FMO DATABASE

FMODB ID: 895RY

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	OptHSide
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	-875877.045946
FMO2-HF: Nuclear repulsion	827875.047334
FMO2-HF: Total energy	-48001.998611
FMO2-MP2: Total energy	-48140.725601

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.
98.891	100.705	-0.016	-0.741	-1.056	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 : -0.986 / q_NPA : -0.998

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	0.004	0.013	3.821	-2.252	-0.438	-0.016	-0.741	-1.056	0.003
4	A	9	GLY	0	0.049	0.018	6.481	-1.319	-1.319	0.000	0.000	0.000	0.000
5	A	10	VAL	0	-0.042	-0.026	8.682	-1.777	-1.777	0.000	0.000	0.000	0.000
6	A	11	LEU	0	0.003	0.018	12.317	-0.228	-0.228	0.000	0.000	0.000	0.000
7	A	12	ILE	0	-0.017	-0.016	15.466	-0.451	-0.451	0.000	0.000	0.000	0.000
8	A	13	VAL	0	-0.007	-0.006	18.623	-0.250	-0.250	0.000	0.000	0.000	0.000
9	A	14	GLU	-1	-0.843	-0.928	22.198	11.156	11.156	0.000	0.000	0.000	0.000
10	A	15	ASP	-1	-0.842	-0.915	24.490	9.751	9.751	0.000	0.000	0.000	0.000
11	A	16	GLY	0	-0.038	-0.014	27.575	-0.267	-0.267	0.000	0.000	0.000	0.000
12	A	17	ARG	1	0.972	0.963	26.541	-9.399	-9.399	0.000	0.000	0.000	0.000
13	A	18	LEU	0	-0.005	-0.002	26.304	0.272	0.272	0.000	0.000	0.000	0.000
14	A	19	ALA	0	0.046	0.041	25.181	0.301	0.301	0.000	0.000	0.000	0.000
15	A	20	ALA	0	0.074	0.038	22.354	0.520	0.520	0.000	0.000	0.000	0.000
16	A	21	ALA	0	-0.037	-0.016	21.209	0.633	0.633	0.000	0.000	0.000	0.000
17	A	22	THR	0	-0.055	-0.050	21.288	0.360	0.360	0.000	0.000	0.000	0.000
18	A	23	LEU	0	0.025	0.011	19.036	0.485	0.485	0.000	0.000	0.000	0.000
19	A	24	ARG	1	0.840	0.923	14.425	-17.328	-17.328	0.000	0.000	0.000	0.000
20	A	25	ILE	0	0.013	0.010	16.137	0.852	0.852	0.000	0.000	0.000	0.000
21	A	26	GLN	0	-0.014	-0.012	16.690	0.671	0.671	0.000	0.000	0.000	0.000
22	A	27	LEU	0	0.013	0.010	13.301	0.610	0.610	0.000	0.000	0.000	0.000
23	A	28	GLU	-1	-0.797	-0.899	11.939	20.020	20.020	0.000	0.000	0.000	0.000
24	A	29	SER	0	-0.107	-0.054	11.956	0.646	0.646	0.000	0.000	0.000	0.000
25	A	30	LEU	0	-0.100	-0.058	12.596	0.503	0.503	0.000	0.000	0.000	0.000
26	A	31	GLY	0	-0.015	0.018	8.625	0.742	0.742	0.000	0.000	0.000	0.000
27	A	32	TYR	0	-0.053	-0.028	7.611	2.562	2.562	0.000	0.000	0.000	0.000
28	A	33	ASP	-1	-0.897	-0.946	7.064	28.822	28.822	0.000	0.000	0.000	0.000
29	A	34	VAL	0	-0.045	-0.022	9.008	-1.376	-1.376	0.000	0.000	0.000	0.000
30	A	35	LEU	0	0.030	0.022	9.153	-0.631	-0.631	0.000	0.000	0.000	0.000
31	A	36	GLY	0	-0.033	-0.019	12.965	-0.700	-0.700	0.000	0.000	0.000	0.000
32	A	37	VAL	0	-0.063	-0.032	16.751	0.165	0.165	0.000	0.000	0.000	0.000
33	A	38	PHE	0	-0.008	-0.007	18.057	-0.310	-0.310	0.000	0.000	0.000	0.000
34	A	39	ASP	-1	-0.863	-0.923	22.685	11.007	11.007	0.000	0.000	0.000	0.000
35	A	40	ASN	0	-0.024	-0.034	25.657	-0.386	-0.386	0.000	0.000	0.000	0.000
36	A	41	GLY	0	0.104	0.035	25.311	0.459	0.459	0.000	0.000	0.000	0.000
37	A	42	GLU	-1	-0.858	-0.934	25.267	10.296	10.296	0.000	0.000	0.000	0.000
38	A	43	GLU	-1	-0.822	-0.910	24.166	11.964	11.964	0.000	0.000	0.000	0.000
39	A	44	ALA	0	0.006	0.025	21.283	0.515	0.515	0.000	0.000	0.000	0.000
40	A	45	VAL	0	-0.026	-0.026	20.795	0.536	0.536	0.000	0.000	0.000	0.000
41	A	46	ARG	1	0.793	0.878	22.237	-11.272	-11.272	0.000	0.000	0.000	0.000
42	A	47	CYS	0	-0.032	-0.015	19.285	0.158	0.158	0.000	0.000	0.000	0.000
43	A	48	ALA	0	0.040	0.024	17.082	0.825	0.825	0.000	0.000	0.000	0.000
44	A	49	PRO	0	0.003	-0.008	16.026	1.111	1.111	0.000	0.000	0.000	0.000
45	A	50	ASP	-1	-0.909	-0.950	16.071	16.158	16.158	0.000	0.000	0.000	0.000
46	A	51	LEU	0	-0.068	-0.022	13.731	1.113	1.113	0.000	0.000	0.000	0.000
47	A	52	ARG	1	0.809	0.902	10.628	-21.872	-21.872	0.000	0.000	0.000	0.000
48	A	53	PRO	0	-0.003	0.002	10.455	1.694	1.694	0.000	0.000	0.000	0.000
49	A	54	ASP	-1	-0.845	-0.910	7.669	30.200	30.200	0.000	0.000	0.000	0.000
50	A	55	ILE	0	-0.075	-0.050	11.115	-1.293	-1.293	0.000	0.000	0.000	0.000
51	A	56	ALA	0	0.021	0.019	14.112	0.180	0.180	0.000	0.000	0.000	0.000
52	A	57	LEU	0	-0.034	-0.014	16.646	-0.497	-0.497	0.000	0.000	0.000	0.000
53	A	58	VAL	0	0.012	-0.002	19.313	-0.097	-0.097	0.000	0.000	0.000	0.000
54	A	59	ASP	-1	-0.819	-0.900	22.735	10.356	10.356	0.000	0.000	0.000	0.000
55	A	60	ILE	0	-0.035	-0.023	25.912	-0.149	-0.149	0.000	0.000	0.000	0.000
56	A	61	MET	0	-0.133	-0.061	28.784	-0.540	-0.540	0.000	0.000	0.000	0.000
57	A	62	LEU	0	0.008	0.001	26.738	0.125	0.125	0.000	0.000	0.000	0.000
58	A	63	CYS	0	-0.089	-0.053	30.500	-0.403	-0.403	0.000	0.000	0.000	0.000
59	A	64	GLY	0	0.047	0.023	31.138	0.280	0.280	0.000	0.000	0.000	0.000
60	A	65	ALA	0	-0.082	-0.044	32.368	-0.233	-0.233	0.000	0.000	0.000	0.000
61	A	66	LEU	0	-0.048	-0.020	27.836	-0.214	-0.214	0.000	0.000	0.000	0.000
62	A	67	ASP	-1	-0.767	-0.878	30.581	9.593	9.593	0.000	0.000	0.000	0.000
63	A	68	GLY	0	0.051	0.032	27.712	0.294	0.294	0.000	0.000	0.000	0.000
64	A	69	VAL	0	-0.033	-0.027	27.063	0.439	0.439	0.000	0.000	0.000	0.000
65	A	70	GLU	-1	-0.811	-0.882	28.285	9.969	9.969	0.000	0.000	0.000	0.000
66	A	71	THR	0	-0.044	-0.035	24.077	0.256	0.256	0.000	0.000	0.000	0.000
67	A	72	ALA	0	0.014	0.006	23.482	0.463	0.463	0.000	0.000	0.000	0.000
68	A	73	ALA	0	-0.022	-0.003	23.901	0.378	0.378	0.000	0.000	0.000	0.000
69	A	74	ARG	1	0.813	0.875	25.435	-9.886	-9.886	0.000	0.000	0.000	0.000
70	A	75	LEU	0	0.001	0.001	19.376	0.289	0.289	0.000	0.000	0.000	0.000
71	A	76	ALA	0	0.007	0.005	20.238	0.646	0.646	0.000	0.000	0.000	0.000
72	A	77	ALA	0	-0.066	-0.020	21.986	0.117	0.117	0.000	0.000	0.000	0.000
73	A	78	GLY	0	-0.036	-0.021	22.833	0.101	0.101	0.000	0.000	0.000	0.000
74	A	79	CYS	0	-0.053	-0.031	17.620	0.116	0.116	0.000	0.000	0.000	0.000
75	A	80	ASN	0	-0.056	-0.008	16.680	0.206	0.206	0.000	0.000	0.000	0.000
76	A	81	LEU	0	0.049	0.027	14.625	0.745	0.745	0.000	0.000	0.000	0.000
77	A	82	PRO	0	-0.007	0.005	14.993	-1.047	-1.047	0.000	0.000	0.000	0.000
78	A	83	ILE	0	-0.021	-0.016	17.753	0.305	0.305	0.000	0.000	0.000	0.000
79	A	84	ILE	0	-0.021	-0.002	17.865	-0.319	-0.319	0.000	0.000	0.000	0.000
80	A	85	PHE	0	-0.014	-0.016	21.188	0.089	0.089	0.000	0.000	0.000	0.000
81	A	86	ILE	0	-0.015	0.000	21.509	0.063	0.063	0.000	0.000	0.000	0.000
82	A	87	THR	0	0.040	0.010	25.102	-0.312	-0.312	0.000	0.000	0.000	0.000
83	A	88	SER	0	-0.012	-0.006	28.798	-0.033	-0.033	0.000	0.000	0.000	0.000
84	A	89	SER	0	0.015	0.000	31.670	-0.013	-0.013	0.000	0.000	0.000	0.000
85	A	90	GLN	0	-0.045	-0.018	33.590	-0.212	-0.212	0.000	0.000	0.000	0.000
86	A	91	ASP	-1	-0.806	-0.893	36.759	8.109	8.109	0.000	0.000	0.000	0.000
87	A	92	VAL	0	0.011	-0.020	39.268	-0.150	-0.150	0.000	0.000	0.000	0.000
88	A	93	GLU	-1	-0.902	-0.961	41.171	7.305	7.305	0.000	0.000	0.000	0.000
89	A	94	THR	0	-0.025	-0.023	38.753	-0.057	-0.057	0.000	0.000	0.000	0.000
90	A	95	PHE	0	0.014	0.005	40.989	-0.147	-0.147	0.000	0.000	0.000	0.000
91	A	96	GLN	0	-0.045	-0.005	44.771	-0.343	-0.343	0.000	0.000	0.000	0.000
92	A	97	ARG	1	0.926	0.955	40.087	-7.583	-7.583	0.000	0.000	0.000	0.000
93	A	98	ALA	0	0.023	0.019	44.576	-0.110	-0.110	0.000	0.000	0.000	0.000
94	A	99	LYS	1	0.929	0.955	46.513	-6.246	-6.246	0.000	0.000	0.000	0.000
95	A	100	ARG	1	0.933	0.970	48.795	-6.389	-6.389	0.000	0.000	0.000	0.000
96	A	101	VAL	0	-0.014	0.005	47.042	-0.067	-0.067	0.000	0.000	0.000	0.000
97	A	102	ASN	0	-0.067	-0.025	50.458	-0.116	-0.116	0.000	0.000	0.000	0.000
98	A	103	PRO	0	0.003	0.021	48.177	-0.058	-0.058	0.000	0.000	0.000	0.000
99	A	104	PHE	0	0.008	-0.002	50.746	-0.076	-0.076	0.000	0.000	0.000	0.000
100	A	105	GLY	0	0.010	-0.003	49.975	-0.086	-0.086	0.000	0.000	0.000	0.000
101	A	106	TYR	0	-0.024	-0.018	44.716	0.128	0.128	0.000	0.000	0.000	0.000
102	A	107	LEU	0	-0.013	-0.005	44.556	-0.078	-0.078	0.000	0.000	0.000	0.000
103	A	108	ALA	0	0.016	0.013	40.833	0.126	0.126	0.000	0.000	0.000	0.000
104	A	109	LYS	1	0.907	0.978	33.227	-9.054	-9.054	0.000	0.000	0.000	0.000
105	A	110	PRO	0	0.045	0.022	37.081	0.082	0.082	0.000	0.000	0.000	0.000
106	A	111	VAL	0	0.003	-0.010	38.984	-0.150	-0.150	0.000	0.000	0.000	0.000
107	A	112	ALA	0	0.037	0.031	42.503	0.046	0.046	0.000	0.000	0.000	0.000
108	A	113	ALA	0	0.041	-0.005	44.893	-0.100	-0.100	0.000	0.000	0.000	0.000
109	A	114	ASP	-1	-0.808	-0.901	46.629	6.241	6.241	0.000	0.000	0.000	0.000
110	A	115	THR	0	0.014	-0.010	47.424	-0.154	-0.154	0.000	0.000	0.000	0.000
111	A	116	LEU	0	-0.010	0.007	44.443	-0.086	-0.086	0.000	0.000	0.000	0.000
112	A	117	HIS	0	-0.017	-0.007	48.035	0.045	0.045	0.000	0.000	0.000	0.000
113	A	118	ARG	1	0.893	0.941	51.007	-6.065	-6.065	0.000	0.000	0.000	0.000
114	A	119	SER	0	-0.027	-0.032	50.103	-0.106	-0.106	0.000	0.000	0.000	0.000
115	A	120	ILE	0	0.004	0.009	48.004	-0.055	-0.055	0.000	0.000	0.000	0.000
116	A	121	GLU	-1	-0.872	-0.930	52.289	5.457	5.457	0.000	0.000	0.000	0.000
117	A	122	MET	0	-0.004	-0.006	54.771	-0.137	-0.137	0.000	0.000	0.000	0.000
118	A	123	ALA	0	0.002	0.013	53.406	-0.086	-0.086	0.000	0.000	0.000	0.000
119	A	124	ILE	0	-0.031	-0.021	53.634	-0.071	-0.071	0.000	0.000	0.000	0.000
120	A	125	HIS	0	-0.040	-0.049	56.900	-0.145	-0.145	0.000	0.000	0.000	0.000
121	A	126	LYS	1	0.843	0.918	57.795	-5.453	-5.453	0.000	0.000	0.000	0.000
122	A	127	LYS	1	0.928	0.954	57.011	-5.463	-5.463	0.000	0.000	0.000	0.000
123	A	128	LYS	1	0.874	0.938	59.437	-5.223	-5.223	0.000	0.000	0.000	0.000
124	A	129	LEU	0	-0.017	0.008	62.385	-0.065	-0.065	0.000	0.000	0.000	0.000
125	A	130	GLU	-1	-0.837	-0.884	60.252	5.176	5.176	0.000	0.000	0.000	0.000
126	A	131	GLU	-1	-0.978	-0.978	61.192	5.044	5.044	0.000	0.000	0.000	0.000

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