FMO DATABASE

FMODB ID: 769MK

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1213600.267888
FMO2-HF: Nuclear repulsion	1161081.637293
FMO2-HF: Total energy	-52518.630595
FMO2-MP2: Total energy	-52675.886623

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.
-11.902	-7.575	7.727	-5.385	-6.668	-0.031

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 : 0.006 / q_NPA : 0.005

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	0.099	0.029	3.665	-3.451	-0.894	-0.010	-1.470	-1.076	0.008
4	A	10	GLU	-1	-0.866	-0.899	6.378	-0.598	-0.598	0.000	0.000	0.000	0.000
5	A	11	GLU	-1	-0.734	-0.849	1.986	-5.690	-6.199	6.976	-3.200	-3.267	-0.038
6	A	12	LEU	0	0.012	0.012	4.040	0.376	0.636	-0.001	-0.033	-0.227	0.000
7	A	13	ARG	1	0.971	0.993	5.070	1.321	1.377	-0.001	-0.002	-0.053	0.000
8	A	14	TYR	0	-0.054	-0.075	7.764	0.319	0.319	0.000	0.000	0.000	0.000
9	A	15	ILE	0	-0.007	-0.001	4.456	0.157	0.240	-0.001	-0.003	-0.079	0.000
10	A	16	SER	0	0.020	0.015	8.373	0.184	0.184	0.000	0.000	0.000	0.000
11	A	17	VAL	0	-0.025	-0.018	10.680	0.099	0.099	0.000	0.000	0.000	0.000
12	A	18	PHE	0	0.013	-0.004	11.579	0.079	0.079	0.000	0.000	0.000	0.000
13	A	19	HIS	0	0.006	0.019	12.604	0.018	0.018	0.000	0.000	0.000	0.000
14	A	20	SER	0	-0.004	0.009	14.393	0.020	0.020	0.000	0.000	0.000	0.000
15	A	21	ILE	0	-0.073	-0.034	16.532	0.023	0.023	0.000	0.000	0.000	0.000
16	A	22	THR	0	-0.031	-0.031	16.108	0.031	0.031	0.000	0.000	0.000	0.000
17	A	23	GLY	0	0.013	0.025	17.553	0.018	0.018	0.000	0.000	0.000	0.000
18	A	24	VAL	0	-0.075	-0.037	15.358	0.025	0.025	0.000	0.000	0.000	0.000
19	A	25	THR	0	0.015	-0.008	11.362	-0.059	-0.059	0.000	0.000	0.000	0.000
20	A	26	ALA	0	-0.036	-0.006	9.759	0.036	0.036	0.000	0.000	0.000	0.000
21	A	27	TYR	0	-0.023	-0.002	7.692	0.177	0.177	0.000	0.000	0.000	0.000
22	A	28	ARG	1	0.822	0.865	2.737	-4.466	-2.586	0.764	-0.677	-1.966	-0.001
23	A	29	CYS	0	-0.017	-0.005	5.532	-0.325	-0.325	0.000	0.000	0.000	0.000
24	A	30	ILE	0	-0.019	-0.006	6.108	-0.255	-0.255	0.000	0.000	0.000	0.000
25	A	31	VAL	0	0.057	0.023	7.064	0.005	0.005	0.000	0.000	0.000	0.000
26	A	32	ASP	-1	-0.754	-0.874	9.555	0.099	0.099	0.000	0.000	0.000	0.000
27	A	33	GLU	-1	-0.751	-0.878	12.487	-0.311	-0.311	0.000	0.000	0.000	0.000
28	A	34	GLU	-1	-0.866	-0.897	14.816	0.026	0.026	0.000	0.000	0.000	0.000
29	A	35	ASN	0	-0.105	-0.059	17.031	0.010	0.010	0.000	0.000	0.000	0.000
30	A	36	ASN	0	0.012	0.013	16.562	-0.024	-0.024	0.000	0.000	0.000	0.000
31	A	37	ARG	1	0.727	0.846	14.767	-0.023	-0.023	0.000	0.000	0.000	0.000
32	A	38	LEU	0	0.020	0.026	10.204	-0.028	-0.028	0.000	0.000	0.000	0.000
33	A	39	ILE	0	-0.042	-0.031	11.249	0.037	0.037	0.000	0.000	0.000	0.000
34	A	40	PHE	0	0.024	0.008	9.999	0.040	0.040	0.000	0.000	0.000	0.000
35	A	41	LEU	0	-0.024	-0.011	9.293	0.012	0.012	0.000	0.000	0.000	0.000
36	A	42	VAL	0	0.031	0.006	11.475	0.049	0.049	0.000	0.000	0.000	0.000
37	A	43	SER	0	0.033	0.009	14.159	0.057	0.057	0.000	0.000	0.000	0.000
38	A	44	GLU	-1	-0.793	-0.877	16.380	0.181	0.181	0.000	0.000	0.000	0.000
39	A	45	GLY	0	-0.022	-0.013	19.533	-0.012	-0.012	0.000	0.000	0.000	0.000
40	A	46	GLU	-1	-0.826	-0.906	17.931	0.103	0.103	0.000	0.000	0.000	0.000
41	A	47	ALA	0	-0.016	-0.014	19.151	-0.022	-0.022	0.000	0.000	0.000	0.000
42	A	48	GLY	0	-0.024	-0.013	20.118	-0.020	-0.020	0.000	0.000	0.000	0.000
43	A	49	ARG	1	0.845	0.896	19.544	-0.088	-0.088	0.000	0.000	0.000	0.000
44	A	50	ALA	0	-0.003	0.011	17.495	-0.018	-0.018	0.000	0.000	0.000	0.000
45	A	51	ILE	0	0.008	0.012	19.348	-0.024	-0.024	0.000	0.000	0.000	0.000
46	A	52	GLY	0	0.064	0.032	21.897	-0.016	-0.016	0.000	0.000	0.000	0.000
47	A	53	ARG	1	0.976	0.971	24.676	-0.006	-0.006	0.000	0.000	0.000	0.000
48	A	54	GLY	0	0.019	0.003	28.078	-0.007	-0.007	0.000	0.000	0.000	0.000
49	A	55	GLY	0	0.025	0.015	24.645	-0.004	-0.004	0.000	0.000	0.000	0.000
50	A	56	ARG	1	0.936	0.959	24.468	0.027	0.027	0.000	0.000	0.000	0.000
51	A	57	LEU	0	0.007	0.003	20.508	-0.013	-0.013	0.000	0.000	0.000	0.000
52	A	58	ILE	0	0.011	0.025	18.943	-0.015	-0.015	0.000	0.000	0.000	0.000
53	A	59	LYS	1	0.778	0.875	20.553	0.062	0.062	0.000	0.000	0.000	0.000
54	A	60	LEU	0	0.017	0.001	21.797	-0.010	-0.010	0.000	0.000	0.000	0.000
55	A	61	LEU	0	0.027	0.034	15.205	-0.022	-0.022	0.000	0.000	0.000	0.000
56	A	62	ARG	1	0.912	0.973	17.755	0.040	0.040	0.000	0.000	0.000	0.000
57	A	63	GLU	-1	-0.875	-0.917	19.627	-0.110	-0.110	0.000	0.000	0.000	0.000
58	A	64	ALA	0	-0.010	-0.006	17.820	-0.013	-0.013	0.000	0.000	0.000	0.000
59	A	65	LEU	0	-0.073	-0.051	12.754	-0.043	-0.043	0.000	0.000	0.000	0.000
60	A	66	GLY	0	0.021	0.031	16.274	-0.024	-0.024	0.000	0.000	0.000	0.000
61	A	67	LYS	1	0.789	0.883	13.288	0.328	0.328	0.000	0.000	0.000	0.000
62	A	68	ASN	0	-0.011	-0.022	17.424	0.021	0.021	0.000	0.000	0.000	0.000
63	A	69	ILE	0	-0.006	-0.001	15.167	-0.013	-0.013	0.000	0.000	0.000	0.000
64	A	70	GLU	-1	-0.819	-0.896	15.321	0.078	0.078	0.000	0.000	0.000	0.000
65	A	71	VAL	0	0.006	0.009	14.755	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	72	VAL	0	-0.031	-0.016	14.881	-0.008	-0.008	0.000	0.000	0.000	0.000
67	A	73	GLU	-1	-0.780	-0.863	14.872	0.225	0.225	0.000	0.000	0.000	0.000
68	A	74	TYR	0	0.023	-0.005	11.105	0.031	0.031	0.000	0.000	0.000	0.000
69	A	75	SER	0	0.018	-0.001	14.099	-0.054	-0.054	0.000	0.000	0.000	0.000
70	A	76	SER	0	0.034	0.018	13.518	0.035	0.035	0.000	0.000	0.000	0.000
71	A	77	ASP	-1	-0.852	-0.925	14.539	0.261	0.261	0.000	0.000	0.000	0.000
72	A	78	LEU	0	0.017	-0.006	15.432	-0.004	-0.004	0.000	0.000	0.000	0.000
73	A	79	GLU	-1	-0.836	-0.917	17.503	0.163	0.163	0.000	0.000	0.000	0.000
74	A	80	ARG	1	0.829	0.898	19.450	-0.226	-0.226	0.000	0.000	0.000	0.000
75	A	81	ILE	0	-0.003	0.002	13.391	-0.010	-0.010	0.000	0.000	0.000	0.000
76	A	82	VAL	0	-0.032	-0.019	17.622	-0.017	-0.017	0.000	0.000	0.000	0.000
77	A	83	LYS	1	0.887	0.916	19.457	-0.176	-0.176	0.000	0.000	0.000	0.000
78	A	84	ASN	0	-0.041	-0.016	18.183	-0.038	-0.038	0.000	0.000	0.000	0.000
79	A	85	LEU	0	-0.039	-0.014	15.253	-0.018	-0.018	0.000	0.000	0.000	0.000
80	A	86	PHE	0	-0.098	-0.039	19.576	-0.020	-0.020	0.000	0.000	0.000	0.000
81	A	87	PRO	0	0.066	0.030	22.221	-0.007	-0.007	0.000	0.000	0.000	0.000
82	A	88	GLY	0	-0.032	0.001	25.086	-0.005	-0.005	0.000	0.000	0.000	0.000
83	A	89	VAL	0	-0.048	-0.035	26.651	-0.006	-0.006	0.000	0.000	0.000	0.000
84	A	90	LYS	1	0.924	0.970	28.305	-0.071	-0.071	0.000	0.000	0.000	0.000
85	A	91	ILE	0	-0.052	-0.039	23.694	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	92	GLU	-1	-0.863	-0.900	27.912	0.090	0.090	0.000	0.000	0.000	0.000
87	A	93	SER	0	0.036	0.011	27.585	0.000	0.000	0.000	0.000	0.000	0.000
88	A	94	ILE	0	0.006	0.015	20.808	-0.003	-0.003	0.000	0.000	0.000	0.000
89	A	95	ASN	0	-0.029	-0.021	23.703	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	96	VAL	0	0.070	0.035	18.237	0.004	0.004	0.000	0.000	0.000	0.000
91	A	97	ARG	1	0.906	0.964	21.412	-0.144	-0.144	0.000	0.000	0.000	0.000
92	A	98	GLU	-1	-0.800	-0.928	17.301	0.286	0.286	0.000	0.000	0.000	0.000
93	A	99	ARG	1	0.938	0.965	20.914	-0.129	-0.129	0.000	0.000	0.000	0.000
94	A	100	ASN	0	-0.021	-0.017	21.556	0.002	0.002	0.000	0.000	0.000	0.000
95	A	101	GLY	0	0.069	0.047	17.617	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	102	VAL	0	-0.025	0.003	16.337	0.027	0.027	0.000	0.000	0.000	0.000
97	A	103	LYS	1	0.955	0.998	13.309	-0.411	-0.411	0.000	0.000	0.000	0.000
98	A	104	GLN	0	-0.048	-0.037	17.292	-0.001	-0.001	0.000	0.000	0.000	0.000
99	A	105	VAL	0	0.022	0.003	17.422	-0.008	-0.008	0.000	0.000	0.000	0.000
100	A	106	VAL	0	-0.066	-0.046	20.292	-0.014	-0.014	0.000	0.000	0.000	0.000
101	A	107	ILE	0	0.028	0.011	20.554	0.003	0.003	0.000	0.000	0.000	0.000
102	A	108	LYS	1	0.884	0.923	24.734	-0.101	-0.101	0.000	0.000	0.000	0.000
103	A	109	VAL	0	0.000	0.005	27.009	0.002	0.002	0.000	0.000	0.000	0.000
104	A	110	SER	0	0.024	-0.009	29.787	-0.005	-0.005	0.000	0.000	0.000	0.000
105	A	111	GLU	-1	-0.939	-0.977	33.165	0.055	0.055	0.000	0.000	0.000	0.000
106	A	112	ASP	-1	-0.870	-0.932	34.346	0.051	0.051	0.000	0.000	0.000	0.000
107	A	113	ASP	-1	-0.797	-0.887	30.158	0.078	0.078	0.000	0.000	0.000	0.000
108	A	114	LYS	1	0.789	0.879	29.039	-0.070	-0.070	0.000	0.000	0.000	0.000
109	A	115	GLY	0	0.063	0.042	29.099	-0.001	-0.001	0.000	0.000	0.000	0.000
110	A	116	ALA	0	-0.006	-0.014	27.791	-0.001	-0.001	0.000	0.000	0.000	0.000
111	A	117	ALA	0	0.006	0.012	25.333	0.005	0.005	0.000	0.000	0.000	0.000
112	A	118	ILE	0	0.055	0.021	23.907	0.011	0.011	0.000	0.000	0.000	0.000
113	A	119	GLY	0	0.029	0.017	23.792	0.002	0.002	0.000	0.000	0.000	0.000
114	A	120	LYS	1	0.960	0.957	25.247	-0.004	-0.004	0.000	0.000	0.000	0.000
115	A	121	GLY	0	0.075	0.049	25.060	-0.005	-0.005	0.000	0.000	0.000	0.000
116	A	122	GLY	0	0.011	0.022	23.178	-0.002	-0.002	0.000	0.000	0.000	0.000
117	A	123	LYS	1	0.935	0.952	20.223	-0.006	-0.006	0.000	0.000	0.000	0.000
118	A	124	ASN	0	-0.057	-0.014	19.643	0.007	0.007	0.000	0.000	0.000	0.000
119	A	125	VAL	0	0.059	0.023	19.406	0.022	0.022	0.000	0.000	0.000	0.000
120	A	126	LYS	1	0.746	0.865	15.179	0.003	0.003	0.000	0.000	0.000	0.000
121	A	127	ARG	1	0.888	0.934	15.182	-0.111	-0.111	0.000	0.000	0.000	0.000
122	A	128	ALA	0	0.009	0.011	14.565	0.048	0.048	0.000	0.000	0.000	0.000
123	A	129	ARG	1	0.858	0.931	14.488	-0.101	-0.101	0.000	0.000	0.000	0.000
124	A	130	LEU	0	0.003	0.007	11.009	0.059	0.059	0.000	0.000	0.000	0.000
125	A	131	VAL	0	0.031	0.013	9.936	0.112	0.112	0.000	0.000	0.000	0.000
126	A	132	LEU	0	-0.013	-0.018	10.341	0.120	0.120	0.000	0.000	0.000	0.000
127	A	133	SER	0	-0.033	-0.027	10.024	0.085	0.085	0.000	0.000	0.000	0.000
128	A	134	LYS	1	0.837	0.908	5.428	-0.489	-0.489	0.000	0.000	0.000	0.000
129	A	135	LEU	0	-0.031	-0.010	5.828	0.308	0.308	0.000	0.000	0.000	0.000
130	A	136	PHE	0	-0.018	-0.014	8.048	-0.044	-0.044	0.000	0.000	0.000	0.000
131	A	137	GLY	0	-0.012	0.012	9.508	-0.077	-0.077	0.000	0.000	0.000	0.000
132	A	138	VAL	0	-0.060	-0.025	10.737	-0.087	-0.087	0.000	0.000	0.000	0.000
133	A	139	GLU	-1	-0.784	-0.862	11.761	0.432	0.432	0.000	0.000	0.000	0.000
134	A	140	LYS	1	0.868	0.940	14.794	-0.170	-0.170	0.000	0.000	0.000	0.000
135	A	141	VAL	0	0.051	0.033	16.833	0.009	0.009	0.000	0.000	0.000	0.000
136	A	142	VAL	0	-0.057	-0.044	19.620	-0.022	-0.022	0.000	0.000	0.000	0.000
137	A	143	ILE	0	0.044	0.040	22.769	0.006	0.006	0.000	0.000	0.000	0.000
138	A	144	ARG	1	0.987	1.014	25.715	-0.121	-0.121	0.000	0.000	0.000	0.000

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