FMO DATABASE

FMODB ID: 39J9L

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	OptH
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	-1360764.505848
FMO2-HF: Nuclear repulsion	1305272.465906
FMO2-HF: Total energy	-55492.039942
FMO2-MP2: Total energy	-55656.557588

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.
-3.303	0.541	1.176	-1.61	-3.41	0.002

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 : -0.003 / q_NPA : -0.005

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	0.972	0.977	3.795	-0.135	1.898	-0.036	-1.001	-0.996	0.000
4	A	7	LEU	0	0.005	0.001	6.918	-0.217	-0.217	0.000	0.000	0.000	0.000
5	A	8	GLY	0	0.025	0.014	10.067	0.075	0.075	0.000	0.000	0.000	0.000
6	A	9	ALA	0	0.056	0.019	13.605	-0.041	-0.041	0.000	0.000	0.000	0.000
7	A	10	GLU	-1	-0.969	-0.978	15.085	-0.051	-0.051	0.000	0.000	0.000	0.000
8	A	11	ASN	0	-0.062	-0.042	9.783	0.030	0.030	0.000	0.000	0.000	0.000
9	A	12	ILE	0	0.018	0.018	13.761	0.006	0.006	0.000	0.000	0.000	0.000
10	A	13	PHE	0	-0.033	-0.025	15.813	-0.022	-0.022	0.000	0.000	0.000	0.000
11	A	14	LEU	0	0.009	-0.001	18.697	-0.005	-0.005	0.000	0.000	0.000	0.000
12	A	15	GLY	0	0.009	0.009	21.282	-0.013	-0.013	0.000	0.000	0.000	0.000
13	A	16	ARG	1	0.863	0.950	21.333	-0.003	-0.003	0.000	0.000	0.000	0.000
14	A	17	LYS	1	0.972	0.966	24.244	-0.013	-0.013	0.000	0.000	0.000	0.000
15	A	18	ALA	0	-0.014	-0.014	25.282	-0.007	-0.007	0.000	0.000	0.000	0.000
16	A	19	ALA	0	0.010	0.025	27.195	0.004	0.004	0.000	0.000	0.000	0.000
17	A	20	THR	0	-0.007	0.000	27.838	-0.003	-0.003	0.000	0.000	0.000	0.000
18	A	21	LYS	1	0.978	0.987	22.959	0.101	0.101	0.000	0.000	0.000	0.000
19	A	22	GLU	-1	-0.907	-0.963	22.862	-0.099	-0.099	0.000	0.000	0.000	0.000
20	A	23	GLU	-1	-0.921	-0.957	23.653	-0.055	-0.055	0.000	0.000	0.000	0.000
21	A	24	ALA	0	0.019	0.010	21.184	-0.004	-0.004	0.000	0.000	0.000	0.000
22	A	25	ILE	0	-0.030	-0.017	18.425	-0.013	-0.013	0.000	0.000	0.000	0.000
23	A	26	ARG	1	0.951	0.982	19.080	0.100	0.100	0.000	0.000	0.000	0.000
24	A	27	PHE	0	0.009	0.017	19.798	-0.011	-0.011	0.000	0.000	0.000	0.000
25	A	28	ALA	0	0.016	-0.005	15.683	-0.006	-0.006	0.000	0.000	0.000	0.000
26	A	29	GLY	0	0.049	-0.005	16.062	-0.033	-0.033	0.000	0.000	0.000	0.000
27	A	30	GLU	-1	-0.964	-0.997	16.756	-0.129	-0.129	0.000	0.000	0.000	0.000
28	A	31	GLN	0	-0.030	-0.009	16.721	0.002	0.002	0.000	0.000	0.000	0.000
29	A	32	LEU	0	-0.032	-0.004	10.572	-0.019	-0.019	0.000	0.000	0.000	0.000
30	A	33	VAL	0	-0.031	-0.007	13.641	-0.039	-0.039	0.000	0.000	0.000	0.000
31	A	34	LYS	1	0.938	0.962	16.267	0.076	0.076	0.000	0.000	0.000	0.000
32	A	35	GLY	0	0.031	0.035	13.900	0.016	0.016	0.000	0.000	0.000	0.000
33	A	36	GLY	0	-0.025	-0.023	13.028	-0.020	-0.020	0.000	0.000	0.000	0.000
34	A	37	TYR	0	-0.067	-0.039	7.445	-0.056	-0.056	0.000	0.000	0.000	0.000
35	A	38	VAL	0	-0.019	-0.012	10.588	-0.120	-0.120	0.000	0.000	0.000	0.000
36	A	39	GLU	-1	-0.881	-0.939	13.192	-0.224	-0.224	0.000	0.000	0.000	0.000
37	A	40	PRO	0	0.045	-0.001	16.773	-0.016	-0.016	0.000	0.000	0.000	0.000
38	A	41	GLU	-1	-0.911	-0.958	19.172	-0.223	-0.223	0.000	0.000	0.000	0.000
39	A	42	TYR	0	-0.040	-0.062	10.847	-0.028	-0.028	0.000	0.000	0.000	0.000
40	A	43	VAL	0	0.017	0.010	16.523	-0.003	-0.003	0.000	0.000	0.000	0.000
41	A	44	GLN	0	-0.039	-0.024	18.711	0.017	0.017	0.000	0.000	0.000	0.000
42	A	45	ALA	0	0.030	0.017	16.269	0.007	0.007	0.000	0.000	0.000	0.000
43	A	46	MET	0	-0.063	-0.016	14.406	-0.011	-0.011	0.000	0.000	0.000	0.000
44	A	47	LEU	0	-0.031	-0.009	17.275	0.019	0.019	0.000	0.000	0.000	0.000
45	A	48	ASP	-1	-0.872	-0.931	20.179	-0.176	-0.176	0.000	0.000	0.000	0.000
46	A	49	ARG	1	0.858	0.912	13.724	0.356	0.356	0.000	0.000	0.000	0.000
47	A	50	GLU	-1	-0.771	-0.859	18.661	-0.144	-0.144	0.000	0.000	0.000	0.000
48	A	51	LYS	1	0.914	0.957	20.692	0.131	0.131	0.000	0.000	0.000	0.000
49	A	52	LEU	0	-0.076	-0.024	19.690	0.008	0.008	0.000	0.000	0.000	0.000
50	A	53	THR	0	-0.084	-0.058	18.774	0.001	0.001	0.000	0.000	0.000	0.000
51	A	54	PRO	0	0.032	0.027	19.310	-0.021	-0.021	0.000	0.000	0.000	0.000
52	A	55	THR	0	-0.108	-0.073	16.238	-0.005	-0.005	0.000	0.000	0.000	0.000
53	A	56	TYR	0	0.050	0.026	17.563	0.003	0.003	0.000	0.000	0.000	0.000
54	A	57	LEU	0	-0.041	-0.036	13.622	-0.014	-0.014	0.000	0.000	0.000	0.000
55	A	58	GLY	0	0.049	0.037	18.368	0.007	0.007	0.000	0.000	0.000	0.000
56	A	59	GLU	-1	-0.868	-0.940	19.390	0.057	0.057	0.000	0.000	0.000	0.000
57	A	60	SER	0	-0.018	-0.003	19.887	0.018	0.018	0.000	0.000	0.000	0.000
58	A	61	ILE	0	0.007	0.008	14.440	0.004	0.004	0.000	0.000	0.000	0.000
59	A	62	ALA	0	0.041	0.026	16.850	-0.021	-0.021	0.000	0.000	0.000	0.000
60	A	63	VAL	0	-0.033	-0.008	12.016	0.004	0.004	0.000	0.000	0.000	0.000
61	A	64	PRO	0	0.083	0.055	13.745	-0.068	-0.068	0.000	0.000	0.000	0.000
62	A	65	HIS	1	0.859	0.909	11.185	0.334	0.334	0.000	0.000	0.000	0.000
63	A	66	GLY	0	0.081	0.051	12.059	0.056	0.056	0.000	0.000	0.000	0.000
64	A	67	THR	0	0.002	0.007	13.801	-0.016	-0.016	0.000	0.000	0.000	0.000
65	A	68	VAL	0	0.032	0.013	13.197	-0.048	-0.048	0.000	0.000	0.000	0.000
66	A	69	GLU	-1	-0.902	-0.970	14.267	-0.306	-0.306	0.000	0.000	0.000	0.000
67	A	70	ALA	0	-0.016	0.002	15.046	0.012	0.012	0.000	0.000	0.000	0.000
68	A	71	LYS	1	0.928	0.959	11.157	0.399	0.399	0.000	0.000	0.000	0.000
69	A	72	ASP	-1	-0.891	-0.946	11.453	-0.517	-0.517	0.000	0.000	0.000	0.000
70	A	73	ARG	1	0.892	0.960	13.761	0.303	0.303	0.000	0.000	0.000	0.000
71	A	74	VAL	0	-0.034	-0.006	7.922	0.001	0.001	0.000	0.000	0.000	0.000
72	A	75	LEU	0	-0.024	-0.010	10.555	-0.032	-0.032	0.000	0.000	0.000	0.000
73	A	76	LYS	1	0.812	0.912	6.911	0.425	0.425	0.000	0.000	0.000	0.000
74	A	77	THR	0	0.015	0.010	2.365	-0.876	0.151	1.203	-0.431	-1.799	0.002
75	A	78	GLY	0	-0.025	-0.021	4.737	-0.199	-0.148	-0.001	-0.015	-0.035	0.000
76	A	79	VAL	0	0.002	0.016	6.199	-0.010	-0.010	0.000	0.000	0.000	0.000
77	A	80	VAL	0	-0.022	0.005	9.055	0.096	0.096	0.000	0.000	0.000	0.000
78	A	81	PHE	0	0.035	0.013	12.245	-0.017	-0.017	0.000	0.000	0.000	0.000
79	A	82	CYS	0	-0.054	-0.030	13.702	0.003	0.003	0.000	0.000	0.000	0.000
80	A	83	GLN	0	0.023	0.016	17.377	-0.021	-0.021	0.000	0.000	0.000	0.000
81	A	84	TYR	0	-0.016	-0.016	19.736	-0.014	-0.014	0.000	0.000	0.000	0.000
82	A	85	PRO	0	0.016	0.009	22.979	-0.003	-0.003	0.000	0.000	0.000	0.000
83	A	86	GLU	-1	-0.952	-0.986	25.074	0.024	0.024	0.000	0.000	0.000	0.000
84	A	87	GLY	0	-0.020	-0.002	24.709	-0.004	-0.004	0.000	0.000	0.000	0.000
85	A	88	VAL	0	-0.029	-0.014	23.591	-0.007	-0.007	0.000	0.000	0.000	0.000
86	A	89	ARG	1	0.945	0.991	24.544	0.042	0.042	0.000	0.000	0.000	0.000
87	A	90	PHE	0	-0.048	-0.046	19.650	-0.012	-0.012	0.000	0.000	0.000	0.000
88	A	91	GLY	0	-0.020	-0.016	23.989	-0.015	-0.015	0.000	0.000	0.000	0.000
89	A	92	GLU	-1	-0.986	-1.002	25.675	-0.070	-0.070	0.000	0.000	0.000	0.000
90	A	93	GLU	-1	-0.995	-0.999	29.142	-0.022	-0.022	0.000	0.000	0.000	0.000
91	A	94	GLU	-1	-0.997	-1.005	29.745	-0.010	-0.010	0.000	0.000	0.000	0.000
92	A	95	ASP	-1	-0.871	-0.941	29.426	0.007	0.007	0.000	0.000	0.000	0.000
93	A	96	ASP	-1	-0.896	-0.894	25.685	-0.024	-0.024	0.000	0.000	0.000	0.000
94	A	97	ILE	0	-0.014	-0.025	25.016	-0.011	-0.011	0.000	0.000	0.000	0.000
95	A	98	ALA	0	-0.029	-0.017	19.972	0.008	0.008	0.000	0.000	0.000	0.000
96	A	99	ARG	1	0.816	0.887	21.011	-0.077	-0.077	0.000	0.000	0.000	0.000
97	A	100	LEU	0	-0.020	0.005	15.581	0.015	0.015	0.000	0.000	0.000	0.000
98	A	101	VAL	0	0.007	0.003	16.767	-0.024	-0.024	0.000	0.000	0.000	0.000
99	A	102	ILE	0	-0.017	-0.016	10.107	0.013	0.013	0.000	0.000	0.000	0.000
100	A	103	GLY	0	0.022	0.020	12.740	-0.050	-0.050	0.000	0.000	0.000	0.000
101	A	104	ILE	0	-0.031	-0.024	7.134	-0.057	-0.057	0.000	0.000	0.000	0.000
102	A	105	ALA	0	0.020	0.045	8.255	0.088	0.088	0.000	0.000	0.000	0.000
103	A	106	ALA	0	0.031	-0.010	5.822	-0.408	-0.408	0.000	0.000	0.000	0.000
104	A	107	ARG	1	0.971	1.007	5.297	1.480	1.480	0.000	0.000	0.000	0.000
105	A	108	ASN	0	0.016	-0.006	7.610	0.039	0.039	0.000	0.000	0.000	0.000
106	A	109	ASN	0	0.023	-0.002	9.570	0.041	0.041	0.000	0.000	0.000	0.000
107	A	110	GLU	-1	-0.910	-0.954	3.988	-2.110	-1.719	0.006	-0.105	-0.291	0.000
108	A	111	HIS	0	0.021	0.008	5.467	-0.270	-0.270	0.000	0.000	0.000	0.000
109	A	112	ILE	0	-0.010	0.009	7.783	0.069	0.069	0.000	0.000	0.000	0.000
110	A	113	GLN	0	0.037	0.002	5.388	-0.020	-0.020	0.000	0.000	0.000	0.000
111	A	114	VAL	0	-0.014	0.003	3.566	-0.287	-0.001	0.005	-0.055	-0.237	0.000
112	A	115	ILE	0	0.057	0.017	5.756	0.324	0.324	0.000	0.000	0.000	0.000
113	A	116	THR	0	-0.012	0.005	8.402	0.158	0.158	0.000	0.000	0.000	0.000
114	A	117	SER	0	-0.093	-0.051	4.745	0.271	0.327	-0.001	-0.003	-0.052	0.000
115	A	118	LEU	0	-0.017	-0.025	6.718	0.246	0.246	0.000	0.000	0.000	0.000
116	A	119	THR	0	0.007	0.002	8.808	0.048	0.048	0.000	0.000	0.000	0.000
117	A	120	ASN	0	-0.024	-0.021	10.178	-0.015	-0.015	0.000	0.000	0.000	0.000
118	A	121	ALA	0	-0.073	-0.026	9.297	0.052	0.052	0.000	0.000	0.000	0.000
119	A	122	LEU	0	-0.067	-0.034	11.307	0.011	0.011	0.000	0.000	0.000	0.000
120	A	123	ASP	-1	-0.880	-0.932	14.137	0.207	0.207	0.000	0.000	0.000	0.000
121	A	124	ASP	-1	-0.896	-0.949	16.553	0.189	0.189	0.000	0.000	0.000	0.000
122	A	125	GLU	-1	-0.841	-0.928	18.828	0.104	0.104	0.000	0.000	0.000	0.000
123	A	126	SER	0	-0.008	-0.011	21.312	0.000	0.000	0.000	0.000	0.000	0.000
124	A	127	VAL	0	-0.061	-0.027	15.465	0.003	0.003	0.000	0.000	0.000	0.000
125	A	128	ILE	0	0.010	0.015	17.096	0.012	0.012	0.000	0.000	0.000	0.000
126	A	129	GLU	-1	-0.810	-0.889	18.808	0.088	0.088	0.000	0.000	0.000	0.000
127	A	130	ARG	1	0.896	0.941	20.271	-0.240	-0.240	0.000	0.000	0.000	0.000
128	A	131	LEU	0	-0.013	0.001	14.630	-0.002	-0.002	0.000	0.000	0.000	0.000
129	A	132	ALA	0	-0.010	0.002	18.815	-0.015	-0.015	0.000	0.000	0.000	0.000
130	A	133	HIS	0	-0.010	-0.009	21.138	-0.020	-0.020	0.000	0.000	0.000	0.000
131	A	134	THR	0	-0.047	-0.030	19.643	-0.010	-0.010	0.000	0.000	0.000	0.000
132	A	135	THR	0	-0.011	-0.008	22.775	-0.005	-0.005	0.000	0.000	0.000	0.000
133	A	136	SER	0	0.001	-0.001	22.216	0.001	0.001	0.000	0.000	0.000	0.000
134	A	137	VAL	0	0.053	0.014	17.182	0.018	0.018	0.000	0.000	0.000	0.000
135	A	138	ASP	-1	-0.913	-0.958	17.520	0.327	0.327	0.000	0.000	0.000	0.000
136	A	139	GLU	-1	-0.827	-0.896	18.046	0.269	0.269	0.000	0.000	0.000	0.000
137	A	140	VAL	0	0.000	0.000	14.006	0.040	0.040	0.000	0.000	0.000	0.000
138	A	141	LEU	0	-0.068	-0.046	12.579	0.094	0.094	0.000	0.000	0.000	0.000
139	A	142	GLU	-1	-0.969	-0.975	13.359	0.502	0.502	0.000	0.000	0.000	0.000
140	A	143	LEU	0	-0.030	-0.019	15.160	0.046	0.046	0.000	0.000	0.000	0.000
141	A	144	LEU	0	0.009	0.015	10.122	0.050	0.050	0.000	0.000	0.000	0.000
142	A	145	ALA	0	-0.024	0.002	9.809	0.383	0.383	0.000	0.000	0.000	0.000
143	A	146	GLY	0	-0.025	-0.007	10.488	0.159	0.159	0.000	0.000	0.000	0.000
144	A	147	ARG	1	0.867	0.934	5.499	-2.813	-2.813	0.000	0.000	0.000	0.000
145	A	148	LYS	1	0.919	0.975	4.826	-0.677	-0.677	0.000	0.000	0.000	0.000

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