FMO DATABASE

FMODB ID: LNVG9

Calculation Name: 2QGO-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2QGO

Chain ID: A

ChEMBL ID:

UniProt ID: Q5FLQ3

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	114
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-907873.829062
FMO2-HF: Nuclear repulsion	863672.517142
FMO2-HF: Total energy	-44201.311919
FMO2-MP2: Total energy	-44330.689182

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:4:LEU)

Summations of interaction energy for fragment #1(A:4:LEU)

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.
-11.491	-2.024	3.745	-3.984	-9.227	-0.013

Interaction energy analysis for fragmet #1(A:4:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.005 / q_NPA : -0.005

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	6	ILE	0	0.021	0.008	3.853	-1.379	0.418	-0.022	-0.892	-0.883	0.002
4	A	7	LYS	1	0.826	0.899	6.856	-0.102	-0.102	0.000	0.000	0.000	0.000
5	A	8	PHE	0	-0.003	-0.005	9.940	-0.040	-0.040	0.000	0.000	0.000	0.000
6	A	9	THR	0	0.043	-0.014	13.484	0.033	0.033	0.000	0.000	0.000	0.000
7	A	10	ASP	-1	-0.869	-0.938	16.991	-0.030	-0.030	0.000	0.000	0.000	0.000
8	A	11	ASN	0	-0.047	-0.018	19.845	-0.003	-0.003	0.000	0.000	0.000	0.000
9	A	12	ALA	0	0.019	0.014	15.584	-0.009	-0.009	0.000	0.000	0.000	0.000
10	A	13	VAL	0	-0.015	-0.012	16.262	-0.016	-0.016	0.000	0.000	0.000	0.000
11	A	14	ASP	-1	-0.812	-0.914	18.042	-0.063	-0.063	0.000	0.000	0.000	0.000
12	A	15	TYR	0	-0.036	-0.010	18.624	0.000	0.000	0.000	0.000	0.000	0.000
13	A	16	LEU	0	0.036	0.001	14.384	-0.003	-0.003	0.000	0.000	0.000	0.000
14	A	17	LYS	1	0.842	0.920	19.025	0.064	0.064	0.000	0.000	0.000	0.000
15	A	18	ARG	1	0.866	0.943	22.144	0.089	0.089	0.000	0.000	0.000	0.000
16	A	19	ARG	1	0.867	0.947	21.036	0.155	0.155	0.000	0.000	0.000	0.000
17	A	20	GLU	-1	-0.943	-0.965	22.870	-0.097	-0.097	0.000	0.000	0.000	0.000
18	A	21	ILE	0	-0.015	-0.019	17.225	-0.007	-0.007	0.000	0.000	0.000	0.000
19	A	22	LEU	0	-0.020	-0.005	15.660	-0.019	-0.019	0.000	0.000	0.000	0.000
20	A	23	ASP	-1	-0.832	-0.903	16.696	-0.142	-0.142	0.000	0.000	0.000	0.000
21	A	24	LYS	1	0.774	0.898	16.926	0.139	0.139	0.000	0.000	0.000	0.000
22	A	25	ILE	0	-0.043	-0.022	13.091	-0.014	-0.014	0.000	0.000	0.000	0.000
23	A	26	LEU	0	-0.008	-0.006	11.391	0.010	0.010	0.000	0.000	0.000	0.000
24	A	27	ILE	0	-0.010	-0.013	10.296	-0.050	-0.050	0.000	0.000	0.000	0.000
25	A	28	LEU	0	-0.002	0.013	5.810	0.062	0.062	0.000	0.000	0.000	0.000
26	A	29	ILE	0	-0.038	-0.002	7.740	-0.154	-0.154	0.000	0.000	0.000	0.000
27	A	30	THR	0	0.004	-0.022	8.668	0.050	0.050	0.000	0.000	0.000	0.000
28	A	31	ASP	-1	-0.842	-0.900	11.056	-0.263	-0.263	0.000	0.000	0.000	0.000
29	A	32	ASP	-1	-0.827	-0.919	14.876	-0.319	-0.319	0.000	0.000	0.000	0.000
30	A	33	GLY	0	-0.030	-0.002	16.931	0.029	0.029	0.000	0.000	0.000	0.000
31	A	34	GLY	0	-0.043	-0.018	18.096	0.023	0.023	0.000	0.000	0.000	0.000
32	A	35	GLY	0	0.012	0.011	15.864	0.003	0.003	0.000	0.000	0.000	0.000
33	A	36	LYS	1	0.750	0.834	15.954	0.289	0.289	0.000	0.000	0.000	0.000
34	A	37	TYR	0	-0.109	-0.089	14.965	0.037	0.037	0.000	0.000	0.000	0.000
35	A	38	SER	0	-0.035	-0.014	17.815	0.003	0.003	0.000	0.000	0.000	0.000
36	A	39	ILE	0	-0.085	-0.062	18.505	0.037	0.037	0.000	0.000	0.000	0.000
37	A	49	HIS	1	0.802	0.895	13.804	0.309	0.309	0.000	0.000	0.000	0.000
38	A	50	PHE	0	-0.011	-0.029	7.444	-0.047	-0.047	0.000	0.000	0.000	0.000
39	A	51	SER	0	0.004	-0.003	11.783	0.054	0.054	0.000	0.000	0.000	0.000
40	A	52	ILE	0	-0.017	-0.011	10.309	-0.071	-0.071	0.000	0.000	0.000	0.000
41	A	53	ILE	0	0.016	0.014	13.264	0.061	0.061	0.000	0.000	0.000	0.000
42	A	54	TRP	0	0.029	0.018	14.300	-0.015	-0.015	0.000	0.000	0.000	0.000
43	A	55	LEU	0	0.001	-0.001	16.441	0.023	0.023	0.000	0.000	0.000	0.000
44	A	56	ASP	-1	-0.832	-0.917	17.864	-0.150	-0.150	0.000	0.000	0.000	0.000
45	A	57	LYS	1	0.874	0.929	18.935	0.152	0.152	0.000	0.000	0.000	0.000
46	A	58	VAL	0	0.028	0.016	14.191	-0.011	-0.011	0.000	0.000	0.000	0.000
47	A	59	ASP	-1	-0.747	-0.843	14.592	-0.252	-0.252	0.000	0.000	0.000	0.000
48	A	60	PRO	0	-0.027	-0.019	13.918	-0.028	-0.028	0.000	0.000	0.000	0.000
49	A	61	ASP	-1	-0.814	-0.885	13.904	-0.267	-0.267	0.000	0.000	0.000	0.000
50	A	62	TYR	0	-0.070	-0.033	9.464	-0.019	-0.019	0.000	0.000	0.000	0.000
51	A	63	PRO	0	0.018	0.011	9.604	-0.001	-0.001	0.000	0.000	0.000	0.000
52	A	64	VAL	0	-0.026	-0.013	3.807	-0.241	0.045	0.005	-0.046	-0.244	0.000
53	A	65	LYS	1	0.918	0.956	5.778	0.181	0.181	0.000	0.000	0.000	0.000
54	A	66	ILE	0	0.006	0.023	2.373	-1.553	-0.294	0.897	-0.438	-1.718	0.000
55	A	67	ALA	0	-0.003	0.000	4.008	0.184	0.499	0.000	-0.068	-0.247	0.000
56	A	68	ASN	0	0.028	-0.003	6.334	0.061	0.061	0.000	0.000	0.000	0.000
57	A	69	GLU	-1	-0.836	-0.902	9.117	0.318	0.318	0.000	0.000	0.000	0.000
58	A	70	GLN	0	-0.014	-0.015	12.316	-0.009	-0.009	0.000	0.000	0.000	0.000
59	A	71	ASN	0	-0.055	-0.025	13.566	-0.004	-0.004	0.000	0.000	0.000	0.000
60	A	72	VAL	0	0.050	0.042	10.966	-0.003	-0.003	0.000	0.000	0.000	0.000
61	A	73	LYS	1	0.853	0.928	10.765	0.103	0.103	0.000	0.000	0.000	0.000
62	A	74	ILE	0	0.001	-0.001	6.890	0.025	0.025	0.000	0.000	0.000	0.000
63	A	75	TYR	0	-0.048	-0.026	6.992	-0.023	-0.023	0.000	0.000	0.000	0.000
64	A	76	THR	0	0.040	0.005	3.501	-0.354	-0.067	0.008	-0.049	-0.247	0.000
65	A	77	SER	0	0.000	-0.030	6.763	0.113	0.113	0.000	0.000	0.000	0.000
66	A	78	ASP	-1	-0.870	-0.949	5.976	-0.729	-0.729	0.000	0.000	0.000	0.000
67	A	79	PHE	0	0.044	0.030	7.295	-0.072	-0.072	0.000	0.000	0.000	0.000
68	A	80	ASP	-1	-0.714	-0.811	7.097	-0.835	-0.835	0.000	0.000	0.000	0.000
69	A	81	LYS	1	0.820	0.902	2.341	-0.776	0.250	1.375	-0.501	-1.900	0.001
70	A	82	THR	0	-0.097	-0.057	3.102	-3.051	-1.273	0.121	-0.928	-0.972	-0.009
71	A	83	MET	0	-0.030	-0.003	5.634	0.314	0.314	0.000	0.000	0.000	0.000
72	A	84	LEU	0	-0.040	-0.013	2.696	-0.503	0.159	0.526	-0.235	-0.953	-0.001
73	A	85	GLY	0	0.070	0.031	4.010	-0.570	-0.236	0.008	-0.092	-0.250	0.000
74	A	86	PRO	0	-0.054	-0.023	3.134	-1.463	-0.249	0.116	-0.559	-0.770	-0.005
75	A	87	ASN	0	-0.054	-0.058	4.846	0.030	0.030	0.000	0.000	0.000	0.000
76	A	88	MET	0	-0.002	0.035	2.569	-0.975	-0.466	0.711	-0.176	-1.043	-0.001
77	A	89	VAL	0	0.000	-0.004	7.192	0.036	0.036	0.000	0.000	0.000	0.000
78	A	90	MET	0	-0.002	0.016	9.929	-0.040	-0.040	0.000	0.000	0.000	0.000
79	A	91	ASP	-1	-0.751	-0.852	12.134	-0.037	-0.037	0.000	0.000	0.000	0.000
80	A	92	TYR	0	-0.082	-0.057	15.965	-0.020	-0.020	0.000	0.000	0.000	0.000
81	A	93	ASN	0	-0.017	-0.020	19.029	0.021	0.021	0.000	0.000	0.000	0.000
82	A	94	ALA	0	0.042	0.011	21.691	-0.010	-0.010	0.000	0.000	0.000	0.000
83	A	95	GLY	0	-0.006	0.009	23.190	0.004	0.004	0.000	0.000	0.000	0.000
84	A	96	SER	0	-0.058	-0.024	19.223	0.001	0.001	0.000	0.000	0.000	0.000
85	A	97	LEU	0	0.015	-0.006	14.463	0.014	0.014	0.000	0.000	0.000	0.000
86	A	98	SER	0	-0.051	-0.003	14.827	0.000	0.000	0.000	0.000	0.000	0.000
87	A	99	LEU	0	0.047	0.006	7.277	0.010	0.010	0.000	0.000	0.000	0.000
88	A	100	SER	0	-0.011	-0.003	10.333	0.028	0.028	0.000	0.000	0.000	0.000
89	A	101	SER	0	0.016	0.011	7.446	-0.090	-0.090	0.000	0.000	0.000	0.000
90	A	102	ASP	-1	-0.833	-0.909	8.833	0.761	0.761	0.000	0.000	0.000	0.000
91	A	103	GLU	-1	-0.956	-0.978	8.361	-0.136	-0.136	0.000	0.000	0.000	0.000
92	A	104	GLY	0	-0.012	0.004	11.545	-0.024	-0.024	0.000	0.000	0.000	0.000
93	A	105	LEU	0	-0.076	-0.050	11.565	-0.033	-0.033	0.000	0.000	0.000	0.000
94	A	106	LEU	0	-0.009	-0.001	7.182	-0.018	-0.018	0.000	0.000	0.000	0.000
95	A	107	ASP	-1	-0.709	-0.855	11.454	-0.306	-0.306	0.000	0.000	0.000	0.000
96	A	108	GLY	0	0.007	0.008	13.928	0.013	0.013	0.000	0.000	0.000	0.000
97	A	109	SER	0	-0.100	-0.050	16.424	0.033	0.033	0.000	0.000	0.000	0.000
98	A	110	VAL	0	-0.027	0.002	12.375	-0.013	-0.013	0.000	0.000	0.000	0.000
99	A	111	ASP	-1	-0.803	-0.885	15.052	-0.216	-0.216	0.000	0.000	0.000	0.000
100	A	112	ILE	0	-0.034	-0.033	15.692	-0.024	-0.024	0.000	0.000	0.000	0.000
101	A	113	GLY	0	0.024	0.021	17.584	0.025	0.025	0.000	0.000	0.000	0.000
102	A	114	ASN	0	-0.040	-0.010	18.536	-0.014	-0.014	0.000	0.000	0.000	0.000
103	A	115	GLY	0	0.120	0.034	18.982	0.006	0.006	0.000	0.000	0.000	0.000
104	A	116	ALA	0	0.005	0.000	19.812	0.008	0.008	0.000	0.000	0.000	0.000
105	A	117	ALA	0	-0.061	-0.041	23.077	0.012	0.012	0.000	0.000	0.000	0.000
106	A	118	LEU	0	0.043	0.037	19.466	0.011	0.011	0.000	0.000	0.000	0.000
107	A	119	LEU	0	0.028	0.018	20.113	0.010	0.010	0.000	0.000	0.000	0.000
108	A	120	LYS	1	0.898	0.953	23.774	0.123	0.123	0.000	0.000	0.000	0.000
109	A	121	ALA	0	-0.009	-0.005	26.452	0.010	0.010	0.000	0.000	0.000	0.000
110	A	122	ASN	0	0.032	0.008	22.497	0.015	0.015	0.000	0.000	0.000	0.000
111	A	123	LYS	1	0.964	0.991	26.600	0.108	0.108	0.000	0.000	0.000	0.000
112	A	124	ASN	0	-0.054	-0.042	28.794	0.006	0.006	0.000	0.000	0.000	0.000
113	A	125	VAL	0	-0.024	0.005	29.204	0.007	0.007	0.000	0.000	0.000	0.000
114	A	126	GLN	0	-0.085	-0.029	27.604	0.009	0.009	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:LEU)