FMO DATABASE

FMODB ID: KR1Z3

Calculation Name: 1N0G-A-Xray315

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: 2021-09-06

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200129

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	143
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1328010.983901
FMO2-HF: Nuclear repulsion	1271171.32531
FMO2-HF: Total energy	-56839.658591
FMO2-MP2: Total energy	-57007.964531

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:21:ACE )

Summations of interaction energy for fragment #1(A:21:ACE )

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.
-2.104	-1.593	2.985	-1.906	-1.59	-0.013

Interaction energy analysis for fragmet #1(A:21:ACE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.032 / q_NPA : -0.022

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	23	GLN	0	0.056	0.025	2.408	-2.149	-1.883	2.983	-1.839	-1.411	-0.013
4	A	24	GLY	0	0.046	0.026	4.685	0.231	0.295	0.000	-0.005	-0.058	0.000
5	A	25	HIS	0	-0.092	-0.052	4.569	-0.035	0.146	0.002	-0.062	-0.121	0.000
6	A	26	MET	0	0.027	0.008	6.535	0.167	0.167	0.000	0.000	0.000	0.000
7	A	27	LEU	0	-0.018	0.033	9.011	0.143	0.143	0.000	0.000	0.000	0.000
8	A	28	LEU	0	0.001	0.002	11.513	0.058	0.058	0.000	0.000	0.000	0.000
9	A	29	GLY	0	-0.002	-0.004	13.999	0.029	0.029	0.000	0.000	0.000	0.000
10	A	30	THR	0	0.056	0.024	16.765	-0.001	-0.001	0.000	0.000	0.000	0.000
11	A	31	PHE	0	-0.077	-0.045	14.291	0.023	0.023	0.000	0.000	0.000	0.000
12	A	32	ASN	0	0.029	0.023	20.342	0.001	0.001	0.000	0.000	0.000	0.000
13	A	33	ILE	0	-0.029	-0.004	21.169	0.009	0.009	0.000	0.000	0.000	0.000
14	A	34	THR	0	0.033	0.017	24.369	-0.001	-0.001	0.000	0.000	0.000	0.000
15	A	35	LEU	0	0.001	0.040	26.867	-0.001	-0.001	0.000	0.000	0.000	0.000
16	A	36	ASP	-1	-0.704	-0.824	28.068	-0.030	-0.030	0.000	0.000	0.000	0.000
17	A	37	ALA	0	0.024	0.007	29.971	-0.001	-0.001	0.000	0.000	0.000	0.000
18	A	38	LYN	0	-0.065	-0.035	30.820	0.002	0.002	0.000	0.000	0.000	0.000
19	A	39	ASN	0	0.046	-0.005	30.714	-0.001	-0.001	0.000	0.000	0.000	0.000
20	A	40	ARG	1	0.735	0.850	25.971	0.027	0.027	0.000	0.000	0.000	0.000
21	A	41	ILE	0	0.027	0.028	21.708	0.002	0.002	0.000	0.000	0.000	0.000
22	A	42	SER	0	0.021	-0.002	21.372	0.004	0.004	0.000	0.000	0.000	0.000
23	A	43	LEU	0	0.062	0.046	16.100	-0.008	-0.008	0.000	0.000	0.000	0.000
24	A	44	PRO	0	0.074	0.041	15.203	0.027	0.027	0.000	0.000	0.000	0.000
25	A	45	ALA	0	-0.078	-0.068	14.680	0.002	0.002	0.000	0.000	0.000	0.000
26	A	46	LYS	1	0.934	0.957	10.146	0.150	0.150	0.000	0.000	0.000	0.000
27	A	47	LEU	0	0.040	0.003	9.786	-0.048	-0.048	0.000	0.000	0.000	0.000
28	A	48	ARG	1	0.878	0.964	11.380	0.011	0.011	0.000	0.000	0.000	0.000
29	A	49	ALA	0	-0.024	0.016	7.635	0.020	0.020	0.000	0.000	0.000	0.000
30	A	50	PHE	0	0.002	0.030	8.720	-0.025	-0.025	0.000	0.000	0.000	0.000
31	A	51	PHE	0	-0.052	-0.038	9.737	0.003	0.003	0.000	0.000	0.000	0.000
32	A	52	GLU	-1	-0.852	-0.910	12.849	-0.123	-0.123	0.000	0.000	0.000	0.000
33	A	53	GLY	0	-0.013	-0.018	14.947	0.012	0.012	0.000	0.000	0.000	0.000
34	A	54	SER	0	0.002	0.013	18.044	0.003	0.003	0.000	0.000	0.000	0.000
35	A	55	ILE	0	-0.023	-0.007	17.477	-0.025	-0.025	0.000	0.000	0.000	0.000
36	A	56	VAL	0	-0.019	-0.008	20.029	0.023	0.023	0.000	0.000	0.000	0.000
37	A	57	ILE	0	-0.043	-0.011	22.055	-0.012	-0.012	0.000	0.000	0.000	0.000
38	A	58	ASN	0	0.067	0.021	24.208	-0.014	-0.014	0.000	0.000	0.000	0.000
39	A	59	ARG	1	0.875	0.949	26.414	0.073	0.073	0.000	0.000	0.000	0.000
40	A	60	GLY	0	0.012	0.019	26.818	-0.004	-0.004	0.000	0.000	0.000	0.000
41	A	61	PHE	0	-0.028	-0.017	27.298	0.014	0.014	0.000	0.000	0.000	0.000
42	A	62	GLU	-1	-0.882	-0.956	28.848	-0.117	-0.117	0.000	0.000	0.000	0.000
43	A	63	ASN	0	-0.096	-0.045	31.098	0.004	0.004	0.000	0.000	0.000	0.000
44	A	64	CYS	0	0.014	0.035	25.749	0.002	0.002	0.000	0.000	0.000	0.000
45	A	65	LEU	0	-0.029	-0.025	25.728	-0.001	-0.001	0.000	0.000	0.000	0.000
46	A	66	GLU	-1	-0.834	-0.891	22.199	-0.181	-0.181	0.000	0.000	0.000	0.000
47	A	67	VAL	0	0.009	-0.001	17.962	0.013	0.013	0.000	0.000	0.000	0.000
48	A	68	ARG	1	0.879	0.923	17.336	0.178	0.178	0.000	0.000	0.000	0.000
49	A	69	LYS	1	0.978	1.003	10.955	0.441	0.441	0.000	0.000	0.000	0.000
50	A	70	PRO	0	0.000	0.000	16.593	-0.003	-0.003	0.000	0.000	0.000	0.000
51	A	71	GLN	0	0.033	0.004	16.301	-0.013	-0.013	0.000	0.000	0.000	0.000
52	A	72	ASP	-1	-0.837	-0.931	14.404	-0.404	-0.404	0.000	0.000	0.000	0.000
53	A	73	PHE	0	-0.044	-0.021	17.726	0.013	0.013	0.000	0.000	0.000	0.000
54	A	74	GLN	0	-0.033	-0.019	20.995	0.017	0.017	0.000	0.000	0.000	0.000
55	A	75	LYS	1	0.940	0.956	15.184	0.348	0.348	0.000	0.000	0.000	0.000
56	A	76	TYR	0	0.016	0.015	21.297	0.012	0.012	0.000	0.000	0.000	0.000
57	A	77	PHE	0	-0.034	-0.024	22.799	0.017	0.017	0.000	0.000	0.000	0.000
58	A	78	GLU	-1	-0.824	-0.897	23.623	-0.119	-0.119	0.000	0.000	0.000	0.000
59	A	79	GLN	0	-0.041	-0.036	22.610	-0.004	-0.004	0.000	0.000	0.000	0.000
60	A	80	PHE	0	-0.022	-0.031	26.628	0.011	0.011	0.000	0.000	0.000	0.000
61	A	81	ASN	0	-0.071	-0.018	29.095	0.014	0.014	0.000	0.000	0.000	0.000
62	A	82	SER	0	-0.040	0.002	29.258	0.008	0.008	0.000	0.000	0.000	0.000
63	A	83	PHE	0	-0.023	-0.005	29.556	0.007	0.007	0.000	0.000	0.000	0.000
64	A	84	PRO	0	0.026	-0.006	33.724	0.004	0.004	0.000	0.000	0.000	0.000
65	A	85	SER	0	0.043	0.040	36.935	0.001	0.001	0.000	0.000	0.000	0.000
66	A	86	THR	0	0.013	-0.002	38.459	0.002	0.002	0.000	0.000	0.000	0.000
67	A	87	GLN	0	0.021	0.021	39.360	0.005	0.005	0.000	0.000	0.000	0.000
68	A	88	LYS	1	0.978	0.962	40.311	0.050	0.050	0.000	0.000	0.000	0.000
69	A	89	ASP	-1	-0.847	-0.922	38.471	-0.066	-0.066	0.000	0.000	0.000	0.000
70	A	90	THR	0	0.044	0.024	34.867	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	91	ARG	1	0.843	0.924	36.005	0.053	0.053	0.000	0.000	0.000	0.000
72	A	92	THR	0	-0.043	-0.021	37.710	0.002	0.002	0.000	0.000	0.000	0.000
73	A	93	LEU	0	0.077	0.039	31.545	0.000	0.000	0.000	0.000	0.000	0.000
74	A	94	LYS	1	0.975	0.989	32.506	0.081	0.081	0.000	0.000	0.000	0.000
75	A	95	ARG	1	0.887	0.945	33.397	0.058	0.058	0.000	0.000	0.000	0.000
76	A	96	LEU	0	-0.004	-0.002	34.673	0.001	0.001	0.000	0.000	0.000	0.000
77	A	97	ILE	0	0.041	0.039	28.285	0.000	0.000	0.000	0.000	0.000	0.000
78	A	98	PHE	0	0.027	0.000	27.124	0.001	0.001	0.000	0.000	0.000	0.000
79	A	99	ALA	0	-0.091	-0.019	31.071	0.002	0.002	0.000	0.000	0.000	0.000
80	A	100	ASN	0	-0.059	-0.054	31.673	0.008	0.008	0.000	0.000	0.000	0.000
81	A	101	ALA	0	0.021	0.020	27.022	-0.004	-0.004	0.000	0.000	0.000	0.000
82	A	102	ASN	0	-0.022	-0.037	27.035	0.004	0.004	0.000	0.000	0.000	0.000
83	A	103	PHE	0	-0.038	0.002	23.118	0.004	0.004	0.000	0.000	0.000	0.000
84	A	104	VAL	0	-0.034	-0.016	23.609	0.009	0.009	0.000	0.000	0.000	0.000
85	A	105	ASP	-1	-0.864	-0.935	22.355	-0.068	-0.068	0.000	0.000	0.000	0.000
86	A	106	VAL	0	-0.090	-0.050	17.855	0.000	0.000	0.000	0.000	0.000	0.000
87	A	107	ASP	-1	-0.800	-0.894	20.862	-0.024	-0.024	0.000	0.000	0.000	0.000
88	A	108	THR	0	0.062	0.012	20.675	-0.004	-0.004	0.000	0.000	0.000	0.000
89	A	109	ALA	0	-0.140	-0.039	20.090	0.006	0.006	0.000	0.000	0.000	0.000
90	A	110	GLY	0	-0.016	-0.024	18.358	-0.003	-0.003	0.000	0.000	0.000	0.000
91	A	111	ARG	1	0.858	0.885	19.140	0.011	0.011	0.000	0.000	0.000	0.000
92	A	112	VAL	0	0.033	0.016	20.526	0.001	0.001	0.000	0.000	0.000	0.000
93	A	113	LEU	0	-0.006	0.006	23.294	0.001	0.001	0.000	0.000	0.000	0.000
94	A	114	ILE	0	0.021	0.012	25.533	-0.006	-0.006	0.000	0.000	0.000	0.000
95	A	115	PRO	0	-0.020	-0.007	27.893	0.006	0.006	0.000	0.000	0.000	0.000
96	A	116	ASN	0	0.080	0.020	31.047	-0.002	-0.002	0.000	0.000	0.000	0.000
97	A	117	ASN	0	0.046	0.044	32.697	0.002	0.002	0.000	0.000	0.000	0.000
98	A	118	LEU	0	0.041	0.015	28.109	-0.001	-0.001	0.000	0.000	0.000	0.000
99	A	119	ILE	0	0.018	0.021	30.351	-0.003	-0.003	0.000	0.000	0.000	0.000
100	A	120	ASN	0	-0.067	-0.048	32.191	0.000	0.000	0.000	0.000	0.000	0.000
101	A	121	ASP	-1	-0.904	-0.961	32.714	-0.070	-0.070	0.000	0.000	0.000	0.000
102	A	122	ALA	0	-0.009	-0.003	29.694	-0.001	-0.001	0.000	0.000	0.000	0.000
103	A	123	LYS	1	0.862	0.933	31.692	0.060	0.060	0.000	0.000	0.000	0.000
104	A	124	LEU	0	-0.017	0.000	27.905	0.000	0.000	0.000	0.000	0.000	0.000
105	A	125	ASP	-1	-0.902	-0.943	31.984	-0.041	-0.041	0.000	0.000	0.000	0.000
106	A	126	LYS	1	0.917	0.948	31.791	0.038	0.038	0.000	0.000	0.000	0.000
107	A	127	GLU	-1	-0.969	-0.982	29.034	-0.053	-0.053	0.000	0.000	0.000	0.000
108	A	128	ILE	0	-0.041	-0.037	24.678	-0.002	-0.002	0.000	0.000	0.000	0.000
109	A	129	VAL	0	0.009	0.010	23.636	0.001	0.001	0.000	0.000	0.000	0.000
110	A	130	LEU	0	-0.040	-0.012	18.660	-0.005	-0.005	0.000	0.000	0.000	0.000
111	A	131	ILE	0	0.030	0.018	19.243	-0.002	-0.002	0.000	0.000	0.000	0.000
112	A	132	GLY	0	-0.053	-0.022	15.546	-0.010	-0.010	0.000	0.000	0.000	0.000
113	A	133	GLN	0	-0.026	-0.016	16.464	0.025	0.025	0.000	0.000	0.000	0.000
114	A	134	PHE	0	-0.019	-0.025	10.431	-0.046	-0.046	0.000	0.000	0.000	0.000
115	A	135	ASP	-1	-0.904	-0.953	13.190	-0.463	-0.463	0.000	0.000	0.000	0.000
116	A	136	HIS	0	-0.042	-0.027	15.054	-0.025	-0.025	0.000	0.000	0.000	0.000
117	A	137	LEU	0	-0.033	-0.028	15.145	-0.026	-0.026	0.000	0.000	0.000	0.000
118	A	138	GLU	-1	-0.821	-0.916	18.258	-0.155	-0.155	0.000	0.000	0.000	0.000
119	A	139	ILE	0	-0.079	-0.047	21.762	0.000	0.000	0.000	0.000	0.000	0.000
120	A	140	TRP	0	0.051	0.013	23.968	0.015	0.015	0.000	0.000	0.000	0.000
121	A	141	ASP	-1	-0.820	-0.913	26.834	-0.065	-0.065	0.000	0.000	0.000	0.000
122	A	142	LYS	1	0.928	0.955	28.843	0.062	0.062	0.000	0.000	0.000	0.000
123	A	143	LYS	1	0.913	0.963	29.769	0.056	0.056	0.000	0.000	0.000	0.000
124	A	144	LEU	0	-0.007	-0.014	31.744	-0.001	-0.001	0.000	0.000	0.000	0.000
125	A	145	TYR	0	0.001	0.003	24.267	-0.006	-0.006	0.000	0.000	0.000	0.000
126	A	146	GLU	-1	-0.905	-0.967	29.684	-0.071	-0.071	0.000	0.000	0.000	0.000
127	A	147	ASP	-1	-0.899	-0.948	31.411	-0.063	-0.063	0.000	0.000	0.000	0.000
128	A	148	TYR	0	-0.049	-0.021	27.601	-0.001	-0.001	0.000	0.000	0.000	0.000
129	A	149	LEU	0	-0.035	-0.039	26.663	-0.002	-0.002	0.000	0.000	0.000	0.000
130	A	150	ALA	0	-0.043	-0.001	30.782	0.002	0.002	0.000	0.000	0.000	0.000
131	A	151	ASN	0	-0.131	-0.051	34.403	0.005	0.005	0.000	0.000	0.000	0.000
132	A	152	SER	0	0.036	0.017	31.345	-0.004	-0.004	0.000	0.000	0.000	0.000
133	A	153	GLU	-1	-0.865	-0.903	33.423	-0.080	-0.080	0.000	0.000	0.000	0.000
134	A	154	SER	0	0.044	0.059	32.024	-0.006	-0.006	0.000	0.000	0.000	0.000
135	A	155	LEU	0	0.062	0.024	25.190	-0.003	-0.003	0.000	0.000	0.000	0.000
136	A	156	GLU	-1	-0.913	-0.980	29.068	-0.102	-0.102	0.000	0.000	0.000	0.000
137	A	157	THR	0	-0.057	-0.054	31.076	0.003	0.003	0.000	0.000	0.000	0.000
138	A	158	VAL	0	-0.028	-0.022	29.177	0.001	0.001	0.000	0.000	0.000	0.000
139	A	159	ALA	0	-0.014	-0.015	27.935	-0.003	-0.003	0.000	0.000	0.000	0.000
140	A	160	GLU	-1	-0.941	-0.953	29.477	-0.089	-0.089	0.000	0.000	0.000	0.000
141	A	161	ARG	1	0.793	0.872	32.720	0.089	0.089	0.000	0.000	0.000	0.000
142	A	162	MET	0	-0.062	-0.016	26.158	0.000	0.000	0.000	0.000	0.000	0.000
143	A	163	NME	0	-0.021	-0.004	30.322	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:21:ACE )