FMO DATABASE

FMODB ID: KG443

Calculation Name: 1N0G-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1N0G

Chain ID: A

ChEMBL ID:

UniProt ID: P75467

Base Structure: X-ray

Registration Date: 2023-09-24

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	141
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1321496.191151
FMO2-HF: Nuclear repulsion	1264827.418402
FMO2-HF: Total energy	-56668.772749
FMO2-MP2: Total energy	-56836.541919

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:22:PHE)

Summations of interaction energy for fragment #1(A:22:PHE)

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.
-1.307	4.181	5.611	-3.759	-7.338	0.002

Interaction energy analysis for fragmet #1(A:22:PHE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.076 / q_NPA : 0.030

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	24	GLY	0	0.039	0.019	2.968	-0.576	1.978	0.024	-1.243	-1.334	0.002
4	A	25	HIS	0	-0.097	-0.054	2.496	0.228	2.140	0.606	-0.916	-1.602	0.001
5	A	26	MET	0	0.028	0.008	2.127	-1.378	-0.355	4.982	-1.597	-4.408	-0.001
6	A	27	LEU	0	-0.012	0.036	4.893	-0.112	-0.113	-0.001	-0.003	0.006	0.000
7	A	28	LEU	0	0.000	0.003	6.192	0.284	0.284	0.000	0.000	0.000	0.000
8	A	29	GLY	0	-0.001	-0.004	9.350	-0.072	-0.072	0.000	0.000	0.000	0.000
9	A	30	THR	0	0.055	0.024	12.108	0.026	0.026	0.000	0.000	0.000	0.000
10	A	31	PHE	0	-0.079	-0.045	11.207	-0.024	-0.024	0.000	0.000	0.000	0.000
11	A	32	ASN	0	0.033	0.024	17.132	0.035	0.035	0.000	0.000	0.000	0.000
12	A	33	ILE	0	-0.030	-0.005	19.128	-0.009	-0.009	0.000	0.000	0.000	0.000
13	A	34	THR	0	0.035	0.017	22.139	0.016	0.016	0.000	0.000	0.000	0.000
14	A	35	LEU	0	-0.004	0.039	25.010	-0.015	-0.015	0.000	0.000	0.000	0.000
15	A	36	ASP	-1	-0.701	-0.824	26.708	-0.166	-0.166	0.000	0.000	0.000	0.000
16	A	37	ALA	0	0.025	0.007	28.495	0.007	0.007	0.000	0.000	0.000	0.000
17	A	38	LYN	0	-0.066	-0.035	29.659	0.004	0.004	0.000	0.000	0.000	0.000
18	A	39	ASN	0	0.047	-0.004	28.957	-0.002	-0.002	0.000	0.000	0.000	0.000
19	A	40	ARG	1	0.734	0.849	24.764	0.172	0.172	0.000	0.000	0.000	0.000
20	A	41	ILE	0	0.026	0.027	19.913	0.001	0.001	0.000	0.000	0.000	0.000
21	A	42	SER	0	0.021	-0.002	20.102	-0.005	-0.005	0.000	0.000	0.000	0.000
22	A	43	LEU	0	0.063	0.046	14.779	-0.029	-0.029	0.000	0.000	0.000	0.000
23	A	44	PRO	0	0.070	0.039	13.255	0.009	0.009	0.000	0.000	0.000	0.000
24	A	45	ALA	0	-0.076	-0.067	13.280	-0.088	-0.088	0.000	0.000	0.000	0.000
25	A	46	LYS	1	0.936	0.958	8.626	0.989	0.989	0.000	0.000	0.000	0.000
26	A	47	LEU	0	0.042	0.003	8.510	-0.273	-0.273	0.000	0.000	0.000	0.000
27	A	48	ARG	1	0.876	0.963	10.130	0.496	0.496	0.000	0.000	0.000	0.000
28	A	49	ALA	0	-0.022	0.016	7.201	0.074	0.074	0.000	0.000	0.000	0.000
29	A	50	PHE	0	0.001	0.028	6.557	0.078	0.078	0.000	0.000	0.000	0.000
30	A	51	PHE	0	-0.053	-0.039	8.712	0.191	0.191	0.000	0.000	0.000	0.000
31	A	52	GLU	-1	-0.851	-0.910	12.394	-0.316	-0.316	0.000	0.000	0.000	0.000
32	A	53	GLY	0	-0.013	-0.019	14.675	-0.030	-0.030	0.000	0.000	0.000	0.000
33	A	54	SER	0	0.005	0.014	17.522	0.020	0.020	0.000	0.000	0.000	0.000
34	A	55	ILE	0	-0.023	-0.007	16.174	-0.032	-0.032	0.000	0.000	0.000	0.000
35	A	56	VAL	0	-0.019	-0.008	18.715	0.036	0.036	0.000	0.000	0.000	0.000
36	A	57	ILE	0	-0.043	-0.011	19.792	-0.015	-0.015	0.000	0.000	0.000	0.000
37	A	58	ASN	0	0.066	0.023	21.657	-0.010	-0.010	0.000	0.000	0.000	0.000
38	A	59	ARG	1	0.874	0.947	23.476	0.095	0.095	0.000	0.000	0.000	0.000
39	A	60	GLY	0	0.007	0.018	23.261	0.002	0.002	0.000	0.000	0.000	0.000
40	A	61	PHE	0	-0.025	-0.017	23.391	0.018	0.018	0.000	0.000	0.000	0.000
41	A	62	GLU	-1	-0.881	-0.955	24.933	-0.117	-0.117	0.000	0.000	0.000	0.000
42	A	63	ASN	0	-0.096	-0.046	27.245	0.000	0.000	0.000	0.000	0.000	0.000
43	A	64	CYS	0	0.016	0.034	21.888	-0.004	-0.004	0.000	0.000	0.000	0.000
44	A	65	LEU	0	-0.029	-0.022	22.757	-0.012	-0.012	0.000	0.000	0.000	0.000
45	A	66	GLU	-1	-0.835	-0.892	18.918	-0.204	-0.204	0.000	0.000	0.000	0.000
46	A	67	VAL	0	0.008	-0.001	15.603	0.008	0.008	0.000	0.000	0.000	0.000
47	A	68	ARG	1	0.877	0.924	14.794	0.167	0.167	0.000	0.000	0.000	0.000
48	A	69	LYS	1	0.979	1.003	10.354	0.402	0.402	0.000	0.000	0.000	0.000
49	A	70	PRO	0	0.002	0.001	15.038	0.032	0.032	0.000	0.000	0.000	0.000
50	A	71	GLN	0	0.034	0.005	15.264	-0.008	-0.008	0.000	0.000	0.000	0.000
51	A	72	ASP	-1	-0.838	-0.934	12.209	-0.292	-0.292	0.000	0.000	0.000	0.000
52	A	73	PHE	0	-0.041	-0.019	15.647	0.025	0.025	0.000	0.000	0.000	0.000
53	A	74	GLN	0	-0.043	-0.025	18.896	0.013	0.013	0.000	0.000	0.000	0.000
54	A	75	LYS	1	0.944	0.959	13.065	0.120	0.120	0.000	0.000	0.000	0.000
55	A	76	TYR	0	0.016	0.016	18.470	0.017	0.017	0.000	0.000	0.000	0.000
56	A	77	PHE	0	-0.025	-0.021	19.738	0.014	0.014	0.000	0.000	0.000	0.000
57	A	78	GLU	-1	-0.831	-0.900	20.990	-0.034	-0.034	0.000	0.000	0.000	0.000
58	A	79	GLN	0	-0.043	-0.037	18.916	-0.005	-0.005	0.000	0.000	0.000	0.000
59	A	80	PHE	0	-0.022	-0.029	23.211	0.009	0.009	0.000	0.000	0.000	0.000
60	A	81	ASN	0	-0.071	-0.019	26.415	0.004	0.004	0.000	0.000	0.000	0.000
61	A	82	SER	0	-0.039	0.001	25.654	0.007	0.007	0.000	0.000	0.000	0.000
62	A	83	PHE	0	-0.023	-0.005	25.508	0.005	0.005	0.000	0.000	0.000	0.000
63	A	84	PRO	0	0.029	-0.005	30.096	-0.001	-0.001	0.000	0.000	0.000	0.000
64	A	85	SER	0	0.040	0.039	33.641	-0.002	-0.002	0.000	0.000	0.000	0.000
65	A	86	THR	0	0.011	-0.002	35.154	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	87	GLN	0	0.024	0.022	35.608	0.001	0.001	0.000	0.000	0.000	0.000
67	A	88	LYS	1	0.978	0.962	36.701	0.034	0.034	0.000	0.000	0.000	0.000
68	A	89	ASP	-1	-0.849	-0.923	34.572	-0.040	-0.040	0.000	0.000	0.000	0.000
69	A	90	THR	0	0.043	0.024	31.300	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	91	ARG	1	0.847	0.925	32.645	0.027	0.027	0.000	0.000	0.000	0.000
71	A	92	THR	0	-0.048	-0.023	34.654	-0.003	-0.003	0.000	0.000	0.000	0.000
72	A	93	LEU	0	0.081	0.040	27.987	-0.004	-0.004	0.000	0.000	0.000	0.000
73	A	94	LYS	1	0.975	0.988	29.494	0.044	0.044	0.000	0.000	0.000	0.000
74	A	95	ARG	1	0.886	0.944	30.571	0.043	0.043	0.000	0.000	0.000	0.000
75	A	96	LEU	0	-0.004	-0.002	31.366	-0.003	-0.003	0.000	0.000	0.000	0.000
76	A	97	ILE	0	0.041	0.038	25.210	-0.006	-0.006	0.000	0.000	0.000	0.000
77	A	98	PHE	0	0.033	0.003	24.447	-0.004	-0.004	0.000	0.000	0.000	0.000
78	A	99	ALA	0	-0.098	-0.022	28.509	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	100	ASN	0	-0.056	-0.054	28.885	0.003	0.003	0.000	0.000	0.000	0.000
80	A	101	ALA	0	0.021	0.020	24.814	-0.012	-0.012	0.000	0.000	0.000	0.000
81	A	102	ASN	0	-0.020	-0.037	24.978	0.006	0.006	0.000	0.000	0.000	0.000
82	A	103	PHE	0	-0.036	0.003	22.118	0.009	0.009	0.000	0.000	0.000	0.000
83	A	104	VAL	0	-0.033	-0.015	22.297	0.012	0.012	0.000	0.000	0.000	0.000
84	A	105	ASP	-1	-0.867	-0.936	21.579	-0.200	-0.200	0.000	0.000	0.000	0.000
85	A	106	VAL	0	-0.088	-0.049	16.976	-0.006	-0.006	0.000	0.000	0.000	0.000
86	A	107	ASP	-1	-0.800	-0.894	20.093	-0.253	-0.253	0.000	0.000	0.000	0.000
87	A	108	THR	0	0.063	0.011	20.118	-0.031	-0.031	0.000	0.000	0.000	0.000
88	A	109	ALA	0	-0.141	-0.039	19.712	-0.020	-0.020	0.000	0.000	0.000	0.000
89	A	110	GLY	0	-0.015	-0.024	17.511	-0.033	-0.033	0.000	0.000	0.000	0.000
90	A	111	ARG	1	0.857	0.885	18.318	0.208	0.208	0.000	0.000	0.000	0.000
91	A	112	VAL	0	0.037	0.017	19.152	0.007	0.007	0.000	0.000	0.000	0.000
92	A	113	LEU	0	-0.010	0.005	22.114	0.004	0.004	0.000	0.000	0.000	0.000
93	A	114	ILE	0	0.021	0.012	23.284	-0.001	-0.001	0.000	0.000	0.000	0.000
94	A	115	PRO	0	-0.020	-0.006	26.068	0.012	0.012	0.000	0.000	0.000	0.000
95	A	116	ASN	0	0.079	0.020	29.116	-0.006	-0.006	0.000	0.000	0.000	0.000
96	A	117	ASN	0	0.045	0.043	30.414	-0.001	-0.001	0.000	0.000	0.000	0.000
97	A	118	LEU	0	0.045	0.016	25.752	0.002	0.002	0.000	0.000	0.000	0.000
98	A	119	ILE	0	0.016	0.020	28.012	-0.004	-0.004	0.000	0.000	0.000	0.000
99	A	120	ASN	0	-0.073	-0.051	29.616	0.002	0.002	0.000	0.000	0.000	0.000
100	A	121	ASP	-1	-0.899	-0.959	29.738	-0.106	-0.106	0.000	0.000	0.000	0.000
101	A	122	ALA	0	-0.008	-0.002	26.498	0.005	0.005	0.000	0.000	0.000	0.000
102	A	123	LYS	1	0.864	0.934	28.487	0.098	0.098	0.000	0.000	0.000	0.000
103	A	124	LEU	0	-0.021	-0.002	25.151	-0.003	-0.003	0.000	0.000	0.000	0.000
104	A	125	ASP	-1	-0.900	-0.942	29.150	-0.118	-0.118	0.000	0.000	0.000	0.000
105	A	126	LYS	1	0.915	0.947	29.448	0.128	0.128	0.000	0.000	0.000	0.000
106	A	127	GLU	-1	-0.966	-0.980	26.528	-0.158	-0.158	0.000	0.000	0.000	0.000
107	A	128	ILE	0	-0.044	-0.038	21.782	0.005	0.005	0.000	0.000	0.000	0.000
108	A	129	VAL	0	0.004	0.009	19.784	-0.013	-0.013	0.000	0.000	0.000	0.000
109	A	130	LEU	0	-0.035	-0.011	16.098	-0.005	-0.005	0.000	0.000	0.000	0.000
110	A	131	ILE	0	0.033	0.019	15.235	-0.029	-0.029	0.000	0.000	0.000	0.000
111	A	132	GLY	0	-0.056	-0.024	11.471	-0.026	-0.026	0.000	0.000	0.000	0.000
112	A	133	GLN	0	-0.026	-0.017	12.464	0.113	0.113	0.000	0.000	0.000	0.000
113	A	134	PHE	0	-0.019	-0.024	5.715	-0.003	-0.003	0.000	0.000	0.000	0.000
114	A	135	ASP	-1	-0.905	-0.954	9.406	-0.377	-0.377	0.000	0.000	0.000	0.000
115	A	136	HIS	0	-0.038	-0.026	11.725	-0.077	-0.077	0.000	0.000	0.000	0.000
116	A	137	LEU	0	-0.034	-0.026	12.049	-0.079	-0.079	0.000	0.000	0.000	0.000
117	A	138	GLU	-1	-0.822	-0.916	14.875	-0.174	-0.174	0.000	0.000	0.000	0.000
118	A	139	ILE	0	-0.083	-0.049	18.340	-0.032	-0.032	0.000	0.000	0.000	0.000
119	A	140	TRP	0	0.053	0.015	20.579	0.031	0.031	0.000	0.000	0.000	0.000
120	A	141	ASP	-1	-0.821	-0.913	23.421	-0.158	-0.158	0.000	0.000	0.000	0.000
121	A	142	LYS	1	0.930	0.955	25.167	0.177	0.177	0.000	0.000	0.000	0.000
122	A	143	LYS	1	0.911	0.962	26.178	0.105	0.105	0.000	0.000	0.000	0.000
123	A	144	LEU	0	-0.008	-0.015	28.064	0.006	0.006	0.000	0.000	0.000	0.000
124	A	145	TYR	0	0.002	0.003	19.453	0.001	0.001	0.000	0.000	0.000	0.000
125	A	146	GLU	-1	-0.900	-0.965	25.445	-0.136	-0.136	0.000	0.000	0.000	0.000
126	A	147	ASP	-1	-0.903	-0.950	26.854	-0.091	-0.091	0.000	0.000	0.000	0.000
127	A	148	TYR	0	-0.050	-0.021	22.725	0.006	0.006	0.000	0.000	0.000	0.000
128	A	149	LEU	0	-0.029	-0.037	21.676	0.006	0.006	0.000	0.000	0.000	0.000
129	A	150	ALA	0	-0.046	-0.002	25.750	0.009	0.009	0.000	0.000	0.000	0.000
130	A	151	ASN	0	-0.131	-0.051	29.301	0.014	0.014	0.000	0.000	0.000	0.000
131	A	152	SER	0	0.036	0.017	26.179	0.000	0.000	0.000	0.000	0.000	0.000
132	A	153	GLU	-1	-0.865	-0.902	28.265	-0.038	-0.038	0.000	0.000	0.000	0.000
133	A	154	SER	0	0.044	0.060	26.591	-0.005	-0.005	0.000	0.000	0.000	0.000
134	A	155	LEU	0	0.062	0.024	19.774	0.000	0.000	0.000	0.000	0.000	0.000
135	A	156	GLU	-1	-0.913	-0.981	23.621	-0.003	-0.003	0.000	0.000	0.000	0.000
136	A	157	THR	0	-0.057	-0.054	25.663	0.006	0.006	0.000	0.000	0.000	0.000
137	A	158	VAL	0	-0.027	-0.022	24.157	0.004	0.004	0.000	0.000	0.000	0.000
138	A	159	ALA	0	-0.012	-0.014	22.728	0.002	0.002	0.000	0.000	0.000	0.000
139	A	160	GLU	-1	-0.943	-0.954	24.384	0.029	0.029	0.000	0.000	0.000	0.000
140	A	161	ARG	1	0.786	0.871	27.706	0.027	0.027	0.000	0.000	0.000	0.000
141	A	162	MET	0	-0.075	-0.018	21.399	-0.002	-0.002	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:22:PHE)