FMO DATABASE

FMODB ID: 6G96Z

Calculation Name: 2BL7-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2BL7

Chain ID: A

ChEMBL ID:

UniProt ID: Q47785

Base Structure: X-ray

Registration Date: 2025-07-10

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
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	155
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-578926.059442
FMO2-HF: Nuclear repulsion	545679.977009
FMO2-HF: Total energy	-33246.082433
FMO2-MP2: Total energy	-33343.707322

3D Structure Molmil

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:3:LYS)

Summations of interaction energy for fragment #1(A:3:LYS)

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.
-2.101	0.292	3.249	-1.695	-3.951	0.002

Interaction energy analysis for fragmet #1(A:3:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.104 / q_NPA : 0.007

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].
4	A	4	ASN	0	-0.062	0.051	4.369	-0.180	0.332	0.001	-0.203	-0.310	0.001
5	A	5	ALA	0	0.175	-0.066	3.800	-4.028	-0.766	-0.021	-2.042	-1.200	0.014
6	A	5	ALA	0	-0.057	0.096	8.132	0.146	0.146	0.000	0.000	0.000	0.000
7	A	6	LYS	0	0.062	-0.136	6.830	-0.112	-0.112	0.000	0.000	0.000	0.000
8	A	6	LYS	1	0.738	1.000	7.634	0.485	0.485	0.000	0.000	0.000	0.000
9	A	7	GLN	0	0.133	-0.081	4.057	0.167	0.271	0.003	-0.038	-0.069	0.000
10	A	7	GLN	0	-0.099	0.103	2.326	0.306	1.092	3.193	-1.967	-2.012	-0.015
11	A	8	ILE	0	0.072	-0.106	4.757	0.535	0.545	-0.002	-0.011	0.002	0.000
12	A	8	ILE	0	-0.062	0.116	3.070	2.105	-0.259	0.081	2.578	-0.295	0.002
13	A	9	VAL	0	0.067	-0.078	5.292	0.595	0.627	-0.002	-0.001	-0.030	0.000
14	A	9	VAL	0	-0.073	0.095	8.832	0.054	0.054	0.000	0.000	0.000	0.000
15	A	10	HIS	0	0.103	-0.080	8.578	0.203	0.203	0.000	0.000	0.000	0.000
16	A	10	HIS	0	-0.058	0.114	8.697	0.007	0.007	0.000	0.000	0.000	0.000
17	A	11	GLU	0	0.085	-0.122	7.515	0.355	0.355	0.000	0.000	0.000	0.000
18	A	11	GLU	-1	-0.865	-0.746	5.548	-1.348	-1.350	-0.001	-0.001	0.004	0.000
19	A	12	LEU	0	0.127	-0.085	8.852	0.235	0.235	0.000	0.000	0.000	0.000
20	A	12	LEU	0	-0.121	0.098	9.544	-0.018	-0.018	0.000	0.000	0.000	0.000
21	A	13	TYR	0	0.071	-0.096	10.684	0.144	0.144	0.000	0.000	0.000	0.000
22	A	13	TYR	0	-0.112	0.062	13.086	0.012	0.012	0.000	0.000	0.000	0.000
23	A	14	ASN	0	0.074	-0.087	12.481	0.079	0.079	0.000	0.000	0.000	0.000
24	A	14	ASN	0	-0.113	0.072	12.338	0.039	0.039	0.000	0.000	0.000	0.000
25	A	15	ASP	0	0.093	-0.102	12.785	0.098	0.098	0.000	0.000	0.000	0.000
26	A	15	ASP	-1	-0.885	-0.809	12.671	-0.340	-0.340	0.000	0.000	0.000	0.000
27	A	16	ILE	0	0.086	-0.088	14.392	0.068	0.068	0.000	0.000	0.000	0.000
28	A	16	ILE	0	-0.107	0.081	14.608	-0.003	-0.003	0.000	0.000	0.000	0.000
29	A	17	SER	0	0.000	-0.110	16.604	0.040	0.040	0.000	0.000	0.000	0.000
30	A	17	SER	0	-0.055	0.064	17.002	0.014	0.014	0.000	0.000	0.000	0.000
31	A	18	ILE	0	0.019	-0.131	17.743	0.031	0.031	0.000	0.000	0.000	0.000
32	A	18	ILE	0	-0.090	0.122	16.146	0.009	0.009	0.000	0.000	0.000	0.000
33	A	19	SER	0	-0.015	-0.087	19.369	0.037	0.037	0.000	0.000	0.000	0.000
34	A	19	SER	0	-0.009	0.071	20.017	-0.009	-0.009	0.000	0.000	0.000	0.000
35	A	20	LYS	0	-0.006	-0.100	21.293	0.015	0.015	0.000	0.000	0.000	0.000
36	A	20	LYS	1	0.877	1.069	23.198	0.098	0.098	0.000	0.000	0.000	0.000
37	A	21	ASP	0	0.144	-0.101	23.524	0.021	0.021	0.000	0.000	0.000	0.000
38	A	21	ASP	-1	-0.901	-0.779	23.766	-0.185	-0.185	0.000	0.000	0.000	0.000
39	A	22	PRO	0	-0.008	-0.127	24.302	-0.020	-0.020	0.000	0.000	0.000	0.000
40	A	23	LYS	0	0.090	0.044	25.657	-0.007	-0.007	0.000	0.000	0.000	0.000
41	A	23	LYS	1	0.785	1.007	23.034	0.216	0.216	0.000	0.000	0.000	0.000
42	A	24	TYR	0	-0.007	-0.138	21.170	-0.012	-0.012	0.000	0.000	0.000	0.000
43	A	24	TYR	0	-0.061	0.098	19.822	0.005	0.005	0.000	0.000	0.000	0.000
44	A	25	SER	0	0.089	-0.103	21.421	-0.040	-0.040	0.000	0.000	0.000	0.000
45	A	25	SER	0	-0.011	0.093	25.283	0.010	0.010	0.000	0.000	0.000	0.000
46	A	26	ASP	0	0.073	-0.117	23.152	-0.011	-0.011	0.000	0.000	0.000	0.000
47	A	26	ASP	-1	-0.913	-0.792	24.311	-0.232	-0.232	0.000	0.000	0.000	0.000
48	A	27	ILE	0	0.020	-0.120	19.449	-0.010	-0.010	0.000	0.000	0.000	0.000
49	A	27	ILE	0	-0.056	0.110	17.498	-0.008	-0.008	0.000	0.000	0.000	0.000
50	A	28	LEU	0	0.067	-0.113	18.178	-0.065	-0.065	0.000	0.000	0.000	0.000
51	A	28	LEU	0	-0.058	0.124	17.193	0.002	0.002	0.000	0.000	0.000	0.000
52	A	29	GLU	0	0.116	-0.107	19.263	-0.024	-0.024	0.000	0.000	0.000	0.000
53	A	29	GLU	-1	-0.883	-0.768	23.209	-0.247	-0.247	0.000	0.000	0.000	0.000
54	A	30	VAL	0	0.024	-0.138	20.112	0.009	0.009	0.000	0.000	0.000	0.000
55	A	30	VAL	0	-0.092	0.112	18.393	-0.003	-0.003	0.000	0.000	0.000	0.000
56	A	31	MET	0	0.051	-0.132	15.858	-0.016	-0.016	0.000	0.000	0.000	0.000
57	A	31	MET	0	-0.064	0.130	12.450	0.015	0.015	0.000	0.000	0.000	0.000
58	A	32	GLN	0	0.155	-0.086	15.910	-0.065	-0.065	0.000	0.000	0.000	0.000
59	A	32	GLN	0	-0.053	0.131	18.698	0.012	0.012	0.000	0.000	0.000	0.000
60	A	33	LYS	0	0.017	-0.105	18.187	0.005	0.005	0.000	0.000	0.000	0.000
61	A	33	LYS	1	0.731	0.970	20.059	0.293	0.293	0.000	0.000	0.000	0.000
62	A	34	VAL	0	0.016	-0.121	15.355	0.049	0.049	0.000	0.000	0.000	0.000
63	A	34	VAL	0	-0.042	0.113	13.399	-0.008	-0.008	0.000	0.000	0.000	0.000
64	A	35	TYR	0	0.087	-0.093	13.808	-0.070	-0.070	0.000	0.000	0.000	0.000
65	A	35	TYR	0	-0.126	0.061	12.340	-0.013	-0.013	0.000	0.000	0.000	0.000
66	A	36	LEU	0	0.139	-0.089	14.755	-0.017	-0.017	0.000	0.000	0.000	0.000
67	A	36	LEU	0	-0.112	0.094	18.136	0.009	0.009	0.000	0.000	0.000	0.000
68	A	37	LYS	0	0.064	-0.101	17.491	0.040	0.040	0.000	0.000	0.000	0.000
69	A	37	LYS	1	0.815	1.031	17.321	0.401	0.401	0.000	0.000	0.000	0.000
70	A	38	LEU	0	0.066	-0.100	12.769	0.061	0.061	0.000	0.000	0.000	0.000
71	A	38	LEU	0	-0.058	0.111	10.562	-0.029	-0.029	0.000	0.000	0.000	0.000
72	A	39	GLU	0	0.076	-0.098	13.667	-0.036	-0.036	0.000	0.000	0.000	0.000
73	A	39	GLU	-1	-0.914	-0.802	12.766	-0.397	-0.397	0.000	0.000	0.000	0.000
74	A	40	LYS	0	0.051	-0.071	15.479	0.060	0.060	0.000	0.000	0.000	0.000
75	A	40	LYS	1	0.816	1.014	18.703	0.274	0.274	0.000	0.000	0.000	0.000
76	A	41	GLN	0	0.155	-0.059	16.817	-0.043	-0.043	0.000	0.000	0.000	0.000
77	A	41	GLN	0	-0.087	0.079	20.243	0.005	0.005	0.000	0.000	0.000	0.000
78	A	42	LYS	0	0.093	-0.032	17.726	-0.018	-0.018	0.000	0.000	0.000	0.000
79	A	42	LYS	1	0.865	1.024	20.210	0.248	0.248	0.000	0.000	0.000	0.000
80	A	43	TYR	0	0.073	-0.083	15.963	0.013	0.013	0.000	0.000	0.000	0.000
81	A	43	TYR	0	-0.106	0.065	15.002	0.015	0.015	0.000	0.000	0.000	0.000
82	A	44	GLU	0	0.157	-0.081	13.533	-0.136	-0.136	0.000	0.000	0.000	0.000
83	A	44	GLU	-1	-0.940	-0.831	12.121	-0.423	-0.423	0.000	0.000	0.000	0.000
84	A	45	LEU	0	0.002	-0.089	13.212	-0.059	-0.059	0.000	0.000	0.000	0.000
85	A	45	LEU	0	-0.113	0.066	16.579	0.011	0.011	0.000	0.000	0.000	0.000
86	A	46	ASP	0	0.098	-0.116	13.800	-0.050	-0.050	0.000	0.000	0.000	0.000
87	A	46	ASP	-1	-0.876	-0.772	14.345	-0.685	-0.685	0.000	0.000	0.000	0.000
88	A	47	PRO	0	0.019	-0.081	10.146	0.026	0.026	0.000	0.000	0.000	0.000
89	A	48	SER	0	0.010	-0.013	12.553	-0.082	-0.082	0.000	0.000	0.000	0.000
90	A	48	SER	0	0.013	0.091	12.816	-0.039	-0.039	0.000	0.000	0.000	0.000
91	A	49	PRO	0	0.031	-0.080	13.437	0.002	0.002	0.000	0.000	0.000	0.000
92	A	50	LEU	0	0.034	-0.038	15.500	0.068	0.068	0.000	0.000	0.000	0.000
93	A	50	LEU	0	-0.113	0.103	14.575	0.028	0.028	0.000	0.000	0.000	0.000
94	A	51	ILE	0	0.053	-0.123	11.524	0.129	0.129	0.000	0.000	0.000	0.000
95	A	51	ILE	0	-0.041	0.150	9.689	0.003	0.003	0.000	0.000	0.000	0.000
96	A	52	ASN	0	0.157	-0.058	12.889	-0.024	-0.024	0.000	0.000	0.000	0.000
97	A	52	ASN	0	-0.122	0.060	14.252	0.049	0.049	0.000	0.000	0.000	0.000
98	A	53	ARG	0	0.086	-0.073	15.257	0.046	0.046	0.000	0.000	0.000	0.000
99	A	53	ARG	1	0.808	1.015	17.945	0.501	0.501	0.000	0.000	0.000	0.000
100	A	54	LEU	0	0.081	-0.084	14.692	0.103	0.103	0.000	0.000	0.000	0.000
101	A	54	LEU	0	-0.094	0.098	12.282	0.000	0.000	0.000	0.000	0.000	0.000
102	A	55	VAL	0	0.102	-0.109	14.189	0.067	0.067	0.000	0.000	0.000	0.000
103	A	55	VAL	0	-0.066	0.134	12.232	-0.003	-0.003	0.000	0.000	0.000	0.000
104	A	56	ASN	0	0.115	-0.073	14.937	0.047	0.047	0.000	0.000	0.000	0.000
105	A	56	ASN	0	-0.152	0.039	18.106	0.039	0.039	0.000	0.000	0.000	0.000
106	A	57	TYR	0	0.082	-0.092	18.420	0.058	0.058	0.000	0.000	0.000	0.000
107	A	57	TYR	0	-0.102	0.066	18.187	0.013	0.013	0.000	0.000	0.000	0.000
108	A	58	LEU	0	0.044	-0.116	16.673	0.077	0.077	0.000	0.000	0.000	0.000
109	A	58	LEU	0	-0.067	0.109	13.980	-0.010	-0.010	0.000	0.000	0.000	0.000
110	A	59	TYR	0	0.116	-0.080	18.161	0.042	0.042	0.000	0.000	0.000	0.000
111	A	59	TYR	0	-0.062	0.108	15.404	-0.020	-0.020	0.000	0.000	0.000	0.000
112	A	60	PHE	0	0.147	-0.067	19.929	0.040	0.040	0.000	0.000	0.000	0.000
113	A	60	PHE	0	-0.099	0.085	22.550	0.001	0.001	0.000	0.000	0.000	0.000
114	A	61	THR	0	0.051	-0.060	22.067	0.038	0.038	0.000	0.000	0.000	0.000
115	A	61	THR	0	-0.051	0.063	20.840	0.011	0.011	0.000	0.000	0.000	0.000
116	A	62	ALA	0	0.087	-0.101	21.382	0.036	0.036	0.000	0.000	0.000	0.000
117	A	62	ALA	0	-0.056	0.121	20.533	-0.007	-0.007	0.000	0.000	0.000	0.000
118	A	63	TYR	0	0.044	-0.081	22.624	0.025	0.025	0.000	0.000	0.000	0.000
119	A	63	TYR	0	-0.104	0.074	24.827	0.004	0.004	0.000	0.000	0.000	0.000
120	A	64	THR	0	0.015	-0.094	25.435	0.023	0.023	0.000	0.000	0.000	0.000
121	A	64	THR	0	-0.068	0.049	26.434	0.005	0.005	0.000	0.000	0.000	0.000
122	A	65	ASN	0	0.012	-0.092	26.215	0.022	0.022	0.000	0.000	0.000	0.000
123	A	65	ASN	0	-0.134	0.060	25.397	0.016	0.016	0.000	0.000	0.000	0.000
124	A	66	LYS	0	0.094	-0.058	26.694	0.006	0.006	0.000	0.000	0.000	0.000
125	A	66	LYS	1	0.839	1.036	28.498	0.160	0.160	0.000	0.000	0.000	0.000
126	A	67	ILE	0	0.077	-0.114	23.041	0.025	0.025	0.000	0.000	0.000	0.000
127	A	67	ILE	0	-0.082	0.097	21.242	-0.002	-0.002	0.000	0.000	0.000	0.000
128	A	68	ARG	0	0.032	-0.132	21.727	-0.018	-0.018	0.000	0.000	0.000	0.000
129	A	68	ARG	1	0.820	1.049	20.400	0.279	0.279	0.000	0.000	0.000	0.000
130	A	69	PHE	0	0.071	-0.083	17.284	0.027	0.027	0.000	0.000	0.000	0.000
131	A	69	PHE	0	-0.073	0.082	16.338	-0.019	-0.019	0.000	0.000	0.000	0.000
132	A	70	THR	0	0.061	-0.058	17.217	0.027	0.027	0.000	0.000	0.000	0.000
133	A	70	THR	0	-0.021	0.054	16.334	-0.014	-0.014	0.000	0.000	0.000	0.000
134	A	71	GLU	0	0.189	-0.056	15.884	-0.073	-0.073	0.000	0.000	0.000	0.000
135	A	71	GLU	-1	-0.891	-0.784	14.952	-0.309	-0.309	0.000	0.000	0.000	0.000
136	A	72	TYR	0	0.056	-0.100	12.859	-0.060	-0.060	0.000	0.000	0.000	0.000
137	A	72	TYR	0	-0.120	0.069	9.083	0.043	0.043	0.000	0.000	0.000	0.000
138	A	73	GLN	0	0.109	-0.101	11.395	-0.135	-0.135	0.000	0.000	0.000	0.000
139	A	73	GLN	0	-0.117	0.064	14.029	0.009	0.009	0.000	0.000	0.000	0.000
140	A	74	GLU	0	0.061	-0.105	11.943	-0.192	-0.192	0.000	0.000	0.000	0.000
141	A	74	GLU	-1	-0.944	-0.825	14.996	-0.355	-0.355	0.000	0.000	0.000	0.000
142	A	75	GLU	0	0.083	-0.106	10.862	-0.122	-0.122	0.000	0.000	0.000	0.000
143	A	75	GLU	-1	-0.899	-0.783	8.831	-0.619	-0.619	0.000	0.000	0.000	0.000
144	A	76	LEU	0	0.085	-0.105	7.366	-0.233	-0.233	0.000	0.000	0.000	0.000
145	A	76	LEU	0	-0.092	0.101	6.417	-0.066	-0.066	0.000	0.000	0.000	0.000
146	A	77	ILE	0	0.099	-0.096	7.955	-0.562	-0.562	0.000	0.000	0.000	0.000
147	A	77	ILE	0	-0.101	0.094	11.980	0.022	0.022	0.000	0.000	0.000	0.000
148	A	78	ARG	0	0.101	-0.110	10.440	-0.123	-0.123	0.000	0.000	0.000	0.000
149	A	78	ARG	1	0.701	0.992	10.264	0.532	0.532	0.000	0.000	0.000	0.000
150	A	79	ASN	0	0.054	-0.102	5.781	0.340	0.356	-0.002	-0.001	-0.014	0.000
151	A	79	ASN	0	-0.104	0.048	4.902	-0.658	-0.621	-0.001	-0.009	-0.027	0.000
152	A	80	MET	0	0.028	-0.090	7.043	-0.504	-0.504	0.000	0.000	0.000	0.000
153	A	80	MET	0	-0.128	0.052	7.515	0.104	0.104	0.000	0.000	0.000	0.000
154	A	81	SER	0	-0.166	-0.169	8.411	0.247	0.247	0.000	0.000	0.000	0.000
155	A	81	SER	0	0.020	0.032	11.287	0.124	0.124	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:LYS)