FMO DATABASE

FMODB ID: 5J11Z

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	OptAll
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	-1321681.866999
FMO2-HF: Nuclear repulsion	1265010.295482
FMO2-HF: Total energy	-56671.571516
FMO2-MP2: Total energy	-56839.007165

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.
-4.359	-0.455	5.679	-3.087	-6.497	-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 : 0.055 / q_NPA : -0.004

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	0.028	0.013	3.181	-1.566	0.514	-0.002	-0.993	-1.085	0.000
4	A	25	HIS	0	-0.086	-0.052	2.220	-0.231	0.773	1.581	-1.076	-1.509	-0.001
5	A	26	MET	0	0.004	0.022	2.243	-2.103	-1.405	4.102	-1.012	-3.789	-0.004
6	A	27	LEU	0	-0.029	0.018	5.342	0.322	0.322	-0.001	-0.002	0.003	0.000
7	A	28	LEU	0	0.008	0.007	5.933	0.196	0.196	0.000	0.000	0.000	0.000
8	A	29	GLY	0	0.011	0.001	9.297	0.043	0.043	0.000	0.000	0.000	0.000
9	A	30	THR	0	0.001	-0.011	12.095	-0.007	-0.007	0.000	0.000	0.000	0.000
10	A	31	PHE	0	-0.036	-0.030	11.235	0.058	0.058	0.000	0.000	0.000	0.000
11	A	32	ASN	0	0.050	0.034	17.319	-0.018	-0.018	0.000	0.000	0.000	0.000
12	A	33	ILE	0	-0.045	-0.015	19.122	0.014	0.014	0.000	0.000	0.000	0.000
13	A	34	THR	0	0.021	0.001	22.411	0.005	0.005	0.000	0.000	0.000	0.000
14	A	35	LEU	0	-0.022	0.005	25.154	-0.007	-0.007	0.000	0.000	0.000	0.000
15	A	36	ASP	-1	-0.772	-0.873	26.705	-0.070	-0.070	0.000	0.000	0.000	0.000
16	A	37	ALA	0	-0.016	-0.012	28.440	-0.002	-0.002	0.000	0.000	0.000	0.000
17	A	38	LYN	0	-0.018	0.008	30.256	0.003	0.003	0.000	0.000	0.000	0.000
18	A	39	ASN	0	0.025	0.011	29.207	-0.003	-0.003	0.000	0.000	0.000	0.000
19	A	40	ARG	1	0.803	0.865	24.791	0.074	0.074	0.000	0.000	0.000	0.000
20	A	41	ILE	0	0.037	0.028	20.501	0.009	0.009	0.000	0.000	0.000	0.000
21	A	42	SER	0	0.023	-0.002	20.180	-0.005	-0.005	0.000	0.000	0.000	0.000
22	A	43	LEU	0	0.072	0.042	14.823	-0.007	-0.007	0.000	0.000	0.000	0.000
23	A	44	PRO	0	0.042	0.028	13.568	0.040	0.040	0.000	0.000	0.000	0.000
24	A	45	ALA	0	-0.029	-0.029	13.198	0.005	0.005	0.000	0.000	0.000	0.000
25	A	46	LYS	1	0.893	0.956	8.258	0.173	0.173	0.000	0.000	0.000	0.000
26	A	47	LEU	0	0.056	0.013	8.610	-0.166	-0.166	0.000	0.000	0.000	0.000
27	A	48	ARG	1	0.805	0.908	10.435	0.107	0.107	0.000	0.000	0.000	0.000
28	A	49	ALA	0	0.011	0.021	7.215	0.068	0.068	0.000	0.000	0.000	0.000
29	A	50	PHE	0	-0.011	0.018	6.674	-0.098	-0.098	0.000	0.000	0.000	0.000
30	A	51	PHE	0	-0.010	-0.028	8.697	0.059	0.059	0.000	0.000	0.000	0.000
31	A	52	GLU	-1	-0.755	-0.841	12.496	-0.477	-0.477	0.000	0.000	0.000	0.000
32	A	53	GLY	0	-0.024	-0.017	15.029	0.013	0.013	0.000	0.000	0.000	0.000
33	A	54	SER	0	-0.015	0.000	17.853	0.016	0.016	0.000	0.000	0.000	0.000
34	A	55	ILE	0	-0.036	-0.014	16.171	-0.050	-0.050	0.000	0.000	0.000	0.000
35	A	56	VAL	0	-0.005	-0.009	18.602	0.040	0.040	0.000	0.000	0.000	0.000
36	A	57	ILE	0	0.005	0.019	19.869	-0.026	-0.026	0.000	0.000	0.000	0.000
37	A	58	ASN	0	-0.044	-0.065	21.703	-0.005	-0.005	0.000	0.000	0.000	0.000
38	A	59	ARG	1	0.828	0.884	23.802	0.135	0.135	0.000	0.000	0.000	0.000
39	A	60	GLY	0	-0.007	0.001	23.762	-0.012	-0.012	0.000	0.000	0.000	0.000
40	A	61	PHE	0	0.005	-0.002	22.895	0.023	0.023	0.000	0.000	0.000	0.000
41	A	62	GLU	-1	-0.833	-0.910	25.192	-0.173	-0.173	0.000	0.000	0.000	0.000
42	A	63	ASN	0	-0.062	-0.029	27.589	0.014	0.014	0.000	0.000	0.000	0.000
43	A	64	CYS	0	-0.048	-0.001	21.523	0.001	0.001	0.000	0.000	0.000	0.000
44	A	65	LEU	0	0.010	-0.001	22.614	-0.012	-0.012	0.000	0.000	0.000	0.000
45	A	66	GLU	-1	-0.708	-0.777	19.329	-0.334	-0.334	0.000	0.000	0.000	0.000
46	A	67	VAL	0	-0.026	-0.024	16.260	0.025	0.025	0.000	0.000	0.000	0.000
47	A	68	ARG	1	0.816	0.888	15.111	0.346	0.346	0.000	0.000	0.000	0.000
48	A	69	LYS	1	0.875	0.936	10.494	0.812	0.812	0.000	0.000	0.000	0.000
49	A	70	PRO	0	0.015	0.003	15.543	0.006	0.006	0.000	0.000	0.000	0.000
50	A	71	GLN	0	-0.013	-0.027	14.472	0.022	0.022	0.000	0.000	0.000	0.000
51	A	72	ASP	-1	-0.825	-0.932	12.449	-0.745	-0.745	0.000	0.000	0.000	0.000
52	A	73	PHE	0	-0.001	-0.004	15.652	0.021	0.021	0.000	0.000	0.000	0.000
53	A	74	GLN	0	-0.030	-0.014	19.116	0.030	0.030	0.000	0.000	0.000	0.000
54	A	75	LYS	1	0.795	0.877	12.111	0.773	0.773	0.000	0.000	0.000	0.000
55	A	76	TYR	0	-0.041	-0.038	18.369	0.031	0.031	0.000	0.000	0.000	0.000
56	A	77	PHE	0	-0.008	-0.003	19.683	0.034	0.034	0.000	0.000	0.000	0.000
57	A	78	GLU	-1	-0.814	-0.897	21.488	-0.216	-0.216	0.000	0.000	0.000	0.000
58	A	79	GLN	0	-0.011	-0.001	18.949	-0.003	-0.003	0.000	0.000	0.000	0.000
59	A	80	PHE	0	0.012	-0.008	22.926	0.029	0.029	0.000	0.000	0.000	0.000
60	A	81	ASN	0	-0.061	-0.034	25.946	0.032	0.032	0.000	0.000	0.000	0.000
61	A	82	SER	0	0.006	0.021	25.387	0.011	0.011	0.000	0.000	0.000	0.000
62	A	83	PHE	0	-0.040	-0.006	24.959	0.013	0.013	0.000	0.000	0.000	0.000
63	A	84	PRO	0	0.059	0.018	29.635	0.003	0.003	0.000	0.000	0.000	0.000
64	A	85	SER	0	0.022	0.030	33.217	0.005	0.005	0.000	0.000	0.000	0.000
65	A	86	THR	0	0.022	-0.001	34.575	0.003	0.003	0.000	0.000	0.000	0.000
66	A	87	GLN	0	0.048	0.037	35.299	0.009	0.009	0.000	0.000	0.000	0.000
67	A	88	LYS	1	0.896	0.931	36.367	0.094	0.094	0.000	0.000	0.000	0.000
68	A	89	ASP	-1	-0.819	-0.895	34.574	-0.107	-0.107	0.000	0.000	0.000	0.000
69	A	90	THR	0	0.038	0.032	30.723	-0.004	-0.004	0.000	0.000	0.000	0.000
70	A	91	ARG	1	0.861	0.912	32.148	0.096	0.096	0.000	0.000	0.000	0.000
71	A	92	THR	0	-0.065	-0.048	34.387	0.002	0.002	0.000	0.000	0.000	0.000
72	A	93	LEU	0	0.058	0.029	28.418	0.000	0.000	0.000	0.000	0.000	0.000
73	A	94	LYS	1	0.861	0.920	28.529	0.168	0.168	0.000	0.000	0.000	0.000
74	A	95	ARG	1	0.911	0.960	30.456	0.105	0.105	0.000	0.000	0.000	0.000
75	A	96	LEU	0	0.000	-0.008	31.801	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	97	ILE	0	0.041	0.034	25.320	0.003	0.003	0.000	0.000	0.000	0.000
77	A	98	PHE	0	0.026	-0.001	24.172	0.000	0.000	0.000	0.000	0.000	0.000
78	A	99	ALA	0	-0.063	-0.016	28.767	0.002	0.002	0.000	0.000	0.000	0.000
79	A	100	ASN	0	-0.089	-0.044	29.547	0.015	0.015	0.000	0.000	0.000	0.000
80	A	101	ALA	0	0.078	0.034	25.040	-0.013	-0.013	0.000	0.000	0.000	0.000
81	A	102	ASN	0	-0.046	-0.028	25.503	0.007	0.007	0.000	0.000	0.000	0.000
82	A	103	PHE	0	0.002	0.006	22.456	0.005	0.005	0.000	0.000	0.000	0.000
83	A	104	VAL	0	-0.029	-0.011	22.427	0.019	0.019	0.000	0.000	0.000	0.000
84	A	105	ASP	-1	-0.882	-0.935	21.503	-0.198	-0.198	0.000	0.000	0.000	0.000
85	A	106	VAL	0	-0.061	-0.033	17.084	0.002	0.002	0.000	0.000	0.000	0.000
86	A	107	ASP	-1	-0.801	-0.896	20.290	-0.100	-0.100	0.000	0.000	0.000	0.000
87	A	108	THR	0	0.040	0.000	20.431	-0.011	-0.011	0.000	0.000	0.000	0.000
88	A	109	ALA	0	-0.043	-0.007	20.277	0.008	0.008	0.000	0.000	0.000	0.000
89	A	110	GLY	0	-0.027	-0.024	17.782	0.003	0.003	0.000	0.000	0.000	0.000
90	A	111	ARG	1	0.823	0.904	18.566	0.073	0.073	0.000	0.000	0.000	0.000
91	A	112	VAL	0	0.055	0.029	18.981	-0.003	-0.003	0.000	0.000	0.000	0.000
92	A	113	LEU	0	-0.006	0.001	22.165	0.007	0.007	0.000	0.000	0.000	0.000
93	A	114	ILE	0	0.038	0.018	23.574	-0.014	-0.014	0.000	0.000	0.000	0.000
94	A	115	PRO	0	0.006	0.005	26.151	0.014	0.014	0.000	0.000	0.000	0.000
95	A	116	ASN	0	0.044	0.014	29.205	-0.005	-0.005	0.000	0.000	0.000	0.000
96	A	117	ASN	0	0.021	0.009	30.525	0.003	0.003	0.000	0.000	0.000	0.000
97	A	118	LEU	0	0.041	0.023	26.238	0.000	0.000	0.000	0.000	0.000	0.000
98	A	119	ILE	0	-0.015	-0.002	28.316	-0.003	-0.003	0.000	0.000	0.000	0.000
99	A	120	ASN	0	-0.042	-0.024	29.951	0.004	0.004	0.000	0.000	0.000	0.000
100	A	121	ASP	-1	-0.805	-0.873	29.489	-0.131	-0.131	0.000	0.000	0.000	0.000
101	A	122	ALA	0	0.024	0.008	26.563	0.003	0.003	0.000	0.000	0.000	0.000
102	A	123	LYS	1	0.789	0.895	28.571	0.114	0.114	0.000	0.000	0.000	0.000
103	A	124	LEU	0	-0.018	0.010	25.492	0.006	0.006	0.000	0.000	0.000	0.000
104	A	125	ASP	-1	-0.797	-0.894	29.600	-0.062	-0.062	0.000	0.000	0.000	0.000
105	A	126	LYS	1	0.767	0.850	29.337	0.068	0.068	0.000	0.000	0.000	0.000
106	A	127	GLU	-1	-0.838	-0.885	26.744	-0.051	-0.051	0.000	0.000	0.000	0.000
107	A	128	ILE	0	-0.016	-0.008	21.938	-0.005	-0.005	0.000	0.000	0.000	0.000
108	A	129	VAL	0	-0.006	0.005	19.901	0.008	0.008	0.000	0.000	0.000	0.000
109	A	130	LEU	0	-0.012	0.000	16.173	-0.019	-0.019	0.000	0.000	0.000	0.000
110	A	131	ILE	0	0.013	0.011	15.427	0.014	0.014	0.000	0.000	0.000	0.000
111	A	132	GLY	0	-0.036	-0.007	11.794	-0.037	-0.037	0.000	0.000	0.000	0.000
112	A	133	GLN	0	-0.003	-0.007	12.718	0.076	0.076	0.000	0.000	0.000	0.000
113	A	134	PHE	0	-0.010	-0.008	4.490	-0.231	-0.109	-0.001	-0.004	-0.117	0.000
114	A	135	ASP	-1	-0.856	-0.926	9.145	-0.997	-0.997	0.000	0.000	0.000	0.000
115	A	136	HIS	0	-0.062	-0.044	11.342	-0.010	-0.010	0.000	0.000	0.000	0.000
116	A	137	LEU	0	-0.029	-0.020	12.824	-0.058	-0.058	0.000	0.000	0.000	0.000
117	A	138	GLU	-1	-0.773	-0.880	15.017	-0.279	-0.279	0.000	0.000	0.000	0.000
118	A	139	ILE	0	-0.066	-0.044	18.595	-0.001	-0.001	0.000	0.000	0.000	0.000
119	A	140	TRP	0	0.058	0.027	20.569	0.031	0.031	0.000	0.000	0.000	0.000
120	A	141	ASP	-1	-0.795	-0.910	23.558	-0.095	-0.095	0.000	0.000	0.000	0.000
121	A	142	LYS	1	0.796	0.895	25.334	0.051	0.051	0.000	0.000	0.000	0.000
122	A	143	LYS	1	0.796	0.901	26.343	0.069	0.069	0.000	0.000	0.000	0.000
123	A	144	LEU	0	0.037	-0.004	27.999	0.002	0.002	0.000	0.000	0.000	0.000
124	A	145	TYR	0	-0.001	0.003	19.204	-0.006	-0.006	0.000	0.000	0.000	0.000
125	A	146	GLU	-1	-0.889	-0.966	25.333	-0.062	-0.062	0.000	0.000	0.000	0.000
126	A	147	ASP	-1	-0.838	-0.908	27.301	-0.067	-0.067	0.000	0.000	0.000	0.000
127	A	148	TYR	0	-0.078	-0.047	22.668	0.002	0.002	0.000	0.000	0.000	0.000
128	A	149	LEU	0	-0.023	-0.018	21.640	-0.001	-0.001	0.000	0.000	0.000	0.000
129	A	150	ALA	0	-0.053	-0.005	25.945	0.008	0.008	0.000	0.000	0.000	0.000
130	A	151	ASN	0	-0.125	-0.059	29.034	0.010	0.010	0.000	0.000	0.000	0.000
131	A	152	SER	0	0.028	0.016	26.593	-0.008	-0.008	0.000	0.000	0.000	0.000
132	A	153	GLU	-1	-0.845	-0.895	28.551	-0.085	-0.085	0.000	0.000	0.000	0.000
133	A	154	SER	0	-0.018	-0.022	26.592	-0.008	-0.008	0.000	0.000	0.000	0.000
134	A	155	LEU	0	0.047	0.018	19.305	-0.008	-0.008	0.000	0.000	0.000	0.000
135	A	156	GLU	-1	-0.840	-0.908	23.574	-0.067	-0.067	0.000	0.000	0.000	0.000
136	A	157	THR	0	-0.011	-0.008	25.548	-0.002	-0.002	0.000	0.000	0.000	0.000
137	A	158	VAL	0	-0.054	-0.022	23.617	-0.003	-0.003	0.000	0.000	0.000	0.000
138	A	159	ALA	0	0.002	-0.004	22.583	-0.007	-0.007	0.000	0.000	0.000	0.000
139	A	160	GLU	-1	-0.946	-0.970	24.026	-0.075	-0.075	0.000	0.000	0.000	0.000
140	A	161	ARG	1	0.729	0.829	27.017	0.101	0.101	0.000	0.000	0.000	0.000
141	A	162	MET	0	-0.081	-0.021	20.619	-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:22:PHE)