FMO DATABASE

FMODB ID: 85Y9Y

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	OptHSide
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	-893222.157676
FMO2-HF: Nuclear repulsion	847667.91612
FMO2-HF: Total energy	-45554.241556
FMO2-MP2: Total energy	-45685.762082

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.
-1.562	0.799	-0.019	-1.23	-1.112	0.002

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 : -0.006

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	-0.022	0.001	3.879	-0.475	1.886	-0.019	-1.230	-1.112	0.002
4	A	4	ASN	0	0.026	0.020	6.155	-0.346	-0.346	0.000	0.000	0.000	0.000
5	A	5	GLN	0	-0.018	-0.035	8.907	0.055	0.055	0.000	0.000	0.000	0.000
6	A	6	LEU	0	-0.012	0.013	10.999	0.088	0.088	0.000	0.000	0.000	0.000
7	A	7	ASP	-1	-0.835	-0.899	13.488	0.030	0.030	0.000	0.000	0.000	0.000
8	A	8	ILE	0	-0.022	-0.011	16.480	0.032	0.032	0.000	0.000	0.000	0.000
9	A	9	ILE	0	0.002	0.006	19.277	-0.007	-0.007	0.000	0.000	0.000	0.000
10	A	10	VAL	0	0.020	0.002	22.038	-0.004	-0.004	0.000	0.000	0.000	0.000
11	A	11	SER	0	-0.005	-0.013	25.595	0.003	0.003	0.000	0.000	0.000	0.000
12	A	12	ASN	0	0.004	-0.002	29.068	-0.002	-0.002	0.000	0.000	0.000	0.000
13	A	13	VAL	0	0.049	0.029	25.468	-0.009	-0.009	0.000	0.000	0.000	0.000
14	A	14	PRO	0	0.035	0.027	27.965	-0.014	-0.014	0.000	0.000	0.000	0.000
15	A	15	GLN	0	-0.033	-0.012	30.740	-0.005	-0.005	0.000	0.000	0.000	0.000
16	A	16	VAL	0	0.015	0.004	25.434	-0.008	-0.008	0.000	0.000	0.000	0.000
17	A	17	CYS	0	-0.014	-0.009	26.498	-0.018	-0.018	0.000	0.000	0.000	0.000
18	A	18	ALA	0	0.004	0.001	27.514	-0.015	-0.015	0.000	0.000	0.000	0.000
19	A	19	ASP	-1	-0.865	-0.939	29.453	-0.066	-0.066	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.030	-0.024	22.196	-0.010	-0.010	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.814	-0.900	26.768	-0.125	-0.125	0.000	0.000	0.000	0.000
22	A	22	HIS	0	-0.001	0.018	28.338	-0.015	-0.015	0.000	0.000	0.000	0.000
23	A	23	ILE	0	-0.018	-0.012	26.451	-0.009	-0.009	0.000	0.000	0.000	0.000
24	A	24	LEU	0	-0.039	-0.027	22.493	-0.016	-0.016	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.936	-0.959	26.320	-0.177	-0.177	0.000	0.000	0.000	0.000
26	A	26	LYS	1	0.778	0.891	21.803	0.254	0.254	0.000	0.000	0.000	0.000
27	A	27	LYS	1	0.850	0.915	27.168	0.112	0.112	0.000	0.000	0.000	0.000
28	A	28	ALA	0	0.008	-0.004	24.359	-0.020	-0.020	0.000	0.000	0.000	0.000
29	A	29	ASP	-1	-0.816	-0.884	20.458	-0.256	-0.256	0.000	0.000	0.000	0.000
30	A	30	TYR	0	-0.023	-0.018	23.216	0.016	0.016	0.000	0.000	0.000	0.000
31	A	31	ALA	0	0.012	-0.003	24.397	-0.003	-0.003	0.000	0.000	0.000	0.000
32	A	32	ASN	0	-0.039	-0.006	25.998	-0.001	-0.001	0.000	0.000	0.000	0.000
33	A	33	ASP	-1	-0.865	-0.941	28.534	0.000	0.000	0.000	0.000	0.000	0.000
34	A	34	GLY	0	0.007	-0.004	27.580	0.003	0.003	0.000	0.000	0.000	0.000
35	A	35	PHE	0	-0.031	-0.028	18.989	0.015	0.015	0.000	0.000	0.000	0.000
36	A	36	ALA	0	0.028	0.020	22.970	-0.005	-0.005	0.000	0.000	0.000	0.000
37	A	37	GLN	0	-0.026	-0.010	18.389	0.027	0.027	0.000	0.000	0.000	0.000
38	A	38	PHE	0	0.011	0.002	19.783	-0.002	-0.002	0.000	0.000	0.000	0.000
39	A	39	THR	0	0.002	-0.020	17.071	-0.037	-0.037	0.000	0.000	0.000	0.000
40	A	40	ILE	0	-0.014	-0.019	17.391	0.041	0.041	0.000	0.000	0.000	0.000
41	A	41	GLY	0	0.027	0.020	17.029	-0.057	-0.057	0.000	0.000	0.000	0.000
42	A	42	SER	0	-0.010	-0.010	12.562	0.063	0.063	0.000	0.000	0.000	0.000
43	A	43	HIS	0	-0.021	-0.012	10.837	-0.227	-0.227	0.000	0.000	0.000	0.000
44	A	44	CYS	0	-0.031	-0.007	13.129	0.076	0.076	0.000	0.000	0.000	0.000
45	A	45	LEU	0	-0.009	-0.006	14.494	-0.005	-0.005	0.000	0.000	0.000	0.000
46	A	46	MET	0	0.015	0.012	15.976	-0.005	-0.005	0.000	0.000	0.000	0.000
47	A	47	LEU	0	-0.026	0.005	18.782	0.017	0.017	0.000	0.000	0.000	0.000
48	A	48	SER	0	-0.005	-0.011	20.850	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	49	GLN	0	0.038	0.021	22.612	0.005	0.005	0.000	0.000	0.000	0.000
50	A	50	ASN	0	-0.015	-0.015	22.870	0.014	0.014	0.000	0.000	0.000	0.000
51	A	51	HIS	1	0.828	0.923	22.297	-0.144	-0.144	0.000	0.000	0.000	0.000
52	A	52	LEU	0	0.045	0.036	16.374	0.004	0.004	0.000	0.000	0.000	0.000
53	A	53	VAL	0	0.026	0.008	17.319	0.030	0.030	0.000	0.000	0.000	0.000
54	A	54	PRO	0	-0.013	-0.025	20.454	-0.035	-0.035	0.000	0.000	0.000	0.000
55	A	55	LEU	0	-0.007	0.010	18.598	0.026	0.026	0.000	0.000	0.000	0.000
56	A	56	GLU	-1	-0.907	-0.954	22.584	0.121	0.121	0.000	0.000	0.000	0.000
57	A	57	ASN	0	-0.033	-0.037	23.151	0.013	0.013	0.000	0.000	0.000	0.000
58	A	58	PHE	0	-0.023	-0.006	20.016	0.008	0.008	0.000	0.000	0.000	0.000
59	A	59	GLN	0	-0.016	0.004	23.435	-0.021	-0.021	0.000	0.000	0.000	0.000
60	A	60	SER	0	0.025	-0.013	24.323	-0.021	-0.021	0.000	0.000	0.000	0.000
61	A	61	GLY	0	-0.023	-0.001	22.086	0.018	0.018	0.000	0.000	0.000	0.000
62	A	62	ILE	0	-0.014	-0.002	17.447	0.006	0.006	0.000	0.000	0.000	0.000
63	A	63	ILE	0	-0.017	-0.012	18.697	-0.004	-0.004	0.000	0.000	0.000	0.000
64	A	64	ILE	0	-0.002	0.011	17.054	-0.028	-0.028	0.000	0.000	0.000	0.000
65	A	65	HIS	1	0.814	0.881	17.116	0.319	0.319	0.000	0.000	0.000	0.000
66	A	66	ILE	0	0.012	0.000	17.400	-0.059	-0.059	0.000	0.000	0.000	0.000
67	A	67	GLU	-1	-0.812	-0.892	18.759	-0.508	-0.508	0.000	0.000	0.000	0.000
68	A	68	VAL	0	-0.055	-0.035	20.549	0.000	0.000	0.000	0.000	0.000	0.000
69	A	69	GLU	-1	-0.920	-0.965	23.970	-0.353	-0.353	0.000	0.000	0.000	0.000
70	A	70	ASP	-1	-0.867	-0.933	26.688	-0.187	-0.187	0.000	0.000	0.000	0.000
71	A	71	VAL	0	0.002	0.006	26.726	0.006	0.006	0.000	0.000	0.000	0.000
72	A	72	ASP	-1	-0.818	-0.880	29.198	-0.165	-0.165	0.000	0.000	0.000	0.000
73	A	73	GLN	0	0.003	-0.006	32.184	0.023	0.023	0.000	0.000	0.000	0.000
74	A	74	ASN	0	-0.015	-0.008	28.001	0.013	0.013	0.000	0.000	0.000	0.000
75	A	75	TYR	0	0.009	0.010	30.846	0.014	0.014	0.000	0.000	0.000	0.000
76	A	76	LYS	1	0.891	0.953	32.861	0.139	0.139	0.000	0.000	0.000	0.000
77	A	77	ARG	1	0.890	0.953	28.373	0.184	0.184	0.000	0.000	0.000	0.000
78	A	78	LEU	0	-0.020	-0.021	28.944	0.010	0.010	0.000	0.000	0.000	0.000
79	A	79	ASN	0	-0.021	-0.027	33.512	0.010	0.010	0.000	0.000	0.000	0.000
80	A	80	GLU	-1	-0.982	-0.992	36.779	-0.102	-0.102	0.000	0.000	0.000	0.000
81	A	81	LEU	0	-0.036	-0.012	33.271	0.006	0.006	0.000	0.000	0.000	0.000
82	A	82	GLY	0	-0.022	0.009	36.897	0.006	0.006	0.000	0.000	0.000	0.000
83	A	83	ILE	0	-0.030	-0.012	30.612	0.006	0.006	0.000	0.000	0.000	0.000
84	A	84	LYS	1	0.885	0.939	32.925	0.074	0.074	0.000	0.000	0.000	0.000
85	A	85	VAL	0	0.055	0.031	31.578	-0.006	-0.006	0.000	0.000	0.000	0.000
86	A	86	LEU	0	-0.082	-0.047	27.930	0.011	0.011	0.000	0.000	0.000	0.000
87	A	87	HIS	0	-0.006	0.005	29.537	0.015	0.015	0.000	0.000	0.000	0.000
88	A	88	GLY	0	0.031	0.025	30.623	-0.010	-0.010	0.000	0.000	0.000	0.000
89	A	89	PRO	0	0.018	-0.001	30.881	-0.005	-0.005	0.000	0.000	0.000	0.000
90	A	90	THR	0	-0.058	-0.012	30.368	0.011	0.011	0.000	0.000	0.000	0.000
91	A	91	VAL	0	0.009	0.004	29.284	-0.016	-0.016	0.000	0.000	0.000	0.000
92	A	92	THR	0	0.001	0.010	25.596	0.013	0.013	0.000	0.000	0.000	0.000
93	A	93	ASP	-1	-0.897	-0.952	28.799	-0.182	-0.182	0.000	0.000	0.000	0.000
94	A	94	TRP	0	-0.051	-0.028	25.613	-0.009	-0.009	0.000	0.000	0.000	0.000
95	A	95	GLY	0	-0.008	-0.019	26.765	-0.022	-0.022	0.000	0.000	0.000	0.000
96	A	96	THR	0	-0.072	-0.034	22.812	-0.022	-0.022	0.000	0.000	0.000	0.000
97	A	97	GLH	0	-0.047	-0.061	25.761	0.016	0.016	0.000	0.000	0.000	0.000
98	A	98	SER	0	0.003	-0.003	24.933	-0.020	-0.020	0.000	0.000	0.000	0.000
99	A	99	LEU	0	0.025	0.031	26.319	0.021	0.021	0.000	0.000	0.000	0.000
100	A	100	LEU	0	-0.011	0.006	23.999	-0.011	-0.011	0.000	0.000	0.000	0.000
101	A	101	VAL	0	0.007	-0.004	26.528	0.016	0.016	0.000	0.000	0.000	0.000
102	A	102	GLN	0	-0.039	-0.025	26.833	0.001	0.001	0.000	0.000	0.000	0.000
103	A	103	GLY	0	0.012	0.001	26.039	-0.005	-0.005	0.000	0.000	0.000	0.000
104	A	104	PRO	0	0.010	0.009	26.230	0.014	0.014	0.000	0.000	0.000	0.000
105	A	105	ALA	0	-0.011	-0.026	25.995	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	106	GLY	0	0.049	0.029	25.933	0.011	0.011	0.000	0.000	0.000	0.000
107	A	107	LEU	0	-0.053	-0.018	20.907	-0.004	-0.004	0.000	0.000	0.000	0.000
108	A	108	VAL	0	0.022	0.024	22.860	-0.001	-0.001	0.000	0.000	0.000	0.000
109	A	109	LEU	0	0.007	-0.002	21.869	-0.013	-0.013	0.000	0.000	0.000	0.000
110	A	110	ASP	-1	-0.825	-0.905	21.440	-0.253	-0.253	0.000	0.000	0.000	0.000
111	A	111	PHE	0	0.006	0.019	21.948	-0.032	-0.032	0.000	0.000	0.000	0.000
112	A	112	TYR	0	-0.058	-0.061	17.862	0.024	0.024	0.000	0.000	0.000	0.000
113	A	113	ARG	1	0.940	0.980	23.197	0.251	0.251	0.000	0.000	0.000	0.000
114	A	114	MET	0	0.005	0.007	18.205	0.028	0.028	0.000	0.000	0.000	0.000
115	A	115	LYS	1	0.951	0.990	23.868	0.298	0.298	0.000	0.000	0.000	0.000

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