FMO DATABASE

FMODB ID: JQNK9

Calculation Name: 1BGF-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1BGF

Chain ID: A

ChEMBL ID:

UniProt ID: P42228

Base Structure: X-ray

Registration Date: 2023-09-23

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

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	124
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1100406.831953
FMO2-HF: Nuclear repulsion	1049523.211324
FMO2-HF: Total energy	-50883.62063
FMO2-MP2: Total energy	-51031.693377

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:0:GLY)

Summations of interaction energy for fragment #1(A:0: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.
0.925	2.252	-0.027	-0.647	-0.651	0

Interaction energy analysis for fragmet #1(A:0:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.012 / q_NPA : -0.020

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].
3	A	2	SER	0	0.002	0.007	3.773	-0.023	1.304	-0.027	-0.647	-0.651
4	A	3	GLN	0	-0.041	-0.042	6.939	0.410	0.410	0.000	0.000	0.000
5	A	4	TRP	0	-0.031	-0.036	9.638	0.114	0.114	0.000	0.000	0.000
6	A	5	ASN	0	-0.032	-0.016	6.165	0.554	0.554	0.000	0.000	0.000
7	A	6	GLN	0	0.042	0.008	6.756	0.223	0.223	0.000	0.000	0.000
8	A	7	VAL	0	0.010	0.006	9.781	0.009	0.009	0.000	0.000	0.000
9	A	8	GLN	0	-0.063	-0.040	11.302	-0.074	-0.074	0.000	0.000	0.000
10	A	9	GLN	0	-0.075	-0.025	9.160	-0.005	-0.005	0.000	0.000	0.000
11	A	10	LEU	0	-0.043	0.007	12.464	0.012	0.012	0.000	0.000	0.000
12	A	11	GLU	-1	-0.933	-0.964	15.726	0.127	0.127	0.000	0.000	0.000
13	A	12	ILE	0	0.072	0.018	18.897	-0.007	-0.007	0.000	0.000	0.000
14	A	13	LYS	1	0.924	0.944	20.604	-0.148	-0.148	0.000	0.000	0.000
15	A	14	PHE	0	0.016	0.017	17.833	-0.005	-0.005	0.000	0.000	0.000
16	A	15	LEU	0	-0.010	0.000	19.795	-0.010	-0.010	0.000	0.000	0.000
17	A	16	GLU	-1	-0.964	-0.983	22.054	0.045	0.045	0.000	0.000	0.000
18	A	17	GLN	0	-0.044	-0.033	23.335	-0.002	-0.002	0.000	0.000	0.000
19	A	18	VAL	0	0.003	-0.003	19.959	-0.001	-0.001	0.000	0.000	0.000
20	A	19	ASP	-1	-0.939	-0.958	23.401	-0.016	-0.016	0.000	0.000	0.000
21	A	20	GLN	0	0.044	0.016	26.214	-0.011	-0.011	0.000	0.000	0.000
22	A	21	PHE	0	-0.089	-0.045	23.364	0.000	0.000	0.000	0.000	0.000
23	A	22	TYR	0	-0.035	-0.016	19.165	-0.023	-0.023	0.000	0.000	0.000
24	A	23	ASP	-1	-0.729	-0.873	25.605	-0.025	-0.025	0.000	0.000	0.000
25	A	24	ASP	-1	-0.955	-0.978	27.942	-0.048	-0.048	0.000	0.000	0.000
26	A	25	ASN	0	-0.171	-0.095	28.082	-0.010	-0.010	0.000	0.000	0.000
27	A	26	PHE	0	-0.012	-0.032	18.909	-0.013	-0.013	0.000	0.000	0.000
28	A	27	PRO	0	0.076	0.065	24.227	0.006	0.006	0.000	0.000	0.000
29	A	28	MET	0	0.067	0.016	19.925	-0.016	-0.016	0.000	0.000	0.000
30	A	29	GLU	-1	-0.870	-0.949	19.925	-0.117	-0.117	0.000	0.000	0.000
31	A	30	ILE	0	-0.020	-0.011	19.954	-0.029	-0.029	0.000	0.000	0.000
32	A	31	ARG	1	0.742	0.859	12.681	0.110	0.110	0.000	0.000	0.000
33	A	32	HIS	0	0.007	0.007	15.041	-0.036	-0.036	0.000	0.000	0.000
34	A	33	LEU	0	-0.047	-0.030	14.934	-0.060	-0.060	0.000	0.000	0.000
35	A	34	LEU	0	-0.041	-0.011	15.777	-0.047	-0.047	0.000	0.000	0.000
36	A	35	ALA	0	0.015	0.027	11.928	0.008	0.008	0.000	0.000	0.000
37	A	36	GLN	0	0.015	-0.011	7.682	-0.298	-0.298	0.000	0.000	0.000
38	A	37	TRP	0	0.043	0.034	11.573	0.055	0.055	0.000	0.000	0.000
39	A	38	ILE	0	0.029	0.003	15.077	0.044	0.044	0.000	0.000	0.000
40	A	39	GLU	-1	-0.729	-0.871	9.828	-0.330	-0.330	0.000	0.000	0.000
41	A	40	THR	0	-0.059	-0.020	12.733	0.011	0.011	0.000	0.000	0.000
42	A	41	GLN	0	-0.075	-0.039	14.328	0.047	0.047	0.000	0.000	0.000
43	A	42	ASP	-1	-0.847	-0.919	17.759	-0.013	-0.013	0.000	0.000	0.000
44	A	43	TRP	0	-0.038	-0.036	18.001	0.009	0.009	0.000	0.000	0.000
45	A	44	GLU	-1	-0.837	-0.937	19.298	-0.014	-0.014	0.000	0.000	0.000
46	A	45	VAL	0	-0.026	-0.001	22.968	0.004	0.004	0.000	0.000	0.000
47	A	46	ALA	0	-0.045	-0.021	24.243	0.000	0.000	0.000	0.000	0.000
48	A	47	SER	0	-0.061	-0.030	25.742	0.001	0.001	0.000	0.000	0.000
49	A	48	ASN	0	-0.039	-0.019	27.583	0.004	0.004	0.000	0.000	0.000
50	A	49	ASN	0	0.034	0.012	28.856	-0.003	-0.003	0.000	0.000	0.000
51	A	50	GLU	-1	-0.851	-0.929	29.933	-0.034	-0.034	0.000	0.000	0.000
52	A	51	THR	0	-0.003	0.003	30.810	-0.005	-0.005	0.000	0.000	0.000
53	A	52	MET	0	-0.022	-0.018	24.271	-0.004	-0.004	0.000	0.000	0.000
54	A	53	ALA	0	0.022	0.018	26.852	-0.009	-0.009	0.000	0.000	0.000
55	A	54	THR	0	-0.031	-0.012	27.770	-0.007	-0.007	0.000	0.000	0.000
56	A	55	ILE	0	-0.010	-0.006	25.533	-0.007	-0.007	0.000	0.000	0.000
57	A	56	LEU	0	0.010	0.007	21.892	-0.011	-0.011	0.000	0.000	0.000
58	A	57	LEU	0	0.017	0.024	24.195	-0.014	-0.014	0.000	0.000	0.000
59	A	58	GLN	0	0.002	-0.015	26.601	0.000	0.000	0.000	0.000	0.000
60	A	59	ASN	0	0.009	-0.007	22.748	-0.006	-0.006	0.000	0.000	0.000
61	A	60	LEU	0	0.007	0.024	21.550	-0.017	-0.017	0.000	0.000	0.000
62	A	61	LEU	0	-0.039	-0.038	23.367	-0.011	-0.011	0.000	0.000	0.000
63	A	62	ILE	0	0.004	0.018	23.868	-0.003	-0.003	0.000	0.000	0.000
64	A	63	GLN	0	0.015	-0.001	18.938	-0.034	-0.034	0.000	0.000	0.000
65	A	64	LEU	0	-0.005	0.003	21.951	-0.013	-0.013	0.000	0.000	0.000
66	A	65	ASP	-1	-0.847	-0.933	23.812	-0.120	-0.120	0.000	0.000	0.000
67	A	66	GLU	-1	-0.965	-0.967	20.629	-0.235	-0.235	0.000	0.000	0.000
68	A	67	GLN	0	-0.030	-0.017	17.979	-0.010	-0.010	0.000	0.000	0.000
69	A	68	LEU	0	-0.029	-0.018	22.120	0.006	0.006	0.000	0.000	0.000
70	A	69	GLY	0	0.006	0.017	25.504	0.008	0.008	0.000	0.000	0.000
71	A	70	ARG	1	0.918	0.960	15.649	0.386	0.386	0.000	0.000	0.000
72	A	71	VAL	0	0.037	0.012	22.475	0.007	0.007	0.000	0.000	0.000
73	A	72	SER	0	-0.059	-0.041	24.545	0.018	0.018	0.000	0.000	0.000
74	A	73	LYS	1	0.909	0.965	25.147	0.171	0.171	0.000	0.000	0.000
75	A	74	GLU	-1	-0.908	-0.963	20.576	-0.245	-0.245	0.000	0.000	0.000
76	A	75	LYS	1	0.905	0.960	25.396	0.110	0.110	0.000	0.000	0.000
77	A	76	ASN	0	0.051	0.035	22.944	0.021	0.021	0.000	0.000	0.000
78	A	77	LEU	0	0.014	-0.017	26.589	0.001	0.001	0.000	0.000	0.000
79	A	78	LEU	0	0.035	0.028	26.248	0.003	0.003	0.000	0.000	0.000
80	A	79	LEU	0	0.066	0.025	21.612	0.004	0.004	0.000	0.000	0.000
81	A	80	ILE	0	0.000	0.016	26.014	0.002	0.002	0.000	0.000	0.000
82	A	81	HIS	0	-0.076	-0.041	28.519	0.008	0.008	0.000	0.000	0.000
83	A	82	ASN	0	0.005	-0.009	26.935	0.010	0.010	0.000	0.000	0.000
84	A	83	LEU	0	0.055	0.020	23.227	0.005	0.005	0.000	0.000	0.000
85	A	84	LYS	1	0.919	0.968	27.349	0.098	0.098	0.000	0.000	0.000
86	A	85	ARG	1	0.905	0.957	30.783	0.064	0.064	0.000	0.000	0.000
87	A	86	ILE	0	0.083	0.052	25.437	0.005	0.005	0.000	0.000	0.000
88	A	87	ARG	1	0.904	0.951	29.096	0.103	0.103	0.000	0.000	0.000
89	A	88	LYS	1	0.910	0.958	29.878	0.063	0.063	0.000	0.000	0.000
90	A	89	VAL	0	0.019	0.015	30.944	0.004	0.004	0.000	0.000	0.000
91	A	90	LEU	0	0.050	0.012	25.834	0.004	0.004	0.000	0.000	0.000
92	A	91	GLN	0	-0.021	-0.010	30.303	0.001	0.001	0.000	0.000	0.000
93	A	92	GLY	0	0.013	0.013	33.015	0.003	0.003	0.000	0.000	0.000
94	A	93	LYS	1	0.908	0.960	30.427	0.045	0.045	0.000	0.000	0.000
95	A	94	PHE	0	-0.045	-0.031	31.346	0.002	0.002	0.000	0.000	0.000
96	A	95	HIS	0	-0.061	-0.030	32.771	0.003	0.003	0.000	0.000	0.000
97	A	96	GLY	0	-0.013	0.010	35.347	0.004	0.004	0.000	0.000	0.000
98	A	97	ASN	0	0.007	-0.006	33.737	0.001	0.001	0.000	0.000	0.000
99	A	98	PRO	0	0.063	0.023	29.919	0.000	0.000	0.000	0.000	0.000
100	A	99	MET	0	0.041	0.016	28.854	-0.003	-0.003	0.000	0.000	0.000
101	A	100	HIS	0	-0.024	-0.002	28.811	0.003	0.003	0.000	0.000	0.000
102	A	101	VAL	0	0.007	0.006	25.367	0.002	0.002	0.000	0.000	0.000
103	A	102	ALA	0	-0.001	0.012	24.442	-0.002	-0.002	0.000	0.000	0.000
104	A	103	VAL	0	0.027	0.036	24.229	0.004	0.004	0.000	0.000	0.000
105	A	104	VAL	0	-0.037	-0.011	24.792	0.006	0.006	0.000	0.000	0.000
106	A	105	ILE	0	-0.010	-0.001	19.691	0.004	0.004	0.000	0.000	0.000
107	A	106	SER	0	0.020	-0.010	20.432	0.005	0.005	0.000	0.000	0.000
108	A	107	ASN	0	-0.077	-0.050	20.885	0.019	0.019	0.000	0.000	0.000
109	A	108	CYS	0	0.011	0.022	20.154	0.016	0.016	0.000	0.000	0.000
110	A	109	LEU	0	0.041	0.020	14.938	0.017	0.017	0.000	0.000	0.000
111	A	110	ARG	1	0.930	0.953	16.918	-0.047	-0.047	0.000	0.000	0.000
112	A	111	GLU	-1	-0.775	-0.866	19.242	0.109	0.109	0.000	0.000	0.000
113	A	112	GLU	-1	-0.755	-0.845	14.803	0.010	0.010	0.000	0.000	0.000
114	A	113	ARG	1	0.931	0.977	14.400	-0.053	-0.053	0.000	0.000	0.000
115	A	114	ARG	1	0.782	0.883	16.152	-0.075	-0.075	0.000	0.000	0.000
116	A	115	ILE	0	-0.010	-0.012	17.995	0.019	0.019	0.000	0.000	0.000
117	A	116	LEU	0	-0.028	-0.023	11.860	0.013	0.013	0.000	0.000	0.000
118	A	117	ALA	0	-0.039	-0.008	15.593	0.040	0.040	0.000	0.000	0.000
119	A	118	ALA	0	-0.056	-0.029	17.333	-0.002	-0.002	0.000	0.000	0.000
120	A	119	ALA	0	-0.018	0.011	16.794	-0.018	-0.018	0.000	0.000	0.000
121	A	120	ASN	0	-0.013	-0.011	18.577	0.028	0.028	0.000	0.000	0.000
122	A	121	MET	0	0.002	-0.007	11.960	0.014	0.014	0.000	0.000	0.000
123	A	122	PRO	0	-0.035	0.003	16.926	-0.023	-0.023	0.000	0.000	0.000
124	A	123	ILE	0	0.011	0.003	17.083	0.055	0.055	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:GLY)