FMO DATABASE

FMODB ID: VK271

Calculation Name: 2EF7-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2EF7

Chain ID: A

ChEMBL ID:

UniProt ID: Q96Y20

Base Structure: X-ray

Registration Date: 2023-09-26

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	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	127
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1030393.192323
FMO2-HF: Nuclear repulsion	980528.382651
FMO2-HF: Total energy	-49864.809672
FMO2-MP2: Total energy	-50008.284621

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.
-7.31	-1.848	1.15	-2.651	-3.959	-0.016

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 : -0.024 / q_NPA : -0.013

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	A	3	GLU	-1	-0.943	-0.979	3.741	-2.816	-0.611	-0.003	-1.149	-1.052	0.003
4	A	4	GLU	-1	-0.778	-0.850	5.968	-0.162	-0.162	0.000	0.000	0.000	0.000
5	A	5	ILE	0	-0.008	-0.018	7.929	-0.043	-0.043	0.000	0.000	0.000	0.000
6	A	6	VAL	0	-0.032	-0.038	11.525	0.138	0.138	0.000	0.000	0.000	0.000
7	A	7	LYS	1	0.840	0.907	14.924	0.401	0.401	0.000	0.000	0.000	0.000
8	A	8	GLU	-1	-0.913	-0.949	11.700	-0.229	-0.229	0.000	0.000	0.000	0.000
9	A	9	TYR	0	-0.085	-0.061	8.955	0.066	0.066	0.000	0.000	0.000	0.000
10	A	10	MET	0	-0.093	-0.032	15.088	0.029	0.029	0.000	0.000	0.000	0.000
11	A	11	LYS	1	0.972	0.995	18.540	0.159	0.159	0.000	0.000	0.000	0.000
12	A	12	THR	0	0.049	0.005	21.164	-0.006	-0.006	0.000	0.000	0.000	0.000
13	A	13	GLN	0	-0.030	-0.023	23.812	0.003	0.003	0.000	0.000	0.000	0.000
14	A	14	VAL	0	-0.018	0.004	25.686	0.010	0.010	0.000	0.000	0.000	0.000
15	A	15	ILE	0	0.010	0.001	28.419	0.004	0.004	0.000	0.000	0.000	0.000
16	A	16	SER	0	0.000	-0.005	31.992	-0.010	-0.010	0.000	0.000	0.000	0.000
17	A	17	VAL	0	-0.031	-0.012	33.733	0.009	0.009	0.000	0.000	0.000	0.000
18	A	18	THR	0	0.018	-0.009	36.837	-0.008	-0.008	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.895	0.923	38.868	0.128	0.128	0.000	0.000	0.000	0.000
20	A	20	ASP	-1	-0.866	-0.921	40.147	-0.092	-0.092	0.000	0.000	0.000	0.000
21	A	21	ALA	0	-0.017	0.008	41.246	0.006	0.006	0.000	0.000	0.000	0.000
22	A	22	LYS	1	0.986	0.988	43.248	0.065	0.065	0.000	0.000	0.000	0.000
23	A	23	LEU	0	0.009	0.009	43.844	0.000	0.000	0.000	0.000	0.000	0.000
24	A	24	ASN	0	-0.012	-0.023	44.169	-0.001	-0.001	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.872	-0.933	44.406	-0.062	-0.062	0.000	0.000	0.000	0.000
26	A	26	ILE	0	-0.015	-0.012	38.880	-0.001	-0.001	0.000	0.000	0.000	0.000
27	A	27	ALA	0	0.008	0.001	40.316	-0.001	-0.001	0.000	0.000	0.000	0.000
28	A	28	LYS	1	0.940	0.997	41.870	0.051	0.051	0.000	0.000	0.000	0.000
29	A	29	VAL	0	-0.007	0.001	37.177	0.003	0.003	0.000	0.000	0.000	0.000
30	A	30	MET	0	-0.012	-0.010	36.233	0.000	0.000	0.000	0.000	0.000	0.000
31	A	31	THR	0	-0.008	-0.009	37.861	0.003	0.003	0.000	0.000	0.000	0.000
32	A	32	GLU	-1	-0.942	-0.994	40.158	-0.048	-0.048	0.000	0.000	0.000	0.000
33	A	33	LYS	1	0.831	0.927	34.917	0.063	0.063	0.000	0.000	0.000	0.000
34	A	34	ASN	0	-0.020	0.008	34.491	0.001	0.001	0.000	0.000	0.000	0.000
35	A	35	ILE	0	-0.044	-0.017	31.926	-0.003	-0.003	0.000	0.000	0.000	0.000
36	A	36	GLY	0	0.085	0.033	32.599	0.003	0.003	0.000	0.000	0.000	0.000
37	A	37	SER	0	-0.066	-0.057	30.469	-0.002	-0.002	0.000	0.000	0.000	0.000
38	A	38	VAL	0	-0.003	0.018	32.473	0.002	0.002	0.000	0.000	0.000	0.000
39	A	39	ILE	0	0.000	-0.004	28.441	-0.005	-0.005	0.000	0.000	0.000	0.000
40	A	40	VAL	0	0.022	0.018	32.030	0.009	0.009	0.000	0.000	0.000	0.000
41	A	41	VAL	0	-0.027	-0.022	32.107	-0.012	-0.012	0.000	0.000	0.000	0.000
42	A	42	ASP	-1	-0.825	-0.906	34.832	-0.124	-0.124	0.000	0.000	0.000	0.000
43	A	43	GLY	0	0.043	0.017	35.584	-0.007	-0.007	0.000	0.000	0.000	0.000
44	A	44	ASN	0	-0.039	-0.034	31.841	-0.002	-0.002	0.000	0.000	0.000	0.000
45	A	45	LYS	1	0.916	0.983	30.909	0.183	0.183	0.000	0.000	0.000	0.000
46	A	46	PRO	0	0.007	0.008	27.973	0.013	0.013	0.000	0.000	0.000	0.000
47	A	47	VAL	0	-0.002	-0.002	31.227	-0.007	-0.007	0.000	0.000	0.000	0.000
48	A	48	GLY	0	0.052	0.012	32.879	0.004	0.004	0.000	0.000	0.000	0.000
49	A	49	ILE	0	-0.068	-0.013	29.465	-0.003	-0.003	0.000	0.000	0.000	0.000
50	A	50	ILE	0	0.019	0.036	33.262	0.004	0.004	0.000	0.000	0.000	0.000
51	A	51	THR	0	-0.023	-0.038	32.813	0.003	0.003	0.000	0.000	0.000	0.000
52	A	52	GLU	-1	-0.860	-0.942	35.475	-0.073	-0.073	0.000	0.000	0.000	0.000
53	A	53	ARG	1	0.940	0.963	37.086	0.095	0.095	0.000	0.000	0.000	0.000
54	A	54	ASP	-1	-0.804	-0.876	36.294	-0.115	-0.115	0.000	0.000	0.000	0.000
55	A	55	ILE	0	0.063	0.034	39.577	0.003	0.003	0.000	0.000	0.000	0.000
56	A	56	VAL	0	0.004	0.000	41.899	0.003	0.003	0.000	0.000	0.000	0.000
57	A	57	LYS	1	0.838	0.920	38.583	0.110	0.110	0.000	0.000	0.000	0.000
58	A	58	ALA	0	0.027	0.010	43.785	0.002	0.002	0.000	0.000	0.000	0.000
59	A	59	ILE	0	0.028	0.016	45.610	0.003	0.003	0.000	0.000	0.000	0.000
60	A	60	GLY	0	-0.014	0.003	47.225	0.003	0.003	0.000	0.000	0.000	0.000
61	A	61	LYS	1	0.840	0.916	46.785	0.076	0.076	0.000	0.000	0.000	0.000
62	A	62	GLY	0	0.006	0.003	49.679	0.000	0.000	0.000	0.000	0.000	0.000
63	A	63	LYS	1	0.804	0.919	47.543	0.077	0.077	0.000	0.000	0.000	0.000
64	A	64	SER	0	0.021	-0.015	50.325	0.001	0.001	0.000	0.000	0.000	0.000
65	A	65	LEU	0	0.051	0.022	49.133	-0.004	-0.004	0.000	0.000	0.000	0.000
66	A	66	GLU	-1	-0.871	-0.918	48.689	-0.059	-0.059	0.000	0.000	0.000	0.000
67	A	67	THR	0	-0.091	-0.045	45.965	-0.002	-0.002	0.000	0.000	0.000	0.000
68	A	68	LYS	1	0.906	0.939	44.687	0.090	0.090	0.000	0.000	0.000	0.000
69	A	69	ALA	0	0.040	0.014	39.584	-0.002	-0.002	0.000	0.000	0.000	0.000
70	A	70	GLU	-1	-0.863	-0.950	40.191	-0.110	-0.110	0.000	0.000	0.000	0.000
71	A	71	GLU	-1	-0.884	-0.933	41.244	-0.084	-0.084	0.000	0.000	0.000	0.000
72	A	72	PHE	0	-0.069	-0.041	40.975	0.002	0.002	0.000	0.000	0.000	0.000
73	A	73	MET	0	-0.048	0.010	36.814	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	74	THR	0	-0.044	-0.006	33.522	0.001	0.001	0.000	0.000	0.000	0.000
75	A	75	ALA	0	-0.009	-0.017	34.528	-0.007	-0.007	0.000	0.000	0.000	0.000
76	A	76	SER	0	-0.018	-0.030	29.295	-0.008	-0.008	0.000	0.000	0.000	0.000
77	A	77	LEU	0	0.046	0.024	30.808	0.003	0.003	0.000	0.000	0.000	0.000
78	A	78	ILE	0	-0.048	-0.003	24.825	-0.014	-0.014	0.000	0.000	0.000	0.000
79	A	79	THR	0	-0.020	-0.013	24.617	0.004	0.004	0.000	0.000	0.000	0.000
80	A	80	ILE	0	0.012	0.008	18.200	-0.018	-0.018	0.000	0.000	0.000	0.000
81	A	81	ARG	1	0.976	0.995	19.794	0.429	0.429	0.000	0.000	0.000	0.000
82	A	82	GLU	-1	-0.764	-0.889	18.201	-0.372	-0.372	0.000	0.000	0.000	0.000
83	A	83	ASP	-1	-0.924	-0.956	15.713	-0.527	-0.527	0.000	0.000	0.000	0.000
84	A	84	SER	0	-0.083	-0.053	14.623	-0.087	-0.087	0.000	0.000	0.000	0.000
85	A	85	PRO	0	0.096	0.060	10.494	0.076	0.076	0.000	0.000	0.000	0.000
86	A	86	ILE	0	0.013	0.002	9.685	0.168	0.168	0.000	0.000	0.000	0.000
87	A	87	THR	0	-0.007	-0.012	9.543	0.251	0.251	0.000	0.000	0.000	0.000
88	A	88	GLY	0	0.039	0.025	12.349	0.118	0.118	0.000	0.000	0.000	0.000
89	A	89	ALA	0	0.009	0.000	15.103	0.101	0.101	0.000	0.000	0.000	0.000
90	A	90	LEU	0	-0.002	0.000	13.504	0.084	0.084	0.000	0.000	0.000	0.000
91	A	91	ALA	0	-0.028	-0.023	16.225	0.074	0.074	0.000	0.000	0.000	0.000
92	A	92	LEU	0	0.014	0.013	18.071	0.060	0.060	0.000	0.000	0.000	0.000
93	A	93	MET	0	-0.016	-0.003	18.883	0.044	0.044	0.000	0.000	0.000	0.000
94	A	94	ARG	1	0.916	0.955	16.910	0.515	0.515	0.000	0.000	0.000	0.000
95	A	95	GLN	0	-0.033	0.005	21.671	0.010	0.010	0.000	0.000	0.000	0.000
96	A	96	PHE	0	-0.007	-0.012	24.001	0.028	0.028	0.000	0.000	0.000	0.000
97	A	97	ASN	0	-0.054	-0.016	24.950	0.016	0.016	0.000	0.000	0.000	0.000
98	A	98	ILE	0	-0.013	0.000	23.995	0.026	0.026	0.000	0.000	0.000	0.000
99	A	99	ARG	1	0.935	0.950	22.360	0.162	0.162	0.000	0.000	0.000	0.000
100	A	100	HIS	0	0.024	0.007	21.927	-0.017	-0.017	0.000	0.000	0.000	0.000
101	A	101	LEU	0	0.007	0.014	19.896	0.004	0.004	0.000	0.000	0.000	0.000
102	A	102	PRO	0	0.019	0.007	22.657	-0.003	-0.003	0.000	0.000	0.000	0.000
103	A	103	VAL	0	-0.001	0.005	19.807	-0.023	-0.023	0.000	0.000	0.000	0.000
104	A	104	VAL	0	0.006	-0.004	22.792	0.035	0.035	0.000	0.000	0.000	0.000
105	A	105	ASP	-1	-0.700	-0.858	22.405	-0.277	-0.277	0.000	0.000	0.000	0.000
106	A	106	ASP	-1	-0.793	-0.899	23.041	-0.292	-0.292	0.000	0.000	0.000	0.000
107	A	107	LYS	1	0.769	0.871	24.395	0.267	0.267	0.000	0.000	0.000	0.000
108	A	108	GLY	0	0.002	-0.012	26.640	0.019	0.019	0.000	0.000	0.000	0.000
109	A	109	ASN	0	-0.101	-0.058	27.818	0.022	0.022	0.000	0.000	0.000	0.000
110	A	110	LEU	0	0.010	0.001	26.511	-0.020	-0.020	0.000	0.000	0.000	0.000
111	A	111	LYS	1	0.842	0.932	23.081	0.233	0.233	0.000	0.000	0.000	0.000
112	A	112	GLY	0	0.039	0.011	22.942	0.016	0.016	0.000	0.000	0.000	0.000
113	A	113	ILE	0	-0.065	-0.010	22.829	-0.007	-0.007	0.000	0.000	0.000	0.000
114	A	114	ILE	0	0.025	0.043	15.523	0.011	0.011	0.000	0.000	0.000	0.000
115	A	115	SER	0	-0.025	-0.054	19.036	0.008	0.008	0.000	0.000	0.000	0.000
116	A	116	ILE	0	0.033	-0.010	16.773	-0.024	-0.024	0.000	0.000	0.000	0.000
117	A	117	ARG	1	0.902	0.947	16.533	0.178	0.178	0.000	0.000	0.000	0.000
118	A	118	ASP	-1	-0.752	-0.828	15.741	-0.240	-0.240	0.000	0.000	0.000	0.000
119	A	119	ILE	0	-0.013	-0.006	12.389	-0.028	-0.028	0.000	0.000	0.000	0.000
120	A	120	THR	0	-0.001	-0.013	11.521	-0.080	-0.080	0.000	0.000	0.000	0.000
121	A	121	ARG	1	0.854	0.942	11.318	0.181	0.181	0.000	0.000	0.000	0.000
122	A	122	ALA	0	0.079	0.043	9.406	0.043	0.043	0.000	0.000	0.000	0.000
123	A	123	ILE	0	-0.098	-0.044	7.110	-0.159	-0.159	0.000	0.000	0.000	0.000
124	A	124	ASP	-1	-0.919	-0.980	6.454	-0.489	-0.489	0.000	0.000	0.000	0.000
125	A	125	ASP	-1	-0.893	-0.951	7.672	0.106	0.106	0.000	0.000	0.000	0.000
126	A	126	MET	0	-0.072	-0.018	3.191	-0.333	0.368	0.067	-0.130	-0.637	0.000
127	A	127	PHE	0	-0.122	-0.056	2.525	-5.309	-2.753	1.086	-1.372	-2.270	-0.019

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