FMO DATABASE

FMODB ID: QVYRY

Calculation Name: 3GT7-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3GT7

Chain ID: A

ChEMBL ID:

UniProt ID: Q2LQE8

Base Structure: X-ray

Registration Date: 2023-09-21

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	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	138
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1256919.300478
FMO2-HF: Nuclear repulsion	1202027.430794
FMO2-HF: Total energy	-54891.869685
FMO2-MP2: Total energy	-55051.639824

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:11:ALA)

Summations of interaction energy for fragment #1(A:11:ALA)

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.
-4.472	-2.053	-0.016	-1.071	-1.332	0.002

Interaction energy analysis for fragmet #1(A:11:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.008 / q_NPA : 0.002

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	13	GLU	-1	-0.894	-0.948	3.866	-2.205	-0.429	-0.016	-0.919	-0.842	0.003
4	A	14	ILE	0	-0.032	-0.026	6.102	0.375	0.375	0.000	0.000	0.000	0.000
5	A	15	LEU	0	0.049	0.026	9.446	0.139	0.139	0.000	0.000	0.000	0.000
6	A	16	ILE	0	-0.010	-0.007	12.862	0.039	0.039	0.000	0.000	0.000	0.000
7	A	17	VAL	0	-0.020	-0.016	15.213	0.068	0.068	0.000	0.000	0.000	0.000
8	A	18	GLU	-1	-0.807	-0.916	18.881	-0.311	-0.311	0.000	0.000	0.000	0.000
9	A	19	ASP	-1	-0.797	-0.860	21.269	-0.192	-0.192	0.000	0.000	0.000	0.000
10	A	20	SER	0	-0.019	-0.008	24.228	0.011	0.011	0.000	0.000	0.000	0.000
11	A	21	PRO	0	0.044	0.007	22.029	-0.027	-0.027	0.000	0.000	0.000	0.000
12	A	22	THR	0	0.026	0.010	21.179	-0.025	-0.025	0.000	0.000	0.000	0.000
13	A	23	GLN	0	0.009	0.005	21.464	-0.026	-0.026	0.000	0.000	0.000	0.000
14	A	24	ALA	0	0.031	0.010	18.209	-0.044	-0.044	0.000	0.000	0.000	0.000
15	A	25	GLU	-1	-0.836	-0.904	16.706	-0.439	-0.439	0.000	0.000	0.000	0.000
16	A	26	HIS	0	-0.062	-0.032	16.793	-0.029	-0.029	0.000	0.000	0.000	0.000
17	A	27	LEU	0	-0.045	-0.037	15.448	-0.050	-0.050	0.000	0.000	0.000	0.000
18	A	28	LYS	1	0.870	0.924	11.209	0.585	0.585	0.000	0.000	0.000	0.000
19	A	29	HIS	0	-0.028	-0.019	11.987	-0.174	-0.174	0.000	0.000	0.000	0.000
20	A	30	ILE	0	-0.001	0.004	12.740	-0.094	-0.094	0.000	0.000	0.000	0.000
21	A	31	LEU	0	-0.071	-0.019	9.468	-0.090	-0.090	0.000	0.000	0.000	0.000
22	A	32	GLU	-1	-0.756	-0.842	7.975	-1.366	-1.366	0.000	0.000	0.000	0.000
23	A	33	GLU	-1	-0.958	-0.982	8.895	-0.550	-0.550	0.000	0.000	0.000	0.000
24	A	34	THR	0	-0.143	-0.094	9.458	0.023	0.023	0.000	0.000	0.000	0.000
25	A	35	GLY	0	-0.029	-0.006	5.697	-0.005	-0.005	0.000	0.000	0.000	0.000
26	A	36	TYR	0	-0.056	-0.028	3.805	-1.771	-1.423	0.002	-0.132	-0.218	-0.001
27	A	37	GLN	0	-0.066	-0.032	4.499	0.736	0.942	-0.001	-0.012	-0.192	0.000
28	A	38	THR	0	-0.064	-0.059	5.796	0.045	0.045	0.000	0.000	0.000	0.000
29	A	39	GLU	-1	-0.842	-0.907	9.336	-0.266	-0.266	0.000	0.000	0.000	0.000
30	A	40	HIS	0	-0.089	-0.059	12.271	-0.039	-0.039	0.000	0.000	0.000	0.000
31	A	41	VAL	0	-0.040	-0.012	15.833	0.061	0.061	0.000	0.000	0.000	0.000
32	A	42	ARG	1	0.851	0.898	19.089	0.184	0.184	0.000	0.000	0.000	0.000
33	A	43	ASN	0	0.011	-0.023	22.497	0.003	0.003	0.000	0.000	0.000	0.000
34	A	44	GLY	0	0.085	0.031	22.332	-0.011	-0.011	0.000	0.000	0.000	0.000
35	A	45	ARG	1	0.898	0.951	23.069	0.143	0.143	0.000	0.000	0.000	0.000
36	A	46	GLU	-1	-0.784	-0.889	21.995	-0.181	-0.181	0.000	0.000	0.000	0.000
37	A	47	ALA	0	0.014	0.015	18.857	0.000	0.000	0.000	0.000	0.000	0.000
38	A	48	VAL	0	-0.023	-0.010	19.199	0.002	0.002	0.000	0.000	0.000	0.000
39	A	49	ARG	1	0.821	0.900	21.200	0.165	0.165	0.000	0.000	0.000	0.000
40	A	50	PHE	0	0.029	0.016	12.205	0.040	0.040	0.000	0.000	0.000	0.000
41	A	51	LEU	0	0.017	-0.005	14.772	0.013	0.013	0.000	0.000	0.000	0.000
42	A	52	SER	0	-0.094	-0.042	17.352	0.026	0.026	0.000	0.000	0.000	0.000
43	A	53	LEU	0	-0.085	-0.033	16.666	0.031	0.031	0.000	0.000	0.000	0.000
44	A	54	THR	0	0.005	0.008	11.574	0.075	0.075	0.000	0.000	0.000	0.000
45	A	55	ARG	1	0.816	0.884	11.184	0.144	0.144	0.000	0.000	0.000	0.000
46	A	56	PRO	0	0.013	0.033	8.729	0.046	0.046	0.000	0.000	0.000	0.000
47	A	57	ASP	-1	-0.879	-0.938	4.654	-1.766	-1.677	-0.001	-0.008	-0.080	0.000
48	A	58	LEU	0	-0.092	-0.056	8.132	0.130	0.130	0.000	0.000	0.000	0.000
49	A	59	ILE	0	0.017	0.015	10.903	-0.027	-0.027	0.000	0.000	0.000	0.000
50	A	60	ILE	0	-0.027	-0.010	13.030	0.023	0.023	0.000	0.000	0.000	0.000
51	A	61	SER	0	0.008	-0.009	16.247	0.027	0.027	0.000	0.000	0.000	0.000
52	A	62	ASP	-1	-0.792	-0.875	19.803	-0.284	-0.284	0.000	0.000	0.000	0.000
53	A	63	VAL	0	0.003	0.002	22.880	0.009	0.009	0.000	0.000	0.000	0.000
54	A	64	LEU	0	-0.042	-0.029	26.364	0.019	0.019	0.000	0.000	0.000	0.000
55	A	65	MET	0	-0.009	0.019	22.895	-0.011	-0.011	0.000	0.000	0.000	0.000
56	A	66	PRO	0	0.018	0.012	27.485	0.012	0.012	0.000	0.000	0.000	0.000
57	A	67	GLU	-1	-0.874	-0.921	28.176	-0.151	-0.151	0.000	0.000	0.000	0.000
58	A	68	MET	0	-0.130	-0.077	25.617	0.012	0.012	0.000	0.000	0.000	0.000
59	A	69	ASP	-1	-0.779	-0.876	26.324	-0.191	-0.191	0.000	0.000	0.000	0.000
60	A	70	GLY	0	0.068	0.030	23.941	-0.004	-0.004	0.000	0.000	0.000	0.000
61	A	71	TYR	0	-0.001	-0.014	24.322	-0.005	-0.005	0.000	0.000	0.000	0.000
62	A	72	ALA	0	-0.042	-0.034	26.673	0.006	0.006	0.000	0.000	0.000	0.000
63	A	73	LEU	0	-0.005	0.009	19.761	0.011	0.011	0.000	0.000	0.000	0.000
64	A	74	CYS	0	-0.020	-0.006	21.907	-0.012	-0.012	0.000	0.000	0.000	0.000
65	A	75	ARG	1	0.968	0.995	22.963	0.164	0.164	0.000	0.000	0.000	0.000
66	A	76	TRP	0	0.005	0.002	20.229	0.009	0.009	0.000	0.000	0.000	0.000
67	A	77	LEU	0	0.014	0.006	17.970	0.016	0.016	0.000	0.000	0.000	0.000
68	A	78	LYS	1	0.834	0.906	18.012	0.323	0.323	0.000	0.000	0.000	0.000
69	A	79	GLY	0	0.020	0.021	22.814	0.020	0.020	0.000	0.000	0.000	0.000
70	A	80	GLN	0	-0.070	-0.037	21.441	0.032	0.032	0.000	0.000	0.000	0.000
71	A	81	PRO	0	-0.042	-0.032	22.394	-0.010	-0.010	0.000	0.000	0.000	0.000
72	A	82	ASP	-1	-0.777	-0.869	18.336	-0.097	-0.097	0.000	0.000	0.000	0.000
73	A	83	LEU	0	0.012	0.006	16.735	-0.021	-0.021	0.000	0.000	0.000	0.000
74	A	84	ARG	1	0.863	0.947	17.454	0.082	0.082	0.000	0.000	0.000	0.000
75	A	85	THR	0	-0.080	-0.055	15.185	-0.022	-0.022	0.000	0.000	0.000	0.000
76	A	86	ILE	0	0.012	0.023	12.279	-0.023	-0.023	0.000	0.000	0.000	0.000
77	A	87	PRO	0	-0.029	-0.004	11.851	0.047	0.047	0.000	0.000	0.000	0.000
78	A	88	VAL	0	0.003	-0.020	14.346	-0.074	-0.074	0.000	0.000	0.000	0.000
79	A	89	ILE	0	-0.034	-0.016	14.628	0.040	0.040	0.000	0.000	0.000	0.000
80	A	90	LEU	0	-0.018	-0.011	17.976	-0.001	-0.001	0.000	0.000	0.000	0.000
81	A	91	LEU	0	-0.017	-0.014	18.810	0.012	0.012	0.000	0.000	0.000	0.000
82	A	92	THR	0	0.029	-0.004	22.374	0.029	0.029	0.000	0.000	0.000	0.000
83	A	93	ILE	0	0.011	0.002	26.163	-0.005	-0.005	0.000	0.000	0.000	0.000
84	A	94	LEU	0	-0.042	-0.026	29.590	0.007	0.007	0.000	0.000	0.000	0.000
85	A	95	SER	0	-0.051	-0.028	32.440	0.007	0.007	0.000	0.000	0.000	0.000
86	A	96	ASP	-1	-0.782	-0.874	35.665	-0.112	-0.112	0.000	0.000	0.000	0.000
87	A	97	PRO	0	0.035	-0.003	36.267	-0.007	-0.007	0.000	0.000	0.000	0.000
88	A	98	ARG	1	0.895	0.926	36.618	0.118	0.118	0.000	0.000	0.000	0.000
89	A	99	ASP	-1	-0.784	-0.845	32.250	-0.160	-0.160	0.000	0.000	0.000	0.000
90	A	100	VAL	0	-0.002	0.016	31.653	-0.013	-0.013	0.000	0.000	0.000	0.000
91	A	101	VAL	0	-0.008	0.002	32.247	-0.006	-0.006	0.000	0.000	0.000	0.000
92	A	102	ARG	1	0.910	0.933	30.992	0.151	0.151	0.000	0.000	0.000	0.000
93	A	103	SER	0	-0.009	-0.028	28.115	-0.015	-0.015	0.000	0.000	0.000	0.000
94	A	104	LEU	0	-0.021	-0.005	27.985	-0.011	-0.011	0.000	0.000	0.000	0.000
95	A	105	GLU	-1	-0.936	-0.972	29.474	-0.128	-0.128	0.000	0.000	0.000	0.000
96	A	106	CYS	0	-0.175	-0.058	25.659	-0.005	-0.005	0.000	0.000	0.000	0.000
97	A	107	GLY	0	0.027	0.010	25.098	-0.004	-0.004	0.000	0.000	0.000	0.000
98	A	108	ALA	0	0.018	-0.009	21.240	-0.009	-0.009	0.000	0.000	0.000	0.000
99	A	109	ASP	-1	-0.812	-0.881	17.741	-0.337	-0.337	0.000	0.000	0.000	0.000
100	A	110	ASP	-1	-0.792	-0.870	18.245	-0.468	-0.468	0.000	0.000	0.000	0.000
101	A	111	PHE	0	0.041	0.024	20.173	0.000	0.000	0.000	0.000	0.000	0.000
102	A	112	ILE	0	-0.049	-0.026	19.485	-0.005	-0.005	0.000	0.000	0.000	0.000
103	A	113	THR	0	0.004	0.010	22.767	0.008	0.008	0.000	0.000	0.000	0.000
104	A	114	LYS	1	0.816	0.901	22.892	0.306	0.306	0.000	0.000	0.000	0.000
105	A	115	PRO	0	-0.010	-0.019	26.058	0.017	0.017	0.000	0.000	0.000	0.000
106	A	116	CYS	0	0.017	0.017	21.599	0.000	0.000	0.000	0.000	0.000	0.000
107	A	117	LYS	1	0.863	0.919	22.272	0.327	0.327	0.000	0.000	0.000	0.000
108	A	118	ASP	-1	-0.734	-0.858	17.915	-0.428	-0.428	0.000	0.000	0.000	0.000
109	A	119	VAL	0	0.054	0.022	16.987	-0.068	-0.068	0.000	0.000	0.000	0.000
110	A	120	VAL	0	-0.028	0.001	17.466	-0.031	-0.031	0.000	0.000	0.000	0.000
111	A	121	LEU	0	0.047	0.031	15.348	-0.010	-0.010	0.000	0.000	0.000	0.000
112	A	122	ALA	0	0.079	0.043	13.131	-0.070	-0.070	0.000	0.000	0.000	0.000
113	A	123	SER	0	-0.047	-0.045	12.940	-0.095	-0.095	0.000	0.000	0.000	0.000
114	A	124	HIS	1	0.784	0.864	14.688	0.475	0.475	0.000	0.000	0.000	0.000
115	A	125	VAL	0	0.084	0.048	9.905	0.056	0.056	0.000	0.000	0.000	0.000
116	A	126	LYS	1	0.942	0.980	9.800	0.667	0.667	0.000	0.000	0.000	0.000
117	A	127	ARG	1	0.771	0.879	10.829	0.511	0.511	0.000	0.000	0.000	0.000
118	A	128	LEU	0	0.018	0.015	12.670	0.071	0.071	0.000	0.000	0.000	0.000
119	A	129	LEU	0	0.070	0.043	6.536	0.144	0.144	0.000	0.000	0.000	0.000
120	A	130	SER	0	-0.072	-0.050	8.569	0.160	0.160	0.000	0.000	0.000	0.000
121	A	131	GLY	0	-0.010	0.005	10.150	0.147	0.147	0.000	0.000	0.000	0.000
122	A	132	VAL	0	0.077	0.032	8.623	0.099	0.099	0.000	0.000	0.000	0.000
123	A	133	LYS	1	0.824	0.914	5.032	-0.255	-0.255	0.000	0.000	0.000	0.000
124	A	134	ARG	1	0.831	0.891	9.510	0.205	0.205	0.000	0.000	0.000	0.000
125	A	135	THR	0	0.007	0.005	11.653	0.017	0.017	0.000	0.000	0.000	0.000
126	A	136	GLU	-1	-0.745	-0.846	11.100	0.129	0.129	0.000	0.000	0.000	0.000
127	A	137	GLU	-1	-0.768	-0.864	6.160	0.805	0.805	0.000	0.000	0.000	0.000
128	A	138	ARG	1	0.735	0.842	10.236	-0.039	-0.039	0.000	0.000	0.000	0.000
129	A	139	TYR	0	-0.058	-0.033	13.518	-0.015	-0.015	0.000	0.000	0.000	0.000
130	A	140	SER	0	-0.044	-0.025	10.946	0.038	0.038	0.000	0.000	0.000	0.000
131	A	141	ARG	1	0.853	0.938	11.964	-0.245	-0.245	0.000	0.000	0.000	0.000
132	A	142	GLU	-1	-0.809	-0.903	13.201	0.251	0.251	0.000	0.000	0.000	0.000
133	A	143	SER	0	-0.021	-0.008	14.596	0.016	0.016	0.000	0.000	0.000	0.000
134	A	144	ILE	0	-0.027	-0.012	16.316	-0.032	-0.032	0.000	0.000	0.000	0.000
135	A	145	THR	0	-0.007	-0.006	17.910	0.002	0.002	0.000	0.000	0.000	0.000
136	A	146	LEU	0	0.011	0.013	20.549	-0.006	-0.006	0.000	0.000	0.000	0.000
137	A	147	ALA	0	0.007	0.011	23.632	-0.007	-0.007	0.000	0.000	0.000	0.000
138	A	148	PHE	0	-0.021	-0.013	24.519	-0.003	-0.003	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:11:ALA)