FMO DATABASE

FMODB ID: K3N63

Calculation Name: 4L1N-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4L1N

Chain ID: A

ChEMBL ID:

UniProt ID: A0PXY7

Base Structure: X-ray

Registration Date: 2023-06-20

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

DOI:

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	161
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1637569.245137
FMO2-HF: Nuclear repulsion	1573476.394076
FMO2-HF: Total energy	-64092.85106
FMO2-MP2: Total energy	-64281.580273

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:80:ASP)

Summations of interaction energy for fragment #1(A:80:ASP)

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.
-147.948	-150.61	24.56	-13.222	-8.677	0.103

Interaction energy analysis for fragmet #1(A:80:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.810 / q_NPA : -0.889

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	82	SER	0	-0.065	-0.066	1.596	-37.483	-42.487	24.426	-12.023	-7.400	0.093
4	A	83	LYS	1	0.957	0.969	4.076	-37.251	-37.042	0.007	-0.133	-0.083	0.001
5	A	84	LYS	1	0.868	0.922	7.340	-24.277	-24.277	0.000	0.000	0.000	0.000
6	A	85	MET	0	-0.011	0.009	9.403	-1.743	-1.743	0.000	0.000	0.000	0.000
7	A	86	PHE	0	0.038	0.026	11.453	-2.233	-2.233	0.000	0.000	0.000	0.000
8	A	87	LEU	0	-0.011	-0.005	12.832	1.345	1.345	0.000	0.000	0.000	0.000
9	A	88	LYS	1	0.855	0.920	14.892	-18.298	-18.298	0.000	0.000	0.000	0.000
10	A	89	LYS	1	0.913	0.963	16.597	-15.104	-15.104	0.000	0.000	0.000	0.000
11	A	90	GLU	-1	-0.919	-0.967	20.441	14.188	14.188	0.000	0.000	0.000	0.000
12	A	91	LEU	0	-0.025	0.002	22.463	-0.476	-0.476	0.000	0.000	0.000	0.000
13	A	92	GLY	0	0.033	0.025	25.597	-0.099	-0.099	0.000	0.000	0.000	0.000
14	A	93	LYS	1	0.953	0.967	28.703	-10.755	-10.755	0.000	0.000	0.000	0.000
15	A	94	ASN	0	-0.019	-0.003	30.361	0.235	0.235	0.000	0.000	0.000	0.000
16	A	95	SER	0	-0.013	0.001	28.311	-0.064	-0.064	0.000	0.000	0.000	0.000
17	A	96	LYS	1	0.947	0.936	29.250	-9.462	-9.462	0.000	0.000	0.000	0.000
18	A	97	PRO	0	0.012	0.031	27.311	-0.157	-0.157	0.000	0.000	0.000	0.000
19	A	98	THR	0	-0.079	-0.036	29.277	-0.391	-0.391	0.000	0.000	0.000	0.000
20	A	99	PHE	0	0.021	0.008	30.596	-0.312	-0.312	0.000	0.000	0.000	0.000
21	A	100	ALA	0	0.028	0.018	26.773	0.315	0.315	0.000	0.000	0.000	0.000
22	A	101	THR	0	-0.011	0.018	24.461	-0.268	-0.268	0.000	0.000	0.000	0.000
23	A	102	LYS	1	0.964	0.969	27.459	-9.949	-9.949	0.000	0.000	0.000	0.000
24	A	103	TRP	0	-0.025	-0.016	22.977	0.340	0.340	0.000	0.000	0.000	0.000
25	A	104	LYS	1	0.962	1.000	22.230	-14.384	-14.384	0.000	0.000	0.000	0.000
26	A	105	ASN	0	-0.018	-0.027	22.433	0.468	0.468	0.000	0.000	0.000	0.000
27	A	106	SER	0	-0.007	0.008	19.280	0.477	0.477	0.000	0.000	0.000	0.000
28	A	107	SER	0	0.011	0.000	19.912	-0.917	-0.917	0.000	0.000	0.000	0.000
29	A	108	ASN	0	0.059	0.031	19.346	-0.842	-0.842	0.000	0.000	0.000	0.000
30	A	109	ASN	0	-0.003	0.001	22.723	-0.432	-0.432	0.000	0.000	0.000	0.000
31	A	110	LYS	1	0.890	0.957	19.603	-15.768	-15.768	0.000	0.000	0.000	0.000
32	A	111	PHE	0	0.035	0.013	17.257	-0.296	-0.296	0.000	0.000	0.000	0.000
33	A	112	SER	0	0.003	-0.007	21.222	-0.366	-0.366	0.000	0.000	0.000	0.000
34	A	113	ALA	0	0.046	0.023	19.121	0.319	0.319	0.000	0.000	0.000	0.000
35	A	114	CYS	0	-0.050	-0.006	21.187	-0.613	-0.613	0.000	0.000	0.000	0.000
36	A	115	ILE	0	0.030	0.018	20.887	0.642	0.642	0.000	0.000	0.000	0.000
37	A	116	GLU	-1	-0.753	-0.895	23.260	10.387	10.387	0.000	0.000	0.000	0.000
38	A	117	GLY	0	0.001	-0.007	25.328	0.400	0.400	0.000	0.000	0.000	0.000
39	A	118	LYS	1	0.822	0.908	24.682	-12.259	-12.259	0.000	0.000	0.000	0.000
40	A	119	GLY	0	0.048	0.036	28.660	-0.181	-0.181	0.000	0.000	0.000	0.000
41	A	120	GLU	-1	-0.958	-0.998	29.234	9.863	9.863	0.000	0.000	0.000	0.000
42	A	121	ASN	0	-0.046	-0.034	28.987	0.388	0.388	0.000	0.000	0.000	0.000
43	A	122	ALA	0	0.009	0.004	25.433	0.251	0.251	0.000	0.000	0.000	0.000
44	A	123	LEU	0	-0.011	-0.020	27.346	0.289	0.289	0.000	0.000	0.000	0.000
45	A	124	GLU	-1	-0.927	-0.935	30.136	9.291	9.291	0.000	0.000	0.000	0.000
46	A	125	GLU	-1	-0.868	-0.929	29.190	10.467	10.467	0.000	0.000	0.000	0.000
47	A	126	GLY	0	0.041	0.029	28.223	-0.161	-0.161	0.000	0.000	0.000	0.000
48	A	127	VAL	0	-0.097	-0.053	22.134	0.367	0.367	0.000	0.000	0.000	0.000
49	A	128	GLY	0	0.005	0.011	23.574	-0.332	-0.332	0.000	0.000	0.000	0.000
50	A	129	LYS	1	0.896	0.947	20.846	-11.947	-11.947	0.000	0.000	0.000	0.000
51	A	130	ILE	0	-0.019	0.000	15.807	-0.379	-0.379	0.000	0.000	0.000	0.000
52	A	131	TYR	0	0.018	0.000	19.396	-0.021	-0.021	0.000	0.000	0.000	0.000
53	A	132	ILE	0	-0.014	-0.006	16.239	0.113	0.113	0.000	0.000	0.000	0.000
54	A	133	LYS	1	0.909	0.956	20.281	-12.393	-12.393	0.000	0.000	0.000	0.000
55	A	134	ASN	0	0.016	0.007	20.656	-0.062	-0.062	0.000	0.000	0.000	0.000
56	A	135	LEU	0	-0.023	-0.030	22.608	-0.570	-0.570	0.000	0.000	0.000	0.000
57	A	136	LYS	1	0.857	0.948	24.340	-12.692	-12.692	0.000	0.000	0.000	0.000
58	A	137	GLU	-1	-0.894	-0.948	23.330	12.509	12.509	0.000	0.000	0.000	0.000
59	A	138	GLN	0	-0.020	-0.012	26.282	-0.099	-0.099	0.000	0.000	0.000	0.000
60	A	139	SER	0	-0.030	-0.010	22.864	-0.479	-0.479	0.000	0.000	0.000	0.000
61	A	140	LYS	1	0.845	0.913	23.387	-10.733	-10.733	0.000	0.000	0.000	0.000
62	A	141	TRP	0	-0.002	-0.003	16.040	-0.913	-0.913	0.000	0.000	0.000	0.000
63	A	142	GLU	-1	-0.829	-0.916	20.049	13.310	13.310	0.000	0.000	0.000	0.000
64	A	143	LEU	0	-0.051	-0.020	13.474	0.660	0.660	0.000	0.000	0.000	0.000
65	A	144	ASP	-1	-0.813	-0.926	17.000	14.553	14.553	0.000	0.000	0.000	0.000
66	A	145	LEU	0	-0.052	-0.028	15.166	1.058	1.058	0.000	0.000	0.000	0.000
67	A	146	ASP	-1	-0.920	-0.956	15.224	17.618	17.618	0.000	0.000	0.000	0.000
68	A	147	GLN	0	-0.017	-0.026	16.905	0.698	0.698	0.000	0.000	0.000	0.000
69	A	148	ASP	-1	-0.889	-0.932	19.750	14.282	14.282	0.000	0.000	0.000	0.000
70	A	149	GLN	0	-0.053	-0.026	23.017	-0.517	-0.517	0.000	0.000	0.000	0.000
71	A	150	GLN	0	0.041	0.020	23.353	0.945	0.945	0.000	0.000	0.000	0.000
72	A	151	LYS	1	0.964	0.980	22.171	-13.842	-13.842	0.000	0.000	0.000	0.000
73	A	152	ASN	0	-0.022	-0.003	19.623	-0.625	-0.625	0.000	0.000	0.000	0.000
74	A	153	THR	0	0.076	0.033	20.854	-0.328	-0.328	0.000	0.000	0.000	0.000
75	A	154	PRO	0	-0.043	0.006	17.884	0.441	0.441	0.000	0.000	0.000	0.000
76	A	155	LYS	1	0.901	0.961	19.364	-13.231	-13.231	0.000	0.000	0.000	0.000
77	A	156	TYR	0	0.045	0.005	19.727	-0.920	-0.920	0.000	0.000	0.000	0.000
78	A	157	ILE	0	-0.022	-0.006	17.447	1.104	1.104	0.000	0.000	0.000	0.000
79	A	158	ASP	-1	-0.831	-0.930	17.565	14.162	14.162	0.000	0.000	0.000	0.000
80	A	159	TRP	0	-0.038	-0.016	15.698	1.673	1.673	0.000	0.000	0.000	0.000
81	A	160	PHE	0	-0.012	0.001	10.913	0.073	0.073	0.000	0.000	0.000	0.000
82	A	161	ASP	-1	-0.819	-0.921	11.602	27.425	27.425	0.000	0.000	0.000	0.000
83	A	162	ASP	-1	-0.867	-0.931	14.817	16.935	16.935	0.000	0.000	0.000	0.000
84	A	163	ASN	0	-0.058	-0.032	11.606	-1.678	-1.678	0.000	0.000	0.000	0.000
85	A	164	ASN	0	-0.059	-0.053	8.444	4.681	4.681	0.000	0.000	0.000	0.000
86	A	165	LEU	0	0.027	0.018	11.628	-1.925	-1.925	0.000	0.000	0.000	0.000
87	A	166	MET	0	-0.039	-0.015	12.075	2.906	2.906	0.000	0.000	0.000	0.000
88	A	167	VAL	0	-0.006	-0.020	13.614	-1.630	-1.630	0.000	0.000	0.000	0.000
89	A	168	VAL	0	0.024	0.023	14.890	1.157	1.157	0.000	0.000	0.000	0.000
90	A	169	ILE	0	-0.029	-0.003	14.135	-0.594	-0.594	0.000	0.000	0.000	0.000
91	A	170	SER	0	0.045	0.027	17.962	0.056	0.056	0.000	0.000	0.000	0.000
92	A	171	ARG	1	0.933	0.955	21.544	-13.578	-13.578	0.000	0.000	0.000	0.000
93	A	172	ALA	0	-0.023	-0.036	24.102	-0.059	-0.059	0.000	0.000	0.000	0.000
94	A	173	HIS	0	-0.029	-0.010	25.656	-0.379	-0.379	0.000	0.000	0.000	0.000
95	A	174	GLY	0	0.000	0.008	28.849	0.252	0.252	0.000	0.000	0.000	0.000
96	A	175	THR	0	0.019	-0.001	30.691	0.242	0.242	0.000	0.000	0.000	0.000
97	A	176	VAL	0	0.065	0.048	28.931	0.058	0.058	0.000	0.000	0.000	0.000
98	A	177	SER	0	-0.036	-0.013	25.931	0.212	0.212	0.000	0.000	0.000	0.000
99	A	178	GLN	0	-0.010	-0.016	26.347	0.353	0.353	0.000	0.000	0.000	0.000
100	A	179	GLY	0	0.031	0.001	22.771	0.246	0.246	0.000	0.000	0.000	0.000
101	A	180	GLY	0	-0.065	-0.036	20.269	-0.333	-0.333	0.000	0.000	0.000	0.000
102	A	181	ILE	0	-0.034	0.005	13.936	0.003	0.003	0.000	0.000	0.000	0.000
103	A	182	LEU	0	0.022	0.023	14.265	-0.013	-0.013	0.000	0.000	0.000	0.000
104	A	183	TYR	0	0.050	0.001	9.950	1.151	1.151	0.000	0.000	0.000	0.000
105	A	184	LYS	1	0.941	0.985	6.377	-46.362	-46.362	0.000	0.000	0.000	0.000
106	A	185	VAL	0	-0.002	-0.014	7.873	4.764	4.764	0.000	0.000	0.000	0.000
107	A	186	ASN	0	0.048	0.029	7.082	-6.199	-6.199	0.000	0.000	0.000	0.000
108	A	187	ILE	0	-0.016	-0.014	9.320	-1.161	-1.161	0.000	0.000	0.000	0.000
109	A	188	GLU	-1	-0.838	-0.885	11.748	17.826	17.826	0.000	0.000	0.000	0.000
110	A	189	THR	0	0.047	0.006	7.458	-0.599	-0.599	0.000	0.000	0.000	0.000
111	A	190	GLY	0	0.019	0.023	10.328	-0.574	-0.574	0.000	0.000	0.000	0.000
112	A	191	GLN	0	-0.031	-0.016	4.266	-6.754	-6.571	-0.001	-0.029	-0.153	0.000
113	A	192	ALA	0	0.014	0.001	6.711	0.131	0.131	0.000	0.000	0.000	0.000
114	A	193	THR	0	0.024	-0.001	3.171	1.394	3.344	0.128	-1.037	-1.041	0.009
115	A	194	GLU	-1	-0.943	-0.964	6.444	21.953	21.953	0.000	0.000	0.000	0.000
116	A	195	LEU	0	-0.087	-0.043	8.792	2.126	2.126	0.000	0.000	0.000	0.000
117	A	196	TYR	0	0.024	-0.003	11.249	-1.316	-1.316	0.000	0.000	0.000	0.000
118	A	197	ASN	0	0.012	0.016	14.088	-2.015	-2.015	0.000	0.000	0.000	0.000
119	A	198	THR	0	-0.021	-0.030	15.673	0.225	0.225	0.000	0.000	0.000	0.000
120	A	199	LYS	1	0.881	0.940	14.607	-20.729	-20.729	0.000	0.000	0.000	0.000
121	A	200	ASP	-1	-0.803	-0.905	19.510	11.909	11.909	0.000	0.000	0.000	0.000
122	A	201	ASN	0	-0.052	-0.024	22.959	0.162	0.162	0.000	0.000	0.000	0.000
123	A	202	LYS	1	0.929	0.972	24.401	-10.968	-10.968	0.000	0.000	0.000	0.000
124	A	203	LYS	1	0.909	0.979	23.345	-12.912	-12.912	0.000	0.000	0.000	0.000
125	A	204	GLN	0	0.017	0.023	22.269	0.845	0.845	0.000	0.000	0.000	0.000
126	A	205	VAL	0	-0.018	-0.002	17.891	-0.343	-0.343	0.000	0.000	0.000	0.000
127	A	206	VAL	0	0.049	0.020	21.005	0.204	0.204	0.000	0.000	0.000	0.000
128	A	207	TYR	0	-0.038	-0.020	21.231	0.177	0.177	0.000	0.000	0.000	0.000
129	A	208	ALA	0	-0.004	-0.009	18.307	0.310	0.310	0.000	0.000	0.000	0.000
130	A	209	VAL	0	0.031	0.027	20.304	-0.095	-0.095	0.000	0.000	0.000	0.000
131	A	210	LYS	1	0.880	0.960	14.257	-20.516	-20.516	0.000	0.000	0.000	0.000
132	A	211	LYS	1	0.954	0.974	19.438	-13.688	-13.688	0.000	0.000	0.000	0.000
133	A	212	GLY	0	-0.014	-0.002	19.456	-0.181	-0.181	0.000	0.000	0.000	0.000
134	A	213	ASP	-1	-0.875	-0.953	16.191	17.793	17.793	0.000	0.000	0.000	0.000
135	A	214	LYS	1	0.936	0.974	16.430	-14.168	-14.168	0.000	0.000	0.000	0.000
136	A	215	ILE	0	-0.020	-0.024	13.963	0.084	0.084	0.000	0.000	0.000	0.000
137	A	216	ASP	-1	-0.819	-0.870	18.274	13.792	13.792	0.000	0.000	0.000	0.000
138	A	217	VAL	0	-0.049	-0.055	17.302	0.266	0.266	0.000	0.000	0.000	0.000
139	A	218	GLN	0	0.042	0.069	20.524	-0.465	-0.465	0.000	0.000	0.000	0.000
140	A	219	ILE	0	-0.046	-0.030	21.083	0.611	0.611	0.000	0.000	0.000	0.000
141	A	220	LEU	0	0.045	0.028	24.025	-0.458	-0.458	0.000	0.000	0.000	0.000
142	A	221	VAL	0	-0.070	-0.054	26.403	0.450	0.450	0.000	0.000	0.000	0.000
143	A	222	TYR	0	0.020	0.010	28.398	-0.404	-0.404	0.000	0.000	0.000	0.000
144	A	223	GLU	-1	-0.832	-0.901	30.796	10.063	10.063	0.000	0.000	0.000	0.000
145	A	224	ASP	-1	-0.884	-0.952	33.507	8.932	8.932	0.000	0.000	0.000	0.000
146	A	225	ASP	-1	-0.910	-0.974	31.925	10.376	10.376	0.000	0.000	0.000	0.000
147	A	226	ASP	-1	-0.932	-0.943	34.018	8.341	8.341	0.000	0.000	0.000	0.000
148	A	227	LEU	0	-0.149	-0.086	31.015	0.050	0.050	0.000	0.000	0.000	0.000
149	A	228	LEU	0	-0.018	-0.005	34.511	-0.015	-0.015	0.000	0.000	0.000	0.000
150	A	229	GLU	-1	-0.925	-0.950	36.209	8.354	8.354	0.000	0.000	0.000	0.000
151	A	230	SER	0	-0.048	-0.030	31.599	0.201	0.201	0.000	0.000	0.000	0.000
152	A	231	HIS	1	0.804	0.886	29.628	-10.711	-10.711	0.000	0.000	0.000	0.000
153	A	232	GLU	-1	-0.894	-0.948	28.703	11.457	11.457	0.000	0.000	0.000	0.000
154	A	233	GLU	-1	-0.950	-0.981	25.687	11.978	11.978	0.000	0.000	0.000	0.000
155	A	234	THR	0	0.036	-0.022	24.636	0.192	0.192	0.000	0.000	0.000	0.000
156	A	235	LYS	1	0.856	0.941	20.842	-13.311	-13.311	0.000	0.000	0.000	0.000
157	A	236	THR	0	0.016	-0.005	20.716	0.457	0.457	0.000	0.000	0.000	0.000
158	A	237	ILE	0	-0.035	-0.010	13.920	0.045	0.045	0.000	0.000	0.000	0.000
159	A	238	THR	0	-0.020	-0.022	16.038	-0.615	-0.615	0.000	0.000	0.000	0.000
160	A	239	VAL	0	-0.037	-0.013	11.548	1.566	1.566	0.000	0.000	0.000	0.000
161	A	240	LYS	1	0.983	0.993	9.674	-24.518	-24.518	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:80:ASP)