FMO DATABASE

FMODB ID: 491RN

Calculation Name: 1VJH-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1VJH

Chain ID: A

ChEMBL ID:

UniProt ID: P0C0B0

Base Structure: X-ray

Registration Date: 2023-09-20

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	OptHSide
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	120
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-981858.90044
FMO2-HF: Nuclear repulsion	934898.269268
FMO2-HF: Total energy	-46960.631172
FMO2-MP2: Total energy	-47099.000282

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:SER)

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

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.
-18.534	-12.251	7.228	-5.881	-7.632	0.032

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.028 / 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	3	LEU	0	-0.010	0.005	2.044	-8.409	-6.104	5.220	-3.541	-3.985	0.026
4	A	4	LYS	1	0.840	0.908	2.251	-3.661	-1.022	1.974	-1.616	-2.998	0.012
5	A	5	GLY	0	0.043	0.023	4.133	-0.817	-0.730	0.001	-0.053	-0.035	0.000
6	A	6	ALA	0	-0.029	-0.017	6.849	0.120	0.120	0.000	0.000	0.000	0.000
7	A	7	LEU	0	-0.006	0.012	10.509	-0.041	-0.041	0.000	0.000	0.000	0.000
8	A	8	SER	0	-0.021	-0.025	13.878	0.038	0.038	0.000	0.000	0.000	0.000
9	A	9	VAL	0	0.005	0.016	17.039	-0.002	-0.002	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.976	0.980	20.748	0.139	0.139	0.000	0.000	0.000	0.000
11	A	11	PHE	0	-0.068	-0.030	23.790	0.003	0.003	0.000	0.000	0.000	0.000
12	A	12	ASP	-1	-0.773	-0.870	27.265	-0.098	-0.098	0.000	0.000	0.000	0.000
13	A	13	VAL	0	-0.052	-0.023	30.176	0.001	0.001	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.875	0.909	32.806	0.050	0.050	0.000	0.000	0.000	0.000
15	A	15	CYS	0	-0.062	-0.019	34.950	0.003	0.003	0.000	0.000	0.000	0.000
16	A	16	PRO	0	0.033	0.021	35.249	-0.004	-0.004	0.000	0.000	0.000	0.000
17	A	17	ALA	0	0.050	0.020	32.225	0.001	0.001	0.000	0.000	0.000	0.000
18	A	18	ASP	-1	-0.819	-0.910	32.831	-0.056	-0.056	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.896	0.953	34.553	0.041	0.041	0.000	0.000	0.000	0.000
20	A	20	PHE	0	0.015	-0.011	28.387	0.001	0.001	0.000	0.000	0.000	0.000
21	A	21	PHE	0	0.025	0.008	26.349	0.000	0.000	0.000	0.000	0.000	0.000
22	A	22	SER	0	-0.020	-0.024	30.463	0.000	0.000	0.000	0.000	0.000	0.000
23	A	23	ALA	0	0.007	0.011	32.780	0.002	0.002	0.000	0.000	0.000	0.000
24	A	24	PHE	0	0.025	0.008	23.567	0.000	0.000	0.000	0.000	0.000	0.000
25	A	25	VAL	0	-0.010	-0.015	27.797	0.001	0.001	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.884	-0.922	29.162	-0.029	-0.029	0.000	0.000	0.000	0.000
27	A	27	ASP	-1	-0.796	-0.876	29.933	-0.037	-0.037	0.000	0.000	0.000	0.000
28	A	28	THR	0	-0.094	-0.056	25.036	0.001	0.001	0.000	0.000	0.000	0.000
29	A	29	ASN	0	-0.062	-0.029	27.174	0.002	0.002	0.000	0.000	0.000	0.000
30	A	30	ARG	1	0.796	0.901	29.559	0.034	0.034	0.000	0.000	0.000	0.000
31	A	31	PRO	0	0.006	0.007	25.422	-0.004	-0.004	0.000	0.000	0.000	0.000
32	A	32	PHE	0	0.020	0.003	22.617	0.000	0.000	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.816	-0.911	21.164	0.016	0.016	0.000	0.000	0.000	0.000
34	A	34	LYS	1	0.908	0.957	25.330	-0.013	-0.013	0.000	0.000	0.000	0.000
35	A	35	ASN	0	-0.036	-0.034	24.464	-0.003	-0.003	0.000	0.000	0.000	0.000
36	A	36	GLY	0	0.021	0.011	22.688	0.003	0.003	0.000	0.000	0.000	0.000
37	A	37	LYS	1	0.809	0.899	19.342	0.018	0.018	0.000	0.000	0.000	0.000
38	A	38	THR	0	0.032	0.005	21.142	-0.005	-0.005	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.833	-0.893	19.737	-0.027	-0.027	0.000	0.000	0.000	0.000
40	A	40	ILE	0	0.032	0.006	20.782	-0.013	-0.013	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.805	-0.877	16.364	-0.137	-0.137	0.000	0.000	0.000	0.000
42	A	42	ALA	0	-0.012	-0.008	20.665	0.003	0.003	0.000	0.000	0.000	0.000
43	A	43	VAL	0	0.020	-0.002	22.507	-0.004	-0.004	0.000	0.000	0.000	0.000
44	A	44	ASP	-1	-0.841	-0.908	25.681	-0.060	-0.060	0.000	0.000	0.000	0.000
45	A	45	LEU	0	0.054	0.013	28.075	-0.004	-0.004	0.000	0.000	0.000	0.000
46	A	46	VAL	0	-0.027	0.000	31.152	0.001	0.001	0.000	0.000	0.000	0.000
47	A	47	LYS	1	0.891	0.930	26.956	0.069	0.069	0.000	0.000	0.000	0.000
48	A	48	LYS	1	0.811	0.932	28.392	0.057	0.057	0.000	0.000	0.000	0.000
49	A	49	THR	0	-0.010	-0.006	23.381	-0.009	-0.009	0.000	0.000	0.000	0.000
50	A	50	MET	0	-0.011	-0.008	23.110	0.012	0.012	0.000	0.000	0.000	0.000
51	A	51	THR	0	0.004	0.023	16.920	-0.015	-0.015	0.000	0.000	0.000	0.000
52	A	52	ILE	0	0.025	0.020	19.236	0.014	0.014	0.000	0.000	0.000	0.000
53	A	53	GLN	0	-0.043	-0.027	14.953	-0.017	-0.017	0.000	0.000	0.000	0.000
54	A	54	MET	0	-0.032	-0.007	16.583	0.016	0.016	0.000	0.000	0.000	0.000
55	A	55	SER	0	-0.016	-0.014	16.596	0.003	0.003	0.000	0.000	0.000	0.000
56	A	56	GLY	0	0.066	0.027	18.310	-0.004	-0.004	0.000	0.000	0.000	0.000
57	A	57	SER	0	-0.024	-0.002	18.895	0.006	0.006	0.000	0.000	0.000	0.000
58	A	58	GLU	-1	-0.839	-0.905	19.806	0.056	0.056	0.000	0.000	0.000	0.000
59	A	59	ILE	0	0.031	0.023	15.509	0.014	0.014	0.000	0.000	0.000	0.000
60	A	60	GLN	0	0.006	-0.016	13.955	0.006	0.006	0.000	0.000	0.000	0.000
61	A	61	LYS	1	0.774	0.888	14.863	-0.026	-0.026	0.000	0.000	0.000	0.000
62	A	62	TYR	0	-0.034	-0.009	13.683	0.034	0.034	0.000	0.000	0.000	0.000
63	A	63	PHE	0	0.021	-0.008	9.718	0.081	0.081	0.000	0.000	0.000	0.000
64	A	64	LYS	1	0.871	0.952	5.774	-0.221	-0.221	0.000	0.000	0.000	0.000
65	A	65	THR	0	-0.039	-0.023	9.087	-0.065	-0.065	0.000	0.000	0.000	0.000
66	A	66	LEU	0	0.020	0.016	10.327	-0.010	-0.010	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.831	0.894	12.481	0.204	0.204	0.000	0.000	0.000	0.000
68	A	68	GLY	0	0.020	0.012	14.665	-0.021	-0.021	0.000	0.000	0.000	0.000
69	A	69	SER	0	-0.027	-0.030	17.406	0.006	0.006	0.000	0.000	0.000	0.000
70	A	70	ILE	0	-0.036	-0.012	18.979	-0.008	-0.008	0.000	0.000	0.000	0.000
71	A	71	ALA	0	0.005	-0.003	22.374	0.002	0.002	0.000	0.000	0.000	0.000
72	A	72	VAL	0	-0.020	-0.004	24.353	-0.003	-0.003	0.000	0.000	0.000	0.000
73	A	73	THR	0	-0.005	-0.012	27.905	0.003	0.003	0.000	0.000	0.000	0.000
74	A	74	PRO	0	0.018	0.005	30.246	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	75	ILE	0	-0.076	-0.022	32.949	-0.005	-0.005	0.000	0.000	0.000	0.000
76	A	76	GLY	0	0.035	0.000	34.581	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	77	VAL	0	-0.090	-0.046	38.074	0.001	0.001	0.000	0.000	0.000	0.000
78	A	78	GLY	0	-0.024	-0.004	40.470	0.001	0.001	0.000	0.000	0.000	0.000
79	A	79	ASP	-1	-0.824	-0.904	38.224	-0.055	-0.055	0.000	0.000	0.000	0.000
80	A	80	GLY	0	0.000	0.019	36.126	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	81	SER	0	-0.075	-0.077	31.555	0.000	0.000	0.000	0.000	0.000	0.000
82	A	82	HIS	1	0.798	0.888	27.971	0.092	0.092	0.000	0.000	0.000	0.000
83	A	83	VAL	0	0.017	0.011	24.877	0.002	0.002	0.000	0.000	0.000	0.000
84	A	84	VAL	0	-0.020	-0.011	20.155	-0.006	-0.006	0.000	0.000	0.000	0.000
85	A	85	TRP	0	0.015	0.009	20.059	0.004	0.004	0.000	0.000	0.000	0.000
86	A	86	THR	0	0.028	0.016	14.275	-0.019	-0.019	0.000	0.000	0.000	0.000
87	A	87	PHE	0	0.026	0.020	13.876	0.020	0.020	0.000	0.000	0.000	0.000
88	A	88	HIS	0	0.006	-0.008	10.772	-0.019	-0.019	0.000	0.000	0.000	0.000
89	A	89	PHE	0	0.020	0.003	7.748	0.036	0.036	0.000	0.000	0.000	0.000
90	A	90	GLU	-1	-0.795	-0.885	3.108	-5.458	-4.206	0.033	-0.671	-0.614	-0.006
91	A	91	LYS	1	0.826	0.898	6.165	-0.120	-0.120	0.000	0.000	0.000	0.000
92	A	92	VAL	0	-0.028	-0.021	7.089	0.177	0.177	0.000	0.000	0.000	0.000
93	A	93	HIS	0	0.015	-0.002	8.316	0.195	0.195	0.000	0.000	0.000	0.000
94	A	94	LYS	1	0.848	0.881	7.489	-0.311	-0.311	0.000	0.000	0.000	0.000
95	A	95	ASP	-1	-0.831	-0.892	8.310	0.060	0.060	0.000	0.000	0.000	0.000
96	A	96	ILE	0	-0.060	-0.002	10.498	-0.086	-0.086	0.000	0.000	0.000	0.000
97	A	97	ASP	-1	-0.844	-0.912	11.361	-0.025	-0.025	0.000	0.000	0.000	0.000
98	A	98	ASP	-1	-0.863	-0.928	10.784	-0.288	-0.288	0.000	0.000	0.000	0.000
99	A	99	PRO	0	-0.021	0.003	12.347	0.013	0.013	0.000	0.000	0.000	0.000
100	A	100	HIS	0	0.029	-0.012	15.239	0.008	0.008	0.000	0.000	0.000	0.000
101	A	101	SER	0	0.027	0.013	18.288	0.004	0.004	0.000	0.000	0.000	0.000
102	A	102	ILE	0	0.044	0.016	16.529	0.000	0.000	0.000	0.000	0.000	0.000
103	A	103	ILE	0	-0.019	0.004	17.081	0.002	0.002	0.000	0.000	0.000	0.000
104	A	104	ASP	-1	-0.793	-0.884	20.110	-0.084	-0.084	0.000	0.000	0.000	0.000
105	A	105	GLU	-1	-0.894	-0.963	23.182	-0.047	-0.047	0.000	0.000	0.000	0.000
106	A	106	SER	0	-0.033	-0.018	21.419	0.002	0.002	0.000	0.000	0.000	0.000
107	A	107	VAL	0	-0.014	0.000	23.409	0.003	0.003	0.000	0.000	0.000	0.000
108	A	108	LYS	1	0.798	0.894	25.753	0.076	0.076	0.000	0.000	0.000	0.000
109	A	109	TYR	0	-0.105	-0.075	26.200	0.004	0.004	0.000	0.000	0.000	0.000
110	A	110	PHE	0	0.038	0.003	23.258	0.004	0.004	0.000	0.000	0.000	0.000
111	A	111	LYS	1	0.932	0.967	28.785	0.089	0.089	0.000	0.000	0.000	0.000
112	A	112	LYS	1	0.934	0.972	30.036	0.049	0.049	0.000	0.000	0.000	0.000
113	A	113	LEU	0	0.036	0.035	30.090	0.003	0.003	0.000	0.000	0.000	0.000
114	A	114	ASP	-1	-0.766	-0.886	32.850	-0.056	-0.056	0.000	0.000	0.000	0.000
115	A	115	GLU	-1	-0.821	-0.894	34.554	-0.045	-0.045	0.000	0.000	0.000	0.000
116	A	116	ALA	0	-0.005	0.009	36.174	0.003	0.003	0.000	0.000	0.000	0.000
117	A	117	ILE	0	-0.037	-0.025	34.678	0.002	0.002	0.000	0.000	0.000	0.000
118	A	118	LEU	0	-0.036	-0.014	38.519	0.002	0.002	0.000	0.000	0.000	0.000
119	A	119	ASN	0	-0.069	-0.041	40.267	0.002	0.002	0.000	0.000	0.000	0.000
120	A	120	PHE	0	-0.027	0.015	41.528	0.002	0.002	0.000	0.000	0.000	0.000

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