FMO DATABASE

FMODB ID: ZVV1N

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1136077.707836
FMO2-HF: Nuclear repulsion	1086279.376091
FMO2-HF: Total energy	-49798.331745
FMO2-MP2: Total energy	-49945.34334

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.
-4.057	-0.251	1.718	-2.022	-3.501	0.004

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 : -0.021

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	MET	0	-0.037	-0.006	3.850	-1.290	0.240	-0.011	-0.732	-0.787	0.001
4	A	5	ASN	0	-0.007	0.006	6.174	0.185	0.185	0.000	0.000	0.000	0.000
5	A	6	VAL	0	-0.009	-0.011	9.590	-0.027	-0.027	0.000	0.000	0.000	0.000
6	A	7	ILE	0	-0.001	0.009	12.391	-0.037	-0.037	0.000	0.000	0.000	0.000
7	A	8	ILE	0	-0.040	-0.018	16.106	0.026	0.026	0.000	0.000	0.000	0.000
8	A	9	ALA	0	-0.012	-0.015	18.683	-0.028	-0.028	0.000	0.000	0.000	0.000
9	A	10	ASP	-1	-0.722	-0.897	22.061	0.192	0.192	0.000	0.000	0.000	0.000
10	A	11	ASP	-1	-0.880	-0.935	25.243	0.127	0.127	0.000	0.000	0.000	0.000
11	A	12	HIS	0	0.015	0.027	27.822	-0.013	-0.013	0.000	0.000	0.000	0.000
12	A	13	PRO	0	0.053	0.018	26.868	0.014	0.014	0.000	0.000	0.000	0.000
13	A	14	ILE	0	-0.034	-0.026	26.022	0.009	0.009	0.000	0.000	0.000	0.000
14	A	15	VAL	0	0.003	0.002	23.241	0.012	0.012	0.000	0.000	0.000	0.000
15	A	16	LEU	0	0.004	0.007	21.777	0.030	0.030	0.000	0.000	0.000	0.000
16	A	17	PHE	0	-0.026	-0.004	21.096	0.018	0.018	0.000	0.000	0.000	0.000
17	A	18	GLY	0	0.005	-0.003	21.312	0.009	0.009	0.000	0.000	0.000	0.000
18	A	19	ILE	0	0.011	0.006	16.988	0.031	0.031	0.000	0.000	0.000	0.000
19	A	20	ARG	1	0.858	0.899	16.893	-0.131	-0.131	0.000	0.000	0.000	0.000
20	A	21	LYS	1	0.851	0.935	16.653	-0.150	-0.150	0.000	0.000	0.000	0.000
21	A	22	SER	0	-0.051	-0.031	15.772	0.030	0.030	0.000	0.000	0.000	0.000
22	A	23	LEU	0	0.003	-0.024	11.889	0.063	0.063	0.000	0.000	0.000	0.000
23	A	24	GLU	-1	-0.910	-0.952	11.900	0.274	0.274	0.000	0.000	0.000	0.000
24	A	25	GLN	0	-0.074	-0.029	13.346	-0.088	-0.088	0.000	0.000	0.000	0.000
25	A	26	ILE	0	-0.079	-0.035	7.334	0.016	0.016	0.000	0.000	0.000	0.000
26	A	27	GLU	-1	-0.918	-0.955	4.507	-0.902	-0.814	-0.001	-0.011	-0.076	0.000
27	A	28	TRP	0	-0.016	-0.011	3.231	-1.154	0.349	0.222	-0.499	-1.226	0.003
28	A	29	VAL	0	-0.005	0.000	5.080	-0.372	-0.382	-0.001	-0.009	0.021	0.000
29	A	30	ASN	0	0.031	0.041	8.131	-0.217	-0.217	0.000	0.000	0.000	0.000
30	A	31	VAL	0	0.021	0.005	11.039	0.012	0.012	0.000	0.000	0.000	0.000
31	A	32	VAL	0	-0.008	-0.004	12.532	-0.049	-0.049	0.000	0.000	0.000	0.000
32	A	33	GLY	0	-0.010	-0.010	15.318	-0.035	-0.035	0.000	0.000	0.000	0.000
33	A	34	GLU	-1	-0.803	-0.869	18.275	0.228	0.228	0.000	0.000	0.000	0.000
34	A	35	PHE	0	-0.075	-0.045	19.697	-0.022	-0.022	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.851	-0.938	23.887	0.133	0.133	0.000	0.000	0.000	0.000
36	A	37	ASP	-1	-0.776	-0.888	26.629	0.093	0.093	0.000	0.000	0.000	0.000
37	A	38	SER	0	-0.004	-0.023	25.836	0.003	0.003	0.000	0.000	0.000	0.000
38	A	39	THR	0	-0.029	-0.033	26.412	-0.002	-0.002	0.000	0.000	0.000	0.000
39	A	40	ALA	0	-0.049	-0.017	26.589	-0.002	-0.002	0.000	0.000	0.000	0.000
40	A	41	LEU	0	0.045	0.035	20.070	0.000	0.000	0.000	0.000	0.000	0.000
41	A	42	ILE	0	-0.023	-0.009	22.344	0.004	0.004	0.000	0.000	0.000	0.000
42	A	43	ASN	0	-0.038	-0.029	23.917	-0.004	-0.004	0.000	0.000	0.000	0.000
43	A	44	ASN	0	-0.074	-0.070	22.143	-0.014	-0.014	0.000	0.000	0.000	0.000
44	A	45	LEU	0	0.035	0.037	17.393	0.003	0.003	0.000	0.000	0.000	0.000
45	A	46	PRO	0	-0.028	-0.014	18.316	0.007	0.007	0.000	0.000	0.000	0.000
46	A	47	LYS	1	0.820	0.922	19.094	-0.089	-0.089	0.000	0.000	0.000	0.000
47	A	48	LEU	0	-0.005	0.020	16.079	-0.006	-0.006	0.000	0.000	0.000	0.000
48	A	49	ASP	-1	-0.882	-0.932	11.922	0.191	0.191	0.000	0.000	0.000	0.000
49	A	50	ALA	0	-0.064	-0.041	11.093	0.042	0.042	0.000	0.000	0.000	0.000
50	A	51	HIS	0	0.012	-0.003	6.495	-0.095	-0.095	0.000	0.000	0.000	0.000
51	A	52	VAL	0	-0.010	-0.008	9.578	-0.013	-0.013	0.000	0.000	0.000	0.000
52	A	53	LEU	0	-0.010	-0.003	12.213	0.001	0.001	0.000	0.000	0.000	0.000
53	A	54	ILE	0	-0.015	-0.012	13.741	0.009	0.009	0.000	0.000	0.000	0.000
54	A	55	THR	0	0.003	-0.020	17.478	-0.022	-0.022	0.000	0.000	0.000	0.000
55	A	56	ASP	-1	-0.805	-0.885	21.101	0.177	0.177	0.000	0.000	0.000	0.000
56	A	57	LEU	0	-0.059	-0.047	24.605	-0.005	-0.005	0.000	0.000	0.000	0.000
57	A	58	SER	0	-0.032	-0.004	26.965	-0.009	-0.009	0.000	0.000	0.000	0.000
58	A	59	MET	0	-0.006	0.028	24.606	-0.002	-0.002	0.000	0.000	0.000	0.000
59	A	60	PRO	0	0.023	0.015	29.597	-0.004	-0.004	0.000	0.000	0.000	0.000
60	A	61	GLY	0	0.087	0.018	30.099	0.007	0.007	0.000	0.000	0.000	0.000
61	A	62	ASP	-1	-0.956	-0.951	31.577	0.076	0.076	0.000	0.000	0.000	0.000
62	A	63	LYS	1	0.863	0.931	31.700	-0.074	-0.074	0.000	0.000	0.000	0.000
63	A	64	TYR	0	-0.007	-0.024	28.368	-0.005	-0.005	0.000	0.000	0.000	0.000
64	A	65	GLY	0	0.019	0.029	29.857	0.003	0.003	0.000	0.000	0.000	0.000
65	A	66	ASP	-1	-0.850	-0.915	28.535	0.118	0.118	0.000	0.000	0.000	0.000
66	A	67	GLY	0	0.028	-0.008	28.411	-0.005	-0.005	0.000	0.000	0.000	0.000
67	A	68	ILE	0	0.002	-0.008	27.348	0.004	0.004	0.000	0.000	0.000	0.000
68	A	69	THR	0	-0.041	-0.019	28.064	0.000	0.000	0.000	0.000	0.000	0.000
69	A	70	LEU	0	0.029	0.042	24.660	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	71	ILE	0	0.030	0.005	22.351	0.003	0.003	0.000	0.000	0.000	0.000
71	A	72	LYS	1	0.953	0.974	23.790	-0.098	-0.098	0.000	0.000	0.000	0.000
72	A	73	TYR	0	0.000	0.001	24.875	-0.004	-0.004	0.000	0.000	0.000	0.000
73	A	74	ILE	0	0.038	0.006	19.689	-0.005	-0.005	0.000	0.000	0.000	0.000
74	A	75	LYS	1	0.920	0.971	18.178	-0.186	-0.186	0.000	0.000	0.000	0.000
75	A	76	ARG	1	0.916	0.972	21.812	-0.090	-0.090	0.000	0.000	0.000	0.000
76	A	77	HIS	0	-0.073	-0.046	23.238	-0.013	-0.013	0.000	0.000	0.000	0.000
77	A	78	PHE	0	-0.001	-0.003	17.877	-0.004	-0.004	0.000	0.000	0.000	0.000
78	A	79	PRO	0	0.015	0.014	18.110	0.013	0.013	0.000	0.000	0.000	0.000
79	A	80	SER	0	-0.042	-0.026	13.536	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	81	LEU	0	-0.031	0.011	13.183	0.009	0.009	0.000	0.000	0.000	0.000
81	A	82	SER	0	-0.032	-0.003	11.979	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	83	ILE	0	-0.012	-0.021	13.894	0.010	0.010	0.000	0.000	0.000	0.000
83	A	84	ILE	0	-0.032	-0.019	13.494	0.011	0.011	0.000	0.000	0.000	0.000
84	A	85	VAL	0	0.006	0.005	17.439	-0.013	-0.013	0.000	0.000	0.000	0.000
85	A	86	LEU	0	-0.008	0.000	19.770	0.019	0.019	0.000	0.000	0.000	0.000
86	A	87	THR	0	0.023	0.001	22.693	-0.027	-0.027	0.000	0.000	0.000	0.000
87	A	88	MET	0	0.025	0.014	25.977	0.011	0.011	0.000	0.000	0.000	0.000
88	A	89	ASN	0	-0.025	-0.012	28.968	-0.005	-0.005	0.000	0.000	0.000	0.000
89	A	90	ASN	0	0.125	0.049	27.153	0.014	0.014	0.000	0.000	0.000	0.000
90	A	91	ASN	0	-0.013	0.002	29.531	-0.006	-0.006	0.000	0.000	0.000	0.000
91	A	92	PRO	0	0.031	0.001	31.119	0.004	0.004	0.000	0.000	0.000	0.000
92	A	93	ALA	0	-0.019	-0.008	31.576	0.003	0.003	0.000	0.000	0.000	0.000
93	A	94	ILE	0	0.015	-0.005	28.919	0.001	0.001	0.000	0.000	0.000	0.000
94	A	95	LEU	0	0.008	0.002	26.164	0.004	0.004	0.000	0.000	0.000	0.000
95	A	96	SER	0	-0.006	0.013	27.042	0.007	0.007	0.000	0.000	0.000	0.000
96	A	97	ALA	0	0.048	0.031	28.426	0.001	0.001	0.000	0.000	0.000	0.000
97	A	98	VAL	0	0.012	-0.007	23.761	-0.002	-0.002	0.000	0.000	0.000	0.000
98	A	99	LEU	0	-0.038	-0.025	22.489	0.008	0.008	0.000	0.000	0.000	0.000
99	A	100	ASP	-1	-0.908	-0.938	24.232	0.128	0.128	0.000	0.000	0.000	0.000
100	A	101	LEU	0	-0.140	-0.073	24.349	-0.008	-0.008	0.000	0.000	0.000	0.000
101	A	102	ASP	-1	-0.916	-0.953	19.929	0.180	0.180	0.000	0.000	0.000	0.000
102	A	103	ILE	0	-0.055	-0.013	18.847	0.006	0.006	0.000	0.000	0.000	0.000
103	A	104	GLU	-1	-0.822	-0.919	13.682	0.259	0.259	0.000	0.000	0.000	0.000
104	A	105	GLY	0	-0.002	-0.017	16.566	0.040	0.040	0.000	0.000	0.000	0.000
105	A	106	ILE	0	-0.031	-0.002	17.798	-0.029	-0.029	0.000	0.000	0.000	0.000
106	A	107	VAL	0	0.008	0.002	17.625	0.020	0.020	0.000	0.000	0.000	0.000
107	A	108	LEU	0	0.014	0.005	20.884	-0.024	-0.024	0.000	0.000	0.000	0.000
108	A	109	LYS	1	0.857	0.911	23.022	-0.166	-0.166	0.000	0.000	0.000	0.000
109	A	110	GLN	0	-0.059	-0.057	23.591	0.010	0.010	0.000	0.000	0.000	0.000
110	A	111	GLY	0	0.047	0.047	22.929	-0.009	-0.009	0.000	0.000	0.000	0.000
111	A	112	ALA	0	0.016	0.005	19.390	0.034	0.034	0.000	0.000	0.000	0.000
112	A	113	PRO	0	0.001	0.002	17.895	0.058	0.058	0.000	0.000	0.000	0.000
113	A	114	THR	0	0.045	0.031	17.031	0.041	0.041	0.000	0.000	0.000	0.000
114	A	115	ASP	-1	-0.910	-0.964	16.659	0.426	0.426	0.000	0.000	0.000	0.000
115	A	116	LEU	0	0.010	0.000	14.422	0.052	0.052	0.000	0.000	0.000	0.000
116	A	117	PRO	0	0.016	0.020	11.563	0.113	0.113	0.000	0.000	0.000	0.000
117	A	118	LYS	1	0.925	0.974	11.048	-0.235	-0.235	0.000	0.000	0.000	0.000
118	A	119	ALA	0	0.009	-0.008	12.868	0.058	0.058	0.000	0.000	0.000	0.000
119	A	120	LEU	0	0.043	0.018	9.202	-0.033	-0.033	0.000	0.000	0.000	0.000
120	A	121	ALA	0	0.021	0.012	8.012	0.185	0.185	0.000	0.000	0.000	0.000
121	A	122	ALA	0	-0.065	-0.033	8.895	-0.029	-0.029	0.000	0.000	0.000	0.000
122	A	123	LEU	0	0.044	0.009	9.719	-0.073	-0.073	0.000	0.000	0.000	0.000
123	A	124	GLN	0	-0.043	-0.011	2.249	-0.378	0.317	1.509	-0.771	-1.433	0.000
124	A	125	LYS	1	0.838	0.939	6.870	-1.134	-1.134	0.000	0.000	0.000	0.000
125	A	126	GLY	0	-0.004	-0.001	9.258	-0.134	-0.134	0.000	0.000	0.000	0.000
126	A	127	LYS	1	0.846	0.933	11.327	-0.417	-0.417	0.000	0.000	0.000	0.000
127	A	128	LYS	1	0.899	0.948	13.538	-0.197	-0.197	0.000	0.000	0.000	0.000
128	A	129	PHE	0	-0.021	-0.006	15.348	0.033	0.033	0.000	0.000	0.000	0.000
129	A	130	THR	0	0.002	-0.001	17.319	-0.017	-0.017	0.000	0.000	0.000	0.000
130	A	131	PRO	0	-0.010	0.002	21.007	0.011	0.011	0.000	0.000	0.000	0.000
131	A	132	GLU	-1	-0.957	-0.975	23.270	0.230	0.230	0.000	0.000	0.000	0.000

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