FMO DATABASE

FMODB ID: QV6YY

Calculation Name: 3G39-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3G39

Chain ID: A

ChEMBL ID:

UniProt ID: D0VX17

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	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	163
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1642712.33379
FMO2-HF: Nuclear repulsion	1577860.737061
FMO2-HF: Total energy	-64851.596729
FMO2-MP2: Total energy	-65037.797805

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:1:ALA)

Summations of interaction energy for fragment #1(A:1: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.
-2.785	0.00099999999999974	0.173	-1.274	-1.684	0.001

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.026 / q_NPA : -0.029

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	3	PRO	0	0.031	0.008	3.460	-1.353	0.697	0.017	-0.958	-1.108	0.001
4	A	4	SER	0	0.022	0.008	5.602	0.394	0.394	0.000	0.000	0.000	0.000
5	A	5	GLN	0	0.020	0.011	7.153	0.245	0.245	0.000	0.000	0.000	0.000
6	A	6	CYS	0	-0.143	-0.072	8.527	-0.013	-0.013	0.000	0.000	0.000	0.000
7	A	7	SER	0	0.003	0.003	9.042	-0.019	-0.019	0.000	0.000	0.000	0.000
8	A	9	SER	0	0.004	0.002	8.545	0.205	0.205	0.000	0.000	0.000	0.000
9	A	10	GLY	0	0.029	0.011	9.918	-0.084	-0.084	0.000	0.000	0.000	0.000
10	A	11	THR	0	-0.044	-0.038	8.908	0.150	0.150	0.000	0.000	0.000	0.000
11	A	12	THR	0	0.040	0.032	10.290	-0.176	-0.176	0.000	0.000	0.000	0.000
12	A	13	VAL	0	-0.007	-0.027	7.294	-0.025	-0.025	0.000	0.000	0.000	0.000
13	A	14	ASP	-1	-0.834	-0.909	10.080	-0.248	-0.248	0.000	0.000	0.000	0.000
14	A	16	SER	0	-0.024	-0.007	13.430	0.017	0.017	0.000	0.000	0.000	0.000
15	A	17	GLY	0	0.081	0.043	17.192	0.000	0.000	0.000	0.000	0.000	0.000
16	A	18	LYS	1	0.796	0.912	13.739	0.374	0.374	0.000	0.000	0.000	0.000
17	A	19	SER	0	-0.023	-0.010	17.227	-0.008	-0.008	0.000	0.000	0.000	0.000
18	A	20	LEU	0	-0.030	0.000	13.558	-0.015	-0.015	0.000	0.000	0.000	0.000
19	A	21	ALA	0	0.042	0.012	17.314	0.032	0.032	0.000	0.000	0.000	0.000
20	A	22	SER	0	-0.067	-0.047	15.083	-0.003	-0.003	0.000	0.000	0.000	0.000
21	A	23	VAL	0	0.042	0.016	11.936	-0.018	-0.018	0.000	0.000	0.000	0.000
22	A	24	PRO	0	0.002	0.003	8.948	-0.040	-0.040	0.000	0.000	0.000	0.000
23	A	25	THR	0	0.045	0.019	7.573	-0.078	-0.078	0.000	0.000	0.000	0.000
24	A	26	GLY	0	-0.025	-0.018	4.874	-0.242	-0.242	0.000	0.000	0.000	0.000
25	A	27	ILE	0	0.017	0.012	4.197	-1.831	-1.866	-0.001	-0.043	0.079	0.000
26	A	28	PRO	0	0.012	0.014	2.611	-0.306	0.410	0.158	-0.265	-0.609	0.000
27	A	29	THR	0	0.013	-0.002	4.627	0.301	0.356	-0.001	-0.008	-0.046	0.000
28	A	30	THR	0	-0.041	-0.008	7.025	-0.043	-0.043	0.000	0.000	0.000	0.000
29	A	31	THR	0	-0.044	-0.038	7.325	0.042	0.042	0.000	0.000	0.000	0.000
30	A	32	GLN	0	0.024	0.039	9.552	0.010	0.010	0.000	0.000	0.000	0.000
31	A	33	VAL	0	0.025	0.030	12.721	-0.043	-0.043	0.000	0.000	0.000	0.000
32	A	34	LEU	0	0.010	0.005	10.525	-0.045	-0.045	0.000	0.000	0.000	0.000
33	A	35	TYR	0	-0.007	0.001	13.257	0.042	0.042	0.000	0.000	0.000	0.000
34	A	36	LEU	0	0.007	-0.013	13.130	-0.086	-0.086	0.000	0.000	0.000	0.000
35	A	37	TYR	0	0.022	0.029	16.414	-0.004	-0.004	0.000	0.000	0.000	0.000
36	A	38	ASP	-1	-0.887	-0.944	19.671	-0.203	-0.203	0.000	0.000	0.000	0.000
37	A	39	ASN	0	-0.080	-0.047	16.851	-0.022	-0.022	0.000	0.000	0.000	0.000
38	A	40	GLN	0	0.033	0.014	20.327	0.036	0.036	0.000	0.000	0.000	0.000
39	A	41	ILE	0	-0.014	0.007	16.838	-0.006	-0.006	0.000	0.000	0.000	0.000
40	A	42	THR	0	0.015	0.008	20.781	0.031	0.031	0.000	0.000	0.000	0.000
41	A	43	LYS	1	0.933	0.948	21.620	0.231	0.231	0.000	0.000	0.000	0.000
42	A	44	LEU	0	0.021	0.013	17.490	-0.030	-0.030	0.000	0.000	0.000	0.000
43	A	45	GLU	-1	-0.894	-0.942	15.180	-0.399	-0.399	0.000	0.000	0.000	0.000
44	A	46	PRO	0	-0.018	-0.032	17.941	-0.003	-0.003	0.000	0.000	0.000	0.000
45	A	47	GLY	0	0.066	0.042	17.467	-0.024	-0.024	0.000	0.000	0.000	0.000
46	A	48	VAL	0	-0.054	-0.014	13.043	-0.034	-0.034	0.000	0.000	0.000	0.000
47	A	49	PHE	0	0.032	0.003	12.607	-0.094	-0.094	0.000	0.000	0.000	0.000
48	A	50	ASP	-1	-0.891	-0.943	14.194	-0.234	-0.234	0.000	0.000	0.000	0.000
49	A	51	ARG	1	0.914	0.940	7.488	0.820	0.820	0.000	0.000	0.000	0.000
50	A	52	LEU	0	-0.023	0.000	8.773	0.068	0.068	0.000	0.000	0.000	0.000
51	A	53	THR	0	0.013	0.000	12.004	0.057	0.057	0.000	0.000	0.000	0.000
52	A	54	GLN	0	-0.038	-0.026	12.457	0.053	0.053	0.000	0.000	0.000	0.000
53	A	55	LEU	0	-0.024	0.003	12.313	0.022	0.022	0.000	0.000	0.000	0.000
54	A	56	THR	0	-0.038	-0.019	14.872	0.011	0.011	0.000	0.000	0.000	0.000
55	A	57	ARG	1	0.801	0.842	16.581	0.094	0.094	0.000	0.000	0.000	0.000
56	A	58	LEU	0	-0.007	0.003	15.291	-0.029	-0.029	0.000	0.000	0.000	0.000
57	A	59	ASP	-1	-0.788	-0.854	17.299	-0.120	-0.120	0.000	0.000	0.000	0.000
58	A	60	LEU	0	0.014	-0.016	17.433	-0.046	-0.046	0.000	0.000	0.000	0.000
59	A	61	ASP	-1	-0.831	-0.890	20.287	-0.164	-0.164	0.000	0.000	0.000	0.000
60	A	62	ASN	0	-0.020	-0.025	22.674	-0.011	-0.011	0.000	0.000	0.000	0.000
61	A	63	ASN	0	-0.021	-0.001	20.006	-0.039	-0.039	0.000	0.000	0.000	0.000
62	A	64	GLN	0	-0.006	-0.005	23.733	0.029	0.029	0.000	0.000	0.000	0.000
63	A	65	LEU	0	-0.036	-0.011	21.083	0.002	0.002	0.000	0.000	0.000	0.000
64	A	66	THR	0	-0.001	-0.009	25.014	0.020	0.020	0.000	0.000	0.000	0.000
65	A	67	VAL	0	-0.059	-0.033	25.954	0.015	0.015	0.000	0.000	0.000	0.000
66	A	68	LEU	0	0.009	0.008	22.428	-0.019	-0.019	0.000	0.000	0.000	0.000
67	A	69	PRO	0	0.002	-0.002	20.568	0.020	0.020	0.000	0.000	0.000	0.000
68	A	70	ALA	0	0.045	0.007	23.835	0.006	0.006	0.000	0.000	0.000	0.000
69	A	71	GLY	0	0.041	0.019	23.717	-0.013	-0.013	0.000	0.000	0.000	0.000
70	A	72	VAL	0	-0.045	-0.008	18.854	-0.008	-0.008	0.000	0.000	0.000	0.000
71	A	73	PHE	0	0.041	0.006	18.899	-0.023	-0.023	0.000	0.000	0.000	0.000
72	A	74	ASP	-1	-0.894	-0.937	20.680	-0.112	-0.112	0.000	0.000	0.000	0.000
73	A	75	LYS	1	0.933	0.960	17.312	0.157	0.157	0.000	0.000	0.000	0.000
74	A	76	LEU	0	-0.008	0.013	15.766	0.021	0.021	0.000	0.000	0.000	0.000
75	A	77	THR	0	-0.036	-0.027	18.828	0.023	0.023	0.000	0.000	0.000	0.000
76	A	78	GLN	0	-0.027	-0.016	17.129	0.023	0.023	0.000	0.000	0.000	0.000
77	A	79	LEU	0	-0.016	0.011	17.939	0.009	0.009	0.000	0.000	0.000	0.000
78	A	80	THR	0	0.020	0.001	20.276	0.008	0.008	0.000	0.000	0.000	0.000
79	A	81	GLN	0	-0.042	0.002	21.353	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	82	LEU	0	0.025	0.020	20.588	-0.014	-0.014	0.000	0.000	0.000	0.000
81	A	83	SER	0	-0.014	-0.021	21.707	0.009	0.009	0.000	0.000	0.000	0.000
82	A	84	LEU	0	0.017	-0.006	22.523	-0.023	-0.023	0.000	0.000	0.000	0.000
83	A	85	ASN	0	-0.036	-0.021	24.959	-0.003	-0.003	0.000	0.000	0.000	0.000
84	A	86	ASP	-1	-0.730	-0.838	26.460	-0.121	-0.121	0.000	0.000	0.000	0.000
85	A	87	ASN	0	-0.034	-0.007	23.853	-0.029	-0.029	0.000	0.000	0.000	0.000
86	A	88	GLN	0	0.020	-0.008	27.781	0.019	0.019	0.000	0.000	0.000	0.000
87	A	89	LEU	0	-0.020	0.006	25.891	0.001	0.001	0.000	0.000	0.000	0.000
88	A	90	LYS	1	0.995	0.991	29.884	0.116	0.116	0.000	0.000	0.000	0.000
89	A	91	SER	0	-0.018	-0.012	31.403	0.007	0.007	0.000	0.000	0.000	0.000
90	A	92	ILE	0	0.036	0.023	27.348	-0.010	-0.010	0.000	0.000	0.000	0.000
91	A	93	PRO	0	-0.013	0.004	26.440	0.010	0.010	0.000	0.000	0.000	0.000
92	A	94	ARG	1	0.970	0.964	29.599	0.080	0.080	0.000	0.000	0.000	0.000
93	A	95	GLY	0	0.049	0.015	30.054	-0.005	-0.005	0.000	0.000	0.000	0.000
94	A	96	ALA	0	-0.028	0.012	25.757	0.000	0.000	0.000	0.000	0.000	0.000
95	A	97	PHE	0	0.020	-0.018	25.172	-0.008	-0.008	0.000	0.000	0.000	0.000
96	A	98	ASP	-1	-0.855	-0.915	27.062	-0.064	-0.064	0.000	0.000	0.000	0.000
97	A	99	ASN	0	-0.047	-0.027	23.889	0.018	0.018	0.000	0.000	0.000	0.000
98	A	100	LEU	0	-0.018	0.007	21.994	0.006	0.006	0.000	0.000	0.000	0.000
99	A	101	LYS	1	0.915	0.944	24.218	0.002	0.002	0.000	0.000	0.000	0.000
100	A	102	SER	0	-0.046	-0.031	23.160	0.014	0.014	0.000	0.000	0.000	0.000
101	A	103	LEU	0	-0.045	0.004	24.150	0.003	0.003	0.000	0.000	0.000	0.000
102	A	104	THR	0	-0.012	-0.046	25.900	0.007	0.007	0.000	0.000	0.000	0.000
103	A	105	HIS	0	-0.029	0.019	25.894	0.001	0.001	0.000	0.000	0.000	0.000
104	A	106	ILE	0	-0.001	0.001	25.651	-0.008	-0.008	0.000	0.000	0.000	0.000
105	A	107	TRP	0	-0.009	0.009	24.471	0.005	0.005	0.000	0.000	0.000	0.000
106	A	108	LEU	0	0.040	-0.004	27.348	-0.012	-0.012	0.000	0.000	0.000	0.000
107	A	109	LEU	0	0.006	0.018	29.964	-0.003	-0.003	0.000	0.000	0.000	0.000
108	A	110	ASN	0	-0.051	-0.028	30.843	-0.002	-0.002	0.000	0.000	0.000	0.000
109	A	111	ASN	0	0.025	0.009	28.444	-0.018	-0.018	0.000	0.000	0.000	0.000
110	A	112	PRO	0	-0.035	0.008	31.955	0.010	0.010	0.000	0.000	0.000	0.000
111	A	113	TRP	0	-0.042	-0.028	29.383	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	114	ASP	-1	-0.866	-0.950	35.581	-0.076	-0.076	0.000	0.000	0.000	0.000
113	A	115	CYS	0	-0.054	-0.029	37.549	-0.005	-0.005	0.000	0.000	0.000	0.000
114	A	116	ALA	0	0.024	0.024	40.500	0.004	0.004	0.000	0.000	0.000	0.000
115	A	167	CYS	0	0.051	0.085	38.475	0.001	0.001	0.000	0.000	0.000	0.000
116	A	118	SER	0	0.040	-0.007	39.699	0.000	0.000	0.000	0.000	0.000	0.000
117	A	119	ASP	-1	-0.911	-0.976	34.878	-0.094	-0.094	0.000	0.000	0.000	0.000
118	A	120	ILE	0	-0.051	-0.014	35.248	-0.003	-0.003	0.000	0.000	0.000	0.000
119	A	121	LEU	0	-0.023	-0.016	36.850	0.002	0.002	0.000	0.000	0.000	0.000
120	A	122	TYR	0	-0.058	-0.030	30.045	0.002	0.002	0.000	0.000	0.000	0.000
121	A	123	LEU	0	0.053	0.036	31.295	0.003	0.003	0.000	0.000	0.000	0.000
122	A	124	SER	0	-0.009	-0.013	34.061	0.005	0.005	0.000	0.000	0.000	0.000
123	A	125	ARG	1	0.869	0.896	37.566	0.056	0.056	0.000	0.000	0.000	0.000
124	A	126	TRP	0	0.013	0.019	29.523	0.004	0.004	0.000	0.000	0.000	0.000
125	A	127	ILE	0	0.031	0.000	33.754	0.004	0.004	0.000	0.000	0.000	0.000
126	A	128	SER	0	-0.078	-0.039	35.533	0.006	0.006	0.000	0.000	0.000	0.000
127	A	129	GLN	0	-0.049	-0.029	36.347	0.006	0.006	0.000	0.000	0.000	0.000
128	A	130	HIS	1	0.867	0.946	32.978	0.048	0.048	0.000	0.000	0.000	0.000
129	A	131	PRO	0	0.046	0.025	34.211	-0.003	-0.003	0.000	0.000	0.000	0.000
130	A	132	GLY	0	0.003	-0.012	35.529	-0.001	-0.001	0.000	0.000	0.000	0.000
131	A	133	LEU	0	-0.010	0.006	29.620	0.003	0.003	0.000	0.000	0.000	0.000
132	A	134	VAL	0	-0.009	0.001	30.381	-0.006	-0.006	0.000	0.000	0.000	0.000
133	A	135	PHE	0	-0.010	0.004	29.993	0.007	0.007	0.000	0.000	0.000	0.000
134	A	136	GLY	0	0.060	0.027	31.555	-0.008	-0.008	0.000	0.000	0.000	0.000
135	A	137	TYR	0	-0.076	-0.085	30.110	0.004	0.004	0.000	0.000	0.000	0.000
136	A	138	LEU	0	-0.025	-0.005	31.825	0.002	0.002	0.000	0.000	0.000	0.000
137	A	139	ASN	0	0.013	-0.001	33.967	0.005	0.005	0.000	0.000	0.000	0.000
138	A	140	LEU	0	-0.017	0.006	34.025	-0.005	-0.005	0.000	0.000	0.000	0.000
139	A	141	ASP	-1	-0.891	-0.972	35.245	-0.045	-0.045	0.000	0.000	0.000	0.000
140	A	142	PRO	0	0.010	0.023	35.729	-0.006	-0.006	0.000	0.000	0.000	0.000
141	A	143	ASP	-1	-0.853	-0.904	36.789	-0.045	-0.045	0.000	0.000	0.000	0.000
142	A	144	SER	0	-0.048	-0.036	34.741	-0.004	-0.004	0.000	0.000	0.000	0.000
143	A	145	ALA	0	-0.016	0.007	33.756	-0.005	-0.005	0.000	0.000	0.000	0.000
144	A	146	ARG	1	0.946	0.973	35.489	0.059	0.059	0.000	0.000	0.000	0.000
145	A	148	SER	0	0.065	0.041	38.177	0.004	0.004	0.000	0.000	0.000	0.000
146	A	149	GLY	0	-0.004	0.008	39.932	0.002	0.002	0.000	0.000	0.000	0.000
147	A	150	THR	0	-0.006	-0.041	43.395	0.002	0.002	0.000	0.000	0.000	0.000
148	A	151	ASN	0	-0.084	-0.032	40.877	0.005	0.005	0.000	0.000	0.000	0.000
149	A	152	THR	0	0.006	0.002	42.795	0.001	0.001	0.000	0.000	0.000	0.000
150	A	153	PRO	0	0.029	0.019	40.195	-0.004	-0.004	0.000	0.000	0.000	0.000
151	A	154	VAL	0	0.055	0.008	36.027	0.002	0.002	0.000	0.000	0.000	0.000
152	A	155	ARG	1	0.838	0.897	38.512	0.041	0.041	0.000	0.000	0.000	0.000
153	A	156	ALA	0	-0.041	-0.005	39.871	0.003	0.003	0.000	0.000	0.000	0.000
154	A	157	VAL	0	-0.008	-0.007	40.917	0.002	0.002	0.000	0.000	0.000	0.000
155	A	158	THR	0	-0.014	-0.013	43.621	0.000	0.000	0.000	0.000	0.000	0.000
156	A	159	GLU	-1	-0.756	-0.856	42.805	-0.048	-0.048	0.000	0.000	0.000	0.000
157	A	160	ALA	0	-0.027	-0.007	45.781	-0.002	-0.002	0.000	0.000	0.000	0.000
158	A	161	SER	0	0.011	0.006	45.150	0.001	0.001	0.000	0.000	0.000	0.000
159	A	162	THR	0	-0.075	-0.020	42.147	-0.002	-0.002	0.000	0.000	0.000	0.000
160	A	163	SER	0	-0.019	-0.015	43.797	0.002	0.002	0.000	0.000	0.000	0.000
161	A	164	PRO	0	0.070	0.028	41.965	-0.003	-0.003	0.000	0.000	0.000	0.000
162	A	165	SER	0	-0.061	-0.039	42.420	-0.003	-0.003	0.000	0.000	0.000	0.000
163	A	166	LYS	1	0.921	0.970	43.632	0.056	0.056	0.000	0.000	0.000	0.000

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