FMO DATABASE

FMODB ID: 432JN

Calculation Name: 4HFF-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4HFF

Chain ID: A

ChEMBL ID:

UniProt ID: Q8ZRL5

Base Structure: X-ray

Registration Date: 2023-06-20

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. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1570369.230849
FMO2-HF: Nuclear repulsion	1508534.387252
FMO2-HF: Total energy	-61834.843597
FMO2-MP2: Total energy	-62015.174275

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.
-4.059	0.198	0.578	-1.998	-2.836	0.003

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 : 0.010 / q_NPA : -0.004

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	4	PRO	0	0.057	0.040	3.585	-3.548	-1.201	-0.007	-1.155	-1.184	-0.001
4	A	5	SER	0	0.006	-0.021	6.318	0.026	0.026	0.000	0.000	0.000	0.000
5	A	6	PHE	0	0.044	-0.005	7.162	0.408	0.408	0.000	0.000	0.000	0.000
6	A	7	ASN	0	0.001	-0.011	10.134	0.217	0.217	0.000	0.000	0.000	0.000
7	A	8	GLU	-1	-0.858	-0.905	9.585	-1.192	-1.192	0.000	0.000	0.000	0.000
8	A	9	ALA	0	0.026	0.017	10.556	0.151	0.151	0.000	0.000	0.000	0.000
9	A	10	TRP	0	0.024	0.003	12.395	0.127	0.127	0.000	0.000	0.000	0.000
10	A	11	LEU	0	-0.039	-0.012	15.183	0.091	0.091	0.000	0.000	0.000	0.000
11	A	12	ALA	0	0.023	-0.001	14.904	0.076	0.076	0.000	0.000	0.000	0.000
12	A	13	PHE	0	0.035	0.008	16.403	0.063	0.063	0.000	0.000	0.000	0.000
13	A	14	ARG	1	0.959	0.979	18.218	0.400	0.400	0.000	0.000	0.000	0.000
14	A	15	LYS	1	0.900	0.957	20.157	0.321	0.321	0.000	0.000	0.000	0.000
15	A	16	VAL	0	0.018	0.020	19.961	0.028	0.028	0.000	0.000	0.000	0.000
16	A	17	ASN	0	-0.046	-0.017	22.545	0.028	0.028	0.000	0.000	0.000	0.000
17	A	18	HIS	0	0.027	0.019	24.099	0.018	0.018	0.000	0.000	0.000	0.000
18	A	19	SER	0	0.044	0.020	27.340	0.001	0.001	0.000	0.000	0.000	0.000
19	A	20	VAL	0	0.055	0.011	27.183	-0.009	-0.009	0.000	0.000	0.000	0.000
20	A	21	ALA	0	0.065	0.031	28.556	-0.003	-0.003	0.000	0.000	0.000	0.000
21	A	22	ASP	-1	-0.838	-0.920	29.314	-0.139	-0.139	0.000	0.000	0.000	0.000
22	A	23	VAL	0	-0.083	-0.045	23.637	-0.009	-0.009	0.000	0.000	0.000	0.000
23	A	24	GLY	0	0.004	-0.006	25.773	-0.007	-0.007	0.000	0.000	0.000	0.000
24	A	25	SER	0	-0.019	-0.020	27.915	0.004	0.004	0.000	0.000	0.000	0.000
25	A	26	ILE	0	-0.085	-0.023	23.775	-0.003	-0.003	0.000	0.000	0.000	0.000
26	A	27	ILE	0	-0.036	-0.012	21.061	-0.006	-0.006	0.000	0.000	0.000	0.000
27	A	28	GLY	0	0.086	0.049	24.161	0.004	0.004	0.000	0.000	0.000	0.000
28	A	29	GLY	0	0.030	0.000	25.826	-0.003	-0.003	0.000	0.000	0.000	0.000
29	A	30	ASN	0	0.001	-0.007	25.508	0.009	0.009	0.000	0.000	0.000	0.000
30	A	31	VAL	0	0.034	0.035	22.212	0.007	0.007	0.000	0.000	0.000	0.000
31	A	32	GLY	0	0.034	0.021	25.500	0.005	0.005	0.000	0.000	0.000	0.000
32	A	33	LYS	1	0.910	0.966	28.463	0.082	0.082	0.000	0.000	0.000	0.000
33	A	34	ASN	0	-0.049	-0.055	27.649	0.012	0.012	0.000	0.000	0.000	0.000
34	A	35	ILE	0	-0.028	-0.004	26.053	0.004	0.004	0.000	0.000	0.000	0.000
35	A	36	THR	0	-0.033	-0.006	30.213	0.004	0.004	0.000	0.000	0.000	0.000
36	A	37	GLY	0	-0.040	-0.020	33.147	0.004	0.004	0.000	0.000	0.000	0.000
37	A	38	GLY	0	0.025	0.022	33.430	0.005	0.005	0.000	0.000	0.000	0.000
38	A	39	TYR	0	-0.042	-0.015	30.617	0.002	0.002	0.000	0.000	0.000	0.000
39	A	40	PHE	0	-0.075	-0.039	25.097	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	41	GLN	0	0.083	0.029	28.833	-0.004	-0.004	0.000	0.000	0.000	0.000
41	A	42	ASN	0	0.000	-0.004	25.388	-0.015	-0.015	0.000	0.000	0.000	0.000
42	A	43	ALA	0	0.060	0.018	24.291	-0.003	-0.003	0.000	0.000	0.000	0.000
43	A	44	CYS	0	-0.023	0.027	20.681	-0.016	-0.016	0.000	0.000	0.000	0.000
44	A	45	PRO	0	-0.002	0.006	18.597	-0.031	-0.031	0.000	0.000	0.000	0.000
45	A	46	ILE	0	0.052	0.024	18.011	-0.029	-0.029	0.000	0.000	0.000	0.000
46	A	47	ARG	1	0.912	0.955	18.797	0.175	0.175	0.000	0.000	0.000	0.000
47	A	48	MET	0	0.011	0.013	13.879	-0.073	-0.073	0.000	0.000	0.000	0.000
48	A	49	SER	0	-0.002	-0.007	14.113	-0.062	-0.062	0.000	0.000	0.000	0.000
49	A	50	TYR	0	0.003	0.004	14.540	-0.037	-0.037	0.000	0.000	0.000	0.000
50	A	51	VAL	0	-0.025	-0.014	12.107	-0.033	-0.033	0.000	0.000	0.000	0.000
51	A	52	LEU	0	-0.006	0.002	8.607	-0.094	-0.094	0.000	0.000	0.000	0.000
52	A	53	ASN	0	0.000	-0.021	10.631	-0.015	-0.015	0.000	0.000	0.000	0.000
53	A	54	ALA	0	-0.070	-0.027	13.120	0.042	0.042	0.000	0.000	0.000	0.000
54	A	55	THR	0	-0.044	-0.024	9.319	-0.069	-0.069	0.000	0.000	0.000	0.000
55	A	56	GLY	0	0.026	0.024	8.438	-0.220	-0.220	0.000	0.000	0.000	0.000
56	A	57	PHE	0	-0.041	-0.016	2.770	-2.365	-0.828	0.579	-0.758	-1.359	0.004
57	A	58	PRO	0	0.026	0.012	7.591	-0.087	-0.087	0.000	0.000	0.000	0.000
58	A	59	ILE	0	-0.029	0.003	9.824	0.017	0.017	0.000	0.000	0.000	0.000
59	A	60	ALA	0	0.020	0.005	11.413	0.044	0.044	0.000	0.000	0.000	0.000
60	A	61	ARG	1	0.985	0.977	12.962	0.068	0.068	0.000	0.000	0.000	0.000
61	A	62	ASN	0	0.017	-0.003	14.114	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	63	SER	0	-0.017	0.020	13.042	0.016	0.016	0.000	0.000	0.000	0.000
63	A	64	PRO	0	0.031	0.033	14.805	-0.006	-0.006	0.000	0.000	0.000	0.000
64	A	65	TYR	0	0.059	0.012	13.921	0.004	0.004	0.000	0.000	0.000	0.000
65	A	66	ALA	0	-0.021	0.012	18.628	-0.005	-0.005	0.000	0.000	0.000	0.000
66	A	67	LYS	1	0.798	0.885	16.283	0.083	0.083	0.000	0.000	0.000	0.000
67	A	68	VAL	0	-0.017	-0.010	20.373	0.016	0.016	0.000	0.000	0.000	0.000
68	A	69	SER	0	0.012	0.003	21.076	-0.013	-0.013	0.000	0.000	0.000	0.000
69	A	70	GLY	0	0.080	0.035	21.259	0.006	0.006	0.000	0.000	0.000	0.000
70	A	71	ALA	0	-0.033	-0.018	22.841	0.011	0.011	0.000	0.000	0.000	0.000
71	A	72	ASP	-1	-0.793	-0.886	19.191	-0.216	-0.216	0.000	0.000	0.000	0.000
72	A	73	ASN	0	-0.080	-0.042	20.554	0.005	0.005	0.000	0.000	0.000	0.000
73	A	74	LYS	1	0.904	0.977	15.053	0.302	0.302	0.000	0.000	0.000	0.000
74	A	75	PHE	0	-0.005	-0.028	16.107	0.018	0.018	0.000	0.000	0.000	0.000
75	A	76	TYR	0	-0.053	-0.032	16.328	-0.045	-0.045	0.000	0.000	0.000	0.000
76	A	77	ILE	0	0.026	0.018	14.866	0.028	0.028	0.000	0.000	0.000	0.000
77	A	78	TYR	0	0.034	0.007	18.715	-0.006	-0.006	0.000	0.000	0.000	0.000
78	A	79	ARG	1	0.943	0.976	21.094	0.065	0.065	0.000	0.000	0.000	0.000
79	A	80	VAL	0	0.032	0.008	20.257	-0.009	-0.009	0.000	0.000	0.000	0.000
80	A	81	ASN	0	0.013	-0.015	19.532	-0.005	-0.005	0.000	0.000	0.000	0.000
81	A	82	ASP	-1	-0.782	-0.885	18.421	-0.057	-0.057	0.000	0.000	0.000	0.000
82	A	83	MET	0	-0.058	-0.018	14.291	-0.022	-0.022	0.000	0.000	0.000	0.000
83	A	84	ILE	0	0.016	-0.003	14.615	-0.024	-0.024	0.000	0.000	0.000	0.000
84	A	85	ASP	-1	-0.881	-0.934	14.813	0.023	0.023	0.000	0.000	0.000	0.000
85	A	86	TYR	0	0.011	-0.003	8.848	0.069	0.069	0.000	0.000	0.000	0.000
86	A	87	LEU	0	0.012	-0.008	10.230	-0.056	-0.056	0.000	0.000	0.000	0.000
87	A	88	THR	0	-0.010	-0.010	10.063	0.060	0.060	0.000	0.000	0.000	0.000
88	A	89	HIS	0	-0.086	-0.053	11.033	0.143	0.143	0.000	0.000	0.000	0.000
89	A	90	THR	0	-0.080	-0.019	6.654	-0.029	-0.029	0.000	0.000	0.000	0.000
90	A	91	MET	0	-0.008	0.009	4.715	-0.519	-0.417	-0.001	-0.020	-0.080	0.000
91	A	92	GLY	0	0.023	0.019	6.787	0.721	0.721	0.000	0.000	0.000	0.000
92	A	93	LYS	1	0.840	0.919	8.639	-0.719	-0.719	0.000	0.000	0.000	0.000
93	A	94	PRO	0	0.002	0.006	9.961	0.247	0.247	0.000	0.000	0.000	0.000
94	A	95	ASP	-1	-0.806	-0.890	9.346	1.023	1.023	0.000	0.000	0.000	0.000
95	A	96	LEU	0	-0.044	-0.016	12.190	-0.045	-0.045	0.000	0.000	0.000	0.000
96	A	97	ILE	0	-0.003	-0.009	15.788	-0.033	-0.033	0.000	0.000	0.000	0.000
97	A	98	VAL	0	-0.009	0.004	18.615	0.008	0.008	0.000	0.000	0.000	0.000
98	A	99	ASN	0	0.022	-0.004	22.120	-0.016	-0.016	0.000	0.000	0.000	0.000
99	A	100	ASN	0	-0.056	-0.036	25.383	-0.006	-0.006	0.000	0.000	0.000	0.000
100	A	101	PRO	0	-0.038	0.015	23.045	-0.002	-0.002	0.000	0.000	0.000	0.000
101	A	102	LYS	1	0.995	0.986	24.791	-0.021	-0.021	0.000	0.000	0.000	0.000
102	A	103	GLN	0	0.013	0.000	23.699	0.014	0.014	0.000	0.000	0.000	0.000
103	A	104	SER	0	-0.028	-0.024	22.922	-0.005	-0.005	0.000	0.000	0.000	0.000
104	A	105	ASP	-1	-0.857	-0.926	22.092	0.028	0.028	0.000	0.000	0.000	0.000
105	A	106	PHE	0	-0.045	-0.028	17.308	0.019	0.019	0.000	0.000	0.000	0.000
106	A	107	ILE	0	0.030	0.035	18.430	-0.040	-0.040	0.000	0.000	0.000	0.000
107	A	108	GLY	0	-0.027	-0.010	18.085	0.019	0.019	0.000	0.000	0.000	0.000
108	A	109	LYS	1	0.922	0.961	13.839	-0.080	-0.080	0.000	0.000	0.000	0.000
109	A	110	LYS	1	0.960	0.985	11.506	0.682	0.682	0.000	0.000	0.000	0.000
110	A	111	GLY	0	-0.010	-0.013	11.066	-0.059	-0.059	0.000	0.000	0.000	0.000
111	A	112	ILE	0	0.004	0.003	9.869	0.009	0.009	0.000	0.000	0.000	0.000
112	A	113	ILE	0	0.010	0.012	13.264	0.092	0.092	0.000	0.000	0.000	0.000
113	A	114	VAL	0	-0.021	-0.015	15.677	-0.030	-0.030	0.000	0.000	0.000	0.000
114	A	115	VAL	0	0.037	0.023	18.047	0.032	0.032	0.000	0.000	0.000	0.000
115	A	116	LYS	1	0.911	0.961	20.806	-0.018	-0.018	0.000	0.000	0.000	0.000
116	A	117	GLY	0	0.109	0.048	23.836	0.008	0.008	0.000	0.000	0.000	0.000
117	A	118	HIS	1	0.786	0.880	27.591	-0.006	-0.006	0.000	0.000	0.000	0.000
118	A	119	GLY	0	0.070	0.026	31.077	-0.003	-0.003	0.000	0.000	0.000	0.000
119	A	120	TRP	0	0.012	0.026	25.792	-0.004	-0.004	0.000	0.000	0.000	0.000
120	A	121	SER	0	-0.016	-0.017	32.001	0.006	0.006	0.000	0.000	0.000	0.000
121	A	122	ASN	0	0.002	0.001	28.739	0.005	0.005	0.000	0.000	0.000	0.000
122	A	123	ALA	0	-0.029	-0.019	25.673	-0.005	-0.005	0.000	0.000	0.000	0.000
123	A	124	ARG	1	0.943	0.971	25.015	0.014	0.014	0.000	0.000	0.000	0.000
124	A	125	GLY	0	0.042	0.019	23.860	0.011	0.011	0.000	0.000	0.000	0.000
125	A	126	HIS	0	-0.021	-0.013	22.336	0.003	0.003	0.000	0.000	0.000	0.000
126	A	127	VAL	0	-0.002	-0.010	15.782	0.014	0.014	0.000	0.000	0.000	0.000
127	A	128	THR	0	-0.018	-0.027	17.856	-0.030	-0.030	0.000	0.000	0.000	0.000
128	A	129	LEU	0	0.011	0.015	13.286	-0.024	-0.024	0.000	0.000	0.000	0.000
129	A	130	TRP	0	0.013	0.003	15.460	0.041	0.041	0.000	0.000	0.000	0.000
130	A	131	ASN	0	0.042	0.007	15.279	-0.034	-0.034	0.000	0.000	0.000	0.000
131	A	132	GLY	0	0.004	0.014	17.098	-0.015	-0.015	0.000	0.000	0.000	0.000
132	A	133	SER	0	-0.057	-0.038	18.374	0.036	0.036	0.000	0.000	0.000	0.000
133	A	134	ILE	0	0.053	0.031	21.138	0.022	0.022	0.000	0.000	0.000	0.000
134	A	135	CYS	0	-0.027	-0.007	20.265	-0.024	-0.024	0.000	0.000	0.000	0.000
135	A	136	SER	0	-0.024	-0.020	18.543	-0.002	-0.002	0.000	0.000	0.000	0.000
136	A	137	ASP	-1	-0.838	-0.886	20.606	-0.192	-0.192	0.000	0.000	0.000	0.000
137	A	138	GLN	0	-0.023	-0.034	23.514	0.020	0.020	0.000	0.000	0.000	0.000
138	A	139	CYS	0	-0.023	-0.037	24.567	0.005	0.005	0.000	0.000	0.000	0.000
139	A	140	HIS	0	0.061	0.031	24.885	-0.006	-0.006	0.000	0.000	0.000	0.000
140	A	141	LEU	0	0.041	0.037	23.772	0.010	0.010	0.000	0.000	0.000	0.000
141	A	142	LEU	0	-0.061	-0.019	21.839	0.013	0.013	0.000	0.000	0.000	0.000
142	A	143	ASN	0	-0.079	-0.074	25.635	0.011	0.011	0.000	0.000	0.000	0.000
143	A	144	ASP	-1	-0.870	-0.910	28.837	-0.076	-0.076	0.000	0.000	0.000	0.000
144	A	145	PRO	0	0.021	-0.001	30.426	0.003	0.003	0.000	0.000	0.000	0.000
145	A	146	ASP	-1	-0.904	-0.934	33.057	-0.043	-0.043	0.000	0.000	0.000	0.000
146	A	147	ASN	0	-0.084	-0.054	35.078	0.000	0.000	0.000	0.000	0.000	0.000
147	A	148	GLY	0	0.021	0.023	34.392	-0.003	-0.003	0.000	0.000	0.000	0.000
148	A	149	PRO	0	-0.013	-0.010	33.916	0.005	0.005	0.000	0.000	0.000	0.000
149	A	150	PHE	0	-0.052	-0.026	25.833	0.005	0.005	0.000	0.000	0.000	0.000
150	A	151	VAL	0	0.039	0.011	31.130	0.000	0.000	0.000	0.000	0.000	0.000
151	A	152	PRO	0	-0.010	-0.008	25.856	0.006	0.006	0.000	0.000	0.000	0.000
152	A	153	GLU	-1	-0.833	-0.893	26.598	0.026	0.026	0.000	0.000	0.000	0.000
153	A	154	VAL	0	-0.002	0.001	20.927	0.013	0.013	0.000	0.000	0.000	0.000
154	A	155	GLY	0	0.007	0.009	20.808	-0.024	-0.024	0.000	0.000	0.000	0.000
155	A	156	THR	0	-0.036	-0.026	14.837	0.049	0.049	0.000	0.000	0.000	0.000
156	A	157	LEU	0	0.004	-0.001	12.750	-0.064	-0.064	0.000	0.000	0.000	0.000
157	A	158	TRP	0	0.007	0.012	8.477	0.031	0.031	0.000	0.000	0.000	0.000
158	A	159	ILE	0	-0.007	-0.010	7.731	-0.272	-0.272	0.000	0.000	0.000	0.000
159	A	160	LEU	0	-0.044	-0.018	6.719	0.091	0.091	0.000	0.000	0.000	0.000
160	A	161	PRO	0	-0.011	0.009	3.531	0.294	0.565	0.007	-0.065	-0.213	0.000

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