FMO DATABASE

FMODB ID: LR1Z9

Calculation Name: 1REG-X-Xray549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1REG

Chain ID: X

ChEMBL ID:

UniProt ID: P69702

Base Structure: X-ray

Registration Date: 2025-10-11

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	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	122
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1140803.264305
FMO2-HF: Nuclear repulsion	1089089.857704
FMO2-HF: Total energy	-51713.4066
FMO2-MP2: Total energy	-51862.15072

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(X:1:MET)

Summations of interaction energy for fragment #1(X:1:MET)

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.
-82.093	-73.788	31.718	-16.133	-23.886	-0.169

Interaction energy analysis for fragmet #1(X:1:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.698 / q_NPA : 0.835

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	X	3	GLU	-1	-0.892	-0.961	3.849	-26.291	-24.682	-0.011	-0.535	-1.064	-0.001
4	X	4	ILE	0	-0.024	-0.011	5.201	1.859	1.926	-0.001	-0.005	-0.060	0.000
39	X	39	LEU	0	-0.023	-0.014	3.248	2.300	2.400	1.553	-0.272	-1.381	0.001
41	X	41	LYS	1	0.890	0.953	2.350	33.103	33.457	0.833	-0.206	-0.981	0.002
46	X	46	TYR	0	0.033	0.006	2.274	-4.550	-2.481	4.850	-1.879	-5.039	-0.022
47	X	47	ILE	0	0.025	0.027	4.191	5.280	5.732	0.000	-0.086	-0.366	0.000
48	X	48	VAL	0	-0.016	-0.017	2.312	-25.234	-21.188	3.497	-2.817	-4.725	-0.030
49	X	49	HIS	0	0.095	0.040	3.351	8.015	8.153	0.042	0.114	-0.294	-0.001
52	X	52	GLU	-1	-0.795	-0.882	1.865	-135.456	-138.127	17.743	-8.480	-6.592	-0.100
55	X	55	ARG	1	0.928	0.963	3.775	52.042	52.290	0.000	-0.050	-0.197	0.000
56	X	56	MET	0	-0.095	-0.053	4.256	-0.481	0.034	0.050	-0.120	-0.445	0.000
63	X	63	MET	0	-0.091	-0.037	4.096	0.667	0.771	-0.001	-0.020	-0.082	0.000
68	X	68	GLU	-1	-0.892	-0.944	5.166	-54.803	-54.780	-0.001	-0.002	-0.019	0.000
71	X	71	ARG	1	0.770	0.834	2.434	65.154	66.405	3.164	-1.775	-2.641	-0.018
5	X	5	THR	0	0.016	0.008	8.178	1.802	1.802	0.000	0.000	0.000	0.000
6	X	6	LEU	0	-0.017	-0.011	11.314	-0.035	-0.035	0.000	0.000	0.000	0.000
7	X	7	LYS	1	0.907	0.929	14.049	17.345	17.345	0.000	0.000	0.000	0.000
8	X	8	LYS	1	0.845	0.933	17.315	14.199	14.199	0.000	0.000	0.000	0.000
9	X	9	PRO	0	0.053	0.020	16.141	-0.717	-0.717	0.000	0.000	0.000	0.000
10	X	10	GLU	-1	-0.790	-0.899	16.123	-14.106	-14.106	0.000	0.000	0.000	0.000
11	X	11	ASP	-1	-0.834	-0.922	15.664	-15.428	-15.428	0.000	0.000	0.000	0.000
12	X	12	PHE	0	0.013	0.003	9.188	-0.398	-0.398	0.000	0.000	0.000	0.000
13	X	13	LEU	0	-0.008	-0.008	13.407	-0.726	-0.726	0.000	0.000	0.000	0.000
14	X	14	LYS	1	0.912	0.961	16.102	16.593	16.593	0.000	0.000	0.000	0.000
15	X	15	VAL	0	0.029	0.022	10.885	0.172	0.172	0.000	0.000	0.000	0.000
16	X	16	LYS	1	0.918	0.967	11.261	19.356	19.356	0.000	0.000	0.000	0.000
17	X	17	GLU	-1	-0.777	-0.850	13.240	-14.487	-14.487	0.000	0.000	0.000	0.000
18	X	18	THR	0	-0.004	-0.004	15.051	0.467	0.467	0.000	0.000	0.000	0.000
19	X	19	LEU	0	0.003	0.005	9.364	0.201	0.201	0.000	0.000	0.000	0.000
20	X	20	THR	0	-0.111	-0.054	13.552	0.313	0.313	0.000	0.000	0.000	0.000
21	X	21	ARG	1	0.775	0.857	16.377	15.590	15.590	0.000	0.000	0.000	0.000
22	X	22	MET	0	-0.003	0.004	13.668	0.625	0.625	0.000	0.000	0.000	0.000
23	X	23	GLY	0	0.031	0.016	14.770	-1.301	-1.301	0.000	0.000	0.000	0.000
24	X	24	ILE	0	0.002	0.016	15.659	0.638	0.638	0.000	0.000	0.000	0.000
25	X	25	ALA	0	-0.016	-0.014	18.252	0.275	0.275	0.000	0.000	0.000	0.000
26	X	26	ASN	0	0.001	0.005	21.875	0.499	0.499	0.000	0.000	0.000	0.000
27	X	27	ASN	0	0.041	-0.010	24.921	0.142	0.142	0.000	0.000	0.000	0.000
28	X	28	LYS	1	0.961	0.989	27.666	9.791	9.791	0.000	0.000	0.000	0.000
29	X	29	ASP	-1	-0.842	-0.900	27.705	-10.909	-10.909	0.000	0.000	0.000	0.000
30	X	30	LYS	1	0.853	0.934	27.140	10.648	10.648	0.000	0.000	0.000	0.000
31	X	31	VAL	0	0.036	0.029	22.105	-0.050	-0.050	0.000	0.000	0.000	0.000
32	X	32	LEU	0	-0.033	-0.019	18.688	0.023	0.023	0.000	0.000	0.000	0.000
33	X	33	TYR	0	0.011	-0.004	16.914	-0.139	-0.139	0.000	0.000	0.000	0.000
34	X	34	GLN	0	0.022	0.014	11.443	0.653	0.653	0.000	0.000	0.000	0.000
35	X	35	SER	0	0.020	0.005	11.152	0.442	0.442	0.000	0.000	0.000	0.000
36	X	36	CYS	0	-0.007	0.019	7.596	-4.436	-4.436	0.000	0.000	0.000	0.000
37	X	37	HIS	0	0.020	0.006	6.999	4.155	4.155	0.000	0.000	0.000	0.000
38	X	38	ILE	0	0.017	0.024	6.098	-3.704	-3.704	0.000	0.000	0.000	0.000
40	X	40	GLN	0	0.055	0.016	6.579	-0.568	-0.568	0.000	0.000	0.000	0.000
42	X	42	LYS	1	0.949	0.963	6.890	17.715	17.715	0.000	0.000	0.000	0.000
43	X	43	GLY	0	0.042	0.028	9.664	0.198	0.198	0.000	0.000	0.000	0.000
44	X	44	LEU	0	0.007	0.034	6.805	0.454	0.454	0.000	0.000	0.000	0.000
45	X	45	TYR	0	0.022	-0.010	7.539	0.412	0.412	0.000	0.000	0.000	0.000
50	X	50	PHE	0	0.044	-0.005	5.942	-0.705	-0.705	0.000	0.000	0.000	0.000
51	X	51	LYS	1	0.856	0.913	7.980	27.309	27.309	0.000	0.000	0.000	0.000
53	X	53	MET	0	-0.044	-0.010	5.560	1.812	1.812	0.000	0.000	0.000	0.000
54	X	54	LEU	0	0.047	0.024	7.457	1.565	1.565	0.000	0.000	0.000	0.000
57	X	57	ASP	-1	-0.830	-0.873	8.814	-20.367	-20.367	0.000	0.000	0.000	0.000
58	X	58	GLY	0	-0.021	-0.013	11.986	1.733	1.733	0.000	0.000	0.000	0.000
59	X	59	ARG	1	0.864	0.935	12.749	18.650	18.650	0.000	0.000	0.000	0.000
60	X	60	GLN	0	0.025	0.008	12.884	-2.492	-2.492	0.000	0.000	0.000	0.000
61	X	61	VAL	0	-0.037	-0.020	10.254	0.945	0.945	0.000	0.000	0.000	0.000
62	X	62	GLU	-1	-0.892	-0.942	10.799	-24.256	-24.256	0.000	0.000	0.000	0.000
64	X	64	THR	0	0.052	0.008	8.750	0.710	0.710	0.000	0.000	0.000	0.000
65	X	65	GLU	-1	-0.871	-0.955	9.506	-25.494	-25.494	0.000	0.000	0.000	0.000
66	X	66	GLU	-1	-0.916	-0.947	10.327	-21.209	-21.209	0.000	0.000	0.000	0.000
67	X	67	ASP	-1	-0.813	-0.884	8.296	-28.116	-28.116	0.000	0.000	0.000	0.000
69	X	69	VAL	0	0.078	0.046	6.875	-1.491	-1.491	0.000	0.000	0.000	0.000
70	X	70	ARG	1	0.853	0.938	9.919	22.277	22.277	0.000	0.000	0.000	0.000
72	X	72	ASP	-1	-0.759	-0.864	5.219	-51.608	-51.608	0.000	0.000	0.000	0.000
73	X	73	SER	0	0.016	-0.003	7.742	3.347	3.347	0.000	0.000	0.000	0.000
74	X	74	ILE	0	-0.041	-0.023	9.366	2.570	2.570	0.000	0.000	0.000	0.000
75	X	75	ALA	0	-0.035	-0.013	7.295	1.739	1.739	0.000	0.000	0.000	0.000
76	X	76	TRP	0	0.054	0.000	9.447	2.284	2.284	0.000	0.000	0.000	0.000
77	X	77	LEU	0	-0.006	0.012	12.603	1.717	1.717	0.000	0.000	0.000	0.000
78	X	78	LEU	0	-0.056	-0.039	10.353	1.513	1.513	0.000	0.000	0.000	0.000
79	X	79	GLU	-1	-0.852	-0.923	13.154	-21.684	-21.684	0.000	0.000	0.000	0.000
80	X	80	ASP	-1	-0.821	-0.891	14.898	-16.528	-16.528	0.000	0.000	0.000	0.000
81	X	81	TRP	0	-0.105	-0.064	16.552	0.776	0.776	0.000	0.000	0.000	0.000
82	X	82	GLY	0	0.026	0.019	18.040	0.649	0.649	0.000	0.000	0.000	0.000
83	X	83	LEU	0	-0.139	-0.073	15.042	0.350	0.350	0.000	0.000	0.000	0.000
84	X	84	ILE	0	-0.066	-0.043	10.349	-0.483	-0.483	0.000	0.000	0.000	0.000
85	X	85	GLU	-1	-0.831	-0.889	12.739	-16.827	-16.827	0.000	0.000	0.000	0.000
86	X	86	ILE	0	-0.021	-0.019	8.781	-2.418	-2.418	0.000	0.000	0.000	0.000
87	X	87	VAL	0	-0.042	-0.004	8.779	2.247	2.247	0.000	0.000	0.000	0.000
88	X	88	PRO	0	0.045	0.020	10.457	-2.235	-2.235	0.000	0.000	0.000	0.000
89	X	89	GLY	0	0.016	0.001	12.681	0.170	0.170	0.000	0.000	0.000	0.000
90	X	90	GLN	0	-0.045	-0.017	6.089	-8.746	-8.746	0.000	0.000	0.000	0.000
91	X	91	ARG	1	0.933	0.961	8.374	30.632	30.632	0.000	0.000	0.000	0.000
92	X	92	THR	0	-0.007	-0.001	6.421	-5.127	-5.127	0.000	0.000	0.000	0.000
93	X	93	PHE	0	0.002	0.004	7.815	3.794	3.794	0.000	0.000	0.000	0.000
94	X	94	MET	0	0.002	-0.004	10.336	0.234	0.234	0.000	0.000	0.000	0.000
95	X	95	LYS	1	0.834	0.897	12.783	17.035	17.035	0.000	0.000	0.000	0.000
96	X	96	ASP	-1	-0.823	-0.896	13.831	-16.037	-16.037	0.000	0.000	0.000	0.000
97	X	97	LEU	0	-0.094	-0.054	13.891	-1.315	-1.315	0.000	0.000	0.000	0.000
98	X	98	THR	0	-0.009	-0.021	16.762	0.646	0.646	0.000	0.000	0.000	0.000
99	X	99	ASN	0	-0.026	0.004	18.315	0.014	0.014	0.000	0.000	0.000	0.000
100	X	100	ASN	0	0.014	0.006	19.034	0.381	0.381	0.000	0.000	0.000	0.000
101	X	101	PHE	0	0.065	0.030	14.669	-1.323	-1.323	0.000	0.000	0.000	0.000
102	X	102	ARG	1	0.887	0.955	18.517	13.630	13.630	0.000	0.000	0.000	0.000
103	X	103	VAL	0	0.087	0.045	18.098	-0.753	-0.753	0.000	0.000	0.000	0.000
104	X	104	ILE	0	-0.031	-0.001	20.351	0.852	0.852	0.000	0.000	0.000	0.000
105	X	105	SER	0	0.020	0.006	22.232	-0.137	-0.137	0.000	0.000	0.000	0.000
106	X	106	PHE	0	0.062	0.014	22.252	0.114	0.114	0.000	0.000	0.000	0.000
107	X	107	LYS	1	0.953	0.966	24.646	10.540	10.540	0.000	0.000	0.000	0.000
108	X	108	GLN	0	0.020	0.016	26.514	-0.009	-0.009	0.000	0.000	0.000	0.000
109	X	109	LYS	1	0.914	0.946	20.945	13.599	13.599	0.000	0.000	0.000	0.000
110	X	110	HIS	1	0.918	0.963	25.318	9.972	9.972	0.000	0.000	0.000	0.000
111	X	111	GLU	-1	-0.878	-0.932	28.196	-10.055	-10.055	0.000	0.000	0.000	0.000
112	X	112	TRP	0	-0.069	-0.034	24.188	0.112	0.112	0.000	0.000	0.000	0.000
113	X	113	LYS	1	0.895	0.947	24.752	10.902	10.902	0.000	0.000	0.000	0.000
114	X	114	LEU	0	0.009	-0.001	19.607	-0.277	-0.277	0.000	0.000	0.000	0.000
115	X	115	VAL	0	0.017	0.005	19.379	0.222	0.222	0.000	0.000	0.000	0.000
116	X	116	PRO	0	-0.009	-0.009	14.270	-0.673	-0.673	0.000	0.000	0.000	0.000
117	X	117	LYS	1	0.939	0.965	13.248	18.948	18.948	0.000	0.000	0.000	0.000
118	X	118	TYR	0	-0.110	-0.070	11.109	0.399	0.399	0.000	0.000	0.000	0.000
119	X	119	THR	0	0.004	-0.008	13.290	0.319	0.319	0.000	0.000	0.000	0.000
120	X	120	ILE	0	-0.056	-0.015	16.870	0.966	0.966	0.000	0.000	0.000	0.000
121	X	121	GLY	0	-0.007	0.002	18.315	-0.532	-0.532	0.000	0.000	0.000	0.000
122	X	122	ASN	-1	-0.958	-0.967	20.115	-14.179	-14.179	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(X:1:MET)