FMO DATABASE

FMODB ID: YVY32

Calculation Name: 2E7S-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2E7S

Chain ID: A

ChEMBL ID:

UniProt ID: P17065

Base Structure: X-ray

Registration Date: 2023-09-21

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	114
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-585780.446466
FMO2-HF: Nuclear repulsion	538904.865846
FMO2-HF: Total energy	-46875.58062
FMO2-MP2: Total energy	-47012.817764

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:31:LEU)

Summations of interaction energy for fragment #1(A:31:LEU)

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.
-0.937	2.458	0.311	-1.12	-2.587	0.001

Interaction energy analysis for fragmet #1(A:31:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.031 / 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	33	GLU	-1	-0.814	-0.887	3.850	-0.848	0.748	-0.004	-0.629	-0.964	0.000
4	A	34	GLN	0	0.009	0.001	2.669	-1.038	0.041	0.313	-0.314	-1.079	0.001
5	A	35	LEU	0	-0.013	0.001	3.703	-0.008	0.572	0.003	-0.171	-0.412	0.000
6	A	36	ASN	0	0.007	-0.001	5.054	0.392	0.532	-0.001	-0.006	-0.132	0.000
7	A	37	LYS	1	0.855	0.908	8.054	-0.175	-0.175	0.000	0.000	0.000	0.000
8	A	38	SER	0	0.000	0.028	7.524	0.158	0.158	0.000	0.000	0.000	0.000
9	A	39	LEU	0	0.041	0.027	8.903	0.118	0.118	0.000	0.000	0.000	0.000
10	A	40	LYS	1	0.965	0.973	10.844	0.228	0.228	0.000	0.000	0.000	0.000
11	A	41	THR	0	-0.026	-0.026	12.267	0.078	0.078	0.000	0.000	0.000	0.000
12	A	42	ILE	0	0.013	0.003	12.655	0.041	0.041	0.000	0.000	0.000	0.000
13	A	43	ALA	0	-0.009	-0.002	14.821	0.032	0.032	0.000	0.000	0.000	0.000
14	A	44	SER	0	0.009	-0.002	16.847	0.035	0.035	0.000	0.000	0.000	0.000
15	A	45	GLN	0	-0.045	-0.019	17.047	0.005	0.005	0.000	0.000	0.000	0.000
16	A	46	LYS	1	0.829	0.892	18.896	0.201	0.201	0.000	0.000	0.000	0.000
17	A	47	ALA	0	0.037	0.017	20.755	0.015	0.015	0.000	0.000	0.000	0.000
18	A	48	ALA	0	-0.008	0.008	22.521	0.015	0.015	0.000	0.000	0.000	0.000
19	A	49	ILE	0	-0.006	-0.006	22.048	0.010	0.010	0.000	0.000	0.000	0.000
20	A	50	GLU	-1	-0.833	-0.895	24.727	-0.149	-0.149	0.000	0.000	0.000	0.000
21	A	51	ASN	0	-0.023	-0.021	26.399	0.013	0.013	0.000	0.000	0.000	0.000
22	A	52	TYR	0	0.013	0.020	28.540	0.009	0.009	0.000	0.000	0.000	0.000
23	A	53	ASN	0	0.003	-0.016	27.899	0.011	0.011	0.000	0.000	0.000	0.000
24	A	54	GLN	0	0.014	0.010	30.822	0.000	0.000	0.000	0.000	0.000	0.000
25	A	55	LEU	0	0.035	0.027	32.723	0.006	0.006	0.000	0.000	0.000	0.000
26	A	56	LYS	1	0.879	0.926	34.008	0.062	0.062	0.000	0.000	0.000	0.000
27	A	57	GLU	-1	-0.929	-0.960	34.388	-0.080	-0.080	0.000	0.000	0.000	0.000
28	A	58	ASP	-1	-0.816	-0.903	36.772	-0.059	-0.059	0.000	0.000	0.000	0.000
29	A	59	TYR	0	-0.048	-0.018	38.399	0.004	0.004	0.000	0.000	0.000	0.000
30	A	60	ASN	0	-0.039	-0.041	38.431	0.006	0.006	0.000	0.000	0.000	0.000
31	A	61	THR	0	0.022	0.021	40.614	0.002	0.002	0.000	0.000	0.000	0.000
32	A	62	LEU	0	0.031	0.010	42.409	0.002	0.002	0.000	0.000	0.000	0.000
33	A	63	LYS	1	0.851	0.933	42.419	0.048	0.048	0.000	0.000	0.000	0.000
34	A	64	ARG	1	0.889	0.959	42.548	0.053	0.053	0.000	0.000	0.000	0.000
35	A	65	GLU	-1	-0.756	-0.868	47.225	-0.037	-0.037	0.000	0.000	0.000	0.000
36	A	66	LEU	0	-0.043	-0.021	48.755	0.002	0.002	0.000	0.000	0.000	0.000
37	A	67	SER	0	-0.031	-0.025	49.677	0.002	0.002	0.000	0.000	0.000	0.000
38	A	68	ASP	-1	-0.902	-0.961	50.198	-0.038	-0.038	0.000	0.000	0.000	0.000
39	A	69	ARG	1	0.745	0.841	51.459	0.035	0.035	0.000	0.000	0.000	0.000
40	A	70	ASP	-1	-0.849	-0.917	54.645	-0.025	-0.025	0.000	0.000	0.000	0.000
41	A	71	ASP	-1	-0.816	-0.891	56.180	-0.028	-0.028	0.000	0.000	0.000	0.000
42	A	72	GLU	-1	-0.908	-0.933	56.554	-0.028	-0.028	0.000	0.000	0.000	0.000
43	A	73	VAL	0	-0.022	-0.019	58.976	0.001	0.001	0.000	0.000	0.000	0.000
44	A	74	LYS	1	0.756	0.868	57.369	0.028	0.028	0.000	0.000	0.000	0.000
45	A	75	ARG	1	0.925	0.954	57.030	0.031	0.031	0.000	0.000	0.000	0.000
46	A	76	LEU	0	0.044	0.029	62.317	0.001	0.001	0.000	0.000	0.000	0.000
47	A	77	ARG	1	0.907	0.948	64.227	0.020	0.020	0.000	0.000	0.000	0.000
48	A	78	GLU	-1	-0.950	-0.968	64.705	-0.022	-0.022	0.000	0.000	0.000	0.000
49	A	79	ASP	-1	-0.916	-0.952	67.461	-0.021	-0.021	0.000	0.000	0.000	0.000
50	A	80	ILE	0	-0.045	-0.029	68.860	0.001	0.001	0.000	0.000	0.000	0.000
51	A	81	ALA	0	-0.017	0.007	71.084	0.001	0.001	0.000	0.000	0.000	0.000
52	A	82	LYS	1	1.000	0.996	72.681	0.020	0.020	0.000	0.000	0.000	0.000
53	A	83	GLU	-1	-0.910	-0.955	73.922	-0.017	-0.017	0.000	0.000	0.000	0.000
54	A	84	ASN	0	-0.065	-0.048	74.519	0.001	0.001	0.000	0.000	0.000	0.000
55	A	85	GLU	-1	-0.967	-0.957	77.118	-0.016	-0.016	0.000	0.000	0.000	0.000
56	A	86	LEU	0	-0.038	-0.028	77.218	0.000	0.000	0.000	0.000	0.000	0.000
57	A	87	ARG	1	0.857	0.901	79.633	0.014	0.014	0.000	0.000	0.000	0.000
58	A	88	THR	0	-0.011	-0.007	81.057	0.001	0.001	0.000	0.000	0.000	0.000
59	A	89	LYS	1	0.964	0.986	83.435	0.014	0.014	0.000	0.000	0.000	0.000
60	A	90	ALA	0	-0.084	-0.040	84.146	0.000	0.000	0.000	0.000	0.000	0.000
61	A	91	GLU	-1	-0.906	-0.931	84.875	-0.012	-0.012	0.000	0.000	0.000	0.000
62	A	92	GLU	-1	-0.899	-0.964	86.901	-0.012	-0.012	0.000	0.000	0.000	0.000
63	A	93	GLU	-1	-0.893	-0.958	89.103	-0.012	-0.012	0.000	0.000	0.000	0.000
64	A	94	ALA	0	-0.010	0.011	90.020	0.000	0.000	0.000	0.000	0.000	0.000
65	A	95	ASP	-1	-0.829	-0.910	91.878	-0.009	-0.009	0.000	0.000	0.000	0.000
66	A	96	LYS	1	0.861	0.928	92.937	0.012	0.012	0.000	0.000	0.000	0.000
67	A	97	LEU	0	-0.012	0.002	94.789	0.000	0.000	0.000	0.000	0.000	0.000
68	A	98	ASN	0	-0.012	-0.016	94.392	0.000	0.000	0.000	0.000	0.000	0.000
69	A	99	LYS	1	0.882	0.926	96.906	0.010	0.010	0.000	0.000	0.000	0.000
70	A	100	GLU	-1	-0.918	-0.945	99.443	-0.010	-0.010	0.000	0.000	0.000	0.000
71	A	101	VAL	0	-0.063	-0.030	100.168	0.000	0.000	0.000	0.000	0.000	0.000
72	A	102	GLU	-1	-0.965	-0.967	101.636	-0.008	-0.008	0.000	0.000	0.000	0.000
73	A	103	ASP	-1	-0.877	-0.940	103.906	-0.008	-0.008	0.000	0.000	0.000	0.000
74	A	104	LEU	0	-0.040	-0.011	105.149	0.000	0.000	0.000	0.000	0.000	0.000
75	A	105	THR	0	-0.062	-0.051	105.403	0.000	0.000	0.000	0.000	0.000	0.000
76	A	106	ALA	0	-0.012	-0.008	108.048	0.000	0.000	0.000	0.000	0.000	0.000
77	A	107	SER	0	-0.010	-0.010	110.009	0.000	0.000	0.000	0.000	0.000	0.000
78	A	108	LEU	0	-0.023	-0.003	110.709	0.000	0.000	0.000	0.000	0.000	0.000
79	A	109	PHE	0	-0.015	-0.011	112.092	0.000	0.000	0.000	0.000	0.000	0.000
80	A	110	ASP	-1	-0.843	-0.914	113.939	-0.007	-0.007	0.000	0.000	0.000	0.000
81	A	111	GLU	-1	-0.897	-0.941	115.284	-0.007	-0.007	0.000	0.000	0.000	0.000
82	A	112	ALA	0	-0.051	-0.021	116.887	0.000	0.000	0.000	0.000	0.000	0.000
83	A	113	ASN	0	-0.076	-0.057	116.627	0.000	0.000	0.000	0.000	0.000	0.000
84	A	114	ASN	0	-0.019	-0.017	118.949	0.000	0.000	0.000	0.000	0.000	0.000
85	A	115	LEU	0	0.004	0.018	121.579	0.000	0.000	0.000	0.000	0.000	0.000
86	A	116	VAL	0	-0.051	-0.035	122.015	0.000	0.000	0.000	0.000	0.000	0.000
87	A	117	ALA	0	-0.023	-0.006	124.162	0.000	0.000	0.000	0.000	0.000	0.000
88	A	118	ASP	-1	-0.867	-0.948	125.979	-0.006	-0.006	0.000	0.000	0.000	0.000
89	A	119	ALA	0	0.037	0.023	127.278	0.000	0.000	0.000	0.000	0.000	0.000
90	A	120	ARG	1	0.877	0.935	127.516	0.006	0.006	0.000	0.000	0.000	0.000
91	A	121	MET	0	0.003	0.007	130.494	0.000	0.000	0.000	0.000	0.000	0.000
92	A	122	GLU	-1	-0.918	-0.957	131.023	-0.006	-0.006	0.000	0.000	0.000	0.000
93	A	123	LYS	1	0.743	0.878	132.809	0.005	0.005	0.000	0.000	0.000	0.000
94	A	124	TYR	0	0.007	-0.024	133.208	0.000	0.000	0.000	0.000	0.000	0.000
95	A	125	ALA	0	0.005	0.016	136.551	0.000	0.000	0.000	0.000	0.000	0.000
96	A	126	ILE	0	0.028	-0.001	136.912	0.000	0.000	0.000	0.000	0.000	0.000
97	A	127	GLU	-1	-0.839	-0.896	138.543	-0.005	-0.005	0.000	0.000	0.000	0.000
98	A	128	ILE	0	0.016	0.004	140.392	0.000	0.000	0.000	0.000	0.000	0.000
99	A	129	LEU	0	-0.032	-0.013	141.222	0.000	0.000	0.000	0.000	0.000	0.000
100	A	130	ASN	0	0.066	0.017	141.063	0.000	0.000	0.000	0.000	0.000	0.000
101	A	131	LYS	1	0.803	0.915	144.521	0.004	0.004	0.000	0.000	0.000	0.000
102	A	132	ARG	1	0.962	0.982	146.229	0.005	0.005	0.000	0.000	0.000	0.000
103	A	133	LEU	0	-0.009	0.000	146.039	0.000	0.000	0.000	0.000	0.000	0.000
104	A	134	THR	0	-0.024	-0.023	147.072	0.000	0.000	0.000	0.000	0.000	0.000
105	A	135	GLU	-1	-0.867	-0.930	149.656	-0.004	-0.004	0.000	0.000	0.000	0.000
106	A	136	GLN	0	-0.042	-0.043	152.118	0.000	0.000	0.000	0.000	0.000	0.000
107	A	137	LEU	0	-0.044	-0.013	150.923	0.000	0.000	0.000	0.000	0.000	0.000
108	A	138	ARG	1	0.984	0.995	152.565	0.004	0.004	0.000	0.000	0.000	0.000
109	A	139	GLU	-1	-0.897	-0.925	156.223	-0.004	-0.004	0.000	0.000	0.000	0.000
110	A	140	LYS	1	0.928	0.959	157.111	0.004	0.004	0.000	0.000	0.000	0.000
111	A	141	ASP	-1	-0.886	-0.943	157.383	-0.004	-0.004	0.000	0.000	0.000	0.000
112	A	142	MET	0	-0.076	-0.025	159.743	0.000	0.000	0.000	0.000	0.000	0.000
113	A	143	LEU	0	-0.049	-0.011	162.170	0.000	0.000	0.000	0.000	0.000	0.000
114	A	144	LEU	0	-0.092	-0.055	162.135	0.000	0.000	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:31:LEU)