FMO DATABASE

FMODB ID: 1NZZZ

Calculation Name: 5AP8-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 5AP8

Chain ID: A

ChEMBL ID:

UniProt ID: Q9UWV6

Base Structure: X-ray

Registration Date: 2023-09-24

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

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
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	151
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1551525.263772
FMO2-HF: Nuclear repulsion	1492078.582951
FMO2-HF: Total energy	-59446.680821
FMO2-MP2: Total energy	-59625.19993

3D Structure Molmil

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:MET)

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

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.
-12.738	-8.5	11.138	-3.472	-11.908	-0.015

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

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 : 0.006

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	VAL	0	0.025	0.013	3.855	-1.638	-0.147	-0.011	-0.664	-0.817	0.004
4	A	4	TYR	0	-0.032	-0.016	6.342	0.448	0.448	0.000	0.000	0.000	0.000
5	A	5	ILE	0	0.018	0.007	9.922	-0.100	-0.100	0.000	0.000	0.000	0.000
6	A	6	ILE	0	-0.010	-0.008	13.019	0.082	0.082	0.000	0.000	0.000	0.000
7	A	7	ASP	-1	-0.795	-0.900	16.329	-0.112	-0.112	0.000	0.000	0.000	0.000
8	A	8	TYR	0	0.002	0.010	19.146	0.043	0.043	0.000	0.000	0.000	0.000
9	A	18	GLY	0	0.050	0.022	15.076	0.013	0.013	0.000	0.000	0.000	0.000
10	A	19	LYS	1	0.826	0.873	14.593	0.082	0.082	0.000	0.000	0.000	0.000
11	A	20	LYS	1	0.879	0.953	14.248	0.456	0.456	0.000	0.000	0.000	0.000
12	A	21	LEU	0	0.065	0.024	9.328	0.016	0.016	0.000	0.000	0.000	0.000
13	A	22	VAL	0	0.021	0.026	10.981	0.030	0.030	0.000	0.000	0.000	0.000
14	A	23	LYS	1	0.909	0.958	13.049	0.150	0.150	0.000	0.000	0.000	0.000
15	A	24	LEU	0	-0.040	-0.033	11.211	0.048	0.048	0.000	0.000	0.000	0.000
16	A	25	LYS	1	0.938	0.976	10.169	-0.691	-0.691	0.000	0.000	0.000	0.000
17	A	26	ILE	0	0.022	0.018	5.698	0.276	0.276	0.000	0.000	0.000	0.000
18	A	27	ALA	0	-0.005	0.000	6.506	-0.266	-0.266	0.000	0.000	0.000	0.000
19	A	28	GLU	-1	-0.846	-0.912	9.195	0.790	0.790	0.000	0.000	0.000	0.000
20	A	29	PHE	0	-0.001	-0.010	12.039	-0.090	-0.090	0.000	0.000	0.000	0.000
21	A	30	THR	0	-0.005	-0.019	13.137	0.089	0.089	0.000	0.000	0.000	0.000
22	A	31	ARG	1	0.898	0.939	15.745	-0.160	-0.160	0.000	0.000	0.000	0.000
23	A	32	VAL	0	-0.028	-0.001	16.249	-0.017	-0.017	0.000	0.000	0.000	0.000
24	A	33	GLY	0	0.034	0.033	13.307	0.030	0.030	0.000	0.000	0.000	0.000
25	A	34	LYS	1	0.811	0.900	9.885	-0.586	-0.586	0.000	0.000	0.000	0.000
26	A	35	GLY	0	0.037	0.027	7.839	-0.031	-0.031	0.000	0.000	0.000	0.000
27	A	36	VAL	0	0.010	0.006	7.593	-0.121	-0.121	0.000	0.000	0.000	0.000
28	A	37	VAL	0	-0.038	-0.013	9.011	-0.118	-0.118	0.000	0.000	0.000	0.000
29	A	38	LEU	0	0.007	0.002	9.061	-0.004	-0.004	0.000	0.000	0.000	0.000
30	A	39	ASP	-1	-0.792	-0.898	12.754	-0.032	-0.032	0.000	0.000	0.000	0.000
31	A	40	PRO	0	-0.023	-0.007	16.548	-0.007	-0.007	0.000	0.000	0.000	0.000
32	A	41	PHE	0	-0.024	-0.020	19.114	0.004	0.004	0.000	0.000	0.000	0.000
33	A	42	ALA	0	-0.038	0.002	17.740	0.023	0.023	0.000	0.000	0.000	0.000
34	A	43	GLN	0	0.020	-0.006	19.730	-0.021	-0.021	0.000	0.000	0.000	0.000
35	A	44	ILE	0	-0.018	0.005	16.834	-0.017	-0.017	0.000	0.000	0.000	0.000
36	A	45	THR	0	-0.046	-0.027	16.392	-0.016	-0.016	0.000	0.000	0.000	0.000
37	A	46	LEU	0	-0.030	-0.002	8.941	0.037	0.037	0.000	0.000	0.000	0.000
38	A	47	SER	0	0.021	0.003	12.146	-0.038	-0.038	0.000	0.000	0.000	0.000
39	A	48	ASN	0	0.005	0.002	11.133	0.092	0.092	0.000	0.000	0.000	0.000
40	A	49	LYS	1	0.818	0.891	12.135	0.137	0.137	0.000	0.000	0.000	0.000
41	A	50	ASP	-1	-0.774	-0.873	10.111	0.169	0.169	0.000	0.000	0.000	0.000
42	A	51	LYS	1	0.893	0.932	6.783	0.219	0.219	0.000	0.000	0.000	0.000
43	A	52	ASP	-1	-0.820	-0.905	6.057	1.553	1.553	0.000	0.000	0.000	0.000
44	A	53	ILE	0	-0.049	-0.017	7.859	0.607	0.607	0.000	0.000	0.000	0.000
45	A	54	VAL	0	0.018	0.013	2.551	-0.583	0.195	0.480	-0.230	-1.029	-0.001
46	A	55	ARG	1	0.850	0.905	2.680	0.107	1.291	6.673	-3.929	-3.929	0.006
47	A	56	ARG	1	0.946	0.979	3.749	0.929	-1.750	-0.066	3.385	-0.641	-0.001
48	A	57	ILE	0	-0.054	-0.020	6.654	-0.133	-0.133	0.000	0.000	0.000	0.000
49	A	58	GLY	0	0.035	0.015	3.503	0.033	0.160	0.004	-0.044	-0.087	0.000
50	A	59	ILE	0	0.005	0.011	3.601	-0.535	-0.066	0.018	-0.075	-0.412	0.000
51	A	60	THR	0	-0.017	-0.026	6.099	-0.032	-0.032	0.000	0.000	0.000	0.000
52	A	61	ILE	0	0.010	0.008	9.468	-0.055	-0.055	0.000	0.000	0.000	0.000
53	A	62	VAL	0	0.020	0.011	12.128	0.076	0.076	0.000	0.000	0.000	0.000
54	A	63	ASP	-1	-0.884	-0.940	15.923	-0.290	-0.290	0.000	0.000	0.000	0.000
55	A	64	THR	0	-0.016	-0.017	17.297	0.026	0.026	0.000	0.000	0.000	0.000
56	A	65	SER	0	0.003	-0.004	19.053	-0.045	-0.045	0.000	0.000	0.000	0.000
57	A	66	TRP	0	0.069	0.016	19.190	0.017	0.017	0.000	0.000	0.000	0.000
58	A	67	ASN	0	-0.028	-0.023	22.369	0.000	0.000	0.000	0.000	0.000	0.000
59	A	68	ASN	0	-0.028	-0.022	25.166	0.001	0.001	0.000	0.000	0.000	0.000
60	A	69	THR	0	-0.037	-0.002	21.602	0.012	0.012	0.000	0.000	0.000	0.000
61	A	70	SER	0	0.005	-0.011	24.129	0.009	0.009	0.000	0.000	0.000	0.000
62	A	71	GLN	0	0.056	0.007	23.247	0.012	0.012	0.000	0.000	0.000	0.000
63	A	72	SER	0	-0.073	-0.043	23.458	0.017	0.017	0.000	0.000	0.000	0.000
64	A	73	GLU	-1	-0.741	-0.809	20.978	-0.060	-0.060	0.000	0.000	0.000	0.000
65	A	74	PHE	0	0.044	0.007	16.169	0.011	0.011	0.000	0.000	0.000	0.000
66	A	75	LYS	1	0.877	0.938	19.612	-0.019	-0.019	0.000	0.000	0.000	0.000
67	A	76	ASN	0	0.004	-0.001	21.864	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	77	ILE	0	-0.011	0.020	15.354	0.034	0.034	0.000	0.000	0.000	0.000
69	A	78	ARG	1	0.962	0.984	16.092	-0.443	-0.443	0.000	0.000	0.000	0.000
70	A	79	GLY	0	0.038	0.009	13.140	0.021	0.021	0.000	0.000	0.000	0.000
71	A	80	GLU	-1	-0.842	-0.913	11.567	0.242	0.242	0.000	0.000	0.000	0.000
72	A	81	HIS	1	0.776	0.874	12.620	-0.125	-0.125	0.000	0.000	0.000	0.000
73	A	82	ARG	1	0.762	0.855	12.213	-0.105	-0.105	0.000	0.000	0.000	0.000
74	A	83	ARG	1	0.829	0.905	14.325	0.171	0.171	0.000	0.000	0.000	0.000
75	A	84	ILE	0	-0.014	-0.020	12.331	-0.023	-0.023	0.000	0.000	0.000	0.000
76	A	85	PRO	0	-0.010	0.005	14.760	0.041	0.041	0.000	0.000	0.000	0.000
77	A	86	ILE	0	-0.043	-0.008	17.850	-0.039	-0.039	0.000	0.000	0.000	0.000
78	A	87	LEU	0	0.025	0.024	14.820	-0.046	-0.046	0.000	0.000	0.000	0.000
79	A	88	PHE	0	0.016	0.000	19.344	0.043	0.043	0.000	0.000	0.000	0.000
80	A	89	ALA	0	0.002	0.016	19.068	-0.050	-0.050	0.000	0.000	0.000	0.000
81	A	90	GLY	0	0.050	0.008	19.012	0.027	0.027	0.000	0.000	0.000	0.000
82	A	91	ASN	0	-0.036	-0.038	18.940	0.057	0.057	0.000	0.000	0.000	0.000
83	A	92	PRO	0	-0.027	-0.024	20.722	0.020	0.020	0.000	0.000	0.000	0.000
84	A	93	ILE	0	-0.058	-0.025	23.046	0.025	0.025	0.000	0.000	0.000	0.000
85	A	94	HIS	0	0.014	-0.006	22.619	0.028	0.028	0.000	0.000	0.000	0.000
86	A	95	TYR	0	0.013	0.017	23.534	-0.004	-0.004	0.000	0.000	0.000	0.000
87	A	96	GLY	0	0.025	0.014	23.632	0.025	0.025	0.000	0.000	0.000	0.000
88	A	97	ILE	0	-0.042	-0.017	24.609	0.014	0.014	0.000	0.000	0.000	0.000
89	A	98	ALA	0	0.046	0.020	22.847	-0.030	-0.030	0.000	0.000	0.000	0.000
90	A	99	TYR	0	-0.008	-0.032	19.594	0.028	0.028	0.000	0.000	0.000	0.000
91	A	100	LYS	1	0.829	0.945	19.227	0.197	0.197	0.000	0.000	0.000	0.000
92	A	101	LEU	0	-0.041	-0.019	14.550	-0.013	-0.013	0.000	0.000	0.000	0.000
93	A	102	SER	0	-0.018	-0.048	15.856	0.013	0.013	0.000	0.000	0.000	0.000
94	A	103	SER	0	0.035	0.002	12.603	-0.081	-0.081	0.000	0.000	0.000	0.000
95	A	104	ILE	0	-0.006	-0.003	10.318	-0.097	-0.097	0.000	0.000	0.000	0.000
96	A	105	GLU	-1	-0.735	-0.805	10.692	-0.692	-0.692	0.000	0.000	0.000	0.000
97	A	106	ALA	0	0.054	0.029	11.880	-0.087	-0.087	0.000	0.000	0.000	0.000
98	A	107	LEU	0	-0.011	0.011	4.405	-0.119	-0.049	-0.001	-0.005	-0.064	0.000
99	A	108	ILE	0	-0.001	-0.003	7.220	-0.346	-0.346	0.000	0.000	0.000	0.000
100	A	109	ALA	0	0.039	0.014	9.233	-0.152	-0.152	0.000	0.000	0.000	0.000
101	A	110	THR	0	-0.031	-0.040	6.214	0.100	0.100	0.000	0.000	0.000	0.000
102	A	111	LEU	0	-0.032	-0.025	2.636	-0.919	-0.080	0.564	-0.232	-1.171	-0.001
103	A	112	TYR	0	-0.031	-0.045	5.826	-0.094	-0.094	0.000	0.000	0.000	0.000
104	A	113	ILE	0	0.014	0.010	9.207	0.119	0.119	0.000	0.000	0.000	0.000
105	A	114	VAL	0	-0.071	-0.031	4.638	0.150	0.224	-0.001	-0.002	-0.071	0.000
106	A	115	ASP	-1	-0.800	-0.917	6.835	-1.106	-1.106	0.000	0.000	0.000	0.000
107	A	116	GLU	-1	-0.839	-0.878	2.449	-9.224	-8.180	3.374	-1.520	-2.898	-0.021
108	A	117	VAL	0	0.013	-0.009	5.022	-0.230	-0.214	-0.001	-0.002	-0.013	0.000
109	A	118	GLU	-1	-0.834	-0.904	5.999	-2.486	-2.486	0.000	0.000	0.000	0.000
110	A	119	GLU	-1	-0.822	-0.914	2.972	-4.227	-3.402	0.105	-0.154	-0.776	-0.001
111	A	120	ALA	0	-0.044	-0.008	6.067	0.499	0.499	0.000	0.000	0.000	0.000
112	A	121	ILE	0	0.017	0.006	8.376	0.366	0.366	0.000	0.000	0.000	0.000
113	A	122	LYS	1	0.786	0.887	5.870	3.121	3.121	0.000	0.000	0.000	0.000
114	A	123	LEU	0	0.013	0.002	6.383	0.421	0.421	0.000	0.000	0.000	0.000
115	A	124	SER	0	-0.058	-0.047	9.093	0.350	0.350	0.000	0.000	0.000	0.000
116	A	125	ASN	0	0.023	0.017	12.211	0.248	0.248	0.000	0.000	0.000	0.000
117	A	126	VAL	0	-0.034	0.001	10.414	0.151	0.151	0.000	0.000	0.000	0.000
118	A	127	VAL	0	-0.043	-0.031	13.593	0.125	0.125	0.000	0.000	0.000	0.000
119	A	128	LYS	1	1.012	1.008	16.749	0.244	0.244	0.000	0.000	0.000	0.000
120	A	129	TRP	0	0.007	0.000	16.419	0.031	0.031	0.000	0.000	0.000	0.000
121	A	130	GLY	0	0.019	0.016	15.216	-0.001	-0.001	0.000	0.000	0.000	0.000
122	A	131	HIS	0	0.016	-0.007	16.041	-0.001	-0.001	0.000	0.000	0.000	0.000
123	A	132	THR	0	0.014	0.003	17.708	-0.003	-0.003	0.000	0.000	0.000	0.000
124	A	133	PHE	0	-0.008	-0.002	13.246	0.013	0.013	0.000	0.000	0.000	0.000
125	A	134	ILE	0	0.026	0.023	12.484	0.000	0.000	0.000	0.000	0.000	0.000
126	A	135	GLU	-1	-0.808	-0.907	16.714	-0.573	-0.573	0.000	0.000	0.000	0.000
127	A	136	LEU	0	-0.074	-0.019	20.218	0.032	0.032	0.000	0.000	0.000	0.000
128	A	137	ASN	0	-0.009	-0.023	17.653	0.067	0.067	0.000	0.000	0.000	0.000
129	A	138	LYS	1	0.851	0.933	17.637	0.592	0.592	0.000	0.000	0.000	0.000
130	A	139	GLU	-1	-0.893	-0.956	17.771	-0.448	-0.448	0.000	0.000	0.000	0.000
131	A	140	LEU	0	0.010	0.013	18.790	0.016	0.016	0.000	0.000	0.000	0.000
132	A	141	LEU	0	-0.036	-0.016	13.047	-0.020	-0.020	0.000	0.000	0.000	0.000
133	A	142	GLU	-1	-0.747	-0.854	14.401	-0.966	-0.966	0.000	0.000	0.000	0.000
134	A	143	ALA	0	-0.006	0.004	16.254	0.022	0.022	0.000	0.000	0.000	0.000
135	A	144	TYR	0	-0.048	-0.060	14.763	0.044	0.044	0.000	0.000	0.000	0.000
136	A	145	LYS	1	0.813	0.907	10.520	1.043	1.043	0.000	0.000	0.000	0.000
137	A	146	ASN	0	-0.074	-0.043	11.246	0.197	0.197	0.000	0.000	0.000	0.000
138	A	147	LYS	1	0.809	0.931	12.505	0.617	0.617	0.000	0.000	0.000	0.000
139	A	148	THR	0	0.000	-0.033	15.047	0.010	0.010	0.000	0.000	0.000	0.000
140	A	149	GLU	-1	-0.745	-0.856	16.933	-0.106	-0.106	0.000	0.000	0.000	0.000
141	A	150	GLU	-1	-0.846	-0.929	17.787	-0.105	-0.105	0.000	0.000	0.000	0.000
142	A	151	ASP	-1	-0.802	-0.871	19.292	-0.227	-0.227	0.000	0.000	0.000	0.000
143	A	152	ILE	0	-0.034	-0.004	14.586	-0.006	-0.006	0.000	0.000	0.000	0.000
144	A	153	LYS	1	0.890	0.932	18.912	0.119	0.119	0.000	0.000	0.000	0.000
145	A	154	LYS	1	0.734	0.862	21.457	0.187	0.187	0.000	0.000	0.000	0.000
146	A	155	ILE	0	0.030	0.007	20.164	0.008	0.008	0.000	0.000	0.000	0.000
147	A	156	GLU	-1	-0.725	-0.818	20.938	-0.256	-0.256	0.000	0.000	0.000	0.000
148	A	157	ARG	1	0.864	0.899	22.823	0.160	0.160	0.000	0.000	0.000	0.000
149	A	158	GLU	-1	-0.780	-0.855	26.255	-0.162	-0.162	0.000	0.000	0.000	0.000
150	A	159	ILE	0	-0.045	-0.009	22.671	0.000	0.000	0.000	0.000	0.000	0.000
151	A	160	ILE	0	-0.056	-0.009	25.105	0.010	0.010	0.000	0.000	0.000	0.000

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