FMO DATABASE

FMODB ID: YVZ62

Calculation Name: 2NWI-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2NWI

Chain ID: A

ChEMBL ID:

UniProt ID: O28875

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	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	160
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1685937.158339
FMO2-HF: Nuclear repulsion	1621088.383105
FMO2-HF: Total energy	-64848.775234
FMO2-MP2: Total energy	-65039.938519

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:1:LEU)

Summations of interaction energy for fragment #1(A:1: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.
-9.38	-0.198	5.016	-4.104	-10.094	-0.015

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.027 / q_NPA : -0.001

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	3	ALA	0	0.030	-0.019	3.798	-1.276	0.505	-0.021	-0.864	-0.895	0.004
4	A	4	ILE	0	0.064	0.036	6.523	0.047	0.047	0.000	0.000	0.000	0.000
5	A	5	HIS	0	0.029	0.002	2.356	-3.531	-0.656	2.376	-1.834	-3.417	-0.017
6	A	6	ARG	1	0.960	0.979	2.423	-0.570	1.259	0.966	-0.639	-2.156	0.002
7	A	7	ILE	0	0.009	0.008	4.400	-0.152	-0.022	0.000	-0.033	-0.097	0.000
8	A	8	LEU	0	-0.021	-0.014	6.742	0.001	0.001	0.000	0.000	0.000	0.000
9	A	9	MET	0	-0.048	-0.009	3.523	-1.285	-0.451	0.250	-0.249	-0.835	-0.002
10	A	10	THR	0	-0.012	-0.002	7.434	0.047	0.047	0.000	0.000	0.000	0.000
11	A	11	THR	0	-0.045	0.013	10.262	0.037	0.037	0.000	0.000	0.000	0.000
12	A	12	ASP	-1	-0.871	-0.929	12.536	-0.124	-0.124	0.000	0.000	0.000	0.000
13	A	13	GLY	0	0.019	0.020	15.522	0.017	0.017	0.000	0.000	0.000	0.000
14	A	14	SER	0	-0.088	-0.048	16.519	0.003	0.003	0.000	0.000	0.000	0.000
15	A	15	ILE	0	0.112	0.045	12.236	0.004	0.004	0.000	0.000	0.000	0.000
16	A	16	THR	0	-0.038	-0.016	15.535	0.019	0.019	0.000	0.000	0.000	0.000
17	A	17	ALA	0	0.030	0.004	18.025	0.011	0.011	0.000	0.000	0.000	0.000
18	A	18	ILE	0	0.006	0.009	11.618	0.005	0.005	0.000	0.000	0.000	0.000
19	A	19	ILE	0	0.004	0.004	13.428	0.021	0.021	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.861	-0.935	15.046	0.075	0.075	0.000	0.000	0.000	0.000
21	A	21	ALA	0	-0.054	-0.011	15.980	0.006	0.006	0.000	0.000	0.000	0.000
22	A	22	VAL	0	-0.044	-0.021	11.457	0.007	0.007	0.000	0.000	0.000	0.000
23	A	23	THR	0	-0.029	-0.020	14.508	0.020	0.020	0.000	0.000	0.000	0.000
24	A	24	GLN	0	-0.021	-0.005	16.835	-0.013	-0.013	0.000	0.000	0.000	0.000
25	A	25	LYS	1	0.882	0.953	19.654	-0.143	-0.143	0.000	0.000	0.000	0.000
26	A	26	LYS	1	0.946	0.977	20.713	-0.056	-0.056	0.000	0.000	0.000	0.000
27	A	27	VAL	0	-0.060	-0.036	18.442	0.011	0.011	0.000	0.000	0.000	0.000
28	A	28	GLU	-1	-0.902	-0.967	21.395	0.045	0.045	0.000	0.000	0.000	0.000
29	A	29	VAL	0	-0.066	-0.029	22.049	0.006	0.006	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.874	-0.933	23.007	0.073	0.073	0.000	0.000	0.000	0.000
31	A	31	THR	0	-0.036	-0.036	23.797	-0.001	-0.001	0.000	0.000	0.000	0.000
32	A	32	LEU	0	0.026	0.023	23.225	-0.001	-0.001	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.935	-0.975	26.029	0.025	0.025	0.000	0.000	0.000	0.000
34	A	34	GLN	0	0.052	0.013	26.885	-0.004	-0.004	0.000	0.000	0.000	0.000
35	A	35	LYS	1	0.893	0.958	29.411	-0.018	-0.018	0.000	0.000	0.000	0.000
36	A	36	ILE	0	0.001	0.011	30.991	-0.003	-0.003	0.000	0.000	0.000	0.000
37	A	37	ILE	0	-0.002	0.005	28.449	0.002	0.002	0.000	0.000	0.000	0.000
38	A	38	ARG	1	0.947	0.978	32.746	0.009	0.009	0.000	0.000	0.000	0.000
39	A	39	ALA	0	-0.018	-0.005	31.424	0.000	0.000	0.000	0.000	0.000	0.000
40	A	40	ASP	-1	-0.771	-0.877	29.851	-0.026	-0.026	0.000	0.000	0.000	0.000
41	A	41	ARG	1	0.967	0.967	31.758	0.035	0.035	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.922	-0.958	25.819	-0.041	-0.041	0.000	0.000	0.000	0.000
43	A	43	LEU	0	0.020	0.010	25.988	-0.005	-0.005	0.000	0.000	0.000	0.000
44	A	44	ALA	0	-0.024	-0.013	28.061	-0.002	-0.002	0.000	0.000	0.000	0.000
45	A	45	GLU	-1	-0.887	-0.942	28.216	-0.053	-0.053	0.000	0.000	0.000	0.000
46	A	46	LEU	0	-0.090	-0.024	21.882	-0.005	-0.005	0.000	0.000	0.000	0.000
47	A	47	LEU	0	-0.055	-0.050	25.343	-0.004	-0.004	0.000	0.000	0.000	0.000
48	A	48	GLU	-1	-0.911	-0.942	27.806	-0.059	-0.059	0.000	0.000	0.000	0.000
49	A	49	ILE	0	-0.193	-0.099	30.540	0.003	0.003	0.000	0.000	0.000	0.000
50	A	50	ASP	-1	-0.885	-0.939	33.272	-0.029	-0.029	0.000	0.000	0.000	0.000
51	A	51	GLU	-1	-0.910	-0.966	34.774	-0.024	-0.024	0.000	0.000	0.000	0.000
52	A	52	GLY	0	-0.087	-0.044	35.496	0.002	0.002	0.000	0.000	0.000	0.000
53	A	53	ASP	-1	-0.788	-0.902	34.661	-0.021	-0.021	0.000	0.000	0.000	0.000
54	A	54	GLU	-1	-0.904	-0.964	34.364	-0.008	-0.008	0.000	0.000	0.000	0.000
55	A	55	VAL	0	-0.044	-0.030	28.348	-0.003	-0.003	0.000	0.000	0.000	0.000
56	A	56	ASN	0	-0.052	-0.033	27.990	0.005	0.005	0.000	0.000	0.000	0.000
57	A	57	TYR	0	0.015	0.008	23.721	-0.005	-0.005	0.000	0.000	0.000	0.000
58	A	58	ARG	1	0.848	0.917	24.535	-0.003	-0.003	0.000	0.000	0.000	0.000
59	A	59	VAL	0	0.024	0.027	21.120	-0.005	-0.005	0.000	0.000	0.000	0.000
60	A	60	VAL	0	-0.039	-0.029	20.403	0.002	0.002	0.000	0.000	0.000	0.000
61	A	61	TYR	0	-0.064	-0.098	18.870	0.006	0.006	0.000	0.000	0.000	0.000
62	A	62	LEU	0	-0.030	-0.017	16.273	-0.011	-0.011	0.000	0.000	0.000	0.000
63	A	63	ARG	1	0.899	0.943	17.560	-0.080	-0.080	0.000	0.000	0.000	0.000
64	A	64	ALA	0	0.078	0.056	17.506	-0.018	-0.018	0.000	0.000	0.000	0.000
65	A	65	ASN	0	-0.033	-0.016	18.787	0.006	0.006	0.000	0.000	0.000	0.000
66	A	66	GLY	0	0.031	0.005	21.619	-0.016	-0.016	0.000	0.000	0.000	0.000
67	A	67	GLU	-1	-0.924	-0.961	16.740	0.330	0.330	0.000	0.000	0.000	0.000
68	A	68	ILE	0	0.006	0.005	15.783	-0.014	-0.014	0.000	0.000	0.000	0.000
69	A	69	TYR	0	-0.009	-0.012	12.489	0.045	0.045	0.000	0.000	0.000	0.000
70	A	70	ALA	0	-0.002	-0.016	12.400	0.003	0.003	0.000	0.000	0.000	0.000
71	A	71	LYS	1	0.891	0.964	14.446	-0.056	-0.056	0.000	0.000	0.000	0.000
72	A	72	ALA	0	-0.016	-0.008	15.382	-0.018	-0.018	0.000	0.000	0.000	0.000
73	A	73	ILE	0	0.005	0.005	17.753	0.009	0.009	0.000	0.000	0.000	0.000
74	A	74	SER	0	-0.025	-0.018	19.866	-0.012	-0.012	0.000	0.000	0.000	0.000
75	A	75	PHE	0	0.070	0.041	22.003	0.007	0.007	0.000	0.000	0.000	0.000
76	A	76	THR	0	-0.012	-0.018	25.326	-0.006	-0.006	0.000	0.000	0.000	0.000
77	A	77	PRO	0	0.063	0.058	27.985	0.005	0.005	0.000	0.000	0.000	0.000
78	A	78	LEU	0	0.042	0.008	31.186	0.000	0.000	0.000	0.000	0.000	0.000
79	A	79	LYS	1	0.865	0.949	34.094	0.028	0.028	0.000	0.000	0.000	0.000
80	A	80	ARG	1	0.749	0.874	30.066	0.039	0.039	0.000	0.000	0.000	0.000
81	A	81	LEU	0	-0.039	-0.006	30.712	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	82	GLU	-1	-0.852	-0.935	34.616	-0.020	-0.020	0.000	0.000	0.000	0.000
83	A	83	ASN	0	0.028	-0.003	36.764	0.001	0.001	0.000	0.000	0.000	0.000
84	A	84	SER	0	0.047	0.026	38.177	0.001	0.001	0.000	0.000	0.000	0.000
85	A	85	PHE	0	-0.015	-0.002	28.508	0.002	0.002	0.000	0.000	0.000	0.000
86	A	86	ARG	1	0.925	0.933	33.551	0.014	0.014	0.000	0.000	0.000	0.000
87	A	87	GLU	-1	-0.909	-0.959	34.717	0.000	0.000	0.000	0.000	0.000	0.000
88	A	88	ASP	-1	-0.793	-0.881	32.689	0.001	0.001	0.000	0.000	0.000	0.000
89	A	89	LEU	0	-0.033	-0.008	28.049	0.002	0.002	0.000	0.000	0.000	0.000
90	A	90	MET	0	0.000	-0.013	31.608	0.003	0.003	0.000	0.000	0.000	0.000
91	A	91	ARG	1	0.906	0.954	33.956	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	92	ALA	0	-0.015	0.014	30.410	0.003	0.003	0.000	0.000	0.000	0.000
93	A	93	ASP	-1	-0.877	-0.935	29.161	0.022	0.022	0.000	0.000	0.000	0.000
94	A	94	ILE	0	-0.032	-0.010	29.448	0.002	0.002	0.000	0.000	0.000	0.000
95	A	95	PRO	0	-0.025	-0.021	24.087	-0.004	-0.004	0.000	0.000	0.000	0.000
96	A	96	ILE	0	0.122	0.048	23.514	-0.003	-0.003	0.000	0.000	0.000	0.000
97	A	97	GLY	0	0.006	0.007	23.628	-0.004	-0.004	0.000	0.000	0.000	0.000
98	A	98	LYS	1	0.951	0.967	24.377	-0.022	-0.022	0.000	0.000	0.000	0.000
99	A	99	ILE	0	-0.001	0.018	27.677	-0.002	-0.002	0.000	0.000	0.000	0.000
100	A	100	MET	0	0.021	-0.008	23.838	-0.002	-0.002	0.000	0.000	0.000	0.000
101	A	101	ARG	1	0.975	0.998	24.439	0.011	0.011	0.000	0.000	0.000	0.000
102	A	102	LYS	1	0.858	0.946	29.393	0.002	0.002	0.000	0.000	0.000	0.000
103	A	103	HIS	1	0.761	0.857	31.911	0.012	0.012	0.000	0.000	0.000	0.000
104	A	104	ASN	0	0.014	0.022	31.759	-0.001	-0.001	0.000	0.000	0.000	0.000
105	A	105	ILE	0	-0.022	-0.018	28.355	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	106	GLU	-1	-0.906	-0.929	28.577	-0.042	-0.042	0.000	0.000	0.000	0.000
107	A	107	ALA	0	-0.045	-0.027	25.315	0.002	0.002	0.000	0.000	0.000	0.000
108	A	108	ARG	1	0.890	0.942	23.307	0.083	0.083	0.000	0.000	0.000	0.000
109	A	109	ARG	1	0.961	0.978	16.562	0.098	0.098	0.000	0.000	0.000	0.000
110	A	110	GLU	-1	-0.843	-0.891	19.102	-0.108	-0.108	0.000	0.000	0.000	0.000
111	A	111	ILE	0	-0.006	-0.012	12.477	0.009	0.009	0.000	0.000	0.000	0.000
112	A	112	ARG	1	0.904	0.948	15.631	0.106	0.106	0.000	0.000	0.000	0.000
113	A	113	TRP	0	-0.023	-0.026	11.213	-0.002	-0.002	0.000	0.000	0.000	0.000
114	A	114	SER	0	-0.043	-0.038	8.332	-0.003	-0.003	0.000	0.000	0.000	0.000
115	A	115	ARG	1	0.882	0.945	6.530	0.136	0.136	0.000	0.000	0.000	0.000
116	A	116	VAL	0	-0.018	-0.011	2.837	-0.860	-0.129	0.400	-0.201	-0.931	-0.001
117	A	117	GLU	-1	-0.807	-0.890	5.653	-0.098	-0.098	0.000	0.000	0.000	0.000
118	A	118	GLU	-1	-0.939	-0.969	8.318	-0.032	-0.032	0.000	0.000	0.000	0.000
119	A	119	ALA	0	-0.015	-0.001	11.231	-0.028	-0.028	0.000	0.000	0.000	0.000
120	A	120	ASP	-1	-0.825	-0.920	13.196	0.094	0.094	0.000	0.000	0.000	0.000
121	A	121	LEU	0	-0.039	-0.040	16.805	0.024	0.024	0.000	0.000	0.000	0.000
122	A	122	ALA	0	0.008	-0.002	19.085	0.017	0.017	0.000	0.000	0.000	0.000
123	A	123	LEU	0	0.081	0.057	13.644	0.007	0.007	0.000	0.000	0.000	0.000
124	A	124	ALA	0	0.008	-0.002	15.374	0.020	0.020	0.000	0.000	0.000	0.000
125	A	125	LYS	1	0.902	0.935	16.352	-0.104	-0.104	0.000	0.000	0.000	0.000
126	A	126	GLU	-1	-0.800	-0.814	18.734	0.089	0.089	0.000	0.000	0.000	0.000
127	A	127	LEU	0	-0.017	-0.009	13.150	-0.001	-0.001	0.000	0.000	0.000	0.000
128	A	128	GLY	0	-0.012	0.004	16.889	0.018	0.018	0.000	0.000	0.000	0.000
129	A	129	ILE	0	-0.099	-0.031	11.689	0.011	0.011	0.000	0.000	0.000	0.000
130	A	130	ALA	0	-0.024	-0.008	14.795	-0.051	-0.051	0.000	0.000	0.000	0.000
131	A	131	ASP	-1	-0.859	-0.935	8.442	1.420	1.420	0.000	0.000	0.000	0.000
132	A	132	ARG	1	0.979	0.968	11.308	-0.259	-0.259	0.000	0.000	0.000	0.000
133	A	133	ARG	1	0.841	0.921	3.810	-2.756	-2.565	-0.001	-0.032	-0.158	0.000
134	A	134	VAL	0	-0.003	-0.009	7.612	0.144	0.144	0.000	0.000	0.000	0.000
135	A	135	ILE	0	-0.007	0.003	3.916	-0.420	-0.164	0.002	-0.041	-0.217	0.000
136	A	136	SER	0	0.030	0.029	6.441	0.118	0.118	0.000	0.000	0.000	0.000
137	A	137	ARG	1	0.787	0.845	9.544	0.105	0.105	0.000	0.000	0.000	0.000
138	A	138	ASN	0	-0.008	0.023	11.545	0.043	0.043	0.000	0.000	0.000	0.000
139	A	139	TYR	0	-0.023	-0.009	14.910	-0.020	-0.020	0.000	0.000	0.000	0.000
140	A	140	ASN	0	0.071	0.056	17.466	0.017	0.017	0.000	0.000	0.000	0.000
141	A	141	ILE	0	-0.016	-0.009	21.023	-0.007	-0.007	0.000	0.000	0.000	0.000
142	A	142	ILE	0	0.010	0.013	23.092	0.006	0.006	0.000	0.000	0.000	0.000
143	A	143	HIS	0	-0.010	-0.046	25.851	0.003	0.003	0.000	0.000	0.000	0.000
144	A	144	ARG	1	0.916	0.962	29.096	0.032	0.032	0.000	0.000	0.000	0.000
145	A	145	GLY	0	-0.009	-0.006	29.820	0.002	0.002	0.000	0.000	0.000	0.000
146	A	146	LYS	1	0.970	0.994	29.839	0.036	0.036	0.000	0.000	0.000	0.000
147	A	147	VAL	0	0.073	0.050	24.927	-0.001	-0.001	0.000	0.000	0.000	0.000
148	A	148	LEU	0	-0.057	-0.022	26.590	0.006	0.006	0.000	0.000	0.000	0.000
149	A	149	ILE	0	-0.015	-0.028	23.206	0.006	0.006	0.000	0.000	0.000	0.000
150	A	150	ASN	0	0.006	-0.006	19.684	-0.003	-0.003	0.000	0.000	0.000	0.000
151	A	151	ILE	0	-0.018	-0.017	16.880	0.013	0.013	0.000	0.000	0.000	0.000
152	A	152	THR	0	0.028	0.018	15.151	-0.024	-0.024	0.000	0.000	0.000	0.000
153	A	153	GLU	-1	-0.835	-0.928	12.840	-0.059	-0.059	0.000	0.000	0.000	0.000
154	A	154	PHE	0	0.037	0.018	10.994	-0.040	-0.040	0.000	0.000	0.000	0.000
155	A	155	PHE	0	-0.003	-0.022	8.116	0.027	0.027	0.000	0.000	0.000	0.000
156	A	156	PRO	0	0.039	0.035	8.232	0.005	0.005	0.000	0.000	0.000	0.000
157	A	157	MET	0	-0.036	-0.022	2.500	-0.952	-0.397	1.044	-0.211	-1.388	-0.001
158	A	158	GLU	-1	-0.789	-0.897	6.440	0.918	0.918	0.000	0.000	0.000	0.000
159	A	159	ARG	1	0.850	0.943	9.335	-0.390	-0.390	0.000	0.000	0.000	0.000
160	A	160	PHE	0	-0.030	-0.009	6.974	-0.064	-0.064	0.000	0.000	0.000	0.000

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