FMO DATABASE

FMODB ID: 16NYZ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1151250.906264
FMO2-HF: Nuclear repulsion	1094646.138072
FMO2-HF: Total energy	-56604.768192
FMO2-MP2: Total energy	-56768.542275

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.
-10.72	-8.585	23.253	-7.06	-18.329	-0.059

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 : -0.030 / 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	0.071	0.033	3.315	-2.354	0.707	0.393	-1.200	-2.255	0.001
4	A	4	ASP	-1	-0.842	-0.893	4.941	0.184	0.286	0.001	-0.017	-0.086	0.000
5	A	5	GLN	0	0.067	0.017	7.847	0.105	0.105	0.000	0.000	0.000	0.000
6	A	6	ILE	0	-0.028	-0.014	9.804	-0.077	-0.077	0.000	0.000	0.000	0.000
7	A	7	ASP	-1	-0.784	-0.900	4.930	3.190	3.496	0.001	-0.056	-0.252	0.000
8	A	8	LEU	0	-0.011	-0.005	7.652	-0.295	-0.295	0.000	0.000	0.000	0.000
9	A	9	ASN	0	0.024	0.019	10.248	-0.173	-0.173	0.000	0.000	0.000	0.000
10	A	10	ILE	0	0.020	0.013	8.751	-0.106	-0.106	0.000	0.000	0.000	0.000
11	A	11	ILE	0	-0.007	-0.001	6.489	-0.160	-0.160	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.910	-0.950	10.613	0.054	0.054	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.891	-0.945	13.895	0.061	0.061	0.000	0.000	0.000	0.000
14	A	14	LEU	0	-0.014	-0.018	10.444	-0.038	-0.038	0.000	0.000	0.000	0.000
15	A	15	LYS	1	0.890	0.944	12.724	0.015	0.015	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.775	0.886	15.503	-0.115	-0.115	0.000	0.000	0.000	0.000
17	A	17	ASP	-1	-0.819	-0.917	17.388	-0.068	-0.068	0.000	0.000	0.000	0.000
18	A	18	SER	0	-0.014	0.012	15.168	0.008	0.008	0.000	0.000	0.000	0.000
19	A	19	ARG	1	0.860	0.916	16.269	0.044	0.044	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.042	0.000	16.334	0.004	0.004	0.000	0.000	0.000	0.000
21	A	21	SER	0	0.002	0.007	16.558	-0.009	-0.009	0.000	0.000	0.000	0.000
22	A	22	MET	0	0.089	0.027	12.868	0.032	0.032	0.000	0.000	0.000	0.000
23	A	23	ARG	1	0.926	0.977	15.989	0.064	0.064	0.000	0.000	0.000	0.000
24	A	24	GLU	-1	-0.902	-0.969	19.334	-0.006	-0.006	0.000	0.000	0.000	0.000
25	A	25	LEU	0	0.050	0.041	11.936	0.012	0.012	0.000	0.000	0.000	0.000
26	A	26	GLY	0	0.022	0.009	16.166	0.036	0.036	0.000	0.000	0.000	0.000
27	A	27	ARG	1	0.912	0.957	17.052	-0.038	-0.038	0.000	0.000	0.000	0.000
28	A	28	LYS	1	0.935	0.962	18.009	-0.048	-0.048	0.000	0.000	0.000	0.000
29	A	29	ILE	0	0.051	0.032	12.478	0.004	0.004	0.000	0.000	0.000	0.000
30	A	30	LYS	1	0.801	0.921	16.438	-0.106	-0.106	0.000	0.000	0.000	0.000
31	A	31	LEU	0	0.035	0.018	11.313	0.027	0.027	0.000	0.000	0.000	0.000
32	A	32	SER	0	0.002	0.000	16.024	-0.025	-0.025	0.000	0.000	0.000	0.000
33	A	33	PRO	0	0.046	0.004	15.498	0.022	0.022	0.000	0.000	0.000	0.000
34	A	34	PRO	0	0.027	0.004	14.982	-0.011	-0.011	0.000	0.000	0.000	0.000
35	A	35	SER	0	0.013	0.008	12.084	0.021	0.021	0.000	0.000	0.000	0.000
36	A	36	VAL	0	0.026	0.016	10.696	0.100	0.100	0.000	0.000	0.000	0.000
37	A	37	THR	0	-0.038	-0.033	10.456	0.020	0.020	0.000	0.000	0.000	0.000
38	A	38	GLU	-1	-0.844	-0.909	7.308	-0.450	-0.450	0.000	0.000	0.000	0.000
39	A	39	ARG	1	0.811	0.881	6.399	-1.479	-1.479	0.000	0.000	0.000	0.000
40	A	40	VAL	0	-0.002	-0.011	5.741	0.119	0.119	0.000	0.000	0.000	0.000
41	A	41	ARG	1	0.881	0.930	6.937	0.565	0.565	0.000	0.000	0.000	0.000
42	A	42	GLN	0	0.038	0.008	2.459	-3.305	-1.511	0.800	-0.603	-1.990	-0.006
43	A	43	LEU	0	0.034	0.006	2.307	-4.269	-2.845	2.739	-1.290	-2.873	-0.013
44	A	44	GLU	-1	-0.786	-0.841	3.285	-0.398	-0.710	-0.001	0.440	-0.127	0.000
45	A	45	SER	0	-0.121	-0.039	4.681	-0.005	0.054	-0.001	-0.006	-0.051	0.000
46	A	46	PHE	0	0.014	-0.007	1.994	-4.466	-5.968	13.786	-3.918	-8.367	-0.037
47	A	47	GLY	0	-0.024	0.011	4.261	0.203	0.313	-0.001	-0.021	-0.088	0.000
48	A	48	ILE	0	-0.042	-0.025	2.100	1.682	-1.225	5.536	-0.389	-2.240	-0.004
49	A	49	ILE	0	-0.035	-0.009	5.518	0.428	0.428	0.000	0.000	0.000	0.000
50	A	50	LYS	1	0.956	0.965	7.950	0.432	0.432	0.000	0.000	0.000	0.000
51	A	51	GLN	0	-0.012	-0.022	10.714	0.006	0.006	0.000	0.000	0.000	0.000
52	A	52	TYR	0	-0.072	-0.056	10.393	0.051	0.051	0.000	0.000	0.000	0.000
53	A	53	THR	0	0.007	-0.013	15.159	0.009	0.009	0.000	0.000	0.000	0.000
54	A	54	LEU	0	-0.037	-0.028	18.336	0.019	0.019	0.000	0.000	0.000	0.000
55	A	55	GLU	-1	-0.874	-0.928	21.427	-0.097	-0.097	0.000	0.000	0.000	0.000
56	A	56	VAL	0	-0.050	-0.013	23.596	0.010	0.010	0.000	0.000	0.000	0.000
57	A	57	ASP	-1	-0.831	-0.933	27.241	-0.063	-0.063	0.000	0.000	0.000	0.000
58	A	58	GLN	0	0.071	0.023	27.807	0.004	0.004	0.000	0.000	0.000	0.000
59	A	59	LYS	1	0.996	1.002	31.922	0.054	0.054	0.000	0.000	0.000	0.000
60	A	60	LYS	1	0.825	0.910	33.891	0.057	0.057	0.000	0.000	0.000	0.000
61	A	61	LEU	0	-0.022	-0.006	30.190	0.001	0.001	0.000	0.000	0.000	0.000
62	A	62	GLY	0	-0.011	0.010	34.609	-0.001	-0.001	0.000	0.000	0.000	0.000
63	A	63	LEU	0	-0.023	0.001	32.449	0.001	0.001	0.000	0.000	0.000	0.000
64	A	64	PRO	0	-0.056	-0.038	34.761	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	65	VAL	0	-0.027	0.000	37.035	0.004	0.004	0.000	0.000	0.000	0.000
66	A	66	SER	0	0.056	0.034	32.444	-0.007	-0.007	0.000	0.000	0.000	0.000
67	A	67	CYS	0	-0.054	-0.009	33.711	0.008	0.008	0.000	0.000	0.000	0.000
68	A	68	ILE	0	-0.005	-0.007	29.579	-0.008	-0.008	0.000	0.000	0.000	0.000
69	A	69	VAL	0	-0.022	-0.011	32.320	0.006	0.006	0.000	0.000	0.000	0.000
70	A	70	GLU	-1	-0.867	-0.940	32.513	-0.081	-0.081	0.000	0.000	0.000	0.000
71	A	71	ALA	0	0.002	-0.010	33.240	0.004	0.004	0.000	0.000	0.000	0.000
72	A	72	THR	0	-0.025	-0.019	34.109	-0.003	-0.003	0.000	0.000	0.000	0.000
73	A	73	VAL	0	0.028	0.008	33.207	0.003	0.003	0.000	0.000	0.000	0.000
74	A	74	LYS	1	0.872	0.917	36.329	0.075	0.075	0.000	0.000	0.000	0.000
75	A	75	ASN	0	-0.008	-0.005	38.847	-0.006	-0.006	0.000	0.000	0.000	0.000
76	A	76	ALA	0	0.036	0.024	36.851	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	77	ASP	-1	-0.892	-0.951	35.944	-0.107	-0.107	0.000	0.000	0.000	0.000
78	A	78	TYR	0	-0.020	-0.033	30.629	-0.002	-0.002	0.000	0.000	0.000	0.000
79	A	79	GLU	-1	-0.915	-0.964	28.933	-0.178	-0.178	0.000	0.000	0.000	0.000
80	A	80	ARG	1	0.877	0.940	32.147	0.084	0.084	0.000	0.000	0.000	0.000
81	A	81	PHE	0	0.017	0.009	30.490	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	82	LYS	1	0.971	0.981	24.506	0.221	0.221	0.000	0.000	0.000	0.000
83	A	83	SER	0	-0.006	-0.009	30.072	-0.007	-0.007	0.000	0.000	0.000	0.000
84	A	84	TYR	0	-0.013	-0.009	31.883	0.001	0.001	0.000	0.000	0.000	0.000
85	A	85	ILE	0	0.012	0.004	28.615	0.001	0.001	0.000	0.000	0.000	0.000
86	A	86	GLN	0	-0.010	-0.023	24.910	0.004	0.004	0.000	0.000	0.000	0.000
87	A	87	THR	0	-0.104	-0.029	29.184	-0.002	-0.002	0.000	0.000	0.000	0.000
88	A	88	LEU	0	-0.032	-0.020	31.137	0.010	0.010	0.000	0.000	0.000	0.000
89	A	89	PRO	0	-0.007	0.008	30.106	-0.011	-0.011	0.000	0.000	0.000	0.000
90	A	90	ASN	0	0.006	-0.011	29.906	0.000	0.000	0.000	0.000	0.000	0.000
91	A	91	ILE	0	0.013	0.020	27.849	0.008	0.008	0.000	0.000	0.000	0.000
92	A	92	GLU	-1	-0.882	-0.933	24.723	-0.143	-0.143	0.000	0.000	0.000	0.000
93	A	93	PHE	0	-0.001	-0.010	23.177	-0.017	-0.017	0.000	0.000	0.000	0.000
94	A	94	CYS	0	-0.011	-0.004	24.241	0.020	0.020	0.000	0.000	0.000	0.000
95	A	95	TYR	0	-0.043	-0.009	20.275	-0.029	-0.029	0.000	0.000	0.000	0.000
96	A	96	ARG	1	0.919	0.971	24.463	0.145	0.145	0.000	0.000	0.000	0.000
97	A	97	ILE	0	-0.044	-0.024	25.216	-0.009	-0.009	0.000	0.000	0.000	0.000
98	A	98	ALA	0	-0.022	0.000	26.885	0.004	0.004	0.000	0.000	0.000	0.000
99	A	99	GLY	0	0.012	-0.020	28.639	0.005	0.005	0.000	0.000	0.000	0.000
100	A	100	ALA	0	-0.023	0.002	32.215	0.000	0.000	0.000	0.000	0.000	0.000
101	A	101	ALA	0	0.033	0.029	33.514	0.001	0.001	0.000	0.000	0.000	0.000
102	A	102	CYM	-1	-0.845	-0.888	31.736	-0.103	-0.103	0.000	0.000	0.000	0.000
103	A	103	TYR	0	0.005	-0.034	27.127	-0.012	-0.012	0.000	0.000	0.000	0.000
104	A	104	MET	0	0.015	0.031	28.149	0.012	0.012	0.000	0.000	0.000	0.000
105	A	105	LEU	0	0.015	-0.007	27.740	-0.016	-0.016	0.000	0.000	0.000	0.000
106	A	106	LYS	1	0.871	0.953	27.473	0.118	0.118	0.000	0.000	0.000	0.000
107	A	107	ILE	0	0.000	0.008	29.360	-0.008	-0.008	0.000	0.000	0.000	0.000
108	A	108	ASN	0	-0.032	-0.029	28.787	0.014	0.014	0.000	0.000	0.000	0.000
109	A	109	ALA	0	0.026	0.005	32.821	-0.003	-0.003	0.000	0.000	0.000	0.000
110	A	110	GLU	-1	-0.845	-0.927	36.412	-0.080	-0.080	0.000	0.000	0.000	0.000
111	A	111	SER	0	-0.027	-0.025	39.246	0.004	0.004	0.000	0.000	0.000	0.000
112	A	112	LEU	0	0.035	-0.008	40.752	-0.003	-0.003	0.000	0.000	0.000	0.000
113	A	113	GLU	-1	-0.924	-0.946	42.646	-0.054	-0.054	0.000	0.000	0.000	0.000
114	A	114	ALA	0	0.054	0.050	39.887	-0.001	-0.001	0.000	0.000	0.000	0.000
115	A	115	VAL	0	-0.040	-0.030	37.618	-0.004	-0.004	0.000	0.000	0.000	0.000
116	A	116	GLU	-1	-0.948	-0.970	39.921	-0.055	-0.055	0.000	0.000	0.000	0.000
117	A	117	ASP	-1	-0.849	-0.939	42.033	-0.065	-0.065	0.000	0.000	0.000	0.000
118	A	118	PHE	0	-0.065	-0.042	34.066	-0.004	-0.004	0.000	0.000	0.000	0.000
119	A	119	ILE	0	0.002	0.001	38.800	-0.003	-0.003	0.000	0.000	0.000	0.000
120	A	120	ASN	0	-0.008	-0.005	40.628	-0.001	-0.001	0.000	0.000	0.000	0.000
121	A	121	LYS	1	0.949	0.985	37.399	0.094	0.094	0.000	0.000	0.000	0.000
122	A	122	THR	0	-0.072	-0.030	36.533	-0.003	-0.003	0.000	0.000	0.000	0.000
123	A	123	SER	0	0.066	0.039	39.242	0.000	0.000	0.000	0.000	0.000	0.000
124	A	124	PRO	0	-0.062	-0.022	41.717	0.002	0.002	0.000	0.000	0.000	0.000
125	A	125	TYR	0	-0.037	-0.017	37.021	0.000	0.000	0.000	0.000	0.000	0.000
126	A	126	ALA	0	0.017	0.000	36.134	-0.004	-0.004	0.000	0.000	0.000	0.000
127	A	127	GLN	0	-0.054	-0.016	38.191	0.002	0.002	0.000	0.000	0.000	0.000
128	A	128	THR	0	0.010	0.002	36.719	-0.004	-0.004	0.000	0.000	0.000	0.000
129	A	129	VAL	0	0.029	0.036	37.678	0.005	0.005	0.000	0.000	0.000	0.000
130	A	130	THR	0	0.011	0.000	37.088	-0.006	-0.006	0.000	0.000	0.000	0.000
131	A	131	HIS	0	-0.036	-0.025	34.962	0.007	0.007	0.000	0.000	0.000	0.000
132	A	132	VAL	0	0.032	0.009	35.877	-0.005	-0.005	0.000	0.000	0.000	0.000
133	A	133	ILE	0	-0.028	-0.015	31.189	0.002	0.002	0.000	0.000	0.000	0.000
134	A	134	PHE	0	-0.022	-0.011	35.571	0.001	0.001	0.000	0.000	0.000	0.000
135	A	135	SER	0	-0.070	-0.041	34.971	0.003	0.003	0.000	0.000	0.000	0.000
136	A	136	GLU	-1	-0.932	-0.966	27.624	-0.076	-0.076	0.000	0.000	0.000	0.000
137	A	137	ILE	0	-0.017	0.001	29.368	0.005	0.005	0.000	0.000	0.000	0.000
138	A	138	ASP	-1	-0.885	-0.948	26.139	-0.037	-0.037	0.000	0.000	0.000	0.000
139	A	139	THR	0	-0.036	-0.022	24.421	0.006	0.006	0.000	0.000	0.000	0.000
140	A	140	LYS	1	0.907	0.973	21.599	0.079	0.079	0.000	0.000	0.000	0.000

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