FMO DATABASE

FMODB ID: 5JNMZ

Calculation Name: 2CX3-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2CX3

Chain ID: A

ChEMBL ID:

UniProt ID: Q9YA14

Base Structure: X-ray

Registration Date: 2023-09-22

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	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	159
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1668519.992592
FMO2-HF: Nuclear repulsion	1604791.43522
FMO2-HF: Total energy	-63728.557372
FMO2-MP2: Total energy	-63915.65268

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:4:LEU)

Summations of interaction energy for fragment #1(A:4:LEU)

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.
-11.182	-4.757	3.409	-3.871	-5.96	-0.009

Interaction energy analysis for fragmet #1(A:4:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.017 / q_NPA : -0.008

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	6	GLU	-1	-0.833	-0.910	2.982	-3.000	0.491	0.608	-1.641	-2.458	-0.001
4	A	7	LEU	0	0.016	0.010	4.565	0.097	0.147	-0.001	-0.010	-0.038	0.000
5	A	8	GLY	0	-0.031	0.007	7.891	-0.143	-0.143	0.000	0.000	0.000	0.000
6	A	9	GLU	-1	-0.897	-0.960	3.933	-5.523	-5.233	0.002	-0.154	-0.138	-0.001
7	A	10	LYS	1	0.879	0.930	8.130	1.157	1.157	0.000	0.000	0.000	0.000
8	A	11	ALA	0	0.008	0.001	8.687	-0.430	-0.430	0.000	0.000	0.000	0.000
9	A	12	PRO	0	0.016	0.021	5.332	0.388	0.388	0.000	0.000	0.000	0.000
10	A	13	ASP	-1	-0.759	-0.850	8.592	-0.346	-0.346	0.000	0.000	0.000	0.000
11	A	14	PHE	0	-0.017	-0.023	10.555	0.015	0.015	0.000	0.000	0.000	0.000
12	A	15	THR	0	0.014	-0.002	12.876	-0.012	-0.012	0.000	0.000	0.000	0.000
13	A	16	LEU	0	-0.044	0.002	13.814	0.043	0.043	0.000	0.000	0.000	0.000
14	A	17	PRO	0	0.009	0.018	17.427	-0.020	-0.020	0.000	0.000	0.000	0.000
15	A	18	ASN	0	0.026	-0.001	20.614	0.020	0.020	0.000	0.000	0.000	0.000
16	A	19	GLN	0	0.008	-0.011	22.683	0.006	0.006	0.000	0.000	0.000	0.000
17	A	20	ASP	-1	-0.840	-0.890	25.583	-0.022	-0.022	0.000	0.000	0.000	0.000
18	A	21	PHE	0	-0.047	-0.035	24.625	0.003	0.003	0.000	0.000	0.000	0.000
19	A	22	GLU	-1	-0.858	-0.901	25.307	-0.083	-0.083	0.000	0.000	0.000	0.000
20	A	23	PRO	0	-0.038	-0.029	21.363	-0.004	-0.004	0.000	0.000	0.000	0.000
21	A	24	VAL	0	-0.001	0.000	18.905	-0.010	-0.010	0.000	0.000	0.000	0.000
22	A	25	ASN	0	-0.015	-0.026	16.231	-0.020	-0.020	0.000	0.000	0.000	0.000
23	A	26	LEU	0	0.010	0.013	11.928	0.008	0.008	0.000	0.000	0.000	0.000
24	A	27	TYR	0	-0.002	-0.043	11.682	0.044	0.044	0.000	0.000	0.000	0.000
25	A	28	GLU	-1	-0.966	-0.972	17.131	-0.198	-0.198	0.000	0.000	0.000	0.000
26	A	29	VAL	0	-0.020	-0.023	18.818	0.036	0.036	0.000	0.000	0.000	0.000
27	A	30	LEU	0	-0.030	0.002	15.032	0.014	0.014	0.000	0.000	0.000	0.000
28	A	31	LYS	1	0.909	0.954	19.631	0.335	0.335	0.000	0.000	0.000	0.000
29	A	32	ARG	1	0.850	0.911	22.340	0.243	0.243	0.000	0.000	0.000	0.000
30	A	33	GLY	0	-0.027	-0.001	23.538	0.025	0.025	0.000	0.000	0.000	0.000
31	A	34	ARG	1	0.833	0.919	23.768	0.211	0.211	0.000	0.000	0.000	0.000
32	A	35	PRO	0	0.024	0.004	19.068	-0.022	-0.022	0.000	0.000	0.000	0.000
33	A	36	ALA	0	-0.002	0.006	16.506	0.048	0.048	0.000	0.000	0.000	0.000
34	A	37	VAL	0	-0.012	-0.003	16.266	-0.069	-0.069	0.000	0.000	0.000	0.000
35	A	38	LEU	0	0.008	0.003	11.377	0.049	0.049	0.000	0.000	0.000	0.000
36	A	39	ILE	0	-0.009	-0.006	14.009	-0.009	-0.009	0.000	0.000	0.000	0.000
37	A	40	PHE	0	0.034	0.025	10.210	0.044	0.044	0.000	0.000	0.000	0.000
38	A	41	PHE	0	-0.027	-0.028	13.957	0.016	0.016	0.000	0.000	0.000	0.000
39	A	42	PRO	0	0.003	-0.006	16.485	0.012	0.012	0.000	0.000	0.000	0.000
40	A	43	ALA	0	0.007	-0.007	17.497	0.012	0.012	0.000	0.000	0.000	0.000
41	A	44	ALA	0	0.011	0.013	20.784	-0.015	-0.015	0.000	0.000	0.000	0.000
42	A	45	PHE	0	-0.035	-0.027	23.600	0.009	0.009	0.000	0.000	0.000	0.000
43	A	46	SER	0	0.025	0.031	23.049	0.015	0.015	0.000	0.000	0.000	0.000
44	A	47	PRO	0	-0.094	-0.036	25.115	-0.013	-0.013	0.000	0.000	0.000	0.000
45	A	48	VAL	0	-0.006	-0.002	22.663	0.018	0.018	0.000	0.000	0.000	0.000
46	A	49	CYS	0	-0.052	-0.043	24.333	0.005	0.005	0.000	0.000	0.000	0.000
47	A	50	THR	0	0.011	0.006	24.780	0.003	0.003	0.000	0.000	0.000	0.000
48	A	51	LYS	1	0.923	0.965	27.016	-0.079	-0.079	0.000	0.000	0.000	0.000
49	A	52	GLU	-1	-0.890	-0.958	27.997	0.069	0.069	0.000	0.000	0.000	0.000
50	A	53	LEU	0	-0.002	0.017	30.269	-0.002	-0.002	0.000	0.000	0.000	0.000
51	A	55	THR	0	-0.041	-0.018	28.890	-0.011	-0.011	0.000	0.000	0.000	0.000
52	A	56	PHE	0	0.063	0.020	28.414	0.005	0.005	0.000	0.000	0.000	0.000
53	A	57	ARG	1	0.921	0.970	29.738	-0.004	-0.004	0.000	0.000	0.000	0.000
54	A	58	ASP	-1	-0.719	-0.832	23.577	0.015	0.015	0.000	0.000	0.000	0.000
55	A	59	LYS	1	0.855	0.942	25.860	0.008	0.008	0.000	0.000	0.000	0.000
56	A	60	MET	0	0.057	0.022	20.756	-0.019	-0.019	0.000	0.000	0.000	0.000
57	A	61	ALA	0	0.046	0.014	24.462	-0.017	-0.017	0.000	0.000	0.000	0.000
58	A	62	GLN	0	-0.077	-0.045	26.217	-0.006	-0.006	0.000	0.000	0.000	0.000
59	A	63	LEU	0	0.007	0.003	20.594	-0.012	-0.012	0.000	0.000	0.000	0.000
60	A	64	GLU	-1	-0.864	-0.928	24.280	-0.096	-0.096	0.000	0.000	0.000	0.000
61	A	65	LYS	1	0.798	0.895	26.957	0.089	0.089	0.000	0.000	0.000	0.000
62	A	66	ALA	0	-0.028	0.000	23.333	-0.005	-0.005	0.000	0.000	0.000	0.000
63	A	67	ASN	0	-0.026	-0.013	25.380	0.002	0.002	0.000	0.000	0.000	0.000
64	A	68	ALA	0	0.009	-0.010	20.884	-0.020	-0.020	0.000	0.000	0.000	0.000
65	A	69	GLU	-1	-0.846	-0.882	20.911	-0.175	-0.175	0.000	0.000	0.000	0.000
66	A	70	VAL	0	-0.008	-0.002	19.794	-0.037	-0.037	0.000	0.000	0.000	0.000
67	A	71	LEU	0	-0.011	-0.020	17.019	0.022	0.022	0.000	0.000	0.000	0.000
68	A	72	ALA	0	-0.010	0.009	16.673	-0.018	-0.018	0.000	0.000	0.000	0.000
69	A	73	ILE	0	-0.019	-0.010	13.059	0.005	0.005	0.000	0.000	0.000	0.000
70	A	74	SER	0	0.040	-0.005	15.589	0.025	0.025	0.000	0.000	0.000	0.000
71	A	75	VAL	0	-0.009	-0.006	15.011	-0.018	-0.018	0.000	0.000	0.000	0.000
72	A	76	ASP	-1	-0.810	-0.864	17.455	0.139	0.139	0.000	0.000	0.000	0.000
73	A	77	SER	0	0.017	0.023	20.718	-0.013	-0.013	0.000	0.000	0.000	0.000
74	A	78	PRO	0	0.062	0.024	22.770	-0.005	-0.005	0.000	0.000	0.000	0.000
75	A	79	TRP	0	0.031	0.009	24.577	-0.005	-0.005	0.000	0.000	0.000	0.000
76	A	80	CYS	0	-0.043	0.000	25.039	-0.008	-0.008	0.000	0.000	0.000	0.000
77	A	81	LEU	0	0.071	0.034	20.496	-0.008	-0.008	0.000	0.000	0.000	0.000
78	A	82	LYS	1	0.800	0.896	24.932	0.013	0.013	0.000	0.000	0.000	0.000
79	A	83	LYS	1	0.870	0.933	28.050	-0.031	-0.031	0.000	0.000	0.000	0.000
80	A	84	PHE	0	0.025	-0.008	23.623	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	85	LYS	1	0.893	0.942	26.375	0.054	0.054	0.000	0.000	0.000	0.000
82	A	86	ASP	-1	-0.910	-0.965	27.845	-0.023	-0.023	0.000	0.000	0.000	0.000
83	A	87	GLU	-1	-0.906	-0.951	31.220	0.025	0.025	0.000	0.000	0.000	0.000
84	A	88	ASN	0	-0.116	-0.054	28.562	0.001	0.001	0.000	0.000	0.000	0.000
85	A	89	ARG	1	0.883	0.937	30.486	0.022	0.022	0.000	0.000	0.000	0.000
86	A	90	LEU	0	0.045	0.043	24.777	-0.006	-0.006	0.000	0.000	0.000	0.000
87	A	91	ALA	0	-0.026	-0.019	28.356	0.001	0.001	0.000	0.000	0.000	0.000
88	A	92	PHE	0	-0.035	-0.010	22.345	-0.006	-0.006	0.000	0.000	0.000	0.000
89	A	93	ASN	0	0.021	0.007	22.396	0.026	0.026	0.000	0.000	0.000	0.000
90	A	94	LEU	0	-0.052	-0.025	20.684	-0.011	-0.011	0.000	0.000	0.000	0.000
91	A	95	LEU	0	-0.004	-0.018	16.477	0.006	0.006	0.000	0.000	0.000	0.000
92	A	96	SER	0	-0.012	-0.039	18.283	0.024	0.024	0.000	0.000	0.000	0.000
93	A	97	ASP	-1	-0.752	-0.900	12.407	0.231	0.231	0.000	0.000	0.000	0.000
94	A	98	TYR	0	-0.032	-0.014	15.859	0.072	0.072	0.000	0.000	0.000	0.000
95	A	99	ASN	0	-0.021	-0.025	16.145	0.030	0.030	0.000	0.000	0.000	0.000
96	A	100	ARG	1	0.829	0.916	12.887	-0.339	-0.339	0.000	0.000	0.000	0.000
97	A	101	GLU	-1	-0.835	-0.904	10.965	0.549	0.549	0.000	0.000	0.000	0.000
98	A	102	VAL	0	0.055	0.022	8.973	0.132	0.132	0.000	0.000	0.000	0.000
99	A	103	ILE	0	-0.022	-0.015	7.857	-0.053	-0.053	0.000	0.000	0.000	0.000
100	A	104	LYS	1	0.827	0.921	7.151	-0.458	-0.458	0.000	0.000	0.000	0.000
101	A	105	LEU	0	-0.059	-0.010	4.831	1.031	1.186	-0.001	-0.006	-0.148	0.000
102	A	106	TYR	0	-0.030	-0.054	3.419	-2.599	-2.073	0.011	-0.289	-0.247	-0.002
103	A	107	ASN	0	-0.050	-0.020	2.324	-3.072	-1.418	2.791	-1.731	-2.713	-0.005
104	A	108	VAL	0	-0.027	-0.015	4.135	-0.444	-0.322	0.000	-0.026	-0.095	0.000
105	A	109	TYR	0	-0.014	-0.006	6.773	-0.213	-0.213	0.000	0.000	0.000	0.000
106	A	110	HIS	0	-0.033	-0.031	10.093	0.142	0.142	0.000	0.000	0.000	0.000
107	A	111	GLU	-1	-0.875	-0.951	11.412	1.183	1.183	0.000	0.000	0.000	0.000
108	A	112	ASP	-1	-0.891	-0.978	13.710	0.373	0.373	0.000	0.000	0.000	0.000
109	A	113	LEU	0	-0.003	0.013	17.317	-0.028	-0.028	0.000	0.000	0.000	0.000
110	A	114	LYS	1	0.912	0.939	18.856	-0.235	-0.235	0.000	0.000	0.000	0.000
111	A	115	GLY	0	0.050	0.034	21.307	-0.036	-0.036	0.000	0.000	0.000	0.000
112	A	116	LEU	0	-0.038	-0.012	20.419	0.008	0.008	0.000	0.000	0.000	0.000
113	A	117	LYS	1	0.946	0.979	17.784	-0.424	-0.424	0.000	0.000	0.000	0.000
114	A	118	MET	0	-0.029	0.005	10.821	-0.047	-0.047	0.000	0.000	0.000	0.000
115	A	119	VAL	0	-0.020	0.017	14.695	-0.094	-0.094	0.000	0.000	0.000	0.000
116	A	120	ALA	0	0.053	0.033	12.234	0.115	0.115	0.000	0.000	0.000	0.000
117	A	121	LYS	1	0.833	0.910	8.216	-1.006	-1.006	0.000	0.000	0.000	0.000
118	A	122	ARG	1	0.882	0.934	12.578	-0.151	-0.151	0.000	0.000	0.000	0.000
119	A	123	ALA	0	-0.023	-0.006	9.844	0.019	0.019	0.000	0.000	0.000	0.000
120	A	124	VAL	0	-0.013	-0.010	11.623	-0.004	-0.004	0.000	0.000	0.000	0.000
121	A	125	PHE	0	0.028	0.012	6.458	-0.089	-0.089	0.000	0.000	0.000	0.000
122	A	126	ILE	0	-0.003	0.017	12.271	0.087	0.087	0.000	0.000	0.000	0.000
123	A	127	VAL	0	-0.023	-0.010	12.164	-0.115	-0.115	0.000	0.000	0.000	0.000
124	A	128	LYS	1	0.941	0.978	14.653	0.616	0.616	0.000	0.000	0.000	0.000
125	A	129	PRO	0	0.032	0.004	17.058	-0.057	-0.057	0.000	0.000	0.000	0.000
126	A	130	ASP	-1	-0.846	-0.894	16.270	-0.687	-0.687	0.000	0.000	0.000	0.000
127	A	131	GLY	0	-0.018	-0.020	14.630	-0.014	-0.014	0.000	0.000	0.000	0.000
128	A	132	THR	0	-0.053	-0.031	11.907	-0.194	-0.194	0.000	0.000	0.000	0.000
129	A	133	VAL	0	-0.024	-0.011	7.938	0.190	0.190	0.000	0.000	0.000	0.000
130	A	134	ALA	0	-0.003	0.003	10.925	-0.003	-0.003	0.000	0.000	0.000	0.000
131	A	135	TYR	0	0.014	-0.011	12.528	0.087	0.087	0.000	0.000	0.000	0.000
132	A	136	LYS	1	0.831	0.889	3.970	1.389	1.526	-0.001	-0.014	-0.123	0.000
133	A	137	TRP	0	-0.024	0.007	10.639	0.079	0.079	0.000	0.000	0.000	0.000
134	A	138	VAL	0	0.018	-0.006	7.317	0.014	0.014	0.000	0.000	0.000	0.000
135	A	139	THR	0	-0.026	0.004	10.694	0.012	0.012	0.000	0.000	0.000	0.000
136	A	140	ASP	-1	-0.790	-0.884	10.545	0.809	0.809	0.000	0.000	0.000	0.000
137	A	141	ASN	0	0.003	0.003	13.352	0.019	0.019	0.000	0.000	0.000	0.000
138	A	142	PRO	0	0.060	0.021	17.050	-0.033	-0.033	0.000	0.000	0.000	0.000
139	A	143	LEU	0	-0.082	-0.034	18.053	-0.029	-0.029	0.000	0.000	0.000	0.000
140	A	144	ASN	0	0.008	-0.002	17.994	-0.015	-0.015	0.000	0.000	0.000	0.000
141	A	145	GLU	-1	-0.831	-0.940	18.729	0.004	0.004	0.000	0.000	0.000	0.000
142	A	146	PRO	0	-0.014	-0.002	17.269	-0.002	-0.002	0.000	0.000	0.000	0.000
143	A	147	ASP	-1	-0.834	-0.912	19.431	-0.086	-0.086	0.000	0.000	0.000	0.000
144	A	148	TYR	0	-0.037	-0.078	20.153	-0.025	-0.025	0.000	0.000	0.000	0.000
145	A	149	ASP	-1	-0.826	-0.902	22.474	-0.104	-0.104	0.000	0.000	0.000	0.000
146	A	150	GLU	-1	-0.850	-0.914	19.839	-0.197	-0.197	0.000	0.000	0.000	0.000
147	A	151	VAL	0	-0.004	-0.003	17.655	-0.024	-0.024	0.000	0.000	0.000	0.000
148	A	152	VAL	0	-0.023	-0.003	20.101	-0.028	-0.028	0.000	0.000	0.000	0.000
149	A	153	ARG	1	0.806	0.906	23.304	0.126	0.126	0.000	0.000	0.000	0.000
150	A	154	GLU	-1	-0.776	-0.881	18.406	-0.343	-0.343	0.000	0.000	0.000	0.000
151	A	155	ALA	0	0.007	0.010	20.055	-0.033	-0.033	0.000	0.000	0.000	0.000
152	A	156	ASN	0	0.014	-0.009	20.954	-0.017	-0.017	0.000	0.000	0.000	0.000
153	A	157	LYS	1	0.784	0.904	19.133	0.336	0.336	0.000	0.000	0.000	0.000
154	A	158	ILE	0	-0.012	-0.003	16.801	-0.009	-0.009	0.000	0.000	0.000	0.000
155	A	159	ALA	0	-0.012	-0.015	20.874	-0.010	-0.010	0.000	0.000	0.000	0.000
156	A	160	GLY	0	-0.001	-0.001	23.495	0.006	0.006	0.000	0.000	0.000	0.000
157	A	161	GLU	-1	-0.865	-0.942	20.404	-0.386	-0.386	0.000	0.000	0.000	0.000
158	A	162	LEU	0	-0.121	-0.041	21.017	-0.010	-0.010	0.000	0.000	0.000	0.000
159	A	163	VAL	0	-0.066	-0.027	24.803	0.021	0.021	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:LEU)