FMO DATABASE

FMODB ID: 8522Y

Calculation Name: 2V4X-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2V4X

Chain ID: A

ChEMBL ID:

UniProt ID: P31622

Base Structure: X-ray

Registration Date: 2023-06-21

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. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1179473.033641
FMO2-HF: Nuclear repulsion	1127138.275306
FMO2-HF: Total energy	-52334.758336
FMO2-MP2: Total energy	-52486.935248

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:PRO)

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

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.
-7.997	-4.485	31.65	-12.452	-22.705	-0.075

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.035 / q_NPA : -0.033

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	PHE	0	-0.014	-0.008	2.414	-1.741	1.367	1.633	-1.663	-3.077	-0.006
4	A	4	GLU	-1	-0.845	-0.924	5.925	-0.363	-0.363	0.000	0.000	0.000	0.000
5	A	5	ASN	0	0.013	0.021	9.689	0.089	0.089	0.000	0.000	0.000	0.000
6	A	6	ASN	0	-0.030	-0.033	12.494	0.027	0.027	0.000	0.000	0.000	0.000
7	A	7	ASN	0	0.003	0.022	15.235	-0.005	-0.005	0.000	0.000	0.000	0.000
8	A	8	GLN	0	-0.047	-0.035	12.049	-0.061	-0.061	0.000	0.000	0.000	0.000
9	A	9	ARG	1	0.812	0.899	8.843	0.477	0.477	0.000	0.000	0.000	0.000
10	A	10	TYR	0	-0.023	-0.013	7.002	0.312	0.312	0.000	0.000	0.000	0.000
11	A	11	TYR	0	-0.062	-0.068	2.899	-4.738	-3.188	0.847	-0.719	-1.678	0.000
12	A	12	GLU	-1	-0.933	-0.958	2.747	-1.271	-0.143	0.038	-0.396	-0.769	0.000
13	A	13	SER	0	0.000	-0.003	1.909	-7.129	-10.010	10.183	-3.844	-3.458	-0.041
14	A	14	LEU	0	0.014	0.008	2.174	-2.790	-1.535	4.387	-1.853	-3.788	0.006
15	A	15	PRO	0	0.011	0.005	2.918	0.850	-0.422	0.131	1.701	-0.560	0.002
16	A	16	PHE	0	0.059	0.021	6.141	0.272	0.272	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.834	0.899	8.908	-0.162	-0.162	0.000	0.000	0.000	0.000
18	A	18	GLN	0	0.060	0.022	4.967	-0.090	-0.090	0.000	0.000	0.000	0.000
19	A	19	LEU	0	0.031	0.030	7.371	0.011	0.011	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.941	0.967	9.340	-0.189	-0.189	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.833	-0.907	12.778	0.280	0.280	0.000	0.000	0.000	0.000
22	A	22	LEU	0	0.057	0.035	10.330	-0.030	-0.030	0.000	0.000	0.000	0.000
23	A	23	LYS	1	0.991	0.988	13.230	-0.333	-0.333	0.000	0.000	0.000	0.000
24	A	24	ILE	0	-0.048	-0.027	14.954	-0.041	-0.041	0.000	0.000	0.000	0.000
25	A	25	ALA	0	0.027	0.018	16.345	-0.027	-0.027	0.000	0.000	0.000	0.000
26	A	26	CYS	0	-0.040	0.000	15.533	-0.009	-0.009	0.000	0.000	0.000	0.000
27	A	27	SER	0	-0.071	-0.037	18.508	-0.034	-0.034	0.000	0.000	0.000	0.000
28	A	28	GLN	0	-0.053	-0.028	21.005	-0.030	-0.030	0.000	0.000	0.000	0.000
29	A	29	TYR	0	-0.024	-0.009	20.084	-0.023	-0.023	0.000	0.000	0.000	0.000
30	A	30	GLY	0	0.062	0.047	21.528	-0.014	-0.014	0.000	0.000	0.000	0.000
31	A	31	PRO	0	0.010	-0.012	18.130	0.020	0.020	0.000	0.000	0.000	0.000
32	A	32	THR	0	-0.004	-0.008	17.893	0.038	0.038	0.000	0.000	0.000	0.000
33	A	33	ALA	0	0.016	0.032	20.331	-0.022	-0.022	0.000	0.000	0.000	0.000
34	A	34	PRO	0	0.047	0.001	19.836	0.033	0.033	0.000	0.000	0.000	0.000
35	A	35	PHE	0	0.005	0.008	17.141	0.025	0.025	0.000	0.000	0.000	0.000
36	A	36	THR	0	0.052	0.005	15.884	0.028	0.028	0.000	0.000	0.000	0.000
37	A	37	ILE	0	0.006	0.014	15.011	0.077	0.077	0.000	0.000	0.000	0.000
38	A	38	ALA	0	-0.002	0.006	15.051	0.051	0.051	0.000	0.000	0.000	0.000
39	A	39	MET	0	-0.031	-0.015	11.684	0.028	0.028	0.000	0.000	0.000	0.000
40	A	40	ILE	0	-0.013	0.003	10.839	0.153	0.153	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.811	-0.906	10.522	0.670	0.670	0.000	0.000	0.000	0.000
42	A	42	ASN	0	-0.014	0.002	9.202	-0.019	-0.019	0.000	0.000	0.000	0.000
43	A	43	LEU	0	0.007	0.019	4.578	-0.036	0.054	-0.001	-0.005	-0.084	0.000
44	A	44	GLY	0	-0.041	-0.024	6.287	0.368	0.368	0.000	0.000	0.000	0.000
45	A	45	THR	0	-0.056	-0.009	8.690	-0.084	-0.084	0.000	0.000	0.000	0.000
46	A	46	GLN	0	-0.029	-0.010	3.222	-0.733	-0.341	0.027	-0.085	-0.334	0.000
47	A	47	ALA	0	0.015	0.015	3.350	-0.395	0.165	0.018	-0.185	-0.393	-0.001
48	A	48	LEU	0	-0.003	-0.005	2.339	-1.844	-0.136	4.622	-2.482	-3.847	-0.018
49	A	49	PRO	0	0.011	0.026	2.379	-2.149	-2.030	1.952	-0.919	-1.153	0.001
50	A	50	PRO	0	0.019	0.006	5.186	0.541	0.601	-0.001	-0.001	-0.058	0.000
51	A	51	ASN	0	-0.031	-0.048	7.863	0.075	0.075	0.000	0.000	0.000	0.000
52	A	52	ASP	-1	-0.707	-0.819	2.582	15.640	13.335	7.814	-2.001	-3.506	-0.018
53	A	53	TRP	0	0.044	0.011	6.029	-0.567	-0.567	0.000	0.000	0.000	0.000
54	A	54	LYS	1	0.765	0.890	8.280	-0.978	-0.978	0.000	0.000	0.000	0.000
55	A	55	GLN	0	-0.014	-0.003	6.534	-0.018	-0.018	0.000	0.000	0.000	0.000
56	A	56	THR	0	0.005	-0.010	6.865	-0.269	-0.269	0.000	0.000	0.000	0.000
57	A	57	ALA	0	0.061	0.019	9.316	-0.203	-0.203	0.000	0.000	0.000	0.000
58	A	58	ARG	1	0.844	0.925	12.500	-0.695	-0.695	0.000	0.000	0.000	0.000
59	A	59	ALA	0	-0.040	-0.006	11.298	-0.091	-0.091	0.000	0.000	0.000	0.000
60	A	60	CYS	0	-0.102	-0.055	11.602	-0.079	-0.079	0.000	0.000	0.000	0.000
61	A	61	LEU	0	0.014	0.023	14.570	-0.051	-0.051	0.000	0.000	0.000	0.000
62	A	62	SER	0	0.036	0.029	17.407	-0.021	-0.021	0.000	0.000	0.000	0.000
63	A	63	GLY	0	0.047	0.007	20.052	0.022	0.022	0.000	0.000	0.000	0.000
64	A	64	GLY	0	-0.008	-0.008	21.494	0.007	0.007	0.000	0.000	0.000	0.000
65	A	65	ASP	-1	-0.813	-0.925	19.928	0.307	0.307	0.000	0.000	0.000	0.000
66	A	66	TYR	0	-0.033	-0.013	14.493	0.000	0.000	0.000	0.000	0.000	0.000
67	A	67	LEU	0	-0.005	-0.013	18.491	0.031	0.031	0.000	0.000	0.000	0.000
68	A	68	LEU	0	0.001	0.010	21.126	-0.004	-0.004	0.000	0.000	0.000	0.000
69	A	69	TRP	0	0.008	0.006	12.165	0.013	0.013	0.000	0.000	0.000	0.000
70	A	70	LYS	1	0.909	0.952	16.338	-0.373	-0.373	0.000	0.000	0.000	0.000
71	A	71	SER	0	0.029	0.012	17.886	-0.004	-0.004	0.000	0.000	0.000	0.000
72	A	72	GLU	-1	-0.818	-0.889	19.607	0.300	0.300	0.000	0.000	0.000	0.000
73	A	73	PHE	0	0.000	-0.009	11.421	0.011	0.011	0.000	0.000	0.000	0.000
74	A	74	PHE	0	-0.034	-0.029	15.501	0.002	0.002	0.000	0.000	0.000	0.000
75	A	75	GLU	-1	-0.873	-0.927	18.431	0.223	0.223	0.000	0.000	0.000	0.000
76	A	76	GLN	0	-0.115	-0.074	17.518	-0.018	-0.018	0.000	0.000	0.000	0.000
77	A	77	CYS	0	-0.038	-0.018	14.830	0.001	0.001	0.000	0.000	0.000	0.000
78	A	78	ALA	0	0.006	0.004	17.361	-0.030	-0.030	0.000	0.000	0.000	0.000
79	A	79	ARG	1	0.918	0.975	19.019	-0.323	-0.323	0.000	0.000	0.000	0.000
80	A	80	ILE	0	-0.040	-0.018	16.019	-0.021	-0.021	0.000	0.000	0.000	0.000
81	A	81	ALA	0	-0.008	-0.004	18.875	-0.024	-0.024	0.000	0.000	0.000	0.000
82	A	82	ASP	-1	-0.915	-0.958	20.013	0.116	0.116	0.000	0.000	0.000	0.000
83	A	83	VAL	0	-0.003	0.000	21.765	-0.019	-0.019	0.000	0.000	0.000	0.000
84	A	84	ASN	0	-0.005	-0.013	16.935	-0.023	-0.023	0.000	0.000	0.000	0.000
85	A	85	ARG	1	0.943	0.976	21.442	-0.110	-0.110	0.000	0.000	0.000	0.000
86	A	86	GLN	0	-0.065	-0.031	24.210	-0.023	-0.023	0.000	0.000	0.000	0.000
87	A	87	GLN	0	-0.031	-0.017	22.910	0.000	0.000	0.000	0.000	0.000	0.000
88	A	88	GLY	0	-0.008	0.019	24.870	-0.010	-0.010	0.000	0.000	0.000	0.000
89	A	89	ILE	0	-0.026	-0.007	18.400	-0.015	-0.015	0.000	0.000	0.000	0.000
90	A	90	GLN	0	-0.014	-0.007	18.371	0.014	0.014	0.000	0.000	0.000	0.000
91	A	91	THR	0	-0.018	-0.034	14.255	-0.005	-0.005	0.000	0.000	0.000	0.000
92	A	92	SER	0	0.020	0.005	16.870	0.023	0.023	0.000	0.000	0.000	0.000
93	A	93	TYR	0	0.084	0.021	16.402	0.041	0.041	0.000	0.000	0.000	0.000
94	A	94	GLU	-1	-0.896	-0.955	16.432	0.194	0.194	0.000	0.000	0.000	0.000
95	A	95	MET	0	-0.038	0.012	13.418	0.037	0.037	0.000	0.000	0.000	0.000
96	A	96	LEU	0	-0.014	-0.013	12.060	0.090	0.090	0.000	0.000	0.000	0.000
97	A	97	ILE	0	0.024	0.010	11.976	0.132	0.132	0.000	0.000	0.000	0.000
98	A	98	GLY	0	-0.014	0.001	11.777	0.075	0.075	0.000	0.000	0.000	0.000
99	A	99	GLU	-1	-0.888	-0.962	12.654	0.376	0.376	0.000	0.000	0.000	0.000
100	A	100	GLY	0	0.069	0.042	16.221	-0.024	-0.024	0.000	0.000	0.000	0.000
101	A	101	PRO	0	-0.035	-0.030	18.197	-0.006	-0.006	0.000	0.000	0.000	0.000
102	A	102	TYR	0	0.008	0.000	13.197	-0.033	-0.033	0.000	0.000	0.000	0.000
103	A	103	GLN	0	-0.008	0.024	12.891	0.086	0.086	0.000	0.000	0.000	0.000
104	A	104	ALA	0	0.038	0.027	12.790	0.081	0.081	0.000	0.000	0.000	0.000
105	A	105	THR	0	0.070	0.034	6.110	0.102	0.102	0.000	0.000	0.000	0.000
106	A	106	ASP	-1	-0.853	-0.917	8.787	-0.700	-0.700	0.000	0.000	0.000	0.000
107	A	107	THR	0	-0.122	-0.065	10.485	-0.032	-0.032	0.000	0.000	0.000	0.000
108	A	108	GLN	0	-0.034	-0.046	7.972	0.345	0.345	0.000	0.000	0.000	0.000
109	A	109	LEU	0	0.034	0.044	6.026	0.124	0.124	0.000	0.000	0.000	0.000
110	A	110	ASN	0	0.006	0.001	8.342	-0.138	-0.138	0.000	0.000	0.000	0.000
111	A	111	PHE	0	0.008	0.029	9.655	0.056	0.056	0.000	0.000	0.000	0.000
112	A	112	LEU	0	0.081	0.023	11.861	-0.078	-0.078	0.000	0.000	0.000	0.000
113	A	113	PRO	0	0.049	0.017	10.914	0.057	0.057	0.000	0.000	0.000	0.000
114	A	114	GLY	0	0.003	-0.003	10.611	0.072	0.072	0.000	0.000	0.000	0.000
115	A	115	ALA	0	0.018	0.017	10.977	0.066	0.066	0.000	0.000	0.000	0.000
116	A	116	TYR	0	-0.004	-0.027	6.052	-0.017	-0.017	0.000	0.000	0.000	0.000
117	A	117	ALA	0	0.026	0.015	8.629	0.190	0.190	0.000	0.000	0.000	0.000
118	A	118	GLN	0	-0.020	-0.015	10.771	0.029	0.029	0.000	0.000	0.000	0.000
119	A	119	ILE	0	0.037	0.020	8.217	-0.009	-0.009	0.000	0.000	0.000	0.000
120	A	120	SER	0	-0.012	-0.011	8.615	0.003	0.003	0.000	0.000	0.000	0.000
121	A	121	ASN	0	-0.042	-0.030	10.397	-0.083	-0.083	0.000	0.000	0.000	0.000
122	A	122	ALA	0	0.057	0.022	13.773	-0.037	-0.037	0.000	0.000	0.000	0.000
123	A	123	ALA	0	-0.004	0.004	10.860	-0.053	-0.053	0.000	0.000	0.000	0.000
124	A	124	ARG	1	0.856	0.912	11.200	-0.777	-0.777	0.000	0.000	0.000	0.000
125	A	125	GLN	0	-0.046	-0.022	13.959	-0.058	-0.058	0.000	0.000	0.000	0.000
126	A	126	ALA	0	0.013	0.010	15.923	-0.045	-0.045	0.000	0.000	0.000	0.000
127	A	127	TRP	0	-0.043	-0.038	12.037	0.001	0.001	0.000	0.000	0.000	0.000
128	A	128	LYS	1	0.842	0.902	16.100	-0.499	-0.499	0.000	0.000	0.000	0.000
129	A	129	ARG	1	0.924	0.980	19.168	-0.329	-0.329	0.000	0.000	0.000	0.000
130	A	130	LEU	0	-0.043	0.000	17.681	-0.021	-0.021	0.000	0.000	0.000	0.000
131	A	131	PRO	0	0.006	0.008	21.744	-0.014	-0.014	0.000	0.000	0.000	0.000

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