FMO DATABASE

FMODB ID: KG513

Calculation Name: 4IPV-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4IPV

Chain ID: A

ChEMBL ID:

UniProt ID: G3XCZ0

Base Structure: X-ray

Registration Date: 2023-09-23

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	128
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1060163.703341
FMO2-HF: Nuclear repulsion	1011989.214286
FMO2-HF: Total energy	-48174.489055
FMO2-MP2: Total energy	-48315.630587

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:31:ASN)

Summations of interaction energy for fragment #1(A:31: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.
1.172	5.161	0.833	-1.779	-3.04	0.001

Interaction energy analysis for fragmet #1(A:31:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.059 / q_NPA : 0.016

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	33	LEU	0	-0.009	-0.003	3.656	-1.090	0.647	-0.004	-0.768	-0.964	0.001
4	A	34	GLN	0	-0.029	-0.022	3.024	-0.407	0.246	0.072	-0.161	-0.563	0.000
5	A	35	SER	0	0.028	0.002	2.898	-1.668	-0.145	0.766	-0.845	-1.444	0.000
6	A	36	ALA	0	0.023	0.014	5.305	0.684	0.760	-0.001	-0.005	-0.069	0.000
7	A	37	ALA	0	-0.014	-0.009	8.040	0.434	0.434	0.000	0.000	0.000	0.000
8	A	38	GLU	-1	-0.854	-0.915	7.501	0.723	0.723	0.000	0.000	0.000	0.000
9	A	39	GLU	-1	-0.787	-0.843	8.228	-2.087	-2.087	0.000	0.000	0.000	0.000
10	A	40	LEU	0	0.015	0.009	10.796	0.185	0.185	0.000	0.000	0.000	0.000
11	A	41	ASN	0	0.014	0.004	13.130	0.149	0.149	0.000	0.000	0.000	0.000
12	A	42	ALA	0	-0.001	-0.006	12.792	0.082	0.082	0.000	0.000	0.000	0.000
13	A	43	MET	0	-0.045	0.001	14.602	0.048	0.048	0.000	0.000	0.000	0.000
14	A	44	LEU	0	0.015	-0.004	16.849	0.067	0.067	0.000	0.000	0.000	0.000
15	A	45	GLN	0	-0.025	-0.029	17.508	0.051	0.051	0.000	0.000	0.000	0.000
16	A	46	TYR	0	-0.030	-0.029	18.834	0.011	0.011	0.000	0.000	0.000	0.000
17	A	47	ALA	0	0.062	0.030	20.497	0.027	0.027	0.000	0.000	0.000	0.000
18	A	48	ARG	1	0.879	0.944	22.815	0.125	0.125	0.000	0.000	0.000	0.000
19	A	49	SER	0	-0.055	-0.039	22.948	0.020	0.020	0.000	0.000	0.000	0.000
20	A	50	GLU	-1	-0.746	-0.835	24.151	-0.157	-0.157	0.000	0.000	0.000	0.000
21	A	51	ALA	0	-0.020	0.003	26.493	0.012	0.012	0.000	0.000	0.000	0.000
22	A	52	VAL	0	-0.032	-0.024	28.017	0.014	0.014	0.000	0.000	0.000	0.000
23	A	53	SER	0	-0.047	-0.039	27.324	0.014	0.014	0.000	0.000	0.000	0.000
24	A	54	GLN	0	-0.020	-0.021	28.128	0.011	0.011	0.000	0.000	0.000	0.000
25	A	55	ARG	1	0.865	0.940	32.003	0.069	0.069	0.000	0.000	0.000	0.000
26	A	56	ARG	1	0.893	0.941	31.512	0.137	0.137	0.000	0.000	0.000	0.000
27	A	57	ALA	0	-0.009	-0.002	31.780	-0.004	-0.004	0.000	0.000	0.000	0.000
28	A	58	ILE	0	-0.035	-0.001	26.116	-0.004	-0.004	0.000	0.000	0.000	0.000
29	A	59	SER	0	-0.017	-0.025	26.924	0.008	0.008	0.000	0.000	0.000	0.000
30	A	60	ILE	0	-0.017	-0.014	19.058	-0.011	-0.011	0.000	0.000	0.000	0.000
31	A	61	GLN	0	-0.023	-0.035	23.072	0.017	0.017	0.000	0.000	0.000	0.000
32	A	62	ALA	0	0.009	0.004	20.608	-0.034	-0.034	0.000	0.000	0.000	0.000
33	A	63	LEU	0	-0.035	-0.022	20.978	0.030	0.030	0.000	0.000	0.000	0.000
34	A	64	LYS	1	0.927	0.947	20.721	0.348	0.348	0.000	0.000	0.000	0.000
35	A	65	ASP	-1	-0.828	-0.897	21.538	-0.328	-0.328	0.000	0.000	0.000	0.000
36	A	66	LYS	1	0.888	0.945	23.131	0.248	0.248	0.000	0.000	0.000	0.000
37	A	67	ASP	-1	-0.805	-0.886	16.585	-0.512	-0.512	0.000	0.000	0.000	0.000
38	A	68	TRP	0	0.016	-0.020	17.409	-0.037	-0.037	0.000	0.000	0.000	0.000
39	A	69	GLY	0	0.018	-0.006	13.750	-0.066	-0.066	0.000	0.000	0.000	0.000
40	A	70	LYS	1	0.750	0.873	13.950	0.458	0.458	0.000	0.000	0.000	0.000
41	A	71	GLY	0	0.058	0.044	16.444	0.036	0.036	0.000	0.000	0.000	0.000
42	A	72	LEU	0	-0.024	-0.016	15.814	0.063	0.063	0.000	0.000	0.000	0.000
43	A	73	SER	0	0.028	0.006	19.268	-0.026	-0.026	0.000	0.000	0.000	0.000
44	A	74	ILE	0	0.015	0.007	19.259	0.010	0.010	0.000	0.000	0.000	0.000
45	A	75	GLY	0	0.053	0.016	23.331	0.001	0.001	0.000	0.000	0.000	0.000
46	A	76	VAL	0	0.026	0.015	26.976	0.006	0.006	0.000	0.000	0.000	0.000
47	A	77	LEU	0	-0.023	0.007	29.195	-0.007	-0.007	0.000	0.000	0.000	0.000
48	A	78	ALA	0	0.003	-0.008	30.966	0.014	0.014	0.000	0.000	0.000	0.000
49	A	79	SER	0	-0.019	-0.020	33.818	-0.006	-0.006	0.000	0.000	0.000	0.000
50	A	80	GLY	0	0.064	0.050	32.308	0.001	0.001	0.000	0.000	0.000	0.000
51	A	81	SER	0	-0.014	-0.017	29.432	-0.016	-0.016	0.000	0.000	0.000	0.000
52	A	82	ILE	0	-0.044	-0.005	25.182	0.012	0.012	0.000	0.000	0.000	0.000
53	A	83	ALA	0	0.000	0.000	28.343	-0.014	-0.014	0.000	0.000	0.000	0.000
54	A	84	ALA	0	0.001	0.004	29.688	0.001	0.001	0.000	0.000	0.000	0.000
55	A	85	PRO	0	-0.065	-0.032	24.199	0.005	0.005	0.000	0.000	0.000	0.000
56	A	86	LEU	0	0.004	0.010	24.719	0.005	0.005	0.000	0.000	0.000	0.000
57	A	87	ARG	1	0.877	0.946	14.933	0.464	0.464	0.000	0.000	0.000	0.000
58	A	88	LYS	1	0.846	0.909	19.400	0.510	0.510	0.000	0.000	0.000	0.000
59	A	89	HIS	0	-0.034	-0.029	10.955	0.153	0.153	0.000	0.000	0.000	0.000
60	A	90	ASP	-1	-0.842	-0.914	14.714	-0.549	-0.549	0.000	0.000	0.000	0.000
61	A	91	GLY	0	0.025	0.022	13.552	0.061	0.061	0.000	0.000	0.000	0.000
62	A	92	PHE	0	-0.057	-0.011	9.107	-0.186	-0.186	0.000	0.000	0.000	0.000
63	A	93	ARG	1	0.814	0.873	7.147	2.664	2.664	0.000	0.000	0.000	0.000
64	A	94	ALA	0	-0.006	-0.001	8.421	0.350	0.350	0.000	0.000	0.000	0.000
65	A	95	ALA	0	0.024	0.008	10.050	0.059	0.059	0.000	0.000	0.000	0.000
66	A	96	THR	0	-0.016	-0.028	11.012	0.028	0.028	0.000	0.000	0.000	0.000
67	A	97	LEU	0	-0.036	-0.008	7.304	0.113	0.113	0.000	0.000	0.000	0.000
68	A	98	THR	0	-0.083	-0.045	11.415	0.023	0.023	0.000	0.000	0.000	0.000
69	A	99	ALA	0	0.003	-0.001	13.378	0.004	0.004	0.000	0.000	0.000	0.000
70	A	100	LYS	1	0.941	0.978	15.006	0.280	0.280	0.000	0.000	0.000	0.000
71	A	101	GLU	-1	-0.713	-0.833	18.471	-0.152	-0.152	0.000	0.000	0.000	0.000
72	A	102	LYS	1	0.867	0.922	21.047	0.117	0.117	0.000	0.000	0.000	0.000
73	A	103	SER	0	-0.092	-0.066	22.887	0.018	0.018	0.000	0.000	0.000	0.000
74	A	104	ALA	0	-0.037	-0.019	23.770	0.003	0.003	0.000	0.000	0.000	0.000
75	A	105	VAL	0	-0.008	-0.001	24.171	-0.003	-0.003	0.000	0.000	0.000	0.000
76	A	106	GLU	-1	-0.849	-0.917	23.921	-0.251	-0.251	0.000	0.000	0.000	0.000
77	A	107	HIS	0	-0.013	-0.006	24.190	-0.019	-0.019	0.000	0.000	0.000	0.000
78	A	108	LEU	0	-0.029	-0.010	22.931	0.017	0.017	0.000	0.000	0.000	0.000
79	A	109	THR	0	0.029	0.013	26.454	-0.016	-0.016	0.000	0.000	0.000	0.000
80	A	110	PHE	0	0.020	0.023	23.012	0.013	0.013	0.000	0.000	0.000	0.000
81	A	111	THR	0	0.030	-0.003	28.577	0.002	0.002	0.000	0.000	0.000	0.000
82	A	112	ALA	0	0.062	0.041	30.799	0.000	0.000	0.000	0.000	0.000	0.000
83	A	113	ASN	0	0.005	0.022	32.821	0.002	0.002	0.000	0.000	0.000	0.000
84	A	114	GLY	0	0.029	0.011	28.595	0.007	0.007	0.000	0.000	0.000	0.000
85	A	115	THR	0	-0.025	-0.012	28.130	-0.003	-0.003	0.000	0.000	0.000	0.000
86	A	116	LEU	0	0.013	0.001	25.198	-0.009	-0.009	0.000	0.000	0.000	0.000
87	A	117	VAL	0	-0.021	0.002	29.209	0.013	0.013	0.000	0.000	0.000	0.000
88	A	118	PRO	0	0.040	0.006	31.276	-0.008	-0.008	0.000	0.000	0.000	0.000
89	A	119	PRO	0	0.034	0.023	30.607	-0.009	-0.009	0.000	0.000	0.000	0.000
90	A	120	THR	0	-0.045	-0.038	28.715	0.005	0.005	0.000	0.000	0.000	0.000
91	A	121	GLU	-1	-0.799	-0.894	25.402	-0.077	-0.077	0.000	0.000	0.000	0.000
92	A	122	ARG	1	0.873	0.948	23.139	0.142	0.142	0.000	0.000	0.000	0.000
93	A	123	THR	0	-0.029	-0.034	19.515	0.017	0.017	0.000	0.000	0.000	0.000
94	A	124	PHE	0	0.025	0.023	16.596	0.000	0.000	0.000	0.000	0.000	0.000
95	A	125	ALA	0	0.003	0.015	15.129	0.021	0.021	0.000	0.000	0.000	0.000
96	A	126	ILE	0	-0.012	-0.013	9.715	-0.033	-0.033	0.000	0.000	0.000	0.000
97	A	127	CYS	0	0.025	0.025	10.839	0.037	0.037	0.000	0.000	0.000	0.000
98	A	128	GLN	0	0.116	0.066	7.018	-0.272	-0.272	0.000	0.000	0.000	0.000
99	A	129	ASN	0	-0.006	-0.014	10.342	0.023	0.023	0.000	0.000	0.000	0.000
100	A	130	GLY	0	0.011	0.017	13.494	0.024	0.024	0.000	0.000	0.000	0.000
101	A	131	LYS	1	0.806	0.891	10.245	-0.116	-0.116	0.000	0.000	0.000	0.000
102	A	132	THR	0	0.045	-0.008	12.923	-0.023	-0.023	0.000	0.000	0.000	0.000
103	A	133	ASP	-1	-0.803	-0.877	12.359	0.117	0.117	0.000	0.000	0.000	0.000
104	A	134	GLY	0	0.000	0.008	8.476	0.021	0.021	0.000	0.000	0.000	0.000
105	A	135	GLY	0	-0.006	0.008	7.675	-0.126	-0.126	0.000	0.000	0.000	0.000
106	A	136	ARG	1	0.785	0.863	7.742	0.145	0.145	0.000	0.000	0.000	0.000
107	A	137	VAL	0	0.019	0.017	11.332	-0.024	-0.024	0.000	0.000	0.000	0.000
108	A	138	LEU	0	-0.004	-0.007	13.673	0.005	0.005	0.000	0.000	0.000	0.000
109	A	139	SER	0	-0.001	-0.012	16.149	-0.013	-0.013	0.000	0.000	0.000	0.000
110	A	140	ILE	0	-0.005	-0.020	19.906	-0.009	-0.009	0.000	0.000	0.000	0.000
111	A	141	SER	0	0.057	0.037	22.684	0.000	0.000	0.000	0.000	0.000	0.000
112	A	142	GLN	0	0.000	-0.006	25.862	-0.006	-0.006	0.000	0.000	0.000	0.000
113	A	143	ALA	0	-0.034	-0.010	28.819	-0.002	-0.002	0.000	0.000	0.000	0.000
114	A	144	GLY	0	-0.017	-0.011	26.510	0.002	0.002	0.000	0.000	0.000	0.000
115	A	145	ARG	1	0.845	0.916	24.382	0.042	0.042	0.000	0.000	0.000	0.000
116	A	146	ILE	0	0.000	0.016	18.289	0.003	0.003	0.000	0.000	0.000	0.000
117	A	147	GLN	0	-0.008	-0.009	17.884	0.036	0.036	0.000	0.000	0.000	0.000
118	A	148	LEU	0	-0.003	0.004	9.858	-0.029	-0.029	0.000	0.000	0.000	0.000
119	A	149	GLU	-1	-0.773	-0.854	14.512	0.041	0.041	0.000	0.000	0.000	0.000
120	A	150	PRO	0	0.049	0.026	12.796	-0.015	-0.015	0.000	0.000	0.000	0.000
121	A	151	SER	0	0.017	-0.011	9.296	-0.051	-0.051	0.000	0.000	0.000	0.000
122	A	152	SER	0	-0.012	0.002	11.237	-0.017	-0.017	0.000	0.000	0.000	0.000
123	A	153	LYS	1	0.824	0.914	14.107	0.011	0.011	0.000	0.000	0.000	0.000
124	A	154	ALA	0	0.046	0.029	13.262	-0.040	-0.040	0.000	0.000	0.000	0.000
125	A	155	PRO	0	-0.048	-0.020	13.177	0.010	0.010	0.000	0.000	0.000	0.000
126	A	156	GLN	0	0.010	-0.005	16.111	0.006	0.006	0.000	0.000	0.000	0.000
127	A	157	SER	0	0.012	0.003	18.719	0.003	0.003	0.000	0.000	0.000	0.000
128	A	159	TYR	0	0.011	0.008	17.265	-0.034	-0.034	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:31:ASN)