FMO DATABASE

FMODB ID: 4J11N

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1322558.668136
FMO2-HF: Nuclear repulsion	1265888.238065
FMO2-HF: Total energy	-56670.430072
FMO2-MP2: Total energy	-56838.048732

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.
-4.487	0.065999999999999	5.01	-2.965	-6.597	-0.005

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 : 0.046 / q_NPA : -0.003

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	0.041	0.016	3.060	-1.673	0.332	0.017	-0.892	-1.130	0.000
4	A	25	HIS	0	-0.095	-0.055	2.469	-0.638	1.041	0.670	-0.856	-1.493	-0.001
5	A	26	MET	0	0.004	0.010	2.169	-1.803	-0.937	4.324	-1.212	-3.977	-0.004
6	A	27	LEU	0	-0.014	0.031	4.914	0.307	0.310	-0.001	-0.005	0.003	0.000
7	A	28	LEU	0	0.005	0.001	5.870	0.201	0.201	0.000	0.000	0.000	0.000
8	A	29	GLY	0	0.005	0.000	9.375	0.041	0.041	0.000	0.000	0.000	0.000
9	A	30	THR	0	0.048	0.021	12.164	-0.025	-0.025	0.000	0.000	0.000	0.000
10	A	31	PHE	0	-0.041	-0.034	11.163	0.056	0.056	0.000	0.000	0.000	0.000
11	A	32	ASN	0	0.043	0.031	17.206	-0.008	-0.008	0.000	0.000	0.000	0.000
12	A	33	ILE	0	-0.038	-0.009	18.790	0.013	0.013	0.000	0.000	0.000	0.000
13	A	34	THR	0	0.071	0.038	22.139	0.004	0.004	0.000	0.000	0.000	0.000
14	A	35	LEU	0	-0.051	0.001	25.017	-0.007	-0.007	0.000	0.000	0.000	0.000
15	A	36	ASP	-1	-0.757	-0.868	26.735	-0.080	-0.080	0.000	0.000	0.000	0.000
16	A	37	ALA	0	0.013	0.009	28.498	-0.003	-0.003	0.000	0.000	0.000	0.000
17	A	38	LYN	0	-0.017	0.009	29.816	0.002	0.002	0.000	0.000	0.000	0.000
18	A	39	ASN	0	0.010	-0.007	28.978	-0.001	-0.001	0.000	0.000	0.000	0.000
19	A	40	ARG	1	0.791	0.856	24.751	0.082	0.082	0.000	0.000	0.000	0.000
20	A	41	ILE	0	0.012	0.014	20.292	0.008	0.008	0.000	0.000	0.000	0.000
21	A	42	SER	0	0.028	0.007	20.181	-0.003	-0.003	0.000	0.000	0.000	0.000
22	A	43	LEU	0	0.075	0.052	14.730	-0.002	-0.002	0.000	0.000	0.000	0.000
23	A	44	PRO	0	0.049	0.029	13.229	0.044	0.044	0.000	0.000	0.000	0.000
24	A	45	ALA	0	-0.064	-0.052	13.353	0.014	0.014	0.000	0.000	0.000	0.000
25	A	46	LYS	1	0.902	0.955	8.712	0.214	0.214	0.000	0.000	0.000	0.000
26	A	47	LEU	0	0.031	0.002	8.562	-0.169	-0.169	0.000	0.000	0.000	0.000
27	A	48	ARG	1	0.873	0.945	10.138	0.105	0.105	0.000	0.000	0.000	0.000
28	A	49	ALA	0	-0.016	0.018	7.325	0.031	0.031	0.000	0.000	0.000	0.000
29	A	50	PHE	0	0.015	0.025	6.648	-0.003	-0.003	0.000	0.000	0.000	0.000
30	A	51	PHE	0	-0.033	-0.034	8.678	0.050	0.050	0.000	0.000	0.000	0.000
31	A	52	GLU	-1	-0.761	-0.851	12.370	-0.488	-0.488	0.000	0.000	0.000	0.000
32	A	53	GLY	0	0.016	-0.001	14.637	0.016	0.016	0.000	0.000	0.000	0.000
33	A	54	SER	0	-0.009	0.008	17.482	0.018	0.018	0.000	0.000	0.000	0.000
34	A	55	ILE	0	-0.022	0.001	16.159	-0.052	-0.052	0.000	0.000	0.000	0.000
35	A	56	VAL	0	-0.016	-0.005	18.704	0.045	0.045	0.000	0.000	0.000	0.000
36	A	57	ILE	0	-0.040	-0.017	19.791	-0.022	-0.022	0.000	0.000	0.000	0.000
37	A	58	ASN	0	0.023	-0.006	21.811	-0.024	-0.024	0.000	0.000	0.000	0.000
38	A	59	ARG	1	0.853	0.912	23.484	0.137	0.137	0.000	0.000	0.000	0.000
39	A	60	GLY	0	0.014	0.014	23.262	-0.009	-0.009	0.000	0.000	0.000	0.000
40	A	61	PHE	0	-0.035	-0.025	23.194	0.023	0.023	0.000	0.000	0.000	0.000
41	A	62	GLU	-1	-0.854	-0.944	24.955	-0.177	-0.177	0.000	0.000	0.000	0.000
42	A	63	ASN	0	-0.110	-0.053	27.267	0.008	0.008	0.000	0.000	0.000	0.000
43	A	64	CYS	0	0.005	0.028	21.869	0.001	0.001	0.000	0.000	0.000	0.000
44	A	65	LEU	0	-0.010	-0.007	22.909	-0.006	-0.006	0.000	0.000	0.000	0.000
45	A	66	GLU	-1	-0.743	-0.813	18.928	-0.338	-0.338	0.000	0.000	0.000	0.000
46	A	67	VAL	0	-0.002	-0.006	15.890	0.019	0.019	0.000	0.000	0.000	0.000
47	A	68	ARG	1	0.808	0.881	14.793	0.347	0.347	0.000	0.000	0.000	0.000
48	A	69	LYS	1	0.895	0.952	10.528	0.857	0.857	0.000	0.000	0.000	0.000
49	A	70	PRO	0	-0.008	-0.004	15.027	0.007	0.007	0.000	0.000	0.000	0.000
50	A	71	GLN	0	-0.014	-0.026	14.768	0.007	0.007	0.000	0.000	0.000	0.000
51	A	72	ASP	-1	-0.802	-0.916	12.725	-0.758	-0.758	0.000	0.000	0.000	0.000
52	A	73	PHE	0	-0.015	-0.003	15.640	0.029	0.029	0.000	0.000	0.000	0.000
53	A	74	GLN	0	-0.029	-0.024	18.892	0.034	0.034	0.000	0.000	0.000	0.000
54	A	75	LYS	1	0.832	0.918	12.689	0.735	0.735	0.000	0.000	0.000	0.000
55	A	76	TYR	0	-0.055	-0.033	18.278	0.030	0.030	0.000	0.000	0.000	0.000
56	A	77	PHE	0	0.012	-0.003	19.623	0.036	0.036	0.000	0.000	0.000	0.000
57	A	78	GLU	-1	-0.833	-0.905	21.422	-0.224	-0.224	0.000	0.000	0.000	0.000
58	A	79	GLN	0	-0.040	-0.030	18.820	-0.004	-0.004	0.000	0.000	0.000	0.000
59	A	80	PHE	0	-0.013	-0.025	22.947	0.027	0.027	0.000	0.000	0.000	0.000
60	A	81	ASN	0	-0.081	-0.034	26.290	0.027	0.027	0.000	0.000	0.000	0.000
61	A	82	SER	0	0.018	0.027	25.386	0.010	0.010	0.000	0.000	0.000	0.000
62	A	83	PHE	0	-0.057	-0.024	25.018	0.015	0.015	0.000	0.000	0.000	0.000
63	A	84	PRO	0	0.043	-0.002	29.805	0.004	0.004	0.000	0.000	0.000	0.000
64	A	85	SER	0	0.052	0.048	33.374	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	86	THR	0	0.025	0.010	34.962	0.002	0.002	0.000	0.000	0.000	0.000
66	A	87	GLN	0	0.037	0.031	35.358	0.009	0.009	0.000	0.000	0.000	0.000
67	A	88	LYS	1	0.970	0.972	36.460	0.090	0.090	0.000	0.000	0.000	0.000
68	A	89	ASP	-1	-0.851	-0.924	34.503	-0.109	-0.109	0.000	0.000	0.000	0.000
69	A	90	THR	0	0.028	0.020	30.984	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	91	ARG	1	0.834	0.907	32.439	0.095	0.095	0.000	0.000	0.000	0.000
71	A	92	THR	0	-0.065	-0.042	34.500	0.002	0.002	0.000	0.000	0.000	0.000
72	A	93	LEU	0	0.076	0.044	28.069	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	94	LYS	1	0.929	0.969	28.816	0.166	0.166	0.000	0.000	0.000	0.000
74	A	95	ARG	1	0.898	0.953	30.575	0.106	0.106	0.000	0.000	0.000	0.000
75	A	96	LEU	0	-0.008	-0.010	31.460	0.001	0.001	0.000	0.000	0.000	0.000
76	A	97	ILE	0	0.035	0.036	25.189	0.000	0.000	0.000	0.000	0.000	0.000
77	A	98	PHE	0	0.042	0.006	24.357	0.001	0.001	0.000	0.000	0.000	0.000
78	A	99	ALA	0	-0.087	-0.017	28.511	0.001	0.001	0.000	0.000	0.000	0.000
79	A	100	ASN	0	-0.063	-0.062	29.153	0.014	0.014	0.000	0.000	0.000	0.000
80	A	101	ALA	0	0.023	0.023	24.831	-0.008	-0.008	0.000	0.000	0.000	0.000
81	A	102	ASN	0	-0.016	-0.038	24.967	0.010	0.010	0.000	0.000	0.000	0.000
82	A	103	PHE	0	-0.031	0.005	22.474	0.006	0.006	0.000	0.000	0.000	0.000
83	A	104	VAL	0	-0.035	-0.015	22.384	0.020	0.020	0.000	0.000	0.000	0.000
84	A	105	ASP	-1	-0.869	-0.936	21.564	-0.208	-0.208	0.000	0.000	0.000	0.000
85	A	106	VAL	0	-0.089	-0.046	16.860	0.006	0.006	0.000	0.000	0.000	0.000
86	A	107	ASP	-1	-0.793	-0.898	20.087	-0.114	-0.114	0.000	0.000	0.000	0.000
87	A	108	THR	0	0.062	0.015	20.137	-0.014	-0.014	0.000	0.000	0.000	0.000
88	A	109	ALA	0	-0.083	-0.029	19.750	0.002	0.002	0.000	0.000	0.000	0.000
89	A	110	GLY	0	-0.023	-0.034	17.568	-0.003	-0.003	0.000	0.000	0.000	0.000
90	A	111	ARG	1	0.819	0.898	18.347	0.080	0.080	0.000	0.000	0.000	0.000
91	A	112	VAL	0	0.028	0.010	18.965	-0.005	-0.005	0.000	0.000	0.000	0.000
92	A	113	LEU	0	0.010	0.016	22.113	0.008	0.008	0.000	0.000	0.000	0.000
93	A	114	ILE	0	0.020	0.007	23.198	-0.012	-0.012	0.000	0.000	0.000	0.000
94	A	115	PRO	0	0.006	0.009	26.068	0.014	0.014	0.000	0.000	0.000	0.000
95	A	116	ASN	0	0.068	0.026	29.115	-0.004	-0.004	0.000	0.000	0.000	0.000
96	A	117	ASN	0	0.038	0.031	30.688	0.001	0.001	0.000	0.000	0.000	0.000
97	A	118	LEU	0	0.054	0.023	25.928	0.000	0.000	0.000	0.000	0.000	0.000
98	A	119	ILE	0	0.013	0.012	27.840	-0.003	-0.003	0.000	0.000	0.000	0.000
99	A	120	ASN	0	-0.046	-0.036	29.624	0.003	0.003	0.000	0.000	0.000	0.000
100	A	121	ASP	-1	-0.819	-0.887	29.669	-0.133	-0.133	0.000	0.000	0.000	0.000
101	A	122	ALA	0	-0.016	-0.009	26.491	0.002	0.002	0.000	0.000	0.000	0.000
102	A	123	LYS	1	0.799	0.897	28.503	0.114	0.114	0.000	0.000	0.000	0.000
103	A	124	LEU	0	-0.010	0.009	25.211	0.003	0.003	0.000	0.000	0.000	0.000
104	A	125	ASP	-1	-0.833	-0.907	29.163	-0.071	-0.071	0.000	0.000	0.000	0.000
105	A	126	LYS	1	0.839	0.893	29.467	0.077	0.077	0.000	0.000	0.000	0.000
106	A	127	GLU	-1	-0.869	-0.911	26.530	-0.065	-0.065	0.000	0.000	0.000	0.000
107	A	128	ILE	0	-0.043	-0.042	21.757	-0.003	-0.003	0.000	0.000	0.000	0.000
108	A	129	VAL	0	0.010	0.012	19.982	0.007	0.007	0.000	0.000	0.000	0.000
109	A	130	LEU	0	-0.032	-0.005	16.063	-0.017	-0.017	0.000	0.000	0.000	0.000
110	A	131	ILE	0	0.022	0.014	15.259	0.013	0.013	0.000	0.000	0.000	0.000
111	A	132	GLY	0	-0.042	-0.021	11.482	-0.041	-0.041	0.000	0.000	0.000	0.000
112	A	133	GLN	0	-0.024	-0.015	12.469	0.081	0.081	0.000	0.000	0.000	0.000
113	A	134	PHE	0	-0.016	-0.027	4.836	-0.122	-0.122	0.000	0.000	0.000	0.000
114	A	135	ASP	-1	-0.873	-0.943	9.420	-0.937	-0.937	0.000	0.000	0.000	0.000
115	A	136	HIS	0	-0.065	-0.045	11.622	-0.070	-0.070	0.000	0.000	0.000	0.000
116	A	137	LEU	0	-0.031	-0.020	12.256	-0.057	-0.057	0.000	0.000	0.000	0.000
117	A	138	GLU	-1	-0.765	-0.872	14.889	-0.275	-0.275	0.000	0.000	0.000	0.000
118	A	139	ILE	0	-0.077	-0.048	18.357	-0.001	-0.001	0.000	0.000	0.000	0.000
119	A	140	TRP	0	0.042	0.002	20.564	0.027	0.027	0.000	0.000	0.000	0.000
120	A	141	ASP	-1	-0.817	-0.901	23.441	-0.104	-0.104	0.000	0.000	0.000	0.000
121	A	142	LYS	1	0.820	0.889	25.205	0.068	0.068	0.000	0.000	0.000	0.000
122	A	143	LYS	1	0.826	0.902	26.225	0.077	0.077	0.000	0.000	0.000	0.000
123	A	144	LEU	0	0.029	-0.003	28.173	0.001	0.001	0.000	0.000	0.000	0.000
124	A	145	TYR	0	-0.013	0.000	19.511	-0.009	-0.009	0.000	0.000	0.000	0.000
125	A	146	GLU	-1	-0.902	-0.964	25.470	-0.075	-0.075	0.000	0.000	0.000	0.000
126	A	147	ASP	-1	-0.854	-0.907	26.890	-0.074	-0.074	0.000	0.000	0.000	0.000
127	A	148	TYR	0	-0.036	-0.015	22.660	0.003	0.003	0.000	0.000	0.000	0.000
128	A	149	LEU	0	-0.026	-0.025	21.666	0.000	0.000	0.000	0.000	0.000	0.000
129	A	150	ALA	0	-0.043	-0.002	25.767	0.007	0.007	0.000	0.000	0.000	0.000
130	A	151	ASN	0	-0.140	-0.061	29.323	0.010	0.010	0.000	0.000	0.000	0.000
131	A	152	SER	0	0.026	0.008	26.137	-0.005	-0.005	0.000	0.000	0.000	0.000
132	A	153	GLU	-1	-0.841	-0.885	28.255	-0.086	-0.086	0.000	0.000	0.000	0.000
133	A	154	SER	0	-0.004	-0.014	26.561	-0.008	-0.008	0.000	0.000	0.000	0.000
134	A	155	LEU	0	0.047	0.020	19.536	-0.008	-0.008	0.000	0.000	0.000	0.000
135	A	156	GLU	-1	-0.853	-0.929	23.604	-0.066	-0.066	0.000	0.000	0.000	0.000
136	A	157	THR	0	-0.042	-0.022	25.637	0.000	0.000	0.000	0.000	0.000	0.000
137	A	158	VAL	0	-0.024	-0.019	23.895	-0.003	-0.003	0.000	0.000	0.000	0.000
138	A	159	ALA	0	-0.019	-0.013	22.644	-0.009	-0.009	0.000	0.000	0.000	0.000
139	A	160	GLU	-1	-0.951	-0.960	24.135	-0.075	-0.075	0.000	0.000	0.000	0.000
140	A	161	ARG	1	0.758	0.851	27.349	0.101	0.101	0.000	0.000	0.000	0.000
141	A	162	MET	0	-0.071	-0.016	20.795	-0.003	-0.003	0.000	0.000	0.000	0.000

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