FMO DATABASE

FMODB ID: 462NN

Calculation Name: 6L2L-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 6L2L

Chain ID: A

ChEMBL ID:

UniProt ID:

Base Structure: X-ray

Registration Date: 2025-10-04

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	147
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1498395.439794
FMO2-HF: Nuclear repulsion	1438282.898068
FMO2-HF: Total energy	-60112.541726
FMO2-MP2: Total energy	-60287.247347

3D Structure Molmil

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:2:ASP)

Summations of interaction energy for fragment #1(A:2: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.
14.465	19.431	1.838	-3.013	-3.794	-0.029

Interaction energy analysis for fragmet #1(A:2:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.127 / q_NPA : -0.054

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	4	PHE	0	0.049	0.010	3.813	-8.052	-6.646	-0.009	-0.621	-0.776	0.000
4	A	5	ASN	0	0.037	0.035	4.239	-2.347	-2.137	-0.001	-0.041	-0.168	0.000
126	A	127	LYS	1	0.921	0.958	3.605	5.390	5.742	0.000	-0.077	-0.277	0.000
127	A	128	ASN	0	-0.050	-0.044	2.263	-25.777	-23.202	1.844	-2.187	-2.233	-0.029
128	A	129	GLN	0	0.037	0.005	4.096	4.765	4.910	0.001	-0.025	-0.121	0.000
129	A	130	LYS	1	0.967	0.995	3.283	24.385	24.663	0.003	-0.062	-0.219	0.000
5	A	6	ASN	0	0.069	0.020	5.919	-0.380	-0.380	0.000	0.000	0.000	0.000
6	A	7	ILE	0	0.034	0.029	9.317	0.033	0.033	0.000	0.000	0.000	0.000
7	A	8	LEU	0	-0.024	-0.026	5.906	-0.359	-0.359	0.000	0.000	0.000	0.000
8	A	9	ASP	-1	-0.912	-0.960	9.656	-2.565	-2.565	0.000	0.000	0.000	0.000
9	A	10	LEU	0	0.025	0.025	11.273	0.210	0.210	0.000	0.000	0.000	0.000
10	A	11	LEU	0	-0.006	0.000	12.529	0.059	0.059	0.000	0.000	0.000	0.000
11	A	12	ILE	0	0.007	-0.005	10.609	0.179	0.179	0.000	0.000	0.000	0.000
12	A	13	ASN	0	0.022	0.016	14.435	0.166	0.166	0.000	0.000	0.000	0.000
13	A	14	GLU	-1	-0.786	-0.876	16.712	-0.697	-0.697	0.000	0.000	0.000	0.000
14	A	15	SER	0	-0.051	-0.034	17.147	0.092	0.092	0.000	0.000	0.000	0.000
15	A	16	LYS	1	0.906	0.944	16.274	2.174	2.174	0.000	0.000	0.000	0.000
16	A	17	LYS	1	0.798	0.888	20.948	0.943	0.943	0.000	0.000	0.000	0.000
17	A	18	ALA	0	0.026	0.017	23.214	0.113	0.113	0.000	0.000	0.000	0.000
18	A	19	ILE	0	0.037	0.022	21.780	0.075	0.075	0.000	0.000	0.000	0.000
19	A	20	LYS	1	0.874	0.934	25.910	0.842	0.842	0.000	0.000	0.000	0.000
20	A	21	HIS	0	-0.022	-0.022	28.337	0.056	0.056	0.000	0.000	0.000	0.000
21	A	22	ASN	0	0.017	0.006	29.482	0.001	0.001	0.000	0.000	0.000	0.000
22	A	23	ASP	-1	-0.767	-0.863	26.340	-0.877	-0.877	0.000	0.000	0.000	0.000
23	A	24	ILE	0	0.003	0.001	21.998	-0.044	-0.044	0.000	0.000	0.000	0.000
24	A	25	PRO	0	0.018	0.025	19.609	0.046	0.046	0.000	0.000	0.000	0.000
25	A	26	VAL	0	-0.003	0.019	18.546	-0.237	-0.237	0.000	0.000	0.000	0.000
26	A	27	SER	0	-0.042	-0.035	16.770	0.225	0.225	0.000	0.000	0.000	0.000
27	A	28	CYS	0	-0.009	0.004	16.405	-0.262	-0.262	0.000	0.000	0.000	0.000
28	A	29	CYS	0	-0.035	0.003	14.961	0.117	0.117	0.000	0.000	0.000	0.000
29	A	30	ILE	0	0.000	0.005	17.340	-0.124	-0.124	0.000	0.000	0.000	0.000
30	A	31	ILE	0	0.010	0.003	12.561	0.060	0.060	0.000	0.000	0.000	0.000
31	A	32	ASP	-1	-0.738	-0.868	16.633	1.154	1.154	0.000	0.000	0.000	0.000
32	A	33	SER	0	-0.011	-0.019	15.426	-0.013	-0.013	0.000	0.000	0.000	0.000
33	A	34	ASN	0	-0.073	-0.026	14.102	0.452	0.452	0.000	0.000	0.000	0.000
34	A	35	ASN	0	-0.036	-0.022	8.874	-0.195	-0.195	0.000	0.000	0.000	0.000
35	A	36	ASN	0	-0.017	-0.008	12.874	-0.034	-0.034	0.000	0.000	0.000	0.000
36	A	37	ILE	0	-0.024	-0.029	14.243	-0.211	-0.211	0.000	0.000	0.000	0.000
37	A	38	LEU	0	-0.021	0.002	17.214	0.049	0.049	0.000	0.000	0.000	0.000
38	A	39	SER	0	-0.005	-0.025	20.323	-0.003	-0.003	0.000	0.000	0.000	0.000
39	A	40	LEU	0	-0.012	-0.021	17.655	-0.073	-0.073	0.000	0.000	0.000	0.000
40	A	41	ALA	0	0.004	0.017	20.288	0.074	0.074	0.000	0.000	0.000	0.000
41	A	42	ILE	0	0.022	0.009	20.299	-0.193	-0.193	0.000	0.000	0.000	0.000
42	A	43	ASN	0	-0.053	-0.023	22.295	0.163	0.163	0.000	0.000	0.000	0.000
43	A	44	SER	0	-0.020	-0.009	24.464	-0.013	-0.013	0.000	0.000	0.000	0.000
44	A	45	ARG	1	0.890	0.963	28.118	0.867	0.867	0.000	0.000	0.000	0.000
45	A	46	TYR	0	-0.008	-0.029	29.700	0.044	0.044	0.000	0.000	0.000	0.000
46	A	47	LYS	1	0.841	0.931	29.779	0.591	0.591	0.000	0.000	0.000	0.000
47	A	48	ASN	0	-0.041	-0.042	31.306	0.053	0.053	0.000	0.000	0.000	0.000
48	A	49	LYS	1	0.945	0.982	34.092	0.505	0.505	0.000	0.000	0.000	0.000
49	A	50	ASP	-1	-0.755	-0.827	33.166	-0.458	-0.458	0.000	0.000	0.000	0.000
50	A	51	ILE	0	0.031	0.001	32.360	-0.054	-0.054	0.000	0.000	0.000	0.000
51	A	52	SER	0	0.007	-0.033	30.906	-0.063	-0.063	0.000	0.000	0.000	0.000
52	A	53	GLN	0	0.006	0.025	28.760	-0.069	-0.069	0.000	0.000	0.000	0.000
53	A	54	HIS	0	-0.023	-0.040	24.243	-0.055	-0.055	0.000	0.000	0.000	0.000
54	A	55	ALA	0	0.001	0.008	20.799	0.076	0.076	0.000	0.000	0.000	0.000
55	A	56	GLU	-1	-0.761	-0.913	19.699	-1.291	-1.291	0.000	0.000	0.000	0.000
56	A	57	ILE	0	0.012	0.001	22.553	0.101	0.101	0.000	0.000	0.000	0.000
57	A	58	ASN	0	-0.039	-0.024	24.976	0.130	0.130	0.000	0.000	0.000	0.000
58	A	59	VAL	0	-0.018	-0.018	20.694	0.080	0.080	0.000	0.000	0.000	0.000
59	A	60	ILE	0	0.011	0.010	23.790	0.097	0.097	0.000	0.000	0.000	0.000
60	A	61	ASN	0	0.008	0.001	25.748	0.099	0.099	0.000	0.000	0.000	0.000
61	A	62	ASP	-1	-0.828	-0.856	25.597	-0.141	-0.141	0.000	0.000	0.000	0.000
62	A	63	LEU	0	0.031	0.008	22.560	0.066	0.066	0.000	0.000	0.000	0.000
63	A	64	ILE	0	-0.030	-0.014	26.311	0.061	0.061	0.000	0.000	0.000	0.000
64	A	65	SER	0	-0.049	-0.023	29.726	0.053	0.053	0.000	0.000	0.000	0.000
65	A	66	LYS	1	0.826	0.889	24.867	0.115	0.115	0.000	0.000	0.000	0.000
66	A	67	LEU	0	-0.035	-0.019	25.347	0.058	0.058	0.000	0.000	0.000	0.000
67	A	68	ASN	0	-0.019	0.006	29.785	-0.002	-0.002	0.000	0.000	0.000	0.000
68	A	69	SER	0	0.003	0.000	30.363	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	70	PHE	0	0.069	0.024	30.158	-0.020	-0.020	0.000	0.000	0.000	0.000
70	A	71	ASN	0	-0.037	-0.001	28.585	-0.043	-0.043	0.000	0.000	0.000	0.000
71	A	72	LEU	0	0.022	0.000	24.312	0.058	0.058	0.000	0.000	0.000	0.000
72	A	73	SER	0	-0.013	-0.026	23.494	0.032	0.032	0.000	0.000	0.000	0.000
73	A	74	LYS	1	0.874	0.955	22.139	-0.382	-0.382	0.000	0.000	0.000	0.000
74	A	75	TYR	0	0.014	0.010	19.433	0.127	0.127	0.000	0.000	0.000	0.000
75	A	76	LYS	1	0.870	0.937	14.756	-0.395	-0.395	0.000	0.000	0.000	0.000
76	A	77	LEU	0	0.021	0.020	16.755	0.036	0.036	0.000	0.000	0.000	0.000
77	A	78	ILE	0	0.000	0.001	11.289	-0.243	-0.243	0.000	0.000	0.000	0.000
78	A	79	THR	0	0.006	-0.017	13.907	0.103	0.103	0.000	0.000	0.000	0.000
79	A	80	THR	0	0.014	-0.003	13.089	-0.484	-0.484	0.000	0.000	0.000	0.000
80	A	81	LEU	0	-0.042	-0.026	14.087	-0.447	-0.447	0.000	0.000	0.000	0.000
81	A	82	GLU	-1	-0.764	-0.862	16.520	-1.700	-1.700	0.000	0.000	0.000	0.000
82	A	83	PRO	0	-0.012	-0.001	17.734	0.147	0.147	0.000	0.000	0.000	0.000
83	A	84	CYS	0	0.017	0.022	20.843	0.073	0.073	0.000	0.000	0.000	0.000
84	A	85	MET	0	0.030	0.004	24.379	0.017	0.017	0.000	0.000	0.000	0.000
85	A	86	MET	0	-0.011	0.015	26.915	0.070	0.070	0.000	0.000	0.000	0.000
86	A	87	CYS	0	-0.012	-0.007	23.363	0.083	0.083	0.000	0.000	0.000	0.000
87	A	88	TYR	0	0.042	0.019	22.158	0.106	0.106	0.000	0.000	0.000	0.000
88	A	89	SER	0	-0.014	-0.004	24.330	0.087	0.087	0.000	0.000	0.000	0.000
89	A	90	ALA	0	0.025	0.014	26.758	0.061	0.061	0.000	0.000	0.000	0.000
90	A	91	ILE	0	0.029	-0.002	20.696	0.058	0.058	0.000	0.000	0.000	0.000
91	A	92	LYS	1	0.953	0.983	24.512	0.543	0.543	0.000	0.000	0.000	0.000
92	A	93	GLN	0	-0.071	-0.029	26.199	0.099	0.099	0.000	0.000	0.000	0.000
93	A	94	VAL	0	-0.006	0.000	25.394	0.053	0.053	0.000	0.000	0.000	0.000
94	A	95	LYS	1	0.919	0.955	26.347	0.151	0.151	0.000	0.000	0.000	0.000
95	A	96	ILE	0	0.000	0.025	20.077	0.055	0.055	0.000	0.000	0.000	0.000
96	A	97	ASN	0	0.090	0.038	19.343	-0.115	-0.115	0.000	0.000	0.000	0.000
97	A	98	THR	0	-0.049	-0.031	14.318	0.087	0.087	0.000	0.000	0.000	0.000
98	A	99	ILE	0	0.031	0.036	16.037	0.056	0.056	0.000	0.000	0.000	0.000
99	A	100	TYR	0	0.033	0.008	10.615	-0.112	-0.112	0.000	0.000	0.000	0.000
100	A	101	TYR	0	0.040	0.011	11.990	0.138	0.138	0.000	0.000	0.000	0.000
101	A	102	LEU	0	-0.033	0.000	7.972	-0.844	-0.844	0.000	0.000	0.000	0.000
102	A	103	VAL	0	-0.009	0.001	10.806	-0.705	-0.705	0.000	0.000	0.000	0.000
103	A	104	ASP	-1	-0.791	-0.892	13.786	-2.642	-2.642	0.000	0.000	0.000	0.000
104	A	105	SER	0	0.005	-0.027	16.374	0.033	0.033	0.000	0.000	0.000	0.000
105	A	106	TYR	0	-0.040	-0.024	19.643	0.142	0.142	0.000	0.000	0.000	0.000
106	A	107	LYS	1	0.833	0.911	14.004	3.671	3.671	0.000	0.000	0.000	0.000
107	A	108	PHE	0	-0.025	-0.019	17.386	-0.016	-0.016	0.000	0.000	0.000	0.000
108	A	109	GLY	0	0.018	0.019	22.273	0.129	0.129	0.000	0.000	0.000	0.000
109	A	110	ILE	0	0.011	0.016	24.579	-0.039	-0.039	0.000	0.000	0.000	0.000
110	A	111	LYS	1	0.967	0.988	20.955	1.403	1.403	0.000	0.000	0.000	0.000
111	A	112	ASN	0	-0.015	-0.005	21.718	0.021	0.021	0.000	0.000	0.000	0.000
112	A	113	ASN	0	0.020	0.004	24.250	-0.063	-0.063	0.000	0.000	0.000	0.000
113	A	114	TYR	0	-0.017	-0.032	20.345	0.115	0.115	0.000	0.000	0.000	0.000
114	A	115	SER	0	-0.044	-0.018	24.331	-0.071	-0.071	0.000	0.000	0.000	0.000
115	A	116	ILE	0	-0.030	-0.034	22.114	0.066	0.066	0.000	0.000	0.000	0.000
116	A	117	ASN	0	-0.021	-0.009	23.053	-0.007	-0.007	0.000	0.000	0.000	0.000
117	A	118	ASP	-1	-0.867	-0.918	22.157	-0.379	-0.379	0.000	0.000	0.000	0.000
118	A	119	GLN	0	0.011	0.015	24.129	0.047	0.047	0.000	0.000	0.000	0.000
119	A	120	ASN	0	-0.041	-0.038	23.325	-0.051	-0.051	0.000	0.000	0.000	0.000
120	A	121	LEU	0	-0.058	-0.014	20.111	0.040	0.040	0.000	0.000	0.000	0.000
121	A	122	ASN	0	0.005	0.018	16.616	-0.074	-0.074	0.000	0.000	0.000	0.000
122	A	123	LEU	0	0.000	-0.005	16.467	-0.037	-0.037	0.000	0.000	0.000	0.000
123	A	124	ILE	0	-0.012	-0.010	10.359	-0.110	-0.110	0.000	0.000	0.000	0.000
124	A	125	GLN	0	-0.023	0.003	9.133	0.397	0.397	0.000	0.000	0.000	0.000
125	A	126	ILE	0	0.035	0.010	5.549	-0.633	-0.633	0.000	0.000	0.000	0.000
130	A	131	LYS	1	0.946	0.990	6.301	8.170	8.170	0.000	0.000	0.000	0.000
131	A	132	GLN	0	-0.005	-0.003	7.776	1.507	1.507	0.000	0.000	0.000	0.000
132	A	133	SER	0	0.003	0.004	9.826	1.322	1.322	0.000	0.000	0.000	0.000
133	A	134	GLU	-1	-0.954	-0.982	10.975	-3.185	-3.185	0.000	0.000	0.000	0.000
134	A	135	TYR	0	0.014	-0.035	12.054	0.563	0.563	0.000	0.000	0.000	0.000
135	A	136	ILE	0	0.032	0.009	13.590	0.484	0.484	0.000	0.000	0.000	0.000
136	A	137	LYS	1	0.953	0.990	14.981	3.581	3.581	0.000	0.000	0.000	0.000
137	A	138	LEU	0	0.006	0.007	16.629	0.304	0.304	0.000	0.000	0.000	0.000
138	A	139	LEU	0	-0.009	0.000	17.133	0.279	0.279	0.000	0.000	0.000	0.000
139	A	140	ASN	0	-0.018	-0.020	19.007	0.354	0.354	0.000	0.000	0.000	0.000
140	A	141	ILE	0	-0.006	0.002	20.441	0.166	0.166	0.000	0.000	0.000	0.000
141	A	142	PHE	0	0.005	0.002	22.468	0.140	0.140	0.000	0.000	0.000	0.000
142	A	143	PHE	0	0.009	-0.016	21.749	0.141	0.141	0.000	0.000	0.000	0.000
143	A	144	ILE	0	-0.052	-0.018	25.624	0.082	0.082	0.000	0.000	0.000	0.000
144	A	145	ASN	0	0.027	0.007	26.907	0.088	0.088	0.000	0.000	0.000	0.000
145	A	146	LYS	1	0.902	0.962	28.413	1.028	1.028	0.000	0.000	0.000	0.000
146	A	147	ARG	1	0.839	0.908	26.536	1.227	1.227	0.000	0.000	0.000	0.000
147	A	148	LEU	-1	-0.914	-0.918	31.680	-0.707	-0.707	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ASP)