FMO DATABASE

FMODB ID: N9YNQ

Calculation Name: 2I7R-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2I7R

Chain ID: A

ChEMBL ID:

UniProt ID: A0A0H2

Base Structure: X-ray

Registration Date: 2023-09-20

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	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	115
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-893880.399733
FMO2-HF: Nuclear repulsion	848325.881612
FMO2-HF: Total energy	-45554.518121
FMO2-MP2: Total energy	-45686.083448

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:1:MET)

Summations of interaction energy for fragment #1(A: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.
-1.431	0.818	-0.02	-1.162	-1.066	0.003

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.001 / q_NPA : -0.005

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	3	LEU	0	-0.024	0.006	3.864	-0.334	1.915	-0.020	-1.162	-1.066	0.003
4	A	4	ASN	0	0.020	0.000	6.216	-0.395	-0.395	0.000	0.000	0.000	0.000
5	A	5	GLN	0	-0.033	-0.032	8.865	0.058	0.058	0.000	0.000	0.000	0.000
6	A	6	LEU	0	0.001	0.009	10.851	0.070	0.070	0.000	0.000	0.000	0.000
7	A	7	ASP	-1	-0.826	-0.897	13.625	0.028	0.028	0.000	0.000	0.000	0.000
8	A	8	ILE	0	-0.034	-0.013	16.727	0.038	0.038	0.000	0.000	0.000	0.000
9	A	9	ILE	0	0.006	0.009	19.285	-0.010	-0.010	0.000	0.000	0.000	0.000
10	A	10	VAL	0	0.023	0.004	22.234	-0.004	-0.004	0.000	0.000	0.000	0.000
11	A	11	SER	0	0.008	-0.006	25.800	-0.001	-0.001	0.000	0.000	0.000	0.000
12	A	12	ASN	0	0.013	0.006	29.097	-0.003	-0.003	0.000	0.000	0.000	0.000
13	A	13	VAL	0	0.035	0.034	25.235	-0.007	-0.007	0.000	0.000	0.000	0.000
14	A	14	PRO	0	0.026	0.013	27.765	-0.013	-0.013	0.000	0.000	0.000	0.000
15	A	15	GLN	0	-0.048	-0.023	30.601	-0.005	-0.005	0.000	0.000	0.000	0.000
16	A	16	VAL	0	0.023	0.002	25.413	-0.008	-0.008	0.000	0.000	0.000	0.000
17	A	17	CYS	0	-0.016	-0.009	26.386	-0.018	-0.018	0.000	0.000	0.000	0.000
18	A	18	ALA	0	0.012	0.009	27.391	-0.015	-0.015	0.000	0.000	0.000	0.000
19	A	19	ASP	-1	-0.859	-0.934	29.567	-0.058	-0.058	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.026	-0.017	22.272	-0.009	-0.009	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.827	-0.904	26.769	-0.119	-0.119	0.000	0.000	0.000	0.000
22	A	22	HIS	0	-0.001	0.010	28.412	-0.016	-0.016	0.000	0.000	0.000	0.000
23	A	23	ILE	0	-0.003	-0.001	26.398	-0.008	-0.008	0.000	0.000	0.000	0.000
24	A	24	LEU	0	-0.026	-0.024	22.362	-0.017	-0.017	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.857	-0.906	26.099	-0.176	-0.176	0.000	0.000	0.000	0.000
26	A	26	LYS	1	0.771	0.888	21.633	0.254	0.254	0.000	0.000	0.000	0.000
27	A	27	LYS	1	0.859	0.909	27.245	0.105	0.105	0.000	0.000	0.000	0.000
28	A	28	ALA	0	0.010	0.003	24.507	-0.020	-0.020	0.000	0.000	0.000	0.000
29	A	29	ASP	-1	-0.807	-0.863	20.028	-0.263	-0.263	0.000	0.000	0.000	0.000
30	A	30	TYR	0	-0.041	-0.037	22.729	0.012	0.012	0.000	0.000	0.000	0.000
31	A	31	ALA	0	0.004	-0.007	24.356	-0.002	-0.002	0.000	0.000	0.000	0.000
32	A	32	ASN	0	-0.028	-0.003	25.629	0.006	0.006	0.000	0.000	0.000	0.000
33	A	33	ASP	-1	-0.882	-0.946	28.490	0.005	0.005	0.000	0.000	0.000	0.000
34	A	34	GLY	0	0.021	-0.004	27.692	0.004	0.004	0.000	0.000	0.000	0.000
35	A	35	PHE	0	-0.029	-0.022	18.896	0.017	0.017	0.000	0.000	0.000	0.000
36	A	36	ALA	0	0.020	0.014	22.979	-0.008	-0.008	0.000	0.000	0.000	0.000
37	A	37	GLN	0	-0.018	-0.016	18.245	0.033	0.033	0.000	0.000	0.000	0.000
38	A	38	PHE	0	0.020	0.006	19.578	0.002	0.002	0.000	0.000	0.000	0.000
39	A	39	THR	0	0.003	-0.024	16.496	-0.039	-0.039	0.000	0.000	0.000	0.000
40	A	40	ILE	0	-0.023	-0.014	17.150	0.044	0.044	0.000	0.000	0.000	0.000
41	A	41	GLY	0	0.028	0.014	16.829	-0.060	-0.060	0.000	0.000	0.000	0.000
42	A	42	SER	0	-0.019	-0.010	12.649	0.055	0.055	0.000	0.000	0.000	0.000
43	A	43	HIS	0	-0.030	-0.009	10.491	-0.255	-0.255	0.000	0.000	0.000	0.000
44	A	44	CYS	0	-0.027	-0.008	12.925	0.078	0.078	0.000	0.000	0.000	0.000
45	A	45	LEU	0	-0.010	-0.005	14.398	0.001	0.001	0.000	0.000	0.000	0.000
46	A	46	MET	0	0.012	0.016	15.618	-0.011	-0.011	0.000	0.000	0.000	0.000
47	A	47	LEU	0	-0.016	0.006	18.786	0.018	0.018	0.000	0.000	0.000	0.000
48	A	48	SER	0	-0.013	-0.021	20.948	-0.002	-0.002	0.000	0.000	0.000	0.000
49	A	49	GLN	0	-0.010	0.005	22.806	0.013	0.013	0.000	0.000	0.000	0.000
50	A	50	ASN	0	0.014	0.009	22.828	0.019	0.019	0.000	0.000	0.000	0.000
51	A	51	HIS	1	0.835	0.921	22.423	-0.150	-0.150	0.000	0.000	0.000	0.000
52	A	52	LEU	0	0.022	0.018	16.189	0.007	0.007	0.000	0.000	0.000	0.000
53	A	53	VAL	0	0.025	0.015	17.130	0.038	0.038	0.000	0.000	0.000	0.000
54	A	54	PRO	0	-0.011	-0.024	20.356	-0.035	-0.035	0.000	0.000	0.000	0.000
55	A	55	LEU	0	-0.013	0.009	18.581	0.028	0.028	0.000	0.000	0.000	0.000
56	A	56	GLU	-1	-0.884	-0.939	22.590	0.125	0.125	0.000	0.000	0.000	0.000
57	A	57	ASN	0	-0.031	-0.037	23.308	0.015	0.015	0.000	0.000	0.000	0.000
58	A	58	PHE	0	-0.013	-0.004	20.188	0.008	0.008	0.000	0.000	0.000	0.000
59	A	59	GLN	0	-0.040	-0.016	23.509	-0.020	-0.020	0.000	0.000	0.000	0.000
60	A	60	SER	0	0.017	-0.010	24.325	-0.020	-0.020	0.000	0.000	0.000	0.000
61	A	61	GLY	0	-0.018	0.001	22.088	0.021	0.021	0.000	0.000	0.000	0.000
62	A	62	ILE	0	-0.034	-0.013	17.399	0.005	0.005	0.000	0.000	0.000	0.000
63	A	63	ILE	0	-0.006	-0.007	18.899	-0.003	-0.003	0.000	0.000	0.000	0.000
64	A	64	ILE	0	-0.008	-0.007	17.440	-0.033	-0.033	0.000	0.000	0.000	0.000
65	A	65	HIS	1	0.828	0.896	17.372	0.288	0.288	0.000	0.000	0.000	0.000
66	A	66	ILE	0	-0.002	0.002	17.702	-0.049	-0.049	0.000	0.000	0.000	0.000
67	A	67	GLU	-1	-0.784	-0.870	19.148	-0.475	-0.475	0.000	0.000	0.000	0.000
68	A	68	VAL	0	-0.047	-0.035	20.931	-0.004	-0.004	0.000	0.000	0.000	0.000
69	A	69	GLU	-1	-0.917	-0.961	24.288	-0.348	-0.348	0.000	0.000	0.000	0.000
70	A	70	ASP	-1	-0.884	-0.936	27.066	-0.179	-0.179	0.000	0.000	0.000	0.000
71	A	71	VAL	0	0.009	0.021	26.828	0.000	0.000	0.000	0.000	0.000	0.000
72	A	72	ASP	-1	-0.804	-0.877	29.381	-0.158	-0.158	0.000	0.000	0.000	0.000
73	A	73	GLN	0	-0.013	-0.019	32.611	0.022	0.022	0.000	0.000	0.000	0.000
74	A	74	ASN	0	0.018	0.003	28.079	0.017	0.017	0.000	0.000	0.000	0.000
75	A	75	TYR	0	0.012	0.011	31.174	0.013	0.013	0.000	0.000	0.000	0.000
76	A	76	LYS	1	0.765	0.881	33.085	0.130	0.130	0.000	0.000	0.000	0.000
77	A	77	ARG	1	0.810	0.887	28.757	0.175	0.175	0.000	0.000	0.000	0.000
78	A	78	LEU	0	-0.022	-0.013	28.990	0.009	0.009	0.000	0.000	0.000	0.000
79	A	79	ASN	0	-0.019	-0.023	33.590	0.011	0.011	0.000	0.000	0.000	0.000
80	A	80	GLU	-1	-0.863	-0.919	36.959	-0.103	-0.103	0.000	0.000	0.000	0.000
81	A	81	LEU	0	-0.042	-0.010	33.248	0.006	0.006	0.000	0.000	0.000	0.000
82	A	82	GLY	0	-0.029	-0.006	36.795	0.005	0.005	0.000	0.000	0.000	0.000
83	A	83	ILE	0	-0.009	-0.001	30.703	0.006	0.006	0.000	0.000	0.000	0.000
84	A	84	LYS	1	0.882	0.934	33.097	0.067	0.067	0.000	0.000	0.000	0.000
85	A	85	VAL	0	0.056	0.026	31.588	-0.003	-0.003	0.000	0.000	0.000	0.000
86	A	86	LEU	0	-0.090	-0.042	27.987	0.011	0.011	0.000	0.000	0.000	0.000
87	A	87	HIS	0	-0.040	-0.026	29.831	0.017	0.017	0.000	0.000	0.000	0.000
88	A	88	GLY	0	0.044	0.022	30.760	-0.009	-0.009	0.000	0.000	0.000	0.000
89	A	89	PRO	0	0.018	0.009	31.282	-0.005	-0.005	0.000	0.000	0.000	0.000
90	A	90	THR	0	-0.055	-0.004	30.815	0.011	0.011	0.000	0.000	0.000	0.000
91	A	91	VAL	0	0.009	-0.003	29.535	-0.015	-0.015	0.000	0.000	0.000	0.000
92	A	92	THR	0	-0.009	0.001	25.944	0.012	0.012	0.000	0.000	0.000	0.000
93	A	93	ASP	-1	-0.872	-0.939	29.189	-0.174	-0.174	0.000	0.000	0.000	0.000
94	A	94	TRP	0	-0.073	-0.042	25.502	-0.011	-0.011	0.000	0.000	0.000	0.000
95	A	95	GLY	0	0.009	-0.007	27.051	-0.023	-0.023	0.000	0.000	0.000	0.000
96	A	96	THR	0	-0.030	-0.016	23.020	-0.008	-0.008	0.000	0.000	0.000	0.000
97	A	97	GLH	0	-0.062	-0.060	25.988	0.017	0.017	0.000	0.000	0.000	0.000
98	A	98	SER	0	-0.004	-0.005	25.228	-0.022	-0.022	0.000	0.000	0.000	0.000
99	A	99	LEU	0	0.015	0.012	26.308	0.019	0.019	0.000	0.000	0.000	0.000
100	A	100	LEU	0	0.002	0.020	24.253	-0.006	-0.006	0.000	0.000	0.000	0.000
101	A	101	VAL	0	0.001	-0.008	26.644	0.014	0.014	0.000	0.000	0.000	0.000
102	A	102	GLN	0	-0.019	-0.019	26.873	-0.001	-0.001	0.000	0.000	0.000	0.000
103	A	103	GLY	0	0.026	0.019	26.035	-0.008	-0.008	0.000	0.000	0.000	0.000
104	A	104	PRO	0	0.015	0.010	26.270	0.014	0.014	0.000	0.000	0.000	0.000
105	A	105	ALA	0	-0.016	-0.028	26.139	0.001	0.001	0.000	0.000	0.000	0.000
106	A	106	GLY	0	0.053	0.037	26.361	0.011	0.011	0.000	0.000	0.000	0.000
107	A	107	LEU	0	-0.032	-0.015	21.083	0.001	0.001	0.000	0.000	0.000	0.000
108	A	108	VAL	0	-0.002	0.007	22.919	-0.001	-0.001	0.000	0.000	0.000	0.000
109	A	109	LEU	0	0.006	0.008	21.893	-0.010	-0.010	0.000	0.000	0.000	0.000
110	A	110	ASP	-1	-0.817	-0.913	21.783	-0.228	-0.228	0.000	0.000	0.000	0.000
111	A	111	PHE	0	0.005	0.019	22.252	-0.034	-0.034	0.000	0.000	0.000	0.000
112	A	112	TYR	0	-0.058	-0.061	18.086	0.020	0.020	0.000	0.000	0.000	0.000
113	A	113	ARG	1	0.915	0.948	23.255	0.253	0.253	0.000	0.000	0.000	0.000
114	A	114	MET	0	-0.023	-0.004	18.058	0.037	0.037	0.000	0.000	0.000	0.000
115	A	115	LYS	1	0.937	0.999	23.678	0.286	0.286	0.000	0.000	0.000	0.000

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