FMO DATABASE

FMODB ID: QYQ2Y

Calculation Name: 2G3A-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2G3A

Chain ID: A

ChEMBL ID:

UniProt ID: Q7CXI0

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:

Apendix: None

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
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	137
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1079409.012676
FMO2-HF: Nuclear repulsion	1025580.051771
FMO2-HF: Total energy	-53828.960904
FMO2-MP2: Total energy	-53984.065418

3D Structure Molmil

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:MET)

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

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.
-2.258	1.561	1.474	-1.482	-3.81	-0.008

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.015 / q_NPA : -0.020

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	PHE	0	0.005	0.005	2.805	-3.365	0.367	1.475	-1.468	-3.738	-0.008
4	A	4	VAL	0	-0.010	-0.005	4.491	0.356	0.443	-0.001	-0.014	-0.072	0.000
5	A	5	LEU	0	-0.023	-0.004	8.106	0.026	0.026	0.000	0.000	0.000	0.000
6	A	6	SER	0	-0.013	-0.018	11.318	0.084	0.084	0.000	0.000	0.000	0.000
7	A	7	ASP	-1	-0.918	-0.956	14.439	-0.003	-0.003	0.000	0.000	0.000	0.000
8	A	8	VAL	0	-0.030	-0.002	17.680	-0.002	-0.002	0.000	0.000	0.000	0.000
9	A	9	ALA	0	-0.011	-0.013	17.415	0.014	0.014	0.000	0.000	0.000	0.000
10	A	10	ASP	-1	-0.829	-0.914	14.990	0.414	0.414	0.000	0.000	0.000	0.000
11	A	11	ALA	0	0.018	0.012	16.424	0.001	0.001	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.890	-0.952	15.708	0.268	0.268	0.000	0.000	0.000	0.000
13	A	13	ALA	0	-0.007	-0.006	11.759	0.043	0.043	0.000	0.000	0.000	0.000
14	A	14	GLU	-1	-0.853	-0.917	12.278	0.100	0.100	0.000	0.000	0.000	0.000
15	A	15	LYS	1	0.776	0.871	14.502	-0.193	-0.193	0.000	0.000	0.000	0.000
16	A	16	ALA	0	0.001	0.000	10.177	-0.039	-0.039	0.000	0.000	0.000	0.000
17	A	17	ILE	0	-0.013	0.002	9.427	0.008	0.008	0.000	0.000	0.000	0.000
18	A	18	ARG	1	0.839	0.890	11.661	-0.149	-0.149	0.000	0.000	0.000	0.000
19	A	19	ASP	-1	-0.783	-0.873	14.325	0.111	0.111	0.000	0.000	0.000	0.000
20	A	20	PRO	0	0.001	0.004	10.289	-0.052	-0.052	0.000	0.000	0.000	0.000
21	A	21	LEU	0	0.013	0.019	13.092	-0.064	-0.064	0.000	0.000	0.000	0.000
22	A	22	VAL	0	0.002	0.001	14.470	-0.034	-0.034	0.000	0.000	0.000	0.000
23	A	23	ALA	0	0.014	0.008	15.358	-0.015	-0.015	0.000	0.000	0.000	0.000
24	A	24	TYR	0	0.010	0.014	14.066	-0.021	-0.021	0.000	0.000	0.000	0.000
25	A	25	ASN	0	-0.056	-0.058	16.191	-0.019	-0.019	0.000	0.000	0.000	0.000
26	A	26	LEU	0	-0.014	0.010	19.299	0.000	0.000	0.000	0.000	0.000	0.000
27	A	27	ALA	0	-0.014	-0.011	18.412	0.000	0.000	0.000	0.000	0.000	0.000
28	A	28	ARG	1	0.867	0.941	17.733	0.228	0.228	0.000	0.000	0.000	0.000
29	A	29	PHE	0	-0.052	-0.035	20.221	-0.007	-0.007	0.000	0.000	0.000	0.000
30	A	30	GLY	0	0.056	0.046	23.884	0.008	0.008	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.909	-0.955	24.879	-0.024	-0.024	0.000	0.000	0.000	0.000
32	A	32	SER	0	-0.025	-0.028	24.868	-0.004	-0.004	0.000	0.000	0.000	0.000
33	A	33	ASP	-1	-0.882	-0.939	27.265	-0.031	-0.031	0.000	0.000	0.000	0.000
34	A	34	LYS	1	0.793	0.891	26.678	-0.006	-0.006	0.000	0.000	0.000	0.000
35	A	35	ARG	1	0.918	0.963	29.127	0.010	0.010	0.000	0.000	0.000	0.000
36	A	36	ASP	-1	-0.813	-0.895	30.645	0.007	0.007	0.000	0.000	0.000	0.000
37	A	37	LEU	0	-0.037	-0.020	33.083	0.000	0.000	0.000	0.000	0.000	0.000
38	A	38	ASN	0	0.030	0.023	33.555	-0.005	-0.005	0.000	0.000	0.000	0.000
39	A	39	ILE	0	-0.005	-0.003	37.657	0.001	0.001	0.000	0.000	0.000	0.000
40	A	40	THR	0	-0.015	0.009	40.063	0.000	0.000	0.000	0.000	0.000	0.000
41	A	41	ILE	0	0.009	-0.010	42.254	0.000	0.000	0.000	0.000	0.000	0.000
42	A	42	ARG	1	0.852	0.905	41.371	-0.017	-0.017	0.000	0.000	0.000	0.000
43	A	43	ASN	0	-0.013	-0.020	47.266	-0.001	-0.001	0.000	0.000	0.000	0.000
44	A	44	ASP	-1	-0.873	-0.938	50.557	0.010	0.010	0.000	0.000	0.000	0.000
45	A	45	ASP	-1	-0.845	-0.875	49.064	0.019	0.019	0.000	0.000	0.000	0.000
46	A	46	ASN	0	-0.038	-0.026	45.662	0.001	0.001	0.000	0.000	0.000	0.000
47	A	47	SER	0	0.017	0.001	45.060	0.002	0.002	0.000	0.000	0.000	0.000
48	A	48	VAL	0	-0.072	-0.039	40.281	-0.002	-0.002	0.000	0.000	0.000	0.000
49	A	49	THR	0	-0.005	-0.007	43.393	0.000	0.000	0.000	0.000	0.000	0.000
50	A	50	GLY	0	-0.001	-0.010	41.896	-0.002	-0.002	0.000	0.000	0.000	0.000
51	A	51	GLY	0	-0.011	0.000	41.287	0.002	0.002	0.000	0.000	0.000	0.000
52	A	52	LEU	0	-0.038	-0.005	37.763	-0.003	-0.003	0.000	0.000	0.000	0.000
53	A	53	VAL	0	0.011	0.002	32.744	0.004	0.004	0.000	0.000	0.000	0.000
54	A	54	GLY	0	0.065	0.022	33.039	-0.005	-0.005	0.000	0.000	0.000	0.000
55	A	55	HIS	0	-0.041	-0.001	28.071	0.009	0.009	0.000	0.000	0.000	0.000
56	A	56	THR	0	0.044	0.026	32.641	-0.003	-0.003	0.000	0.000	0.000	0.000
57	A	57	ALA	0	0.035	0.020	28.046	0.005	0.005	0.000	0.000	0.000	0.000
58	A	58	ARG	1	0.862	0.922	23.496	0.069	0.069	0.000	0.000	0.000	0.000
59	A	59	GLY	0	0.068	0.049	30.337	-0.004	-0.004	0.000	0.000	0.000	0.000
60	A	60	TRP	0	-0.051	-0.016	32.188	0.000	0.000	0.000	0.000	0.000	0.000
61	A	61	LEU	0	-0.016	-0.015	33.047	0.003	0.003	0.000	0.000	0.000	0.000
62	A	62	TYR	0	-0.088	-0.052	29.415	-0.002	-0.002	0.000	0.000	0.000	0.000
63	A	63	VAL	0	-0.028	-0.026	33.176	0.007	0.007	0.000	0.000	0.000	0.000
64	A	64	GLN	0	0.030	0.021	27.969	-0.003	-0.003	0.000	0.000	0.000	0.000
65	A	65	LEU	0	-0.006	-0.008	32.069	0.000	0.000	0.000	0.000	0.000	0.000
66	A	66	LEU	0	-0.005	-0.008	35.046	0.001	0.001	0.000	0.000	0.000	0.000
67	A	67	PHE	0	0.008	0.005	38.847	-0.002	-0.002	0.000	0.000	0.000	0.000
68	A	68	VAL	0	0.013	0.008	41.110	0.001	0.001	0.000	0.000	0.000	0.000
69	A	69	PRO	0	0.058	0.024	44.920	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	70	GLU	-1	-0.815	-0.895	46.855	-0.006	-0.006	0.000	0.000	0.000	0.000
71	A	71	ALA	0	0.021	0.007	48.754	-0.001	-0.001	0.000	0.000	0.000	0.000
72	A	72	MET	0	0.007	0.018	49.324	0.000	0.000	0.000	0.000	0.000	0.000
73	A	73	ARG	1	0.810	0.892	45.087	0.006	0.006	0.000	0.000	0.000	0.000
74	A	74	GLY	0	0.006	0.000	49.891	0.000	0.000	0.000	0.000	0.000	0.000
75	A	75	GLN	0	-0.046	-0.027	51.997	0.000	0.000	0.000	0.000	0.000	0.000
76	A	76	GLY	0	0.010	0.002	51.037	0.001	0.001	0.000	0.000	0.000	0.000
77	A	77	ILE	0	0.007	0.006	46.801	-0.001	-0.001	0.000	0.000	0.000	0.000
78	A	78	ALA	0	0.049	0.024	44.368	0.000	0.000	0.000	0.000	0.000	0.000
79	A	79	PRO	0	0.025	-0.003	44.957	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	80	LYS	1	0.965	0.997	46.777	0.005	0.005	0.000	0.000	0.000	0.000
81	A	81	LEU	0	-0.005	-0.002	42.436	0.000	0.000	0.000	0.000	0.000	0.000
82	A	82	LEU	0	0.010	0.006	40.574	0.000	0.000	0.000	0.000	0.000	0.000
83	A	83	ALA	0	0.022	0.018	43.160	-0.001	-0.001	0.000	0.000	0.000	0.000
84	A	84	MET	0	-0.008	-0.009	44.901	0.000	0.000	0.000	0.000	0.000	0.000
85	A	85	ALA	0	0.022	0.011	39.462	0.001	0.001	0.000	0.000	0.000	0.000
86	A	86	GLU	-1	-0.753	-0.819	40.757	-0.031	-0.031	0.000	0.000	0.000	0.000
87	A	87	GLU	-1	-0.851	-0.908	42.354	-0.012	-0.012	0.000	0.000	0.000	0.000
88	A	88	GLU	-1	-0.792	-0.881	39.763	-0.006	-0.006	0.000	0.000	0.000	0.000
89	A	89	ALA	0	0.020	0.000	38.488	0.000	0.000	0.000	0.000	0.000	0.000
90	A	90	ARG	1	0.845	0.903	39.726	0.027	0.027	0.000	0.000	0.000	0.000
91	A	91	LYS	1	0.799	0.884	42.644	0.010	0.010	0.000	0.000	0.000	0.000
92	A	92	ARG	1	0.680	0.807	35.171	0.010	0.010	0.000	0.000	0.000	0.000
93	A	93	GLY	0	0.018	0.025	38.347	-0.002	-0.002	0.000	0.000	0.000	0.000
94	A	94	CYS	0	-0.100	-0.037	36.808	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	95	MET	0	0.027	-0.002	36.929	0.000	0.000	0.000	0.000	0.000	0.000
96	A	96	GLY	0	-0.005	0.000	37.749	-0.002	-0.002	0.000	0.000	0.000	0.000
97	A	97	ALA	0	-0.019	0.005	36.375	0.002	0.002	0.000	0.000	0.000	0.000
98	A	98	TYR	0	-0.009	-0.010	28.419	-0.003	-0.003	0.000	0.000	0.000	0.000
99	A	99	ILE	0	-0.028	-0.007	34.345	0.005	0.005	0.000	0.000	0.000	0.000
100	A	100	ASP	-1	-0.827	-0.896	31.008	-0.062	-0.062	0.000	0.000	0.000	0.000
101	A	101	THR	0	0.010	-0.005	34.093	0.007	0.007	0.000	0.000	0.000	0.000
102	A	102	MET	0	0.062	0.040	33.197	-0.006	-0.006	0.000	0.000	0.000	0.000
103	A	103	ASN	0	0.010	0.012	35.630	0.002	0.002	0.000	0.000	0.000	0.000
104	A	104	PRO	0	0.097	0.022	39.249	0.000	0.000	0.000	0.000	0.000	0.000
105	A	105	ASP	-1	-0.814	-0.886	42.267	-0.029	-0.029	0.000	0.000	0.000	0.000
106	A	106	ALA	0	0.002	0.019	40.068	0.001	0.001	0.000	0.000	0.000	0.000
107	A	107	LEU	0	0.031	0.026	38.999	0.000	0.000	0.000	0.000	0.000	0.000
108	A	108	ARG	1	0.869	0.914	41.462	0.030	0.030	0.000	0.000	0.000	0.000
109	A	109	THR	0	-0.064	-0.038	44.428	0.002	0.002	0.000	0.000	0.000	0.000
110	A	110	TYR	0	0.010	0.003	37.320	0.003	0.003	0.000	0.000	0.000	0.000
111	A	111	GLU	-1	-0.766	-0.870	42.578	-0.050	-0.050	0.000	0.000	0.000	0.000
112	A	112	ARG	1	0.829	0.900	44.607	0.027	0.027	0.000	0.000	0.000	0.000
113	A	113	TYR	0	-0.050	-0.045	43.421	0.002	0.002	0.000	0.000	0.000	0.000
114	A	114	GLY	0	0.019	0.010	45.882	0.001	0.001	0.000	0.000	0.000	0.000
115	A	115	PHE	0	-0.060	-0.035	38.055	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	116	THR	0	0.013	0.003	40.171	0.001	0.001	0.000	0.000	0.000	0.000
117	A	117	LYS	1	0.792	0.858	38.173	0.053	0.053	0.000	0.000	0.000	0.000
118	A	118	ILE	0	-0.010	0.001	32.909	0.000	0.000	0.000	0.000	0.000	0.000
119	A	119	GLY	0	0.022	0.018	33.040	-0.007	-0.007	0.000	0.000	0.000	0.000
120	A	120	SER	0	-0.045	-0.025	33.245	0.005	0.005	0.000	0.000	0.000	0.000
121	A	121	LEU	0	0.008	0.015	27.606	-0.008	-0.008	0.000	0.000	0.000	0.000
122	A	122	GLY	0	0.000	0.003	31.917	0.008	0.008	0.000	0.000	0.000	0.000
123	A	123	PRO	0	-0.004	0.009	33.096	-0.005	-0.005	0.000	0.000	0.000	0.000
124	A	124	LEU	0	0.028	-0.002	29.893	-0.007	-0.007	0.000	0.000	0.000	0.000
125	A	125	SER	0	0.023	0.004	30.887	0.002	0.002	0.000	0.000	0.000	0.000
126	A	126	SER	0	-0.025	-0.020	32.737	0.002	0.002	0.000	0.000	0.000	0.000
127	A	127	GLY	0	0.002	0.003	35.445	0.005	0.005	0.000	0.000	0.000	0.000
128	A	128	GLN	0	-0.039	0.000	35.934	-0.002	-0.002	0.000	0.000	0.000	0.000
129	A	129	SER	0	0.032	0.009	34.178	-0.005	-0.005	0.000	0.000	0.000	0.000
130	A	130	ILE	0	0.002	0.011	28.842	0.006	0.006	0.000	0.000	0.000	0.000
131	A	131	THR	0	-0.046	-0.034	32.984	-0.006	-0.006	0.000	0.000	0.000	0.000
132	A	132	TRP	0	0.041	0.019	28.105	0.003	0.003	0.000	0.000	0.000	0.000
133	A	133	LEU	0	-0.043	-0.031	33.969	-0.001	-0.001	0.000	0.000	0.000	0.000
134	A	134	GLU	-1	-0.803	-0.885	35.772	-0.066	-0.066	0.000	0.000	0.000	0.000
135	A	135	LYS	1	0.847	0.909	37.534	0.035	0.035	0.000	0.000	0.000	0.000
136	A	136	ARG	1	0.908	0.942	36.508	0.067	0.067	0.000	0.000	0.000	0.000
137	A	137	PHE	0	-0.035	-0.015	40.097	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:1:MET)