FMO DATABASE

FMODB ID: VQGG1

Calculation Name: 2QVG-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2QVG

Chain ID: A

ChEMBL ID:

UniProt ID: Q5ZSR0

Base Structure: X-ray

Registration Date: 2023-09-23

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	OptAll
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	129
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1198946.687745
FMO2-HF: Nuclear repulsion	1147402.394662
FMO2-HF: Total energy	-51544.293083
FMO2-MP2: Total energy	-51696.591342

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:7:LYS)

Summations of interaction energy for fragment #1(A:7:LYS)

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.
-211.301	-204.86	21.788	-13.991	-14.237	-0.162

Interaction energy analysis for fragmet #1(A:7:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.840 / q_NPA : 0.929

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

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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	9	ASP	-1	-0.844	-0.909	3.872	-29.383	-27.409	-0.011	-0.978	-0.986	0.002
4	A	10	ILE	0	-0.012	-0.021	6.687	2.899	2.899	0.000	0.000	0.000	0.000
5	A	11	LEU	0	0.010	0.019	6.936	-4.032	-4.032	0.000	0.000	0.000	0.000
6	A	12	TYR	0	-0.030	-0.040	8.889	3.472	3.472	0.000	0.000	0.000	0.000
7	A	13	LEU	0	0.001	0.007	11.685	-0.675	-0.675	0.000	0.000	0.000	0.000
8	A	14	GLH	0	-0.025	-0.061	13.784	1.984	1.984	0.000	0.000	0.000	0.000
9	A	15	ASP	-1	-0.828	-0.913	15.194	-16.530	-16.530	0.000	0.000	0.000	0.000
10	A	16	ASP	-1	-0.830	-0.892	17.798	-14.021	-14.021	0.000	0.000	0.000	0.000
11	A	17	GLU	-1	-0.774	-0.891	16.894	-19.634	-19.634	0.000	0.000	0.000	0.000
12	A	18	VAL	0	-0.023	-0.008	18.841	-0.351	-0.351	0.000	0.000	0.000	0.000
13	A	19	ASP	-1	-0.822	-0.894	19.015	-14.821	-14.821	0.000	0.000	0.000	0.000
14	A	20	ILE	0	-0.036	-0.007	13.776	-0.439	-0.439	0.000	0.000	0.000	0.000
15	A	21	GLN	0	0.026	0.015	16.075	0.816	0.816	0.000	0.000	0.000	0.000
16	A	22	SER	0	-0.078	-0.045	18.001	0.601	0.601	0.000	0.000	0.000	0.000
17	A	23	VAL	0	0.006	0.000	15.036	0.177	0.177	0.000	0.000	0.000	0.000
18	A	24	GLU	-1	-0.837	-0.921	12.614	-23.396	-23.396	0.000	0.000	0.000	0.000
19	A	25	ARG	1	0.824	0.905	15.068	15.874	15.874	0.000	0.000	0.000	0.000
20	A	26	VAL	0	-0.045	-0.017	18.271	0.717	0.717	0.000	0.000	0.000	0.000
21	A	27	PHE	0	0.042	0.006	13.817	0.378	0.378	0.000	0.000	0.000	0.000
22	A	28	HIS	0	0.007	0.006	15.065	-0.622	-0.622	0.000	0.000	0.000	0.000
23	A	29	LYS	1	0.884	0.934	15.921	14.026	14.026	0.000	0.000	0.000	0.000
24	A	30	ILE	0	-0.049	0.004	15.739	0.837	0.837	0.000	0.000	0.000	0.000
25	A	31	SER	0	0.011	-0.017	13.116	0.126	0.126	0.000	0.000	0.000	0.000
26	A	32	SER	0	0.016	0.022	13.408	-0.711	-0.711	0.000	0.000	0.000	0.000
27	A	33	LEU	0	-0.044	-0.020	9.895	-1.139	-1.139	0.000	0.000	0.000	0.000
28	A	34	ILE	0	-0.016	0.012	8.342	-1.939	-1.939	0.000	0.000	0.000	0.000
29	A	35	LYS	1	0.852	0.928	4.454	33.446	33.732	-0.001	-0.042	-0.243	0.000
30	A	36	ILE	0	0.002	-0.011	6.932	-0.145	-0.145	0.000	0.000	0.000	0.000
31	A	37	GLU	-1	-0.805	-0.891	1.782	-120.103	-119.881	9.803	-5.695	-4.329	-0.084
32	A	38	ILE	0	-0.015	-0.018	6.193	4.714	4.714	0.000	0.000	0.000	0.000
33	A	39	ALA	0	0.003	0.004	9.080	-1.152	-1.152	0.000	0.000	0.000	0.000
34	A	40	LYS	1	0.832	0.886	10.787	22.929	22.929	0.000	0.000	0.000	0.000
35	A	41	SER	0	0.005	-0.013	13.705	1.623	1.623	0.000	0.000	0.000	0.000
36	A	42	GLY	0	0.077	0.026	13.643	-1.473	-1.473	0.000	0.000	0.000	0.000
37	A	43	ASN	0	0.006	0.005	14.011	-0.870	-0.870	0.000	0.000	0.000	0.000
38	A	44	GLN	0	0.019	0.009	9.643	1.100	1.100	0.000	0.000	0.000	0.000
39	A	45	ALA	0	0.043	0.019	9.474	-3.299	-3.299	0.000	0.000	0.000	0.000
40	A	46	LEU	0	-0.009	0.004	9.599	-2.725	-2.725	0.000	0.000	0.000	0.000
41	A	47	ASP	-1	-0.822	-0.898	10.521	-24.505	-24.505	0.000	0.000	0.000	0.000
42	A	48	MET	0	-0.029	-0.011	5.548	-1.870	-1.870	0.000	0.000	0.000	0.000
43	A	49	LEU	0	-0.015	-0.006	5.882	-5.792	-5.792	0.000	0.000	0.000	0.000
44	A	50	TYR	0	-0.085	-0.088	8.153	0.416	0.416	0.000	0.000	0.000	0.000
45	A	51	GLY	0	-0.062	-0.020	6.829	0.103	0.103	0.000	0.000	0.000	0.000
46	A	52	ARG	1	0.839	0.921	7.708	25.691	25.691	0.000	0.000	0.000	0.000
47	A	53	ASN	0	-0.008	-0.035	10.176	-0.682	-0.682	0.000	0.000	0.000	0.000
48	A	54	LYS	1	0.869	0.924	10.456	22.158	22.158	0.000	0.000	0.000	0.000
49	A	55	GLU	-1	-0.818	-0.875	6.699	-41.395	-41.395	0.000	0.000	0.000	0.000
50	A	56	ASN	0	-0.045	-0.027	2.957	3.479	3.968	0.073	-0.131	-0.430	-0.001
51	A	57	LYS	1	0.890	0.957	2.719	10.115	12.891	0.546	-1.801	-1.521	-0.019
52	A	58	ILE	0	-0.059	-0.011	1.989	-37.177	-37.205	11.357	-5.309	-6.020	-0.060
53	A	59	HIS	0	0.053	0.017	3.314	10.428	10.980	0.022	0.004	-0.578	0.000
54	A	60	PRO	0	-0.029	0.006	4.212	-0.766	-0.596	-0.001	-0.039	-0.130	0.000
55	A	61	LYS	1	0.903	0.948	5.780	27.021	27.021	0.000	0.000	0.000	0.000
56	A	62	LEU	0	-0.019	-0.011	7.531	2.642	2.642	0.000	0.000	0.000	0.000
57	A	63	ILE	0	0.008	0.007	10.146	-2.831	-2.831	0.000	0.000	0.000	0.000
58	A	64	LEU	0	-0.040	-0.007	12.761	2.004	2.004	0.000	0.000	0.000	0.000
59	A	65	LEU	0	0.031	0.008	14.246	-1.096	-1.096	0.000	0.000	0.000	0.000
60	A	66	ASP	-1	-0.758	-0.826	16.859	-13.946	-13.946	0.000	0.000	0.000	0.000
61	A	67	ILE	0	-0.002	0.000	19.452	-0.141	-0.141	0.000	0.000	0.000	0.000
62	A	68	ASN	0	-0.085	-0.042	22.392	0.670	0.670	0.000	0.000	0.000	0.000
63	A	69	ILE	0	0.037	0.025	19.103	0.335	0.335	0.000	0.000	0.000	0.000
64	A	70	PRO	0	-0.006	-0.014	22.980	-0.224	-0.224	0.000	0.000	0.000	0.000
65	A	71	LYS	1	0.839	0.914	22.155	14.200	14.200	0.000	0.000	0.000	0.000
66	A	72	MET	0	-0.026	0.005	16.856	-0.780	-0.780	0.000	0.000	0.000	0.000
67	A	73	ASN	0	0.010	-0.005	20.777	-0.083	-0.083	0.000	0.000	0.000	0.000
68	A	74	GLY	0	0.050	0.020	19.437	-0.449	-0.449	0.000	0.000	0.000	0.000
69	A	75	ILE	0	-0.005	-0.004	20.409	-0.290	-0.290	0.000	0.000	0.000	0.000
70	A	76	GLU	-1	-0.931	-0.965	22.166	-12.627	-12.627	0.000	0.000	0.000	0.000
71	A	77	PHE	0	0.038	0.008	12.842	-0.062	-0.062	0.000	0.000	0.000	0.000
72	A	78	LEU	0	0.000	-0.019	17.430	-0.598	-0.598	0.000	0.000	0.000	0.000
73	A	79	LYS	1	0.912	0.984	19.269	12.768	12.768	0.000	0.000	0.000	0.000
74	A	80	GLU	-1	-0.796	-0.901	16.478	-18.704	-18.704	0.000	0.000	0.000	0.000
75	A	81	LEU	0	-0.076	-0.041	13.214	-0.533	-0.533	0.000	0.000	0.000	0.000
76	A	82	ARG	1	0.747	0.848	14.868	17.435	17.435	0.000	0.000	0.000	0.000
77	A	83	ASP	-1	-0.908	-0.943	19.278	-13.335	-13.335	0.000	0.000	0.000	0.000
78	A	84	ASP	-1	-0.815	-0.847	15.967	-18.981	-18.981	0.000	0.000	0.000	0.000
79	A	85	SER	0	0.036	0.008	16.815	-0.370	-0.370	0.000	0.000	0.000	0.000
80	A	86	SER	0	-0.096	-0.064	12.902	-0.042	-0.042	0.000	0.000	0.000	0.000
81	A	87	PHE	0	-0.035	-0.025	10.280	-2.263	-2.263	0.000	0.000	0.000	0.000
82	A	88	THR	0	-0.047	-0.028	13.214	0.393	0.393	0.000	0.000	0.000	0.000
83	A	89	ASP	-1	-0.930	-0.968	11.520	-17.605	-17.605	0.000	0.000	0.000	0.000
84	A	90	ILE	0	-0.046	0.004	9.245	-0.487	-0.487	0.000	0.000	0.000	0.000
85	A	91	GLU	-1	-0.805	-0.879	11.682	-14.858	-14.858	0.000	0.000	0.000	0.000
86	A	92	VAL	0	-0.013	-0.020	13.406	-1.339	-1.339	0.000	0.000	0.000	0.000
87	A	93	PHE	0	-0.019	-0.012	16.093	1.392	1.392	0.000	0.000	0.000	0.000
88	A	94	VAL	0	0.014	0.016	18.172	-0.740	-0.740	0.000	0.000	0.000	0.000
89	A	95	LEU	0	-0.018	-0.023	18.959	0.579	0.579	0.000	0.000	0.000	0.000
90	A	96	THR	0	0.021	-0.002	21.459	0.032	0.032	0.000	0.000	0.000	0.000
91	A	97	ALA	0	0.020	0.010	24.695	0.111	0.111	0.000	0.000	0.000	0.000
92	A	98	ALA	0	-0.026	-0.016	27.772	0.459	0.459	0.000	0.000	0.000	0.000
93	A	99	TYR	0	0.023	0.031	26.018	-0.176	-0.176	0.000	0.000	0.000	0.000
94	A	100	THR	0	-0.035	-0.049	29.500	0.524	0.524	0.000	0.000	0.000	0.000
95	A	101	SER	0	0.041	-0.005	31.605	-0.248	-0.248	0.000	0.000	0.000	0.000
96	A	102	LYS	1	0.963	0.991	30.113	10.339	10.339	0.000	0.000	0.000	0.000
97	A	103	ASP	-1	-0.782	-0.867	27.372	-11.484	-11.484	0.000	0.000	0.000	0.000
98	A	104	LYS	1	0.786	0.871	28.253	9.864	9.864	0.000	0.000	0.000	0.000
99	A	105	LEU	0	-0.003	-0.013	29.433	-0.097	-0.097	0.000	0.000	0.000	0.000
100	A	106	ALA	0	-0.062	-0.021	27.543	-0.064	-0.064	0.000	0.000	0.000	0.000
101	A	107	PHE	0	0.003	-0.016	23.061	-0.391	-0.391	0.000	0.000	0.000	0.000
102	A	108	GLU	-1	-0.823	-0.868	24.875	-10.642	-10.642	0.000	0.000	0.000	0.000
103	A	109	SER	0	-0.022	-0.016	26.329	-0.170	-0.170	0.000	0.000	0.000	0.000
104	A	110	LEU	0	-0.005	0.003	21.854	-0.131	-0.131	0.000	0.000	0.000	0.000
105	A	111	ASN	0	0.011	0.016	18.029	-0.213	-0.213	0.000	0.000	0.000	0.000
106	A	112	ILE	0	0.015	0.020	19.118	-0.937	-0.937	0.000	0.000	0.000	0.000
107	A	113	ARG	1	0.873	0.930	16.239	15.933	15.933	0.000	0.000	0.000	0.000
108	A	114	GLY	0	0.011	0.000	19.977	0.532	0.532	0.000	0.000	0.000	0.000
109	A	115	HIS	0	-0.006	0.002	21.455	-0.790	-0.790	0.000	0.000	0.000	0.000
110	A	116	LEU	0	-0.050	-0.035	18.911	0.198	0.198	0.000	0.000	0.000	0.000
111	A	117	ILE	0	0.010	0.006	23.478	0.012	0.012	0.000	0.000	0.000	0.000
112	A	118	LYS	1	0.813	0.909	21.769	14.229	14.229	0.000	0.000	0.000	0.000
113	A	119	PRO	0	0.005	-0.006	24.305	0.483	0.483	0.000	0.000	0.000	0.000
114	A	120	LEU	0	0.027	0.013	18.053	0.190	0.190	0.000	0.000	0.000	0.000
115	A	121	ASP	-1	-0.807	-0.903	21.491	-12.959	-12.959	0.000	0.000	0.000	0.000
116	A	122	TYR	0	0.045	0.011	21.210	-0.474	-0.474	0.000	0.000	0.000	0.000
117	A	123	GLY	0	0.019	0.007	21.496	-0.307	-0.307	0.000	0.000	0.000	0.000
118	A	124	GLH	0	-0.070	-0.072	21.409	-0.424	-0.424	0.000	0.000	0.000	0.000
119	A	125	ALA	0	0.037	0.018	17.662	-0.489	-0.489	0.000	0.000	0.000	0.000
120	A	126	ILE	0	0.002	-0.005	16.961	-0.766	-0.766	0.000	0.000	0.000	0.000
121	A	127	LYS	1	0.900	0.969	18.142	13.506	13.506	0.000	0.000	0.000	0.000
122	A	128	LEU	0	-0.001	0.001	14.836	-0.131	-0.131	0.000	0.000	0.000	0.000
123	A	129	PHE	0	0.016	0.011	12.507	-0.906	-0.906	0.000	0.000	0.000	0.000
124	A	130	TRP	0	0.037	0.002	13.698	-0.456	-0.456	0.000	0.000	0.000	0.000
125	A	131	ILE	0	-0.032	0.002	13.659	0.248	0.248	0.000	0.000	0.000	0.000
126	A	132	LEU	0	0.054	0.027	8.674	-0.123	-0.123	0.000	0.000	0.000	0.000
127	A	133	GLN	0	-0.061	-0.020	10.402	-0.429	-0.429	0.000	0.000	0.000	0.000
128	A	134	SER	0	-0.088	-0.039	12.615	0.493	0.493	0.000	0.000	0.000	0.000
129	A	135	MET	0	-0.035	-0.009	9.856	-1.164	-1.164	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:7:LYS)