FMO DATABASE

FMODB ID: MM73Z

Calculation Name: 2CXC-A-Xray308

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: 2021-09-06

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200116

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	139
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1219394.281249
FMO2-HF: Nuclear repulsion	1166725.535866
FMO2-HF: Total energy	-52668.745384
FMO2-MP2: Total energy	-52826.559956

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:ACE )

Summations of interaction energy for fragment #1(A:6:ACE )

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.
5.988	3.277	14.855	-6.975	-5.171	-0.021

Interaction energy analysis for fragmet #1(A:6:ACE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.056 / q_NPA : -0.006

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	8	THR	0	-0.017	-0.010	3.730	1.214	1.874	-0.010	-0.204	-0.447	0.000
4	A	9	LEU	0	0.100	0.029	4.664	0.216	0.283	0.000	-0.005	-0.061	0.000
5	A	10	GLU	-1	-0.889	-0.931	7.219	0.222	0.222	0.000	0.000	0.000	0.000
6	A	11	GLU	-1	-0.778	-0.889	2.450	4.325	1.548	8.613	-3.671	-2.166	-0.021
7	A	12	LEU	0	0.016	0.011	3.546	0.521	0.855	0.015	-0.085	-0.264	0.000
8	A	13	ARG	1	0.966	0.992	4.719	-0.342	-0.316	0.000	-0.005	-0.021	0.000
9	A	14	TYR	0	-0.044	-0.045	6.516	-0.026	-0.026	0.000	0.000	0.000	0.000
10	A	15	ILE	0	-0.008	0.002	2.908	-0.132	-0.009	0.549	-0.290	-0.383	-0.001
11	A	16	SER	0	-0.012	0.002	6.815	-0.249	-0.249	0.000	0.000	0.000	0.000
12	A	17	VAL	0	0.002	-0.007	9.533	-0.126	-0.126	0.000	0.000	0.000	0.000
13	A	18	PHE	0	0.015	-0.002	9.872	-0.089	-0.089	0.000	0.000	0.000	0.000
14	A	19	HIS	0	0.047	0.028	11.026	-0.046	-0.046	0.000	0.000	0.000	0.000
15	A	20	SER	0	-0.057	-0.014	12.808	-0.090	-0.090	0.000	0.000	0.000	0.000
16	A	21	ILE	0	-0.035	-0.012	15.029	-0.047	-0.047	0.000	0.000	0.000	0.000
17	A	22	THR	0	-0.048	-0.042	14.353	-0.035	-0.035	0.000	0.000	0.000	0.000
18	A	23	GLY	0	0.009	0.021	15.913	-0.034	-0.034	0.000	0.000	0.000	0.000
19	A	24	VAL	0	-0.081	-0.039	12.982	-0.018	-0.018	0.000	0.000	0.000	0.000
20	A	25	THR	0	0.024	0.003	8.976	0.041	0.041	0.000	0.000	0.000	0.000
21	A	26	ALA	0	-0.043	-0.015	7.455	-0.089	-0.089	0.000	0.000	0.000	0.000
22	A	27	TYR	0	-0.023	0.000	6.151	0.422	0.422	0.000	0.000	0.000	0.000
23	A	28	ARG	1	0.852	0.909	1.984	1.367	0.172	5.688	-2.677	-1.816	0.001
24	A	29	CYS	0	-0.029	-0.002	4.164	-0.576	-0.525	0.000	-0.038	-0.013	0.000
25	A	30	ILE	0	-0.007	-0.005	5.809	-0.206	-0.206	0.000	0.000	0.000	0.000
26	A	31	VAL	0	0.058	0.024	7.577	0.032	0.032	0.000	0.000	0.000	0.000
27	A	32	ASP	-1	-0.781	-0.895	9.903	-0.053	-0.053	0.000	0.000	0.000	0.000
28	A	33	GLU	-1	-0.814	-0.933	13.199	0.048	0.048	0.000	0.000	0.000	0.000
29	A	34	GLU	-1	-0.939	-0.944	15.568	-0.010	-0.010	0.000	0.000	0.000	0.000
30	A	35	ASN	0	-0.094	-0.053	17.559	0.008	0.008	0.000	0.000	0.000	0.000
31	A	36	ASN	0	0.010	0.010	16.824	0.018	0.018	0.000	0.000	0.000	0.000
32	A	37	ARG	1	0.710	0.833	14.622	-0.058	-0.058	0.000	0.000	0.000	0.000
33	A	38	LEU	0	0.008	0.014	9.522	-0.009	-0.009	0.000	0.000	0.000	0.000
34	A	39	ILE	0	-0.029	-0.016	10.768	-0.005	-0.005	0.000	0.000	0.000	0.000
35	A	40	PHE	0	0.013	-0.001	8.208	0.064	0.064	0.000	0.000	0.000	0.000
36	A	41	LEU	0	-0.027	-0.011	7.318	-0.146	-0.146	0.000	0.000	0.000	0.000
37	A	42	VAL	0	0.033	0.007	8.617	0.168	0.168	0.000	0.000	0.000	0.000
38	A	43	SER	0	0.038	0.009	11.266	-0.048	-0.048	0.000	0.000	0.000	0.000
39	A	44	GLU	-1	-0.808	-0.905	13.383	0.090	0.090	0.000	0.000	0.000	0.000
40	A	45	GLY	0	-0.025	-0.012	16.786	0.002	0.002	0.000	0.000	0.000	0.000
41	A	46	GLU	-1	-0.846	-0.925	14.990	0.260	0.260	0.000	0.000	0.000	0.000
42	A	47	ALA	0	-0.015	-0.008	16.480	0.018	0.018	0.000	0.000	0.000	0.000
43	A	48	GLY	0	-0.013	-0.009	17.409	0.000	0.000	0.000	0.000	0.000	0.000
44	A	49	ARG	1	0.862	0.921	17.484	-0.255	-0.255	0.000	0.000	0.000	0.000
45	A	50	ALA	0	0.013	0.014	15.185	0.003	0.003	0.000	0.000	0.000	0.000
46	A	51	ILE	0	0.002	0.022	17.068	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	52	GLY	0	0.069	0.029	19.732	-0.009	-0.009	0.000	0.000	0.000	0.000
48	A	53	ARG	1	0.972	0.971	22.578	-0.107	-0.107	0.000	0.000	0.000	0.000
49	A	54	GLY	0	0.021	0.004	26.192	0.001	0.001	0.000	0.000	0.000	0.000
50	A	55	GLY	0	0.023	0.010	22.716	-0.003	-0.003	0.000	0.000	0.000	0.000
51	A	56	ARG	1	0.917	0.950	22.720	-0.134	-0.134	0.000	0.000	0.000	0.000
52	A	57	LEU	0	0.014	0.008	18.706	-0.005	-0.005	0.000	0.000	0.000	0.000
53	A	58	ILE	0	0.021	0.031	17.370	0.019	0.019	0.000	0.000	0.000	0.000
54	A	59	LYS	1	0.904	0.946	19.009	-0.105	-0.105	0.000	0.000	0.000	0.000
55	A	60	LEU	0	0.033	0.014	20.074	-0.005	-0.005	0.000	0.000	0.000	0.000
56	A	61	LEU	0	0.020	0.032	13.667	0.006	0.006	0.000	0.000	0.000	0.000
57	A	62	ARG	1	0.933	0.981	16.348	-0.128	-0.128	0.000	0.000	0.000	0.000
58	A	63	GLU	-1	-1.007	-0.993	18.366	0.118	0.118	0.000	0.000	0.000	0.000
59	A	64	ALA	0	-0.005	-0.008	16.459	-0.006	-0.006	0.000	0.000	0.000	0.000
60	A	65	LEU	0	-0.085	-0.061	11.371	0.009	0.009	0.000	0.000	0.000	0.000
61	A	66	GLY	0	0.024	0.034	15.304	-0.013	-0.013	0.000	0.000	0.000	0.000
62	A	67	LYS	1	0.862	0.937	13.254	-0.119	-0.119	0.000	0.000	0.000	0.000
63	A	68	ASN	0	-0.045	-0.031	16.814	0.016	0.016	0.000	0.000	0.000	0.000
64	A	69	ILE	0	-0.002	-0.003	13.679	0.018	0.018	0.000	0.000	0.000	0.000
65	A	70	GLU	-1	-0.846	-0.916	14.245	0.085	0.085	0.000	0.000	0.000	0.000
66	A	71	VAL	0	0.001	0.008	13.305	0.053	0.053	0.000	0.000	0.000	0.000
67	A	72	VAL	0	-0.027	-0.014	12.841	-0.049	-0.049	0.000	0.000	0.000	0.000
68	A	73	GLU	-1	-0.805	-0.885	12.443	0.218	0.218	0.000	0.000	0.000	0.000
69	A	74	TYR	0	0.013	-0.015	10.144	-0.030	-0.030	0.000	0.000	0.000	0.000
70	A	75	SER	0	0.012	-0.005	12.269	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	76	SER	0	0.018	0.014	13.924	-0.012	-0.012	0.000	0.000	0.000	0.000
72	A	77	ASP	-1	-0.832	-0.912	14.783	-0.022	-0.022	0.000	0.000	0.000	0.000
73	A	78	LEU	0	0.035	-0.005	17.082	0.010	0.010	0.000	0.000	0.000	0.000
74	A	79	GLU	-1	-0.876	-0.946	18.485	0.014	0.014	0.000	0.000	0.000	0.000
75	A	80	ARG	1	0.848	0.921	18.102	-0.065	-0.065	0.000	0.000	0.000	0.000
76	A	81	ILE	0	-0.005	-0.006	12.378	0.012	0.012	0.000	0.000	0.000	0.000
77	A	82	VAL	0	-0.030	-0.011	16.865	0.007	0.007	0.000	0.000	0.000	0.000
78	A	83	LYS	1	0.944	0.963	19.319	-0.019	-0.019	0.000	0.000	0.000	0.000
79	A	84	ASN	0	-0.027	0.000	16.398	-0.007	-0.007	0.000	0.000	0.000	0.000
80	A	85	LEU	0	-0.062	-0.026	14.525	0.012	0.012	0.000	0.000	0.000	0.000
81	A	86	PHE	0	-0.092	-0.023	18.305	-0.003	-0.003	0.000	0.000	0.000	0.000
82	A	87	PRO	0	0.060	0.023	20.603	-0.005	-0.005	0.000	0.000	0.000	0.000
83	A	88	GLY	0	-0.033	0.000	23.356	-0.003	-0.003	0.000	0.000	0.000	0.000
84	A	89	VAL	0	-0.025	-0.015	25.817	-0.005	-0.005	0.000	0.000	0.000	0.000
85	A	90	LYS	1	0.971	1.009	27.267	-0.013	-0.013	0.000	0.000	0.000	0.000
86	A	91	ILE	0	-0.043	-0.035	23.730	-0.005	-0.005	0.000	0.000	0.000	0.000
87	A	92	GLU	-1	-0.905	-0.960	27.856	0.002	0.002	0.000	0.000	0.000	0.000
88	A	93	SER	0	0.012	-0.001	28.557	-0.001	-0.001	0.000	0.000	0.000	0.000
89	A	94	ILE	0	0.021	0.018	22.221	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	95	ASN	0	-0.028	-0.016	25.671	-0.006	-0.006	0.000	0.000	0.000	0.000
91	A	96	VAL	0	0.059	0.030	21.469	-0.003	-0.003	0.000	0.000	0.000	0.000
92	A	97	ARG	1	0.910	0.959	24.372	0.051	0.051	0.000	0.000	0.000	0.000
93	A	98	GLU	-1	-0.844	-0.941	22.198	-0.128	-0.128	0.000	0.000	0.000	0.000
94	A	99	ARG	1	0.925	0.958	25.366	0.077	0.077	0.000	0.000	0.000	0.000
95	A	100	ASN	0	-0.015	-0.010	26.573	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	101	GLY	0	0.062	0.041	22.992	-0.007	-0.007	0.000	0.000	0.000	0.000
97	A	102	VAL	0	-0.023	0.005	21.456	-0.014	-0.014	0.000	0.000	0.000	0.000
98	A	103	LYS	1	0.976	0.996	17.362	0.178	0.178	0.000	0.000	0.000	0.000
99	A	104	GLN	0	-0.029	-0.032	21.140	-0.003	-0.003	0.000	0.000	0.000	0.000
100	A	105	VAL	0	0.005	0.000	19.565	0.005	0.005	0.000	0.000	0.000	0.000
101	A	106	VAL	0	-0.060	-0.043	22.839	0.002	0.002	0.000	0.000	0.000	0.000
102	A	107	ILE	0	0.006	-0.005	21.952	0.001	0.001	0.000	0.000	0.000	0.000
103	A	108	LYS	1	0.918	0.983	25.985	0.005	0.005	0.000	0.000	0.000	0.000
104	A	109	VAL	0	-0.057	-0.020	27.164	0.004	0.004	0.000	0.000	0.000	0.000
105	A	110	SER	0	0.038	0.013	30.136	-0.002	-0.002	0.000	0.000	0.000	0.000
106	A	111	GLU	-1	-0.951	-0.982	33.370	0.004	0.004	0.000	0.000	0.000	0.000
107	A	112	ASP	-1	-0.924	-0.952	34.603	0.009	0.009	0.000	0.000	0.000	0.000
108	A	113	ASP	-1	-0.813	-0.915	29.782	0.023	0.023	0.000	0.000	0.000	0.000
109	A	114	LYS	1	0.866	0.913	29.329	0.007	0.007	0.000	0.000	0.000	0.000
110	A	115	GLY	0	0.062	0.038	29.397	-0.001	-0.001	0.000	0.000	0.000	0.000
111	A	116	ALA	0	-0.011	-0.018	26.683	0.001	0.001	0.000	0.000	0.000	0.000
112	A	117	ALA	0	0.002	0.009	25.061	0.003	0.003	0.000	0.000	0.000	0.000
113	A	118	ILE	0	0.054	0.007	23.898	-0.001	-0.001	0.000	0.000	0.000	0.000
114	A	119	GLY	0	0.025	0.015	23.950	0.001	0.001	0.000	0.000	0.000	0.000
115	A	120	LYS	1	0.935	0.945	24.970	-0.036	-0.036	0.000	0.000	0.000	0.000
116	A	121	GLY	0	0.068	0.045	25.266	0.002	0.002	0.000	0.000	0.000	0.000
117	A	122	GLY	0	0.016	0.022	24.326	-0.003	-0.003	0.000	0.000	0.000	0.000
118	A	123	LYS	1	0.994	0.987	20.547	-0.070	-0.070	0.000	0.000	0.000	0.000
119	A	124	ASN	0	-0.013	0.014	19.674	0.014	0.014	0.000	0.000	0.000	0.000
120	A	125	VAL	0	0.036	0.019	19.468	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	126	LYS	1	0.840	0.935	16.442	0.014	0.014	0.000	0.000	0.000	0.000
122	A	127	ARG	1	0.863	0.921	14.853	-0.112	-0.112	0.000	0.000	0.000	0.000
123	A	128	ALA	0	0.005	0.009	14.803	-0.004	-0.004	0.000	0.000	0.000	0.000
124	A	129	ARG	1	0.853	0.928	15.578	0.032	0.032	0.000	0.000	0.000	0.000
125	A	130	LEU	0	0.002	0.005	12.446	-0.037	-0.037	0.000	0.000	0.000	0.000
126	A	131	VAL	0	0.037	0.017	10.634	-0.051	-0.051	0.000	0.000	0.000	0.000
127	A	132	LEU	0	-0.006	-0.017	11.394	-0.038	-0.038	0.000	0.000	0.000	0.000
128	A	133	SER	0	-0.048	-0.028	13.469	-0.046	-0.046	0.000	0.000	0.000	0.000
129	A	134	LYS	1	0.863	0.937	7.848	0.247	0.247	0.000	0.000	0.000	0.000
130	A	135	LEU	0	-0.050	-0.021	6.829	-0.121	-0.121	0.000	0.000	0.000	0.000
131	A	136	PHE	0	-0.024	-0.012	10.135	0.009	0.009	0.000	0.000	0.000	0.000
132	A	137	GLY	0	0.003	0.012	13.198	0.018	0.018	0.000	0.000	0.000	0.000
133	A	138	VAL	0	-0.064	-0.020	14.990	0.026	0.026	0.000	0.000	0.000	0.000
134	A	139	GLU	-1	-0.781	-0.880	16.122	-0.240	-0.240	0.000	0.000	0.000	0.000
135	A	140	LYS	1	0.854	0.941	18.808	0.080	0.080	0.000	0.000	0.000	0.000
136	A	141	VAL	0	0.031	0.018	18.883	0.002	0.002	0.000	0.000	0.000	0.000
137	A	142	VAL	0	-0.043	-0.030	22.006	0.002	0.002	0.000	0.000	0.000	0.000
138	A	143	ILE	0	0.026	0.026	23.667	0.001	0.001	0.000	0.000	0.000	0.000
139	A	144	ARG	0	0.099	0.045	27.106	0.022	0.022	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

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