FMO DATABASE

FMODB ID: K9433

Calculation Name: 2BK0-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2BK0

Chain ID: A

ChEMBL ID:

UniProt ID: P49372

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	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	153
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1313877.282673
FMO2-HF: Nuclear repulsion	1257837.475376
FMO2-HF: Total energy	-56039.807298
FMO2-MP2: Total energy	-56205.82834

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:2:GLY)

Summations of interaction energy for fragment #1(A:2:GLY)

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.
-11.889	-12.963	16.725	-8.223	-7.426	-0.069

Interaction energy analysis for fragmet #1(A:2:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.016 / q_NPA : -0.010

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	4	GLN	0	-0.002	0.007	3.860	0.794	1.695	-0.010	-0.400	-0.491	0.001
4	A	5	THR	0	-0.009	-0.005	6.578	0.031	0.031	0.000	0.000	0.000	0.000
5	A	6	HIS	0	-0.004	0.000	10.328	0.025	0.025	0.000	0.000	0.000	0.000
6	A	7	VAL	0	-0.020	-0.013	13.429	0.003	0.003	0.000	0.000	0.000	0.000
7	A	8	LEU	0	-0.028	-0.001	17.127	0.003	0.003	0.000	0.000	0.000	0.000
8	A	9	GLU	-1	-0.859	-0.923	20.316	-0.141	-0.141	0.000	0.000	0.000	0.000
9	A	10	LEU	0	-0.034	-0.014	23.776	0.005	0.005	0.000	0.000	0.000	0.000
10	A	11	THR	0	-0.012	-0.002	26.960	0.005	0.005	0.000	0.000	0.000	0.000
11	A	12	SER	0	-0.058	-0.052	30.389	-0.003	-0.003	0.000	0.000	0.000	0.000
12	A	13	SER	0	-0.027	-0.011	32.934	0.007	0.007	0.000	0.000	0.000	0.000
13	A	14	VAL	0	0.004	0.001	34.726	0.006	0.006	0.000	0.000	0.000	0.000
14	A	15	SER	0	0.050	0.037	34.800	-0.005	-0.005	0.000	0.000	0.000	0.000
15	A	16	ALA	0	0.036	0.006	32.085	-0.004	-0.004	0.000	0.000	0.000	0.000
16	A	17	GLU	-1	-0.917	-0.955	32.592	-0.070	-0.070	0.000	0.000	0.000	0.000
17	A	18	LYS	1	0.858	0.932	34.626	0.075	0.075	0.000	0.000	0.000	0.000
18	A	19	ILE	0	0.011	0.008	29.882	-0.005	-0.005	0.000	0.000	0.000	0.000
19	A	20	PHE	0	0.035	0.008	26.947	-0.006	-0.006	0.000	0.000	0.000	0.000
20	A	21	GLN	0	-0.040	-0.043	31.045	-0.004	-0.004	0.000	0.000	0.000	0.000
21	A	22	GLY	0	-0.001	-0.004	33.330	-0.003	-0.003	0.000	0.000	0.000	0.000
22	A	23	PHE	0	-0.015	-0.020	25.559	-0.006	-0.006	0.000	0.000	0.000	0.000
23	A	24	VAL	0	-0.053	-0.020	26.702	-0.016	-0.016	0.000	0.000	0.000	0.000
24	A	25	ILE	0	-0.070	-0.023	28.881	0.001	0.001	0.000	0.000	0.000	0.000
25	A	26	ASP	-1	-0.814	-0.894	32.025	-0.094	-0.094	0.000	0.000	0.000	0.000
26	A	27	VAL	0	0.004	0.010	27.940	0.000	0.000	0.000	0.000	0.000	0.000
27	A	28	ASP	-1	-0.783	-0.884	29.102	-0.171	-0.171	0.000	0.000	0.000	0.000
28	A	29	THR	0	-0.051	-0.023	31.786	0.006	0.006	0.000	0.000	0.000	0.000
29	A	30	VAL	0	-0.051	-0.024	33.232	0.006	0.006	0.000	0.000	0.000	0.000
30	A	31	LEU	0	0.049	0.022	27.893	0.003	0.003	0.000	0.000	0.000	0.000
31	A	32	PRO	0	-0.021	-0.009	32.443	0.001	0.001	0.000	0.000	0.000	0.000
32	A	33	LYS	1	0.848	0.929	35.197	0.102	0.102	0.000	0.000	0.000	0.000
33	A	34	ALA	0	-0.034	-0.013	33.785	0.004	0.004	0.000	0.000	0.000	0.000
34	A	35	ALA	0	-0.003	-0.010	31.409	0.000	0.000	0.000	0.000	0.000	0.000
35	A	36	PRO	0	-0.012	-0.004	32.392	-0.009	-0.009	0.000	0.000	0.000	0.000
36	A	37	GLY	0	0.004	0.011	33.198	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	38	ALA	0	-0.034	-0.016	28.205	-0.006	-0.006	0.000	0.000	0.000	0.000
38	A	39	TYR	0	-0.032	-0.023	27.570	-0.017	-0.017	0.000	0.000	0.000	0.000
39	A	40	LYS	1	0.802	0.897	29.111	0.169	0.169	0.000	0.000	0.000	0.000
40	A	41	SER	0	-0.011	-0.023	29.686	0.016	0.016	0.000	0.000	0.000	0.000
41	A	42	VAL	0	0.004	-0.001	27.970	-0.015	-0.015	0.000	0.000	0.000	0.000
42	A	43	GLU	-1	-0.851	-0.900	28.007	-0.144	-0.144	0.000	0.000	0.000	0.000
43	A	44	ILE	0	-0.001	-0.006	27.525	-0.016	-0.016	0.000	0.000	0.000	0.000
44	A	45	LYS	1	0.776	0.875	26.803	0.168	0.168	0.000	0.000	0.000	0.000
45	A	46	GLY	0	0.036	0.004	26.986	-0.008	-0.008	0.000	0.000	0.000	0.000
46	A	47	ASP	-1	-0.917	-0.943	29.146	-0.100	-0.100	0.000	0.000	0.000	0.000
47	A	48	GLY	0	0.012	0.002	29.182	0.003	0.003	0.000	0.000	0.000	0.000
48	A	49	GLY	0	-0.001	0.002	27.933	-0.009	-0.009	0.000	0.000	0.000	0.000
49	A	50	PRO	0	-0.034	-0.028	23.650	-0.011	-0.011	0.000	0.000	0.000	0.000
50	A	51	GLY	0	-0.006	0.006	22.596	0.015	0.015	0.000	0.000	0.000	0.000
51	A	52	THR	0	-0.045	-0.024	23.591	-0.006	-0.006	0.000	0.000	0.000	0.000
52	A	53	LEU	0	0.001	0.005	20.897	-0.022	-0.022	0.000	0.000	0.000	0.000
53	A	54	LYS	1	0.813	0.878	22.988	0.209	0.209	0.000	0.000	0.000	0.000
54	A	55	ILE	0	0.012	0.026	22.993	-0.027	-0.027	0.000	0.000	0.000	0.000
55	A	56	ILE	0	0.010	-0.005	23.402	0.026	0.026	0.000	0.000	0.000	0.000
56	A	57	THR	0	0.006	0.013	24.120	-0.016	-0.016	0.000	0.000	0.000	0.000
57	A	58	LEU	0	-0.002	-0.004	22.500	0.013	0.013	0.000	0.000	0.000	0.000
58	A	59	PRO	0	0.008	-0.008	26.900	0.010	0.010	0.000	0.000	0.000	0.000
59	A	60	ASP	-1	-0.818	-0.898	28.385	-0.172	-0.172	0.000	0.000	0.000	0.000
60	A	61	GLY	0	-0.036	0.001	29.307	-0.003	-0.003	0.000	0.000	0.000	0.000
61	A	62	GLY	0	0.021	0.007	26.129	0.006	0.006	0.000	0.000	0.000	0.000
62	A	63	PRO	0	-0.059	-0.041	21.300	0.000	0.000	0.000	0.000	0.000	0.000
63	A	64	ILE	0	-0.015	0.008	18.471	-0.026	-0.026	0.000	0.000	0.000	0.000
64	A	65	THR	0	-0.042	-0.014	21.834	0.035	0.035	0.000	0.000	0.000	0.000
65	A	66	THR	0	-0.022	-0.047	21.494	0.037	0.037	0.000	0.000	0.000	0.000
66	A	67	MET	0	-0.064	-0.021	19.267	-0.044	-0.044	0.000	0.000	0.000	0.000
67	A	68	THR	0	-0.019	-0.029	18.778	0.054	0.054	0.000	0.000	0.000	0.000
68	A	69	LEU	0	-0.002	-0.001	18.127	-0.052	-0.052	0.000	0.000	0.000	0.000
69	A	70	ARG	1	0.861	0.909	15.102	0.341	0.341	0.000	0.000	0.000	0.000
70	A	71	ILE	0	0.016	0.018	19.447	-0.029	-0.029	0.000	0.000	0.000	0.000
71	A	72	ASP	-1	-0.808	-0.870	17.313	-0.288	-0.288	0.000	0.000	0.000	0.000
72	A	73	GLY	0	0.001	-0.005	20.625	0.029	0.029	0.000	0.000	0.000	0.000
73	A	74	VAL	0	0.006	-0.003	23.231	-0.016	-0.016	0.000	0.000	0.000	0.000
74	A	75	ASN	0	-0.058	-0.029	26.485	0.013	0.013	0.000	0.000	0.000	0.000
75	A	76	LYS	1	0.976	0.990	28.964	0.077	0.077	0.000	0.000	0.000	0.000
76	A	77	GLU	-1	-0.863	-0.931	31.942	-0.062	-0.062	0.000	0.000	0.000	0.000
77	A	78	ALA	0	-0.015	-0.001	28.731	0.004	0.004	0.000	0.000	0.000	0.000
78	A	79	LEU	0	-0.041	0.000	28.608	-0.007	-0.007	0.000	0.000	0.000	0.000
79	A	80	THR	0	-0.001	-0.013	23.450	-0.010	-0.010	0.000	0.000	0.000	0.000
80	A	81	PHE	0	-0.034	-0.031	23.397	0.007	0.007	0.000	0.000	0.000	0.000
81	A	82	ASP	-1	-0.812	-0.883	19.159	-0.196	-0.196	0.000	0.000	0.000	0.000
82	A	83	TYR	0	-0.004	-0.001	18.482	0.031	0.031	0.000	0.000	0.000	0.000
83	A	84	SER	0	0.004	-0.012	14.242	-0.072	-0.072	0.000	0.000	0.000	0.000
84	A	85	VAL	0	-0.034	-0.015	14.027	0.068	0.068	0.000	0.000	0.000	0.000
85	A	86	ILE	0	-0.025	-0.035	13.327	-0.109	-0.109	0.000	0.000	0.000	0.000
86	A	87	ASP	-1	-0.827	-0.893	14.722	-0.358	-0.358	0.000	0.000	0.000	0.000
87	A	88	GLY	0	0.019	0.021	16.625	0.001	0.001	0.000	0.000	0.000	0.000
88	A	89	ASP	-1	-0.764	-0.874	16.316	-0.435	-0.435	0.000	0.000	0.000	0.000
89	A	90	ILE	0	0.045	0.019	14.664	-0.035	-0.035	0.000	0.000	0.000	0.000
90	A	91	LEU	0	-0.032	-0.003	11.092	-0.081	-0.081	0.000	0.000	0.000	0.000
91	A	92	LEU	0	-0.042	-0.012	11.733	-0.155	-0.155	0.000	0.000	0.000	0.000
92	A	93	GLY	0	-0.012	-0.023	12.031	0.124	0.124	0.000	0.000	0.000	0.000
93	A	94	PHE	0	-0.004	0.000	6.575	0.056	0.056	0.000	0.000	0.000	0.000
94	A	95	ILE	0	0.010	0.021	6.645	-0.695	-0.695	0.000	0.000	0.000	0.000
95	A	96	GLU	-1	-0.989	-1.002	6.598	-0.551	-0.551	0.000	0.000	0.000	0.000
96	A	97	SER	0	-0.001	-0.007	8.061	0.380	0.380	0.000	0.000	0.000	0.000
97	A	98	ILE	0	-0.008	-0.004	8.979	-0.341	-0.341	0.000	0.000	0.000	0.000
98	A	99	GLU	-1	-0.784	-0.840	11.075	-0.268	-0.268	0.000	0.000	0.000	0.000
99	A	100	ASN	0	-0.057	-0.044	12.899	-0.057	-0.057	0.000	0.000	0.000	0.000
100	A	101	HIS	1	0.782	0.846	14.444	0.340	0.340	0.000	0.000	0.000	0.000
101	A	102	VAL	0	-0.020	-0.008	18.508	-0.010	-0.010	0.000	0.000	0.000	0.000
102	A	103	VAL	0	0.020	0.013	21.735	0.017	0.017	0.000	0.000	0.000	0.000
103	A	104	LEU	0	-0.019	-0.005	24.721	-0.006	-0.006	0.000	0.000	0.000	0.000
104	A	105	VAL	0	-0.003	0.002	27.445	0.011	0.011	0.000	0.000	0.000	0.000
105	A	106	PRO	0	0.022	-0.004	30.219	-0.003	-0.003	0.000	0.000	0.000	0.000
106	A	107	THR	0	-0.040	-0.034	33.077	0.001	0.001	0.000	0.000	0.000	0.000
107	A	108	ALA	0	-0.025	-0.021	35.594	0.002	0.002	0.000	0.000	0.000	0.000
108	A	109	ASP	-1	-0.873	-0.911	37.408	-0.064	-0.064	0.000	0.000	0.000	0.000
109	A	110	GLY	0	-0.015	-0.004	39.061	0.001	0.001	0.000	0.000	0.000	0.000
110	A	111	GLY	0	-0.008	0.008	36.350	-0.002	-0.002	0.000	0.000	0.000	0.000
111	A	112	SER	0	-0.041	-0.050	31.732	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	113	ILE	0	-0.002	-0.005	26.988	-0.002	-0.002	0.000	0.000	0.000	0.000
113	A	114	CYS	0	-0.017	0.011	25.470	-0.002	-0.002	0.000	0.000	0.000	0.000
114	A	115	LYS	1	0.891	0.937	20.056	0.149	0.149	0.000	0.000	0.000	0.000
115	A	116	THR	0	0.019	0.003	19.373	-0.003	-0.003	0.000	0.000	0.000	0.000
116	A	117	THR	0	-0.013	-0.017	14.869	0.013	0.013	0.000	0.000	0.000	0.000
117	A	118	ALA	0	0.026	0.021	13.512	0.016	0.016	0.000	0.000	0.000	0.000
118	A	119	ILE	0	-0.016	-0.020	8.153	0.035	0.035	0.000	0.000	0.000	0.000
119	A	120	PHE	0	0.000	0.005	7.216	0.124	0.124	0.000	0.000	0.000	0.000
120	A	121	HIS	0	0.015	0.004	4.947	-1.148	-1.148	0.000	0.000	0.000	0.000
121	A	122	THR	0	-0.045	-0.052	2.512	-0.884	0.220	1.803	-1.434	-1.473	-0.009
122	A	123	LYS	1	0.878	0.946	1.936	-3.594	-6.130	7.797	-3.179	-2.082	-0.028
123	A	124	GLY	0	0.007	0.002	3.090	0.200	0.722	0.085	-0.159	-0.447	0.000
124	A	125	ASP	-1	-0.913	-0.963	1.976	-3.944	-5.483	7.045	-2.825	-2.681	-0.032
125	A	126	ALA	0	-0.036	-0.006	4.073	0.247	0.331	-0.001	-0.048	-0.035	0.000
126	A	127	VAL	0	0.002	0.011	3.694	-1.383	-0.993	0.006	-0.178	-0.217	-0.001
127	A	128	VAL	0	-0.022	-0.020	6.264	0.148	0.148	0.000	0.000	0.000	0.000
128	A	129	PRO	0	0.015	0.012	8.932	0.116	0.116	0.000	0.000	0.000	0.000
129	A	130	GLU	-1	-0.880	-0.939	12.301	-0.289	-0.289	0.000	0.000	0.000	0.000
130	A	131	GLU	-1	-0.894	-0.954	14.756	-0.346	-0.346	0.000	0.000	0.000	0.000
131	A	132	ASN	0	-0.026	-0.021	13.557	-0.002	-0.002	0.000	0.000	0.000	0.000
132	A	133	ILE	0	0.029	0.022	10.805	0.014	0.014	0.000	0.000	0.000	0.000
133	A	134	LYS	1	0.804	0.889	15.062	0.268	0.268	0.000	0.000	0.000	0.000
134	A	135	TYR	0	0.008	-0.005	18.600	0.040	0.040	0.000	0.000	0.000	0.000
135	A	136	ALA	0	0.024	0.011	16.553	0.028	0.028	0.000	0.000	0.000	0.000
136	A	137	ASN	0	0.044	0.017	18.043	0.002	0.002	0.000	0.000	0.000	0.000
137	A	138	GLU	-1	-0.852	-0.887	20.181	-0.186	-0.186	0.000	0.000	0.000	0.000
138	A	139	GLN	0	0.005	-0.001	21.971	0.031	0.031	0.000	0.000	0.000	0.000
139	A	140	ASN	0	-0.039	-0.029	19.638	0.032	0.032	0.000	0.000	0.000	0.000
140	A	141	THR	0	-0.015	-0.015	23.194	0.025	0.025	0.000	0.000	0.000	0.000
141	A	142	ALA	0	-0.032	-0.013	25.703	0.019	0.019	0.000	0.000	0.000	0.000
142	A	143	LEU	0	0.013	0.007	25.115	0.015	0.015	0.000	0.000	0.000	0.000
143	A	144	PHE	0	0.029	0.000	26.390	0.013	0.013	0.000	0.000	0.000	0.000
144	A	145	LYS	1	0.981	0.980	28.282	0.143	0.143	0.000	0.000	0.000	0.000
145	A	146	ALA	0	-0.010	0.014	31.082	0.011	0.011	0.000	0.000	0.000	0.000
146	A	147	LEU	0	0.010	-0.003	29.360	0.011	0.011	0.000	0.000	0.000	0.000
147	A	148	GLU	-1	-0.821	-0.883	32.314	-0.104	-0.104	0.000	0.000	0.000	0.000
148	A	149	ALA	0	0.007	0.001	34.028	0.009	0.009	0.000	0.000	0.000	0.000
149	A	150	TYR	0	0.000	-0.005	36.020	0.007	0.007	0.000	0.000	0.000	0.000
150	A	151	LEU	0	0.007	-0.006	33.519	0.007	0.007	0.000	0.000	0.000	0.000
151	A	152	ILE	0	-0.033	-0.016	37.414	0.007	0.007	0.000	0.000	0.000	0.000
152	A	153	ALA	0	-0.040	-0.011	39.912	0.005	0.005	0.000	0.000	0.000	0.000
153	A	154	ASN	0	-0.034	0.011	40.540	0.005	0.005	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:GLY)