FMO DATABASE

FMODB ID: 2J68R

Calculation Name: 2B7L-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2B7L

Chain ID: A

ChEMBL ID:

UniProt ID: Q2G2X2

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:

Apendix: None

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
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1082579.247742
FMO2-HF: Nuclear repulsion	1033162.642382
FMO2-HF: Total energy	-49416.60536
FMO2-MP2: Total energy	-49559.525375

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.
-13.217	-12.465	19.291	-6.93	-13.114	-0.037

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 : -0.095 / q_NPA : -0.054

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	ARG	1	0.855	0.945	1.650	6.215	0.786	15.861	-3.329	-7.104	-0.002
4	A	4	VAL	0	0.029	0.021	4.566	0.626	0.758	0.000	-0.022	-0.110	0.000
5	A	5	ILE	0	0.007	0.014	7.897	0.231	0.231	0.000	0.000	0.000	0.000
6	A	6	THR	0	-0.045	-0.029	10.833	0.090	0.090	0.000	0.000	0.000	0.000
7	A	7	TYR	0	0.011	-0.039	14.498	-0.001	-0.001	0.000	0.000	0.000	0.000
8	A	8	GLY	0	0.022	0.011	17.545	0.029	0.029	0.000	0.000	0.000	0.000
9	A	9	THR	0	-0.048	-0.025	20.603	-0.005	-0.005	0.000	0.000	0.000	0.000
10	A	10	TYR	0	0.025	-0.001	17.902	0.031	0.031	0.000	0.000	0.000	0.000
11	A	11	ASP	-1	-0.704	-0.848	22.415	-0.057	-0.057	0.000	0.000	0.000	0.000
12	A	12	LEU	0	-0.042	-0.008	25.402	0.011	0.011	0.000	0.000	0.000	0.000
13	A	13	LEU	0	-0.030	-0.004	20.629	0.000	0.000	0.000	0.000	0.000	0.000
14	A	14	HIS	0	0.087	0.089	24.799	0.019	0.019	0.000	0.000	0.000	0.000
15	A	15	TYR	0	0.007	-0.012	21.290	-0.004	-0.004	0.000	0.000	0.000	0.000
16	A	16	GLY	0	0.018	-0.015	23.055	0.002	0.002	0.000	0.000	0.000	0.000
17	A	17	HIS	0	0.023	-0.019	21.083	-0.019	-0.019	0.000	0.000	0.000	0.000
18	A	18	ILE	0	0.014	0.015	18.986	-0.011	-0.011	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.825	-0.890	18.190	0.047	0.047	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.022	-0.004	16.827	0.000	0.000	0.000	0.000	0.000	0.000
21	A	21	LEU	0	0.036	0.013	14.934	-0.029	-0.029	0.000	0.000	0.000	0.000
22	A	22	ARG	1	0.802	0.888	13.491	-0.106	-0.106	0.000	0.000	0.000	0.000
23	A	23	ARG	1	0.860	0.919	13.399	0.085	0.085	0.000	0.000	0.000	0.000
24	A	24	ALA	0	0.024	0.010	12.352	-0.032	-0.032	0.000	0.000	0.000	0.000
25	A	25	ARG	1	0.833	0.927	6.036	-1.141	-1.141	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.961	-0.989	8.668	0.114	0.114	0.000	0.000	0.000	0.000
27	A	27	MET	0	-0.084	-0.028	9.991	0.067	0.067	0.000	0.000	0.000	0.000
28	A	28	GLY	0	-0.001	-0.010	5.850	-0.354	-0.354	0.000	0.000	0.000	0.000
29	A	29	ASP	-1	-0.883	-0.941	2.328	-2.676	0.391	1.516	-1.982	-2.601	-0.017
30	A	30	TYR	0	-0.024	-0.035	2.659	-1.460	1.498	1.914	-1.534	-3.338	-0.018
31	A	31	LEU	0	-0.055	-0.030	4.769	-1.283	-1.248	0.001	-0.034	-0.002	0.000
32	A	32	ILE	0	-0.029	-0.009	7.107	0.241	0.241	0.000	0.000	0.000	0.000
33	A	33	VAL	0	0.009	-0.011	9.687	-0.039	-0.039	0.000	0.000	0.000	0.000
34	A	34	ALA	0	-0.005	-0.005	13.394	0.030	0.030	0.000	0.000	0.000	0.000
35	A	35	LEU	0	-0.026	0.002	15.741	0.024	0.024	0.000	0.000	0.000	0.000
36	A	36	SER	0	-0.033	-0.026	18.503	0.003	0.003	0.000	0.000	0.000	0.000
37	A	37	THR	0	0.043	0.024	21.748	0.023	0.023	0.000	0.000	0.000	0.000
38	A	38	ASP	-1	-0.717	-0.868	23.639	-0.100	-0.100	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.901	-0.950	27.143	-0.128	-0.128	0.000	0.000	0.000	0.000
40	A	40	PHE	0	0.032	0.000	23.352	0.007	0.007	0.000	0.000	0.000	0.000
41	A	41	ASN	0	0.011	-0.016	26.436	-0.008	-0.008	0.000	0.000	0.000	0.000
42	A	42	GLN	0	0.027	0.024	27.494	0.008	0.008	0.000	0.000	0.000	0.000
43	A	43	ILE	0	-0.004	0.020	28.765	0.005	0.005	0.000	0.000	0.000	0.000
44	A	44	LYS	1	0.827	0.946	24.614	0.178	0.178	0.000	0.000	0.000	0.000
45	A	45	HIS	0	-0.134	-0.078	29.648	0.012	0.012	0.000	0.000	0.000	0.000
46	A	46	LYS	1	0.867	0.938	29.408	0.127	0.127	0.000	0.000	0.000	0.000
47	A	47	LYS	1	0.972	0.981	31.660	0.066	0.066	0.000	0.000	0.000	0.000
48	A	48	SER	0	-0.071	-0.031	27.684	0.002	0.002	0.000	0.000	0.000	0.000
49	A	49	TYR	0	-0.054	-0.029	29.636	0.003	0.003	0.000	0.000	0.000	0.000
50	A	50	TYR	0	-0.040	-0.026	26.362	0.010	0.010	0.000	0.000	0.000	0.000
51	A	51	ASP	-1	-0.808	-0.897	26.022	-0.066	-0.066	0.000	0.000	0.000	0.000
52	A	52	TYR	0	0.000	-0.042	18.087	0.005	0.005	0.000	0.000	0.000	0.000
53	A	53	GLU	-1	-0.902	-0.953	21.904	-0.073	-0.073	0.000	0.000	0.000	0.000
54	A	54	GLN	0	-0.023	-0.012	21.789	0.009	0.009	0.000	0.000	0.000	0.000
55	A	55	ARG	1	0.702	0.854	21.960	0.128	0.128	0.000	0.000	0.000	0.000
56	A	56	LYS	1	0.892	0.944	15.573	0.064	0.064	0.000	0.000	0.000	0.000
57	A	57	MET	0	0.001	0.000	17.649	0.018	0.018	0.000	0.000	0.000	0.000
58	A	58	MET	0	-0.019	0.002	18.829	0.032	0.032	0.000	0.000	0.000	0.000
59	A	59	LEU	0	0.008	0.022	15.764	0.026	0.026	0.000	0.000	0.000	0.000
60	A	60	GLU	-1	-0.847	-0.935	13.976	0.034	0.034	0.000	0.000	0.000	0.000
61	A	61	SER	0	-0.119	-0.063	14.498	0.055	0.055	0.000	0.000	0.000	0.000
62	A	62	ILE	0	-0.049	-0.032	15.417	0.030	0.030	0.000	0.000	0.000	0.000
63	A	63	ARG	1	0.948	0.957	13.711	-0.324	-0.324	0.000	0.000	0.000	0.000
64	A	64	TYR	0	-0.033	-0.036	11.842	0.111	0.111	0.000	0.000	0.000	0.000
65	A	65	VAL	0	0.021	0.018	10.686	-0.032	-0.032	0.000	0.000	0.000	0.000
66	A	66	ASP	-1	-0.819	-0.881	6.005	1.362	1.362	0.000	0.000	0.000	0.000
67	A	67	LEU	0	-0.035	-0.019	7.649	-0.037	-0.037	0.000	0.000	0.000	0.000
68	A	68	VAL	0	-0.001	0.018	9.568	-0.089	-0.089	0.000	0.000	0.000	0.000
69	A	69	ILE	0	-0.003	0.003	11.753	0.022	0.022	0.000	0.000	0.000	0.000
70	A	70	PRO	0	-0.072	-0.029	14.502	0.011	0.011	0.000	0.000	0.000	0.000
71	A	71	GLU	-1	-0.761	-0.887	18.213	-0.346	-0.346	0.000	0.000	0.000	0.000
72	A	72	LYS	1	0.910	0.920	19.806	0.272	0.272	0.000	0.000	0.000	0.000
73	A	73	GLY	0	-0.005	-0.004	22.399	0.028	0.028	0.000	0.000	0.000	0.000
74	A	74	TRP	0	0.029	0.002	22.458	-0.027	-0.027	0.000	0.000	0.000	0.000
75	A	75	GLY	0	-0.021	0.004	22.796	-0.020	-0.020	0.000	0.000	0.000	0.000
76	A	76	GLN	0	-0.016	-0.026	17.303	0.059	0.059	0.000	0.000	0.000	0.000
77	A	77	LYS	1	0.914	0.992	16.896	0.376	0.376	0.000	0.000	0.000	0.000
78	A	78	GLU	-1	-0.889	-0.948	16.009	-0.535	-0.535	0.000	0.000	0.000	0.000
79	A	79	ASP	-1	-0.929	-0.969	16.200	-0.627	-0.627	0.000	0.000	0.000	0.000
80	A	80	ASP	-1	-0.816	-0.859	13.623	-0.649	-0.649	0.000	0.000	0.000	0.000
81	A	81	VAL	0	-0.015	-0.028	11.716	-0.131	-0.131	0.000	0.000	0.000	0.000
82	A	82	GLU	-1	-0.918	-0.936	11.049	-1.406	-1.406	0.000	0.000	0.000	0.000
83	A	83	LYS	1	0.921	0.961	11.650	0.430	0.430	0.000	0.000	0.000	0.000
84	A	84	PHE	0	-0.135	-0.091	8.618	0.146	0.146	0.000	0.000	0.000	0.000
85	A	85	ASP	-1	-0.939	-0.958	5.238	-5.099	-5.099	0.000	0.000	0.000	0.000
86	A	86	VAL	0	-0.041	-0.019	6.400	-0.942	-0.942	0.000	0.000	0.000	0.000
87	A	87	ASP	-1	-0.792	-0.886	4.849	-6.377	-6.388	-0.001	-0.029	0.041	0.000
88	A	88	VAL	0	-0.046	-0.035	8.336	0.620	0.620	0.000	0.000	0.000	0.000
89	A	89	PHE	0	0.019	-0.003	10.293	0.007	0.007	0.000	0.000	0.000	0.000
90	A	90	VAL	0	0.007	0.001	12.221	0.120	0.120	0.000	0.000	0.000	0.000
91	A	91	MET	0	-0.047	0.001	14.791	0.019	0.019	0.000	0.000	0.000	0.000
92	A	92	GLY	0	0.008	-0.005	18.293	0.016	0.016	0.000	0.000	0.000	0.000
93	A	93	HIS	0	-0.029	-0.036	21.200	-0.007	-0.007	0.000	0.000	0.000	0.000
94	A	94	ASP	-1	-0.919	-0.954	23.760	-0.137	-0.137	0.000	0.000	0.000	0.000
95	A	95	TRP	0	-0.028	-0.019	22.290	-0.006	-0.006	0.000	0.000	0.000	0.000
96	A	96	GLU	-1	-0.908	-0.964	23.519	-0.203	-0.203	0.000	0.000	0.000	0.000
97	A	97	GLY	0	-0.019	-0.018	23.708	0.015	0.015	0.000	0.000	0.000	0.000
98	A	98	GLU	-1	-0.978	-0.992	24.212	-0.233	-0.233	0.000	0.000	0.000	0.000
99	A	99	PHE	0	-0.040	-0.050	20.022	-0.009	-0.009	0.000	0.000	0.000	0.000
100	A	100	ASP	-1	-0.841	-0.917	20.497	-0.362	-0.362	0.000	0.000	0.000	0.000
101	A	101	PHE	0	-0.041	-0.019	20.877	-0.021	-0.021	0.000	0.000	0.000	0.000
102	A	102	LEU	0	0.066	0.037	16.552	-0.016	-0.016	0.000	0.000	0.000	0.000
103	A	103	LYS	1	0.848	0.941	16.948	0.301	0.301	0.000	0.000	0.000	0.000
104	A	104	ASP	-1	-0.920	-0.955	17.005	-0.539	-0.539	0.000	0.000	0.000	0.000
105	A	105	LYS	1	0.850	0.925	15.106	0.577	0.577	0.000	0.000	0.000	0.000
106	A	106	CYS	0	-0.024	-0.002	11.650	-0.144	-0.144	0.000	0.000	0.000	0.000
107	A	107	GLU	-1	-0.919	-0.947	12.076	-0.531	-0.531	0.000	0.000	0.000	0.000
108	A	108	VAL	0	-0.017	0.003	13.611	-0.064	-0.064	0.000	0.000	0.000	0.000
109	A	109	ILE	0	-0.028	-0.030	14.635	0.084	0.084	0.000	0.000	0.000	0.000
110	A	110	TYR	0	0.024	0.035	16.826	-0.020	-0.020	0.000	0.000	0.000	0.000
111	A	111	LEU	0	-0.052	-0.030	16.064	0.044	0.044	0.000	0.000	0.000	0.000
112	A	112	LYN	0	0.159	0.081	18.602	0.025	0.025	0.000	0.000	0.000	0.000
113	A	113	ARG	1	0.917	0.960	23.155	0.025	0.025	0.000	0.000	0.000	0.000
114	A	114	THR	0	-0.052	-0.024	20.360	0.006	0.006	0.000	0.000	0.000	0.000
115	A	115	GLU	-1	-0.910	-0.937	23.657	-0.075	-0.075	0.000	0.000	0.000	0.000

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