FMO DATABASE

FMODB ID: MN59Z

Calculation Name: 2CXC-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2CXC

Chain ID: A

ChEMBL ID:

UniProt ID: Q9YAU4

Base Structure: X-ray

Registration Date: 2023-09-24

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	138
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1213552.496791
FMO2-HF: Nuclear repulsion	1161034.898971
FMO2-HF: Total energy	-52517.59782
FMO2-MP2: Total energy	-52674.945437

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:7:ILE)

Summations of interaction energy for fragment #1(A:7:ILE)

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.
-8.204	-2.092	2.424	-3.549	-4.987	-0.025

Interaction energy analysis for fragmet #1(A:7:ILE)

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 : -0.016

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	9	LEU	0	0.108	0.034	3.825	0.186	1.980	-0.007	-0.911	-0.876	0.005
4	A	10	GLU	-1	-0.894	-0.934	6.683	0.131	0.131	0.000	0.000	0.000	0.000
5	A	11	GLU	-1	-0.762	-0.894	2.393	-7.016	-4.354	1.693	-2.116	-2.239	-0.027
6	A	12	LEU	0	0.026	0.016	4.522	0.191	0.441	-0.001	-0.029	-0.220	0.000
7	A	13	ARG	1	0.960	0.989	5.955	-0.602	-0.602	0.000	0.000	0.000	0.000
8	A	14	TYR	0	-0.045	-0.046	7.672	-0.062	-0.062	0.000	0.000	0.000	0.000
9	A	15	ILE	0	-0.009	0.001	5.191	-0.156	-0.156	0.000	0.000	0.000	0.000
10	A	16	SER	0	-0.010	0.002	8.981	-0.168	-0.168	0.000	0.000	0.000	0.000
11	A	17	VAL	0	0.004	-0.004	11.601	-0.097	-0.097	0.000	0.000	0.000	0.000
12	A	18	PHE	0	0.011	-0.004	12.069	-0.065	-0.065	0.000	0.000	0.000	0.000
13	A	19	HIS	0	0.005	0.011	13.316	-0.040	-0.040	0.000	0.000	0.000	0.000
14	A	20	SER	0	-0.018	0.005	15.169	-0.054	-0.054	0.000	0.000	0.000	0.000
15	A	21	ILE	0	-0.043	-0.016	17.156	-0.032	-0.032	0.000	0.000	0.000	0.000
16	A	22	THR	0	-0.047	-0.043	16.628	-0.022	-0.022	0.000	0.000	0.000	0.000
17	A	23	GLY	0	0.016	0.027	18.283	-0.020	-0.020	0.000	0.000	0.000	0.000
18	A	24	VAL	0	-0.080	-0.039	15.608	-0.006	-0.006	0.000	0.000	0.000	0.000
19	A	25	THR	0	0.017	-0.004	11.464	0.028	0.028	0.000	0.000	0.000	0.000
20	A	26	ALA	0	-0.034	-0.009	9.964	-0.057	-0.057	0.000	0.000	0.000	0.000
21	A	27	TYR	0	-0.024	-0.002	7.784	0.153	0.153	0.000	0.000	0.000	0.000
22	A	28	ARG	1	0.847	0.895	2.782	-0.459	0.947	0.739	-0.493	-1.652	-0.003
23	A	29	CYS	0	-0.017	0.004	5.532	0.038	0.038	0.000	0.000	0.000	0.000
24	A	30	ILE	0	-0.016	-0.009	6.107	-0.239	-0.239	0.000	0.000	0.000	0.000
25	A	31	VAL	0	0.063	0.026	7.317	0.103	0.103	0.000	0.000	0.000	0.000
26	A	32	ASP	-1	-0.785	-0.897	9.548	-0.097	-0.097	0.000	0.000	0.000	0.000
27	A	33	GLU	-1	-0.813	-0.932	12.479	-0.071	-0.071	0.000	0.000	0.000	0.000
28	A	34	GLU	-1	-0.940	-0.945	14.799	-0.046	-0.046	0.000	0.000	0.000	0.000
29	A	35	ASN	0	-0.096	-0.054	17.018	0.019	0.019	0.000	0.000	0.000	0.000
30	A	36	ASN	0	0.014	0.011	16.586	0.007	0.007	0.000	0.000	0.000	0.000
31	A	37	ARG	1	0.707	0.831	14.938	0.048	0.048	0.000	0.000	0.000	0.000
32	A	38	LEU	0	0.016	0.019	9.991	-0.025	-0.025	0.000	0.000	0.000	0.000
33	A	39	ILE	0	-0.039	-0.020	11.258	0.024	0.024	0.000	0.000	0.000	0.000
34	A	40	PHE	0	0.021	0.004	10.034	-0.033	-0.033	0.000	0.000	0.000	0.000
35	A	41	LEU	0	-0.029	-0.013	9.101	-0.032	-0.032	0.000	0.000	0.000	0.000
36	A	42	VAL	0	0.024	0.004	11.134	0.069	0.069	0.000	0.000	0.000	0.000
37	A	43	SER	0	0.045	0.015	13.808	-0.031	-0.031	0.000	0.000	0.000	0.000
38	A	44	GLU	-1	-0.814	-0.912	15.852	0.043	0.043	0.000	0.000	0.000	0.000
39	A	45	GLY	0	-0.022	-0.011	19.166	0.006	0.006	0.000	0.000	0.000	0.000
40	A	46	GLU	-1	-0.848	-0.927	17.589	0.144	0.144	0.000	0.000	0.000	0.000
41	A	47	ALA	0	-0.014	-0.007	18.991	0.008	0.008	0.000	0.000	0.000	0.000
42	A	48	GLY	0	-0.017	-0.011	19.924	0.000	0.000	0.000	0.000	0.000	0.000
43	A	49	ARG	1	0.865	0.922	20.075	-0.146	-0.146	0.000	0.000	0.000	0.000
44	A	50	ALA	0	0.012	0.013	17.651	0.004	0.004	0.000	0.000	0.000	0.000
45	A	51	ILE	0	0.003	0.023	19.560	-0.001	-0.001	0.000	0.000	0.000	0.000
46	A	52	GLY	0	0.070	0.029	21.913	-0.002	-0.002	0.000	0.000	0.000	0.000
47	A	53	ARG	1	0.971	0.971	24.853	-0.057	-0.057	0.000	0.000	0.000	0.000
48	A	54	GLY	0	0.022	0.004	28.162	0.001	0.001	0.000	0.000	0.000	0.000
49	A	55	GLY	0	0.022	0.010	24.613	-0.003	-0.003	0.000	0.000	0.000	0.000
50	A	56	ARG	1	0.918	0.950	24.418	-0.075	-0.075	0.000	0.000	0.000	0.000
51	A	57	LEU	0	0.015	0.009	20.737	-0.002	-0.002	0.000	0.000	0.000	0.000
52	A	58	ILE	0	0.019	0.030	19.044	0.009	0.009	0.000	0.000	0.000	0.000
53	A	59	LYS	1	0.902	0.945	20.490	-0.050	-0.050	0.000	0.000	0.000	0.000
54	A	60	LEU	0	0.038	0.016	21.904	-0.003	-0.003	0.000	0.000	0.000	0.000
55	A	61	LEU	0	0.018	0.032	15.451	0.005	0.005	0.000	0.000	0.000	0.000
56	A	62	ARG	1	0.934	0.980	17.671	-0.044	-0.044	0.000	0.000	0.000	0.000
57	A	63	GLU	-1	-1.010	-0.994	19.547	0.062	0.062	0.000	0.000	0.000	0.000
58	A	64	ALA	0	-0.001	-0.006	17.958	-0.002	-0.002	0.000	0.000	0.000	0.000
59	A	65	LEU	0	-0.084	-0.060	12.546	0.008	0.008	0.000	0.000	0.000	0.000
60	A	66	GLY	0	0.025	0.034	16.171	-0.014	-0.014	0.000	0.000	0.000	0.000
61	A	67	LYS	1	0.860	0.937	13.118	0.017	0.017	0.000	0.000	0.000	0.000
62	A	68	ASN	0	-0.045	-0.031	17.354	0.018	0.018	0.000	0.000	0.000	0.000
63	A	69	ILE	0	0.000	-0.002	14.950	-0.002	-0.002	0.000	0.000	0.000	0.000
64	A	70	GLU	-1	-0.848	-0.917	15.306	-0.008	-0.008	0.000	0.000	0.000	0.000
65	A	71	VAL	0	0.006	0.010	14.753	0.011	0.011	0.000	0.000	0.000	0.000
66	A	72	VAL	0	-0.031	-0.016	14.836	-0.015	-0.015	0.000	0.000	0.000	0.000
67	A	73	GLU	-1	-0.806	-0.885	14.691	0.082	0.082	0.000	0.000	0.000	0.000
68	A	74	TYR	0	0.011	-0.016	10.779	-0.017	-0.017	0.000	0.000	0.000	0.000
69	A	75	SER	0	0.013	-0.003	14.286	0.010	0.010	0.000	0.000	0.000	0.000
70	A	76	SER	0	0.023	0.016	13.730	-0.009	-0.009	0.000	0.000	0.000	0.000
71	A	77	ASP	-1	-0.831	-0.910	14.757	-0.013	-0.013	0.000	0.000	0.000	0.000
72	A	78	LEU	0	0.037	-0.004	15.631	0.002	0.002	0.000	0.000	0.000	0.000
73	A	79	GLU	-1	-0.884	-0.952	17.645	-0.003	-0.003	0.000	0.000	0.000	0.000
74	A	80	ARG	1	0.849	0.921	19.343	-0.030	-0.030	0.000	0.000	0.000	0.000
75	A	81	ILE	0	0.000	-0.003	13.520	0.002	0.002	0.000	0.000	0.000	0.000
76	A	82	VAL	0	-0.034	-0.013	17.779	-0.002	-0.002	0.000	0.000	0.000	0.000
77	A	83	LYS	1	0.936	0.958	19.569	-0.003	-0.003	0.000	0.000	0.000	0.000
78	A	84	ASN	0	-0.021	0.002	18.363	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	85	LEU	0	-0.060	-0.023	15.412	0.002	0.002	0.000	0.000	0.000	0.000
80	A	86	PHE	0	-0.096	-0.026	19.429	-0.004	-0.004	0.000	0.000	0.000	0.000
81	A	87	PRO	0	0.061	0.024	22.179	0.000	0.000	0.000	0.000	0.000	0.000
82	A	88	GLY	0	-0.026	0.004	24.987	0.001	0.001	0.000	0.000	0.000	0.000
83	A	89	VAL	0	-0.030	-0.018	26.726	-0.002	-0.002	0.000	0.000	0.000	0.000
84	A	90	LYS	1	0.983	1.015	28.392	0.001	0.001	0.000	0.000	0.000	0.000
85	A	91	ILE	0	-0.048	-0.039	23.845	-0.003	-0.003	0.000	0.000	0.000	0.000
86	A	92	GLU	-1	-0.893	-0.956	28.007	-0.007	-0.007	0.000	0.000	0.000	0.000
87	A	93	SER	0	0.021	0.003	27.700	0.001	0.001	0.000	0.000	0.000	0.000
88	A	94	ILE	0	0.020	0.016	20.930	-0.002	-0.002	0.000	0.000	0.000	0.000
89	A	95	ASN	0	-0.030	-0.016	23.776	-0.002	-0.002	0.000	0.000	0.000	0.000
90	A	96	VAL	0	0.066	0.033	18.366	-0.002	-0.002	0.000	0.000	0.000	0.000
91	A	97	ARG	1	0.912	0.960	21.451	0.033	0.033	0.000	0.000	0.000	0.000
92	A	98	GLU	-1	-0.842	-0.941	17.417	-0.064	-0.064	0.000	0.000	0.000	0.000
93	A	99	ARG	1	0.925	0.959	20.868	0.047	0.047	0.000	0.000	0.000	0.000
94	A	100	ASN	0	-0.009	-0.007	21.475	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	101	GLY	0	0.064	0.042	17.539	-0.004	-0.004	0.000	0.000	0.000	0.000
96	A	102	VAL	0	-0.021	0.006	16.262	-0.005	-0.005	0.000	0.000	0.000	0.000
97	A	103	LYS	1	0.977	0.997	13.341	0.080	0.080	0.000	0.000	0.000	0.000
98	A	104	GLN	0	-0.034	-0.033	17.242	-0.004	-0.004	0.000	0.000	0.000	0.000
99	A	105	VAL	0	0.013	0.005	17.323	0.004	0.004	0.000	0.000	0.000	0.000
100	A	106	VAL	0	-0.062	-0.046	20.304	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	107	ILE	0	0.035	0.014	20.760	0.001	0.001	0.000	0.000	0.000	0.000
102	A	108	LYS	1	0.861	0.930	24.777	0.009	0.009	0.000	0.000	0.000	0.000
103	A	109	VAL	0	-0.020	-0.004	27.116	0.002	0.002	0.000	0.000	0.000	0.000
104	A	110	SER	0	0.039	0.013	29.842	-0.001	-0.001	0.000	0.000	0.000	0.000
105	A	111	GLU	-1	-0.950	-0.982	33.253	-0.007	-0.007	0.000	0.000	0.000	0.000
106	A	112	ASP	-1	-0.916	-0.948	34.675	-0.008	-0.008	0.000	0.000	0.000	0.000
107	A	113	ASP	-1	-0.812	-0.912	30.275	-0.001	-0.001	0.000	0.000	0.000	0.000
108	A	114	LYS	1	0.867	0.910	29.317	0.014	0.014	0.000	0.000	0.000	0.000
109	A	115	GLY	0	0.069	0.042	29.430	-0.002	-0.002	0.000	0.000	0.000	0.000
110	A	116	ALA	0	-0.002	-0.012	27.778	-0.001	-0.001	0.000	0.000	0.000	0.000
111	A	117	ALA	0	-0.005	0.004	25.583	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	118	ILE	0	0.050	0.004	24.202	-0.004	-0.004	0.000	0.000	0.000	0.000
113	A	119	GLY	0	0.026	0.017	24.106	-0.003	-0.003	0.000	0.000	0.000	0.000
114	A	120	LYS	1	0.938	0.946	25.304	0.003	0.003	0.000	0.000	0.000	0.000
115	A	121	GLY	0	0.072	0.048	25.096	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	122	GLY	0	0.013	0.021	23.411	-0.004	-0.004	0.000	0.000	0.000	0.000
117	A	123	LYS	1	0.999	0.988	20.609	0.001	0.001	0.000	0.000	0.000	0.000
118	A	124	ASN	0	-0.012	0.014	19.699	0.000	0.000	0.000	0.000	0.000	0.000
119	A	125	VAL	0	0.032	0.015	19.683	-0.004	-0.004	0.000	0.000	0.000	0.000
120	A	126	LYS	1	0.839	0.935	15.510	0.079	0.079	0.000	0.000	0.000	0.000
121	A	127	ARG	1	0.871	0.925	15.348	-0.012	-0.012	0.000	0.000	0.000	0.000
122	A	128	ALA	0	0.000	0.007	14.826	-0.008	-0.008	0.000	0.000	0.000	0.000
123	A	129	ARG	1	0.853	0.927	14.712	0.047	0.047	0.000	0.000	0.000	0.000
124	A	130	LEU	0	0.006	0.007	10.984	-0.008	-0.008	0.000	0.000	0.000	0.000
125	A	131	VAL	0	0.041	0.019	10.256	-0.025	-0.025	0.000	0.000	0.000	0.000
126	A	132	LEU	0	-0.009	-0.019	10.397	-0.006	-0.006	0.000	0.000	0.000	0.000
127	A	133	SER	0	-0.050	-0.029	10.060	-0.008	-0.008	0.000	0.000	0.000	0.000
128	A	134	LYS	1	0.868	0.938	5.733	0.194	0.194	0.000	0.000	0.000	0.000
129	A	135	LEU	0	-0.050	-0.021	5.877	-0.004	-0.004	0.000	0.000	0.000	0.000
130	A	136	PHE	0	-0.023	-0.011	8.159	0.007	0.007	0.000	0.000	0.000	0.000
131	A	137	GLY	0	0.005	0.013	9.529	0.005	0.005	0.000	0.000	0.000	0.000
132	A	138	VAL	0	-0.062	-0.021	10.719	0.005	0.005	0.000	0.000	0.000	0.000
133	A	139	GLU	-1	-0.777	-0.878	11.676	-0.114	-0.114	0.000	0.000	0.000	0.000
134	A	140	LYS	1	0.857	0.943	14.893	0.054	0.054	0.000	0.000	0.000	0.000
135	A	141	VAL	0	0.037	0.022	17.099	0.002	0.002	0.000	0.000	0.000	0.000
136	A	142	VAL	0	-0.031	-0.025	19.789	0.000	0.000	0.000	0.000	0.000	0.000
137	A	143	ILE	0	0.048	0.041	23.051	0.001	0.001	0.000	0.000	0.000	0.000
138	A	144	ARG	1	0.950	0.995	25.877	0.029	0.029	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:7:ILE)