FMO DATABASE

FMODB ID: QVVJY

Calculation Name: 5I4C-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5I4C

Chain ID: A

ChEMBL ID:

UniProt ID: P0DMC7

Base Structure: X-ray

Registration Date: 2023-09-21

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	131
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1139731.048843
FMO2-HF: Nuclear repulsion	1089931.632906
FMO2-HF: Total energy	-49799.415937
FMO2-MP2: Total energy	-49946.481234

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:ASN)

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

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.
-21.66	-15.485	4.951	-4.354	-6.773	-0.008

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

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 : -0.022

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

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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	MET	0	-0.021	0.004	3.858	-0.655	0.743	-0.010	-0.620	-0.768	0.001
4	A	5	ASN	0	-0.009	-0.006	6.433	-0.037	-0.037	0.000	0.000	0.000	0.000
5	A	6	VAL	0	-0.017	-0.017	9.675	0.113	0.113	0.000	0.000	0.000	0.000
6	A	7	ILE	0	0.004	0.011	12.642	-0.064	-0.064	0.000	0.000	0.000	0.000
7	A	8	ILE	0	-0.016	0.000	16.394	0.050	0.050	0.000	0.000	0.000	0.000
8	A	9	ALA	0	-0.009	-0.014	18.913	-0.027	-0.027	0.000	0.000	0.000	0.000
9	A	10	ASP	-1	-0.730	-0.890	22.524	0.111	0.111	0.000	0.000	0.000	0.000
10	A	11	ASP	-1	-0.863	-0.920	25.322	0.046	0.046	0.000	0.000	0.000	0.000
11	A	12	HIS	0	-0.042	-0.013	27.499	-0.011	-0.011	0.000	0.000	0.000	0.000
12	A	13	PRO	0	0.061	0.027	26.664	0.003	0.003	0.000	0.000	0.000	0.000
13	A	14	ILE	0	-0.035	-0.018	25.651	-0.008	-0.008	0.000	0.000	0.000	0.000
14	A	15	VAL	0	0.001	0.004	23.179	0.000	0.000	0.000	0.000	0.000	0.000
15	A	16	LEU	0	-0.022	0.007	21.878	0.010	0.010	0.000	0.000	0.000	0.000
16	A	17	PHE	0	0.001	-0.004	20.736	-0.012	-0.012	0.000	0.000	0.000	0.000
17	A	18	GLY	0	0.012	0.002	20.637	-0.016	-0.016	0.000	0.000	0.000	0.000
18	A	19	ILE	0	-0.002	-0.005	16.935	0.010	0.010	0.000	0.000	0.000	0.000
19	A	20	ARG	1	0.808	0.866	16.616	0.104	0.104	0.000	0.000	0.000	0.000
20	A	21	LYS	1	0.744	0.849	15.929	0.135	0.135	0.000	0.000	0.000	0.000
21	A	22	SER	0	-0.054	-0.027	15.277	-0.015	-0.015	0.000	0.000	0.000	0.000
22	A	23	LEU	0	-0.001	-0.024	11.906	0.006	0.006	0.000	0.000	0.000	0.000
23	A	24	GLU	-1	-0.782	-0.873	11.019	-0.313	-0.313	0.000	0.000	0.000	0.000
24	A	25	GLN	0	-0.081	-0.026	11.755	-0.150	-0.150	0.000	0.000	0.000	0.000
25	A	26	ILE	0	-0.055	-0.020	6.469	0.026	0.026	0.000	0.000	0.000	0.000
26	A	27	GLU	-1	-0.905	-0.960	2.509	-14.534	-12.232	0.517	-1.377	-1.442	-0.020
27	A	28	TRP	0	-0.008	0.004	2.423	0.186	2.072	1.846	-1.118	-2.614	0.002
28	A	29	VAL	0	0.007	0.005	4.546	0.491	0.531	-0.001	-0.031	-0.009	0.000
29	A	30	ASN	0	-0.017	-0.001	8.120	-0.232	-0.232	0.000	0.000	0.000	0.000
30	A	31	VAL	0	0.007	-0.002	10.851	0.114	0.114	0.000	0.000	0.000	0.000
31	A	32	VAL	0	-0.004	-0.004	12.759	-0.046	-0.046	0.000	0.000	0.000	0.000
32	A	33	GLY	0	-0.002	-0.005	15.549	0.006	0.006	0.000	0.000	0.000	0.000
33	A	34	GLU	-1	-0.785	-0.858	18.538	-0.042	-0.042	0.000	0.000	0.000	0.000
34	A	35	PHE	0	-0.043	-0.025	20.265	-0.009	-0.009	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.838	-0.929	24.386	0.006	0.006	0.000	0.000	0.000	0.000
36	A	37	ASP	-1	-0.729	-0.864	27.228	0.030	0.030	0.000	0.000	0.000	0.000
37	A	38	SER	0	-0.014	-0.016	26.393	-0.004	-0.004	0.000	0.000	0.000	0.000
38	A	39	THR	0	-0.080	-0.065	26.914	0.002	0.002	0.000	0.000	0.000	0.000
39	A	40	ALA	0	-0.030	-0.025	27.249	-0.003	-0.003	0.000	0.000	0.000	0.000
40	A	41	LEU	0	0.038	0.036	20.570	-0.007	-0.007	0.000	0.000	0.000	0.000
41	A	42	ILE	0	0.010	0.006	23.059	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	43	ASN	0	-0.033	-0.009	24.545	0.003	0.003	0.000	0.000	0.000	0.000
43	A	44	ASN	0	-0.076	-0.061	22.894	-0.016	-0.016	0.000	0.000	0.000	0.000
44	A	45	LEU	0	0.054	0.043	17.593	-0.008	-0.008	0.000	0.000	0.000	0.000
45	A	46	PRO	0	-0.050	-0.029	18.800	0.000	0.000	0.000	0.000	0.000	0.000
46	A	47	LYS	1	0.806	0.917	20.227	0.012	0.012	0.000	0.000	0.000	0.000
47	A	48	LEU	0	0.018	0.013	16.265	-0.020	-0.020	0.000	0.000	0.000	0.000
48	A	49	ASP	-1	-0.892	-0.916	11.956	0.011	0.011	0.000	0.000	0.000	0.000
49	A	50	ALA	0	-0.050	-0.038	11.245	-0.008	-0.008	0.000	0.000	0.000	0.000
50	A	51	HIS	0	0.012	0.003	6.912	-0.059	-0.059	0.000	0.000	0.000	0.000
51	A	52	VAL	0	-0.018	-0.019	9.957	0.063	0.063	0.000	0.000	0.000	0.000
52	A	53	LEU	0	-0.006	0.008	12.611	-0.056	-0.056	0.000	0.000	0.000	0.000
53	A	54	ILE	0	-0.021	-0.013	13.692	0.039	0.039	0.000	0.000	0.000	0.000
54	A	55	THR	0	-0.001	-0.021	17.735	-0.042	-0.042	0.000	0.000	0.000	0.000
55	A	56	ASP	-1	-0.793	-0.875	21.488	0.125	0.125	0.000	0.000	0.000	0.000
56	A	57	LEU	0	-0.032	-0.029	24.857	0.002	0.002	0.000	0.000	0.000	0.000
57	A	58	SER	0	-0.025	-0.015	27.534	-0.002	-0.002	0.000	0.000	0.000	0.000
58	A	59	MET	0	-0.014	0.020	24.707	-0.009	-0.009	0.000	0.000	0.000	0.000
59	A	60	PRO	0	0.027	0.011	30.185	0.002	0.002	0.000	0.000	0.000	0.000
60	A	61	GLY	0	0.078	0.033	30.514	0.003	0.003	0.000	0.000	0.000	0.000
61	A	62	ASP	-1	-0.932	-0.951	31.734	0.036	0.036	0.000	0.000	0.000	0.000
62	A	63	LYS	1	0.844	0.917	31.860	-0.029	-0.029	0.000	0.000	0.000	0.000
63	A	64	TYR	0	-0.057	-0.040	28.816	0.000	0.000	0.000	0.000	0.000	0.000
64	A	65	GLY	0	0.010	0.020	30.316	0.007	0.007	0.000	0.000	0.000	0.000
65	A	66	ASP	-1	-0.834	-0.919	29.221	0.079	0.079	0.000	0.000	0.000	0.000
66	A	67	GLY	0	0.040	0.010	28.847	0.003	0.003	0.000	0.000	0.000	0.000
67	A	68	ILE	0	-0.011	-0.020	27.877	0.005	0.005	0.000	0.000	0.000	0.000
68	A	69	THR	0	-0.035	-0.009	28.883	0.004	0.004	0.000	0.000	0.000	0.000
69	A	70	LEU	0	0.029	0.028	25.105	0.001	0.001	0.000	0.000	0.000	0.000
70	A	71	ILE	0	0.037	0.015	22.583	0.003	0.003	0.000	0.000	0.000	0.000
71	A	72	LYS	1	0.937	0.975	24.177	-0.104	-0.104	0.000	0.000	0.000	0.000
72	A	73	TYR	0	0.002	0.004	25.301	-0.002	-0.002	0.000	0.000	0.000	0.000
73	A	74	ILE	0	0.007	-0.005	20.059	-0.004	-0.004	0.000	0.000	0.000	0.000
74	A	75	LYS	1	0.844	0.911	18.012	-0.261	-0.261	0.000	0.000	0.000	0.000
75	A	76	ARG	1	0.875	0.948	22.129	-0.083	-0.083	0.000	0.000	0.000	0.000
76	A	77	HIS	0	-0.060	-0.029	23.650	-0.010	-0.010	0.000	0.000	0.000	0.000
77	A	78	PHE	0	0.013	0.001	18.322	-0.010	-0.010	0.000	0.000	0.000	0.000
78	A	79	PRO	0	0.022	0.016	18.383	0.016	0.016	0.000	0.000	0.000	0.000
79	A	80	SER	0	-0.065	-0.038	14.249	0.010	0.010	0.000	0.000	0.000	0.000
80	A	81	LEU	0	-0.040	0.007	13.526	0.013	0.013	0.000	0.000	0.000	0.000
81	A	82	SER	0	-0.010	0.002	11.853	0.031	0.031	0.000	0.000	0.000	0.000
82	A	83	ILE	0	-0.020	-0.024	14.222	-0.024	-0.024	0.000	0.000	0.000	0.000
83	A	84	ILE	0	-0.014	-0.009	13.265	0.031	0.031	0.000	0.000	0.000	0.000
84	A	85	VAL	0	0.016	0.006	17.643	-0.035	-0.035	0.000	0.000	0.000	0.000
85	A	86	LEU	0	-0.006	-0.004	19.663	0.025	0.025	0.000	0.000	0.000	0.000
86	A	87	THR	0	0.027	-0.004	22.719	-0.025	-0.025	0.000	0.000	0.000	0.000
87	A	88	MET	0	0.023	0.024	26.183	0.005	0.005	0.000	0.000	0.000	0.000
88	A	89	ASN	0	-0.066	-0.031	28.875	0.000	0.000	0.000	0.000	0.000	0.000
89	A	90	ASN	0	0.109	0.042	27.159	0.017	0.017	0.000	0.000	0.000	0.000
90	A	91	ASN	0	0.013	0.016	29.460	0.003	0.003	0.000	0.000	0.000	0.000
91	A	92	PRO	0	0.057	0.015	31.050	0.005	0.005	0.000	0.000	0.000	0.000
92	A	93	ALA	0	0.010	0.016	31.417	0.006	0.006	0.000	0.000	0.000	0.000
93	A	94	ILE	0	-0.029	-0.016	29.104	0.001	0.001	0.000	0.000	0.000	0.000
94	A	95	LEU	0	0.000	-0.003	26.187	0.005	0.005	0.000	0.000	0.000	0.000
95	A	96	SER	0	-0.021	-0.014	27.195	0.010	0.010	0.000	0.000	0.000	0.000
96	A	97	ALA	0	0.008	0.005	28.482	0.006	0.006	0.000	0.000	0.000	0.000
97	A	98	VAL	0	-0.009	-0.010	24.627	-0.005	-0.005	0.000	0.000	0.000	0.000
98	A	99	LEU	0	-0.001	-0.003	22.610	0.013	0.013	0.000	0.000	0.000	0.000
99	A	100	ASP	-1	-0.863	-0.924	24.772	0.174	0.174	0.000	0.000	0.000	0.000
100	A	101	LEU	0	-0.132	-0.064	24.858	-0.012	-0.012	0.000	0.000	0.000	0.000
101	A	102	ASP	-1	-0.822	-0.915	20.137	0.297	0.297	0.000	0.000	0.000	0.000
102	A	103	ILE	0	-0.005	0.008	19.676	0.014	0.014	0.000	0.000	0.000	0.000
103	A	104	GLU	-1	-0.771	-0.888	14.270	0.340	0.340	0.000	0.000	0.000	0.000
104	A	105	GLY	0	0.024	-0.003	16.396	0.074	0.074	0.000	0.000	0.000	0.000
105	A	106	ILE	0	-0.029	0.009	18.245	-0.042	-0.042	0.000	0.000	0.000	0.000
106	A	107	VAL	0	0.007	-0.004	17.494	0.033	0.033	0.000	0.000	0.000	0.000
107	A	108	LEU	0	0.022	0.015	20.939	-0.033	-0.033	0.000	0.000	0.000	0.000
108	A	109	LYS	1	0.818	0.873	22.738	-0.090	-0.090	0.000	0.000	0.000	0.000
109	A	110	GLN	0	-0.012	-0.035	23.354	-0.008	-0.008	0.000	0.000	0.000	0.000
110	A	111	GLY	0	0.030	0.033	22.461	-0.013	-0.013	0.000	0.000	0.000	0.000
111	A	112	ALA	0	0.019	0.012	19.055	0.027	0.027	0.000	0.000	0.000	0.000
112	A	113	PRO	0	0.025	0.001	17.531	0.040	0.040	0.000	0.000	0.000	0.000
113	A	114	THR	0	0.006	0.023	17.014	-0.011	-0.011	0.000	0.000	0.000	0.000
114	A	115	ASP	-1	-0.846	-0.935	16.048	0.402	0.402	0.000	0.000	0.000	0.000
115	A	116	LEU	0	0.002	0.007	14.284	0.087	0.087	0.000	0.000	0.000	0.000
116	A	117	PRO	0	0.020	0.012	11.200	0.161	0.161	0.000	0.000	0.000	0.000
117	A	118	LYS	1	0.781	0.899	10.884	-0.114	-0.114	0.000	0.000	0.000	0.000
118	A	119	ALA	0	0.005	0.001	12.372	0.164	0.164	0.000	0.000	0.000	0.000
119	A	120	LEU	0	0.041	0.012	9.039	0.064	0.064	0.000	0.000	0.000	0.000
120	A	121	ALA	0	0.049	0.029	7.606	0.406	0.406	0.000	0.000	0.000	0.000
121	A	122	ALA	0	-0.072	-0.038	8.674	0.167	0.167	0.000	0.000	0.000	0.000
122	A	123	LEU	0	0.033	0.009	9.708	-0.001	-0.001	0.000	0.000	0.000	0.000
123	A	124	GLN	0	-0.030	-0.005	2.214	-5.667	-5.118	2.599	-1.208	-1.940	0.009
124	A	125	LYS	1	0.892	0.968	6.456	-1.982	-1.982	0.000	0.000	0.000	0.000
125	A	126	GLY	0	0.024	0.024	9.041	-0.291	-0.291	0.000	0.000	0.000	0.000
126	A	127	LYS	1	0.752	0.858	11.242	-0.910	-0.910	0.000	0.000	0.000	0.000
127	A	128	LYS	1	0.838	0.929	13.312	-0.293	-0.293	0.000	0.000	0.000	0.000
128	A	129	PHE	0	-0.013	-0.012	15.358	0.049	0.049	0.000	0.000	0.000	0.000
129	A	130	THR	0	0.016	0.008	17.312	-0.054	-0.054	0.000	0.000	0.000	0.000
130	A	131	PRO	0	-0.035	-0.006	20.984	0.020	0.020	0.000	0.000	0.000	0.000
131	A	132	GLU	-1	-0.918	-0.948	21.477	0.297	0.297	0.000	0.000	0.000	0.000

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