FMO DATABASE

FMODB ID: 2J11R

Calculation Name: 3VOE-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3VOE

Chain ID: A

ChEMBL ID:

UniProt ID: P27245

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	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	136
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1090417.651233
FMO2-HF: Nuclear repulsion	1036575.847092
FMO2-HF: Total energy	-53841.804141
FMO2-MP2: Total energy	-53995.597472

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:9:ASN)

Summations of interaction energy for fragment #1(A:9: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.
3.279	4.518	-0.021	-0.531	-0.687	0.001

Interaction energy analysis for fragmet #1(A:9:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.024 / q_NPA : -0.023

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	11	ILE	0	0.017	0.001	3.815	2.982	4.221	-0.021	-0.531	-0.687	0.001
4	A	12	ILE	0	-0.024	-0.008	5.769	-0.272	-0.272	0.000	0.000	0.000	0.000
5	A	13	PRO	0	-0.006	-0.010	8.648	0.194	0.194	0.000	0.000	0.000	0.000
6	A	14	LEU	0	0.099	0.045	11.952	0.113	0.113	0.000	0.000	0.000	0.000
7	A	15	GLY	0	0.018	0.015	13.700	0.034	0.034	0.000	0.000	0.000	0.000
8	A	16	ARG	1	0.974	0.972	12.702	-0.010	-0.010	0.000	0.000	0.000	0.000
9	A	17	LEU	0	0.019	0.018	8.480	-0.005	-0.005	0.000	0.000	0.000	0.000
10	A	18	ILE	0	0.058	0.024	12.532	0.019	0.019	0.000	0.000	0.000	0.000
11	A	19	HIS	0	-0.018	-0.002	16.000	-0.049	-0.049	0.000	0.000	0.000	0.000
12	A	20	MET	0	0.002	-0.002	9.484	-0.055	-0.055	0.000	0.000	0.000	0.000
13	A	21	VAL	0	0.025	0.013	13.055	-0.034	-0.034	0.000	0.000	0.000	0.000
14	A	22	ASN	0	-0.013	-0.001	15.404	-0.056	-0.056	0.000	0.000	0.000	0.000
15	A	23	GLN	0	0.001	-0.011	17.666	-0.041	-0.041	0.000	0.000	0.000	0.000
16	A	24	LYS	1	0.951	0.979	13.981	-0.884	-0.884	0.000	0.000	0.000	0.000
17	A	25	LYS	1	0.968	0.995	17.882	-0.442	-0.442	0.000	0.000	0.000	0.000
18	A	26	ASP	-1	-0.890	-0.961	20.505	0.285	0.285	0.000	0.000	0.000	0.000
19	A	27	ARG	1	0.891	0.944	15.942	-0.480	-0.480	0.000	0.000	0.000	0.000
20	A	28	LEU	0	0.051	0.027	19.033	-0.019	-0.019	0.000	0.000	0.000	0.000
21	A	29	LEU	0	-0.016	-0.006	22.751	-0.024	-0.024	0.000	0.000	0.000	0.000
22	A	30	ASN	0	-0.046	-0.045	25.637	-0.041	-0.041	0.000	0.000	0.000	0.000
23	A	31	GLU	-1	-0.943	-0.956	22.898	0.303	0.303	0.000	0.000	0.000	0.000
24	A	32	TYR	0	0.005	-0.002	23.251	-0.021	-0.021	0.000	0.000	0.000	0.000
25	A	33	LEU	0	-0.022	-0.020	28.500	-0.010	-0.010	0.000	0.000	0.000	0.000
26	A	34	SER	0	-0.031	-0.007	30.601	-0.020	-0.020	0.000	0.000	0.000	0.000
27	A	35	PRO	0	-0.001	0.004	31.726	-0.013	-0.013	0.000	0.000	0.000	0.000
28	A	36	LEU	0	-0.023	-0.007	34.647	-0.007	-0.007	0.000	0.000	0.000	0.000
29	A	37	ASP	-1	-0.936	-0.949	36.148	0.122	0.122	0.000	0.000	0.000	0.000
30	A	38	ILE	0	-0.075	-0.048	34.652	-0.009	-0.009	0.000	0.000	0.000	0.000
31	A	39	THR	0	0.000	0.002	32.539	0.011	0.011	0.000	0.000	0.000	0.000
32	A	40	ALA	0	0.112	0.051	28.491	0.002	0.002	0.000	0.000	0.000	0.000
33	A	41	ALA	0	-0.051	-0.026	30.463	0.002	0.002	0.000	0.000	0.000	0.000
34	A	42	GLN	0	0.029	-0.012	32.457	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	43	PHE	0	0.072	0.045	30.332	-0.005	-0.005	0.000	0.000	0.000	0.000
36	A	44	LYS	1	0.933	0.967	26.690	-0.272	-0.272	0.000	0.000	0.000	0.000
37	A	45	VAL	0	0.000	-0.002	33.027	-0.003	-0.003	0.000	0.000	0.000	0.000
38	A	46	LEU	0	0.002	0.004	36.539	-0.005	-0.005	0.000	0.000	0.000	0.000
39	A	47	CYS	0	0.019	0.014	34.070	0.000	0.000	0.000	0.000	0.000	0.000
40	A	48	SER	0	-0.008	-0.002	34.864	0.001	0.001	0.000	0.000	0.000	0.000
41	A	49	ILE	0	-0.046	-0.025	37.071	-0.006	-0.006	0.000	0.000	0.000	0.000
42	A	50	ARG	1	0.905	0.967	37.950	-0.183	-0.183	0.000	0.000	0.000	0.000
43	A	51	CYS	0	-0.097	-0.046	36.488	0.001	0.001	0.000	0.000	0.000	0.000
44	A	52	ALA	0	0.003	0.013	39.255	-0.003	-0.003	0.000	0.000	0.000	0.000
45	A	53	ALA	0	0.030	0.017	41.985	-0.004	-0.004	0.000	0.000	0.000	0.000
46	A	54	CYS	0	-0.062	-0.035	45.023	-0.006	-0.006	0.000	0.000	0.000	0.000
47	A	55	ILE	0	0.047	0.038	40.633	0.000	0.000	0.000	0.000	0.000	0.000
48	A	56	THR	0	0.005	0.010	44.892	-0.006	-0.006	0.000	0.000	0.000	0.000
49	A	57	PRO	0	0.048	0.014	43.325	0.005	0.005	0.000	0.000	0.000	0.000
50	A	58	VAL	0	0.016	0.003	42.035	0.004	0.004	0.000	0.000	0.000	0.000
51	A	59	GLU	-1	-0.913	-0.980	41.334	0.108	0.108	0.000	0.000	0.000	0.000
52	A	60	LEU	0	0.058	0.037	38.641	0.006	0.006	0.000	0.000	0.000	0.000
53	A	61	LYS	1	0.942	0.966	37.639	-0.070	-0.070	0.000	0.000	0.000	0.000
54	A	62	LYS	1	0.867	0.935	36.515	-0.087	-0.087	0.000	0.000	0.000	0.000
55	A	63	VAL	0	0.025	0.020	34.936	0.005	0.005	0.000	0.000	0.000	0.000
56	A	64	LEU	0	-0.026	-0.009	33.085	0.013	0.013	0.000	0.000	0.000	0.000
57	A	65	SER	0	-0.021	0.002	31.559	0.003	0.003	0.000	0.000	0.000	0.000
58	A	66	VAL	0	-0.026	0.001	32.490	-0.001	-0.001	0.000	0.000	0.000	0.000
59	A	67	ASP	-1	-0.845	-0.943	34.500	0.060	0.060	0.000	0.000	0.000	0.000
60	A	68	LEU	0	0.009	-0.010	37.249	0.005	0.005	0.000	0.000	0.000	0.000
61	A	69	GLY	0	0.043	0.042	40.628	0.000	0.000	0.000	0.000	0.000	0.000
62	A	70	ALA	0	-0.021	-0.016	36.839	0.001	0.001	0.000	0.000	0.000	0.000
63	A	71	LEU	0	0.013	0.017	38.380	0.003	0.003	0.000	0.000	0.000	0.000
64	A	72	THR	0	0.006	-0.011	39.658	0.002	0.002	0.000	0.000	0.000	0.000
65	A	73	ARG	1	0.983	0.993	40.870	-0.060	-0.060	0.000	0.000	0.000	0.000
66	A	74	MET	0	-0.056	-0.020	35.383	0.003	0.003	0.000	0.000	0.000	0.000
67	A	75	LEU	0	-0.007	-0.022	40.441	0.003	0.003	0.000	0.000	0.000	0.000
68	A	76	ASP	-1	-0.869	-0.927	42.992	0.073	0.073	0.000	0.000	0.000	0.000
69	A	77	ARG	1	0.887	0.935	40.146	-0.086	-0.086	0.000	0.000	0.000	0.000
70	A	78	LEU	0	-0.001	-0.006	39.059	0.001	0.001	0.000	0.000	0.000	0.000
71	A	79	VAL	0	0.001	0.011	43.168	0.001	0.001	0.000	0.000	0.000	0.000
72	A	80	CYS	0	-0.069	-0.030	46.029	-0.003	-0.003	0.000	0.000	0.000	0.000
73	A	81	LYS	1	0.899	0.960	40.341	-0.115	-0.115	0.000	0.000	0.000	0.000
74	A	82	GLY	0	0.049	0.050	45.561	0.001	0.001	0.000	0.000	0.000	0.000
75	A	83	TRP	0	-0.033	-0.031	39.310	0.005	0.005	0.000	0.000	0.000	0.000
76	A	84	VAL	0	0.019	-0.001	42.682	0.005	0.005	0.000	0.000	0.000	0.000
77	A	85	GLU	-1	-0.900	-0.945	45.751	0.084	0.084	0.000	0.000	0.000	0.000
78	A	86	ARG	1	0.916	0.943	46.797	-0.075	-0.075	0.000	0.000	0.000	0.000
79	A	87	LEU	0	0.054	0.036	50.522	-0.003	-0.003	0.000	0.000	0.000	0.000
80	A	88	PRO	0	0.020	0.004	52.290	0.001	0.001	0.000	0.000	0.000	0.000
81	A	89	ASN	0	0.004	0.005	51.167	0.002	0.002	0.000	0.000	0.000	0.000
82	A	90	PRO	0	0.011	0.008	53.857	-0.004	-0.004	0.000	0.000	0.000	0.000
83	A	91	ASN	0	0.014	-0.003	52.710	-0.004	-0.004	0.000	0.000	0.000	0.000
84	A	92	ASP	-1	-0.926	-0.943	52.646	0.057	0.057	0.000	0.000	0.000	0.000
85	A	93	LYS	1	0.968	0.966	55.389	-0.054	-0.054	0.000	0.000	0.000	0.000
86	A	94	ARG	1	0.952	0.981	53.454	-0.048	-0.048	0.000	0.000	0.000	0.000
87	A	95	GLY	0	-0.019	0.008	51.411	0.001	0.001	0.000	0.000	0.000	0.000
88	A	96	VAL	0	-0.067	-0.048	48.696	-0.001	-0.001	0.000	0.000	0.000	0.000
89	A	97	LEU	0	-0.003	-0.020	48.303	0.002	0.002	0.000	0.000	0.000	0.000
90	A	98	VAL	0	-0.030	-0.003	43.777	-0.002	-0.002	0.000	0.000	0.000	0.000
91	A	99	LYS	1	1.014	0.999	45.444	-0.093	-0.093	0.000	0.000	0.000	0.000
92	A	100	LEU	0	-0.007	0.000	40.746	-0.002	-0.002	0.000	0.000	0.000	0.000
93	A	101	THR	0	-0.002	0.015	45.241	-0.003	-0.003	0.000	0.000	0.000	0.000
94	A	102	THR	0	0.073	0.024	45.949	0.006	0.006	0.000	0.000	0.000	0.000
95	A	103	GLY	0	0.041	0.024	45.808	0.005	0.005	0.000	0.000	0.000	0.000
96	A	104	GLY	0	0.067	0.016	42.760	0.006	0.006	0.000	0.000	0.000	0.000
97	A	105	ALA	0	-0.057	-0.025	41.449	0.009	0.009	0.000	0.000	0.000	0.000
98	A	106	ALA	0	0.006	0.002	41.351	0.009	0.009	0.000	0.000	0.000	0.000
99	A	107	ILE	0	0.029	0.014	38.627	0.009	0.009	0.000	0.000	0.000	0.000
100	A	108	CYS	0	-0.048	-0.013	36.289	0.012	0.012	0.000	0.000	0.000	0.000
101	A	109	GLU	-1	-0.890	-0.963	36.265	0.191	0.191	0.000	0.000	0.000	0.000
102	A	110	GLN	0	0.007	0.001	36.474	0.008	0.008	0.000	0.000	0.000	0.000
103	A	111	CYS	0	-0.051	-0.030	33.489	0.008	0.008	0.000	0.000	0.000	0.000
104	A	112	HIS	0	-0.008	-0.007	31.028	0.012	0.012	0.000	0.000	0.000	0.000
105	A	113	GLN	0	-0.021	-0.003	31.863	0.017	0.017	0.000	0.000	0.000	0.000
106	A	114	LEU	0	-0.030	-0.011	31.630	0.016	0.016	0.000	0.000	0.000	0.000
107	A	115	VAL	0	0.006	0.007	27.123	0.012	0.012	0.000	0.000	0.000	0.000
108	A	116	GLY	0	-0.003	0.001	27.381	0.028	0.028	0.000	0.000	0.000	0.000
109	A	117	GLN	0	-0.040	-0.024	27.274	0.035	0.035	0.000	0.000	0.000	0.000
110	A	118	ASP	-1	-0.846	-0.931	25.966	0.367	0.367	0.000	0.000	0.000	0.000
111	A	119	LEU	0	-0.025	0.000	22.746	0.037	0.037	0.000	0.000	0.000	0.000
112	A	120	HIS	0	-0.022	-0.010	21.798	0.050	0.050	0.000	0.000	0.000	0.000
113	A	121	GLN	0	0.025	0.024	21.203	0.082	0.082	0.000	0.000	0.000	0.000
114	A	122	GLU	-1	-0.842	-0.901	19.124	0.575	0.575	0.000	0.000	0.000	0.000
115	A	123	LEU	0	-0.126	-0.081	17.325	0.082	0.082	0.000	0.000	0.000	0.000
116	A	124	THR	0	-0.089	-0.060	16.228	0.123	0.123	0.000	0.000	0.000	0.000
117	A	125	LYS	1	0.910	0.963	16.037	-0.627	-0.627	0.000	0.000	0.000	0.000
118	A	126	ASN	0	-0.098	-0.059	12.034	-0.126	-0.126	0.000	0.000	0.000	0.000
119	A	127	LEU	0	-0.008	0.004	13.175	0.168	0.168	0.000	0.000	0.000	0.000
120	A	128	THR	0	0.017	0.027	15.834	-0.176	-0.176	0.000	0.000	0.000	0.000
121	A	129	ALA	0	0.053	0.012	18.546	0.021	0.021	0.000	0.000	0.000	0.000
122	A	130	ASP	-1	-0.874	-0.942	19.516	0.726	0.726	0.000	0.000	0.000	0.000
123	A	131	GLU	-1	-0.887	-0.942	13.630	1.624	1.624	0.000	0.000	0.000	0.000
124	A	132	VAL	0	-0.002	-0.006	17.191	0.025	0.025	0.000	0.000	0.000	0.000
125	A	133	ALA	0	0.015	0.018	18.971	-0.035	-0.035	0.000	0.000	0.000	0.000
126	A	134	THR	0	-0.018	-0.019	16.799	-0.059	-0.059	0.000	0.000	0.000	0.000
127	A	135	LEU	0	-0.036	-0.020	14.629	-0.014	-0.014	0.000	0.000	0.000	0.000
128	A	136	GLU	-1	-0.889	-0.965	17.396	0.522	0.522	0.000	0.000	0.000	0.000
129	A	137	TYR	0	-0.060	-0.032	20.859	-0.078	-0.078	0.000	0.000	0.000	0.000
130	A	138	LEU	0	-0.011	-0.016	15.977	-0.068	-0.068	0.000	0.000	0.000	0.000
131	A	139	LEU	0	0.005	0.004	17.114	-0.051	-0.051	0.000	0.000	0.000	0.000
132	A	140	LYS	1	0.955	0.977	20.077	-0.514	-0.514	0.000	0.000	0.000	0.000
133	A	141	LYS	1	0.919	0.966	21.547	-0.491	-0.491	0.000	0.000	0.000	0.000
134	A	142	VAL	0	-0.057	-0.017	19.051	-0.033	-0.033	0.000	0.000	0.000	0.000
135	A	143	LEU	0	-0.046	-0.016	22.418	-0.031	-0.031	0.000	0.000	0.000	0.000
136	A	144	PRO	0	-0.034	0.007	25.643	-0.028	-0.028	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:9:ASN)