FMO DATABASE

FMODB ID: MN1KZ

Calculation Name: 3CO1-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3CO1

Chain ID: A

ChEMBL ID:

UniProt ID: Q9UPY8

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	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	132
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1274080.772956
FMO2-HF: Nuclear repulsion	1219461.406555
FMO2-HF: Total energy	-54619.366401
FMO2-MP2: Total energy	-54776.061062

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:GLY)

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

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.
-0.58	0.745	-0.006	-0.651	-0.666	0.003

Interaction energy analysis for fragmet #1(A:-1:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.032 / q_NPA : 0.013

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	1	MET	0	-0.043	-0.030	3.859	0.041	1.331	-0.005	-0.644	-0.640	0.003
4	A	2	ALA	0	-0.010	-0.002	6.522	0.245	0.245	0.000	0.000	0.000	0.000
5	A	3	VAL	0	0.007	0.016	9.315	0.001	0.001	0.000	0.000	0.000	0.000
6	A	4	ASN	0	-0.026	-0.024	12.308	0.122	0.122	0.000	0.000	0.000	0.000
7	A	5	VAL	0	0.007	0.007	15.148	0.025	0.025	0.000	0.000	0.000	0.000
8	A	6	TYR	0	-0.028	-0.036	17.643	0.026	0.026	0.000	0.000	0.000	0.000
9	A	7	SER	0	-0.023	-0.022	22.037	0.007	0.007	0.000	0.000	0.000	0.000
10	A	8	THR	0	0.009	0.000	24.537	0.013	0.013	0.000	0.000	0.000	0.000
11	A	9	SER	0	-0.002	0.011	20.527	-0.012	-0.012	0.000	0.000	0.000	0.000
12	A	10	VAL	0	0.025	0.017	22.894	0.023	0.023	0.000	0.000	0.000	0.000
13	A	11	THR	0	-0.060	-0.046	21.262	-0.027	-0.027	0.000	0.000	0.000	0.000
14	A	12	SER	0	-0.002	-0.004	23.268	0.018	0.018	0.000	0.000	0.000	0.000
15	A	13	GLU	-1	-0.809	-0.885	25.299	-0.137	-0.137	0.000	0.000	0.000	0.000
16	A	14	ASN	0	-0.037	-0.022	26.753	-0.019	-0.019	0.000	0.000	0.000	0.000
17	A	15	LEU	0	0.046	0.035	25.697	0.008	0.008	0.000	0.000	0.000	0.000
18	A	16	SER	0	-0.003	-0.031	29.355	0.000	0.000	0.000	0.000	0.000	0.000
19	A	17	ARG	1	0.915	0.933	30.626	0.044	0.044	0.000	0.000	0.000	0.000
20	A	18	HIS	0	-0.017	-0.005	31.196	0.008	0.008	0.000	0.000	0.000	0.000
21	A	19	ASP	-1	-0.732	-0.837	29.565	-0.046	-0.046	0.000	0.000	0.000	0.000
22	A	20	MET	0	-0.020	0.018	25.085	0.001	0.001	0.000	0.000	0.000	0.000
23	A	21	LEU	0	-0.043	-0.029	26.173	0.003	0.003	0.000	0.000	0.000	0.000
24	A	22	ALA	0	0.021	0.022	27.624	0.008	0.008	0.000	0.000	0.000	0.000
25	A	23	TRP	0	0.089	0.045	18.811	0.003	0.003	0.000	0.000	0.000	0.000
26	A	24	VAL	0	-0.053	-0.026	22.905	0.008	0.008	0.000	0.000	0.000	0.000
27	A	25	ASN	0	-0.040	-0.018	23.482	0.015	0.015	0.000	0.000	0.000	0.000
28	A	26	ASP	-1	-0.851	-0.933	24.681	0.030	0.030	0.000	0.000	0.000	0.000
29	A	27	SER	0	-0.078	-0.045	19.303	0.012	0.012	0.000	0.000	0.000	0.000
30	A	28	LEU	0	-0.050	-0.035	17.920	0.026	0.026	0.000	0.000	0.000	0.000
31	A	29	HIS	0	-0.007	0.009	21.507	0.013	0.013	0.000	0.000	0.000	0.000
32	A	30	LEU	0	-0.086	-0.025	23.069	0.001	0.001	0.000	0.000	0.000	0.000
33	A	31	ASN	0	0.022	-0.007	26.579	-0.006	-0.006	0.000	0.000	0.000	0.000
34	A	32	TYR	0	-0.066	-0.036	25.904	0.001	0.001	0.000	0.000	0.000	0.000
35	A	33	THR	0	0.049	0.020	30.003	-0.003	-0.003	0.000	0.000	0.000	0.000
36	A	34	LYS	1	0.877	0.921	31.796	0.010	0.010	0.000	0.000	0.000	0.000
37	A	35	ILE	0	0.024	0.034	28.511	0.002	0.002	0.000	0.000	0.000	0.000
38	A	36	GLU	-1	-0.792	-0.917	28.930	-0.045	-0.045	0.000	0.000	0.000	0.000
39	A	37	GLN	0	0.044	0.033	29.394	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	38	LEU	0	0.008	0.015	23.654	0.008	0.008	0.000	0.000	0.000	0.000
41	A	39	CYS	0	-0.058	-0.012	25.225	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	40	SER	0	0.015	-0.011	26.286	0.001	0.001	0.000	0.000	0.000	0.000
43	A	41	GLY	0	0.024	0.019	22.660	0.010	0.010	0.000	0.000	0.000	0.000
44	A	42	ALA	0	-0.014	-0.027	20.869	-0.004	-0.004	0.000	0.000	0.000	0.000
45	A	43	ALA	0	0.027	0.022	20.095	0.014	0.014	0.000	0.000	0.000	0.000
46	A	44	TYR	0	0.053	0.023	18.513	0.003	0.003	0.000	0.000	0.000	0.000
47	A	45	CYS	0	-0.057	-0.020	16.198	-0.020	-0.020	0.000	0.000	0.000	0.000
48	A	46	GLN	0	0.033	0.021	15.087	0.002	0.002	0.000	0.000	0.000	0.000
49	A	47	PHE	0	0.063	0.030	15.166	0.027	0.027	0.000	0.000	0.000	0.000
50	A	48	MET	0	-0.013	-0.003	10.919	-0.019	-0.019	0.000	0.000	0.000	0.000
51	A	49	ASP	-1	-0.844	-0.925	10.574	0.450	0.450	0.000	0.000	0.000	0.000
52	A	50	MET	0	-0.014	0.013	10.707	0.089	0.089	0.000	0.000	0.000	0.000
53	A	51	LEU	0	-0.007	0.023	10.094	0.050	0.050	0.000	0.000	0.000	0.000
54	A	52	PHE	0	0.022	-0.010	5.877	0.012	0.012	0.000	0.000	0.000	0.000
55	A	53	PRO	0	0.074	0.049	6.935	0.062	0.062	0.000	0.000	0.000	0.000
56	A	54	GLY	0	0.012	0.018	7.176	0.383	0.383	0.000	0.000	0.000	0.000
57	A	55	CYS	0	-0.105	-0.039	7.489	-0.055	-0.055	0.000	0.000	0.000	0.000
58	A	56	VAL	0	0.035	0.012	8.885	-0.128	-0.128	0.000	0.000	0.000	0.000
59	A	57	HIS	0	0.011	0.010	12.713	0.053	0.053	0.000	0.000	0.000	0.000
60	A	58	LEU	0	0.079	0.028	14.925	-0.041	-0.041	0.000	0.000	0.000	0.000
61	A	59	ARG	1	0.982	0.989	17.151	-0.364	-0.364	0.000	0.000	0.000	0.000
62	A	60	LYS	1	0.861	0.935	18.330	-0.118	-0.118	0.000	0.000	0.000	0.000
63	A	61	VAL	0	-0.020	0.016	18.795	-0.027	-0.027	0.000	0.000	0.000	0.000
64	A	62	LYS	1	0.881	0.925	21.764	-0.033	-0.033	0.000	0.000	0.000	0.000
65	A	63	PHE	0	0.044	-0.006	19.574	-0.022	-0.022	0.000	0.000	0.000	0.000
66	A	64	GLN	0	-0.014	0.002	25.334	-0.008	-0.008	0.000	0.000	0.000	0.000
67	A	65	ALA	0	-0.009	0.004	27.603	-0.003	-0.003	0.000	0.000	0.000	0.000
68	A	66	LYS	1	0.895	0.941	29.461	-0.036	-0.036	0.000	0.000	0.000	0.000
69	A	67	LEU	0	0.021	0.020	32.054	-0.004	-0.004	0.000	0.000	0.000	0.000
70	A	68	GLU	-1	-0.754	-0.866	31.253	-0.043	-0.043	0.000	0.000	0.000	0.000
71	A	69	HIS	0	0.055	0.020	30.092	-0.009	-0.009	0.000	0.000	0.000	0.000
72	A	70	GLU	-1	-0.807	-0.894	28.323	0.030	0.030	0.000	0.000	0.000	0.000
73	A	71	TYR	0	0.015	0.014	26.542	0.005	0.005	0.000	0.000	0.000	0.000
74	A	72	ILE	0	0.018	0.006	25.386	-0.008	-0.008	0.000	0.000	0.000	0.000
75	A	73	HIS	0	-0.071	-0.039	23.756	-0.019	-0.019	0.000	0.000	0.000	0.000
76	A	74	ASN	0	0.004	-0.013	21.997	0.012	0.012	0.000	0.000	0.000	0.000
77	A	75	PHE	0	0.043	0.010	20.620	-0.007	-0.007	0.000	0.000	0.000	0.000
78	A	76	LYS	1	0.904	0.967	20.596	0.064	0.064	0.000	0.000	0.000	0.000
79	A	77	VAL	0	-0.027	-0.010	17.118	-0.017	-0.017	0.000	0.000	0.000	0.000
80	A	78	LEU	0	0.023	0.015	15.961	-0.008	-0.008	0.000	0.000	0.000	0.000
81	A	79	GLN	0	0.007	-0.001	15.817	-0.027	-0.027	0.000	0.000	0.000	0.000
82	A	80	ALA	0	-0.036	-0.021	15.729	-0.057	-0.057	0.000	0.000	0.000	0.000
83	A	81	ALA	0	0.021	0.011	11.990	-0.048	-0.048	0.000	0.000	0.000	0.000
84	A	82	PHE	0	0.032	-0.004	11.234	-0.116	-0.116	0.000	0.000	0.000	0.000
85	A	83	LYS	1	0.949	0.982	12.365	0.188	0.188	0.000	0.000	0.000	0.000
86	A	84	LYS	1	0.810	0.903	7.101	-0.585	-0.585	0.000	0.000	0.000	0.000
87	A	85	MET	0	0.012	0.015	4.313	-0.007	0.028	-0.001	-0.007	-0.026	0.000
88	A	86	GLY	0	0.023	0.024	8.614	-0.243	-0.243	0.000	0.000	0.000	0.000
89	A	87	VAL	0	-0.032	-0.011	11.472	0.053	0.053	0.000	0.000	0.000	0.000
90	A	88	ASP	-1	-0.844	-0.902	13.768	-0.486	-0.486	0.000	0.000	0.000	0.000
91	A	89	LYS	1	0.840	0.946	17.233	0.320	0.320	0.000	0.000	0.000	0.000
92	A	90	ILE	0	0.024	0.007	19.098	0.015	0.015	0.000	0.000	0.000	0.000
93	A	91	ILE	0	0.019	0.020	18.072	0.018	0.018	0.000	0.000	0.000	0.000
94	A	92	PRO	0	-0.008	0.014	22.246	0.014	0.014	0.000	0.000	0.000	0.000
95	A	93	VAL	0	0.011	-0.018	23.618	0.017	0.017	0.000	0.000	0.000	0.000
96	A	94	GLU	-1	-0.919	-0.962	26.195	-0.080	-0.080	0.000	0.000	0.000	0.000
97	A	95	LYS	1	0.858	0.914	29.498	0.119	0.119	0.000	0.000	0.000	0.000
98	A	96	LEU	0	-0.026	0.005	24.580	0.008	0.008	0.000	0.000	0.000	0.000
99	A	97	VAL	0	-0.008	-0.016	27.525	0.010	0.010	0.000	0.000	0.000	0.000
100	A	98	LYS	1	0.838	0.911	29.780	0.060	0.060	0.000	0.000	0.000	0.000
101	A	99	GLY	0	0.035	0.018	31.736	0.004	0.004	0.000	0.000	0.000	0.000
102	A	100	LYS	1	0.798	0.899	32.828	0.077	0.077	0.000	0.000	0.000	0.000
103	A	101	PHE	0	0.056	0.023	32.138	-0.006	-0.006	0.000	0.000	0.000	0.000
104	A	102	GLN	0	-0.022	-0.014	31.774	0.002	0.002	0.000	0.000	0.000	0.000
105	A	103	ASP	-1	-0.729	-0.847	29.803	-0.096	-0.096	0.000	0.000	0.000	0.000
106	A	104	ASN	0	-0.025	-0.038	27.346	-0.013	-0.013	0.000	0.000	0.000	0.000
107	A	105	PHE	0	-0.009	0.005	26.979	-0.006	-0.006	0.000	0.000	0.000	0.000
108	A	106	GLU	-1	-0.869	-0.934	27.594	-0.128	-0.128	0.000	0.000	0.000	0.000
109	A	107	PHE	0	-0.039	-0.024	19.723	-0.021	-0.021	0.000	0.000	0.000	0.000
110	A	108	ILE	0	0.013	0.001	22.055	-0.018	-0.018	0.000	0.000	0.000	0.000
111	A	109	GLN	0	0.002	-0.019	23.163	-0.015	-0.015	0.000	0.000	0.000	0.000
112	A	110	TRP	0	0.003	-0.015	16.505	0.010	0.010	0.000	0.000	0.000	0.000
113	A	111	PHE	0	0.006	-0.012	15.976	-0.028	-0.028	0.000	0.000	0.000	0.000
114	A	112	LYS	1	0.814	0.899	18.422	0.121	0.121	0.000	0.000	0.000	0.000
115	A	113	LYS	1	0.867	0.944	19.335	0.173	0.173	0.000	0.000	0.000	0.000
116	A	114	PHE	0	-0.019	-0.005	12.037	-0.021	-0.021	0.000	0.000	0.000	0.000
117	A	115	PHE	0	0.048	0.011	14.835	-0.062	-0.062	0.000	0.000	0.000	0.000
118	A	116	ASP	-1	-0.813	-0.897	15.049	-0.183	-0.183	0.000	0.000	0.000	0.000
119	A	117	ALA	0	-0.047	-0.012	15.397	0.000	0.000	0.000	0.000	0.000	0.000
120	A	118	ASN	0	-0.061	-0.057	10.660	-0.305	-0.305	0.000	0.000	0.000	0.000
121	A	119	TYR	0	-0.047	-0.033	10.684	-0.025	-0.025	0.000	0.000	0.000	0.000
122	A	120	ASP	-1	-0.821	-0.897	9.375	0.226	0.226	0.000	0.000	0.000	0.000
123	A	121	GLY	0	0.013	0.010	11.850	0.037	0.037	0.000	0.000	0.000	0.000
124	A	122	LYS	1	0.697	0.847	8.784	-0.231	-0.231	0.000	0.000	0.000	0.000
125	A	123	ASP	-1	-0.865	-0.919	13.797	0.211	0.211	0.000	0.000	0.000	0.000
126	A	124	TYR	0	-0.058	-0.063	13.996	0.027	0.027	0.000	0.000	0.000	0.000
127	A	125	ASN	0	0.046	0.019	16.586	-0.057	-0.057	0.000	0.000	0.000	0.000
128	A	126	PRO	0	0.031	0.015	18.794	0.025	0.025	0.000	0.000	0.000	0.000
129	A	127	LEU	0	0.047	0.008	20.242	-0.012	-0.012	0.000	0.000	0.000	0.000
130	A	128	LEU	0	-0.014	0.011	16.947	-0.005	-0.005	0.000	0.000	0.000	0.000
131	A	129	ALA	0	-0.039	-0.008	17.797	0.016	0.016	0.000	0.000	0.000	0.000
132	A	130	ARG	1	0.808	0.898	19.245	-0.148	-0.148	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

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