FMO DATABASE

FMODB ID: G56J1

Calculation Name: 3CG0-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3CG0

Chain ID: A

ChEMBL ID:

UniProt ID: Q311G8

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:

Apendix: None

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	126
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-874974.911589
FMO2-HF: Nuclear repulsion	826973.635772
FMO2-HF: Total energy	-48001.275816
FMO2-MP2: Total energy	-48139.944146

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:6:ASP)

Summations of interaction energy for fragment #1(A:6:ASP)

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.
100.18	101.862	-0.015	-0.688	-0.979	0.003

Interaction energy analysis for fragmet #1(A:6:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.993 / q_NPA : -1.000

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	8	PRO	0	-0.008	0.011	3.821	-2.480	-0.798	-0.015	-0.688	-0.979	0.003
4	A	9	GLY	0	0.058	0.024	6.484	-1.214	-1.214	0.000	0.000	0.000	0.000
5	A	10	VAL	0	-0.040	-0.022	8.695	-1.737	-1.737	0.000	0.000	0.000	0.000
6	A	11	LEU	0	0.008	0.018	12.331	-0.224	-0.224	0.000	0.000	0.000	0.000
7	A	12	ILE	0	-0.019	-0.016	15.481	-0.422	-0.422	0.000	0.000	0.000	0.000
8	A	13	VAL	0	-0.016	-0.012	18.640	-0.253	-0.253	0.000	0.000	0.000	0.000
9	A	14	GLU	-1	-0.843	-0.932	22.214	11.104	11.104	0.000	0.000	0.000	0.000
10	A	15	ASP	-1	-0.872	-0.934	24.508	9.963	9.963	0.000	0.000	0.000	0.000
11	A	16	GLY	0	-0.060	-0.012	27.612	-0.265	-0.265	0.000	0.000	0.000	0.000
12	A	17	ARG	1	0.971	0.961	26.541	-9.376	-9.376	0.000	0.000	0.000	0.000
13	A	18	LEU	0	0.003	0.002	26.304	0.262	0.262	0.000	0.000	0.000	0.000
14	A	19	ALA	0	0.045	0.061	25.107	0.319	0.319	0.000	0.000	0.000	0.000
15	A	20	ALA	0	0.080	0.040	22.340	0.512	0.512	0.000	0.000	0.000	0.000
16	A	21	ALA	0	-0.044	-0.015	21.209	0.631	0.631	0.000	0.000	0.000	0.000
17	A	22	THR	0	-0.053	-0.080	21.288	0.332	0.332	0.000	0.000	0.000	0.000
18	A	23	LEU	0	0.030	0.011	19.023	0.477	0.477	0.000	0.000	0.000	0.000
19	A	24	ARG	1	0.962	1.003	15.802	-15.809	-15.809	0.000	0.000	0.000	0.000
20	A	25	ILE	0	0.002	0.003	16.137	0.840	0.840	0.000	0.000	0.000	0.000
21	A	26	GLN	0	-0.016	-0.026	16.662	0.679	0.679	0.000	0.000	0.000	0.000
22	A	27	LEU	0	-0.003	0.002	13.280	0.630	0.630	0.000	0.000	0.000	0.000
23	A	28	GLU	-1	-0.880	-0.952	11.916	20.011	20.011	0.000	0.000	0.000	0.000
24	A	29	SER	0	-0.100	-0.040	11.929	0.694	0.694	0.000	0.000	0.000	0.000
25	A	30	LEU	0	-0.110	-0.063	12.570	0.508	0.508	0.000	0.000	0.000	0.000
26	A	31	GLY	0	-0.009	0.021	8.599	0.798	0.798	0.000	0.000	0.000	0.000
27	A	32	TYR	0	-0.068	-0.034	7.584	2.487	2.487	0.000	0.000	0.000	0.000
28	A	33	ASP	-1	-0.890	-0.942	7.048	29.340	29.340	0.000	0.000	0.000	0.000
29	A	34	VAL	0	-0.042	-0.024	9.024	-1.382	-1.382	0.000	0.000	0.000	0.000
30	A	35	LEU	0	0.022	0.019	9.331	-0.556	-0.556	0.000	0.000	0.000	0.000
31	A	36	GLY	0	-0.035	-0.019	12.991	-0.699	-0.699	0.000	0.000	0.000	0.000
32	A	37	VAL	0	-0.069	-0.034	16.776	0.171	0.171	0.000	0.000	0.000	0.000
33	A	38	PHE	0	-0.009	-0.014	18.131	-0.232	-0.232	0.000	0.000	0.000	0.000
34	A	39	ASP	-1	-0.901	-0.949	22.706	10.969	10.969	0.000	0.000	0.000	0.000
35	A	40	ASN	0	0.016	0.002	25.664	-0.469	-0.469	0.000	0.000	0.000	0.000
36	A	41	GLY	0	0.096	0.035	25.329	0.456	0.456	0.000	0.000	0.000	0.000
37	A	42	GLU	-1	-0.899	-0.973	25.281	10.224	10.224	0.000	0.000	0.000	0.000
38	A	43	GLU	-1	-0.951	-0.987	24.103	12.070	12.070	0.000	0.000	0.000	0.000
39	A	44	ALA	0	0.003	0.024	21.300	0.492	0.492	0.000	0.000	0.000	0.000
40	A	45	VAL	0	-0.033	-0.027	20.809	0.522	0.522	0.000	0.000	0.000	0.000
41	A	46	ARG	1	0.904	0.945	22.248	-11.029	-11.029	0.000	0.000	0.000	0.000
42	A	47	CYS	0	-0.012	-0.005	19.240	0.149	0.149	0.000	0.000	0.000	0.000
43	A	48	ALA	0	0.041	0.025	17.094	0.786	0.786	0.000	0.000	0.000	0.000
44	A	49	PRO	0	-0.004	-0.008	16.037	1.094	1.094	0.000	0.000	0.000	0.000
45	A	50	ASP	-1	-0.915	-0.955	16.080	15.856	15.856	0.000	0.000	0.000	0.000
46	A	51	LEU	0	-0.079	-0.040	13.749	1.021	1.021	0.000	0.000	0.000	0.000
47	A	52	ARG	1	0.829	0.927	10.463	-21.868	-21.868	0.000	0.000	0.000	0.000
48	A	53	PRO	0	0.001	0.007	10.463	1.641	1.641	0.000	0.000	0.000	0.000
49	A	54	ASP	-1	-0.845	-0.921	7.724	29.195	29.195	0.000	0.000	0.000	0.000
50	A	55	ILE	0	-0.067	-0.040	11.113	-1.233	-1.233	0.000	0.000	0.000	0.000
51	A	56	ALA	0	0.023	0.017	14.113	0.156	0.156	0.000	0.000	0.000	0.000
52	A	57	LEU	0	-0.032	-0.016	16.854	-0.476	-0.476	0.000	0.000	0.000	0.000
53	A	58	VAL	0	0.009	0.000	19.322	-0.103	-0.103	0.000	0.000	0.000	0.000
54	A	59	ASP	-1	-0.802	-0.898	22.744	10.318	10.318	0.000	0.000	0.000	0.000
55	A	60	ILE	0	-0.046	-0.025	25.923	-0.160	-0.160	0.000	0.000	0.000	0.000
56	A	61	MET	0	-0.150	-0.072	28.792	-0.529	-0.529	0.000	0.000	0.000	0.000
57	A	62	LEU	0	0.017	0.002	26.516	0.123	0.123	0.000	0.000	0.000	0.000
58	A	63	CYS	0	-0.072	-0.038	30.514	-0.382	-0.382	0.000	0.000	0.000	0.000
59	A	64	GLY	0	0.070	0.037	31.155	0.268	0.268	0.000	0.000	0.000	0.000
60	A	65	ALA	0	-0.073	-0.027	32.266	-0.229	-0.229	0.000	0.000	0.000	0.000
61	A	66	LEU	0	-0.064	-0.024	27.770	-0.214	-0.214	0.000	0.000	0.000	0.000
62	A	67	ASP	-1	-0.822	-0.901	30.593	9.347	9.347	0.000	0.000	0.000	0.000
63	A	68	GLY	0	0.055	0.015	27.720	0.279	0.279	0.000	0.000	0.000	0.000
64	A	69	VAL	0	-0.009	-0.013	27.069	0.405	0.405	0.000	0.000	0.000	0.000
65	A	70	GLU	-1	-0.886	-0.940	28.288	9.975	9.975	0.000	0.000	0.000	0.000
66	A	71	THR	0	-0.014	-0.014	24.062	0.250	0.250	0.000	0.000	0.000	0.000
67	A	72	ALA	0	0.020	0.005	23.494	0.442	0.442	0.000	0.000	0.000	0.000
68	A	73	ALA	0	-0.017	0.001	23.902	0.369	0.369	0.000	0.000	0.000	0.000
69	A	74	ARG	1	0.886	0.937	25.437	-9.830	-9.830	0.000	0.000	0.000	0.000
70	A	75	LEU	0	0.001	-0.004	19.361	0.268	0.268	0.000	0.000	0.000	0.000
71	A	76	ALA	0	0.011	0.010	20.238	0.609	0.609	0.000	0.000	0.000	0.000
72	A	77	ALA	0	-0.063	-0.019	21.982	0.113	0.113	0.000	0.000	0.000	0.000
73	A	78	GLY	0	-0.050	-0.029	22.833	0.099	0.099	0.000	0.000	0.000	0.000
74	A	79	CYS	0	-0.041	-0.024	17.649	0.151	0.151	0.000	0.000	0.000	0.000
75	A	80	ASN	0	-0.059	-0.009	17.107	0.358	0.358	0.000	0.000	0.000	0.000
76	A	81	LEU	0	0.050	0.028	14.690	0.726	0.726	0.000	0.000	0.000	0.000
77	A	82	PRO	0	-0.015	0.002	14.990	-1.037	-1.037	0.000	0.000	0.000	0.000
78	A	83	ILE	0	-0.012	-0.008	17.751	0.292	0.292	0.000	0.000	0.000	0.000
79	A	84	ILE	0	-0.025	-0.007	17.743	-0.303	-0.303	0.000	0.000	0.000	0.000
80	A	85	PHE	0	-0.021	-0.017	21.188	0.065	0.065	0.000	0.000	0.000	0.000
81	A	86	ILE	0	0.000	0.007	21.442	0.075	0.075	0.000	0.000	0.000	0.000
82	A	87	THR	0	0.003	-0.004	25.102	-0.299	-0.299	0.000	0.000	0.000	0.000
83	A	88	SER	0	0.008	-0.001	28.798	0.040	0.040	0.000	0.000	0.000	0.000
84	A	89	SER	0	0.028	0.005	31.340	-0.048	-0.048	0.000	0.000	0.000	0.000
85	A	90	GLN	0	-0.069	-0.027	33.590	-0.245	-0.245	0.000	0.000	0.000	0.000
86	A	91	ASP	-1	-0.805	-0.889	37.068	8.128	8.128	0.000	0.000	0.000	0.000
87	A	92	VAL	0	0.002	-0.029	39.268	-0.153	-0.153	0.000	0.000	0.000	0.000
88	A	93	GLU	-1	-0.903	-0.961	40.477	7.393	7.393	0.000	0.000	0.000	0.000
89	A	94	THR	0	-0.023	-0.013	38.527	-0.055	-0.055	0.000	0.000	0.000	0.000
90	A	95	PHE	0	0.022	0.004	41.083	-0.145	-0.145	0.000	0.000	0.000	0.000
91	A	96	GLN	0	-0.062	-0.025	44.771	-0.318	-0.318	0.000	0.000	0.000	0.000
92	A	97	ARG	1	0.920	0.952	40.288	-7.569	-7.569	0.000	0.000	0.000	0.000
93	A	98	ALA	0	0.025	0.017	44.599	-0.109	-0.109	0.000	0.000	0.000	0.000
94	A	99	LYS	1	0.960	0.980	46.513	-6.213	-6.213	0.000	0.000	0.000	0.000
95	A	100	ARG	1	0.936	0.970	48.285	-6.400	-6.400	0.000	0.000	0.000	0.000
96	A	101	VAL	0	-0.018	0.010	47.097	-0.064	-0.064	0.000	0.000	0.000	0.000
97	A	102	ASN	0	-0.056	-0.023	50.458	-0.065	-0.065	0.000	0.000	0.000	0.000
98	A	103	PRO	0	-0.002	0.019	48.305	-0.061	-0.061	0.000	0.000	0.000	0.000
99	A	104	PHE	0	-0.002	-0.011	50.746	-0.078	-0.078	0.000	0.000	0.000	0.000
100	A	105	GLY	0	0.012	-0.003	49.978	-0.086	-0.086	0.000	0.000	0.000	0.000
101	A	106	TYR	0	-0.019	-0.016	44.540	0.128	0.128	0.000	0.000	0.000	0.000
102	A	107	LEU	0	-0.015	-0.005	44.552	-0.078	-0.078	0.000	0.000	0.000	0.000
103	A	108	ALA	0	0.012	0.011	40.806	0.126	0.126	0.000	0.000	0.000	0.000
104	A	109	LYS	1	0.965	0.998	34.352	-8.736	-8.736	0.000	0.000	0.000	0.000
105	A	110	PRO	0	0.069	0.032	37.117	0.077	0.077	0.000	0.000	0.000	0.000
106	A	111	VAL	0	-0.013	-0.015	38.999	-0.150	-0.150	0.000	0.000	0.000	0.000
107	A	112	ALA	0	0.037	0.028	42.518	0.050	0.050	0.000	0.000	0.000	0.000
108	A	113	ALA	0	0.037	-0.005	44.909	-0.091	-0.091	0.000	0.000	0.000	0.000
109	A	114	ASP	-1	-0.864	-0.939	46.647	6.275	6.275	0.000	0.000	0.000	0.000
110	A	115	THR	0	-0.021	-0.026	47.464	-0.160	-0.160	0.000	0.000	0.000	0.000
111	A	116	LEU	0	0.005	0.030	44.489	-0.089	-0.089	0.000	0.000	0.000	0.000
112	A	117	HIS	0	0.022	0.016	48.052	0.024	0.024	0.000	0.000	0.000	0.000
113	A	118	ARG	1	0.995	1.002	51.159	-5.994	-5.994	0.000	0.000	0.000	0.000
114	A	119	SER	0	-0.030	-0.049	50.162	-0.098	-0.098	0.000	0.000	0.000	0.000
115	A	120	ILE	0	0.003	0.010	48.136	-0.055	-0.055	0.000	0.000	0.000	0.000
116	A	121	GLU	-1	-0.922	-0.952	52.309	5.422	5.422	0.000	0.000	0.000	0.000
117	A	122	MET	0	0.006	-0.004	54.924	-0.122	-0.122	0.000	0.000	0.000	0.000
118	A	123	ALA	0	-0.003	0.012	53.452	-0.083	-0.083	0.000	0.000	0.000	0.000
119	A	124	ILE	0	-0.027	-0.018	53.784	-0.069	-0.069	0.000	0.000	0.000	0.000
120	A	125	HIS	0	-0.053	-0.052	56.921	-0.143	-0.143	0.000	0.000	0.000	0.000
121	A	126	LYS	1	0.907	0.974	57.464	-5.465	-5.465	0.000	0.000	0.000	0.000
122	A	127	LYS	1	0.948	0.969	56.676	-5.523	-5.523	0.000	0.000	0.000	0.000
123	A	128	LYS	1	0.880	0.942	59.437	-5.219	-5.219	0.000	0.000	0.000	0.000
124	A	129	LEU	0	-0.015	0.006	62.404	-0.064	-0.064	0.000	0.000	0.000	0.000
125	A	130	GLU	-1	-0.903	-0.943	60.628	5.120	5.120	0.000	0.000	0.000	0.000
126	A	131	GLU	-1	-1.001	-0.993	61.244	5.034	5.034	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:6:ASP)