FMO DATABASE

FMODB ID: 6NQQZ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1091907.73202
FMO2-HF: Nuclear repulsion	1038065.010851
FMO2-HF: Total energy	-53842.721169
FMO2-MP2: Total energy	-53996.540253

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.
4.099	5.342	-0.021	-0.54	-0.682	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 : -0.034 / q_NPA : -0.032

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	0.002	-0.004	3.815	2.877	4.120	-0.021	-0.540	-0.682	0.001
4	A	12	ILE	0	-0.023	-0.004	6.228	0.057	0.057	0.000	0.000	0.000	0.000
5	A	13	PRO	0	-0.007	-0.012	8.633	0.166	0.166	0.000	0.000	0.000	0.000
6	A	14	LEU	0	0.103	0.044	11.940	0.141	0.141	0.000	0.000	0.000	0.000
7	A	15	GLY	0	0.016	0.014	13.685	0.063	0.063	0.000	0.000	0.000	0.000
8	A	16	ARG	1	0.969	0.973	12.712	0.249	0.249	0.000	0.000	0.000	0.000
9	A	17	LEU	0	0.030	0.019	8.367	0.038	0.038	0.000	0.000	0.000	0.000
10	A	18	ILE	0	0.050	0.019	12.528	0.051	0.051	0.000	0.000	0.000	0.000
11	A	19	HIS	0	-0.006	0.007	15.974	-0.012	-0.012	0.000	0.000	0.000	0.000
12	A	20	MET	0	0.001	-0.003	9.277	-0.065	-0.065	0.000	0.000	0.000	0.000
13	A	21	VAL	0	0.040	0.020	12.973	-0.011	-0.011	0.000	0.000	0.000	0.000
14	A	22	ASN	0	0.002	0.011	15.376	-0.043	-0.043	0.000	0.000	0.000	0.000
15	A	23	GLN	0	-0.013	-0.022	17.562	-0.016	-0.016	0.000	0.000	0.000	0.000
16	A	24	LYS	1	0.875	0.943	15.067	-0.770	-0.770	0.000	0.000	0.000	0.000
17	A	25	LYS	1	0.887	0.956	17.859	-0.382	-0.382	0.000	0.000	0.000	0.000
18	A	26	ASP	-1	-0.831	-0.926	20.479	0.245	0.245	0.000	0.000	0.000	0.000
19	A	27	ARG	1	0.921	0.972	16.021	-0.427	-0.427	0.000	0.000	0.000	0.000
20	A	28	LEU	0	0.061	0.033	18.994	-0.011	-0.011	0.000	0.000	0.000	0.000
21	A	29	LEU	0	-0.027	-0.010	22.729	-0.022	-0.022	0.000	0.000	0.000	0.000
22	A	30	ASN	0	-0.054	-0.058	25.604	-0.038	-0.038	0.000	0.000	0.000	0.000
23	A	31	GLU	-1	-0.920	-0.949	22.530	0.316	0.316	0.000	0.000	0.000	0.000
24	A	32	TYR	0	-0.025	-0.015	23.717	-0.010	-0.010	0.000	0.000	0.000	0.000
25	A	33	LEU	0	-0.020	-0.013	28.479	-0.010	-0.010	0.000	0.000	0.000	0.000
26	A	34	SER	0	-0.033	-0.010	30.379	-0.018	-0.018	0.000	0.000	0.000	0.000
27	A	35	PRO	0	0.006	0.008	31.614	-0.013	-0.013	0.000	0.000	0.000	0.000
28	A	36	LEU	0	-0.025	-0.010	34.619	-0.007	-0.007	0.000	0.000	0.000	0.000
29	A	37	ASP	-1	-0.924	-0.941	36.101	0.114	0.114	0.000	0.000	0.000	0.000
30	A	38	ILE	0	-0.067	-0.045	34.485	-0.011	-0.011	0.000	0.000	0.000	0.000
31	A	39	THR	0	0.019	0.010	32.447	0.010	0.010	0.000	0.000	0.000	0.000
32	A	40	ALA	0	0.100	0.044	28.481	0.001	0.001	0.000	0.000	0.000	0.000
33	A	41	ALA	0	-0.054	-0.028	30.439	0.000	0.000	0.000	0.000	0.000	0.000
34	A	42	GLN	0	0.049	-0.003	32.433	0.000	0.000	0.000	0.000	0.000	0.000
35	A	43	PHE	0	0.063	0.039	30.317	-0.006	-0.006	0.000	0.000	0.000	0.000
36	A	44	LYS	1	0.911	0.947	26.391	-0.226	-0.226	0.000	0.000	0.000	0.000
37	A	45	VAL	0	0.001	0.001	33.000	-0.005	-0.005	0.000	0.000	0.000	0.000
38	A	46	LEU	0	0.002	0.006	36.513	-0.005	-0.005	0.000	0.000	0.000	0.000
39	A	47	CYS	0	0.009	0.007	34.059	0.000	0.000	0.000	0.000	0.000	0.000
40	A	48	SER	0	-0.024	-0.015	35.060	0.000	0.000	0.000	0.000	0.000	0.000
41	A	49	ILE	0	-0.047	-0.030	37.054	-0.006	-0.006	0.000	0.000	0.000	0.000
42	A	50	ARG	1	0.824	0.909	38.207	-0.154	-0.154	0.000	0.000	0.000	0.000
43	A	51	CYS	0	-0.096	-0.043	36.533	0.001	0.001	0.000	0.000	0.000	0.000
44	A	52	ALA	0	-0.011	0.004	39.228	-0.003	-0.003	0.000	0.000	0.000	0.000
45	A	53	ALA	0	0.044	0.024	41.959	-0.003	-0.003	0.000	0.000	0.000	0.000
46	A	54	CYS	0	-0.071	-0.041	44.993	-0.004	-0.004	0.000	0.000	0.000	0.000
47	A	55	ILE	0	0.021	0.028	40.569	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	56	THR	0	-0.026	-0.012	44.892	-0.004	-0.004	0.000	0.000	0.000	0.000
49	A	57	PRO	0	0.052	0.014	43.304	0.003	0.003	0.000	0.000	0.000	0.000
50	A	58	VAL	0	0.012	0.002	42.035	0.003	0.003	0.000	0.000	0.000	0.000
51	A	59	GLU	-1	-0.865	-0.952	41.334	0.071	0.071	0.000	0.000	0.000	0.000
52	A	60	LEU	0	0.067	0.044	38.273	0.004	0.004	0.000	0.000	0.000	0.000
53	A	61	LYS	1	0.922	0.959	37.639	-0.039	-0.039	0.000	0.000	0.000	0.000
54	A	62	LYS	1	0.890	0.947	36.515	-0.054	-0.054	0.000	0.000	0.000	0.000
55	A	63	VAL	0	0.013	0.013	35.124	0.002	0.002	0.000	0.000	0.000	0.000
56	A	64	LEU	0	-0.017	-0.004	33.096	0.010	0.010	0.000	0.000	0.000	0.000
57	A	65	SER	0	-0.031	-0.004	31.512	0.001	0.001	0.000	0.000	0.000	0.000
58	A	66	VAL	0	-0.018	0.006	32.490	-0.001	-0.001	0.000	0.000	0.000	0.000
59	A	67	ASP	-1	-0.805	-0.918	34.500	0.036	0.036	0.000	0.000	0.000	0.000
60	A	68	LEU	0	0.011	-0.004	37.249	0.005	0.005	0.000	0.000	0.000	0.000
61	A	69	GLY	0	0.030	0.026	40.624	0.001	0.001	0.000	0.000	0.000	0.000
62	A	70	ALA	0	-0.039	-0.033	36.806	0.002	0.002	0.000	0.000	0.000	0.000
63	A	71	LEU	0	0.013	0.015	37.978	0.004	0.004	0.000	0.000	0.000	0.000
64	A	72	THR	0	0.010	-0.008	39.658	0.003	0.003	0.000	0.000	0.000	0.000
65	A	73	ARG	1	0.975	0.990	40.890	-0.043	-0.043	0.000	0.000	0.000	0.000
66	A	74	MET	0	-0.057	-0.018	35.203	0.005	0.005	0.000	0.000	0.000	0.000
67	A	75	LEU	0	-0.002	-0.015	40.441	0.004	0.004	0.000	0.000	0.000	0.000
68	A	76	ASP	-1	-0.806	-0.883	42.992	0.059	0.059	0.000	0.000	0.000	0.000
69	A	77	ARG	1	0.912	0.953	40.233	-0.072	-0.072	0.000	0.000	0.000	0.000
70	A	78	LEU	0	0.005	0.000	39.025	0.002	0.002	0.000	0.000	0.000	0.000
71	A	79	VAL	0	-0.009	0.002	43.144	0.001	0.001	0.000	0.000	0.000	0.000
72	A	80	CYS	0	-0.081	-0.039	46.064	-0.002	-0.002	0.000	0.000	0.000	0.000
73	A	81	LYS	1	0.839	0.931	40.001	-0.110	-0.110	0.000	0.000	0.000	0.000
74	A	82	GLY	0	0.048	0.048	45.538	0.002	0.002	0.000	0.000	0.000	0.000
75	A	83	TRP	0	-0.037	-0.037	39.155	0.004	0.004	0.000	0.000	0.000	0.000
76	A	84	VAL	0	0.029	0.005	42.608	0.003	0.003	0.000	0.000	0.000	0.000
77	A	85	GLU	-1	-0.787	-0.874	45.725	0.074	0.074	0.000	0.000	0.000	0.000
78	A	86	ARG	1	0.859	0.894	46.966	-0.058	-0.058	0.000	0.000	0.000	0.000
79	A	87	LEU	0	0.042	0.032	50.518	-0.002	-0.002	0.000	0.000	0.000	0.000
80	A	88	PRO	0	0.034	0.009	52.290	0.000	0.000	0.000	0.000	0.000	0.000
81	A	89	ASN	0	0.011	0.007	51.091	0.001	0.001	0.000	0.000	0.000	0.000
82	A	90	PRO	0	0.019	0.015	53.907	-0.003	-0.003	0.000	0.000	0.000	0.000
83	A	91	ASN	0	0.003	-0.014	52.801	-0.003	-0.003	0.000	0.000	0.000	0.000
84	A	92	ASP	-1	-0.903	-0.936	52.528	0.036	0.036	0.000	0.000	0.000	0.000
85	A	93	LYS	1	0.942	0.963	55.389	-0.040	-0.040	0.000	0.000	0.000	0.000
86	A	94	ARG	1	0.934	0.972	53.181	-0.029	-0.029	0.000	0.000	0.000	0.000
87	A	95	GLY	0	-0.004	0.019	51.410	0.000	0.000	0.000	0.000	0.000	0.000
88	A	96	VAL	0	-0.066	-0.050	48.609	0.000	0.000	0.000	0.000	0.000	0.000
89	A	97	LEU	0	-0.015	-0.022	48.298	0.001	0.001	0.000	0.000	0.000	0.000
90	A	98	VAL	0	-0.017	0.001	43.864	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	99	LYS	1	0.931	0.951	45.415	-0.078	-0.078	0.000	0.000	0.000	0.000
92	A	100	LEU	0	-0.004	0.003	40.739	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	101	THR	0	-0.041	-0.016	45.213	-0.003	-0.003	0.000	0.000	0.000	0.000
94	A	102	THR	0	0.063	0.016	45.922	0.005	0.005	0.000	0.000	0.000	0.000
95	A	103	GLY	0	0.036	0.029	45.781	0.005	0.005	0.000	0.000	0.000	0.000
96	A	104	GLY	0	0.066	0.017	42.737	0.006	0.006	0.000	0.000	0.000	0.000
97	A	105	ALA	0	-0.060	-0.024	41.422	0.007	0.007	0.000	0.000	0.000	0.000
98	A	106	ALA	0	0.017	0.002	41.324	0.008	0.008	0.000	0.000	0.000	0.000
99	A	107	ILE	0	0.034	0.014	38.787	0.009	0.009	0.000	0.000	0.000	0.000
100	A	108	CYS	0	-0.054	-0.015	36.362	0.011	0.011	0.000	0.000	0.000	0.000
101	A	109	GLU	-1	-0.803	-0.898	36.237	0.165	0.165	0.000	0.000	0.000	0.000
102	A	110	GLN	0	0.008	0.003	36.447	0.006	0.006	0.000	0.000	0.000	0.000
103	A	111	CYS	0	-0.046	-0.026	33.509	0.009	0.009	0.000	0.000	0.000	0.000
104	A	112	HIS	0	-0.015	-0.008	31.365	0.010	0.010	0.000	0.000	0.000	0.000
105	A	113	GLN	0	-0.015	-0.003	31.835	0.017	0.017	0.000	0.000	0.000	0.000
106	A	114	LEU	0	-0.026	-0.003	31.605	0.016	0.016	0.000	0.000	0.000	0.000
107	A	115	VAL	0	-0.006	-0.008	27.056	0.014	0.014	0.000	0.000	0.000	0.000
108	A	116	GLY	0	0.008	0.009	27.355	0.024	0.024	0.000	0.000	0.000	0.000
109	A	117	GLN	0	-0.073	-0.046	27.247	0.025	0.025	0.000	0.000	0.000	0.000
110	A	118	ASP	-1	-0.816	-0.911	25.942	0.355	0.355	0.000	0.000	0.000	0.000
111	A	119	LEU	0	-0.005	0.008	22.325	0.037	0.037	0.000	0.000	0.000	0.000
112	A	120	HIS	0	-0.006	-0.003	21.773	0.057	0.057	0.000	0.000	0.000	0.000
113	A	121	GLN	0	0.016	0.018	21.177	0.065	0.065	0.000	0.000	0.000	0.000
114	A	122	GLU	-1	-0.747	-0.849	17.971	0.664	0.664	0.000	0.000	0.000	0.000
115	A	123	LEU	0	-0.102	-0.065	17.437	0.076	0.076	0.000	0.000	0.000	0.000
116	A	124	THR	0	-0.089	-0.057	16.202	0.113	0.113	0.000	0.000	0.000	0.000
117	A	125	LYS	1	0.881	0.941	16.145	-0.631	-0.631	0.000	0.000	0.000	0.000
118	A	126	ASN	0	-0.076	-0.048	11.125	-0.137	-0.137	0.000	0.000	0.000	0.000
119	A	127	LEU	0	-0.030	-0.006	13.346	0.167	0.167	0.000	0.000	0.000	0.000
120	A	128	THR	0	-0.002	-0.007	15.811	-0.163	-0.163	0.000	0.000	0.000	0.000
121	A	129	ALA	0	0.041	0.008	18.524	0.002	0.002	0.000	0.000	0.000	0.000
122	A	130	ASP	-1	-0.879	-0.945	19.514	0.646	0.646	0.000	0.000	0.000	0.000
123	A	131	GLU	-1	-0.823	-0.888	13.344	1.484	1.484	0.000	0.000	0.000	0.000
124	A	132	VAL	0	-0.012	-0.010	17.180	-0.005	-0.005	0.000	0.000	0.000	0.000
125	A	133	ALA	0	0.000	0.007	18.955	-0.046	-0.046	0.000	0.000	0.000	0.000
126	A	134	THR	0	-0.008	-0.015	16.822	-0.068	-0.068	0.000	0.000	0.000	0.000
127	A	135	LEU	0	-0.026	-0.017	14.471	-0.038	-0.038	0.000	0.000	0.000	0.000
128	A	136	GLU	-1	-0.856	-0.947	17.382	0.378	0.378	0.000	0.000	0.000	0.000
129	A	137	TYR	0	-0.032	-0.014	20.829	-0.075	-0.075	0.000	0.000	0.000	0.000
130	A	138	LEU	0	-0.020	-0.019	15.930	-0.063	-0.063	0.000	0.000	0.000	0.000
131	A	139	LEU	0	0.001	0.001	17.130	-0.052	-0.052	0.000	0.000	0.000	0.000
132	A	140	LYS	1	0.897	0.945	20.061	-0.432	-0.432	0.000	0.000	0.000	0.000
133	A	141	LYS	1	0.912	0.963	21.625	-0.338	-0.338	0.000	0.000	0.000	0.000
134	A	142	VAL	0	-0.067	-0.024	18.995	-0.032	-0.032	0.000	0.000	0.000	0.000
135	A	143	LEU	0	-0.044	-0.012	22.406	-0.025	-0.025	0.000	0.000	0.000	0.000
136	A	144	PRO	0	-0.032	0.007	25.628	-0.021	-0.021	0.000	0.000	0.000	0.000

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