FMO DATABASE

FMODB ID: K9643

Calculation Name: 3N77-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3N77

Chain ID: A

ChEMBL ID:

UniProt ID: Q8ZNF5

Base Structure: X-ray

Registration Date: 2023-09-20

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

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	141
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1312355.21058
FMO2-HF: Nuclear repulsion	1254864.927838
FMO2-HF: Total energy	-57490.282742
FMO2-MP2: Total energy	-57654.630455

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.
-8.581	-2.243	0.731	-3.171	-3.898	-0.01

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 : 0.028 / q_NPA : 0.023

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	GLN	0	0.036	-0.004	3.828	-1.402	0.926	-0.022	-1.216	-1.089	0.007
4	A	4	ARG	1	0.896	0.954	6.668	1.593	1.593	0.000	0.000	0.000	0.000
5	A	5	THR	0	0.041	0.020	10.026	-0.005	-0.005	0.000	0.000	0.000	0.000
6	A	6	ILE	0	-0.030	-0.006	13.260	-0.003	-0.003	0.000	0.000	0.000	0.000
7	A	7	VAL	0	-0.003	0.008	15.932	0.035	0.035	0.000	0.000	0.000	0.000
8	A	8	CYS	0	0.002	0.002	19.223	-0.013	-0.013	0.000	0.000	0.000	0.000
9	A	9	PRO	0	0.012	0.026	21.551	0.018	0.018	0.000	0.000	0.000	0.000
10	A	10	LEU	0	-0.005	-0.004	25.311	0.001	0.001	0.000	0.000	0.000	0.000
11	A	11	ILE	0	0.002	-0.002	27.214	0.012	0.012	0.000	0.000	0.000	0.000
12	A	12	GLN	0	-0.012	-0.006	30.504	0.012	0.012	0.000	0.000	0.000	0.000
13	A	13	ASN	0	0.042	0.020	33.706	0.004	0.004	0.000	0.000	0.000	0.000
14	A	14	ASP	-1	-0.934	-0.967	37.373	-0.080	-0.080	0.000	0.000	0.000	0.000
15	A	15	GLY	0	-0.005	0.008	38.001	0.003	0.003	0.000	0.000	0.000	0.000
16	A	16	CYS	0	-0.104	-0.045	36.121	0.002	0.002	0.000	0.000	0.000	0.000
17	A	17	TYR	0	0.035	-0.002	30.535	-0.004	-0.004	0.000	0.000	0.000	0.000
18	A	18	LEU	0	0.002	0.018	30.077	0.004	0.004	0.000	0.000	0.000	0.000
19	A	19	LEU	0	-0.056	-0.020	26.965	-0.011	-0.011	0.000	0.000	0.000	0.000
20	A	20	CYS	0	0.046	0.015	26.838	0.016	0.016	0.000	0.000	0.000	0.000
21	A	21	LYS	1	0.889	0.966	26.844	0.137	0.137	0.000	0.000	0.000	0.000
22	A	22	MET	0	0.007	-0.002	19.748	-0.005	-0.005	0.000	0.000	0.000	0.000
23	A	23	ALA	0	0.078	0.040	25.517	0.017	0.017	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.836	-0.935	25.193	-0.172	-0.172	0.000	0.000	0.000	0.000
25	A	25	ASN	0	-0.104	-0.047	23.921	0.005	0.005	0.000	0.000	0.000	0.000
26	A	26	ARG	1	0.889	0.964	20.883	0.258	0.258	0.000	0.000	0.000	0.000
27	A	27	GLY	0	0.023	0.018	18.255	0.014	0.014	0.000	0.000	0.000	0.000
28	A	28	VAL	0	-0.080	-0.051	15.464	-0.005	-0.005	0.000	0.000	0.000	0.000
29	A	29	PHE	0	-0.002	-0.002	18.482	0.029	0.029	0.000	0.000	0.000	0.000
30	A	30	PRO	0	0.029	0.027	22.055	-0.012	-0.012	0.000	0.000	0.000	0.000
31	A	31	GLY	0	0.043	0.029	24.366	0.016	0.016	0.000	0.000	0.000	0.000
32	A	32	GLN	0	-0.067	-0.034	21.629	-0.013	-0.013	0.000	0.000	0.000	0.000
33	A	33	TRP	0	-0.008	-0.013	25.264	-0.011	-0.011	0.000	0.000	0.000	0.000
34	A	34	ALA	0	-0.059	-0.046	22.249	-0.007	-0.007	0.000	0.000	0.000	0.000
35	A	35	LEU	0	-0.010	0.002	22.547	0.018	0.018	0.000	0.000	0.000	0.000
36	A	36	SER	0	0.028	0.024	22.657	-0.015	-0.015	0.000	0.000	0.000	0.000
37	A	37	GLY	0	-0.059	-0.053	20.812	0.000	0.000	0.000	0.000	0.000	0.000
38	A	38	GLY	0	0.090	0.065	18.527	-0.010	-0.010	0.000	0.000	0.000	0.000
39	A	39	GLY	0	-0.063	-0.028	16.628	-0.023	-0.023	0.000	0.000	0.000	0.000
40	A	40	VAL	0	-0.038	-0.019	16.899	0.059	0.059	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.931	-0.975	17.661	-0.574	-0.574	0.000	0.000	0.000	0.000
42	A	42	PRO	0	-0.041	-0.040	17.888	0.028	0.028	0.000	0.000	0.000	0.000
43	A	43	GLY	0	-0.032	-0.018	20.194	0.023	0.023	0.000	0.000	0.000	0.000
44	A	44	GLU	-1	-0.763	-0.829	22.167	-0.330	-0.330	0.000	0.000	0.000	0.000
45	A	45	ARG	1	0.880	0.934	22.477	0.180	0.180	0.000	0.000	0.000	0.000
46	A	46	ILE	0	0.047	0.005	20.013	-0.003	-0.003	0.000	0.000	0.000	0.000
47	A	47	GLU	-1	-0.836	-0.908	22.673	-0.182	-0.182	0.000	0.000	0.000	0.000
48	A	48	GLU	-1	-0.901	-0.960	26.055	-0.215	-0.215	0.000	0.000	0.000	0.000
49	A	49	ALA	0	0.042	0.031	21.649	0.005	0.005	0.000	0.000	0.000	0.000
50	A	50	LEU	0	0.000	-0.005	23.541	0.001	0.001	0.000	0.000	0.000	0.000
51	A	51	ARG	1	0.846	0.904	24.784	0.180	0.180	0.000	0.000	0.000	0.000
52	A	52	ARG	1	0.725	0.856	21.698	0.371	0.371	0.000	0.000	0.000	0.000
53	A	53	GLU	-1	-0.796	-0.910	21.383	-0.390	-0.390	0.000	0.000	0.000	0.000
54	A	54	ILE	0	-0.023	-0.009	25.397	0.011	0.011	0.000	0.000	0.000	0.000
55	A	55	ARG	1	0.913	0.962	28.219	0.208	0.208	0.000	0.000	0.000	0.000
56	A	56	GLU	-1	-0.918	-0.950	25.098	-0.295	-0.295	0.000	0.000	0.000	0.000
57	A	57	GLU	-1	-0.811	-0.914	23.228	-0.306	-0.306	0.000	0.000	0.000	0.000
58	A	58	LEU	0	-0.062	-0.044	28.007	0.013	0.013	0.000	0.000	0.000	0.000
59	A	59	GLY	0	0.073	0.051	31.041	0.015	0.015	0.000	0.000	0.000	0.000
60	A	60	GLU	-1	-0.954	-1.004	33.643	-0.167	-0.167	0.000	0.000	0.000	0.000
61	A	61	GLN	0	-0.052	-0.021	35.794	0.010	0.010	0.000	0.000	0.000	0.000
62	A	62	LEU	0	0.019	0.040	32.308	0.008	0.008	0.000	0.000	0.000	0.000
63	A	63	ILE	0	-0.022	-0.012	35.586	-0.005	-0.005	0.000	0.000	0.000	0.000
64	A	64	LEU	0	-0.007	-0.020	31.133	0.003	0.003	0.000	0.000	0.000	0.000
65	A	65	SER	0	-0.080	-0.037	35.406	0.005	0.005	0.000	0.000	0.000	0.000
66	A	66	ASP	-1	-0.865	-0.948	34.721	-0.121	-0.121	0.000	0.000	0.000	0.000
67	A	67	ILE	0	-0.058	-0.030	28.323	-0.007	-0.007	0.000	0.000	0.000	0.000
68	A	68	THR	0	-0.001	0.004	29.910	0.008	0.008	0.000	0.000	0.000	0.000
69	A	69	PRO	0	-0.032	-0.007	25.137	-0.007	-0.007	0.000	0.000	0.000	0.000
70	A	70	TRP	0	0.036	0.020	23.994	0.013	0.013	0.000	0.000	0.000	0.000
71	A	71	THR	0	-0.022	-0.019	21.606	0.011	0.011	0.000	0.000	0.000	0.000
72	A	72	PHE	0	-0.023	-0.006	16.712	-0.025	-0.025	0.000	0.000	0.000	0.000
73	A	73	ARG	1	0.812	0.896	15.363	0.378	0.378	0.000	0.000	0.000	0.000
74	A	74	ASP	-1	-0.816	-0.824	11.285	-0.417	-0.417	0.000	0.000	0.000	0.000
75	A	75	ASP	-1	-0.762	-0.869	10.879	-0.260	-0.260	0.000	0.000	0.000	0.000
76	A	76	ILE	0	-0.021	0.008	6.044	-0.250	-0.250	0.000	0.000	0.000	0.000
77	A	77	ARG	1	0.921	0.966	7.687	0.843	0.843	0.000	0.000	0.000	0.000
78	A	78	ILE	0	0.032	0.016	7.198	-0.275	-0.275	0.000	0.000	0.000	0.000
79	A	79	LYS	1	0.799	0.903	6.550	1.633	1.633	0.000	0.000	0.000	0.000
80	A	80	THR	0	0.032	0.000	8.634	0.115	0.115	0.000	0.000	0.000	0.000
81	A	81	TYR	0	-0.043	-0.026	6.925	-0.032	-0.032	0.000	0.000	0.000	0.000
82	A	82	ALA	0	0.018	-0.002	12.588	0.050	0.050	0.000	0.000	0.000	0.000
83	A	83	ASP	-1	-0.847	-0.903	14.123	0.008	0.008	0.000	0.000	0.000	0.000
84	A	84	GLY	0	0.006	0.006	14.726	0.044	0.044	0.000	0.000	0.000	0.000
85	A	85	ARG	1	0.875	0.924	10.140	-0.049	-0.049	0.000	0.000	0.000	0.000
86	A	86	GLN	0	-0.010	-0.005	8.270	-0.044	-0.044	0.000	0.000	0.000	0.000
87	A	87	GLU	-1	-0.850	-0.919	2.804	-3.786	-3.188	0.099	-0.212	-0.485	-0.001
88	A	88	GLU	-1	-0.893	-0.941	3.102	-0.500	0.524	0.055	-0.255	-0.825	0.000
89	A	89	ILE	0	-0.081	-0.069	2.815	-4.855	-2.625	0.600	-1.478	-1.352	-0.016
90	A	90	TYR	0	-0.097	-0.125	4.573	0.483	0.641	-0.001	-0.010	-0.147	0.000
91	A	91	MET	0	-0.036	-0.007	6.033	-0.213	-0.213	0.000	0.000	0.000	0.000
92	A	92	ILE	0	0.071	0.035	9.687	0.152	0.152	0.000	0.000	0.000	0.000
93	A	93	TYR	0	-0.032	-0.031	12.523	-0.039	-0.039	0.000	0.000	0.000	0.000
94	A	94	LEU	0	-0.009	-0.014	15.976	0.050	0.050	0.000	0.000	0.000	0.000
95	A	95	ILE	0	0.001	0.002	19.081	-0.003	-0.003	0.000	0.000	0.000	0.000
96	A	96	PHE	0	0.019	0.000	22.058	0.020	0.020	0.000	0.000	0.000	0.000
97	A	97	ASP	-1	-0.813	-0.903	25.542	-0.147	-0.147	0.000	0.000	0.000	0.000
98	A	98	CYS	0	-0.034	-0.017	28.414	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	99	VAL	0	0.026	0.027	30.916	0.004	0.004	0.000	0.000	0.000	0.000
100	A	100	SER	0	0.012	0.007	34.548	-0.003	-0.003	0.000	0.000	0.000	0.000
101	A	101	ALA	0	-0.017	-0.013	36.038	0.007	0.007	0.000	0.000	0.000	0.000
102	A	102	ASN	0	-0.050	-0.023	38.596	0.002	0.002	0.000	0.000	0.000	0.000
103	A	103	ARG	1	0.871	0.897	37.534	0.095	0.095	0.000	0.000	0.000	0.000
104	A	104	ASP	-1	-0.901	-0.934	37.950	-0.108	-0.108	0.000	0.000	0.000	0.000
105	A	105	ILE	0	-0.010	0.003	32.786	-0.006	-0.006	0.000	0.000	0.000	0.000
106	A	106	CYS	0	-0.101	-0.060	34.452	0.008	0.008	0.000	0.000	0.000	0.000
107	A	107	ILE	0	-0.013	0.012	30.622	-0.007	-0.007	0.000	0.000	0.000	0.000
108	A	108	ASN	0	0.054	0.028	25.807	0.013	0.013	0.000	0.000	0.000	0.000
109	A	109	ASP	-1	-0.894	-0.961	26.171	-0.256	-0.256	0.000	0.000	0.000	0.000
110	A	110	GLU	-1	-0.968	-0.981	23.054	-0.347	-0.347	0.000	0.000	0.000	0.000
111	A	111	PHE	0	-0.028	-0.033	24.305	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	112	GLN	0	-0.119	-0.081	27.917	0.018	0.018	0.000	0.000	0.000	0.000
113	A	113	ASP	-1	-0.886	-0.948	30.739	-0.117	-0.117	0.000	0.000	0.000	0.000
114	A	114	TYR	0	-0.024	-0.011	30.945	-0.013	-0.013	0.000	0.000	0.000	0.000
115	A	115	ALA	0	0.003	0.009	32.541	0.011	0.011	0.000	0.000	0.000	0.000
116	A	116	TRP	0	0.019	0.008	33.211	-0.007	-0.007	0.000	0.000	0.000	0.000
117	A	117	VAL	0	-0.023	-0.012	32.631	0.009	0.009	0.000	0.000	0.000	0.000
118	A	118	ALA	0	0.058	0.027	34.733	-0.001	-0.001	0.000	0.000	0.000	0.000
119	A	119	PRO	0	0.052	-0.003	33.701	-0.002	-0.002	0.000	0.000	0.000	0.000
120	A	120	ALA	0	-0.003	-0.001	33.704	-0.001	-0.001	0.000	0.000	0.000	0.000
121	A	121	ALA	0	-0.011	0.002	35.095	0.003	0.003	0.000	0.000	0.000	0.000
122	A	122	LEU	0	0.016	0.016	29.633	-0.003	-0.003	0.000	0.000	0.000	0.000
123	A	123	ALA	0	-0.016	-0.007	29.144	-0.007	-0.007	0.000	0.000	0.000	0.000
124	A	124	LEU	0	-0.006	-0.014	29.712	0.000	0.000	0.000	0.000	0.000	0.000
125	A	125	TYR	0	0.008	0.024	29.302	0.004	0.004	0.000	0.000	0.000	0.000
126	A	126	ASP	-1	-0.871	-0.928	26.188	-0.148	-0.148	0.000	0.000	0.000	0.000
127	A	127	LEU	0	-0.043	-0.017	24.212	-0.015	-0.015	0.000	0.000	0.000	0.000
128	A	128	ASN	0	0.048	0.039	19.856	0.007	0.007	0.000	0.000	0.000	0.000
129	A	129	VAL	0	0.022	-0.006	16.558	0.005	0.005	0.000	0.000	0.000	0.000
130	A	130	ALA	0	-0.020	-0.005	16.367	0.008	0.008	0.000	0.000	0.000	0.000
131	A	131	THR	0	0.066	0.022	17.889	0.010	0.010	0.000	0.000	0.000	0.000
132	A	132	ARG	1	0.866	0.933	21.599	0.151	0.151	0.000	0.000	0.000	0.000
133	A	133	HIS	0	-0.028	-0.030	16.119	0.052	0.052	0.000	0.000	0.000	0.000
134	A	134	THR	0	0.014	0.008	20.152	0.010	0.010	0.000	0.000	0.000	0.000
135	A	135	LEU	0	0.038	0.009	21.712	0.017	0.017	0.000	0.000	0.000	0.000
136	A	136	ALA	0	-0.034	-0.018	23.304	0.016	0.016	0.000	0.000	0.000	0.000
137	A	137	LEU	0	-0.018	0.004	20.664	0.014	0.014	0.000	0.000	0.000	0.000
138	A	138	LYS	1	0.814	0.908	24.328	0.143	0.143	0.000	0.000	0.000	0.000
139	A	139	GLY	0	-0.017	0.002	27.184	0.009	0.009	0.000	0.000	0.000	0.000
140	A	140	LEU	0	-0.039	-0.019	28.812	0.007	0.007	0.000	0.000	0.000	0.000
141	A	141	LEU	0	-0.059	-0.010	25.799	0.006	0.006	0.000	0.000	0.000	0.000

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