-0.012	33.955	0.001	0.001	0.000	0.000	0.000	0.000
105	A	106	GLY	0	0.026	0.025	36.546	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	107	ASP	-1	-0.903	-0.963	39.152	0.031	0.031	0.000	0.000	0.000	0.000
107	A	108	GLY	0	0.047	0.030	39.871	0.001	0.001	0.000	0.000	0.000	0.000
108	A	109	ALA	0	-0.025	-0.012	35.194	0.003	0.003	0.000	0.000	0.000	0.000
109	A	110	LEU	0	0.003	-0.003	36.694	0.002	0.002	0.000	0.000	0.000	0.000
110	A	111	GLU	-1	-0.925	-0.962	38.761	0.034	0.034	0.000	0.000	0.000	0.000
111	A	112	PHE	0	0.004	0.006	32.542	0.000	0.000	0.000	0.000	0.000	0.000
112	A	113	ALA	0	0.047	0.030	35.355	0.002	0.002	0.000	0.000	0.000	0.000
113	A	114	LEU	0	-0.023	-0.017	36.305	0.001	0.001	0.000	0.000	0.000	0.000
114	A	115	SER	0	-0.116	-0.059	38.246	0.000	0.000	0.000	0.000	0.000	0.000
115	A	116	GLN	0	-0.041	-0.028	33.848	0.005	0.005	0.000	0.000	0.000	0.000
116	A	117	GLY	0	-0.029	-0.004	35.717	0.002	0.002	0.000	0.000	0.000	0.000
117	A	118	PHE	0	-0.064	-0.020	30.548	0.000	0.000	0.000	0.000	0.000	0.000
118	A	119	LYS	1	0.865	0.913	36.469	-0.033	-0.033	0.000	0.000	0.000	0.000
119	A	120	LYS	1	0.937	0.974	38.303	-0.028	-0.028	0.000	0.000	0.000	0.000
120	A	121	GLU	-1	-0.853	-0.926	37.718	0.031	0.031	0.000	0.000	0.000	0.000
121	A	122	ASN	0	-0.004	-0.014	40.683	0.001	0.001	0.000	0.000	0.000	0.000
122	A	123	LEU	0	0.000	0.000	35.967	-0.001	-0.001	0.000	0.000	0.000	0.000
123	A	124	LEU	0	0.039	0.033	38.916	-0.001	-0.001	0.000	0.000	0.000	0.000
124	A	125	THR	0	0.062	0.031	39.083	-0.001	-0.001	0.000	0.000	0.000	0.000
125	A	126	ALA	0	0.025	-0.001	42.033	-0.001	-0.001	0.000	0.000	0.000	0.000
126	A	127	GLU	-1	-0.823	-0.909	40.106	0.012	0.012	0.000	0.000	0.000	0.000
127	A	128	SER	0	0.053	0.027	38.918	-0.001	-0.001	0.000	0.000	0.000	0.000
128	A	129	GLU	-1	-0.824	-0.881	42.011	0.013	0.013	0.000	0.000	0.000	0.000
129	A	130	LYS	1	0.749	0.851	45.316	-0.013	-0.013	0.000	0.000	0.000	0.000
130	A	131	GLU	-1	-0.723	-0.809	40.818	0.012	0.012	0.000	0.000	0.000	0.000
131	A	132	TRP	0	-0.007	0.017	43.928	-0.001	-0.001	0.000	0.000	0.000	0.000
132	A	133	LYS	1	0.872	0.913	45.391	-0.013	-0.013	0.000	0.000	0.000	0.000
133	A	134	GLU	-1	-0.933	-0.965	47.464	0.008	0.008	0.000	0.000	0.000	0.000
134	A	135	TRP	0	-0.019	-0.003	44.792	0.000	0.000	0.000	0.000	0.000	0.000
135	A	136	LEU	0	-0.053	-0.030	47.423	0.000	0.000	0.000	0.000	0.000	0.000
136	A	137	LYS	1	0.891	0.966	49.868	-0.009	-0.009	0.000	0.000	0.000	0.000
137	A	138	THR	0	-0.015	-0.006	48.328	0.000	0.000	0.000	0.000	0.000	0.000
138	A	139	SER	0	-0.052	-0.010	47.515	0.000	0.000	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:THR)