FMO DATABASE

FMODB ID: GY5R1

Calculation Name: 2CFX-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2CFX

Chain ID: A

ChEMBL ID:

UniProt ID: P96582

Base Structure: X-ray

Registration Date: 2023-09-27

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	140
LigandCharge	CYM=-1
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1151546.751125
FMO2-HF: Nuclear repulsion	1094940.46303
FMO2-HF: Total energy	-56606.288095
FMO2-MP2: Total energy	-56769.958274

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:MET)

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

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.
-14.381	-7.661	16.475	-5.886	-17.31	-0.038

Interaction energy analysis for fragmet #1(A:1:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.012 / 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	3	LEU	0	0.063	0.034	3.172	-2.723	0.541	0.731	-1.278	-2.718	0.001
4	A	4	ASP	-1	-0.843	-0.897	4.704	0.064	0.175	0.002	-0.012	-0.101	0.000
5	A	5	GLN	0	0.030	-0.004	7.708	0.120	0.120	0.000	0.000	0.000	0.000
6	A	6	ILE	0	-0.003	-0.005	9.554	-0.082	-0.082	0.000	0.000	0.000	0.000
7	A	7	ASP	-1	-0.774	-0.873	5.039	2.980	3.207	0.001	-0.040	-0.188	0.000
8	A	8	LEU	0	0.006	0.005	7.460	-0.312	-0.312	0.000	0.000	0.000	0.000
9	A	9	ASN	0	0.018	0.020	10.010	-0.159	-0.159	0.000	0.000	0.000	0.000
10	A	10	ILE	0	0.030	0.016	8.376	-0.122	-0.122	0.000	0.000	0.000	0.000
11	A	11	ILE	0	-0.008	0.000	6.489	-0.167	-0.167	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.901	-0.949	10.572	0.078	0.078	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.879	-0.949	13.728	0.033	0.033	0.000	0.000	0.000	0.000
14	A	14	LEU	0	-0.015	-0.018	10.062	-0.045	-0.045	0.000	0.000	0.000	0.000
15	A	15	LYS	1	0.886	0.943	12.417	-0.100	-0.100	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.804	0.907	15.520	-0.132	-0.132	0.000	0.000	0.000	0.000
17	A	17	ASP	-1	-0.797	-0.874	17.247	-0.096	-0.096	0.000	0.000	0.000	0.000
18	A	18	SER	0	-0.019	0.009	15.237	0.004	0.004	0.000	0.000	0.000	0.000
19	A	19	ARG	1	0.842	0.874	16.032	0.056	0.056	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.062	-0.014	16.028	-0.002	-0.002	0.000	0.000	0.000	0.000
21	A	21	SER	0	-0.027	-0.044	16.141	-0.027	-0.027	0.000	0.000	0.000	0.000
22	A	22	MET	0	0.104	0.036	12.402	0.025	0.025	0.000	0.000	0.000	0.000
23	A	23	ARG	1	0.885	0.945	15.422	0.136	0.136	0.000	0.000	0.000	0.000
24	A	24	GLU	-1	-0.801	-0.871	18.771	-0.063	-0.063	0.000	0.000	0.000	0.000
25	A	25	LEU	0	0.046	0.033	11.615	0.023	0.023	0.000	0.000	0.000	0.000
26	A	26	GLY	0	0.035	0.009	15.701	0.043	0.043	0.000	0.000	0.000	0.000
27	A	27	ARG	1	0.924	0.967	16.510	0.015	0.015	0.000	0.000	0.000	0.000
28	A	28	LYS	1	0.888	0.959	17.445	-0.011	-0.011	0.000	0.000	0.000	0.000
29	A	29	ILE	0	0.037	0.021	12.384	0.012	0.012	0.000	0.000	0.000	0.000
30	A	30	LYS	1	0.789	0.907	16.317	-0.069	-0.069	0.000	0.000	0.000	0.000
31	A	31	LEU	0	0.041	0.017	11.545	0.027	0.027	0.000	0.000	0.000	0.000
32	A	32	SER	0	-0.012	-0.006	15.985	-0.032	-0.032	0.000	0.000	0.000	0.000
33	A	33	PRO	0	0.070	0.014	15.197	0.006	0.006	0.000	0.000	0.000	0.000
34	A	34	PRO	0	0.027	0.013	14.529	-0.024	-0.024	0.000	0.000	0.000	0.000
35	A	35	SER	0	0.006	0.005	12.136	-0.033	-0.033	0.000	0.000	0.000	0.000
36	A	36	VAL	0	0.003	0.012	10.562	0.058	0.058	0.000	0.000	0.000	0.000
37	A	37	THR	0	0.023	-0.011	9.815	0.005	0.005	0.000	0.000	0.000	0.000
38	A	38	GLU	-1	-0.870	-0.908	7.444	-1.279	-1.279	0.000	0.000	0.000	0.000
39	A	39	ARG	1	0.807	0.868	5.969	-1.677	-1.677	0.000	0.000	0.000	0.000
40	A	40	VAL	0	0.000	-0.015	5.118	-0.233	-0.166	-0.001	0.000	-0.066	0.000
41	A	41	ARG	1	0.846	0.906	6.450	0.973	0.973	0.000	0.000	0.000	0.000
42	A	42	GLN	0	0.003	-0.016	2.165	-3.245	-2.546	1.312	-0.474	-1.537	-0.002
43	A	43	LEU	0	0.015	0.001	2.202	-4.067	-3.319	4.499	-1.736	-3.511	-0.008
44	A	44	GLU	-1	-0.779	-0.846	3.026	0.458	-0.408	0.009	1.049	-0.192	-0.001
45	A	45	SER	0	-0.068	-0.025	5.030	0.264	0.264	0.000	0.000	0.000	0.000
46	A	46	PHE	0	-0.034	-0.021	2.159	-6.525	-3.699	7.224	-3.080	-6.970	-0.029
47	A	47	GLY	0	-0.020	0.014	4.192	0.442	0.552	-0.001	-0.025	-0.084	0.000
48	A	48	ILE	0	-0.044	-0.024	2.323	0.399	-0.067	2.699	-0.290	-1.943	0.001
49	A	49	ILE	0	-0.040	-0.015	5.981	0.392	0.392	0.000	0.000	0.000	0.000
50	A	50	LYS	1	0.956	0.970	8.127	0.302	0.302	0.000	0.000	0.000	0.000
51	A	51	GLN	0	-0.003	-0.018	10.969	0.004	0.004	0.000	0.000	0.000	0.000
52	A	52	TYR	0	-0.071	-0.035	10.218	0.079	0.079	0.000	0.000	0.000	0.000
53	A	53	THR	0	0.009	-0.015	15.137	0.009	0.009	0.000	0.000	0.000	0.000
54	A	54	LEU	0	-0.028	-0.026	18.389	0.014	0.014	0.000	0.000	0.000	0.000
55	A	55	GLU	-1	-0.853	-0.907	21.486	-0.068	-0.068	0.000	0.000	0.000	0.000
56	A	56	VAL	0	-0.019	-0.007	23.719	0.006	0.006	0.000	0.000	0.000	0.000
57	A	57	ASP	-1	-0.809	-0.904	27.363	-0.049	-0.049	0.000	0.000	0.000	0.000
58	A	58	GLN	0	0.081	0.022	28.051	0.000	0.000	0.000	0.000	0.000	0.000
59	A	59	LYS	1	0.987	0.998	32.130	0.041	0.041	0.000	0.000	0.000	0.000
60	A	60	LYS	1	0.795	0.883	33.970	0.049	0.049	0.000	0.000	0.000	0.000
61	A	61	LEU	0	-0.032	-0.006	30.192	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	62	GLY	0	-0.004	0.012	34.750	-0.002	-0.002	0.000	0.000	0.000	0.000
63	A	63	LEU	0	-0.031	-0.004	32.647	0.001	0.001	0.000	0.000	0.000	0.000
64	A	64	PRO	0	-0.059	-0.040	35.026	0.000	0.000	0.000	0.000	0.000	0.000
65	A	65	VAL	0	-0.028	0.002	37.327	0.004	0.004	0.000	0.000	0.000	0.000
66	A	66	SER	0	0.039	0.003	32.047	-0.005	-0.005	0.000	0.000	0.000	0.000
67	A	67	CYS	0	-0.041	0.004	34.109	0.007	0.007	0.000	0.000	0.000	0.000
68	A	68	ILE	0	0.017	0.010	30.192	-0.007	-0.007	0.000	0.000	0.000	0.000
69	A	69	VAL	0	-0.028	-0.013	32.727	0.004	0.004	0.000	0.000	0.000	0.000
70	A	70	GLU	-1	-0.849	-0.926	32.810	-0.043	-0.043	0.000	0.000	0.000	0.000
71	A	71	ALA	0	0.002	-0.014	33.381	0.002	0.002	0.000	0.000	0.000	0.000
72	A	72	THR	0	-0.002	-0.012	34.376	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	73	VAL	0	0.033	0.016	33.481	0.001	0.001	0.000	0.000	0.000	0.000
74	A	74	LYS	1	0.840	0.912	36.593	0.054	0.054	0.000	0.000	0.000	0.000
75	A	75	ASN	0	-0.007	-0.021	39.005	-0.005	-0.005	0.000	0.000	0.000	0.000
76	A	76	ALA	0	0.032	0.022	36.815	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	77	ASP	-1	-0.812	-0.899	35.911	-0.085	-0.085	0.000	0.000	0.000	0.000
78	A	78	TYR	0	-0.053	-0.103	30.710	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	79	GLU	-1	-0.797	-0.889	28.694	-0.151	-0.151	0.000	0.000	0.000	0.000
80	A	80	ARG	1	0.810	0.921	32.368	0.063	0.063	0.000	0.000	0.000	0.000
81	A	81	PHE	0	0.018	0.004	30.642	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	82	LYS	1	0.854	0.911	25.567	0.162	0.162	0.000	0.000	0.000	0.000
83	A	83	SER	0	-0.024	-0.026	30.198	-0.009	-0.009	0.000	0.000	0.000	0.000
84	A	84	TYR	0	0.003	0.005	32.005	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	85	ILE	0	0.015	0.007	28.860	0.000	0.000	0.000	0.000	0.000	0.000
86	A	86	GLN	0	-0.019	-0.022	25.126	0.001	0.001	0.000	0.000	0.000	0.000
87	A	87	THR	0	-0.109	-0.038	29.379	-0.004	-0.004	0.000	0.000	0.000	0.000
88	A	88	LEU	0	-0.021	-0.009	31.441	0.008	0.008	0.000	0.000	0.000	0.000
89	A	89	PRO	0	-0.018	0.001	30.461	-0.010	-0.010	0.000	0.000	0.000	0.000
90	A	90	ASN	0	-0.003	-0.016	30.158	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	91	ILE	0	0.029	0.026	27.876	0.009	0.009	0.000	0.000	0.000	0.000
92	A	92	GLU	-1	-0.839	-0.892	25.015	-0.104	-0.104	0.000	0.000	0.000	0.000
93	A	93	PHE	0	0.003	-0.007	23.618	-0.012	-0.012	0.000	0.000	0.000	0.000
94	A	94	CYS	0	-0.005	-0.008	24.545	0.016	0.016	0.000	0.000	0.000	0.000
95	A	95	TYR	0	-0.033	-0.005	20.864	-0.022	-0.022	0.000	0.000	0.000	0.000
96	A	96	ARG	1	0.904	0.970	24.744	0.091	0.091	0.000	0.000	0.000	0.000
97	A	97	ILE	0	-0.049	-0.031	25.335	-0.002	-0.002	0.000	0.000	0.000	0.000
98	A	98	ALA	0	-0.024	-0.004	26.816	0.001	0.001	0.000	0.000	0.000	0.000
99	A	99	GLY	0	0.019	-0.013	28.638	0.006	0.006	0.000	0.000	0.000	0.000
100	A	100	ALA	0	-0.023	-0.002	32.215	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	101	ALA	0	0.036	0.031	33.824	-0.001	-0.001	0.000	0.000	0.000	0.000
102	A	102	CYM	-1	-0.818	-0.837	31.752	-0.063	-0.063	0.000	0.000	0.000	0.000
103	A	103	TYR	0	-0.006	-0.036	27.307	-0.013	-0.013	0.000	0.000	0.000	0.000
104	A	104	MET	0	0.000	0.029	28.464	0.008	0.008	0.000	0.000	0.000	0.000
105	A	105	LEU	0	0.001	0.001	27.999	-0.012	-0.012	0.000	0.000	0.000	0.000
106	A	106	LYS	1	0.845	0.927	27.585	0.085	0.085	0.000	0.000	0.000	0.000
107	A	107	ILE	0	0.012	0.015	29.795	-0.009	-0.009	0.000	0.000	0.000	0.000
108	A	108	ASN	0	-0.051	-0.033	29.093	0.014	0.014	0.000	0.000	0.000	0.000
109	A	109	ALA	0	0.022	-0.003	33.166	-0.004	-0.004	0.000	0.000	0.000	0.000
110	A	110	GLU	-1	-0.840	-0.923	36.739	-0.068	-0.068	0.000	0.000	0.000	0.000
111	A	111	SER	0	-0.031	-0.030	39.530	0.004	0.004	0.000	0.000	0.000	0.000
112	A	112	LEU	0	0.047	0.000	41.107	-0.002	-0.002	0.000	0.000	0.000	0.000
113	A	113	GLU	-1	-0.927	-0.945	43.023	-0.044	-0.044	0.000	0.000	0.000	0.000
114	A	114	ALA	0	0.057	0.045	40.248	-0.001	-0.001	0.000	0.000	0.000	0.000
115	A	115	VAL	0	-0.033	-0.022	38.141	-0.003	-0.003	0.000	0.000	0.000	0.000
116	A	116	GLU	-1	-0.917	-0.956	40.330	-0.042	-0.042	0.000	0.000	0.000	0.000
117	A	117	ASP	-1	-0.861	-0.942	42.667	-0.055	-0.055	0.000	0.000	0.000	0.000
118	A	118	PHE	0	-0.083	-0.047	34.369	-0.004	-0.004	0.000	0.000	0.000	0.000
119	A	119	ILE	0	0.015	0.003	38.671	-0.002	-0.002	0.000	0.000	0.000	0.000
120	A	120	ASN	0	-0.022	-0.001	40.978	0.000	0.000	0.000	0.000	0.000	0.000
121	A	121	LYS	1	0.956	0.984	38.055	0.079	0.079	0.000	0.000	0.000	0.000
122	A	122	THR	0	-0.080	-0.038	36.496	-0.003	-0.003	0.000	0.000	0.000	0.000
123	A	123	SER	0	0.046	0.011	39.461	0.000	0.000	0.000	0.000	0.000	0.000
124	A	124	PRO	0	-0.039	-0.009	41.670	0.003	0.003	0.000	0.000	0.000	0.000
125	A	125	TYR	0	-0.037	-0.022	37.208	0.000	0.000	0.000	0.000	0.000	0.000
126	A	126	ALA	0	0.022	0.003	36.308	-0.002	-0.002	0.000	0.000	0.000	0.000
127	A	127	GLN	0	-0.059	-0.016	38.411	0.002	0.002	0.000	0.000	0.000	0.000
128	A	128	THR	0	0.027	0.012	36.827	-0.002	-0.002	0.000	0.000	0.000	0.000
129	A	129	VAL	0	0.011	0.025	37.923	0.004	0.004	0.000	0.000	0.000	0.000
130	A	130	THR	0	0.012	0.003	37.410	-0.004	-0.004	0.000	0.000	0.000	0.000
131	A	131	HIS	0	-0.054	-0.033	35.689	0.006	0.006	0.000	0.000	0.000	0.000
132	A	132	VAL	0	0.045	0.001	36.351	-0.004	-0.004	0.000	0.000	0.000	0.000
133	A	133	ILE	0	-0.043	-0.017	31.816	0.004	0.004	0.000	0.000	0.000	0.000
134	A	134	PHE	0	-0.019	-0.009	35.986	0.000	0.000	0.000	0.000	0.000	0.000
135	A	135	SER	0	-0.053	-0.035	35.295	0.000	0.000	0.000	0.000	0.000	0.000
136	A	136	GLU	-1	-0.944	-0.970	28.025	-0.042	-0.042	0.000	0.000	0.000	0.000
137	A	137	ILE	0	-0.022	-0.004	30.098	0.004	0.004	0.000	0.000	0.000	0.000
138	A	138	ASP	-1	-0.870	-0.940	26.243	-0.001	-0.001	0.000	0.000	0.000	0.000
139	A	139	THR	0	-0.043	-0.029	24.972	0.006	0.006	0.000	0.000	0.000	0.000
140	A	140	LYS	1	0.855	0.952	21.977	0.049	0.049	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

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