FMO DATABASE

FMODB ID: 94842

Calculation Name: 1A3A-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1A3A

Chain ID: A

ChEMBL ID:

UniProt ID: P00550

Base Structure: X-ray

Registration Date: 2023-06-22

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	OptAll
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	145
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1363951.079229
FMO2-HF: Nuclear repulsion	1308458.048372
FMO2-HF: Total energy	-55493.030857
FMO2-MP2: Total energy	-55657.565591

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:4:LEU)

Summations of interaction energy for fragment #1(A:4:LEU)

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.
-3.019	0.853	1.053	-1.442	-3.481	-0.001

Interaction energy analysis for fragmet #1(A:4:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.005 / 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].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	6	LYS	1	0.969	0.988	3.864	0.483	2.235	-0.021	-0.894	-0.837	-0.001
4	A	7	LEU	0	-0.006	0.001	7.138	-0.223	-0.223	0.000	0.000	0.000	0.000
5	A	8	GLY	0	0.041	0.012	9.930	0.083	0.083	0.000	0.000	0.000	0.000
6	A	9	ALA	0	0.046	0.013	13.693	-0.045	-0.045	0.000	0.000	0.000	0.000
7	A	10	GLU	-1	-0.927	-0.943	13.839	-0.064	-0.064	0.000	0.000	0.000	0.000
8	A	11	ASN	0	-0.040	-0.037	9.712	0.051	0.051	0.000	0.000	0.000	0.000
9	A	12	ILE	0	0.006	0.015	13.213	0.010	0.010	0.000	0.000	0.000	0.000
10	A	13	PHE	0	-0.034	-0.030	15.574	-0.013	-0.013	0.000	0.000	0.000	0.000
11	A	14	LEU	0	0.041	0.019	18.494	-0.007	-0.007	0.000	0.000	0.000	0.000
12	A	15	GLY	0	-0.010	-0.005	20.939	-0.013	-0.013	0.000	0.000	0.000	0.000
13	A	16	ARG	1	0.817	0.941	20.639	0.017	0.017	0.000	0.000	0.000	0.000
14	A	17	LYS	1	0.841	0.880	23.620	-0.007	-0.007	0.000	0.000	0.000	0.000
15	A	18	ALA	0	-0.028	-0.021	24.905	-0.005	-0.005	0.000	0.000	0.000	0.000
16	A	19	ALA	0	0.017	0.014	26.832	0.005	0.005	0.000	0.000	0.000	0.000
17	A	20	THR	0	-0.016	-0.007	27.415	-0.004	-0.004	0.000	0.000	0.000	0.000
18	A	21	LYS	1	0.884	0.938	22.517	0.109	0.109	0.000	0.000	0.000	0.000
19	A	22	GLU	-1	-0.838	-0.931	22.491	-0.117	-0.117	0.000	0.000	0.000	0.000
20	A	23	GLU	-1	-0.867	-0.926	23.307	-0.065	-0.065	0.000	0.000	0.000	0.000
21	A	24	ALA	0	0.020	0.010	21.069	-0.004	-0.004	0.000	0.000	0.000	0.000
22	A	25	ILE	0	-0.022	-0.014	18.159	-0.013	-0.013	0.000	0.000	0.000	0.000
23	A	26	ARG	1	0.890	0.934	18.839	0.105	0.105	0.000	0.000	0.000	0.000
24	A	27	PHE	0	0.009	0.007	19.280	-0.009	-0.009	0.000	0.000	0.000	0.000
25	A	28	ALA	0	0.054	0.027	15.553	0.000	0.000	0.000	0.000	0.000	0.000
26	A	29	GLY	0	0.045	0.006	16.007	-0.027	-0.027	0.000	0.000	0.000	0.000
27	A	30	GLU	-1	-0.883	-0.949	16.897	-0.127	-0.127	0.000	0.000	0.000	0.000
28	A	31	GLN	0	-0.016	-0.004	16.966	0.019	0.019	0.000	0.000	0.000	0.000
29	A	32	LEU	0	0.010	0.011	10.865	-0.008	-0.008	0.000	0.000	0.000	0.000
30	A	33	VAL	0	-0.032	-0.005	14.081	-0.026	-0.026	0.000	0.000	0.000	0.000
31	A	34	LYS	1	0.860	0.927	16.714	0.082	0.082	0.000	0.000	0.000	0.000
32	A	35	GLY	0	0.034	0.029	14.527	0.022	0.022	0.000	0.000	0.000	0.000
33	A	36	GLY	0	0.008	0.004	13.625	-0.018	-0.018	0.000	0.000	0.000	0.000
34	A	37	TYR	0	-0.098	-0.063	8.363	-0.066	-0.066	0.000	0.000	0.000	0.000
35	A	38	VAL	0	-0.027	-0.012	10.796	-0.104	-0.104	0.000	0.000	0.000	0.000
36	A	39	GLU	-1	-0.816	-0.887	13.460	-0.185	-0.185	0.000	0.000	0.000	0.000
37	A	40	PRO	0	0.014	-0.017	17.120	-0.016	-0.016	0.000	0.000	0.000	0.000
38	A	41	GLU	-1	-0.805	-0.886	19.790	-0.195	-0.195	0.000	0.000	0.000	0.000
39	A	42	TYR	0	-0.030	-0.042	10.748	-0.017	-0.017	0.000	0.000	0.000	0.000
40	A	43	VAL	0	-0.003	-0.001	16.697	-0.010	-0.010	0.000	0.000	0.000	0.000
41	A	44	GLN	0	-0.077	-0.039	18.709	0.018	0.018	0.000	0.000	0.000	0.000
42	A	45	ALA	0	0.052	0.026	16.508	0.002	0.002	0.000	0.000	0.000	0.000
43	A	46	MET	0	-0.088	-0.029	14.682	-0.022	-0.022	0.000	0.000	0.000	0.000
44	A	47	LEU	0	-0.029	0.000	17.156	0.014	0.014	0.000	0.000	0.000	0.000
45	A	48	ASP	-1	-0.826	-0.918	20.012	-0.174	-0.174	0.000	0.000	0.000	0.000
46	A	49	ARG	1	0.839	0.922	13.439	0.353	0.353	0.000	0.000	0.000	0.000
47	A	50	GLU	-1	-0.745	-0.839	18.517	-0.158	-0.158	0.000	0.000	0.000	0.000
48	A	51	LYS	1	0.820	0.909	20.646	0.135	0.135	0.000	0.000	0.000	0.000
49	A	52	LEU	0	-0.035	-0.010	20.329	0.010	0.010	0.000	0.000	0.000	0.000
50	A	53	THR	0	-0.118	-0.077	17.843	-0.005	-0.005	0.000	0.000	0.000	0.000
51	A	54	PRO	0	0.013	0.018	18.679	-0.023	-0.023	0.000	0.000	0.000	0.000
52	A	55	THR	0	-0.066	-0.055	15.850	-0.010	-0.010	0.000	0.000	0.000	0.000
53	A	56	TYR	0	-0.017	-0.031	16.873	-0.012	-0.012	0.000	0.000	0.000	0.000
54	A	57	LEU	0	-0.050	-0.036	13.413	-0.020	-0.020	0.000	0.000	0.000	0.000
55	A	58	GLY	0	0.059	0.048	18.115	0.007	0.007	0.000	0.000	0.000	0.000
56	A	59	GLU	-1	-0.888	-0.953	19.196	-0.002	-0.002	0.000	0.000	0.000	0.000
57	A	60	SER	0	0.019	0.030	19.698	0.015	0.015	0.000	0.000	0.000	0.000
58	A	61	ILE	0	0.001	0.001	14.192	0.001	0.001	0.000	0.000	0.000	0.000
59	A	62	ALA	0	0.032	0.019	16.300	-0.015	-0.015	0.000	0.000	0.000	0.000
60	A	63	VAL	0	-0.026	-0.003	11.510	-0.005	-0.005	0.000	0.000	0.000	0.000
61	A	64	PRO	0	0.061	0.050	13.281	-0.065	-0.065	0.000	0.000	0.000	0.000
62	A	65	HIS	1	0.860	0.899	10.827	0.389	0.389	0.000	0.000	0.000	0.000
63	A	66	GLY	0	0.078	0.040	12.254	0.053	0.053	0.000	0.000	0.000	0.000
64	A	67	THR	0	-0.028	-0.028	13.533	-0.024	-0.024	0.000	0.000	0.000	0.000
65	A	68	VAL	0	-0.001	0.000	13.276	-0.038	-0.038	0.000	0.000	0.000	0.000
66	A	69	GLU	-1	-0.848	-0.927	14.405	-0.277	-0.277	0.000	0.000	0.000	0.000
67	A	70	ALA	0	-0.001	0.005	15.118	0.010	0.010	0.000	0.000	0.000	0.000
68	A	71	LYS	1	0.865	0.950	11.080	0.341	0.341	0.000	0.000	0.000	0.000
69	A	72	ASP	-1	-0.888	-0.961	11.644	-0.432	-0.432	0.000	0.000	0.000	0.000
70	A	73	ARG	1	0.775	0.870	13.805	0.254	0.254	0.000	0.000	0.000	0.000
71	A	74	VAL	0	-0.016	0.005	8.165	0.008	0.008	0.000	0.000	0.000	0.000
72	A	75	LEU	0	-0.009	0.006	11.225	-0.007	-0.007	0.000	0.000	0.000	0.000
73	A	76	LYS	1	0.762	0.873	7.639	0.374	0.374	0.000	0.000	0.000	0.000
74	A	77	THR	0	0.021	0.006	2.376	-0.710	0.127	1.000	-0.327	-1.510	0.001
75	A	78	GLY	0	-0.029	-0.021	4.917	-0.048	0.011	-0.001	-0.010	-0.047	0.000
76	A	79	VAL	0	0.003	0.011	6.244	-0.082	-0.082	0.000	0.000	0.000	0.000
77	A	80	VAL	0	-0.028	-0.007	9.020	0.112	0.112	0.000	0.000	0.000	0.000
78	A	81	PHE	0	0.052	0.031	11.873	-0.017	-0.017	0.000	0.000	0.000	0.000
79	A	82	CYS	0	-0.063	-0.028	13.280	0.015	0.015	0.000	0.000	0.000	0.000
80	A	83	GLN	0	0.024	0.012	16.916	-0.023	-0.023	0.000	0.000	0.000	0.000
81	A	84	TYR	0	-0.027	-0.024	19.076	-0.006	-0.006	0.000	0.000	0.000	0.000
82	A	85	PRO	0	0.020	0.010	22.352	-0.004	-0.004	0.000	0.000	0.000	0.000
83	A	86	GLU	-1	-0.854	-0.918	24.594	0.011	0.011	0.000	0.000	0.000	0.000
84	A	87	GLY	0	0.005	0.013	24.206	-0.003	-0.003	0.000	0.000	0.000	0.000
85	A	88	VAL	0	-0.050	-0.026	23.264	-0.004	-0.004	0.000	0.000	0.000	0.000
86	A	89	ARG	1	0.867	0.945	24.159	0.056	0.056	0.000	0.000	0.000	0.000
87	A	90	PHE	0	-0.037	-0.046	19.293	-0.011	-0.011	0.000	0.000	0.000	0.000
88	A	91	GLY	0	0.018	0.019	23.506	-0.016	-0.016	0.000	0.000	0.000	0.000
89	A	92	GLU	-1	-0.884	-0.953	24.841	-0.085	-0.085	0.000	0.000	0.000	0.000
90	A	93	GLU	-1	-0.961	-0.965	28.543	-0.035	-0.035	0.000	0.000	0.000	0.000
91	A	94	GLU	-1	-0.962	-0.994	29.114	-0.030	-0.030	0.000	0.000	0.000	0.000
92	A	95	ASP	-1	-0.888	-0.952	29.063	-0.013	-0.013	0.000	0.000	0.000	0.000
93	A	96	ASP	-1	-0.856	-0.866	24.943	-0.052	-0.052	0.000	0.000	0.000	0.000
94	A	97	ILE	0	-0.021	-0.029	24.674	-0.011	-0.011	0.000	0.000	0.000	0.000
95	A	98	ALA	0	-0.029	-0.007	19.625	0.005	0.005	0.000	0.000	0.000	0.000
96	A	99	ARG	1	0.772	0.808	20.631	-0.036	-0.036	0.000	0.000	0.000	0.000
97	A	100	LEU	0	-0.039	-0.005	15.451	0.017	0.017	0.000	0.000	0.000	0.000
98	A	101	VAL	0	0.007	0.007	16.374	-0.027	-0.027	0.000	0.000	0.000	0.000
99	A	102	ILE	0	0.004	-0.004	9.765	0.012	0.012	0.000	0.000	0.000	0.000
100	A	103	GLY	0	0.034	0.024	11.990	-0.069	-0.069	0.000	0.000	0.000	0.000
101	A	104	ILE	0	-0.030	-0.022	6.879	-0.067	-0.067	0.000	0.000	0.000	0.000
102	A	105	ALA	0	0.016	0.034	8.372	0.124	0.124	0.000	0.000	0.000	0.000
103	A	106	ALA	0	0.013	-0.013	5.070	-0.451	-0.451	0.000	0.000	0.000	0.000
104	A	107	ARG	1	0.882	0.950	6.124	1.031	1.031	0.000	0.000	0.000	0.000
105	A	108	ASN	0	-0.015	-0.042	7.672	0.052	0.052	0.000	0.000	0.000	0.000
106	A	109	ASN	0	0.034	0.010	8.819	0.060	0.060	0.000	0.000	0.000	0.000
107	A	110	GLU	-1	-0.809	-0.892	3.597	-1.248	-1.035	0.004	-0.032	-0.185	0.000
108	A	111	HIS	0	0.036	0.013	4.867	-0.389	-0.329	-0.001	-0.002	-0.057	0.000
109	A	112	ILE	0	0.004	0.012	7.202	0.021	0.021	0.000	0.000	0.000	0.000
110	A	113	GLN	0	0.029	0.021	4.360	-0.094	0.044	-0.001	-0.009	-0.128	0.000
111	A	114	VAL	0	-0.011	-0.002	2.935	-0.818	-0.176	0.075	-0.146	-0.570	-0.001
112	A	115	ILE	0	0.064	0.026	5.105	0.301	0.342	-0.001	-0.002	-0.038	0.000
113	A	116	THR	0	-0.026	-0.008	8.029	0.194	0.194	0.000	0.000	0.000	0.000
114	A	117	SER	0	-0.085	-0.055	4.272	0.373	0.503	-0.001	-0.020	-0.109	0.000
115	A	118	LEU	0	-0.014	-0.015	6.105	0.321	0.321	0.000	0.000	0.000	0.000
116	A	119	THR	0	0.032	0.002	8.238	0.083	0.083	0.000	0.000	0.000	0.000
117	A	120	ASN	0	-0.098	-0.053	9.626	0.047	0.047	0.000	0.000	0.000	0.000
118	A	121	ALA	0	-0.058	-0.030	9.329	0.109	0.109	0.000	0.000	0.000	0.000
119	A	122	LEU	0	-0.033	-0.022	11.254	0.019	0.019	0.000	0.000	0.000	0.000
120	A	123	ASP	-1	-0.875	-0.925	14.020	0.144	0.144	0.000	0.000	0.000	0.000
121	A	124	ASP	-1	-0.827	-0.922	16.608	0.143	0.143	0.000	0.000	0.000	0.000
122	A	125	GLU	-1	-0.869	-0.935	18.683	0.068	0.068	0.000	0.000	0.000	0.000
123	A	126	SER	0	0.002	-0.001	21.199	0.004	0.004	0.000	0.000	0.000	0.000
124	A	127	VAL	0	-0.051	-0.010	14.805	0.007	0.007	0.000	0.000	0.000	0.000
125	A	128	ILE	0	-0.001	0.009	17.022	0.009	0.009	0.000	0.000	0.000	0.000
126	A	129	GLU	-1	-0.780	-0.854	18.571	0.054	0.054	0.000	0.000	0.000	0.000
127	A	130	ARG	1	0.836	0.910	19.892	-0.198	-0.198	0.000	0.000	0.000	0.000
128	A	131	LEU	0	-0.020	-0.004	14.113	0.000	0.000	0.000	0.000	0.000	0.000
129	A	132	ALA	0	0.003	0.006	18.190	-0.011	-0.011	0.000	0.000	0.000	0.000
130	A	133	HIS	0	-0.017	-0.011	20.591	-0.019	-0.019	0.000	0.000	0.000	0.000
131	A	134	THR	0	-0.039	-0.023	19.666	-0.009	-0.009	0.000	0.000	0.000	0.000
132	A	135	THR	0	-0.006	-0.008	22.060	0.000	0.000	0.000	0.000	0.000	0.000
133	A	136	SER	0	0.006	0.010	21.760	0.003	0.003	0.000	0.000	0.000	0.000
134	A	137	VAL	0	0.040	-0.003	17.164	0.014	0.014	0.000	0.000	0.000	0.000
135	A	138	ASP	-1	-0.907	-0.953	17.077	0.296	0.296	0.000	0.000	0.000	0.000
136	A	139	GLU	-1	-0.819	-0.891	17.522	0.236	0.236	0.000	0.000	0.000	0.000
137	A	140	VAL	0	0.004	-0.003	13.789	0.035	0.035	0.000	0.000	0.000	0.000
138	A	141	LEU	0	-0.063	-0.031	12.382	0.084	0.084	0.000	0.000	0.000	0.000
139	A	142	GLU	-1	-0.978	-0.985	12.976	0.459	0.459	0.000	0.000	0.000	0.000
140	A	143	LEU	0	-0.020	-0.011	14.540	0.052	0.052	0.000	0.000	0.000	0.000
141	A	144	LEU	0	0.018	0.017	9.682	0.046	0.046	0.000	0.000	0.000	0.000
142	A	145	ALA	0	-0.036	-0.001	9.294	0.389	0.389	0.000	0.000	0.000	0.000
143	A	146	GLY	0	0.013	0.009	10.478	0.104	0.104	0.000	0.000	0.000	0.000
144	A	147	ARG	1	0.884	0.954	4.811	-2.933	-2.933	0.000	0.000	0.000	0.000
145	A	148	LYS	1	0.845	0.929	4.909	-0.903	-0.903	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:LEU)