FMO DATABASE

FMODB ID: 66VMZ

Calculation Name: 1REG-X-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1REG

Chain ID: X

ChEMBL ID:

UniProt ID: P69702

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:

Apendix: None

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	122
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1143431.527503
FMO2-HF: Nuclear repulsion	1091717.714952
FMO2-HF: Total energy	-51713.812552
FMO2-MP2: Total energy	-51862.640672

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(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.
-26.411	-18.231	21.716	-10.87	-19.02	-0.072

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 : 0 / q_Mulliken : -0.099 / q_NPA : -0.063

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

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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	-0.823	-0.898	3.871	-1.719	-0.289	-0.014	-0.535	-0.882	0.002
4	X	4	ILE	0	-0.035	-0.016	5.416	0.482	0.482	0.000	0.000	0.000	0.000
5	X	5	THR	0	-0.004	-0.028	8.503	0.179	0.179	0.000	0.000	0.000	0.000
6	X	6	LEU	0	-0.032	-0.019	11.106	0.045	0.045	0.000	0.000	0.000	0.000
7	X	7	LYS	1	0.851	0.904	13.977	0.122	0.122	0.000	0.000	0.000	0.000
8	X	8	LYS	1	0.825	0.898	17.336	-0.108	-0.108	0.000	0.000	0.000	0.000
9	X	9	PRO	0	0.049	0.020	16.287	0.017	0.017	0.000	0.000	0.000	0.000
10	X	10	GLU	-1	-0.776	-0.882	16.231	0.190	0.190	0.000	0.000	0.000	0.000
11	X	11	ASP	-1	-0.814	-0.899	16.280	0.115	0.115	0.000	0.000	0.000	0.000
12	X	12	PHE	0	0.026	0.009	9.101	0.003	0.003	0.000	0.000	0.000	0.000
13	X	13	LEU	0	-0.008	-0.004	13.440	0.047	0.047	0.000	0.000	0.000	0.000
14	X	14	LYS	1	0.882	0.946	16.107	-0.109	-0.109	0.000	0.000	0.000	0.000
15	X	15	VAL	0	0.037	0.027	11.275	-0.006	-0.006	0.000	0.000	0.000	0.000
16	X	16	LYS	1	0.863	0.934	10.259	-0.757	-0.757	0.000	0.000	0.000	0.000
17	X	17	GLU	-1	-0.772	-0.849	13.396	0.185	0.185	0.000	0.000	0.000	0.000
18	X	18	THR	0	-0.002	-0.011	15.370	-0.022	-0.022	0.000	0.000	0.000	0.000
19	X	19	LEU	0	0.000	0.006	9.654	-0.012	-0.012	0.000	0.000	0.000	0.000
20	X	20	THR	0	-0.109	-0.052	13.657	-0.011	-0.011	0.000	0.000	0.000	0.000
21	X	21	ARG	1	0.763	0.859	16.498	-0.186	-0.186	0.000	0.000	0.000	0.000
22	X	22	MET	0	-0.006	0.003	13.648	-0.025	-0.025	0.000	0.000	0.000	0.000
23	X	23	GLY	0	0.027	0.014	14.855	0.035	0.035	0.000	0.000	0.000	0.000
24	X	24	ILE	0	0.012	0.023	15.412	-0.020	-0.020	0.000	0.000	0.000	0.000
25	X	25	ALA	0	-0.017	-0.017	18.295	0.011	0.011	0.000	0.000	0.000	0.000
26	X	26	ASN	0	0.003	-0.002	21.867	-0.019	-0.019	0.000	0.000	0.000	0.000
27	X	27	ASN	0	0.053	0.007	25.059	0.009	0.009	0.000	0.000	0.000	0.000
28	X	28	LYS	1	0.973	0.996	27.884	-0.052	-0.052	0.000	0.000	0.000	0.000
29	X	29	ASP	-1	-0.819	-0.893	27.977	0.092	0.092	0.000	0.000	0.000	0.000
30	X	30	LYS	1	0.802	0.899	27.143	-0.084	-0.084	0.000	0.000	0.000	0.000
31	X	31	VAL	0	0.019	0.022	22.276	0.009	0.009	0.000	0.000	0.000	0.000
32	X	32	LEU	0	-0.024	-0.018	18.817	-0.013	-0.013	0.000	0.000	0.000	0.000
33	X	33	TYR	0	0.010	-0.004	17.112	0.010	0.010	0.000	0.000	0.000	0.000
34	X	34	GLN	0	0.032	0.022	11.833	-0.034	-0.034	0.000	0.000	0.000	0.000
35	X	35	SER	0	0.004	-0.001	11.204	0.015	0.015	0.000	0.000	0.000	0.000
36	X	36	CYS	0	-0.001	0.020	7.455	0.027	0.027	0.000	0.000	0.000	0.000
37	X	37	HIS	0	0.025	0.004	7.215	-0.021	-0.021	0.000	0.000	0.000	0.000
38	X	38	ILE	0	0.027	0.032	6.674	-0.011	-0.011	0.000	0.000	0.000	0.000
39	X	39	LEU	0	0.006	0.002	3.461	-0.724	-0.065	0.301	-0.195	-0.764	0.001
40	X	40	GLN	0	0.048	0.017	6.497	-0.259	-0.259	0.000	0.000	0.000	0.000
41	X	41	LYS	1	0.857	0.933	2.360	-3.216	-2.390	0.717	-0.311	-1.231	0.004
42	X	42	LYS	1	0.948	0.963	7.284	-0.837	-0.837	0.000	0.000	0.000	0.000
43	X	43	GLY	0	0.032	0.022	10.020	-0.186	-0.186	0.000	0.000	0.000	0.000
44	X	44	LEU	0	0.008	0.031	6.998	-0.062	-0.062	0.000	0.000	0.000	0.000
45	X	45	TYR	0	0.011	-0.018	7.259	0.685	0.685	0.000	0.000	0.000	0.000
46	X	46	TYR	0	-0.015	-0.038	2.293	-1.255	0.998	4.137	-1.674	-4.716	-0.015
47	X	47	ILE	0	0.009	0.018	4.379	0.513	0.874	-0.001	-0.062	-0.298	0.000
48	X	48	VAL	0	-0.001	-0.008	2.306	-3.367	-1.085	3.334	-2.203	-3.412	-0.018
49	X	49	HIS	0	0.078	0.032	3.442	0.075	0.222	0.023	0.077	-0.245	0.000
50	X	50	PHE	0	0.033	-0.016	6.116	-0.056	-0.056	0.000	0.000	0.000	0.000
51	X	51	LYS	1	0.812	0.906	8.165	0.249	0.249	0.000	0.000	0.000	0.000
52	X	52	GLU	-1	-0.764	-0.861	1.886	-13.617	-15.731	10.698	-4.351	-4.232	-0.052
53	X	53	MET	0	-0.066	-0.017	5.782	0.670	0.670	0.000	0.000	0.000	0.000
54	X	54	LEU	0	0.038	0.017	7.445	0.066	0.066	0.000	0.000	0.000	0.000
55	X	55	ARG	1	0.910	0.943	3.654	0.377	0.706	0.003	-0.072	-0.260	0.000
56	X	56	MET	0	-0.082	-0.043	4.583	0.654	1.211	0.138	-0.149	-0.546	0.000
57	X	57	ASP	-1	-0.828	-0.867	8.700	0.909	0.909	0.000	0.000	0.000	0.000
58	X	58	GLY	0	-0.005	-0.002	11.681	-0.148	-0.148	0.000	0.000	0.000	0.000
59	X	59	ARG	1	0.809	0.896	12.747	-0.467	-0.467	0.000	0.000	0.000	0.000
60	X	60	GLN	0	0.024	0.004	12.945	-0.036	-0.036	0.000	0.000	0.000	0.000
61	X	61	VAL	0	-0.063	-0.026	10.495	0.000	0.000	0.000	0.000	0.000	0.000
62	X	62	GLU	-1	-0.824	-0.918	11.138	-0.298	-0.298	0.000	0.000	0.000	0.000
63	X	63	MET	0	-0.058	-0.028	4.612	0.044	0.104	-0.001	-0.003	-0.055	0.000
64	X	64	THR	0	0.022	0.001	9.215	-0.015	-0.015	0.000	0.000	0.000	0.000
65	X	65	GLU	-1	-0.878	-0.956	9.740	-0.233	-0.233	0.000	0.000	0.000	0.000
66	X	66	GLU	-1	-0.860	-0.913	10.868	0.071	0.071	0.000	0.000	0.000	0.000
67	X	67	ASP	-1	-0.793	-0.876	8.124	0.009	0.009	0.000	0.000	0.000	0.000
68	X	68	GLU	-1	-0.827	-0.905	5.244	-0.556	-0.556	0.000	0.000	0.000	0.000
69	X	69	VAL	0	0.060	0.039	7.208	0.293	0.293	0.000	0.000	0.000	0.000
70	X	70	ARG	1	0.843	0.930	10.322	-0.097	-0.097	0.000	0.000	0.000	0.000
71	X	71	ARG	1	0.738	0.812	2.271	-3.331	-1.941	2.381	-1.392	-2.379	0.006
72	X	72	ASP	-1	-0.739	-0.855	5.879	1.386	1.386	0.000	0.000	0.000	0.000
73	X	73	SER	0	0.003	-0.007	8.141	-0.233	-0.233	0.000	0.000	0.000	0.000
74	X	74	ILE	0	-0.040	-0.024	9.429	-0.073	-0.073	0.000	0.000	0.000	0.000
75	X	75	ALA	0	-0.027	-0.009	7.310	-0.065	-0.065	0.000	0.000	0.000	0.000
76	X	76	TRP	0	0.048	0.000	9.452	-0.080	-0.080	0.000	0.000	0.000	0.000
77	X	77	LEU	0	-0.015	0.006	12.689	-0.018	-0.018	0.000	0.000	0.000	0.000
78	X	78	LEU	0	-0.054	-0.042	10.338	-0.002	-0.002	0.000	0.000	0.000	0.000
79	X	79	GLU	-1	-0.855	-0.922	13.080	-0.275	-0.275	0.000	0.000	0.000	0.000
80	X	80	ASP	-1	-0.805	-0.886	14.799	-0.033	-0.033	0.000	0.000	0.000	0.000
81	X	81	TRP	0	-0.101	-0.059	16.335	0.015	0.015	0.000	0.000	0.000	0.000
82	X	82	GLY	0	0.026	0.018	17.945	0.012	0.012	0.000	0.000	0.000	0.000
83	X	83	LEU	0	-0.130	-0.071	15.160	0.011	0.011	0.000	0.000	0.000	0.000
84	X	84	ILE	0	-0.059	-0.035	9.900	0.043	0.043	0.000	0.000	0.000	0.000
85	X	85	GLU	-1	-0.789	-0.856	12.393	-0.214	-0.214	0.000	0.000	0.000	0.000
86	X	86	ILE	0	-0.002	0.002	8.904	-0.085	-0.085	0.000	0.000	0.000	0.000
87	X	87	VAL	0	-0.022	0.001	9.035	0.103	0.103	0.000	0.000	0.000	0.000
88	X	88	PRO	0	0.028	0.016	10.779	-0.174	-0.174	0.000	0.000	0.000	0.000
89	X	89	GLY	0	0.020	0.001	12.606	-0.025	-0.025	0.000	0.000	0.000	0.000
90	X	90	GLN	0	-0.052	-0.022	6.307	-1.197	-1.197	0.000	0.000	0.000	0.000
91	X	91	ARG	1	0.932	0.962	8.438	1.079	1.079	0.000	0.000	0.000	0.000
92	X	92	THR	0	0.001	0.002	6.954	-0.192	-0.192	0.000	0.000	0.000	0.000
93	X	93	PHE	0	-0.023	-0.006	8.538	-0.077	-0.077	0.000	0.000	0.000	0.000
94	X	94	MET	0	-0.005	-0.009	11.197	0.021	0.021	0.000	0.000	0.000	0.000
95	X	95	LYS	1	0.821	0.893	13.646	0.076	0.076	0.000	0.000	0.000	0.000
96	X	96	ASP	-1	-0.817	-0.888	14.396	-0.029	-0.029	0.000	0.000	0.000	0.000
97	X	97	LEU	0	-0.065	-0.048	14.034	0.036	0.036	0.000	0.000	0.000	0.000
98	X	98	THR	0	-0.038	-0.041	17.026	0.009	0.009	0.000	0.000	0.000	0.000
99	X	99	ASN	0	-0.062	-0.020	17.693	0.003	0.003	0.000	0.000	0.000	0.000
100	X	100	ASN	0	0.006	-0.009	18.861	0.011	0.011	0.000	0.000	0.000	0.000
101	X	101	PHE	0	0.046	0.031	14.774	0.017	0.017	0.000	0.000	0.000	0.000
102	X	102	ARG	1	0.868	0.942	18.507	-0.096	-0.096	0.000	0.000	0.000	0.000
103	X	103	VAL	0	0.083	0.044	18.030	0.018	0.018	0.000	0.000	0.000	0.000
104	X	104	ILE	0	-0.032	0.000	20.246	-0.014	-0.014	0.000	0.000	0.000	0.000
105	X	105	SER	0	0.032	0.005	22.071	0.006	0.006	0.000	0.000	0.000	0.000
106	X	106	PHE	0	0.098	0.028	22.555	0.004	0.004	0.000	0.000	0.000	0.000
107	X	107	LYS	1	0.947	0.958	24.836	-0.069	-0.069	0.000	0.000	0.000	0.000
108	X	108	GLN	0	0.021	0.029	26.447	-0.001	-0.001	0.000	0.000	0.000	0.000
109	X	109	LYS	1	0.892	0.934	22.191	-0.182	-0.182	0.000	0.000	0.000	0.000
110	X	110	HIS	1	0.861	0.941	25.301	-0.095	-0.095	0.000	0.000	0.000	0.000
111	X	111	GLU	-1	-0.828	-0.906	28.127	0.085	0.085	0.000	0.000	0.000	0.000
112	X	112	TRP	0	-0.028	-0.023	24.180	-0.009	-0.009	0.000	0.000	0.000	0.000
113	X	113	LYS	1	0.867	0.945	24.630	-0.101	-0.101	0.000	0.000	0.000	0.000
114	X	114	LEU	0	0.020	0.005	19.781	-0.005	-0.005	0.000	0.000	0.000	0.000
115	X	115	VAL	0	-0.009	-0.010	19.519	0.009	0.009	0.000	0.000	0.000	0.000
116	X	116	PRO	0	0.013	0.002	14.433	-0.011	-0.011	0.000	0.000	0.000	0.000
117	X	117	LYS	1	0.913	0.957	13.431	-0.155	-0.155	0.000	0.000	0.000	0.000
118	X	118	TYR	0	-0.109	-0.073	11.212	-0.050	-0.050	0.000	0.000	0.000	0.000
119	X	119	THR	0	0.038	0.017	13.715	0.019	0.019	0.000	0.000	0.000	0.000
120	X	120	ILE	0	-0.054	-0.016	17.245	-0.027	-0.027	0.000	0.000	0.000	0.000
121	X	121	GLY	0	0.035	0.033	19.100	0.001	0.001	0.000	0.000	0.000	0.000
122	X	122	ASN	0	-0.046	-0.025	19.957	-0.027	-0.027	0.000	0.000	0.000	0.000

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