FMO DATABASE

FMODB ID: QKYYY

Calculation Name: 1B6W-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1B6W

Chain ID: A

ChEMBL ID:

UniProt ID: P19267

Base Structure: X-ray

Registration Date: 2025-07-14

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	129
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-346160.879537
FMO2-HF: Nuclear repulsion	319882.494269
FMO2-HF: Total energy	-26278.385268
FMO2-MP2: Total energy	-26354.921392

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:MED)

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

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.
-26.666	-18.758	9.948	-5.003	-12.851	-0.054

Interaction energy analysis for fragmet #1(A:1:MED)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.059 / q_NPA : -0.025

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	2	GLU	-1	-1.019	-0.860	3.413	-6.805	-6.157	0.015	-0.180	-0.483	0.000
4	A	3	LEU	0	0.024	-0.125	3.333	1.242	3.387	0.004	-0.960	-1.189	0.003
5	A	3	LEU	0	-0.111	0.103	3.151	0.058	0.490	0.069	-0.108	-0.392	0.000
6	A	4	PRO	0	0.013	-0.076	2.781	-2.719	-1.405	0.401	-0.805	-0.911	-0.010
7	A	5	ILE	0	0.097	-0.023	5.152	0.105	0.105	0.000	0.000	0.000	0.000
8	A	5	ILE	0	-0.048	0.145	2.911	-0.905	-0.276	0.278	-0.179	-0.729	0.002
9	A	6	ALA	0	0.114	-0.090	5.728	0.246	0.246	0.000	0.000	0.000	0.000
10	A	6	ALA	0	-0.066	0.107	10.432	0.001	0.001	0.000	0.000	0.000	0.000
11	A	7	PRO	0	-0.053	-0.155	7.981	0.201	0.201	0.000	0.000	0.000	0.000
12	A	8	ILE	0	0.107	0.000	7.163	0.095	0.095	0.000	0.000	0.000	0.000
13	A	8	ILE	0	-0.063	0.159	5.408	0.049	0.049	0.000	0.000	0.000	0.000
14	A	9	GLY	0	0.020	-0.120	8.563	0.214	0.214	0.000	0.000	0.000	0.000
15	A	10	ARG	0	0.066	-0.003	11.011	0.114	0.114	0.000	0.000	0.000	0.000
16	A	10	ARG	1	0.909	1.062	13.042	0.702	0.702	0.000	0.000	0.000	0.000
17	A	11	ILE	0	0.110	-0.040	11.998	0.058	0.058	0.000	0.000	0.000	0.000
18	A	11	ILE	0	-0.089	0.094	10.314	-0.017	-0.017	0.000	0.000	0.000	0.000
19	A	12	ILE	0	0.097	-0.068	12.475	0.024	0.024	0.000	0.000	0.000	0.000
20	A	12	ILE	0	-0.098	0.057	9.819	0.027	0.027	0.000	0.000	0.000	0.000
21	A	13	LYS	0	0.034	-0.129	13.943	0.051	0.051	0.000	0.000	0.000	0.000
22	A	13	LYS	1	0.698	0.947	15.848	-0.045	-0.045	0.000	0.000	0.000	0.000
23	A	14	ASP	0	0.115	-0.057	16.518	0.050	0.050	0.000	0.000	0.000	0.000
24	A	14	ASP	-1	-1.025	-0.859	16.928	-0.352	-0.352	0.000	0.000	0.000	0.000
25	A	15	ALA	0	0.069	-0.111	17.100	-0.004	-0.004	0.000	0.000	0.000	0.000
26	A	15	ALA	0	-0.119	0.093	17.047	0.003	0.003	0.000	0.000	0.000	0.000
27	A	16	GLY	0	-0.017	-0.108	18.701	0.026	0.026	0.000	0.000	0.000	0.000
28	A	17	ALA	0	0.099	0.007	17.466	0.017	0.017	0.000	0.000	0.000	0.000
29	A	17	ALA	0	-0.089	0.103	16.898	0.009	0.009	0.000	0.000	0.000	0.000
30	A	18	GLU	0	0.147	-0.119	18.930	-0.034	-0.034	0.000	0.000	0.000	0.000
31	A	18	GLU	-1	-0.869	-0.759	21.814	0.128	0.128	0.000	0.000	0.000	0.000
32	A	19	ARG	0	-0.059	-0.131	18.506	-0.031	-0.031	0.000	0.000	0.000	0.000
33	A	19	ARG	1	0.808	1.032	18.863	-0.170	-0.170	0.000	0.000	0.000	0.000
34	A	20	VAL	0	0.087	-0.109	13.991	0.014	0.014	0.000	0.000	0.000	0.000
35	A	20	VAL	0	-0.090	0.127	12.082	-0.011	-0.011	0.000	0.000	0.000	0.000
36	A	21	SER	0	0.056	-0.066	13.732	-0.061	-0.061	0.000	0.000	0.000	0.000
37	A	21	SER	0	0.011	0.085	13.469	0.016	0.016	0.000	0.000	0.000	0.000
38	A	22	ASP	0	0.119	-0.093	10.385	-0.064	-0.064	0.000	0.000	0.000	0.000
39	A	22	ASP	-1	-0.891	-0.798	10.412	0.788	0.788	0.000	0.000	0.000	0.000
40	A	23	ASP	0	0.027	-0.143	8.600	0.327	0.327	0.000	0.000	0.000	0.000
41	A	23	ASP	-1	-0.951	-0.828	10.533	2.023	2.023	0.000	0.000	0.000	0.000
42	A	24	ALA	0	0.124	-0.095	8.487	0.362	0.362	0.000	0.000	0.000	0.000
43	A	24	ALA	0	-0.081	0.100	11.251	-0.051	-0.051	0.000	0.000	0.000	0.000
44	A	25	ARG	0	0.004	-0.106	7.674	-0.117	-0.117	0.000	0.000	0.000	0.000
45	A	25	ARG	1	0.817	1.002	7.592	-0.480	-0.480	0.000	0.000	0.000	0.000
46	A	26	ILE	0	0.094	-0.074	4.032	-0.898	-0.790	0.000	-0.022	-0.085	0.000
47	A	26	ILE	0	-0.096	0.099	4.147	-0.020	0.320	0.017	-0.099	-0.259	0.001
48	A	27	THR	0	0.038	-0.090	3.594	-0.139	0.452	0.012	-0.288	-0.315	-0.002
49	A	27	THR	0	-0.048	0.090	7.700	0.114	0.114	0.000	0.000	0.000	0.000
50	A	28	LEU	0	0.130	-0.090	5.959	-0.061	-0.061	0.000	0.000	0.000	0.000
51	A	28	LEU	0	-0.074	0.106	7.438	-0.008	-0.008	0.000	0.000	0.000	0.000
52	A	29	ALA	0	0.060	-0.104	2.808	3.049	-0.221	-0.024	3.567	-0.272	-0.002
53	A	29	ALA	0	-0.060	0.089	2.246	0.498	-0.504	3.219	-1.419	-0.797	0.001
54	A	30	LYS	0	0.067	-0.110	2.964	-3.786	-2.443	0.674	-0.666	-1.350	-0.009
55	A	30	LYS	1	0.893	1.077	2.543	-8.799	-7.956	1.419	-0.517	-1.745	0.002
56	A	31	ILE	0	0.162	-0.037	3.545	-0.369	-0.333	0.034	0.101	-0.170	0.000
57	A	31	ILE	0	-0.096	0.091	7.514	-0.012	-0.012	0.000	0.000	0.000	0.000
58	A	32	LEU	0	0.039	-0.115	6.233	-0.033	-0.033	0.000	0.000	0.000	0.000
59	A	32	LEU	0	-0.086	0.083	6.407	-0.036	-0.036	0.000	0.000	0.000	0.000
60	A	33	GLU	0	0.139	-0.088	4.208	0.256	0.368	0.000	-0.029	-0.083	0.000
61	A	33	GLU	-1	-0.869	-0.753	2.431	-15.859	-12.501	3.828	-3.331	-3.856	-0.040
62	A	34	GLU	0	0.031	-0.170	5.560	-0.136	-0.136	0.000	0.000	0.000	0.000
63	A	34	GLU	-1	-0.982	-0.829	6.679	1.728	1.728	0.000	0.000	0.000	0.000
64	A	35	MET	0	0.108	-0.094	8.117	0.017	0.017	0.000	0.000	0.000	0.000
65	A	35	MET	0	-0.108	0.101	10.299	0.049	0.049	0.000	0.000	0.000	0.000
66	A	36	GLY	0	-0.034	-0.123	9.121	0.062	0.062	0.000	0.000	0.000	0.000
67	A	37	ARG	0	0.049	-0.029	9.179	-0.045	-0.045	0.000	0.000	0.000	0.000
68	A	37	ARG	1	0.814	1.028	3.393	1.172	1.453	0.002	-0.068	-0.215	0.000
69	A	38	ASP	0	0.126	-0.098	10.123	0.030	0.030	0.000	0.000	0.000	0.000
70	A	38	ASP	-1	-1.005	-0.828	13.329	-0.035	-0.035	0.000	0.000	0.000	0.000
71	A	39	ILE	0	0.036	-0.119	13.446	0.074	0.074	0.000	0.000	0.000	0.000
72	A	39	ILE	0	-0.091	0.107	13.363	-0.004	-0.004	0.000	0.000	0.000	0.000
73	A	40	ALA	0	0.093	-0.111	12.903	0.108	0.108	0.000	0.000	0.000	0.000
74	A	40	ALA	0	-0.056	0.124	12.173	-0.046	-0.046	0.000	0.000	0.000	0.000
75	A	41	SER	0	0.035	-0.089	13.840	0.016	0.016	0.000	0.000	0.000	0.000
76	A	41	SER	0	-0.039	0.081	13.809	0.026	0.026	0.000	0.000	0.000	0.000
77	A	42	GLU	0	0.016	-0.145	15.306	0.048	0.048	0.000	0.000	0.000	0.000
78	A	42	GLU	-1	-0.841	-0.766	18.492	-0.222	-0.222	0.000	0.000	0.000	0.000
79	A	43	ALA	0	0.104	-0.101	17.620	0.067	0.067	0.000	0.000	0.000	0.000
80	A	43	ALA	0	-0.045	0.119	17.356	-0.017	-0.017	0.000	0.000	0.000	0.000
81	A	44	ILE	0	0.098	-0.102	17.750	0.026	0.026	0.000	0.000	0.000	0.000
82	A	44	ILE	0	-0.108	0.100	14.811	0.001	0.001	0.000	0.000	0.000	0.000
83	A	45	LYS	0	0.013	-0.157	19.037	0.020	0.020	0.000	0.000	0.000	0.000
84	A	45	LYS	1	0.795	1.013	18.927	0.250	0.250	0.000	0.000	0.000	0.000
85	A	46	LEU	0	0.030	-0.090	21.742	0.037	0.037	0.000	0.000	0.000	0.000
86	A	46	LEU	0	-0.091	0.103	21.898	0.004	0.004	0.000	0.000	0.000	0.000
87	A	47	ALA	0	0.122	-0.092	22.301	0.041	0.041	0.000	0.000	0.000	0.000
88	A	47	ALA	0	-0.062	0.112	21.956	-0.011	-0.011	0.000	0.000	0.000	0.000
89	A	48	ARG	0	0.089	-0.083	23.368	0.011	0.011	0.000	0.000	0.000	0.000
90	A	48	ARG	1	0.841	1.061	21.876	0.258	0.258	0.000	0.000	0.000	0.000
91	A	49	HIS	0	0.061	-0.087	25.000	0.017	0.017	0.000	0.000	0.000	0.000
92	A	49	HIS	0	-0.115	0.082	26.915	0.003	0.003	0.000	0.000	0.000	0.000
93	A	50	ALA	0	0.043	-0.107	27.105	0.028	0.028	0.000	0.000	0.000	0.000
94	A	50	ALA	0	-0.093	0.102	27.343	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	51	GLY	0	-0.019	-0.113	28.510	0.001	0.001	0.000	0.000	0.000	0.000
96	A	52	ARG	0	-0.011	-0.035	26.090	0.007	0.007	0.000	0.000	0.000	0.000
97	A	52	ARG	1	0.704	0.944	23.884	0.390	0.390	0.000	0.000	0.000	0.000
98	A	53	LYS	0	0.128	-0.081	23.120	0.004	0.004	0.000	0.000	0.000	0.000
99	A	53	LYS	1	0.889	1.077	23.047	0.339	0.339	0.000	0.000	0.000	0.000
100	A	54	THR	0	0.014	-0.097	21.383	-0.051	-0.051	0.000	0.000	0.000	0.000
101	A	54	THR	0	-0.039	0.074	22.094	0.020	0.020	0.000	0.000	0.000	0.000
102	A	55	ILE	0	0.083	-0.089	18.875	0.077	0.077	0.000	0.000	0.000	0.000
103	A	55	ILE	0	-0.063	0.137	17.402	-0.010	-0.010	0.000	0.000	0.000	0.000
104	A	56	LYS	0	0.086	-0.105	20.370	-0.057	-0.057	0.000	0.000	0.000	0.000
105	A	56	LYS	1	0.745	0.991	23.872	0.392	0.392	0.000	0.000	0.000	0.000
106	A	57	ALA	0	0.168	-0.089	21.300	-0.021	-0.021	0.000	0.000	0.000	0.000
107	A	57	ALA	0	-0.066	0.126	22.707	0.004	0.004	0.000	0.000	0.000	0.000
108	A	58	GLU	0	0.061	-0.107	22.353	-0.007	-0.007	0.000	0.000	0.000	0.000
109	A	58	GLU	-1	-0.864	-0.783	25.006	-0.364	-0.364	0.000	0.000	0.000	0.000
110	A	59	ASP	0	0.060	-0.108	21.810	0.043	0.043	0.000	0.000	0.000	0.000
111	A	59	ASP	-1	-0.810	-0.740	20.992	-0.450	-0.450	0.000	0.000	0.000	0.000
112	A	60	ILE	0	0.068	-0.079	19.025	0.036	0.036	0.000	0.000	0.000	0.000
113	A	60	ILE	0	-0.038	0.106	16.262	-0.007	-0.007	0.000	0.000	0.000	0.000
114	A	61	GLU	0	0.095	-0.106	19.740	0.009	0.009	0.000	0.000	0.000	0.000
115	A	61	GLU	-1	-0.927	-0.812	22.267	-0.362	-0.362	0.000	0.000	0.000	0.000
116	A	62	LEU	0	0.110	-0.083	22.127	0.029	0.029	0.000	0.000	0.000	0.000
117	A	62	LEU	0	-0.109	0.093	24.284	0.006	0.006	0.000	0.000	0.000	0.000
118	A	63	ALA	0	0.116	-0.122	19.759	0.064	0.064	0.000	0.000	0.000	0.000
119	A	63	ALA	0	-0.067	0.110	19.053	-0.012	-0.012	0.000	0.000	0.000	0.000
120	A	64	VAL	0	0.003	-0.139	18.941	0.039	0.039	0.000	0.000	0.000	0.000
121	A	64	VAL	0	-0.077	0.122	17.157	-0.006	-0.006	0.000	0.000	0.000	0.000
122	A	65	ARG	0	0.140	-0.068	19.716	0.038	0.038	0.000	0.000	0.000	0.000
123	A	65	ARG	1	0.725	0.991	23.553	0.279	0.279	0.000	0.000	0.000	0.000
124	A	66	ARG	0	-0.108	-0.140	22.578	0.042	0.042	0.000	0.000	0.000	0.000
125	A	66	ARG	1	0.830	1.039	22.590	0.204	0.204	0.000	0.000	0.000	0.000
126	A	67	PHE	0	0.148	-0.072	19.490	0.018	0.018	0.000	0.000	0.000	0.000
127	A	67	PHE	0	-0.053	0.117	16.036	-0.010	-0.010	0.000	0.000	0.000	0.000
128	A	68	LYS	0	-0.097	-0.136	20.911	0.023	0.023	0.000	0.000	0.000	0.000
129	A	68	LYS	1	0.990	0.999	24.099	0.072	0.072	0.000	0.000	0.000	0.000

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