FMO DATABASE

FMODB ID: G6351

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

Total energy (hartree)

FMO2-HF: Electronic energy	-892721.316757
FMO2-HF: Nuclear repulsion	847167.673009
FMO2-HF: Total energy	-45553.643748
FMO2-MP2: Total energy	-45685.176608

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.
-0.439	1.304	-0.018	-0.815	-0.91	-0.001

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 : -0.035 / q_NPA : -0.038

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	-0.025	-0.003	3.887	-0.162	1.581	-0.018	-0.815	-0.910	-0.001
4	A	4	ASN	0	0.063	0.030	6.223	-0.081	-0.081	0.000	0.000	0.000	0.000
5	A	5	GLN	0	-0.037	-0.037	8.840	0.097	0.097	0.000	0.000	0.000	0.000
6	A	6	LEU	0	-0.017	0.009	11.074	0.011	0.011	0.000	0.000	0.000	0.000
7	A	7	ASP	-1	-0.825	-0.904	13.533	0.161	0.161	0.000	0.000	0.000	0.000
8	A	8	ILE	0	-0.028	-0.013	16.532	-0.001	-0.001	0.000	0.000	0.000	0.000
9	A	9	ILE	0	-0.001	0.001	19.334	0.006	0.006	0.000	0.000	0.000	0.000
10	A	10	VAL	0	0.014	0.000	22.053	-0.013	-0.013	0.000	0.000	0.000	0.000
11	A	11	SER	0	-0.017	-0.021	25.609	0.006	0.006	0.000	0.000	0.000	0.000
12	A	12	ASN	0	0.025	0.009	29.096	0.005	0.005	0.000	0.000	0.000	0.000
13	A	13	VAL	0	0.044	0.026	25.645	-0.008	-0.008	0.000	0.000	0.000	0.000
14	A	14	PRO	0	0.039	0.031	28.039	-0.008	-0.008	0.000	0.000	0.000	0.000
15	A	15	GLN	0	-0.027	-0.003	30.713	-0.001	-0.001	0.000	0.000	0.000	0.000
16	A	16	VAL	0	0.007	0.000	25.458	-0.007	-0.007	0.000	0.000	0.000	0.000
17	A	17	CYS	0	0.003	-0.001	26.580	-0.009	-0.009	0.000	0.000	0.000	0.000
18	A	18	ALA	0	0.004	0.003	27.587	-0.008	-0.008	0.000	0.000	0.000	0.000
19	A	19	ASP	-1	-0.876	-0.948	29.504	-0.022	-0.022	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.032	-0.028	22.427	-0.010	-0.010	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.865	-0.926	26.816	-0.015	-0.015	0.000	0.000	0.000	0.000
22	A	22	HIS	0	-0.013	0.012	28.400	-0.009	-0.009	0.000	0.000	0.000	0.000
23	A	23	ILE	0	-0.017	-0.012	26.209	-0.008	-0.008	0.000	0.000	0.000	0.000
24	A	24	LEU	0	-0.045	-0.036	22.539	-0.014	-0.014	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.962	-0.966	26.363	-0.068	-0.068	0.000	0.000	0.000	0.000
26	A	26	LYS	1	0.877	0.945	21.907	0.076	0.076	0.000	0.000	0.000	0.000
27	A	27	LYS	1	0.919	0.953	27.106	0.011	0.011	0.000	0.000	0.000	0.000
28	A	28	ALA	0	0.019	-0.002	24.308	-0.006	-0.006	0.000	0.000	0.000	0.000
29	A	29	ASP	-1	-0.869	-0.878	20.662	0.006	0.006	0.000	0.000	0.000	0.000
30	A	30	TYR	0	-0.036	-0.026	23.409	0.012	0.012	0.000	0.000	0.000	0.000
31	A	31	ALA	0	0.007	-0.003	24.354	-0.002	-0.002	0.000	0.000	0.000	0.000
32	A	32	ASN	0	-0.026	0.002	26.374	-0.003	-0.003	0.000	0.000	0.000	0.000
33	A	33	ASP	-1	-0.879	-0.953	28.460	0.050	0.050	0.000	0.000	0.000	0.000
34	A	34	GLY	0	-0.006	-0.013	27.447	-0.003	-0.003	0.000	0.000	0.000	0.000
35	A	35	PHE	0	-0.024	-0.027	18.968	0.009	0.009	0.000	0.000	0.000	0.000
36	A	36	ALA	0	0.033	0.022	22.846	-0.006	-0.006	0.000	0.000	0.000	0.000
37	A	37	GLN	0	-0.022	-0.014	18.462	0.024	0.024	0.000	0.000	0.000	0.000
38	A	38	PHE	0	0.013	0.004	19.705	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	39	THR	0	0.020	-0.036	17.052	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	40	ILE	0	-0.046	-0.040	17.363	0.006	0.006	0.000	0.000	0.000	0.000
41	A	41	GLY	0	0.010	0.011	17.019	-0.043	-0.043	0.000	0.000	0.000	0.000
42	A	42	SER	0	-0.007	-0.006	12.430	0.047	0.047	0.000	0.000	0.000	0.000
43	A	43	HIS	0	-0.020	-0.011	11.244	-0.124	-0.124	0.000	0.000	0.000	0.000
44	A	44	CYS	0	-0.022	-0.001	13.070	0.050	0.050	0.000	0.000	0.000	0.000
45	A	45	LEU	0	-0.008	-0.006	14.467	-0.027	-0.027	0.000	0.000	0.000	0.000
46	A	46	MET	0	0.007	0.005	16.087	0.001	0.001	0.000	0.000	0.000	0.000
47	A	47	LEU	0	-0.027	0.004	18.716	-0.008	-0.008	0.000	0.000	0.000	0.000
48	A	48	SER	0	-0.014	-0.015	20.821	0.013	0.013	0.000	0.000	0.000	0.000
49	A	49	GLN	0	0.031	0.020	22.619	-0.006	-0.006	0.000	0.000	0.000	0.000
50	A	50	ASN	0	-0.025	-0.015	22.143	-0.005	-0.005	0.000	0.000	0.000	0.000
51	A	51	HIS	1	0.830	0.924	22.332	-0.120	-0.120	0.000	0.000	0.000	0.000
52	A	52	LEU	0	0.052	0.035	16.310	0.001	0.001	0.000	0.000	0.000	0.000
53	A	53	VAL	0	0.022	0.009	17.292	0.020	0.020	0.000	0.000	0.000	0.000
54	A	54	PRO	0	-0.018	-0.027	20.342	-0.025	-0.025	0.000	0.000	0.000	0.000
55	A	55	LEU	0	-0.013	0.008	18.565	0.013	0.013	0.000	0.000	0.000	0.000
56	A	56	GLU	-1	-0.939	-0.969	22.541	0.069	0.069	0.000	0.000	0.000	0.000
57	A	57	ASN	0	-0.007	-0.023	23.105	0.013	0.013	0.000	0.000	0.000	0.000
58	A	58	PHE	0	-0.025	-0.006	20.121	-0.001	-0.001	0.000	0.000	0.000	0.000
59	A	59	GLN	0	-0.002	0.005	23.370	-0.010	-0.010	0.000	0.000	0.000	0.000
60	A	60	SER	0	0.021	-0.013	24.189	-0.014	-0.014	0.000	0.000	0.000	0.000
61	A	61	GLY	0	-0.024	-0.002	21.911	0.009	0.009	0.000	0.000	0.000	0.000
62	A	62	ILE	0	-0.005	0.002	17.396	-0.009	-0.009	0.000	0.000	0.000	0.000
63	A	63	ILE	0	-0.018	-0.012	18.531	0.007	0.007	0.000	0.000	0.000	0.000
64	A	64	ILE	0	0.006	0.016	17.184	-0.038	-0.038	0.000	0.000	0.000	0.000
65	A	65	HIS	1	0.810	0.877	17.057	0.313	0.313	0.000	0.000	0.000	0.000
66	A	66	ILE	0	0.013	-0.001	17.344	-0.037	-0.037	0.000	0.000	0.000	0.000
67	A	67	GLU	-1	-0.907	-0.952	18.563	-0.378	-0.378	0.000	0.000	0.000	0.000
68	A	68	VAL	0	-0.057	-0.030	20.518	0.019	0.019	0.000	0.000	0.000	0.000
69	A	69	GLU	-1	-0.922	-0.971	23.964	-0.188	-0.188	0.000	0.000	0.000	0.000
70	A	70	ASP	-1	-0.873	-0.944	26.678	-0.117	-0.117	0.000	0.000	0.000	0.000
71	A	71	VAL	0	-0.003	0.007	26.603	0.006	0.006	0.000	0.000	0.000	0.000
72	A	72	ASP	-1	-0.817	-0.888	29.148	-0.116	-0.116	0.000	0.000	0.000	0.000
73	A	73	GLN	0	-0.002	-0.008	32.241	0.014	0.014	0.000	0.000	0.000	0.000
74	A	74	ASN	0	-0.004	-0.002	27.714	0.013	0.013	0.000	0.000	0.000	0.000
75	A	75	TYR	0	0.012	0.001	30.831	0.008	0.008	0.000	0.000	0.000	0.000
76	A	76	LYS	1	0.898	0.960	32.814	0.073	0.073	0.000	0.000	0.000	0.000
77	A	77	ARG	1	0.921	0.967	28.415	0.091	0.091	0.000	0.000	0.000	0.000
78	A	78	LEU	0	-0.017	-0.022	29.163	0.007	0.007	0.000	0.000	0.000	0.000
79	A	79	ASN	0	-0.016	-0.018	33.491	0.004	0.004	0.000	0.000	0.000	0.000
80	A	80	GLU	-1	-0.995	-0.996	36.738	-0.050	-0.050	0.000	0.000	0.000	0.000
81	A	81	LEU	0	-0.031	-0.008	33.162	0.005	0.005	0.000	0.000	0.000	0.000
82	A	82	GLY	0	-0.028	0.005	36.895	0.004	0.004	0.000	0.000	0.000	0.000
83	A	83	ILE	0	-0.016	-0.006	30.621	0.003	0.003	0.000	0.000	0.000	0.000
84	A	84	LYS	1	0.923	0.968	32.606	0.058	0.058	0.000	0.000	0.000	0.000
85	A	85	VAL	0	0.036	0.019	31.495	-0.006	-0.006	0.000	0.000	0.000	0.000
86	A	86	LEU	0	-0.099	-0.063	27.844	0.006	0.006	0.000	0.000	0.000	0.000
87	A	87	HIS	0	-0.006	0.004	29.470	0.008	0.008	0.000	0.000	0.000	0.000
88	A	88	GLY	0	0.025	0.023	30.497	-0.005	-0.005	0.000	0.000	0.000	0.000
89	A	89	PRO	0	0.016	-0.001	30.769	-0.007	-0.007	0.000	0.000	0.000	0.000
90	A	90	THR	0	-0.060	-0.014	30.237	0.004	0.004	0.000	0.000	0.000	0.000
91	A	91	VAL	0	0.012	0.005	29.206	-0.011	-0.011	0.000	0.000	0.000	0.000
92	A	92	THR	0	0.002	0.008	25.448	0.008	0.008	0.000	0.000	0.000	0.000
93	A	93	ASP	-1	-0.896	-0.955	28.589	-0.172	-0.172	0.000	0.000	0.000	0.000
94	A	94	TRP	0	-0.053	-0.023	25.379	-0.005	-0.005	0.000	0.000	0.000	0.000
95	A	95	GLY	0	-0.005	-0.017	26.629	-0.014	-0.014	0.000	0.000	0.000	0.000
96	A	96	THR	0	-0.064	-0.026	22.780	-0.016	-0.016	0.000	0.000	0.000	0.000
97	A	97	GLH	0	-0.051	-0.059	25.732	0.008	0.008	0.000	0.000	0.000	0.000
98	A	98	SER	0	-0.049	-0.026	24.911	-0.013	-0.013	0.000	0.000	0.000	0.000
99	A	99	LEU	0	0.046	0.040	26.201	0.017	0.017	0.000	0.000	0.000	0.000
100	A	100	LEU	0	0.011	0.020	23.919	-0.008	-0.008	0.000	0.000	0.000	0.000
101	A	101	VAL	0	-0.006	-0.011	26.434	0.013	0.013	0.000	0.000	0.000	0.000
102	A	102	GLN	0	-0.044	-0.024	26.745	-0.007	-0.007	0.000	0.000	0.000	0.000
103	A	103	GLY	0	0.010	-0.004	25.994	0.001	0.001	0.000	0.000	0.000	0.000
104	A	104	PRO	0	0.007	0.008	26.202	0.005	0.005	0.000	0.000	0.000	0.000
105	A	105	ALA	0	-0.009	-0.023	25.816	-0.002	-0.002	0.000	0.000	0.000	0.000
106	A	106	GLY	0	0.050	0.028	25.871	0.005	0.005	0.000	0.000	0.000	0.000
107	A	107	LEU	0	-0.050	-0.019	20.863	-0.010	-0.010	0.000	0.000	0.000	0.000
108	A	108	VAL	0	0.023	0.027	22.763	0.003	0.003	0.000	0.000	0.000	0.000
109	A	109	LEU	0	-0.011	-0.005	21.941	-0.013	-0.013	0.000	0.000	0.000	0.000
110	A	110	ASP	-1	-0.790	-0.888	21.344	-0.222	-0.222	0.000	0.000	0.000	0.000
111	A	111	PHE	0	0.006	0.017	21.875	-0.019	-0.019	0.000	0.000	0.000	0.000
112	A	112	TYR	0	0.001	-0.014	17.605	0.007	0.007	0.000	0.000	0.000	0.000
113	A	113	ARG	1	0.961	0.992	23.136	0.185	0.185	0.000	0.000	0.000	0.000
114	A	114	MET	0	0.000	0.004	18.258	-0.002	-0.002	0.000	0.000	0.000	0.000
115	A	115	LYS	1	0.949	0.983	23.848	0.267	0.267	0.000	0.000	0.000	0.000

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