FMO DATABASE

FMODB ID: 39Z8L

Calculation Name: 3CNW-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3CNW

Chain ID: A

ChEMBL ID:

UniProt ID: Q81AY6

Base Structure: X-ray

Registration Date: 2023-06-22

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	142
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1316820.122836
FMO2-HF: Nuclear repulsion	1260811.595982
FMO2-HF: Total energy	-56008.526853
FMO2-MP2: Total energy	-56173.562785

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:3:MET)

Summations of interaction energy for fragment #1(A:3: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.
-20.163	-9.674	7.102	-6.235	-11.352	-0.041

Interaction energy analysis for fragmet #1(A:3:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.051 / q_NPA : -0.019

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	5	HIS	0	0.026	-0.003	2.666	-1.662	1.403	0.325	-1.494	-1.896	0.002
4	A	6	THR	0	-0.031	-0.004	6.026	0.252	0.252	0.000	0.000	0.000	0.000
5	A	7	THR	0	0.009	-0.010	9.613	0.218	0.218	0.000	0.000	0.000	0.000
6	A	8	THR	0	-0.004	0.012	12.666	-0.048	-0.048	0.000	0.000	0.000	0.000
7	A	9	SER	0	0.018	-0.002	16.269	0.032	0.032	0.000	0.000	0.000	0.000
8	A	10	MET	0	-0.041	-0.013	19.375	-0.014	-0.014	0.000	0.000	0.000	0.000
9	A	11	GLU	-1	-0.875	-0.927	22.877	-0.142	-0.142	0.000	0.000	0.000	0.000
10	A	12	ILE	0	-0.006	-0.005	24.374	-0.011	-0.011	0.000	0.000	0.000	0.000
11	A	13	PHE	0	0.023	0.001	28.302	0.012	0.012	0.000	0.000	0.000	0.000
12	A	14	GLY	0	0.081	0.026	31.115	0.002	0.002	0.000	0.000	0.000	0.000
13	A	15	SER	0	-0.007	0.013	30.203	-0.004	-0.004	0.000	0.000	0.000	0.000
14	A	16	PRO	0	0.056	0.017	26.802	-0.006	-0.006	0.000	0.000	0.000	0.000
15	A	17	GLU	-1	-0.833	-0.926	27.311	-0.013	-0.013	0.000	0.000	0.000	0.000
16	A	18	GLN	0	-0.029	-0.002	29.314	-0.001	-0.001	0.000	0.000	0.000	0.000
17	A	19	VAL	0	0.035	0.013	24.951	-0.002	-0.002	0.000	0.000	0.000	0.000
18	A	20	TRP	0	0.013	0.003	20.239	-0.016	-0.016	0.000	0.000	0.000	0.000
19	A	21	GLN	0	-0.059	-0.028	25.647	0.006	0.006	0.000	0.000	0.000	0.000
20	A	22	LEU	0	-0.045	-0.005	26.815	0.002	0.002	0.000	0.000	0.000	0.000
21	A	23	ILE	0	0.012	0.004	21.410	-0.008	-0.008	0.000	0.000	0.000	0.000
22	A	24	GLY	0	0.017	0.010	21.698	-0.010	-0.010	0.000	0.000	0.000	0.000
23	A	25	GLY	0	-0.006	0.002	21.907	0.019	0.019	0.000	0.000	0.000	0.000
24	A	26	PHE	0	-0.001	-0.013	15.657	-0.017	-0.017	0.000	0.000	0.000	0.000
25	A	27	ASN	0	-0.012	-0.024	20.477	-0.028	-0.028	0.000	0.000	0.000	0.000
26	A	28	SER	0	0.033	0.010	23.021	0.004	0.004	0.000	0.000	0.000	0.000
27	A	29	LEU	0	-0.011	0.022	18.041	-0.005	-0.005	0.000	0.000	0.000	0.000
28	A	30	PRO	0	0.017	0.012	22.609	-0.012	-0.012	0.000	0.000	0.000	0.000
29	A	31	ASP	-1	-0.939	-0.959	25.684	-0.115	-0.115	0.000	0.000	0.000	0.000
30	A	32	TRP	0	-0.047	-0.042	19.094	-0.008	-0.008	0.000	0.000	0.000	0.000
31	A	33	LEU	0	-0.047	0.003	18.824	-0.019	-0.019	0.000	0.000	0.000	0.000
32	A	34	PRO	0	-0.001	0.002	23.219	0.008	0.008	0.000	0.000	0.000	0.000
33	A	35	TYR	0	0.018	0.004	17.839	-0.007	-0.007	0.000	0.000	0.000	0.000
34	A	36	ILE	0	-0.030	-0.025	18.686	-0.011	-0.011	0.000	0.000	0.000	0.000
35	A	37	PRO	0	0.038	0.026	22.614	0.027	0.027	0.000	0.000	0.000	0.000
36	A	38	SER	0	-0.020	-0.009	24.965	0.029	0.029	0.000	0.000	0.000	0.000
37	A	39	SER	0	0.032	0.004	22.655	-0.024	-0.024	0.000	0.000	0.000	0.000
38	A	40	LYS	1	0.918	0.967	23.307	0.079	0.079	0.000	0.000	0.000	0.000
39	A	41	LEU	0	0.055	0.053	21.964	-0.004	-0.004	0.000	0.000	0.000	0.000
40	A	42	THR	0	-0.037	-0.040	22.012	0.001	0.001	0.000	0.000	0.000	0.000
41	A	43	GLU	-1	-0.820	-0.897	20.056	0.104	0.104	0.000	0.000	0.000	0.000
42	A	44	GLY	0	-0.027	-0.021	23.024	0.013	0.013	0.000	0.000	0.000	0.000
43	A	45	GLY	0	0.012	0.007	23.303	0.005	0.005	0.000	0.000	0.000	0.000
44	A	46	ARG	1	0.860	0.924	18.621	-0.117	-0.117	0.000	0.000	0.000	0.000
45	A	47	VAL	0	-0.015	0.008	17.446	0.000	0.000	0.000	0.000	0.000	0.000
46	A	48	ARG	1	0.810	0.896	15.346	0.250	0.250	0.000	0.000	0.000	0.000
47	A	49	HIS	0	-0.070	-0.045	18.678	-0.031	-0.031	0.000	0.000	0.000	0.000
48	A	50	LEU	0	-0.015	-0.021	17.448	0.017	0.017	0.000	0.000	0.000	0.000
49	A	51	ALA	0	0.021	0.024	21.092	-0.005	-0.005	0.000	0.000	0.000	0.000
50	A	52	ASN	0	0.025	0.012	19.602	0.029	0.029	0.000	0.000	0.000	0.000
51	A	53	PRO	0	-0.006	-0.014	22.145	0.028	0.028	0.000	0.000	0.000	0.000
52	A	54	ASP	-1	-0.975	-0.976	23.376	-0.319	-0.319	0.000	0.000	0.000	0.000
53	A	55	GLY	0	-0.058	-0.024	25.121	0.015	0.015	0.000	0.000	0.000	0.000
54	A	56	ASP	-1	-0.878	-0.924	20.331	-0.337	-0.337	0.000	0.000	0.000	0.000
55	A	57	THR	0	-0.092	-0.061	20.561	0.018	0.018	0.000	0.000	0.000	0.000
56	A	58	ILE	0	0.005	-0.005	15.226	-0.028	-0.028	0.000	0.000	0.000	0.000
57	A	59	ILE	0	-0.034	-0.012	16.438	0.043	0.043	0.000	0.000	0.000	0.000
58	A	60	GLU	-1	-0.781	-0.884	13.511	-0.450	-0.450	0.000	0.000	0.000	0.000
59	A	61	ARG	1	0.909	0.925	13.116	-0.066	-0.066	0.000	0.000	0.000	0.000
60	A	62	LEU	0	-0.051	-0.009	13.162	-0.011	-0.011	0.000	0.000	0.000	0.000
61	A	63	GLU	-1	-0.913	-0.937	10.022	0.296	0.296	0.000	0.000	0.000	0.000
62	A	64	VAL	0	-0.040	-0.030	12.909	0.054	0.054	0.000	0.000	0.000	0.000
63	A	65	PHE	0	0.020	0.014	15.434	-0.053	-0.053	0.000	0.000	0.000	0.000
64	A	66	ASN	0	-0.021	-0.010	18.632	0.003	0.003	0.000	0.000	0.000	0.000
65	A	67	ASP	-1	-0.848	-0.912	21.160	0.004	0.004	0.000	0.000	0.000	0.000
66	A	68	LYS	1	0.864	0.933	24.251	-0.044	-0.044	0.000	0.000	0.000	0.000
67	A	69	GLU	-1	-0.906	-0.948	20.899	0.169	0.169	0.000	0.000	0.000	0.000
68	A	70	ARG	1	0.813	0.907	21.664	0.010	0.010	0.000	0.000	0.000	0.000
69	A	71	TYR	0	0.013	-0.010	16.079	-0.008	-0.008	0.000	0.000	0.000	0.000
70	A	72	TYR	0	-0.036	-0.008	15.634	0.019	0.019	0.000	0.000	0.000	0.000
71	A	73	THR	0	-0.033	-0.021	10.191	-0.008	-0.008	0.000	0.000	0.000	0.000
72	A	74	TYR	0	0.018	0.001	11.354	0.082	0.082	0.000	0.000	0.000	0.000
73	A	75	SER	0	-0.005	-0.024	8.252	-0.120	-0.120	0.000	0.000	0.000	0.000
74	A	76	ILE	0	0.008	0.008	8.866	0.056	0.056	0.000	0.000	0.000	0.000
75	A	77	MET	0	-0.089	-0.039	10.267	0.046	0.046	0.000	0.000	0.000	0.000
76	A	78	ASN	0	-0.018	-0.027	13.011	0.014	0.014	0.000	0.000	0.000	0.000
77	A	79	ALA	0	0.009	0.017	13.377	0.013	0.013	0.000	0.000	0.000	0.000
78	A	80	PRO	0	0.040	0.034	14.869	-0.010	-0.010	0.000	0.000	0.000	0.000
79	A	81	PHE	0	-0.007	-0.010	11.926	-0.033	-0.033	0.000	0.000	0.000	0.000
80	A	82	PRO	0	0.049	0.042	11.785	0.029	0.029	0.000	0.000	0.000	0.000
81	A	83	VAL	0	-0.017	-0.009	6.821	-0.296	-0.296	0.000	0.000	0.000	0.000
82	A	84	THR	0	-0.002	0.003	5.394	0.502	0.502	0.000	0.000	0.000	0.000
83	A	85	ASN	0	-0.033	-0.019	2.174	-1.269	-1.246	2.160	-0.676	-1.506	-0.001
84	A	86	TYR	0	0.009	0.022	2.938	-2.197	-1.147	0.321	-0.590	-0.782	-0.006
85	A	87	LEU	0	0.008	-0.006	4.407	0.518	0.664	-0.001	-0.006	-0.138	0.000
86	A	88	SER	0	-0.031	-0.008	6.284	-0.195	-0.195	0.000	0.000	0.000	0.000
87	A	89	THR	0	-0.006	-0.002	9.613	0.159	0.159	0.000	0.000	0.000	0.000
88	A	90	ILE	0	0.024	0.030	12.516	-0.074	-0.074	0.000	0.000	0.000	0.000
89	A	91	GLN	0	0.008	-0.007	16.089	0.049	0.049	0.000	0.000	0.000	0.000
90	A	92	VAL	0	-0.016	0.008	18.670	-0.038	-0.038	0.000	0.000	0.000	0.000
91	A	93	LYS	1	0.815	0.893	17.559	0.135	0.135	0.000	0.000	0.000	0.000
92	A	94	GLU	-1	-0.935	-0.980	23.669	-0.024	-0.024	0.000	0.000	0.000	0.000
93	A	95	GLY	0	0.033	0.020	26.434	-0.012	-0.012	0.000	0.000	0.000	0.000
94	A	96	THR	0	-0.087	-0.039	28.440	0.014	0.014	0.000	0.000	0.000	0.000
95	A	97	GLU	-1	-0.915	-0.953	31.090	-0.064	-0.064	0.000	0.000	0.000	0.000
96	A	98	SER	0	-0.056	-0.024	32.532	-0.002	-0.002	0.000	0.000	0.000	0.000
97	A	99	ASN	0	-0.039	-0.043	33.897	0.004	0.004	0.000	0.000	0.000	0.000
98	A	100	THR	0	-0.027	0.007	30.599	-0.005	-0.005	0.000	0.000	0.000	0.000
99	A	101	SER	0	-0.016	-0.019	26.356	0.008	0.008	0.000	0.000	0.000	0.000
100	A	102	LEU	0	0.022	0.020	21.667	-0.020	-0.020	0.000	0.000	0.000	0.000
101	A	103	VAL	0	-0.016	0.002	19.890	0.020	0.020	0.000	0.000	0.000	0.000
102	A	104	GLU	-1	-0.833	-0.916	16.414	-0.224	-0.224	0.000	0.000	0.000	0.000
103	A	105	TRP	0	0.019	0.013	13.301	0.056	0.056	0.000	0.000	0.000	0.000
104	A	106	SER	0	-0.003	-0.004	10.526	-0.052	-0.052	0.000	0.000	0.000	0.000
105	A	107	GLY	0	0.028	0.016	8.145	0.153	0.153	0.000	0.000	0.000	0.000
106	A	108	THR	0	-0.028	-0.021	2.288	-0.269	-0.062	2.027	-0.451	-1.783	-0.001
107	A	109	PHE	0	0.020	-0.005	2.918	-0.879	0.512	0.230	-0.459	-1.161	-0.003
108	A	110	THR	0	-0.015	-0.015	2.611	-8.704	-4.457	2.031	-2.492	-3.785	-0.032
109	A	111	PRO	0	0.004	0.007	3.662	0.624	0.949	0.010	-0.062	-0.273	0.000
110	A	112	VAL	0	-0.030	-0.029	6.535	0.343	0.343	0.000	0.000	0.000	0.000
111	A	113	GLU	-1	-0.950	-0.984	9.607	-0.457	-0.457	0.000	0.000	0.000	0.000
112	A	114	VAL	0	-0.035	-0.006	9.744	0.068	0.068	0.000	0.000	0.000	0.000
113	A	115	SER	0	-0.040	-0.048	9.713	-0.169	-0.169	0.000	0.000	0.000	0.000
114	A	116	ASP	-1	-0.840	-0.951	4.950	-4.810	-4.775	-0.001	-0.005	-0.028	0.000
115	A	117	GLU	-1	-0.916	-0.964	7.876	-1.719	-1.719	0.000	0.000	0.000	0.000
116	A	118	GLU	-1	-0.855	-0.885	11.230	-0.845	-0.845	0.000	0.000	0.000	0.000
117	A	119	ALA	0	0.000	0.009	7.905	0.115	0.115	0.000	0.000	0.000	0.000
118	A	120	ILE	0	-0.021	-0.018	7.578	0.105	0.105	0.000	0.000	0.000	0.000
119	A	121	ASN	0	-0.066	-0.047	10.445	0.307	0.307	0.000	0.000	0.000	0.000
120	A	122	LEU	0	0.001	0.024	12.822	0.134	0.134	0.000	0.000	0.000	0.000
121	A	123	PHE	0	0.053	0.011	9.784	0.143	0.143	0.000	0.000	0.000	0.000
122	A	124	HIS	0	-0.038	0.002	12.925	0.236	0.236	0.000	0.000	0.000	0.000
123	A	125	GLY	0	0.009	0.004	14.334	0.124	0.124	0.000	0.000	0.000	0.000
124	A	126	ILE	0	-0.017	-0.005	14.684	0.091	0.091	0.000	0.000	0.000	0.000
125	A	127	TYR	0	-0.007	-0.017	10.435	0.006	0.006	0.000	0.000	0.000	0.000
126	A	128	SER	0	0.008	-0.009	16.768	0.083	0.083	0.000	0.000	0.000	0.000
127	A	129	ASP	-1	-0.897	-0.955	19.566	-0.310	-0.310	0.000	0.000	0.000	0.000
128	A	130	GLY	0	0.049	0.007	20.283	0.045	0.045	0.000	0.000	0.000	0.000
129	A	131	LEU	0	-0.010	-0.019	18.299	0.041	0.041	0.000	0.000	0.000	0.000
130	A	132	LYS	1	0.826	0.917	22.068	0.293	0.293	0.000	0.000	0.000	0.000
131	A	133	ALA	0	0.028	0.014	24.755	0.028	0.028	0.000	0.000	0.000	0.000
132	A	134	LEU	0	0.020	0.018	23.353	0.025	0.025	0.000	0.000	0.000	0.000
133	A	135	GLN	0	-0.036	-0.028	26.209	0.011	0.011	0.000	0.000	0.000	0.000
134	A	136	GLN	0	-0.038	-0.031	28.026	0.005	0.005	0.000	0.000	0.000	0.000
135	A	137	ALA	0	0.032	0.024	29.493	0.013	0.013	0.000	0.000	0.000	0.000
136	A	138	PHE	0	-0.016	-0.017	28.596	0.014	0.014	0.000	0.000	0.000	0.000
137	A	139	LEU	0	-0.070	-0.020	32.270	0.009	0.009	0.000	0.000	0.000	0.000
138	A	140	ASP	-1	-0.939	-0.940	34.168	-0.131	-0.131	0.000	0.000	0.000	0.000
139	A	141	LEU	0	-0.040	-0.030	36.439	0.008	0.008	0.000	0.000	0.000	0.000
140	A	142	GLU	-1	-0.958	-0.983	38.232	-0.081	-0.081	0.000	0.000	0.000	0.000
141	A	143	HIS	0	-0.024	-0.022	41.455	0.008	0.008	0.000	0.000	0.000	0.000
142	A	144	HIS	0	-0.094	-0.029	42.543	0.005	0.005	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:MET)